From 6b3fbc594c491fb6abddb1d07ad012a46424af30 Mon Sep 17 00:00:00 2001 From: Michiel van Setten Date: Tue, 17 Oct 2017 09:34:51 +0200 Subject: [PATCH 1/4] some examples of tests 1 produce an intermediate file using the current code 2 save the file in test_files 3 switch of saving the reference file 4 from now on test if the code still reproduces the reference fiel 5 optimize the code but keep running the test in between to test if the resutls stay the same. some optimization almost everywhere the outputfile is opened again and again in the inner loop, although it is already open. --- License.txt | 19 ---------- tests/tests.py | 95 ++++++++++++++++++++++++++++++++++++++++++++------ ymap/ymap.py | 64 ++++++++++++++++++++-------------- 3 files changed, 121 insertions(+), 57 deletions(-) delete mode 100644 License.txt diff --git a/License.txt b/License.txt deleted file mode 100644 index 36f1bba..0000000 --- a/License.txt +++ /dev/null @@ -1,19 +0,0 @@ -yMap - Yeast Genotype to Phenotype Map (release year 2016) - -The MIT License (MIT) -Copyright (c) <2016> - -Permission is hereby granted, free of charge, to any person obtaining a copy of this software -and associated documentation files (the "Software"), to deal in the Software without restriction, -including without limitation the rights to use, copy, modify, merge, publish, distribute, sublicense, -and/or sell copies of the Software, and to permit persons to whom the Software is furnished to do so, -subject to the following conditions: - -The above copyright notice and this permission notice shall be included in all copies or substantial -portions of the Software. - -THE SOFTWARE IS PROVIDED "AS IS", WITHOUT WARRANTY OF ANY KIND, EXPRESS OR IMPLIED, INCLUDING -BUT NOT LIMITED TO THE WARRANTIES OF MERCHANTABILITY, FITNESS FOR A PARTICULAR PURPOSE AND NONINFRINGEMENT. -IN NO EVENT SHALL THE AUTHORS OR COPYRIGHT HOLDERS BE LIABLE FOR ANY CLAIM, DAMAGES OR OTHER LIABILITY, -WHETHER IN AN ACTION OF CONTRACT, TORT OR OTHERWISE, ARISING FROM, OUT OF OR IN CONNECTION WITH THE SOFTWARE -OR THE USE OR OTHER DEALINGS IN THE SOFTWARE. diff --git a/tests/tests.py b/tests/tests.py index d6104da..6ab075a 100644 --- a/tests/tests.py +++ b/tests/tests.py @@ -1,18 +1,91 @@ +from __future__ import print_function, absolute_import, division, unicode_literals import unittest -from ymap.ymap import data, ymap_proteins, ymap_genes, web +import tempfile +import shutil +import os +import time +import filecmp +from ymap.ymap import data, ymap_proteins, ymap_genes, web, YGtPM -class PimpMyPackage(unittest.TestCase): - def test_data(self): - self.assertTrue(True) +ref_dir = os.path.abspath('test_files') - def test_ymap_proteins(self): - self.assertTrue(True) - def test_ymap_genes(self): - self.assertTrue(True) +class Timer: + def __enter__(self): + self.start = time.clock() + return self - def test_web(self): - self.assertTrue(True) + def __exit__(self, *args): + self.end = time.clock() + self.interval = self.end - self.start + + +class YGtPMTest(unittest.TestCase): + """ + YMap tests + """ + + def setUp(self): + # Create a temporary directory + # self.ref_dir = os.path.abspath('test_files') + self.test_dir = tempfile.mkdtemp() + os.chdir(self.test_dir) + self.c = YGtPM() + self.store_ref = False + # at various places out put is compared to stored reference files. put this to true + # to regenerate all reference files + + def tearDown(self): + # Remove the directory after the test + shutil.rmtree(self.test_dir) + + def test_class_creation(self): + """ + testing the creation of YGtPM + """ + self.assertIsInstance(self.c, YGtPM) + + def test_data(self): + """ + testing the steps in data() + """ + self.assertIsInstance(self.c, YGtPM) + try: # the actual download can only be performed a limit number of times per hour + raise RuntimeError # this is to prevent connecting the database during development comment for real tesing + self.c.pTMdata() + if self.store_ref: + shutil.copy('uniprot_mod_raw.txt', ref_dir) # saving the reference data + except: + shutil.copy(os.path.join(ref_dir, 'uniprot_mod_raw.txt'), '.') + self.assertTrue(os.path.isfile('uniprot_mod_raw.txt')) + + self.c.clean('uniprot_mod_raw.txt') # produces PTMs.txt + self.assertTrue(os.path.isfile('PTMs.txt')) + if self.store_ref: + shutil.copy('PTMs.txt', ref_dir) # saving the reference data + self.assertTrue(filecmp.cmp('PTMs.txt', os.path.join(ref_dir, 'PTMs.txt'))) + + self.c.iD() + self.assertTrue(os.path.isfile('yeastID.txt')) + if self.store_ref: + shutil.copy('yeastID.txt', ref_dir) # saving the reference data + self.assertTrue(filecmp.cmp('yeastID.txt', os.path.join(ref_dir, 'yeastID.txt'))) + + self.c.pmap('yeastID.txt', 'PTMs.txt') + self.assertTrue(os.path.isfile('PTM_id_file.txt')) + if self.store_ref: + shutil.copy('PTM_id_file.txt', ref_dir) # saving the reference data + self.assertTrue(filecmp.cmp('PTM_id_file.txt', os.path.join(ref_dir, 'PTM_id_file.txt'))) + self.assertTrue(False) + + def test_ymap_proteins(self): + self.assertTrue(True) + + def test_ymap_genes(self): + self.assertTrue(True) + + def test_web(self): + self.assertTrue(True) if __name__ == '__main__': - unittest.main() + unittest.main() diff --git a/ymap/ymap.py b/ymap/ymap.py index 77218f3..959bd34 100644 --- a/ymap/ymap.py +++ b/ymap/ymap.py @@ -31,14 +31,14 @@ from __future__ import absolute_import from __future__ import division from __future__ import unicode_literals -try: - from builtins import next - from builtins import str - from builtins import range - from builtins import object - from builtins import bytes -except ImportError: - pass +#try: +# from builtins import next +# from builtins import str +# from builtins import range +# from builtins import object +# from builtins import bytes +#except ImportError: +# pass import os import sys import math @@ -262,10 +262,8 @@ def pTMdata(self): fil = open('uniprot_mod_raw.txt','wb') fil.write(page) fil.close() - - - def clean(self, UniProt_file): - + + def clean(self, UniProt_file): """ cleans file uniprot_mod_raw.txt into a tab separated PTMs.txt """ @@ -280,7 +278,9 @@ def clean(self, UniProt_file): ll = ll[2].split('=') p = line[0]+'\t'+line[4]+'\t'+ll[1] if p > str(0): - out = open('PTMs.txt', 'a') + # PTMs.txt is already open under out and being opened again and again... + # this could cause problems check if you cannot just remove all the opens... + # out = open('PTMs.txt', 'a') out.write(p+'\n') continue if line[2] == 'Glycosylation': @@ -289,7 +289,7 @@ def clean(self, UniProt_file): gg = gg[2].split('=') p1 = line[0]+'\t'+line[4]+'\t'+gg[1] if p1 > str(0): - out = open('PTMs.txt', 'a+') + # out = open('PTMs.txt', 'a+') out.write(p1+'\n') continue if line[2] == 'Modified': @@ -299,7 +299,7 @@ def clean(self, UniProt_file): mm = mm[1].split(';') p2 = line[0]+'\t'+line[4]+'\t'+mm[0] if p2 > str(0): - out = open('PTMs.txt', 'a+') + #out = open('PTMs.txt', 'a+') out.write(p2+'\n') continue if line[2] == 'Cross-link': #ubiquitination @@ -308,8 +308,8 @@ def clean(self, UniProt_file): cc = cc[2].split('=') p3 = line[0]+'\t'+line[4]+'\t'+cc[1] if p3 > str(0): - with open('PTMs.txt', 'a+') as out: - out.write(p3+'\n') + #with open('PTMs.txt', 'a+') as out: + out.write(p3+'\n') def iD(self): @@ -321,10 +321,10 @@ def iD(self): file_1.write(page1) file_1.close() - + # TODO: there seems to be a serious bit of optimization possible here. The second input file should be opened once def pmap(self, file_id, file_PTMs): - - """ if proteins ids are not SDG or uniprot or common names, this method maps the ids + """ + if proteins ids are not SDG or uniprot or common names, this method maps the ids """ with open('PTM_id_file.txt', 'w') as file3: with open(file_id, 'r') as file_id_name: @@ -337,7 +337,7 @@ def pmap(self, file_id, file_PTMs): if line[0] == i[0]: result3 = line[0]+'\t'+line[1]+'\t'+line[2]+'\t'+i[1]+'\t'+i[2] if result3 > str(0): - file3 = open('PTM_id_file.txt', 'a') + # file3 = open('PTM_id_file.txt', 'a') file3.write(result3+'\n') @@ -909,7 +909,11 @@ def betweenPro(fileb, mutation): with open('ptm_between_proteins.txt', 'a+') as file1: file1.write(take3+'\n') - + +# TODO: yeastID.txt is openen each line of mutation, suggestion to open it once store the di[0] and d1[2] in a +# dictionary di[2] as keys list of di[0]'s as values, for a given fi[1] you can then retreive all corresponging di[0]'s +# don't open hotspot again and again it is already +# there are many other cases where something similar hapens def hotspot(fileh, mutation): """ PTMs containing motifs in a close proximity are named hotspots (Beltrao et al. Cell 2012)""" @@ -947,6 +951,10 @@ def sum_file_map(): def resc(): + """ + documentation needed.... + """ + try: r = resource_stream("ymap", "/data/PTMcode+PTMfunc_data/3DID_aceksites_interfaceRes_sc.txt").read().decode() with open('3DID_aceksites_interfaceRes_sc.txt','w') as h: @@ -1019,6 +1027,7 @@ def resc(): c = YGtPM() wd = os.getcwd() +# TODO : remove the variables that store the resutls of the functions that don't return anything def data(): """ this function will download and clean required data to run ymap methods smoothly """ @@ -1029,15 +1038,15 @@ def data(): except IOError: pass try: - dat = c.pTMdata() + c.pTMdata() except IOError: pass try: - cl = c.clean('uniprot_mod_raw.txt') + c.clean('uniprot_mod_raw.txt') except IOError: pass try: - i = c.iD() + c.iD() # this method does not return anything, all the rest below also don't except IOError: pass try: @@ -1659,9 +1668,10 @@ def path(): parser = argparse.ArgumentParser() parser.add_argument('-d', '--ydata', help='downloads required data to run yMap successfully') - parser.add_argument('-g','--ygenes', help='performs the yMap on genes level mutation positions') + parser.add_argument('-g', '--ygenes', help='performs the yMap on genes level mutation positions') parser.add_argument('-p', '--yproteins', help='performs the yMap on proteins level mutation positions') - parser.add_argument('-w', '--yweb', help='generates BioGrid web pages for interactome visualisation; paste the path to biog.txt file') + parser.add_argument('-w', '--yweb', help='generates BioGrid web pages for interactome visualisation; ' + 'paste the path to biog.txt file') args = parser.parse_args() if args.ydata: From ce661ec158dcdcd549ba592b3db0f8692696d0d1 Mon Sep 17 00:00:00 2001 From: Michiel van Setten Date: Tue, 17 Oct 2017 09:39:34 +0200 Subject: [PATCH 2/4] fixing the accidenital removal of License.txt --- License.txt | 19 +++++++++++++++++++ 1 file changed, 19 insertions(+) create mode 100644 License.txt diff --git a/License.txt b/License.txt new file mode 100644 index 0000000..36f1bba --- /dev/null +++ b/License.txt @@ -0,0 +1,19 @@ +yMap - Yeast Genotype to Phenotype Map (release year 2016) + +The MIT License (MIT) +Copyright (c) <2016> + +Permission is hereby granted, free of charge, to any person obtaining a copy of this software +and associated documentation files (the "Software"), to deal in the Software without restriction, +including without limitation the rights to use, copy, modify, merge, publish, distribute, sublicense, +and/or sell copies of the Software, and to permit persons to whom the Software is furnished to do so, +subject to the following conditions: + +The above copyright notice and this permission notice shall be included in all copies or substantial +portions of the Software. + +THE SOFTWARE IS PROVIDED "AS IS", WITHOUT WARRANTY OF ANY KIND, EXPRESS OR IMPLIED, INCLUDING +BUT NOT LIMITED TO THE WARRANTIES OF MERCHANTABILITY, FITNESS FOR A PARTICULAR PURPOSE AND NONINFRINGEMENT. +IN NO EVENT SHALL THE AUTHORS OR COPYRIGHT HOLDERS BE LIABLE FOR ANY CLAIM, DAMAGES OR OTHER LIABILITY, +WHETHER IN AN ACTION OF CONTRACT, TORT OR OTHERWISE, ARISING FROM, OUT OF OR IN CONNECTION WITH THE SOFTWARE +OR THE USE OR OTHER DEALINGS IN THE SOFTWARE. From efb1f5cab68749aebf828aa82f7a6e5547437255 Mon Sep 17 00:00:00 2001 From: Michiel van Setten Date: Fri, 20 Oct 2017 15:43:58 +0200 Subject: [PATCH 3/4] reference files --- test_files/PTM_id_file.txt | 9258 ++++ test_files/PTMs.txt | 9881 ++++ test_files/uniprot_mod_raw.txt | 92278 +++++++++++++++++++++++++++++++ test_files/yeastID.txt | 6730 +++ tests/tests.py | 2 +- ymap/ymap.py | 4 +- 6 files changed, 118150 insertions(+), 3 deletions(-) create mode 100644 test_files/PTM_id_file.txt create mode 100644 test_files/PTMs.txt create mode 100644 test_files/uniprot_mod_raw.txt create mode 100644 test_files/yeastID.txt diff --git a/test_files/PTM_id_file.txt b/test_files/PTM_id_file.txt new file mode 100644 index 0000000..1a5cee8 --- /dev/null +++ b/test_files/PTM_id_file.txt @@ -0,0 +1,9258 @@ +P12688 YKL126W YPK1 57 Phosphothreonine +P12688 YKL126W YPK1 61 Phosphoserine +P12688 YKL126W YPK1 64 Phosphoserine +P12688 YKL126W YPK1 71 Phosphoserine +P12688 YKL126W YPK1 170 Phosphoserine +P12688 YKL126W YPK1 502 Phosphothreonine +P12688 YKL126W YPK1 504 Phosphothreonine%3B +P12688 YKL126W YPK1 644 Phosphoserine +P12688 YKL126W YPK1 653 Phosphoserine +P12688 YKL126W YPK1 662 Phosphothreonine%3B +P12688 YKL126W YPK1 671 Phosphoserine +P25491 YNL064C YDJ1 406 Cysteine +P25491 YNL064C YDJ1 406 S-farnesyl +P25491 YNL064C YDJ1 198 Glycyl +P16521 YLR249W YEF3 2 N-acetylserine +P16521 YLR249W YEF3 187 N6%2CN6%2CN6-trimethyllysine +P16521 YLR249W YEF3 196 N6%2CN6%2CN6-trimethyllysine +P16521 YLR249W YEF3 642 Phosphoserine +P16521 YLR249W YEF3 789 N6%2CN6%2CN6-trimethyllysine +P16521 YLR249W YEF3 972 Phosphothreonine +P16521 YLR249W YEF3 974 Phosphoserine +P16521 YLR249W YEF3 1039 Phosphoserine +P16521 YLR249W YEF3 1040 Phosphoserine +P16521 YLR249W YEF3 350 Glycyl +P16521 YLR249W YEF3 636 Glycyl +P11484 YDL229W SSB1 2 N-acetylalanine +P11484 YDL229W SSB1 47 Phosphothreonine +P11484 YDL229W SSB1 431 Phosphothreonine +P39940 YER125W RSP5 258 Glycyl +Q06224 YLR277C YSH1 517 Phosphoserine%3B +P02829 YPL240C HSP82 657 Phosphoserine +P10591 YAL005C SSA1 2 N-acetylserine +P10591 YAL005C SSA1 62 Phosphoserine +P10591 YAL005C SSA1 551 Phosphoserine +P10591 YAL005C SSA1 603 Phosphoserine +P10591 YAL005C SSA1 556 Glycyl +P41800 YLL006W MMM1 6 N-linked +P41800 YLL006W MMM1 50 N-linked +P41800 YLL006W MMM1 55 N-linked +P41800 YLL006W MMM1 59 N-linked +P00546 YBR160W CDC28 2 N-acetylserine +P00546 YBR160W CDC28 19 Phosphotyrosine +P00546 YBR160W CDC28 169 Phosphothreonine +P15108 YMR186W HSC82 653 Phosphoserine +P31539 YLL026W HSP104 1 N-acetylmethionine +P31539 YLL026W HSP104 206 Phosphoserine +P31539 YLL026W HSP104 306 Phosphoserine +P31539 YLL026W HSP104 499 Phosphothreonine +P31539 YLL026W HSP104 535 Phosphoserine +P31539 YLL026W HSP104 442 Glycyl +P31539 YLL026W HSP104 620 Glycyl +P25623 YCR030C SYP1 264 Phosphoserine +P25623 YCR030C SYP1 331 Phosphoserine +P25623 YCR030C SYP1 416 Phosphothreonine +P25623 YCR030C SYP1 496 Phosphoserine +P25623 YCR030C SYP1 500 Phosphoserine +P25623 YCR030C SYP1 577 Phosphothreonine +P25623 YCR030C SYP1 256 Glycyl +P08539 YHR005C GPA1 2 N-myristoyl +P08539 YHR005C GPA1 3 S-palmitoyl +P08539 YHR005C GPA1 165 Glycyl +P15442 YDR283C GCN2 761 Phosphoserine +P15442 YDR283C GCN2 882 Phosphothreonine%3B +P15442 YDR283C GCN2 887 Phosphothreonine%3B +P10592 YLL024C SSA2 2 N-acetylserine +P10592 YLL024C SSA2 20 Phosphoserine +P10592 YLL024C SSA2 551 Phosphoserine +P10592 YLL024C SSA2 603 Phosphoserine +P10592 YLL024C SSA2 556 Glycyl +P06782 YDR477W SNF1 210 Phosphothreonine%3B +P06782 YDR477W SNF1 413 Phosphoserine +P06782 YDR477W SNF1 487 Phosphoserine +P06782 YDR477W SNF1 632 Phosphoserine +P06782 YDR477W SNF1 461 Glycyl +P06782 YDR477W SNF1 549 Glycyl +P22147 YGL173C XRN1 1506 Phosphothreonine +P22147 YGL173C XRN1 1510 Phosphoserine +P32598 YER133W GLC7 1 N-acetylmethionine +P32598 YER133W GLC7 22 Glycyl +P32598 YER133W GLC7 47 Glycyl +P35202 YOR143C THI80 2 N-acetylserine +P16120 YCR053W THR4 124 N6-(pyridoxal +P16120 YCR053W THR4 467 Phosphoserine +P40328 YPL074W YTA6 255 Phosphoserine +P39077 YJL014W CCT3 1 N-acetylmethionine +P39077 YJL014W CCT3 257 Phosphoserine +P35691 YKL056C TMA19 9 Phosphoserine +P35691 YKL056C TMA19 15 Phosphoserine +P29056 YGR246C BRF1 381 Phosphoserine +P29056 YGR246C BRF1 384 Phosphoserine +P32318 YGR144W THI4 205 2%2C3-didehydroalanine +Q08144 YOL018C TLG2 109 Phosphoserine +P07273 YGL043W DST1 116 Phosphoserine +P00927 YER086W ILV1 109 N6-(pyridoxal +P41338 YPL028W ERG10 2 N-acetylserine +O74700 YEL020W-A TIM9 1 N-acetylmethionine +Q12218 YOR009W TIR4 465 GPI-anchor +Q12218 YOR009W TIR4 327 N-linked +Q12218 YOR009W TIR4 348 N-linked +Q12218 YOR009W TIR4 368 N-linked +Q12218 YOR009W TIR4 403 N-linked +Q12218 YOR009W TIR4 404 N-linked +Q05998 YLR237W THI7 560 Phosphoserine +P40040 YER063W THO1 22 Phosphoserine +P40040 YER063W THO1 58 Phosphoserine +P40040 YER063W THO1 68 Phosphoserine +P27654 YBR067C TIP1 186 GPI-anchor +P10863 YER011W TIR1 233 GPI-anchor +P32802 YLR083C EMP70 61 N-linked +P32802 YLR083C EMP70 282 N-linked +Q03290 YDR460W TFB3 157 Phosphoserine +Q03290 YDR460W TFB3 258 Phosphothreonine +P46678 YNL039W BDP1 49 Phosphoserine +P46678 YNL039W BDP1 178 Phosphoserine +Q12415 YOR110W TFC7 365 Phosphoserine +P42883 YNL332W THI12 62 N6-(pyridoxal +P40340 YGR270W YTA7 2 N-acetylalanine +P40340 YGR270W YTA7 11 Phosphoserine +P40340 YGR270W YTA7 17 Phosphoserine +P40340 YGR270W YTA7 94 Phosphoserine +P40340 YGR270W YTA7 212 Phosphothreonine +P40340 YGR270W YTA7 229 Phosphothreonine +P40340 YGR270W YTA7 241 Phosphoserine +P40340 YGR270W YTA7 259 Phosphoserine +P40340 YGR270W YTA7 285 Phosphoserine +P40340 YGR270W YTA7 367 Phosphoserine +P40340 YGR270W YTA7 369 Phosphoserine +P40340 YGR270W YTA7 370 Phosphoserine +P40340 YGR270W YTA7 735 Phosphoserine +P40340 YGR270W YTA7 1142 Phosphoserine +P40340 YGR270W YTA7 1256 Phosphoserine +Q08921 YPL180W TCO89 52 Phosphothreonine +Q08921 YPL180W TCO89 82 Phosphothreonine +Q08921 YPL180W TCO89 84 Phosphoserine +Q08921 YPL180W TCO89 104 Phosphoserine +Q08921 YPL180W TCO89 107 Phosphoserine +Q08921 YPL180W TCO89 115 Phosphoserine +Q08921 YPL180W TCO89 144 Phosphoserine +Q08921 YPL180W TCO89 203 Phosphoserine +Q08921 YPL180W TCO89 215 Phosphoserine +Q08921 YPL180W TCO89 290 Phosphoserine +Q08921 YPL180W TCO89 397 Phosphoserine +Q08921 YPL180W TCO89 575 Phosphoserine +Q08921 YPL180W TCO89 707 Phosphoserine +P32776 YDR311W TFB1 150 Phosphothreonine +P33339 YGR047C TFC4 311 Phosphoserine +Q08686 YOR251C TUM1 201 Phosphoserine +Q08686 YOR251C TUM1 264 Phosphoserine +P33315 YBR117C TKL2 286 Phosphoserine +P33315 YBR117C TKL2 648 Glycyl +P36165 YKR089C TGL4 55 Phosphoserine +P36165 YKR089C TGL4 737 Phosphoserine +P36165 YKR089C TGL4 749 Phosphoserine +P36165 YKR089C TGL4 751 Phosphoserine +P36165 YKR089C TGL4 836 Phosphoserine +P47183 YJR156C THI11 62 N6-(pyridoxal +P43534 YFL058W THI5 62 N6-(pyridoxal +P89886 YER007C-A TMA20 1 N-acetylmethionine +Q12049 YPR045C THP3 1 N-acetylmethionine +P40462 YIL137C TMA108 2 N-acetylserine +Q12513 YDL110C TMA17 24 Phosphoserine +Q12513 YDL110C TMA17 68 Phosphoserine +P53840 YNL273W TOF1 626 Phosphoserine +P53840 YNL273W TOF1 654 Phosphoserine +P53840 YNL273W TOF1 1056 Phosphoserine +P53840 YNL273W TOF1 1058 Phosphoserine +P53840 YNL273W TOF1 1213 Phosphoserine +P40310 YJL093C TOK1 119 Phosphoserine +Q03280 YDR457W TOM1 1890 Phosphoserine +Q03280 YDR457W TOM1 2096 Phosphothreonine +Q03280 YDR457W TOM1 2119 Phosphoserine +Q03280 YDR457W TOM1 2376 Phosphoserine +Q03280 YDR457W TOM1 2406 Phosphoserine +Q03280 YDR457W TOM1 2418 Phosphoserine +P35180 YGR082W TOM20 172 Phosphoserine +P38825 YHR117W TOM71 55 Phosphoserine +P32830 YBR091C TIM12 2 N-acetylserine +P33890 YOR010C TIR2 231 GPI-anchor +Q08422 YOR052C TMC1 2 N-acetylserine +Q08422 YOR052C TMC1 43 Phosphoserine +Q08422 YOR052C TMC1 54 Phosphoserine +P04786 YOL006C TOP1 14 Phosphoserine +P04786 YOL006C TOP1 15 Phosphoserine +P04786 YOL006C TOP1 24 Phosphoserine +P04786 YOL006C TOP1 49 Phosphoserine +P04786 YOL006C TOP1 76 Phosphoserine +P06786 YNL088W TOP2 1086 Phosphothreonine%3B +P06786 YNL088W TOP2 1087 Phosphoserine%3B +P06786 YNL088W TOP2 1252 Phosphoserine +P06786 YNL088W TOP2 1258 Phosphothreonine%3B +P06786 YNL088W TOP2 1266 Phosphoserine%3B +P06786 YNL088W TOP2 1269 Phosphoserine%3B +P06786 YNL088W TOP2 1272 Phosphoserine%3B +P06786 YNL088W TOP2 1353 Phosphoserine%3B +P06786 YNL088W TOP2 1356 Phosphoserine%3B +P06786 YNL088W TOP2 1408 Phosphoserine%3B +P06786 YNL088W TOP2 1423 Phosphoserine%3B +Q06177 YLR327C TMA10 28 Phosphoserine +Q06177 YLR327C TMA10 79 Phosphoserine +P49334 YNL131W TOM22 44 Phosphoserine +P49334 YNL131W TOM22 46 Phosphoserine +P38288 YBR162C TOS1 236 N-linked +P38288 YBR162C TOS1 417 N-linked +P12685 YJL129C TRK1 15 Phosphoserine +P12685 YJL129C TRK1 414 Phosphoserine +P12685 YJL129C TRK1 534 Phosphoserine +P12685 YJL129C TRK1 100 N-linked +P12685 YJL129C TRK1 169 N-linked +P12685 YJL129C TRK1 222 N-linked +P12685 YJL129C TRK1 227 N-linked +P12685 YJL129C TRK1 251 N-linked +P12685 YJL129C TRK1 369 N-linked +P12685 YJL129C TRK1 383 N-linked +P12685 YJL129C TRK1 497 N-linked +P12685 YJL129C TRK1 501 N-linked +P12685 YJL129C TRK1 532 N-linked +P12685 YJL129C TRK1 580 N-linked +P12685 YJL129C TRK1 677 N-linked +P12685 YJL129C TRK1 919 N-linked +P12685 YJL129C TRK1 1030 N-linked +P12685 YJL129C TRK1 1135 N-linked +Q12400 YOL093W TRM10 16 Phosphothreonine +Q12400 YOL093W TRM10 283 Phosphoserine +Q02648 YPL030W TRM44 107 Phosphoserine +P32643 YER175C TMT1 2 N-acetylserine +P32600 YKL203C TOR2 10 Phosphothreonine +P17536 YNL079C TPM1 195 Phosphoserine +P17536 YNL079C TPM1 39 Glycyl +P17536 YNL079C TPM1 59 Glycyl +P17536 YNL079C TPM1 187 Glycyl +P53283 YGR138C TPO2 50 Phosphoserine +Q12256 YOR273C TPO4 589 Phosphothreonine +Q12256 YOR273C TPO4 606 Phosphothreonine +Q12256 YOR273C TPO4 608 Phosphothreonine +Q12256 YOR273C TPO4 633 Phosphoserine +Q12256 YOR273C TPO4 646 Phosphoserine +Q05024 YMR233W TRI1 113 Phosphoserine +Q05024 YMR233W TRI1 225 Phosphoserine +Q05024 YMR233W TRI1 201 Glycyl +Q05024 YMR233W TRI1 215 Glycyl +P33753 YKR056W TRM2 92 Phosphoserine +P33753 YKR056W TRM2 93 Phosphoserine +P22217 YLR043C TRX1 54 Glycyl +P22217 YLR043C TRX1 66 Glycyl +P22217 YLR043C TRX1 96 Glycyl +P34760 YML028W TSA1 174 Phosphothreonine +P34760 YML028W TSA1 14 Glycyl +P34760 YML028W TSA1 89 Glycyl +P34760 YML028W TSA1 132 Glycyl +P40061 YER093C TSC11 19 Phosphoserine +P40061 YER093C TSC11 81 Phosphoserine +P40061 YER093C TSC11 84 Phosphoserine +P40061 YER093C TSC11 87 Phosphoserine +P40061 YER093C TSC11 141 Phosphoserine +P40552 YIL011W TIR3 245 GPI-anchor +P40552 YIL011W TIR3 234 N-linked +Q12000 YOR091W TMA46 301 Phosphoserine +Q06266 YLR183C TOS4 40 Phosphoserine +Q06266 YLR183C TOS4 100 Phosphoserine +Q07824 YLL028W TPO1 19 Phosphoserine%3B +Q07824 YLL028W TPO1 52 Phosphothreonine%3B +Q07824 YLL028W TPO1 72 Phosphoserine +Q07824 YLL028W TPO1 76 Phosphoserine +Q07824 YLL028W TPO1 89 Phosphothreonine +Q07824 YLL028W TPO1 91 Phosphoserine +Q07824 YLL028W TPO1 342 Phosphoserine%3B +Q12199 YPR040W TIP41 55 Phosphothreonine +P23254 YPR074C TKL1 286 Phosphoserine +P23254 YPR074C TKL1 335 Phosphoserine +P23254 YPR074C TKL1 402 Phosphoserine +P23254 YPR074C TKL1 492 Phosphoserine +P23254 YPR074C TKL1 647 Glycyl +Q03322 YDR468C TLG1 31 Phosphothreonine%3B +Q03322 YDR468C TLG1 205 S-palmitoyl +Q03322 YDR468C TLG1 206 S-palmitoyl +Q03322 YDR468C TLG1 183 Glycyl +P53322 YGR260W TNA1 27 Phosphoserine +P53322 YGR260W TNA1 283 Glycyl +Q08919 YPL176C TRE1 139 N-linked +Q08919 YPL176C TRE1 213 N-linked +Q08919 YPL176C TRE1 529 N-linked +Q03774 YDR165W TRM82 93 Phosphoserine +P32893 YGR166W TRS65 393 Phosphoserine +P32893 YGR166W TRS65 398 Phosphoserine +Q02208 YKR010C TOF2 397 Phosphoserine +Q02208 YKR010C TOF2 405 Phosphothreonine +P07213 YNL121C TOM70 174 Phosphoserine +P48560 YNL300W TOS6 80 GPI-anchor +P48560 YNL300W TOS6 69 N-linked +P00942 YDR050C TPI1 4 Phosphothreonine +P00942 YDR050C TPI1 71 Phosphoserine +P00942 YDR050C TPI1 215 Phosphoserine +P00942 YDR050C TPI1 223 Glycyl +P40414 YIL138C TPM2 55 Phosphoserine +P40414 YIL138C TPM2 116 Phosphoserine +P40414 YIL138C TPM2 157 Phosphoserine +Q06451 YPR156C TPO3 55 Phosphoserine +Q06451 YPR156C TPO3 98 Phosphothreonine +Q06451 YPR156C TPO3 101 Phosphoserine +Q06451 YPR156C TPO3 132 Phosphoserine +P36029 YKL174C TPO5 569 Phosphoserine +Q04183 YDR407C TRS120 379 Phosphoserine +Q04183 YDR407C TRS120 387 Phosphoserine +P38427 YML100W TSL1 49 Phosphoserine +P38427 YML100W TSL1 53 Phosphoserine +P38427 YML100W TSL1 56 Phosphoserine +P38427 YML100W TSL1 71 Phosphoserine +P38427 YML100W TSL1 77 Phosphoserine +P38427 YML100W TSL1 135 Phosphoserine +P38427 YML100W TSL1 147 Phosphoserine +P38427 YML100W TSL1 161 Phosphoserine +P38427 YML100W TSL1 229 Phosphoserine +P38427 YML100W TSL1 251 Phosphothreonine +P38427 YML100W TSL1 303 Phosphoserine +P38427 YML100W TSL1 815 Phosphothreonine +P35172 YBR001C NTH2 52 Phosphoserine +P35172 YBR001C NTH2 53 Phosphoserine +P35172 YBR001C NTH2 88 Phosphothreonine +P35172 YBR001C NTH2 112 Phosphoserine +P34219 YBL054W TOD6 280 Phosphoserine +P34219 YBL054W TOD6 333 Phosphoserine +P34219 YBL054W TOD6 341 Phosphoserine +P34219 YBL054W TOD6 366 Phosphoserine +P33448 YOR045W TOM6 1 N-acetylmethionine +P38811 YHR099W TRA1 2 N-acetylserine +P38811 YHR099W TRA1 172 Phosphoserine +P38811 YHR099W TRA1 542 Phosphoserine +Q08693 YOR256C TRE2 228 N-linked +Q08693 YOR256C TRE2 669 N-linked +Q08693 YOR256C TRE2 736 N-linked +P48561 YNL299W TRF5 596 Phosphoserine +P48561 YNL299W TRF5 602 Phosphoserine +P28584 YKR050W TRK2 216 N-linked +P28584 YKR050W TRK2 233 N-linked +P28584 YKR050W TRK2 265 N-linked +P33122 YOR344C TYE7 104 Phosphoserine +P33122 YOR344C TYE7 237 Phosphothreonine +P21734 YDR177W UBC1 93 Glycyl +P33296 YER100W UBC6 139 Phosphoserine +P33296 YER100W UBC6 178 Phosphothreonine +P32571 YDR069C DOA4 443 Phosphoserine +P19812 YGR184C UBR1 296 Phosphoserine +P19812 YGR184C UBR1 300 Phosphoserine +P19812 YGR184C UBR1 1938 Phosphoserine +Q07963 YLR024C UBR2 1218 Phosphoserine +Q07963 YLR024C UBR2 1222 Phosphoserine +Q07963 YLR024C UBR2 709 Glycyl +Q06682 YDR330W UBX5 139 Phosphoserine +P29509 YDR353W TRR1 303 Phosphoserine +P38962 YDR084C TVP23 63 N-linked +P38962 YDR084C TVP23 86 N-linked +P38962 YDR084C TVP23 185 N-linked +P22803 YGR209C TRX2 62 Phosphoserine +P22803 YGR209C TRX2 67 Glycyl +P22803 YGR209C TRX2 97 Glycyl +Q12094 YOR006C TSR3 286 Phosphoserine +Q12094 YOR006C TSR3 289 Phosphoserine +Q08747 YOR295W UAF30 218 Phosphoserine +Q08747 YOR295W UAF30 220 Phosphoserine +Q08747 YOR295W UAF30 223 Phosphoserine +P14682 YDR054C CDC34 186 Phosphoserine +P14682 YDR054C CDC34 282 Phosphoserine +P14682 YDR054C CDC34 292 Phosphoserine +P40032 YER049W TPA1 607 Phosphoserine +P38426 YMR261C TPS3 148 Phosphoserine +P38426 YMR261C TPS3 150 Phosphoserine +P38426 YMR261C TPS3 181 Phosphoserine +P38426 YMR261C TPS3 265 Phosphothreonine +P38426 YMR261C TPS3 267 Phosphoserine +P38426 YMR261C TPS3 273 Phosphoserine +P38426 YMR261C TPS3 960 Phosphoserine +P46959 YJL125C GCD14 302 Phosphoserine +Q12009 YDL201W TRM8 7 Phosphoserine%3B +Q12009 YDL201W TRM8 59 Phosphoserine +P53250 YGR080W TWF1 167 Phosphoserine +P53250 YGR080W TWF1 172 Phosphoserine +P00899 YER090W TRP2 81 Phosphoserine +P00899 YER090W TRP2 223 Phosphothreonine +P00937 YKL211C TRP3 2 Phosphoserine +P00931 YGL026C TRP5 384 N6-(pyridoxal +P00931 YGL026C TRP5 540 Phosphoserine +P00931 YGL026C TRP5 683 Phosphoserine +Q04767 YMR071C TVP18 146 Phosphothreonine +Q04767 YMR071C TVP18 153 Phosphothreonine +Q04767 YMR071C TVP18 22 N-linked +Q99394 YOR115C TRS33 2 N-acetylserine +Q04120 YDR453C TSA2 174 Phosphothreonine +Q04120 YDR453C TSA2 14 Glycyl +Q04120 YDR453C TSA2 89 Glycyl +Q04120 YDR453C TSA2 132 Glycyl +P36097 YKL033W TTI1 817 Phosphoserine +P16649 YCR084C TUP1 439 Phosphoserine +P32356 YDR001C NTH1 2 N-acetylserine +P32356 YDR001C NTH1 20 Phosphoserine +P32356 YDR001C NTH1 21 Phosphoserine +P32356 YDR001C NTH1 23 Phosphoserine +P32356 YDR001C NTH1 58 Phosphothreonine +P32356 YDR001C NTH1 60 Phosphoserine +P32356 YDR001C NTH1 66 Phosphoserine +P32356 YDR001C NTH1 83 Phosphoserine +P53044 YGR048W UFD1 354 Phosphoserine +P33202 YKL010C UFD4 87 Phosphothreonine +P33202 YKL010C UFD4 349 Glycyl +Q02724 YPL020C ULP1 2 N-acetylserine +Q02724 YPL020C ULP1 21 Phosphoserine +Q02724 YPL020C ULP1 25 Phosphoserine +Q02724 YPL020C ULP1 179 Phosphothreonine +Q02724 YPL020C ULP1 264 Phosphoserine +P28274 YBL039C URA7 422 Glycyl +P40362 YJL069C UTP18 182 Phosphoserine +P40362 YJL069C UTP18 184 Phosphoserine +P40498 YIL091C UTP25 53 Phosphoserine +P40498 YIL091C UTP25 63 Phosphoserine +P40498 YIL091C UTP25 196 Phosphoserine +P16140 YBR127C VMA2 4 Phosphoserine +P16140 YBR127C VMA2 137 Phosphoserine +P16140 YBR127C VMA2 503 Phosphoserine +P16140 YBR127C VMA2 504 Phosphoserine +P16140 YBR127C VMA2 511 Phosphoserine%3B +P16140 YBR127C VMA2 515 Phosphoserine +P16140 YBR127C VMA2 14 Glycyl +P16140 YBR127C VMA2 508 Glycyl +P38358 YBR293W VBA2 420 N-linked +Q04602 YDR119W VBA4 62 Phosphoserine +Q04602 YDR119W VBA4 99 Phosphoserine +Q04602 YDR119W VBA4 106 Phosphoserine +Q04602 YDR119W VBA4 160 Phosphoserine +Q04602 YDR119W VBA4 192 Phosphoserine +Q04602 YDR119W VBA4 480 N-linked +Q04602 YDR119W VBA4 553 N-linked +P39538 YJL197W UBP12 84 Phosphoserine +P39538 YJL197W UBP12 1160 Phosphoserine +P47049 YJL048C UBX6 369 Phosphoserine +P40554 YIL008W URM1 99 1-thioglycine +P40554 YIL008W URM1 99 Glycyl +Q04500 YML093W UTP14 34 Phosphoserine +Q04500 YML093W UTP14 35 Phosphoserine +Q04500 YML093W UTP14 151 Phosphoserine +Q04500 YML093W UTP14 423 Phosphoserine +Q04500 YML093W UTP14 424 Phosphoserine +Q04500 YML093W UTP14 488 Phosphoserine +Q04500 YML093W UTP14 500 Phosphoserine +Q04500 YML093W UTP14 562 Phosphoserine +Q04500 YML093W UTP14 668 Phosphoserine +Q04500 YML093W UTP14 738 Phosphoserine +Q12339 YOR004W UTP23 182 Phosphoserine +P43123 YDL103C QRI1 218 Phosphoserine +P43123 YDL103C QRI1 461 Phosphoserine +P52490 YDR092W UBC13 92 Glycyl +Q02159 YMR022W UBC7 89 Glycyl +Q08562 YOR191W ULS1 121 Phosphoserine +P25386 YDL058W USO1 1770 Phosphoserine +P42945 YJL109C UTP10 2 N-acetylserine +Q06078 YLR409C UTP21 2 N-acetylserine +Q06078 YLR409C UTP21 772 Phosphoserine +P53254 YGR090W UTP22 10 Phosphoserine +P53254 YGR090W UTP22 58 Phosphoserine +P53254 YGR090W UTP22 60 Phosphothreonine +P53254 YGR090W UTP22 64 Phosphoserine +P53276 YGR128C UTP8 95 Phosphothreonine +P53276 YGR128C UTP8 148 Phosphoserine +P53276 YGR128C UTP8 150 Phosphoserine +P21373 YJR049C UTR1 499 Phosphoserine +P21373 YJR049C UTR1 503 Phosphoserine +Q01476 YOR124C UBP2 907 Phosphoserine +P43593 YFR010W UBP6 389 Phosphothreonine +P43593 YFR010W UBP6 470 Phosphoserine +P38882 YHR196W UTP9 547 Phosphoserine +P38882 YHR196W UTP9 564 Phosphoserine +P25591 YCL063W VAC17 2 N-acetylalanine +P25591 YCL063W VAC17 119 Phosphoserine +P25591 YCL063W VAC17 149 Phosphothreonine +P25591 YCL063W VAC17 178 Phosphoserine +P25591 YCL063W VAC17 248 Phosphothreonine +P25591 YCL063W VAC17 269 Phosphoserine +P17255 YDL185W VMA1 2 N-acetylalanine +P17255 YDL185W VMA1 131 Phosphothreonine +P17255 YDL185W VMA1 858 Phosphoserine +P17255 YDL185W VMA1 928 Phosphoserine +P06104 YGL058W RAD6 120 Phosphoserine%3B +P38349 YBR273C UBX7 388 Phosphoserine +P38349 YBR273C UBX7 19 Glycyl +P53177 YGL050W TYW3 26 Phosphoserine +P53177 YGL050W TYW3 238 Phosphoserine +P22515 YKL210W UBA1 2 N-acetylserine +P22515 YKL210W UBA1 265 Phosphoserine +P22515 YKL210W UBA1 914 Phosphoserine +P22515 YKL210W UBA1 595 Glycyl +P22515 YKL210W UBA1 608 Glycyl +P52491 YLR306W UBC12 1 N-acetylmethionine +P15732 YDR059C UBC5 12 Phosphoserine +P15732 YDR059C UBC5 91 Glycyl +P38187 YBL067C UBP13 198 Phosphoserine +P25037 YDL122W UBP1 530 Phosphoserine +P25037 YDL122W UBP1 531 Phosphoserine +P25037 YDL122W UBP1 555 Phosphoserine +P25037 YDL122W UBP1 618 Phosphoserine +P25037 YDL122W UBP1 638 Phosphoserine +P25037 YDL122W UBP1 652 Phosphothreonine +P25037 YDL122W UBP1 653 Phosphoserine +P25037 YDL122W UBP1 654 Phosphoserine +P25037 YDL122W UBP1 670 Phosphoserine +P25037 YDL122W UBP1 755 Phosphoserine +P32861 YKL035W UGP1 2 N-acetylserine +P32861 YKL035W UGP1 17 Phosphoserine +P32861 YKL035W UGP1 19 Phosphothreonine +P32861 YKL035W UGP1 21 Phosphoserine +P32861 YKL035W UGP1 79 Phosphoserine +P32861 YKL035W UGP1 369 Omega-N-methylarginine +Q08960 YPL207W TYW1 496 Glycyl +P38820 YHR111W UBA4 1 N-acetylmethionine +P38820 YHR111W UBA4 326 Phosphoserine +P15731 YBR082C UBC4 12 Phosphoserine +P15731 YBR082C UBC4 91 Glycyl +P34223 YBL058W SHP1 128 Phosphoserine +P34223 YBL058W SHP1 210 Phosphoserine +P34223 YBL058W SHP1 224 Phosphoserine +P34223 YBL058W SHP1 315 Phosphoserine +P34223 YBL058W SHP1 321 Phosphoserine +P34223 YBL058W SHP1 322 Phosphoserine +P34223 YBL058W SHP1 331 Phosphothreonine +P34223 YBL058W SHP1 241 Glycyl +Q04511 YML088W UFO1 511 Phosphoserine +Q04511 YML088W UFO1 514 Phosphothreonine +P40537 YIL031W ULP2 788 Phosphoserine +P40537 YIL031W ULP2 903 Phosphoserine +P40537 YIL031W ULP2 983 Phosphoserine +P40537 YIL031W ULP2 984 Phosphoserine +Q12151 YDR213W UPC2 122 Phosphothreonine +Q12151 YDR213W UPC2 519 Phosphoserine +P50623 YDL064W UBC9 2 N-acetylserine +P0CG63 YLL039C UBI4 76 Glycyl +Q03327 YDR470C UGO1 1 N-acetylmethionine +P39547 YAR027W UIP3 11 Glycyl +P39547 YAR027W UIP3 218 Glycyl +P18562 YHR128W FUR1 82 Phosphoserine +P27515 YNR012W URK1 17 Phosphoserine +P27515 YNR012W URK1 276 Phosphoserine +P32366 YLR447C VMA6 1 N-acetylmethionine +Q06708 YLR386W VAC14 767 Phosphoserine +Q06708 YLR386W VAC14 805 Phosphoserine +Q06708 YLR386W VAC14 867 Phosphoserine +Q99385 YDL128W VCX1 1 N-acetylmethionine +Q99385 YDL128W VCX1 13 Phosphoserine +P53058 YGL258W VEL1 26 N-linked +P53058 YGL258W VEL1 48 N-linked +P53058 YGL258W VEL1 91 N-linked +P53058 YGL258W VEL1 139 N-linked +P53058 YGL258W VEL1 152 N-linked +Q08926 YPL186C UIP4 140 Phosphoserine +Q08926 YPL186C UIP4 185 Phosphoserine +Q08926 YPL186C UIP4 205 Phosphoserine +P39001 YDR207C UME6 114 Phosphoserine +P39001 YDR207C UME6 141 Phosphoserine +P39001 YDR207C UME6 150 Phosphoserine +P39001 YDR207C UME6 228 Phosphoserine +P39001 YDR207C UME6 316 Phosphoserine +P39001 YDR207C UME6 318 Phosphoserine +P39001 YDR207C UME6 645 Phosphoserine +P23202 YNL229C URE2 2 N-acetylmethionine +Q03714 YML029W USA1 374 Phosphoserine +Q03714 YML029W USA1 376 Phosphoserine +Q03714 YML029W USA1 379 Phosphoserine +P36172 YKR105C VBA5 70 N-linked +P36172 YKR105C VBA5 423 N-linked +P04840 YNL055C POR1 109 Phosphoserine +P04840 YNL055C POR1 117 Phosphothreonine +P40157 YNL212W VID27 170 Phosphoserine +P40157 YNL212W VID27 195 Phosphoserine +P40157 YNL212W VID27 196 Phosphoserine +P40157 YNL212W VID27 222 Phosphoserine +P40157 YNL212W VID27 486 Phosphothreonine +Q06685 YLR410W VIP1 31 Phosphoserine +Q06685 YLR410W VIP1 54 Phosphoserine +Q06685 YLR410W VIP1 77 Phosphoserine +Q06685 YLR410W VIP1 895 Phosphoserine +Q06685 YLR410W VIP1 1107 Phosphoserine +P39968 YEL013W VAC8 11 Phosphoserine +P39968 YEL013W VAC8 16 Phosphoserine +P39968 YEL013W VAC8 2 N-myristoyl +P39968 YEL013W VAC8 4 S-palmitoyl +P39968 YEL013W VAC8 5 S-palmitoyl +P39968 YEL013W VAC8 7 S-palmitoyl +P39968 YEL013W VAC8 77 Glycyl +P39968 YEL013W VAC8 515 Glycyl +Q05934 YLR373C VID22 21 N-linked +Q05934 YLR373C VID22 242 N-linked +Q05934 YLR373C VID22 291 N-linked +Q05934 YLR373C VID22 540 N-linked +Q05934 YLR373C VID22 645 N-linked +Q05934 YLR373C VID22 649 N-linked +Q05934 YLR373C VID22 652 N-linked +Q05934 YLR373C VID22 662 N-linked +Q05934 YLR373C VID22 669 N-linked +Q05934 YLR373C VID22 673 N-linked +Q05934 YLR373C VID22 688 N-linked +Q05934 YLR373C VID22 722 N-linked +P23642 YML115C VAN1 25 Phosphoserine +P23642 YML115C VAN1 215 N-linked +P23642 YML115C VAN1 251 N-linked +P48836 YHR039C-A VMA10 2 N-acetylserine +P32319 YBL017C PEP1 96 N-linked +P32319 YBL017C PEP1 170 N-linked +P32319 YBL017C PEP1 447 N-linked +P32319 YBL017C PEP1 793 N-linked +P32319 YBL017C PEP1 1010 N-linked +P32319 YBL017C PEP1 1303 N-linked +P32913 YOR132W VPS17 544 Phosphoserine +Q04272 YMR077C VPS20 2 N-myristoyl +P39702 YAL002W VPS8 1 N-acetylmethionine +P38329 YBR235W VHC1 34 Phosphoserine +P38329 YBR235W VHC1 654 Phosphoserine +P38329 YBR235W VHC1 915 Phosphoserine +P38329 YBR235W VHC1 918 Phosphoserine +P40522 YIL056W VHR1 409 Phosphoserine +Q08438 YOR054C VHS3 90 Phosphothreonine +P53285 YGR141W VPS62 74 N-linked +P53285 YGR141W VPS62 145 N-linked +Q06525 YPR152C URN1 150 Phosphoserine +Q12132 YPL230W USV1 162 Phosphoserine +Q12132 YPL230W USV1 163 Phosphoserine +P53950 YNL054W VAC7 164 Phosphoserine +P53950 YNL054W VAC7 1020 N-linked +P53950 YNL054W VAC7 1099 N-linked +P47161 YJR126C VPS70 55 N-linked +P47161 YJR126C VPS70 237 N-linked +P47161 YJR126C VPS70 568 N-linked +P47161 YJR126C VPS70 599 N-linked +P47161 YJR126C VPS70 670 N-linked +P37370 YLR337C VRP1 519 Phosphoserine +P37370 YLR337C VRP1 762 Phosphoserine +P37370 YLR337C VRP1 109 N-linked +P37370 YLR337C VRP1 212 N-linked +P37370 YLR337C VRP1 337 N-linked +P37370 YLR337C VRP1 383 N-linked +P37370 YLR337C VRP1 784 N-linked +P37370 YLR337C VRP1 796 N-linked +Q03631 YML076C WAR1 128 Phosphothreonine +P31412 YKL080W VMA5 2 N-acetylalanine +P22203 YOR332W VMA4 2 N-acetylserine +Q04301 YMR088C VBA1 123 N-linked +Q04301 YMR088C VBA1 324 N-linked +Q04301 YMR088C VBA1 504 N-linked +P25594 YCL069W VBA3 195 N-linked +P53262 YGR106C VOA1 69 N-linked +P53262 YGR106C VOA1 104 N-linked +P53262 YGR106C VOA1 172 N-linked +P32563 YOR270C VPH1 2 N-acetylalanine +P38959 YDR080W VPS41 26 Phosphoserine +P38959 YDR080W VPS41 53 Phosphoserine +Q12071 YDR027C VPS54 69 Phosphoserine +Q12071 YDR027C VPS54 72 Phosphoserine +Q12071 YDR027C VPS54 74 Phosphothreonine +P47111 YJR044C VPS55 137 Phosphoserine +Q12016 YOL129W VPS68 1 N-acetylmethionine +Q12016 YOL129W VPS68 8 Phosphoserine +Q12016 YOL129W VPS68 52 N-linked +Q06385 YDR372C VPS74 14 Phosphoserine +Q06385 YDR372C VPS74 19 Phosphoserine +Q07655 YDL224C WHI4 22 Phosphoserine +Q07655 YDL224C WHI4 206 Phosphoserine +Q07655 YDL224C WHI4 258 Phosphoserine +Q07655 YDL224C WHI4 283 Phosphoserine +P42839 YNL321W VNX1 26 Phosphothreonine +P42839 YNL321W VNX1 32 Phosphoserine +P42839 YNL321W VNX1 33 Phosphothreonine +P42839 YNL321W VNX1 110 Phosphoserine +P42839 YNL321W VNX1 118 Phosphothreonine +P42839 YNL321W VNX1 121 Phosphoserine +P42839 YNL321W VNX1 361 N-linked +P39904 YDR484W VPS52 602 Phosphoserine +P54787 YML097C VPS9 375 Phosphoserine +Q06263 YLR181C VTA1 183 Phosphoserine +Q06263 YLR181C VTA1 195 Phosphothreonine +Q06263 YLR181C VTA1 233 Phosphoserine +P47165 YJR133W XPT1 79 Phosphoserine +P53076 YGL227W VID30 2 N-acetylserine +P53076 YGL227W VID30 147 Phosphoserine +P53076 YGL227W VID30 246 Phosphoserine +P53076 YGL227W VID30 248 Phosphoserine +P53076 YGL227W VID30 277 Phosphoserine +P22219 YBR097W VPS15 2 N-myristoyl +P21576 YKR001C VPS1 579 Phosphoserine +P21576 YKR001C VPS1 599 Phosphoserine +Q04338 YMR197C VTI1 2 N-acetylserine +Q04338 YMR197C VTI1 110 Phosphoserine +Q04338 YMR197C VTI1 149 Phosphoserine +P40438 YIL173W VTH1 479 N-linked +P40438 YIL173W VTH1 769 N-linked +P40438 YIL173W VTH1 986 N-linked +P40890 YJL222W VTH2 479 N-linked +P40890 YJL222W VTH2 769 N-linked +P40890 YJL222W VTH2 986 N-linked +P34761 YNL197C WHI3 231 Phosphoserine +P40463 YIL135C VHS2 53 Phosphoserine +P40463 YIL135C VHS2 61 Phosphoserine +P40463 YIL135C VHS2 102 Phosphoserine +P40463 YIL135C VHS2 172 Phosphoserine +P40463 YIL135C VHS2 299 Phosphoserine +P40463 YIL135C VHS2 301 Phosphoserine +P40463 YIL135C VHS2 303 Phosphoserine +P40463 YIL135C VHS2 325 Phosphoserine +Q07878 YLL040C VPS13 1364 Phosphoserine +Q07878 YLL040C VPS13 1382 Phosphoserine +Q07878 YLL040C VPS13 1715 Phosphoserine +Q07878 YLL040C VPS13 1729 Phosphoserine +Q07878 YLL040C VPS13 1731 Phosphoserine +Q03390 YDR486C VPS60 12 Phosphoserine +P53853 YNL246W VPS75 3 Phosphoserine +Q12215 YOL105C WSC3 84 N-linked +Q12215 YOL105C WSC3 367 N-linked +Q12215 YOL105C WSC3 370 N-linked +P38739 YHL028W WSC4 340 N-linked +P38739 YHL028W WSC4 386 N-linked +P38739 YHL028W WSC4 389 N-linked +P38739 YHL028W WSC4 398 N-linked +P38739 YHL028W WSC4 479 N-linked +P38739 YHL028W WSC4 553 N-linked +P38739 YHL028W WSC4 583 N-linked +P43582 YFL010C WWM1 75 Phosphoserine +P43582 YFL010C WWM1 78 Phosphothreonine +P43582 YFL010C WWM1 50 Glycyl +P43582 YFL010C WWM1 60 Glycyl +P53241 YGR065C VHT1 32 Phosphoserine +P53241 YGR065C VHT1 33 Phosphoserine +P53241 YGR065C VHT1 43 Phosphoserine +P40547 YIL017C VID28 226 Phosphoserine +P38735 YHL035C VMR1 11 N-linked +P38735 YHL035C VMR1 370 N-linked +P20795 YLR396C VPS33 626 Phosphoserine +P34110 YJL154C VPS35 846 Phosphoserine +P34110 YJL154C VPS35 848 Phosphoserine +P34110 YJL154C VPS35 868 Phosphoserine +Q02725 YPL019C VTC3 43 Phosphoserine +Q02725 YPL019C VTC3 45 Phosphoserine +Q02725 YPL019C VTC3 50 Phosphoserine +Q02725 YPL019C VTC3 183 Phosphothreonine +Q02725 YPL019C VTC3 195 Phosphoserine +Q02725 YPL019C VTC3 198 Phosphoserine +Q02725 YPL019C VTC3 270 Phosphoserine +Q02725 YPL019C VTC3 274 Phosphoserine +Q02725 YPL019C VTC3 589 Phosphoserine +Q02725 YPL019C VTC3 592 Phosphoserine +Q02725 YPL019C VTC3 621 Phosphoserine +Q02725 YPL019C VTC3 622 Phosphoserine +P47075 YJL012C VTC4 75 Glycyl +Q12416 YOR083W WHI5 47 Phosphothreonine +Q12416 YOR083W WHI5 57 Phosphothreonine +Q12416 YOR083W WHI5 59 Phosphoserine +Q12416 YOR083W WHI5 62 Phosphoserine +Q12416 YOR083W WHI5 88 Phosphoserine +Q12416 YOR083W WHI5 113 Phosphoserine +Q12416 YOR083W WHI5 115 Phosphoserine +Q12416 YOR083W WHI5 154 Phosphoserine +Q12416 YOR083W WHI5 156 Phosphoserine +Q12416 YOR083W WHI5 161 Phosphoserine +Q12416 YOR083W WHI5 262 Phosphoserine +Q12416 YOR083W WHI5 288 Phosphoserine +Q12416 YOR083W WHI5 290 Phosphothreonine +Q12363 YOR230W WTM1 187 Phosphothreonine +Q12363 YOR230W WTM1 200 Phosphoserine +Q12363 YOR230W WTM1 370 Phosphothreonine +Q12363 YOR230W WTM1 406 Phosphothreonine +P36095 YKL041W VPS24 203 Glycyl +P40343 YNR006W VPS27 157 Phosphoserine +P40343 YNR006W VPS27 495 Phosphoserine +P40343 YNR006W VPS27 613 Phosphoserine +P40343 YNR006W VPS27 294 Glycyl +P36116 YKR020W VPS51 2 N-acetylalanine +Q03388 YDR485C VPS72 425 Phosphoserine +P40046 YER072W VTC1 2 N-acetylserine +P43585 YFL004W VTC2 182 Phosphoserine +P43585 YFL004W VTC2 187 Phosphoserine +P43585 YFL004W VTC2 196 Phosphoserine +P43585 YFL004W VTC2 264 Phosphoserine +P43585 YFL004W VTC2 583 Phosphoserine +P43585 YFL004W VTC2 615 Phosphoserine +P43585 YFL004W VTC2 616 Phosphoserine +P43585 YFL004W VTC2 620 Phosphothreonine +P43585 YFL004W VTC2 626 Phosphoserine +P43585 YFL004W VTC2 657 Phosphoserine +P53832 YNL283C WSC2 402 Phosphothreonine +P53832 YNL283C WSC2 455 Phosphoserine +P53832 YNL283C WSC2 458 Phosphoserine +P42826 YGR194C XKS1 244 Phosphoserine +P33301 YDR369C XRS2 349 Phosphoserine +P33301 YDR369C XRS2 533 Phosphoserine +P33301 YDR369C XRS2 534 Phosphoserine +P33301 YDR369C XRS2 553 Phosphoserine +P33301 YDR369C XRS2 555 Phosphothreonine +Q02792 YOR048C RAT1 574 Phosphoserine +P30822 YGR218W CRM1 1080 Phosphoserine +P36017 YOR089C VPS21 188 Phosphoserine +P36017 YOR089C VPS21 210 Cysteine +P36017 YOR089C VPS21 208 S-geranylgeranyl +P36017 YOR089C VPS21 210 S-geranylgeranyl +Q03897 YDR128W MTC5 759 Phosphoserine +P32386 YLL048C YBT1 936 Phosphoserine +P32386 YLL048C YBT1 940 Phosphoserine +P32386 YLL048C YBT1 955 Phosphoserine +P32386 YLL048C YBT1 6 N-linked +P32386 YLL048C YBT1 97 N-linked +P25349 YCR004C YCP4 244 Cysteine +P25349 YCR004C YCP4 243 S-palmitoyl +P25349 YCR004C YCP4 244 S-farnesyl +P34225 YBL060W YEL1 290 Phosphothreonine +P34225 YBL060W YEL1 293 Phosphoserine +P34225 YBL060W YEL1 299 Phosphoserine +Q92393 YOR142W-B TY1B-OR 416 Phosphoserine +P53049 YGR281W YOR1 10 Phosphoserine +P53049 YGR281W YOR1 24 Phosphoserine +P53049 YGR281W YOR1 53 Phosphothreonine +P53049 YGR281W YOR1 661 N-linked +P53049 YGR281W YOR1 759 N-linked +P53049 YGR281W YOR1 799 N-linked +P18961 YMR104C YPK2 63 Phosphothreonine +P18961 YMR104C YPK2 66 Phosphothreonine +P18961 YMR104C YPK2 72 Phosphoserine +P18961 YMR104C YPK2 499 Phosphothreonine +P18961 YMR104C YPK2 501 Phosphothreonine%3B +P18961 YMR104C YPK2 641 Phosphoserine%3B +P18961 YMR104C YPK2 650 Phosphoserine +P18961 YMR104C YPK2 659 Phosphothreonine%3B +P18961 YMR104C YPK2 669 Phosphoserine +P32939 YML001W YPT7 208 Cysteine +P32939 YML001W YPT7 206 S-geranylgeranyl +P32939 YML001W YPT7 208 S-geranylgeranyl +P32939 YML001W YPT7 147 Glycyl +P36036 YKL214C YRA2 1 N-acetylmethionine +P38079 YBR054W YRO2 293 Phosphoserine +P38079 YBR054W YRO2 341 Phosphothreonine +P38079 YBR054W YRO2 343 Phosphoserine +P38079 YBR054W YRO2 286 Glycyl +P39109 YDR135C YCF1 251 Phosphoserine +P39109 YDR135C YCF1 873 Phosphoserine +P39109 YDR135C YCF1 903 Phosphoserine +P39109 YDR135C YCF1 908 Phosphoserine +P39109 YDR135C YCF1 911 Phosphothreonine +P39109 YDR135C YCF1 914 Phosphoserine +Q12316 YGR161C-D TY1B-GR3 416 Phosphoserine +Q12222 YOL128C YGK3 211 Phosphoserine +Q99219 YIL082W TY3A-I 2 N-acetylserine +P53845 YNL263C YIF1 2 N-acetylserine +P47098 YJR027W TY1B-JR1 416 Phosphoserine +P36015 YKL196C YKT6 158 Phosphothreonine +P36015 YKL196C YKT6 197 Cysteine +P36015 YKL196C YKT6 196 S-palmitoyl +P36015 YKL196C YKT6 197 S-farnesyl +Q06328 YDR352W YPQ2 136 Phosphoserine +P40583 YIR039C YPS6 515 GPI-anchor +P40583 YIR039C YPS6 57 N-linked +P40583 YIR039C YPS6 149 N-linked +P40583 YIR039C YPS6 156 N-linked +P40583 YIR039C YPS6 161 N-linked +P40583 YIR039C YPS6 183 N-linked +P40583 YIR039C YPS6 195 N-linked +P40583 YIR039C YPS6 311 N-linked +P40583 YIR039C YPS6 363 N-linked +P40583 YIR039C YPS6 375 N-linked +P40583 YIR039C YPS6 379 N-linked +P40583 YIR039C YPS6 472 N-linked +P48559 YNL304W YPT11 415 S-geranylgeranyl +P48559 YNL304W YPT11 416 S-geranylgeranyl +P51996 YGL210W YPT32 2 N-acetylserine +P51996 YGL210W YPT32 221 S-geranylgeranyl +P51996 YGL210W YPT32 222 S-geranylgeranyl +P40517 YIL063C YRB2 31 Phosphothreonine +P40517 YIL063C YRB2 179 Phosphoserine +P50111 YMR273C ZDS1 229 Phosphoserine +P0CX65 YDR316W-A TY1A-DR5 416 Phosphoserine +Q99315 YGR109W-B TY3B-G 2 N-acetylserine +P47100 YJR029W TY1B-JR2 416 Phosphoserine +P0CX68 YLR035C-B TY1A-LR1 416 Phosphoserine +P0CX59 YOR142W-A TY1A-OR 416 Phosphoserine +P0C2I9 YPR137C-B TY1B-PR1 416 Phosphoserine +P0C2J1 YPR158C-D TY1B-PR3 416 Phosphoserine +P43587 YFR003C YPI1 2 N-acetylserine +P43587 YFR003C YPI1 22 Phosphoserine +P43587 YFR003C YPI1 133 Phosphoserine +P36019 YNL093W YPT53 220 Cysteine +P36019 YNL093W YPT53 218 S-geranylgeranyl +P36019 YNL093W YPT53 220 S-geranylgeranyl +P0CX57 YAR010C TY1A-A 416 Phosphoserine +P38749 YHL009C YAP3 135 Phosphoserine +Q12217 YBR012W-A TY1A-BR 416 Phosphoserine +Q12193 YBR012W-B TY1B-BR 416 Phosphoserine +Q12235 YLL055W YCT1 500 Phosphoserine +Q12235 YLL055W YCT1 501 Phosphoserine +Q12235 YLL055W YCT1 146 N-linked +Q03855 YDR098C-B TY1B-DR1 416 Phosphoserine +P0CX66 YER159C-A TY1A-ER2 416 Phosphoserine +P40028 YER041W YEN1 730 Phosphoserine +P40028 YER041W YEN1 731 Phosphoserine +Q12141 YGR027W-B TY1B-GR1 416 Phosphoserine +P0CX72 YLR157C-A TY1A-LR2 416 Phosphoserine +Q12441 YDR210C-C TY1A-DR3 416 Phosphoserine +Q99231 YDR210C-D TY1B-DR3 416 Phosphoserine +P0CX71 YER137C-A TY1A-ER1 416 Phosphoserine +P0C2I7 YLR256W-B/YLR256W-C TY1B-LR4 416 Phosphoserine +Q12402 YPR028W YOP1 2 N-acetylserine +Q6Q5H1 YPR158C-C TY1A-PR3 416 Phosphoserine +Q07688 YDL235C YPD1 64 Phosphohistidine +Q04116 YDR451C YHP1 315 Phosphoserine +P40017 YER024W YAT2 2 N-acetylserine +P40017 YER024W YAT2 783 Phosphoserine +P42937 YGR203W YCH1 1 N-acetylmethionine +P0CX67 YGR161C-C TY1A-GR3 416 Phosphoserine +P0CX74 YJR026W TY1A-JR1 416 Phosphoserine +P40544 YIL023C YKE4 184 N-linked +P40544 YIL023C YKE4 274 N-linked +P40544 YIL023C YKE4 285 N-linked +P0C2I3 YDR365W-B TY1B-DR6 416 Phosphoserine +Q12085 YGR027W-A TY1A-GR1 416 Phosphoserine +Q12485 YGR038C-A TY1A-GR2 416 Phosphoserine +Q12269 YGR038C-B TY1B-GR2 416 Phosphoserine +P0C2I6 YLR227W-B TY1B-LR3 416 Phosphoserine +P0CX76 YML040W TY1A-ML2 416 Phosphoserine +P38806 YHR090C YNG2 183 Phosphoserine +P38806 YHR090C YNG2 185 Phosphothreonine +P38806 YHR090C YNG2 188 Phosphoserine +P0CX73 YPL257W-A TY1A-PL 416 Phosphoserine +P0CX58 YPR137C-A TY1A-PR1 416 Phosphoserine +Q07950 YLR020C YEH2 73 Phosphoserine +Q07950 YLR020C YEH2 107 Phosphoserine +P25637 YCR059C YIH1 187 Glycyl +P53108 YGL161C YIP5 60 Phosphoserine +Q03434 YML039W TY1B-ML2 416 Phosphoserine +P38070 YBR028C YPK3 90 Phosphoserine +P38070 YBR028C YPK3 105 Phosphoserine +P38070 YBR028C YPK3 107 Phosphothreonine +P38070 YBR028C YPK3 321 Phosphoserine%3B +P38070 YBR028C YPK3 490 Phosphothreonine%3B +P38070 YBR028C YPK3 513 Phosphoserine%3B +P53057 YGL259W YPS5 57 N-linked +P38815 YHR105W YPT35 65 Phosphoserine +P38815 YHR105W YPT35 66 Phosphoserine +Q99260 YLR262C YPT6 215 Cysteine +Q99260 YLR262C YPT6 213 S-geranylgeranyl +Q99260 YLR262C YPT6 215 S-geranylgeranyl +P31111 YDR285W ZIP1 481 Phosphoserine +P40021 YER033C ZRG8 275 Phosphoserine +P40021 YER033C ZRG8 354 Phosphoserine +P40021 YER033C ZRG8 403 Phosphoserine +P40021 YER033C ZRG8 407 Phosphoserine +P40021 YER033C ZRG8 632 Phosphoserine +P40021 YER033C ZRG8 676 Phosphoserine +Q12512 YOL154W ZPS1 28 N-linked +Q12512 YOL154W ZPS1 57 N-linked +Q12512 YOL154W ZPS1 98 N-linked +Q12512 YOL154W ZPS1 217 N-linked +Q06325 YDR349C YPS7 26 N-linked +Q06325 YDR349C YPS7 59 N-linked +Q06325 YDR349C YPS7 106 N-linked +Q06325 YDR349C YPS7 131 N-linked +Q06325 YDR349C YPS7 140 N-linked +Q06325 YDR349C YPS7 143 N-linked +Q06325 YDR349C YPS7 148 N-linked +Q06325 YDR349C YPS7 175 N-linked +Q06325 YDR349C YPS7 308 N-linked +Q06325 YDR349C YPS7 391 N-linked +Q06325 YDR349C YPS7 455 N-linked +Q06325 YDR349C YPS7 478 N-linked +Q06325 YDR349C YPS7 484 N-linked +Q06325 YDR349C YPS7 549 N-linked +Q06325 YDR349C YPS7 552 N-linked +P38146 YBR264C YPT10 199 Cysteine +P38146 YBR264C YPT10 197 S-geranylgeranyl +P38146 YBR264C YPT10 199 S-geranylgeranyl +P38555 YER031C YPT31 2 N-acetylserine +P38555 YER031C YPT31 222 S-geranylgeranyl +P38555 YER031C YPT31 223 S-geranylgeranyl +P36018 YKR014C YPT52 139 Phosphoserine +P36018 YKR014C YPT52 142 Phosphoserine +P36018 YKR014C YPT52 232 S-geranylgeranyl +P36018 YKR014C YPT52 233 S-geranylgeranyl +P36018 YKR014C YPT52 151 Glycyl +P38280 YBR148W YSW1 159 Phosphoserine +P38280 YBR148W YSW1 160 Phosphoserine +Q12324 YOR087W YVC1 636 Phosphothreonine +P53303 YGR211W ZPR1 23 Phosphoserine +P53303 YGR211W ZPR1 407 Phosphothreonine +P0C2I5 YLR157C-B TY1B-LR2 416 Phosphoserine +Q04670 YMR050C TY1B-MR2 416 Phosphoserine +Q12470 YNL054W-A TY1A-NL2 416 Phosphoserine +Q92392 YOL103W-A TY1A-OL 416 Phosphoserine +P0CX60 YPR158W-A TY1A-PR2 416 Phosphoserine +Q12159 YDR381W YRA1 2 N-acetylserine +Q12159 YDR381W YRA1 8 Phosphoserine +Q12159 YDR381W YRA1 100 Phosphoserine +P53107 YGL164C YRB30 272 Phosphothreonine +Q12436 YLR130C ZRT2 148 Phosphoserine +Q12436 YLR130C ZRT2 149 Phosphoserine +Q12436 YLR130C ZRT2 162 Phosphoserine +Q12436 YLR130C ZRT2 170 Phosphoserine +Q12436 YLR130C ZRT2 188 Phosphothreonine +P32527 YGR285C ZUO1 50 Phosphoserine +P0CX75 YLR227W-A TY1A-LR3 416 Phosphoserine +Q04706 YML045W-A TY1A-ML1 416 Phosphoserine +P0CX69 YMR051C TY1A-MR2 416 Phosphoserine +Q03697 YML038C YMD8 209 Phosphoserine +Q03697 YML038C YMD8 99 N-linked +Q12273 YOL103W-B TY1B-OL 416 Phosphoserine +Q12697 YOR291W YPK9 1 N-acetylmethionine +Q12697 YOR291W YPK9 95 Phosphothreonine +Q12697 YOR291W YPK9 108 Phosphoserine +Q12697 YOR291W YPK9 1117 Phosphoserine +Q12697 YOR291W YPK9 1120 Phosphoserine +Q12303 YLR121C YPS3 483 GPI-anchor +Q12303 YLR121C YPS3 75 N-linked +Q12303 YLR121C YPS3 120 N-linked +Q12303 YLR121C YPS3 160 N-linked +Q12303 YLR121C YPS3 163 N-linked +Q12303 YLR121C YPS3 275 N-linked +Q12303 YLR121C YPS3 309 N-linked +Q12303 YLR121C YPS3 328 N-linked +Q12303 YLR121C YPS3 367 N-linked +Q12303 YLR121C YPS3 422 N-linked +Q12303 YLR121C YPS3 445 N-linked +Q12303 YLR121C YPS3 462 N-linked +P41920 YDR002W YRB1 60 Phosphoserine +Q08245 YOL109W ZEO1 2 N-acetylserine +Q08245 YOL109W ZEO1 2 Phosphoserine +Q08245 YOL109W ZEO1 25 Phosphoserine +Q08245 YOL109W ZEO1 40 Phosphoserine +Q08245 YOL109W ZEO1 49 Phosphothreonine +Q08245 YOL109W ZEO1 18 Glycyl +Q08245 YOL109W ZEO1 23 Glycyl +Q08245 YOL109W ZEO1 29 Glycyl +Q08245 YOL109W ZEO1 34 Glycyl +Q08245 YOL109W ZEO1 45 Glycyl +Q08245 YOL109W ZEO1 57 Glycyl +Q08245 YOL109W ZEO1 82 Glycyl +P32329 YLR120C YPS1 548 GPI-anchor +P32329 YLR120C YPS1 95 N-linked +P32329 YLR120C YPS1 203 N-linked +P32329 YLR120C YPS1 232 N-linked +P32329 YLR120C YPS1 242 N-linked +P32329 YLR120C YPS1 245 N-linked +P32329 YLR120C YPS1 299 N-linked +P32329 YLR120C YPS1 358 N-linked +P32329 YLR120C YPS1 480 N-linked +P32329 YLR120C YPS1 522 N-linked +P32329 YLR120C YPS1 532 N-linked +P01123 YFL038C YPT1 1 N-acetylmethionine +P01123 YFL038C YPT1 172 Phosphoserine +P01123 YFL038C YPT1 174 Phosphoserine +P01123 YFL038C YPT1 23 S-palmitoyl +P01123 YFL038C YPT1 123 S-palmitoyl +P01123 YFL038C YPT1 205 S-geranylgeranyl +P01123 YFL038C YPT1 206 S-geranylgeranyl +P01123 YFL038C YPT1 144 Glycyl +P47043 YJL056C ZAP1 156 Phosphoserine +P47043 YJL056C ZAP1 166 Phosphoserine +P47043 YJL056C ZAP1 515 Phosphoserine +P54786 YML109W ZDS2 50 Phosphoserine +P35723 YKL065C YET1 190 Glycyl +Q12173 YGR109W-A TY3A-G 2 N-acetylserine +P38616 YNL160W YGP1 40 N-linked +P38616 YNL160W YGP1 50 N-linked +P38616 YNL160W YGP1 53 N-linked +P38616 YNL160W YGP1 58 N-linked +P38616 YNL160W YGP1 61 N-linked +P38616 YNL160W YGP1 65 N-linked +P38616 YNL160W YGP1 87 N-linked +P38616 YNL160W YGP1 94 N-linked +P38616 YNL160W YGP1 100 N-linked +P38616 YNL160W YGP1 106 N-linked +P38616 YNL160W YGP1 118 N-linked +P38616 YNL160W YGP1 172 N-linked +P38616 YNL160W YGP1 239 N-linked +P38616 YNL160W YGP1 286 N-linked +P47099 YJR028W TY1A-JR2 416 Phosphoserine +P0C2I8 YLR256W-A TY1A-LR4 416 Phosphoserine +Q12414 YPL257W-B TY1B-PL 416 Phosphoserine +Q12010 YOL092W YPQ1 9 N-linked +Q12010 YOL092W YPQ1 189 N-linked +Q12010 YOL092W YPQ1 275 N-linked +P32793 YHR016C YSC84 301 Phosphoserine +P32793 YHR016C YSC84 311 Phosphoserine +P26725 YJL139C YUR1 77 N-linked +P26725 YJL139C YUR1 82 N-linked +P26725 YJL139C YUR1 92 N-linked +P26725 YJL139C YUR1 167 N-linked +P26725 YJL139C YUR1 414 N-linked +P53735 YNR039C ZRG17 16 Phosphoserine +P53735 YNR039C ZRG17 131 Phosphoserine +P53735 YNR039C ZRG17 498 Phosphoserine +P20107 YMR243C ZRC1 387 Phosphoserine +P20107 YMR243C ZRC1 393 Phosphoserine +P20107 YMR243C ZRC1 397 Phosphoserine +P20107 YMR243C ZRC1 357 Glycyl +P34240 YKL175W ZRT3 178 Phosphoserine +P34240 YKL175W ZRT3 188 Phosphoserine +Q06681 YDR326C YSP2 13 Phosphoserine +Q06681 YDR326C YSP2 411 Phosphoserine +Q06681 YDR326C YSP2 596 Phosphoserine +Q06681 YDR326C YSP2 1032 Phosphoserine +Q06681 YDR326C YSP2 1306 N-linked +Q06681 YDR326C YSP2 1373 N-linked +Q06681 YDR326C YSP2 1430 N-linked +P15891 YCR088W ABP1 2 N-acetylalanine +P15891 YCR088W ABP1 165 Phosphothreonine +P15891 YCR088W ABP1 167 Phosphoserine +P15891 YCR088W ABP1 169 Phosphoserine +P15891 YCR088W ABP1 181 Phosphothreonine +P15891 YCR088W ABP1 183 Phosphoserine +P15891 YCR088W ABP1 313 Phosphoserine +P15891 YCR088W ABP1 365 Phosphoserine +P15891 YCR088W ABP1 389 Phosphoserine +P15891 YCR088W ABP1 458 Phosphoserine +P15891 YCR088W ABP1 481 Phosphoserine +P15891 YCR088W ABP1 464 Glycyl +P32316 YBL015W ACH1 2 N-acetylthreonine +P32316 YBL015W ACH1 350 Phosphoserine +Q00362 YGL190C CDC55 124 Phosphoserine +P47096 YJR025C BNA1 176 Phosphoserine +P32357 YBL074C AAR2 253 Phosphoserine +P32357 YBL074C AAR2 274 Phosphothreonine +P32357 YBL074C AAR2 328 Phosphotyrosine +P32357 YBL074C AAR2 331 Phosphoserine +P32357 YBL074C AAR2 345 Phosphothreonine +P07248 YDR216W ADR1 54 Phosphoserine +P07248 YDR216W ADR1 188 Phosphothreonine +P07248 YDR216W ADR1 193 Phosphothreonine +P07248 YDR216W ADR1 230 Phosphoserine%3B +P07248 YDR216W ADR1 258 Phosphoserine +P07248 YDR216W ADR1 259 Phosphothreonine +P07248 YDR216W ADR1 299 Phosphoserine +P07248 YDR216W ADR1 323 Phosphoserine +P07248 YDR216W ADR1 325 Phosphoserine +P07248 YDR216W ADR1 327 Phosphothreonine +P38903 YOR014W RTS1 242 Phosphothreonine +P38903 YOR014W RTS1 257 Phosphothreonine +P47129 YJR083C ACF4 44 Phosphoserine +P47129 YJR083C ACF4 71 Phosphoserine +P47129 YJR083C ACF4 74 Phosphoserine +P47129 YJR083C ACF4 78 Phosphoserine +P47129 YJR083C ACF4 165 Phosphoserine +P47129 YJR083C ACF4 288 Phosphoserine +P14164 YKL112W ABF1 189 Phosphothreonine +P14164 YKL112W ABF1 193 Phosphoserine +P14164 YKL112W ABF1 467 Phosphoserine +P14164 YKL112W ABF1 554 Phosphoserine +P14164 YKL112W ABF1 618 Phosphoserine +P14164 YKL112W ABF1 624 Phosphoserine%3B +P14164 YKL112W ABF1 720 Phosphoserine%3B +P14164 YKL112W ABF1 18 Glycyl +P40535 YIL036W CST6 171 Phosphoserine +P40535 YIL036W CST6 179 Phosphoserine +P40535 YIL036W CST6 399 Phosphoserine +P40535 YIL036W CST6 557 Phosphoserine +P40535 YIL036W CST6 559 Phosphothreonine +P31787 YGR037C ACB1 51 Glycyl +P31787 YGR037C ACB1 72 Glycyl +P32323 YNR044W AGA1 699 GPI-anchor +Q12471 YOL136C PFK27 55 Glycyl +P23542 YLR027C AAT2 2 N-acetylserine +P23542 YLR027C AAT2 255 N6-(pyridoxal +P23542 YLR027C AAT2 389 Phosphoserine +Q07622 YDL203C ACK1 184 Glycyl +Q07622 YDL203C ACK1 191 Glycyl +Q03771 YDR161W ACL4 2 N-acetylserine +P21192 YLR131C ACE2 80 Phosphoserine +P21192 YLR131C ACE2 122 Phosphoserine +P21192 YLR131C ACE2 247 Phosphoserine +P21192 YLR131C ACE2 249 Phosphoserine +P21192 YLR131C ACE2 253 Phosphoserine +P21192 YLR131C ACE2 259 Phosphothreonine +P21192 YLR131C ACE2 385 Phosphoserine +P21192 YLR131C ACE2 392 Phosphoserine +P21192 YLR131C ACE2 483 Phosphoserine +P21192 YLR131C ACE2 486 Phosphothreonine +P21192 YLR131C ACE2 501 Phosphothreonine +P21192 YLR131C ACE2 564 Phosphoserine +P21192 YLR131C ACE2 709 Phosphoserine +P21192 YLR131C ACE2 714 Phosphoserine +P28240 YER065C ICL1 53 Phosphothreonine +P38720 YHR183W GND1 50 Phosphoserine +Q01802 YKL106W AAT1 286 N6-(pyridoxal +Q08641 YOR239W ABP140 93 Phosphoserine +Q08641 YOR239W ABP140 150 Phosphothreonine +Q08641 YOR239W ABP140 321 Phosphoserine +Q08641 YOR239W ABP140 326 Phosphoserine +Q08641 YOR239W ABP140 347 Phosphothreonine +P40433 YIL107C PFK26 92 Phosphoserine +P40433 YIL107C PFK26 157 Phosphothreonine +P40433 YIL107C PFK26 644 Phosphoserine +P40433 YIL107C PFK26 652 Phosphoserine +P40433 YIL107C PFK26 659 Phosphoserine +P40433 YIL107C PFK26 667 Phosphoserine +Q00955 YNR016C ACC1 2 N-acetylserine +Q00955 YNR016C ACC1 2 Phosphoserine +Q00955 YNR016C ACC1 735 N6-biotinyllysine +Q00955 YNR016C ACC1 790 Phosphoserine +Q00955 YNR016C ACC1 1148 Phosphoserine +Q00955 YNR016C ACC1 1157 Phosphoserine +Q00955 YNR016C ACC1 1162 Phosphoserine +P40529 YIL044C AGE2 2 N-acetylserine +P40529 YIL044C AGE2 180 Phosphoserine +P40529 YIL044C AGE2 183 Phosphoserine +P40529 YIL044C AGE2 207 Phosphoserine +P46680 YMR092C AIP1 2 N-acetylserine +P52893 YLR089C ALT1 77 Phosphoserine +P52893 YLR089C ALT1 412 N6-(pyridoxal +P38065 YBL037W APL3 727 Phosphothreonine +P38065 YBL037W APL3 733 Phosphoserine +P53886 YNL172W APC1 1462 Phosphoserine +P36154 YKR074W AIM29 78 Phosphoserine +P46367 YOR374W ALD4 96 Phosphoserine +P46367 YOR374W ALD4 216 Phosphothreonine +P46367 YOR374W ALD4 500 Phosphoserine +P40350 YPL227C ALG5 83 N-linked +P40350 YPL227C ALG5 119 N-linked +P43633 YGL021W ALK1 76 Phosphoserine +P43633 YGL021W ALK1 79 Phosphoserine +Q08269 YOL130W ALR1 2 N-acetylserine +Q08269 YOL130W ALR1 77 Phosphotyrosine +Q08269 YOL130W ALR1 85 Phosphoserine +Q08269 YOL130W ALR1 185 Phosphoserine +Q08269 YOL130W ALR1 188 Phosphoserine +Q08269 YOL130W ALR1 220 Phosphoserine +Q08269 YOL130W ALR1 221 Phosphoserine +Q08269 YOL130W ALR1 236 Phosphoserine +Q08269 YOL130W ALR1 242 Phosphothreonine +Q08269 YOL130W ALR1 850 Phosphoserine +P14904 YKL103C APE1 356 Phosphoserine +P14904 YKL103C APE1 107 N-linked +P14904 YKL103C APE1 110 N-linked +P14904 YKL103C APE1 448 N-linked +P60010 YFL039C ACT1 1 N-acetylmethionine +P60010 YFL039C ACT1 191 Glycyl +P25371 YCR011C ADP1 659 Phosphoserine +P25371 YCR011C ADP1 702 Phosphoserine +P25371 YCR011C ADP1 50 N-linked +P25371 YCR011C ADP1 114 N-linked +P25371 YCR011C ADP1 165 N-linked +P25371 YCR011C ADP1 221 N-linked +P25371 YCR011C ADP1 935 N-linked +P33304 YDR085C AFR1 472 Phosphoserine +P33304 YDR085C AFR1 526 Phosphoserine +P43636 YGL065C ALG2 170 N-linked +P43636 YGL065C ALG2 303 N-linked +P43636 YGL065C ALG2 371 N-linked +P43636 YGL065C ALG2 400 N-linked +P47029 YJL084C ALY2 155 Phosphoserine +P47029 YJL084C ALY2 162 Phosphoserine +P47029 YJL084C ALY2 213 Phosphoserine +P47029 YJL084C ALY2 586 Phosphoserine +P47029 YJL084C ALY2 826 Phosphoserine +P47029 YJL084C ALY2 838 Phosphoserine +P47029 YJL084C ALY2 900 Phosphoserine +P47029 YJL084C ALY2 1022 Phosphoserine +P47029 YJL084C ALY2 1023 Phosphoserine +P40502 YIL087C AIM19 2 N-acetylserine +P40563 YIR003W AIM21 18 Phosphothreonine +P40563 YIR003W AIM21 36 Phosphoserine +P40563 YIR003W AIM21 58 Phosphothreonine +P40563 YIR003W AIM21 70 Phosphoserine +P40563 YIR003W AIM21 85 Phosphothreonine +P40563 YIR003W AIM21 104 Phosphoserine +P40563 YIR003W AIM21 183 Phosphoserine +P40563 YIR003W AIM21 206 Phosphoserine +P40563 YIR003W AIM21 231 Phosphoserine +P40563 YIR003W AIM21 277 Phosphothreonine +P40563 YIR003W AIM21 284 Phosphoserine +P40563 YIR003W AIM21 324 Phosphoserine +P40563 YIR003W AIM21 552 Phosphothreonine +P40563 YIR003W AIM21 576 Phosphoserine +P40563 YIR003W AIM21 620 Phosphoserine +P40563 YIR003W AIM21 623 Phosphoserine +P40563 YIR003W AIM21 625 Phosphoserine +P40563 YIR003W AIM21 627 Phosphoserine +P40563 YIR003W AIM21 667 Phosphoserine +P40563 YIR003W AIM21 671 Phosphoserine +P40563 YIR003W AIM21 675 Phosphoserine +P40563 YIR003W AIM21 678 Phosphoserine +P16550 YCL050C APA1 60 Phosphothreonine +P00330 YOL086C ADH1 2 N-acetylserine +P00330 YOL086C ADH1 213 Phosphoserine +P00330 YOL086C ADH1 223 Phosphothreonine +P00330 YOL086C ADH1 279 Phosphoserine +P00330 YOL086C ADH1 316 Phosphoserine +P00330 YOL086C ADH1 226 Glycyl +P00330 YOL086C ADH1 234 Glycyl +P00330 YOL086C ADH1 287 Glycyl +P00330 YOL086C ADH1 319 Glycyl +P00331 YMR303C ADH2 2 N-acetylserine +P00331 YMR303C ADH2 213 Phosphoserine +P00331 YMR303C ADH2 223 Phosphothreonine +P00331 YMR303C ADH2 279 Phosphoserine +P00331 YMR303C ADH2 316 Phosphoserine +P00331 YMR303C ADH2 226 Glycyl +P00331 YMR303C ADH2 234 Glycyl +P00331 YMR303C ADH2 287 Glycyl +P00331 YMR303C ADH2 319 Glycyl +Q04894 YMR318C ADH6 131 Phosphoserine +Q04894 YMR318C ADH6 315 Phosphoserine +Q04894 YMR318C ADH6 359 Phosphoserine +P38266 YBR108W AIM3 57 Phosphoserine +P38266 YBR108W AIM3 58 Phosphoserine +P38266 YBR108W AIM3 64 Phosphoserine +P38266 YBR108W AIM3 476 Phosphoserine +P38266 YBR108W AIM3 729 Phosphothreonine +P38266 YBR108W AIM3 861 Phosphothreonine +Q99299 YPL158C AIM44 25 Phosphoserine +P53954 YNL048W ALG11 262 N-linked +P53954 YNL048W ALG11 393 N-linked +P53954 YNL048W ALG11 480 N-linked +P53954 YNL048W ALG11 490 N-linked +P38313 YBR211C AME1 41 Phosphoserine +P38313 YBR211C AME1 45 Phosphoserine +P38313 YBR211C AME1 53 Phosphoserine +P38313 YBR211C AME1 59 Phosphoserine +P38313 YBR211C AME1 101 Phosphoserine +P52910 YLR153C ACS2 679 Phosphoserine +P52910 YLR153C ACS2 506 Glycyl +P25376 YCL025C AGP1 6 Phosphoserine +P25376 YCL025C AGP1 633 S-palmitoyl +P25376 YCL025C AGP1 11 Glycyl +P10869 YER052C HOM3 333 Phosphothreonine +Q08548 YOR175C ALE1 513 Phosphoserine +Q08548 YOR175C ALE1 605 Phosphoserine +Q08548 YOR175C ALE1 610 Phosphoserine +Q08548 YOR175C ALE1 615 Phosphoserine +P36117 YKR021W ALY1 220 Phosphoserine +P38113 YBR145W ADH5 226 Phosphothreonine +P38113 YBR145W ADH5 282 Phosphoserine +P38113 YBR145W ADH5 319 Phosphoserine +P38113 YBR145W ADH5 229 Glycyl +P38113 YBR145W ADH5 237 Glycyl +P38113 YBR145W ADH5 290 Glycyl +Q12013 YOR034C AKR2 534 N-linked +P52892 YDR111C ALT2 327 N6-(pyridoxal +P14540 YKL060C FBA1 11 Phosphothreonine +P14540 YKL060C FBA1 56 Phosphoserine +P14540 YKL060C FBA1 63 Phosphoserine +P14540 YKL060C FBA1 76 Phosphoserine +P14540 YKL060C FBA1 83 Phosphoserine +P14540 YKL060C FBA1 96 Phosphoserine +P14540 YKL060C FBA1 147 Phosphoserine +P14540 YKL060C FBA1 150 Phosphothreonine +P14540 YKL060C FBA1 179 Phosphothreonine +P14540 YKL060C FBA1 268 Phosphoserine +P14540 YKL060C FBA1 290 Phosphothreonine +P14540 YKL060C FBA1 310 Phosphotyrosine +P14540 YKL060C FBA1 313 Phosphoserine +P14540 YKL060C FBA1 27 Glycyl +P14540 YKL060C FBA1 73 Glycyl +P14540 YKL060C FBA1 85 Glycyl +P14540 YKL060C FBA1 308 Glycyl +P50076 YGR227W DIE2 31 N-linked +P50076 YGR227W DIE2 278 N-linked +P50076 YGR227W DIE2 372 N-linked +P32375 YIR027C DAL1 157 N6-carboxylysine +P54783 YML086C ALO1 56 Pros-8alpha-FAD +P38971 YNL270C ALP1 39 Phosphothreonine +Q08981 YPL267W ACM1 48 Phosphoserine +Q08981 YPL267W ACM1 161 Phosphothreonine +Q08981 YPL267W ACM1 202 Phosphoserine +P32463 YKL192C ACP1 82 O-(pantetheine +P25377 YCR105W ADH7 132 Phosphoserine +P25377 YCR105W ADH7 316 Phosphoserine +P32781 YGL032C AGA2 22 O-linked +P32781 YGL032C AGA2 30 O-linked +P32781 YGL032C AGA2 32 O-linked +P32781 YGL032C AGA2 39 O-linked +P32781 YGL032C AGA2 63 O-linked +P32781 YGL032C AGA2 66 O-linked +P32781 YGL032C AGA2 75 O-linked +P38628 YEL058W PCM1 67 Phosphoserine +P43567 YFL030W AGX1 201 N6-(pyridoxal +Q12476 YDL175C AIR2 31 Phosphoserine +Q12476 YDL175C AIR2 49 Phosphoserine +P19414 YLR304C ACO1 391 Phosphoserine +P19414 YLR304C ACO1 409 Phosphothreonine +P19414 YLR304C ACO1 556 Phosphoserine +Q03233 YMR184W ADD37 79 Phosphoserine +Q12433 YOR023C AHC1 282 Phosphoserine +Q12433 YOR023C AHC1 505 Phosphoserine +P38013 YLR109W AHP1 2 N-acetylserine +P38013 YLR109W AHP1 28 Phosphoserine +P38013 YLR109W AHP1 59 Phosphoserine +P38013 YLR109W AHP1 116 Phosphoserine +P38013 YLR109W AHP1 32 Glycyl +P38013 YLR109W AHP1 48 Glycyl +P38013 YLR109W AHP1 113 Glycyl +Q12156 YDR063W AIM7 2 N-acetylserine +Q12156 YDR063W AIM7 137 Phosphoserine +P40507 YIL079C AIR1 37 Phosphoserine +P39010 YDR264C AKR1 51 Phosphoserine +P39010 YDR264C AKR1 57 Phosphoserine +P38840 YHR137W ARO9 90 Phosphoserine +P38840 YHR137W ARO9 92 Phosphoserine +P80428 YJL081C ARP4 349 Phosphoserine +P40467 YIL130W ASG1 166 Phosphoserine%3B +P40467 YIL130W ASG1 186 Phosphoserine +P40467 YIL130W ASG1 963 Phosphoserine +P34233 YKL185W ASH1 56 Phosphoserine +P34233 YKL185W ASH1 465 Phosphoserine +P49435 YML022W APT1 68 Phosphoserine +P18544 YOL140W ARG8 276 N6-(pyridoxal +P53974 YNL020C ARK1 478 Phosphoserine +P53974 YNL020C ARK1 522 Phosphoserine +P53974 YNL020C ARK1 535 Phosphoserine +P38116 YBR164C ARL1 2 N-myristoyl +P40994 YOR094W ARF3 2 N-myristoyl +P53090 YGL202W ARO8 100 Phosphoserine +P32449 YBR249C ARO4 2 N-acetylserine +P53946 YNL059C ARP5 7 Phosphoserine +P53946 YNL059C ARP5 24 Phosphothreonine +P53946 YNL059C ARP5 383 Phosphoserine +P53946 YNL059C ARP5 12 Glycyl +Q12386 YOR141C ARP8 65 Phosphoserine +Q12386 YOR141C ARP8 70 Phosphoserine +P53731 YNR035C ARC35 155 Phosphothreonine +P53731 YNR035C ARC35 324 Phosphoserine +P38986 YDR321W ASP1 350 Phosphoserine +P40024 YER036C ARB1 43 Phosphoserine +P40024 YER036C ARB1 65 Phosphoserine +P40024 YER036C ARB1 196 Phosphoserine +P40024 YER036C ARB1 446 Phosphothreonine +P11076 YDL192W ARF1 2 N-myristoyl +P11076 YDL192W ARF1 127 Glycyl +P00812 YPL111W CAR1 1 N-acetylmethionine +P00812 YPL111W CAR1 16 Phosphoserine +P00812 YPL111W CAR1 77 Phosphothreonine +P00812 YPL111W CAR1 270 Phosphothreonine +P15274 YML035C AMD1 19 Phosphoserine +P15274 YML035C AMD1 58 Phosphoserine +P15274 YML035C AMD1 61 Phosphoserine +P15274 YML035C AMD1 138 Phosphoserine +Q08951 YPL195W APL5 2 N-acetylthreonine +Q08951 YPL195W APL5 700 Phosphoserine +Q08951 YPL195W APL5 727 Phosphoserine +Q08951 YPL195W APL5 767 Phosphothreonine +Q08951 YPL195W APL5 770 Phosphoserine +Q08951 YPL195W APL5 773 Phosphoserine +Q08951 YPL195W APL5 798 Phosphoserine +Q08951 YPL195W APL5 888 Phosphoserine +Q08951 YPL195W APL5 918 Phosphoserine +P36973 YDR441C APT2 2 N-acetylserine +P25628 YCR048W ARE1 21 Phosphoserine +P25628 YCR048W ARE1 45 Phosphoserine +P36090 YKL047W ANR2 511 S-palmitoyl +P36090 YKL047W ANR2 516 S-palmitoyl +P46682 YGR261C APL6 693 Phosphoserine +P46682 YGR261C APL6 698 Phosphoserine +P46682 YGR261C APL6 724 Phosphoserine +P46682 YGR261C APL6 726 Phosphoserine +P04076 YHR018C ARG4 27 Phosphoserine +P38832 YHR126C ANS1 137 GPI-anchor +P37302 YBR286W APE3 85 N-linked +P37302 YBR286W APE3 96 N-linked +P37302 YBR286W APE3 115 N-linked +P37302 YBR286W APE3 150 N-linked +P37302 YBR286W APE3 162 N-linked +P37302 YBR286W APE3 371 N-linked +P37302 YBR286W APE3 427 N-linked +P37302 YBR286W APE3 480 N-linked +P22936 YKL114C APN1 356 Phosphoserine +Q06408 YDR380W ARO10 588 Glycyl +P38080 YBR059C AKL1 2 N-acetylserine +P38080 YBR059C AKL1 10 Phosphoserine +P38080 YBR059C AKL1 407 Phosphoserine +P38080 YBR059C AKL1 471 Phosphothreonine +P38080 YBR059C AKL1 504 Phosphoserine +P38080 YBR059C AKL1 541 Phosphoserine +P38080 YBR059C AKL1 574 Phosphoserine +P38080 YBR059C AKL1 801 Phosphoserine +P38080 YBR059C AKL1 846 Phosphoserine +P38080 YBR059C AKL1 953 Phosphoserine +P38080 YBR059C AKL1 960 Phosphoserine +P38080 YBR059C AKL1 1048 Phosphoserine +P38080 YBR059C AKL1 1072 Phosphoserine +P38080 YBR059C AKL1 1008 Glycyl +P38080 YBR059C AKL1 1046 Glycyl +P54115 YPL061W ALD6 3 Glycyl +P54115 YPL061W ALD6 142 Glycyl +P54115 YPL061W ALD6 196 Glycyl +P16661 YBR110W ALG1 88 N-linked +P16661 YBR110W ALG1 199 N-linked +P16661 YBR110W ALG1 425 N-linked +P19880 YML007W YAP1 9 Phosphoserine +P19880 YML007W YAP1 14 Phosphoserine +P19880 YML007W YAP1 17 Phosphoserine +P19880 YML007W YAP1 165 Phosphothreonine +P19880 YML007W YAP1 204 Phosphoserine +P19880 YML007W YAP1 372 Phosphoserine +P19880 YML007W YAP1 528 Phosphoserine +P27351 YJR005W APL1 649 Phosphoserine +P27351 YJR005W APL1 652 Phosphothreonine +P27351 YJR005W APL1 683 Phosphoserine +Q99186 YOL062C APM4 179 Phosphoserine +Q99186 YOL062C APM4 180 Phosphoserine +Q99186 YOL062C APM4 181 Phosphoserine +P38115 YBR149W ARA1 151 Phosphothreonine +P53309 YGR241C YAP1802 449 Phosphothreonine +P53309 YGR241C YAP1802 282 Glycyl +P13586 YGL167C PMR1 2 N-acetylserine +P13586 YGL167C PMR1 227 Phosphoserine +Q12675 YDR093W DNF2 70 Phosphothreonine +Q12675 YDR093W DNF2 85 Phosphoserine +Q12675 YDR093W DNF2 389 Phosphoserine +Q12675 YDR093W DNF2 392 Phosphoserine +Q12675 YDR093W DNF2 396 Phosphoserine +Q12675 YDR093W DNF2 403 Phosphoserine +Q12675 YDR093W DNF2 406 Phosphotyrosine +Q12675 YDR093W DNF2 782 Phosphothreonine +Q12675 YDR093W DNF2 1542 Phosphoserine +Q12675 YDR093W DNF2 1592 Phosphoserine +Q12675 YDR093W DNF2 938 Glycyl +P40527 YIL048W NEO1 102 Phosphoserine +P40527 YIL048W NEO1 551 Phosphoserine +P38316 YBR217W ATG12 186 Glycyl +Q06628 YPR185W ATG13 344 Phosphoserine%3B +Q06628 YPR185W ATG13 348 Phosphoserine%3B +Q06628 YPR185W ATG13 355 Phosphoserine +Q06628 YPR185W ATG13 437 Phosphoserine%3B +Q06628 YPR185W ATG13 438 Phosphoserine%3B +Q06628 YPR185W ATG13 461 Phosphoserine +Q06628 YPR185W ATG13 496 Phosphoserine%3B +Q06628 YPR185W ATG13 535 Phosphoserine%3B +Q06628 YPR185W ATG13 541 Phosphoserine%3B +Q06628 YPR185W ATG13 554 Phosphoserine +Q06628 YPR185W ATG13 581 Phosphoserine%3B +Q06628 YPR185W ATG13 646 Phosphoserine%3B +Q06628 YPR185W ATG13 649 Phosphoserine%3B +P21306 YPL271W ATP15 52 Phosphothreonine +P00830 YJR121W ATP2 112 Phosphothreonine +P00830 YJR121W ATP2 237 Phosphothreonine +P00830 YJR121W ATP2 373 Phosphoserine +P05626 YPL078C ATP4 144 Phosphoserine +Q07528 YDL113C ATG20 2 N-acetylserine +Q07528 YDL113C ATG20 361 Phosphoserine +Q07528 YDL113C ATG20 363 Phosphoserine +P48016 YPR026W ATH1 28 N-linked +P48016 YPR026W ATH1 32 N-linked +P48016 YPR026W ATH1 98 N-linked +P48016 YPR026W ATH1 207 N-linked +P48016 YPR026W ATH1 238 N-linked +P48016 YPR026W ATH1 247 N-linked +P48016 YPR026W ATH1 255 N-linked +P48016 YPR026W ATH1 259 N-linked +P48016 YPR026W ATH1 325 N-linked +P48016 YPR026W ATH1 370 N-linked +P48016 YPR026W ATH1 376 N-linked +P48016 YPR026W ATH1 488 N-linked +P48016 YPR026W ATH1 539 N-linked +P48016 YPR026W ATH1 568 N-linked +P48016 YPR026W ATH1 628 N-linked +P48016 YPR026W ATH1 638 N-linked +P48016 YPR026W ATH1 696 N-linked +P48016 YPR026W ATH1 705 N-linked +P48016 YPR026W ATH1 879 N-linked +P48016 YPR026W ATH1 897 N-linked +P48016 YPR026W ATH1 910 N-linked +P48016 YPR026W ATH1 972 N-linked +P48016 YPR026W ATH1 990 N-linked +P48016 YPR026W ATH1 1031 N-linked +P48016 YPR026W ATH1 1049 N-linked +P48016 YPR026W ATH1 1064 N-linked +P48016 YPR026W ATH1 1147 N-linked +P48016 YPR026W ATH1 1157 N-linked +Q12233 YPR020W ATP20 1 N-acetylmethionine +Q12233 YPR020W ATP20 3 Phosphoserine +Q12233 YPR020W ATP20 62 Phosphoserine +Q12500 YLR114C AVL9 519 Phosphoserine +Q12500 YLR114C AVL9 524 Phosphoserine +Q05933 YLR370C ARC18 29 Glycyl +P0CX79 YLR160C ASP3-4 29 N-linked +P0CX79 YLR160C ASP3-4 93 N-linked +P0CX79 YLR160C ASP3-4 239 N-linked +P25641 YCR068W ATG15 173 N-linked +P25641 YCR068W ATG15 202 N-linked +P25641 YCR068W ATG15 208 N-linked +P35193 YOL082W ATG19 136 Phosphoserine +P35193 YOL082W ATG19 141 Phosphoserine +P35193 YOL082W ATG19 243 Phosphoserine +P35193 YOL082W ATG19 213 Glycyl +P35193 YOL082W ATG19 216 Glycyl +P53104 YGL180W ATG1 34 Phosphoserine +P53104 YGL180W ATG1 129 Phosphothreonine +P53104 YGL180W ATG1 226 Phosphothreonine%3B +P53104 YGL180W ATG1 304 Phosphoserine +P53104 YGL180W ATG1 365 Phosphoserine +P53104 YGL180W ATG1 390 Phosphoserine +P53104 YGL180W ATG1 508 Phosphoserine%3B +P53104 YGL180W ATG1 515 Phosphoserine%3B +P53104 YGL180W ATG1 533 Phosphoserine +P53104 YGL180W ATG1 551 Phosphoserine +P53104 YGL180W ATG1 552 Phosphoserine +P53104 YGL180W ATG1 590 Phosphothreonine +P53104 YGL180W ATG1 621 Phosphoserine +P53104 YGL180W ATG1 635 Phosphoserine +P53104 YGL180W ATG1 638 Phosphoserine +P53104 YGL180W ATG1 647 Phosphoserine +P53104 YGL180W ATG1 677 Phosphoserine +P53104 YGL180W ATG1 680 Phosphoserine +P53104 YGL180W ATG1 683 Phosphoserine +P53104 YGL180W ATG1 769 Phosphoserine +P53104 YGL180W ATG1 783 Phosphoserine +P53867 YNL223W ATG4 488 Phosphoserine +Q12380 YPL149W ATG5 149 Glycyl +Q12092 YPL166W ATG29 106 Phosphoserine +Q12092 YPL166W ATG29 187 Phosphoserine +Q12092 YPL166W ATG29 188 Phosphoserine +P40458 YIL146C ATG32 114 Phosphoserine +P40458 YIL146C ATG32 119 Phosphoserine +P38182 YBL078C ATG8 116 Phosphatidylethanolamine +P32453 YNL315C ATP11 109 Phosphoserine +P40851 YPR122W AXL1 262 Phosphoserine +Q06541 YLR242C ARV1 296 N-linked +P46993 YJL170C ASG7 121 Phosphoserine +P46993 YJL170C ASG7 123 Phosphoserine +P46993 YJL170C ASG7 125 Phosphoserine +P46993 YJL170C ASG7 153 Phosphothreonine +P54074 YMR119W ASI1 2 N-linked +P54074 YMR119W ASI1 19 N-linked +P54074 YMR119W ASI1 29 N-linked +P48361 YGR097W ASK10 344 Phosphoserine +P48361 YGR097W ASK10 793 Phosphoserine +P48361 YGR097W ASK10 808 Phosphothreonine +P48361 YGR097W ASK10 944 Phosphoserine +P48361 YGR097W ASK10 969 Phosphoserine +P48361 YGR097W ASK10 1017 Phosphothreonine +P48361 YGR097W ASK10 1070 Phosphoserine +P48361 YGR097W ASK10 1095 Phosphoserine +P48361 YGR097W ASK10 1098 Phosphoserine +P32660 YER166W DNF1 53 Phosphoserine +P32660 YER166W DNF1 70 Phosphothreonine +P32660 YER166W DNF1 81 Phosphoserine +P32660 YER166W DNF1 85 Phosphothreonine +P32660 YER166W DNF1 92 Phosphoserine +P32660 YER166W DNF1 94 Phosphothreonine +P32660 YER166W DNF1 104 Phosphoserine +P32660 YER166W DNF1 109 Phosphothreonine +P32660 YER166W DNF1 351 Phosphoserine +P32660 YER166W DNF1 354 Phosphoserine +P32660 YER166W DNF1 358 Phosphoserine +P32660 YER166W DNF1 365 Phosphoserine +P32660 YER166W DNF1 368 Phosphotyrosine +P32660 YER166W DNF1 1506 Phosphoserine +P32660 YER166W DNF1 1551 Phosphothreonine +P32660 YER166W DNF1 1552 Phosphoserine +P32660 YER166W DNF1 1563 Phosphoserine +P32660 YER166W DNF1 895 Glycyl +Q12674 YMR162C DNF3 627 Phosphoserine +P30902 YKL016C ATP7 2 N-acetylserine +P40518 YIL062C ARC15 142 Phosphothreonine +Q06598 YPR201W ARR3 201 N-linked +Q06598 YPR201W ARR3 365 N-linked +P35734 YKL052C ASK1 26 Phosphoserine +P35734 YKL052C ASK1 118 Phosphoserine +P35734 YKL052C ASK1 134 Phosphoserine +P35734 YKL052C ASK1 140 Phosphothreonine +P35734 YKL052C ASK1 155 Phosphoserine +P35734 YKL052C ASK1 156 Phosphoserine +P35734 YKL052C ASK1 200 Phosphoserine%3B +P35734 YKL052C ASK1 216 Phosphoserine +P35734 YKL052C ASK1 250 Phosphoserine%3B +P53855 YNL242W ATG2 236 Phosphoserine +Q05789 YLR211C ATG38 2 N-acetylserine +P36107 YKL004W AUR1 392 Phosphoserine +P36107 YKL004W AUR1 395 Phosphoserine +P36107 YKL004W AUR1 132 N-linked +P36062 YKL146W AVT3 59 Phosphoserine +P36062 YKL146W AVT3 119 Phosphoserine +P36062 YKL146W AVT3 121 Phosphoserine +P36062 YKL146W AVT3 165 Phosphoserine +P53629 YNR019W ARE2 175 Phosphoserine +P53629 YNR019W ARE2 176 Phosphoserine +P19146 YDL137W ARF2 2 N-myristoyl +P19146 YDL137W ARF2 127 Glycyl +P49089 YPR145W ASN1 265 Phosphoserine +P49089 YPR145W ASN1 509 Phosphoserine +P43601 YFR021W ATG18 354 Phosphoserine +Q02887 YPL100W ATG21 213 Phosphothreonine +Q02887 YPL100W ATG21 237 Phosphoserine +P25568 YCL038C ATG22 278 Phosphoserine +Q06485 YLR356W ATG33 127 Phosphoserine +Q06485 YLR356W ATG33 129 Phosphoserine +P40344 YNR007C ATG3 19 N6-acetyllysine%3B +P40344 YNR007C ATG3 48 N6-acetyllysine%3B +P32907 YNR002C ATO2 2 N-acetylserine +P32907 YNR002C ATO2 2 Phosphoserine +P32907 YNR002C ATO2 7 Phosphoserine +P32907 YNR002C ATO2 21 Phosphoserine +P32907 YNR002C ATO2 22 Phosphoserine +P32907 YNR002C ATO2 28 Phosphoserine +P32907 YNR002C ATO2 40 Phosphoserine +P32454 YKL157W APE2 381 N-linked +P32454 YKL157W APE2 713 N-linked +P32381 YDL029W ARP2 1 N-acetylmethionine +P53244 YGR068C ART5 364 Glycyl +P53983 YNL008C ASI3 24 N-linked +P53983 YNL008C ASI3 34 N-linked +P53983 YNL008C ASI3 46 N-linked +P53983 YNL008C ASI3 66 N-linked +P0CZ17 YLR155C ASP3-1 29 N-linked +P0CZ17 YLR155C ASP3-1 93 N-linked +P0CZ17 YLR155C ASP3-1 239 N-linked +P39524 YAL026C DRS2 102 Phosphoserine +P39986 YEL031W SPF1 324 Phosphoserine +P39986 YEL031W SPF1 936 Phosphoserine +Q01217 YER069W ARG5,6 359 Phosphoserine +Q02804 YPL051W ARL3 1 N-acetylmethionine +Q02804 YPL051W ARL3 50 Glycyl +P28777 YGL148W ARO2 2 N-acetylserine +P18634 YLR392C ART10 118 Glycyl +P50275 YOR058C ASE1 17 Phosphoserine +P0CX77 YLR157C ASP3-2 29 N-linked +P0CX77 YLR157C ASP3-2 93 N-linked +P0CX77 YLR157C ASP3-2 239 N-linked +P0CX78 YLR158C ASP3-3 29 N-linked +P0CX78 YLR158C ASP3-3 93 N-linked +P0CX78 YLR158C ASP3-3 239 N-linked +Q06321 YLR189C ATG26 76 Phosphoserine +Q06321 YLR189C ATG26 693 Phosphoserine +Q12142 YDL149W ATG9 143 Phosphoserine +Q12142 YDL149W ATG9 144 Phosphoserine +Q12142 YDL149W ATG9 787 Phosphoserine +Q12359 YDR384C ATO3 4 Phosphoserine +P61829 Q0130 OLI1 1 N-formylmethionine +P35817 YLR399C BDF1 270 Phosphoserine +P35817 YLR399C BDF1 429 Phosphoserine +P35817 YLR399C BDF1 615 Phosphoserine +P35817 YLR399C BDF1 659 Phosphoserine +P39714 YAL060W BDH1 63 Phosphoserine +P07251 YBL099W ATP1 57 Phosphoserine +P07251 YBL099W ATP1 178 Phosphoserine +P13090 YML116W ATR1 394 N-linked +P13090 YML116W ATR1 471 N-linked +Q01389 YJL095W BCK1 407 Phosphothreonine +Q01389 YJL095W BCK1 411 Phosphoserine +Q01389 YJL095W BCK1 491 Phosphoserine +Q01389 YJL095W BCK1 747 Phosphoserine +Q01389 YJL095W BCK1 816 Phosphoserine +Q01389 YJL095W BCK1 1058 Phosphoserine +Q01389 YJL095W BCK1 1061 Phosphoserine +Q01389 YJL095W BCK1 1134 Phosphoserine%3B +P39713 YAL061W BDH2 63 Phosphoserine +Q08347 YOL164W BDS1 1 N-acetylmethionine +P81449 YDR322C-A TIM11 2 N-acetylserine +P41815 YDR046C BAP3 14 Phosphoserine +P41815 YDR046C BAP3 79 Phosphoserine +P47068 YJL020C BBC1 103 Phosphoserine +P47068 YJL020C BBC1 158 Phosphoserine +P47068 YJL020C BBC1 166 Phosphoserine +P47068 YJL020C BBC1 565 Phosphoserine +P47068 YJL020C BBC1 621 Phosphoserine +P47068 YJL020C BBC1 631 Phosphoserine +P47068 YJL020C BBC1 634 Phosphoserine +P47068 YJL020C BBC1 636 Phosphothreonine +P47068 YJL020C BBC1 638 Phosphoserine +P47068 YJL020C BBC1 647 Phosphoserine +P47068 YJL020C BBC1 850 Phosphothreonine +P47068 YJL020C BBC1 889 Phosphoserine +P47068 YJL020C BBC1 894 Phosphothreonine +P47068 YJL020C BBC1 895 Phosphothreonine +P47068 YJL020C BBC1 1012 Glycyl +Q08236 YOL078W AVO1 1 N-acetylmethionine +Q08236 YOL078W AVO1 140 Phosphoserine +Q08236 YOL078W AVO1 144 Phosphoserine +Q08236 YOL078W AVO1 400 Phosphoserine +Q08236 YOL078W AVO1 509 Phosphoserine +Q08236 YOL078W AVO1 510 Phosphothreonine +Q08236 YOL078W AVO1 552 Phosphoserine +P47082 YJR001W AVT1 8 Phosphoserine +P47082 YJR001W AVT1 15 Phosphoserine +P47082 YJR001W AVT1 35 Phosphoserine +P47082 YJR001W AVT1 181 Phosphothreonine +P47082 YJR001W AVT1 187 Phosphoserine +P38084 YBR068C BAP2 3 Phosphoserine +P38084 YBR068C BAP2 15 Phosphothreonine +P38084 YBR068C BAP2 16 Phosphoserine +P38084 YBR068C BAP2 19 Phosphoserine +P38084 YBR068C BAP2 21 Phosphoserine +P38084 YBR068C BAP2 24 Phosphoserine +P38084 YBR068C BAP2 76 Phosphoserine +P38084 YBR068C BAP2 84 Phosphoserine +P39960 YER155C BEM2 129 Phosphoserine +P39960 YER155C BEM2 283 Phosphoserine +P39960 YER155C BEM2 1012 Phosphoserine +P39960 YER155C BEM2 1016 Phosphoserine +P39960 YER155C BEM2 1038 Phosphothreonine +P39960 YER155C BEM2 1046 Phosphoserine +P39960 YER155C BEM2 1054 Phosphoserine +P39960 YER155C BEM2 1128 Phosphoserine +P39960 YER155C BEM2 27 Glycyl +P36149 YKR068C BET3 80 S-palmitoyl +P47134 YJR089W BIR1 477 Phosphoserine +P47134 YJR089W BIR1 508 Phosphoserine +P47134 YJR089W BIR1 552 Phosphoserine +P47134 YJR089W BIR1 587 Phosphoserine +P47134 YJR089W BIR1 751 Phosphoserine +P47134 YJR089W BIR1 765 Phosphoserine +P47041 YJL058C BIT61 58 Phosphotyrosine +P47041 YJL058C BIT61 59 Phosphoserine +P47041 YJL058C BIT61 139 Phosphoserine +P47041 YJL058C BIT61 144 Phosphoserine +Q08235 YOL077C BRX1 285 Phosphoserine +Q05611 YDR275W BSC2 177 Phosphoserine +Q08280 YOL137W BSC6 37 Phosphoserine +Q08280 YOL137W BSC6 41 Phosphoserine +Q08280 YOL137W BSC6 49 N-linked +P47176 YJR148W BAT2 202 N6-(pyridoxal +P15703 YGR282C BGL2 202 N-linked +P15703 YGR282C BGL2 284 N-linked +P50277 YNR058W BIO3 314 N6-(pyridoxal +Q08965 YPL217C BMS1 438 Phosphoserine +Q08965 YPL217C BMS1 478 Phosphoserine +Q08965 YPL217C BMS1 492 Phosphoserine +Q08965 YPL217C BMS1 504 Phosphothreonine +Q08965 YPL217C BMS1 516 Phosphothreonine +Q08965 YPL217C BMS1 518 Phosphoserine +Q08965 YPL217C BMS1 523 Phosphoserine +Q08965 YPL217C BMS1 574 Phosphoserine +Q08965 YPL217C BMS1 578 Phosphoserine +P47039 YJL060W BNA3 271 N6-(pyridoxal +P40450 YIL159W BNR1 621 Phosphoserine +P40450 YIL159W BNR1 751 Phosphoserine +Q07660 YDL231C BRE4 830 N-linked +P53755 YNR069C BSC5 111 Phosphoserine +P53755 YNR069C BSC5 350 Phosphoserine +Q06604 YPR171W BSP1 46 Phosphoserine +Q06604 YPR171W BSP1 79 Phosphoserine +Q06604 YPR171W BSP1 88 Phosphoserine +Q06604 YPR171W BSP1 185 Phosphoserine +Q06604 YPR171W BSP1 220 Phosphoserine +Q06604 YPR171W BSP1 309 Phosphoserine +Q06604 YPR171W BSP1 320 Phosphoserine +P50944 YNL101W AVT4 88 Phosphoserine +P50944 YNL101W AVT4 130 Phosphoserine +P50944 YNL101W AVT4 165 Phosphoserine +P41696 YOR113W AZF1 61 Phosphoserine +P41696 YOR113W AZF1 286 Phosphoserine +P41696 YOR113W AZF1 325 Phosphoserine +Q12365 YPL255W BBP1 29 Phosphoserine +Q12365 YPL255W BBP1 73 Phosphoserine +Q12365 YPL255W BBP1 115 Phosphoserine +P38928 YIL140W AXL2 642 Phosphoserine +P38928 YIL140W AXL2 673 Phosphoserine +P38928 YIL140W AXL2 676 Phosphoserine +P38928 YIL140W AXL2 41 N-linked +P38928 YIL140W AXL2 50 N-linked +P38928 YIL140W AXL2 96 N-linked +P38928 YIL140W AXL2 117 N-linked +P38928 YIL140W AXL2 163 N-linked +P38928 YIL140W AXL2 260 N-linked +P38928 YIL140W AXL2 266 N-linked +P38928 YIL140W AXL2 304 N-linked +P38928 YIL140W AXL2 324 N-linked +P38928 YIL140W AXL2 359 N-linked +P38928 YIL140W AXL2 382 N-linked +P38928 YIL140W AXL2 389 N-linked +P38928 YIL140W AXL2 403 N-linked +P38928 YIL140W AXL2 447 N-linked +P38928 YIL140W AXL2 451 N-linked +P38928 YIL140W AXL2 495 N-linked +P33306 YER167W BCK2 334 Phosphoserine +P33306 YER167W BCK2 757 Phosphoserine +P33306 YER167W BCK2 761 Phosphoserine +Q07442 YDL070W BDF2 264 Phosphoserine +P53858 YNL233W BNI4 43 Phosphoserine +P53858 YNL233W BNI4 133 Phosphoserine +P53858 YNL233W BNI4 281 Phosphoserine +P53858 YNL233W BNI4 364 Phosphoserine +P53858 YNL233W BNI4 394 Phosphoserine +P53858 YNL233W BNI4 410 Phosphothreonine +P53858 YNL233W BNI4 476 Phosphoserine +P53858 YNL233W BNI4 500 Phosphoserine +P53858 YNL233W BNI4 503 Phosphoserine +P53858 YNL233W BNI4 618 Phosphoserine +P53858 YNL233W BNI4 703 Phosphothreonine +P53858 YNL233W BNI4 746 Phosphoserine +P53858 YNL233W BNI4 825 Phosphoserine +Q06338 YDR361C BCP1 205 Phosphothreonine +Q06338 YDR361C BCP1 209 Phosphothreonine +P47113 YJR053W BFA1 317 Phosphoserine +P40013 YER016W BIM1 2 N-acetylserine +P40013 YER016W BIM1 157 Phosphoserine +P29366 YBR200W BEM1 1 N-acetylmethionine +P29366 YBR200W BEM1 47 Phosphoserine +P29366 YBR200W BEM1 255 Phosphoserine +P29366 YBR200W BEM1 258 Phosphoserine +P29366 YBR200W BEM1 458 Phosphoserine +P29366 YBR200W BEM1 461 Phosphoserine +P38813 YHR101C BIG1 24 N-linked +P38813 YHR101C BIG1 144 N-linked +P43583 YFL007W BLM10 11 Phosphoserine +P43583 YFL007W BLM10 29 Phosphoserine +P43583 YFL007W BLM10 56 Phosphoserine +P43583 YFL007W BLM10 62 Phosphoserine +P43583 YFL007W BLM10 64 Phosphothreonine +P43583 YFL007W BLM10 66 Phosphothreonine +P43583 YFL007W BLM10 1041 Phosphoserine +Q04347 YMR014W BUD22 257 Phosphothreonine +Q04347 YMR014W BUD22 367 Phosphoserine +Q04347 YMR014W BUD22 371 Phosphothreonine +Q04347 YMR014W BUD22 375 Phosphoserine +P33314 YKL092C BUD2 2 N-acetylserine +P33314 YKL092C BUD2 854 Phosphoserine +P47136 YJR092W BUD4 10 Phosphoserine +P47136 YJR092W BUD4 78 Phosphoserine +P47136 YJR092W BUD4 81 Phosphoserine +P47136 YJR092W BUD4 91 Phosphoserine +P47136 YJR092W BUD4 96 Phosphoserine +P47136 YJR092W BUD4 167 Phosphoserine +P47136 YJR092W BUD4 365 Phosphothreonine +P47136 YJR092W BUD4 367 Phosphoserine +P47136 YJR092W BUD4 511 Phosphoserine +P47136 YJR092W BUD4 616 Phosphoserine +P47136 YJR092W BUD4 805 Phosphoserine +P47136 YJR092W BUD4 811 Phosphoserine +P41697 YLR319C BUD6 12 Phosphothreonine +P41697 YLR319C BUD6 233 Phosphoserine +P41697 YLR319C BUD6 327 Phosphoserine +P41697 YLR319C BUD6 342 Phosphoserine +P38822 YHR114W BZZ1 327 Phosphoserine +P38822 YHR114W BZZ1 463 Phosphoserine +P38822 YHR114W BZZ1 472 Phosphoserine +P38822 YHR114W BZZ1 476 Phosphoserine +Q04749 YMR068W AVO2 315 Phosphoserine +Q04749 YMR068W AVO2 350 Phosphoserine +P40074 YER119C AVT6 344 Phosphoserine +P12630 YIL015W BAR1 84 N-linked +P12630 YIL015W BAR1 90 N-linked +P12630 YIL015W BAR1 268 N-linked +P12630 YIL015W BAR1 308 N-linked +P12630 YIL015W BAR1 366 N-linked +P12630 YIL015W BAR1 398 N-linked +P12630 YIL015W BAR1 468 N-linked +P12630 YIL015W BAR1 503 N-linked +P12630 YIL015W BAR1 551 N-linked +Q12186 YLR116W MSL5 93 Phosphoserine +Q12186 YLR116W MSL5 95 Phosphoserine +Q12186 YLR116W MSL5 100 Phosphotyrosine +Q12186 YLR116W MSL5 382 Phosphoserine +P38891 YHR208W BAT1 219 N6-(pyridoxal +P38891 YHR208W BAT1 315 Phosphothreonine +P38772 YHR040W BCD1 330 Phosphoserine +P32873 YPL115C BEM3 254 Phosphoserine +Q06631 YDR299W BFR2 41 Phosphoserine +Q06631 YDR299W BFR2 44 Phosphoserine +Q06631 YDR299W BFR2 366 Phosphoserine +Q06631 YDR299W BFR2 372 Phosphoserine +Q06631 YDR299W BFR2 379 Phosphoserine +P11709 YCL029C BIK1 95 Phosphoserine +P11709 YCL029C BIK1 110 Phosphoserine +Q08492 YOR078W BUD21 16 Phosphoserine +Q08492 YOR078W BUD21 45 Phosphoserine +Q08492 YOR078W BUD21 65 Phosphoserine +Q08492 YOR078W BUD21 144 Phosphoserine +Q05949 YLR226W BUR2 24 Phosphoserine +P27614 YJL172W CPS1 88 N-linked +P27614 YJL172W CPS1 176 N-linked +P27614 YJL172W CPS1 228 N-linked +P27614 YJL172W CPS1 381 N-linked +P27614 YJL172W CPS1 525 N-linked +P27614 YJL172W CPS1 8 Glycyl +P00729 YMR297W PRC1 124 N-linked +P00729 YMR297W PRC1 198 N-linked +P00729 YMR297W PRC1 279 N-linked +P00729 YMR297W PRC1 479 N-linked +P34730 YDR099W BMH2 2 N-acetylserine +P38041 YBL085W BOI1 104 Phosphoserine +P38041 YBL085W BOI1 106 Phosphoserine +P38041 YBL085W BOI1 128 Phosphoserine +P38041 YBL085W BOI1 151 Phosphothreonine +P38041 YBL085W BOI1 158 Phosphothreonine +P38041 YBL085W BOI1 209 Phosphoserine +P38041 YBL085W BOI1 393 Phosphoserine +P38041 YBL085W BOI1 412 Phosphoserine +P38041 YBL085W BOI1 525 Phosphoserine +P38041 YBL085W BOI1 528 Phosphoserine +P38041 YBL085W BOI1 589 Phosphoserine +P38041 YBL085W BOI1 590 Phosphoserine +P38041 YBL085W BOI1 593 Phosphoserine +P38041 YBL085W BOI1 644 Phosphoserine +P38041 YBL085W BOI1 655 Phosphoserine +P38041 YBL085W BOI1 735 Phosphoserine +P38041 YBL085W BOI1 919 Phosphothreonine +P53836 YNL278W CAF120 491 Phosphoserine +P53836 YNL278W CAF120 510 Phosphoserine +P53836 YNL278W CAF120 518 Phosphoserine +P53836 YNL278W CAF120 538 Phosphoserine +P53836 YNL278W CAF120 556 Phosphoserine +P53836 YNL278W CAF120 871 Phosphoserine +P53836 YNL278W CAF120 885 Phosphoserine +P39101 YER048C CAJ1 132 Glycyl +P17555 YNL138W SRV2 454 Phosphoserine +P06787 YBR109C CMD1 82 Phosphoserine +P06787 YBR109C CMD1 102 Phosphoserine +P27825 YAL058W CNE1 25 N-linked +P27825 YAL058W CNE1 104 N-linked +P27825 YAL058W CNE1 296 N-linked +P27825 YAL058W CNE1 416 N-linked +P27825 YAL058W CNE1 425 N-linked +P04817 YEL063C CAN1 54 Phosphoserine +P04817 YEL063C CAN1 66 Phosphoserine +P28495 YKL007W CAP1 2 N-acetylserine +P28495 YKL007W CAP1 17 Phosphoserine +P34237 YKL179C COY1 364 Phosphoserine +P34237 YKL179C COY1 450 Phosphoserine +P34237 YKL179C COY1 453 Phosphoserine +P34237 YKL179C COY1 555 Phosphoserine +P15202 YDR256C CTA1 2 N-acetylserine +Q06071 YLR408C BLS1 33 Phosphoserine +P29311 YER177W BMH1 2 N-acetylserine +P29311 YER177W BMH1 89 Phosphoserine +P29311 YER177W BMH1 76 Glycyl +P48582 YPL084W BRO1 740 Phosphoserine +P32639 YER172C BRR2 403 Phosphoserine +P25558 YCL014W BUD3 766 Phosphoserine +P25558 YCL014W BUD3 1045 Phosphothreonine +P25558 YCL014W BUD3 1063 Phosphoserine +P25558 YCL014W BUD3 1075 Phosphoserine +P25558 YCL014W BUD3 1134 Phosphoserine +P25558 YCL014W BUD3 1149 Phosphoserine +P25558 YCL014W BUD3 1157 Phosphothreonine +P25558 YCL014W BUD3 1160 Phosphoserine +P25558 YCL014W BUD3 1228 Phosphoserine +P25558 YCL014W BUD3 1254 Phosphoserine +P25558 YCL014W BUD3 1257 Phosphoserine +P25558 YCL014W BUD3 1390 Phosphoserine +P25558 YCL014W BUD3 1412 Phosphoserine +P25558 YCL014W BUD3 1429 Phosphothreonine +P25558 YCL014W BUD3 1440 Phosphothreonine +P25558 YCL014W BUD3 1443 Phosphoserine +P25558 YCL014W BUD3 1501 Phosphoserine +P25558 YCL014W BUD3 1549 Phosphoserine +P25558 YCL014W BUD3 1589 Phosphoserine +P25558 YCL014W BUD3 1614 Phosphoserine +P25558 YCL014W BUD3 792 Glycyl +P25558 YCL014W BUD3 963 Glycyl +Q12191 YDL099W BUG1 2 N-acetylserine +Q12191 YDL099W BUG1 87 Phosphoserine +Q12191 YDL099W BUG1 170 Phosphoserine +Q12191 YDL099W BUG1 292 Phosphothreonine +Q03758 YML111W BUL2 22 Phosphothreonine +Q03758 YML111W BUL2 557 Phosphoserine +P12962 YOR276W CAF20 78 Phosphoserine +P12962 YOR276W CAF20 91 Phosphoserine +P12962 YOR276W CAF20 99 Phosphothreonine +P12962 YOR276W CAF20 101 Phosphothreonine +P12962 YOR276W CAF20 102 Phosphothreonine +P12962 YOR276W CAF20 154 Phosphoserine +P53890 YNL166C BNI5 70 Phosphoserine +P53890 YNL166C BNI5 179 Phosphoserine +P53890 YNL166C BNI5 194 Phosphoserine +P53890 YNL166C BNI5 257 Phosphothreonine +P53890 YNL166C BNI5 270 Phosphoserine +P53890 YNL166C BNI5 273 Phosphoserine +P53890 YNL166C BNI5 274 Phosphothreonine +P53890 YNL166C BNI5 332 Phosphoserine +P53890 YNL166C BNI5 340 Phosphoserine +P53890 YNL166C BNI5 344 Phosphotyrosine +P53890 YNL166C BNI5 346 Phosphoserine +P53890 YNL166C BNI5 350 Phosphoserine +P39969 YER114C BOI2 18 Phosphoserine +P39969 YER114C BOI2 24 Phosphoserine +P39969 YER114C BOI2 28 Phosphoserine +P39969 YER114C BOI2 450 Phosphoserine +P39969 YER114C BOI2 519 Phosphoserine +P39969 YER114C BOI2 523 Phosphoserine +P39969 YER114C BOI2 546 Phosphoserine +P39969 YER114C BOI2 652 Phosphoserine +P43132 YLR015W BRE2 227 Phosphoserine +P38356 YBR290W BSD2 312 Glycyl +P43573 YFL023W BUD27 580 Phosphoserine +P53323 YGR262C BUD32 187 Phosphoserine%3B +P53323 YGR262C BUD32 189 Phosphoserine%3B +P41698 YLR353W BUD8 92 N-linked +P41698 YLR353W BUD8 110 N-linked +P41698 YLR353W BUD8 211 N-linked +P41698 YLR353W BUD8 240 N-linked +P41698 YLR353W BUD8 271 N-linked +P41698 YLR353W BUD8 333 N-linked +P41698 YLR353W BUD8 396 N-linked +P41698 YLR353W BUD8 423 N-linked +P53226 YGR041W BUD9 112 Phosphoserine +P53226 YGR041W BUD9 189 Phosphoserine +P53226 YGR041W BUD9 83 N-linked +P53226 YGR041W BUD9 139 N-linked +P53226 YGR041W BUD9 142 N-linked +P53226 YGR041W BUD9 221 N-linked +P53226 YGR041W BUD9 259 N-linked +P53226 YGR041W BUD9 263 N-linked +P53226 YGR041W BUD9 289 N-linked +P53226 YGR041W BUD9 299 N-linked +P53226 YGR041W BUD9 340 N-linked +P48524 YMR275C BUL1 58 Phosphoserine +P48524 YMR275C BUL1 70 Phosphoserine +P07245 YGR204W ADE3 176 Phosphoserine +P07245 YGR204W ADE3 318 Phosphothreonine +P07245 YGR204W ADE3 322 Phosphoserine +P36076 YKL088W CAB3 42 Phosphoserine +P36076 YKL088W CAB3 116 Phosphoserine +P36076 YKL088W CAB3 121 Phosphoserine +P36076 YKL088W CAB3 124 Phosphoserine +P36076 YKL088W CAB3 264 Phosphoserine +P13517 YIL034C CAP2 2 N-acetylserine +P13517 YIL034C CAP2 85 Phosphoserine +P13517 YIL034C CAP2 92 Phosphoserine +Q02948 YPL120W VPS30 142 Phosphothreonine +P38934 YOR198C BFR1 260 Phosphoserine +P38934 YOR198C BFR1 336 Phosphothreonine +P38934 YOR198C BFR1 369 Phosphoserine +Q06150 YLR267W BOP2 383 Phosphoserine +P53741 YNR051C BRE5 187 Phosphoserine +P53741 YNR051C BRE5 282 Phosphoserine +P53741 YNR051C BRE5 336 Phosphothreonine +P53741 YNR051C BRE5 340 Phosphoserine +P53741 YNR051C BRE5 398 Phosphoserine +P43571 YFL025C BST1 19 N-linked +P43571 YFL025C BST1 295 N-linked +P43571 YFL025C BST1 302 N-linked +P43571 YFL025C BST1 447 N-linked +P43571 YFL025C BST1 456 N-linked +P43571 YFL025C BST1 485 N-linked +P43571 YFL025C BST1 565 N-linked +P43571 YFL025C BST1 651 N-linked +P43571 YFL025C BST1 668 N-linked +P43571 YFL025C BST1 694 N-linked +P43571 YFL025C BST1 918 N-linked +P41832 YNL271C BNI1 311 Phosphoserine +P41832 YNL271C BNI1 325 Phosphoserine +P41832 YNL271C BNI1 1085 Phosphoserine +P41832 YNL271C BNI1 1170 Phosphoserine +P41832 YNL271C BNI1 1338 Phosphoserine +P41832 YNL271C BNI1 1344 Phosphoserine +P41832 YNL271C BNI1 1918 Phosphothreonine +P25385 YLR078C BOS1 1 N-acetylmethionine +P14772 YLL015W BPT1 645 Phosphoserine +P14772 YLL015W BPT1 885 Phosphoserine +P14772 YLL015W BPT1 889 Phosphothreonine +P14772 YLL015W BPT1 893 Phosphoserine +P14772 YLL015W BPT1 895 Phosphoserine +P14772 YLL015W BPT1 916 Phosphothreonine +P14772 YLL015W BPT1 927 Phosphoserine +P14772 YLL015W BPT1 931 Phosphoserine +P14772 YLL015W BPT1 934 Phosphothreonine +P14772 YLL015W BPT1 1011 N-linked +P23293 YPR161C SGV1 240 Phosphothreonine%3B +P23293 YPR161C SGV1 400 Phosphoserine +P23293 YPR161C SGV1 405 Phosphothreonine +P23293 YPR161C SGV1 417 Phosphoserine +P23293 YPR161C SGV1 634 Phosphoserine +P36106 YKL005C BYE1 177 Phosphoserine +P32797 YDL220C CDC13 306 Phosphoserine +P32797 YDL220C CDC13 308 Phosphothreonine +P32797 YDL220C CDC13 333 Phosphoserine +P25656 YCR094W CDC50 199 N-linked +P25656 YCR094W CDC50 216 N-linked +P25656 YCR094W CDC50 237 N-linked +P25656 YCR094W CDC50 288 N-linked +P25656 YCR094W CDC50 329 N-linked +P09119 YJL194W CDC6 368 Phosphothreonine +P53197 YGL003C CDH1 213 Phosphoserine +Q12453 YOR112W CEX1 754 Phosphoserine +P07267 YPL154C PEP4 144 N-linked +P07267 YPL154C PEP4 345 N-linked +P32582 YGR155W CYS4 53 N6-(pyridoxal +P32582 YGR155W CYS4 134 Phosphoserine +P32582 YGR155W CYS4 350 Phosphoserine +P32582 YGR155W CYS4 424 Phosphoserine +Q06703 YLR308W CDA2 142 N-linked +Q06703 YLR308W CDA2 181 N-linked +Q06703 YLR308W CDA2 199 N-linked +Q06703 YLR308W CDA2 246 N-linked +Q06703 YLR308W CDA2 263 N-linked +P27636 YAR019C CDC15 561 Phosphoserine +P27636 YAR019C CDC15 567 Phosphoserine +P27636 YAR019C CDC15 870 Phosphothreonine +P04821 YLR310C CDC25 151 Phosphoserine +P04821 YLR310C CDC25 154 Phosphoserine +P04821 YLR310C CDC25 423 Phosphoserine +P04821 YLR310C CDC25 580 Phosphoserine +P04821 YLR310C CDC25 596 Phosphoserine +P04821 YLR310C CDC25 632 Phosphoserine +P04821 YLR310C CDC25 635 Phosphothreonine +P04821 YLR310C CDC25 649 Phosphoserine +P25694 YDL126C CDC48 472 Phosphoserine +P25694 YDL126C CDC48 519 Phosphoserine +P25694 YDL126C CDC48 735 Phosphothreonine +P25694 YDL126C CDC48 770 Phosphoserine +P25694 YDL126C CDC48 305 Glycyl +P25694 YDL126C CDC48 322 Glycyl +P25694 YDL126C CDC48 346 Glycyl +P25694 YDL126C CDC48 522 Glycyl +P25694 YDL126C CDC48 539 Glycyl +P25694 YDL126C CDC48 594 Glycyl +P25694 YDL126C CDC48 673 Glycyl +P40969 YMR168C CEP3 575 Phosphoserine +P53894 YNL161W CBK1 109 Phosphothreonine +P24869 YPR119W CLB2 2 N-acetylserine +P80235 YAR035W YAT1 517 Phosphoserine +P25296 YKL190W CNB1 2 N-myristoyl +P07253 YBR120C CBP6 2 N-acetylserine +P07253 YBR120C CBP6 97 Phosphothreonine +P31384 YAL021C CCR4 33 Phosphothreonine +P31384 YAL021C CCR4 278 Phosphoserine +P31384 YAL021C CCR4 285 Phosphothreonine +Q12127 YLR110C CCW12 112 GPI-anchor +Q12127 YLR110C CCW12 21 N-linked +Q12127 YLR110C CCW12 23 O-linked +Q12127 YLR110C CCW12 24 O-linked +Q12127 YLR110C CCW12 26 O-linked +Q12127 YLR110C CCW12 28 O-linked +Q12127 YLR110C CCW12 31 O-linked +Q12127 YLR110C CCW12 32 O-linked +Q12127 YLR110C CCW12 33 O-linked +Q12127 YLR110C CCW12 36 O-linked +Q12127 YLR110C CCW12 38 O-linked +Q12127 YLR110C CCW12 39 O-linked +Q12127 YLR110C CCW12 46 O-linked +Q12127 YLR110C CCW12 48 O-linked +Q12127 YLR110C CCW12 81 N-linked +Q12127 YLR110C CCW12 97 N-linked +Q12127 YLR110C CCW12 80 Glycyl +P32457 YLR314C CDC3 2 N-acetylserine +P32457 YLR314C CDC3 2 Phosphoserine +P32457 YLR314C CDC3 9 Phosphoserine +P32457 YLR314C CDC3 47 Phosphothreonine +P32457 YLR314C CDC3 60 Phosphoserine +P32457 YLR314C CDC3 77 Phosphoserine +P32457 YLR314C CDC3 175 Phosphoserine +P32457 YLR314C CDC3 468 Phosphothreonine +P32457 YLR314C CDC3 509 Phosphoserine +P32457 YLR314C CDC3 4 Glycyl +P32457 YLR314C CDC3 11 Glycyl +P32457 YLR314C CDC3 30 Glycyl +P32457 YLR314C CDC3 63 Glycyl +P32457 YLR314C CDC3 287 Glycyl +Q06697 YLR418C CDC73 114 Phosphoserine +Q06697 YLR418C CDC73 150 Phosphoserine +P17106 YJR060W CBF1 1 N-acetylmethionine +P17106 YJR060W CBF1 45 Phosphoserine%3B +P17106 YJR060W CBF1 48 Phosphoserine +P17106 YJR060W CBF1 84 Phosphoserine +P17106 YJR060W CBF1 138 Phosphothreonine +Q06702 YLR307W CDA1 26 N-linked +Q06702 YLR307W CDA1 50 N-linked +Q06702 YLR307W CDA1 68 N-linked +Q06702 YLR307W CDA1 189 N-linked +P25342 YCR002C CDC10 1 N-acetylmethionine +P25342 YCR002C CDC10 216 Phosphothreonine +P32468 YHR107C CDC12 2 N-acetylserine +P16522 YHR166C CDC23 59 Phosphoserine%3B +P06704 YOR257W CDC31 130 Phosphothreonine +P25356 YCR032W BPH1 1667 Glycyl +P27637 YAR014C BUD14 2 N-acetylserine +P27637 YAR014C BUD14 159 Phosphotyrosine +P27637 YAR014C BUD14 160 Phosphoserine +P27637 YAR014C BUD14 162 Phosphoserine +P27637 YAR014C BUD14 177 Phosphothreonine +P27637 YAR014C BUD14 212 Phosphoserine +P27637 YAR014C BUD14 222 Phosphoserine +P27637 YAR014C BUD14 376 Phosphoserine +P27637 YAR014C BUD14 378 Phosphoserine +P27637 YAR014C BUD14 401 Phosphoserine +P27637 YAR014C BUD14 507 Phosphoserine +P27637 YAR014C BUD14 655 Phosphoserine +P27637 YAR014C BUD14 658 Phosphoserine +P27637 YAR014C BUD14 670 Phosphoserine +P32504 YGR140W CBF2 566 Phosphoserine +P32504 YGR140W CBF2 706 Phosphotyrosine +P33322 YLR175W CBF5 47 Phosphoserine +P33322 YLR175W CBF5 378 Phosphothreonine +P33322 YLR175W CBF5 9 Glycyl +P33322 YLR175W CBF5 267 Glycyl +P50077 YGR217W CCH1 284 Phosphoserine +P00431 YKR066C CCP1 220 Phosphotyrosine +Q7LHD1 YDR134C CCW22 115 GPI-anchor +Q7LHD1 YDR134C CCW22 21 N-linked +Q7LHD1 YDR134C CCW22 82 N-linked +P19073 YLR229C CDC42 188 Cysteine +P19073 YLR229C CDC42 188 S-geranylgeranyl +P32458 YJR076C CDC11 2 N-acetylserine +P32458 YJR076C CDC11 2 Phosphoserine +P32458 YJR076C CDC11 305 Phosphoserine +P32458 YJR076C CDC11 327 Phosphothreonine +P32458 YJR076C CDC11 412 Glycyl +P14724 YFR036W CDC26 12 Phosphoserine +P06101 YDR168W CDC37 14 Phosphoserine +P06101 YDR168W CDC37 17 Phosphoserine +P06101 YDR168W CDC37 367 Phosphoserine +P06101 YDR168W CDC37 466 Phosphoserine +P06101 YDR168W CDC37 484 Phosphoserine +Q12018 YDL132W CDC53 760 Glycyl +P38910 YOR020C HSP10 2 N-acetylserine +P38910 YOR020C HSP10 31 Phosphoserine +P47818 YLR220W CCC1 29 Phosphoserine +P47818 YLR220W CCC1 53 Phosphoserine +P47818 YLR220W CCC1 68 Phosphoserine +P47818 YLR220W CCC1 71 Phosphoserine +P47818 YLR220W CCC1 83 Phosphoserine +O13547 YLR390W-A CCW14 217 GPI-anchor +O13547 YLR390W-A CCW14 87 N-linked +O13547 YLR390W-A CCW14 161 Glycyl +Q00684 YFR028C CDC14 467 Phosphoserine +O13297 YPL228W CET1 2 N-acetylserine +O13297 YPL228W CET1 15 Phosphoserine +O13297 YPL228W CET1 124 Phosphoserine +P29029 YLR286C CTS1 553 N-linked +Q12114 YLR330W CHS5 305 Phosphothreonine +Q12114 YLR330W CHS5 338 Phosphoserine +Q12114 YLR330W CHS5 362 Phosphoserine +Q12114 YLR330W CHS5 365 Phosphoserine +Q12114 YLR330W CHS5 383 Phosphoserine +Q12114 YLR330W CHS5 384 Phosphoserine +Q12114 YLR330W CHS5 573 Phosphoserine +Q12114 YLR330W CHS5 579 Phosphoserine +Q12114 YLR330W CHS5 590 Phosphoserine +Q12114 YLR330W CHS5 584 Glycyl +P43634 YLR098C CHA4 164 Phosphoserine +P43634 YLR098C CHA4 166 Phosphoserine +P22516 YPL008W CHL1 86 Phosphoserine +P22516 YPL008W CHL1 172 Phosphoserine +Q08032 YLR103C CDC45 453 Phosphothreonine +P07834 YFL009W CDC4 104 Phosphoserine +P32562 YMR001C CDC5 23 Phosphothreonine +P32562 YMR001C CDC5 419 Phosphoserine +P40558 YIL003W CFD1 291 Phosphoserine +P53280 YGR134W CAF130 1042 Phosphoserine +P08004 YNL192W CHS1 34 Phosphoserine +P08004 YNL192W CHS1 35 Phosphoserine +P08004 YNL192W CHS1 270 Phosphoserine +P08004 YNL192W CHS1 299 Phosphoserine +P08004 YNL192W CHS1 318 Phosphoserine +P08004 YNL192W CHS1 328 Phosphothreonine +P08004 YNL192W CHS1 358 Phosphoserine +P14180 YBR038W CHS2 40 Phosphoserine +P14180 YBR038W CHS2 82 Phosphoserine +P14180 YBR038W CHS2 86 Phosphoserine +P14180 YBR038W CHS2 100 Phosphoserine +P14180 YBR038W CHS2 133 Phosphoserine +P14180 YBR038W CHS2 217 Phosphoserine +P14180 YBR038W CHS2 22 N-linked +P14180 YBR038W CHS2 197 N-linked +P14180 YBR038W CHS2 447 N-linked +P32657 YER164W CHD1 36 Phosphoserine +P32657 YER164W CHD1 72 Phosphoserine +P32657 YER164W CHD1 987 Phosphoserine +P32657 YER164W CHD1 989 Phosphoserine +P32657 YER164W CHD1 1336 Phosphoserine +P32657 YER164W CHD1 1364 Phosphoserine +P32657 YER164W CHD1 1372 Phosphoserine +P32657 YER164W CHD1 1144 Glycyl +Q06350 YDR371W CTS2 147 N-linked +Q06350 YDR371W CTS2 228 N-linked +Q06350 YDR371W CTS2 456 N-linked +Q06350 YDR371W CTS2 472 N-linked +P05374 YGR157W CHO2 2 N-acetylserine +P29465 YBR023C CHS3 537 Phosphoserine +P29465 YBR023C CHS3 538 Phosphothreonine +P29465 YBR023C CHS3 82 N-linked +P29465 YBR023C CHS3 114 N-linked +P29465 YBR023C CHS3 152 N-linked +P29465 YBR023C CHS3 163 N-linked +P29465 YBR023C CHS3 303 N-linked +P29465 YBR023C CHS3 332 N-linked +P29465 YBR023C CHS3 371 N-linked +P29465 YBR023C CHS3 136 Glycyl +P40019 YER030W CHZ1 2 N-acetylserine +P40019 YER030W CHZ1 68 Phosphoserine +P40019 YER030W CHZ1 70 Phosphoserine +Q07897 YLR003C CMS1 59 Phosphoserine +P27895 YEL061C CIN8 972 Phosphoserine +P48562 YNL298W CLA4 29 Phosphoserine +P48562 YNL298W CLA4 46 Phosphoserine +P48562 YNL298W CLA4 351 Phosphoserine +P48562 YNL298W CLA4 367 Phosphoserine +P48562 YNL298W CLA4 425 Phosphoserine +P22137 YGL206C CHC1 1107 Glycyl +Q06156 YLR272C YCS4 464 Phosphoserine +Q06156 YLR272C YCS4 475 Phosphoserine +P53079 YGL223C COG1 1 N-acetylmethionine +P53079 YGL223C COG1 305 Phosphoserine +Q12510 YDL156W CMR1 64 Phosphoserine +Q12510 YDL156W CMR1 69 Phosphothreonine +Q12510 YDL156W CMR1 224 Phosphoserine +Q06680 YDR325W YCG1 198 Phosphoserine +Q06680 YDR325W YCG1 933 Phosphoserine +Q06680 YDR325W YCG1 981 Phosphoserine +Q06680 YDR325W YCG1 1008 Phosphoserine +P47001 YJL158C CIS3 68 O-linked +P47001 YJL158C CIS3 78 O-linked +P47001 YJL158C CIS3 105 O-linked +P47001 YJL158C CIS3 106 O-linked +P47001 YJL158C CIS3 107 O-linked +P47001 YJL158C CIS3 109 O-linked +P47001 YJL158C CIS3 111 O-linked +P47001 YJL158C CIS3 112 O-linked +P47001 YJL158C CIS3 113 O-linked +P47001 YJL158C CIS3 114 N-linked +P47001 YJL158C CIS3 116 O-linked +P47001 YJL158C CIS3 117 O-linked +P47001 YJL158C CIS3 118 O-linked +Q03690 YMR012W CLU1 1247 Phosphoserine +P53865 YNL225C CNM67 17 Phosphoserine +P53865 YNL225C CNM67 20 Phosphoserine +P53865 YNL225C CNM67 72 Phosphoserine +P53865 YNL225C CNM67 85 Phosphoserine +P53865 YNL225C CNM67 89 Phosphoserine +P53865 YNL225C CNM67 151 Phosphoserine +P41810 YDR238C SEC26 181 Phosphoserine +P41810 YDR238C SEC26 540 Phosphoserine +Q01519 YLR038C COX12 82 Phosphoserine +Q03048 YLL050C COF1 4 Phosphoserine +P00401 Q0045 COX1 245 1'-histidyl-3'-tyrosine +P38287 YBR161W CSH1 354 Phosphoserine +P43639 YGL019W CKB1 2 N-acetylserine +P43639 YGL019W CKB1 2 Phosphoserine +P46946 YGL175C SAE2 143 Phosphoserine +P46946 YGL175C SAE2 267 Phosphoserine%3B +P32074 YNL287W SEC21 638 Phosphothreonine +P32074 YNL287W SEC21 643 Phosphoserine +P32074 YNL287W SEC21 653 Phosphoserine +P32074 YNL287W SEC21 647 Glycyl +P32798 YOR316C COT1 225 Phosphoserine +P32798 YOR316C COT1 301 Glycyl +P04037 YGL187C COX4 55 Phosphothreonine +P10614 YHR007C ERG11 458 Phosphoserine +P10614 YHR007C ERG11 116 Glycyl +P10614 YHR007C ERG11 353 Glycyl +P10614 YHR007C ERG11 454 Glycyl +P08679 YCR005C CIT2 21 Phosphoserine +P08679 YCR005C CIT2 218 Glycyl +P08679 YCR005C CIT2 239 Glycyl +P08679 YCR005C CIT2 354 Glycyl +P08679 YCR005C CIT2 385 Glycyl +P17891 YGR167W CLC1 49 Phosphothreonine +P17891 YGR167W CLC1 52 Phosphoserine +P41811 YGL137W SEC27 326 Phosphoserine +P38170 YBL097W BRN1 245 Phosphoserine +P38170 YBL097W BRN1 548 Phosphoserine +P43621 YFR051C RET2 277 Phosphothreonine +Q06705 YLR380W CSR1 2 N-acetylserine +Q06705 YLR380W CSR1 2 Phosphoserine +Q03957 YKL139W CTK1 14 Phosphoserine%3B +Q03957 YKL139W CTK1 338 Phosphothreonine +P40094 YER157W COG3 507 Phosphoserine +P40094 YER157W COG3 647 Phosphoserine +Q06440 YLR429W CRN1 441 Phosphoserine +Q06440 YLR429W CRN1 454 Phosphoserine +Q06440 YLR429W CRN1 456 Phosphoserine +Q06440 YLR429W CRN1 517 Phosphothreonine +Q06440 YLR429W CRN1 529 Phosphothreonine +Q06440 YLR429W CRN1 573 Phosphoserine +Q06440 YLR429W CRN1 579 Phosphoserine +Q12150 YLR087C CSF1 82 N-linked +Q12150 YLR087C CSF1 117 N-linked +Q12150 YLR087C CSF1 144 N-linked +Q12150 YLR087C CSF1 271 N-linked +Q12150 YLR087C CSF1 478 N-linked +Q12150 YLR087C CSF1 530 N-linked +Q12150 YLR087C CSF1 816 N-linked +Q12150 YLR087C CSF1 821 N-linked +Q12150 YLR087C CSF1 839 N-linked +Q12150 YLR087C CSF1 892 N-linked +Q12150 YLR087C CSF1 1309 N-linked +Q12150 YLR087C CSF1 1368 N-linked +Q12150 YLR087C CSF1 1453 N-linked +Q12150 YLR087C CSF1 1785 N-linked +Q12150 YLR087C CSF1 1921 N-linked +Q12150 YLR087C CSF1 2130 N-linked +Q12150 YLR087C CSF1 2146 N-linked +Q12150 YLR087C CSF1 2280 N-linked +Q12150 YLR087C CSF1 2337 N-linked +Q12150 YLR087C CSF1 2520 N-linked +Q12150 YLR087C CSF1 2578 N-linked +Q12150 YLR087C CSF1 2719 N-linked +Q12150 YLR087C CSF1 2869 N-linked +Q12748 YLR381W CTF3 2 N-acetylserine +Q08923 YPL181W CTI6 174 Phosphothreonine +Q08923 YPL181W CTI6 175 Phosphoserine +Q08923 YPL181W CTI6 177 Phosphothreonine +Q08923 YPL181W CTI6 216 Phosphoserine +Q08923 YPL181W CTI6 267 Phosphoserine +Q12734 YPR030W CSR2 23 Phosphoserine +Q12734 YPR030W CSR2 46 Phosphoserine +Q12734 YPR030W CSR2 127 Phosphoserine +Q12734 YPR030W CSR2 327 Phosphoserine +Q12734 YPR030W CSR2 987 Phosphoserine +Q12734 YPR030W CSR2 841 Glycyl +P25618 YCR017C CWH43 419 N-linked +P25618 YCR017C CWH43 490 N-linked +P25618 YCR017C CWH43 767 N-linked +P25618 YCR017C CWH43 792 N-linked +P25618 YCR017C CWH43 825 N-linked +Q04632 YML071C COG8 410 Phosphoserine +P38845 YHR146W CRP1 153 Phosphoserine +P38845 YHR146W CRP1 156 Phosphoserine +P38845 YHR146W CRP1 182 Phosphothreonine +P38845 YHR146W CRP1 271 Phosphoserine +P38845 YHR146W CRP1 295 Phosphothreonine +P38845 YHR146W CRP1 319 Phosphoserine +P38845 YHR146W CRP1 343 Phosphoserine +P38845 YHR146W CRP1 366 Phosphothreonine +P38845 YHR146W CRP1 394 Phosphoserine +P38845 YHR146W CRP1 440 Phosphoserine +P43497 YKL096W-A CWP2 71 GPI-anchor +P53968 YNL027W CRZ1 170 Phosphothreonine +P53968 YNL027W CRZ1 175 Phosphoserine +P53968 YNL027W CRZ1 245 Phosphoserine +P53968 YNL027W CRZ1 385 Phosphoserine +P14306 YLR178C TFS1 1 N-acetylmethionine +P53301 YGR189C CRH1 482 GPI-anchor +P53301 YGR189C CRH1 117 N-linked +P53301 YGR189C CRH1 177 N-linked +P53301 YGR189C CRH1 201 N-linked +Q06538 YLR241W CSC1 171 N-linked +P35206 YBR036C CSG2 35 N-linked +P35206 YBR036C CSG2 49 N-linked +P25355 YCR054C CTR86 433 Phosphothreonine +P25355 YCR054C CTR86 559 Phosphoserine +P53923 YNL119W NCS2 489 Phosphoserine +P53830 YNL286W CUS2 163 Phosphoserine +P00044 YJR048W CYC1 78 N6%2CN6%2CN6-trimethyllysine%3B +P00044 YJR048W CYC1 79 N6%2CN6%2CN6-trimethyllysine +P32898 YDR430C CYM1 920 Phosphoserine +P32623 YEL040W UTR2 445 GPI-anchor +P32623 YEL040W UTR2 28 N-linked +P32623 YEL040W UTR2 96 N-linked +P32623 YEL040W UTR2 190 N-linked +P32623 YEL040W UTR2 196 N-linked +P32623 YEL040W UTR2 233 N-linked +P32623 YEL040W UTR2 237 N-linked +P32623 YEL040W UTR2 261 N-linked +P32623 YEL040W UTR2 297 N-linked +P32623 YEL040W UTR2 310 N-linked +P49573 YPR124W CTR1 344 Phosphoserine +P49573 YPR124W CTR1 349 Phosphoserine +P49573 YPR124W CTR1 356 Phosphothreonine +P49573 YPR124W CTR1 369 Phosphoserine +P49573 YPR124W CTR1 113 N-linked +P49573 YPR124W CTR1 148 N-linked +P49573 YPR124W CTR1 345 Glycyl +P89105 YOL145C CTR9 1015 Phosphoserine +P89105 YOL145C CTR9 1017 Phosphoserine +Q04201 YML101C CUE4 48 Phosphoserine +Q04201 YML101C CUE4 37 Glycyl +Q08412 YOR042W CUE5 21 Phosphoserine +Q08412 YOR042W CUE5 36 Phosphoserine +Q08412 YOR042W CUE5 70 Phosphothreonine +Q08412 YOR042W CUE5 91 Phosphoserine +Q08412 YOR042W CUE5 167 Phosphothreonine +Q08412 YOR042W CUE5 220 Phosphoserine +Q08412 YOR042W CUE5 309 Phosphoserine +Q08412 YOR042W CUE5 318 Phosphoserine +Q08412 YOR042W CUE5 346 Phosphothreonine +Q08412 YOR042W CUE5 348 Phosphoserine +Q08412 YOR042W CUE5 352 Phosphothreonine +Q08412 YOR042W CUE5 364 Phosphothreonine +Q08412 YOR042W CUE5 367 Phosphothreonine +Q08412 YOR042W CUE5 407 Phosphoserine +Q08412 YOR042W CUE5 15 Glycyl +Q08412 YOR042W CUE5 59 Glycyl +Q08412 YOR042W CUE5 76 Glycyl +Q08412 YOR042W CUE5 156 Glycyl +Q08412 YOR042W CUE5 354 Glycyl +Q08412 YOR042W CUE5 396 Glycyl +P47050 YJL047C RTT101 791 Glycyl +P53854 YNL245C CWC25 129 Phosphoserine +Q12046 YDL209C CWC2 335 Phosphoserine +Q12046 YDL209C CWC2 336 Phosphoserine +P53008 YGL027C CWH41 42 N-linked +P53008 YGL027C CWH41 122 N-linked +P53008 YGL027C CWH41 135 N-linked +P53008 YGL027C CWH41 787 N-linked +P28319 YKL096W CWP1 217 GPI-anchor +Q08226 YOL063C CRT10 704 Phosphoserine +P53859 YNL232W CSL4 94 Phosphoserine +P21657 YIR023W DAL81 833 Phosphoserine +P47179 YJR151C DAN4 1137 GPI-anchor +P22204 YGR092W DBF2 17 Phosphoserine +P22204 YGR092W DBF2 20 Phosphoserine +P22204 YGR092W DBF2 74 Phosphoserine +P22204 YGR092W DBF2 374 Phosphoserine%3B +P22204 YGR092W DBF2 544 Phosphothreonine%3B +P24309 YKL149C DBR1 269 Phosphoserine +P36091 YKL046C DCW1 428 GPI-anchor +P36091 YKL046C DCW1 34 N-linked +P36091 YKL046C DCW1 84 N-linked +P36091 YKL046C DCW1 109 N-linked +P36091 YKL046C DCW1 133 N-linked +P36091 YKL046C DCW1 203 N-linked +P36091 YKL046C DCW1 225 N-linked +P36091 YKL046C DCW1 240 N-linked +P36091 YKL046C DCW1 265 N-linked +P36091 YKL046C DCW1 281 N-linked +P36091 YKL046C DCW1 337 N-linked +P36091 YKL046C DCW1 362 N-linked +P36091 YKL046C DCW1 420 N-linked +P53899 YNL155W CUZ1 273 Phosphoserine +P08678 YJL005W CYR1 2 N-acetylserine +P08678 YJL005W CYR1 376 Phosphothreonine +P08678 YJL005W CYR1 389 Phosphothreonine +P08678 YJL005W CYR1 433 Phosphoserine +P08678 YJL005W CYR1 487 Phosphoserine +P08678 YJL005W CYR1 497 Phosphoserine +P08678 YJL005W CYR1 562 Phosphoserine +P47178 YJR150C DAN1 275 GPI-anchor +P18962 YHR028C DAP2 63 N-linked +P18962 YHR028C DAP2 79 N-linked +P18962 YHR028C DAP2 110 N-linked +P18962 YHR028C DAP2 139 N-linked +P18962 YHR028C DAP2 372 N-linked +P18962 YHR028C DAP2 392 N-linked +P18962 YHR028C DAP2 421 N-linked +P18962 YHR028C DAP2 738 N-linked +Q12123 YOR173W DCS2 341 Phosphoserine +P46963 YML112W CTK3 35 Phosphothreonine +P53137 YGL110C CUE3 377 Phosphoserine +Q12389 YDL031W DBP10 101 Phosphoserine +Q12389 YDL031W DBP10 398 Phosphoserine +Q12389 YDL031W DBP10 400 Phosphoserine +P24783 YNL112W DBP2 88 Phosphoserine +P24783 YNL112W DBP2 90 Phosphoserine +P24783 YNL112W DBP2 474 Glycyl +P20449 YOR046C DBP5 86 Phosphoserine +P20449 YOR046C DBP5 93 Phosphoserine +P20449 YOR046C DBP5 162 Phosphoserine +P53734 YNR038W DBP6 73 Phosphoserine +P53734 YNR038W DBP6 77 Phosphoserine +P53734 YNR038W DBP6 78 Phosphoserine +P21182 YOL052C SPE2 88 Pyruvic +P08432 YKL184W SPE1 116 N6-(pyridoxal +P06634 YOR204W DED1 2 N-acetylalanine +P06634 YOR204W DED1 62 Dimethylated +P06634 YOR204W DED1 215 Phosphoserine +P06634 YOR204W DED1 218 Phosphoserine +P06634 YOR204W DED1 263 Phosphoserine +P06634 YOR204W DED1 535 Phosphoserine +P06634 YOR204W DED1 539 Phosphoserine +P06634 YOR204W DED1 543 Phosphoserine +P06634 YOR204W DED1 572 Phosphoserine +P06634 YOR204W DED1 576 Phosphoserine +P06634 YOR204W DED1 598 Phosphoserine +P06634 YOR204W DED1 158 Glycyl +P38307 YBR201W DER1 1 N-acetylmethionine +Q01454 YPR135W CTF4 377 Phosphoserine +Q01454 YPR135W CTF4 379 Phosphoserine +Q01454 YPR135W CTF4 398 Phosphoserine +Q01454 YPR135W CTF4 401 Phosphothreonine +Q01454 YPR135W CTF4 411 Phosphothreonine +Q01454 YPR135W CTF4 463 Phosphoserine +P53769 YLR323C CWC24 33 Phosphoserine +P53769 YLR323C CWC24 105 Phosphoserine +P35176 YDR304C CPR5 139 N-linked +P14832 YDR155C CPR1 2 N-acetylserine +P14832 YDR155C CPR1 71 Phosphothreonine +P14832 YDR155C CPR1 142 Phosphoserine +P14832 YDR155C CPR1 145 Phosphoserine +P14832 YDR155C CPR1 29 Glycyl +P14832 YDR155C CPR1 42 Glycyl +P14832 YDR155C CPR1 123 Glycyl +P14832 YDR155C CPR1 139 Glycyl +P14832 YDR155C CPR1 151 Glycyl +P14832 YDR155C CPR1 158 Glycyl +P31373 YAL012W CYS3 204 N6-(pyridoxal +P31373 YAL012W CYS3 362 Phosphoserine +Q12248 YDR016C DAD1 91 Phosphoserine +P25334 YCR069W CPR4 166 N-linked +P06106 YLR303W MET17 44 Phosphoserine +P06106 YLR303W MET17 209 N6-(pyridoxal +P06106 YLR303W MET17 160 Glycyl +Q99288 YDR051C DET1 248 Phosphoserine +Q05080 YMR032W HOF1 337 Phosphoserine +Q05080 YMR032W HOF1 366 Phosphoserine +Q05080 YMR032W HOF1 421 Phosphoserine +P20448 YJL033W HCA4 692 Phosphoserine +P20448 YJL033W HCA4 710 Phosphoserine +P20448 YJL033W HCA4 714 Phosphoserine +P20448 YJL033W HCA4 743 Phosphoserine +P40087 YER143W DDI1 171 Glycyl +P40087 YER143W DDI1 257 Glycyl +P69851 YDR320C-A DAD4 1 N-acetylmethionine +P32328 YPR111W DBF20 17 Phosphoserine +P32328 YPR111W DBF20 366 Phosphoserine +P32328 YPR111W DBF20 536 Phosphothreonine +P53550 YNL118C DCP2 116 Phosphoserine +P53550 YNL118C DCP2 439 Phosphoserine +P53550 YNL118C DCP2 677 Phosphothreonine +P53550 YNL118C DCP2 679 Phosphoserine +P53550 YNL118C DCP2 682 Phosphoserine +P53550 YNL118C DCP2 751 Phosphoserine +P53550 YNL118C DCP2 771 Phosphoserine +P53550 YNL118C DCP2 773 Phosphoserine +P53550 YNL118C DCP2 778 Phosphoserine +P18899 YMR173W DDR48 183 Phosphoserine +P18899 YMR173W DDR48 191 Phosphoserine +P18899 YMR173W DDR48 314 Phosphoserine +P18899 YMR173W DDR48 322 Phosphoserine +P31385 YAL013W DEP1 56 Phosphoserine +P31385 YAL013W DEP1 120 Phosphoserine +P31385 YAL013W DEP1 370 Phosphoserine +P14922 YBR112C CYC8 429 Phosphoserine +P14922 YBR112C CYC8 475 Phosphothreonine +P14922 YBR112C CYC8 710 Phosphoserine +P14922 YBR112C CYC8 741 Phosphoserine +P14922 YBR112C CYC8 768 Phosphoserine +P14922 YBR112C CYC8 815 Phosphoserine +P14922 YBR112C CYC8 817 Phosphoserine +P14922 YBR112C CYC8 866 Phosphoserine +P14922 YBR112C CYC8 943 Phosphoserine +Q07533 YDL117W CYK3 209 Phosphoserine +Q07533 YDL117W CYK3 292 Phosphoserine +Q07533 YDL117W CYK3 313 Phosphoserine +Q07533 YDL117W CYK3 354 Phosphoserine +Q07533 YDL117W CYK3 391 Phosphothreonine +P36162 YKR083C DAD2 1 N-acetylmethionine +P53267 YGR113W DAM1 2 N-acetylserine +P53267 YGR113W DAM1 20 Phosphoserine%3B +P53267 YGR113W DAM1 31 Phosphoserine +P53267 YGR113W DAM1 257 Phosphoserine%3B +P53267 YGR113W DAM1 265 Phosphoserine%3B +P53267 YGR113W DAM1 292 Phosphoserine%3B +P53202 YGR003W CUL3 688 Glycyl +Q02554 YMR240C CUS1 104 Phosphothreonine +Q02554 YMR240C CUS1 112 Phosphothreonine +Q02554 YMR240C CUS1 114 Phosphoserine +P54838 YML070W DAK1 2 N-acetylserine +P54838 YML070W DAK1 2 Phosphoserine +P54838 YML070W DAK1 5 Phosphoserine +P54838 YML070W DAK1 365 Phosphoserine +P54838 YML070W DAK1 512 Phosphoserine +Q12382 YOR311C DGK1 44 Phosphoserine +Q12382 YOR311C DGK1 45 Phosphoserine +Q12382 YOR311C DGK1 46 Phosphoserine +Q12382 YOR311C DGK1 11 N-linked +Q12382 YOR311C DGK1 197 N-linked +Q12382 YOR311C DGK1 270 N-linked +P54861 YLL001W DNM1 629 Phosphoserine +P40059 YER088C DOT6 245 Phosphoserine +P40059 YER088C DOT6 247 Phosphoserine +P40059 YER088C DOT6 487 Phosphoserine +P40059 YER088C DOT6 489 Phosphothreonine +P40059 YER088C DOT6 491 Phosphoserine +P32469 YLR172C DPH5 172 Phosphoserine +P32469 YLR172C DPH5 298 Phosphoserine +P32892 YLL008W DRS1 208 Phosphoserine +P23501 YKR053C YSR3 62 N-linked +P07262 YOR375C GDH1 2 N-acetylserine +P07262 YOR375C GDH1 325 Glycyl +P07262 YOR375C GDH1 371 Glycyl +P07262 YOR375C GDH1 433 Glycyl +Q08496 YOR080W DIA2 393 Phosphoserine +P04819 YDL164C CDC9 58 Phosphoserine +P04819 YDL164C CDC9 75 Phosphoserine +P04819 YDL164C CDC9 119 Phosphoserine +P04819 YDL164C CDC9 123 Phosphoserine +Q03921 YDR141C DOP1 244 Phosphoserine +P46957 YJR006W POL31 1 N-acetylmethionine +P46957 YJR006W POL31 20 Phosphoserine +P36152 YKR071C DRE2 206 Phosphoserine +Q04792 YMR250W GAD1 318 N6-(pyridoxal +P35732 YKL054C DEF1 260 Phosphoserine +P35732 YKL054C DEF1 273 Phosphoserine +P35732 YKL054C DEF1 307 Phosphoserine +P35732 YKL054C DEF1 338 Phosphothreonine +P35732 YKL054C DEF1 646 Phosphoserine +P32330 YKL121W DGR2 716 Phosphoserine +P39708 YAL062W GDH3 326 Glycyl +P39708 YAL062W GDH3 372 Glycyl +P39708 YAL062W GDH3 436 Glycyl +Q04603 YDR121W DPB4 183 Phosphoserine%3B +Q04217 YMR128W ECM16 181 Phosphoserine +P40318 YIL030C SSM4 1 N-acetylmethionine +P47110 YJR043C POL32 223 Phosphothreonine +P47110 YJR043C POL32 230 Phosphoserine +P53255 YGR093W DRN1 242 Phosphoserine +P32325 YDR052C DBF4 59 Phosphoserine +P32325 YDR052C DBF4 84 Phosphoserine +P32325 YDR052C DBF4 235 Phosphoserine +P32325 YDR052C DBF4 623 Phosphoserine +Q03373 YDR480W DIG2 34 Phosphoserine +Q03373 YDR480W DIG2 225 Phosphoserine +Q03373 YDR480W DIG2 266 Phosphoserine +Q03373 YDR480W DIG2 270 Phosphoserine +P40366 YJL065C DLS1 17 Phosphoserine +Q06819 YPR082C DIB1 2 N-acetylalanine +P39976 YEL071W DLD3 17 Glycyl +P31116 YJR139C HOM6 290 Glycyl +P36037 YKL213C DOA1 332 Phosphoserine +Q12395 YLR128W DCN1 12 Phosphoserine +Q06151 YLR270W DCS1 2 N-acetylserine +Q06151 YLR270W DCS1 60 Phosphoserine +Q06151 YLR270W DCS1 66 Phosphothreonine +Q06151 YLR270W DCS1 66 Phosphothreonine%3B +Q06151 YLR270W DCS1 70 Phosphotyrosine +Q06151 YLR270W DCS1 120 Phosphothreonine +P89113 YOL052C-A DDR2 24 N-linked +P89113 YOL052C-A DDR2 27 N-linked +P69771 YKR035W-A DID2 5 Phosphoserine +P38823 YHR115C DMA1 150 Glycyl +P38823 YHR115C DMA1 204 Glycyl +P38823 YHR115C DMA1 217 Glycyl +P38823 YHR115C DMA1 237 Glycyl +P38823 YHR115C DMA1 240 Glycyl +P38823 YHR115C DMA1 260 Glycyl +P38823 YHR115C DMA1 300 Glycyl +P38823 YHR115C DMA1 306 Glycyl +P38823 YHR115C DMA1 313 Glycyl +P38823 YHR115C DMA1 317 Glycyl +Q08949 YPL194W DDC1 436 Phosphoserine +Q05031 YMR238W DFG5 437 GPI-anchor +Q05031 YMR238W DFG5 89 N-linked +Q05031 YMR238W DFG5 114 N-linked +Q05031 YMR238W DFG5 138 N-linked +Q05031 YMR238W DFG5 208 N-linked +Q05031 YMR238W DFG5 231 N-linked +Q05031 YMR238W DFG5 245 N-linked +Q05031 YMR238W DFG5 270 N-linked +Q05031 YMR238W DFG5 273 N-linked +Q05031 YMR238W DFG5 417 N-linked +Q08650 YOR245C DGA1 17 Phosphoserine +P13663 YDR158W HOM2 13 Phosphothreonine +P13663 YDR158W HOM2 318 Phosphoserine +P13663 YDR158W HOM2 323 Phosphoserine +Q03063 YPL049C DIG1 45 Phosphoserine +Q03063 YPL049C DIG1 126 Phosphoserine +Q03063 YPL049C DIG1 142 Phosphoserine +Q03063 YPL049C DIG1 272 Phosphoserine +Q03063 YPL049C DIG1 275 Phosphoserine +Q03063 YPL049C DIG1 330 Phosphoserine +Q03063 YPL049C DIG1 379 Phosphothreonine +Q03063 YPL049C DIG1 395 Phosphoserine +Q03063 YPL049C DIG1 428 Phosphoserine +P53388 YPL265W DIP5 22 Phosphoserine +P53388 YPL265W DIP5 76 Glycyl +P53924 YNL116W DMA2 206 Phosphoserine +P53924 YNL116W DMA2 211 Glycyl +P53924 YNL116W DMA2 256 Glycyl +P53924 YNL116W DMA2 258 Glycyl +P53924 YNL116W DMA2 288 Glycyl +P53924 YNL116W DMA2 310 Glycyl +P53924 YNL116W DMA2 333 Glycyl +P53924 YNL116W DMA2 343 Glycyl +P53924 YNL116W DMA2 346 Glycyl +P53924 YNL116W DMA2 366 Glycyl +P53924 YNL116W DMA2 406 Glycyl +P53924 YNL116W DMA2 412 Glycyl +P53924 YNL116W DMA2 423 Glycyl +P38859 YHR164C DNA2 4 Phosphothreonine +P38859 YHR164C DNA2 17 Phosphoserine%3B +P38859 YHR164C DNA2 237 Phosphoserine%3B +P38859 YHR164C DNA2 962 Phosphothreonine +P02994 YPR080W; YBR118W 2 N%2CN%2CN-trimethylglycine%3B +P02994 YPR080W; YBR118W 3 N6%2CN6-dimethyllysine%3B +P02994 YPR080W; YBR118W 3 N6-methyllysine%3B +P02994 YPR080W; YBR118W 18 Phosphoserine +P02994 YPR080W; YBR118W 30 N6-methyllysine%3B +P02994 YPR080W; YBR118W 72 Phosphothreonine +P02994 YPR080W; YBR118W 79 N6%2CN6%2CN6-trimethyllysine%3B +P02994 YPR080W; YBR118W 82 Phosphothreonine +P02994 YPR080W; YBR118W 163 Phosphoserine +P02994 YPR080W; YBR118W 259 Phosphothreonine +P02994 YPR080W; YBR118W 289 Phosphoserine +P02994 YPR080W; YBR118W 316 N6%2CN6-dimethyllysine%3B +P02994 YPR080W; YBR118W 316 N6-methyllysine%3B +P02994 YPR080W; YBR118W 390 N6-methyllysine%3B +P02994 YPR080W; YBR118W 414 Phosphoserine +P02994 YPR080W; YBR118W 430 Phosphothreonine +P02994 YPR080W; YBR118W 458 Lysine +P02994 YPR080W; YBR118W 224 Glycyl +P02994 YPR080W; YBR118W 242 Glycyl +P02994 YPR080W; YBR118W 253 Glycyl +P02994 YPR080W; YBR118W 271 Glycyl +P02994 YPR080W; YBR118W 393 Glycyl +P02994 YPR080W; YBR118W 437 Glycyl +Q03653 YMR212C EFR3 227 Phosphoserine +Q03653 YMR212C EFR3 231 Phosphothreonine +Q03653 YMR212C EFR3 564 Phosphoserine +Q03653 YMR212C EFR3 625 Phosphoserine +Q03653 YMR212C EFR3 632 Phosphoserine +Q03653 YMR212C EFR3 643 Phosphoserine +Q03653 YMR212C EFR3 675 Phosphoserine +Q03653 YMR212C EFR3 687 Phosphothreonine +Q03653 YMR212C EFR3 690 Phosphothreonine +Q03653 YMR212C EFR3 735 Phosphoserine +Q03653 YMR212C EFR3 771 Phosphoserine +Q03653 YMR212C EFR3 774 Phosphoserine +P09032 YOR260W GCD1 296 Phosphoserine +P09032 YOR260W GCD1 300 Phosphoserine +P09032 YOR260W GCD1 306 Phosphothreonine +P38121 YBL035C POL12 126 Phosphoserine +P13382 YNL102W POL1 2 N-acetylserine +P13382 YNL102W POL1 31 Phosphoserine +P13382 YNL102W POL1 82 Phosphoserine +P13382 YNL102W POL1 83 Phosphoserine +P13382 YNL102W POL1 84 Phosphoserine +P13382 YNL102W POL1 169 Phosphoserine +P13382 YNL102W POL1 170 Phosphoserine +P13382 YNL102W POL1 172 Phosphothreonine +P13382 YNL102W POL1 240 Phosphoserine +P13382 YNL102W POL1 274 Phosphoserine +P13382 YNL102W POL1 309 Phosphothreonine +P13382 YNL102W POL1 313 Phosphothreonine +Q05521 YDR284C DPP1 285 Phosphoserine +Q08729 YOR264W DSE3 395 Phosphoserine +P48510 YMR276W DSK2 13 Glycyl +P48510 YMR276W DSK2 76 Glycyl +P40568 YIR010W DSN1 250 Phosphoserine +P36049 YKL172W EBP2 104 Phosphoserine +P36049 YKL172W EBP2 177 Phosphoserine +P36049 YKL172W EBP2 183 Phosphoserine +Q99252 YOR092W ECM3 291 Phosphoserine +Q99252 YOR092W ECM3 338 Phosphoserine +P53168 YGL061C DUO1 2 N-acetylserine +P36041 YKL204W EAP1 30 Phosphoserine +P36041 YKL204W EAP1 281 Phosphoserine +P36041 YKL204W EAP1 282 Phosphoserine +P36041 YKL204W EAP1 327 Phosphoserine +P36041 YKL204W EAP1 344 Phosphoserine +P36041 YKL204W EAP1 387 Phosphoserine +P42835 YNL327W EGT2 1020 GPI-anchor +P42835 YNL327W EGT2 65 N-linked +P42835 YNL327W EGT2 103 N-linked +P42835 YNL327W EGT2 161 N-linked +P42835 YNL327W EGT2 175 N-linked +P42835 YNL327W EGT2 249 N-linked +P42835 YNL327W EGT2 332 N-linked +P42835 YNL327W EGT2 401 N-linked +P42835 YNL327W EGT2 435 N-linked +P42835 YNL327W EGT2 465 N-linked +P42835 YNL327W EGT2 485 N-linked +P42835 YNL327W EGT2 506 N-linked +P42835 YNL327W EGT2 526 N-linked +P42835 YNL327W EGT2 544 N-linked +P42835 YNL327W EGT2 556 N-linked +P42835 YNL327W EGT2 635 N-linked +P42835 YNL327W EGT2 636 N-linked +P42835 YNL327W EGT2 657 N-linked +P42835 YNL327W EGT2 709 N-linked +P42835 YNL327W EGT2 756 N-linked +P47120 YJR070C LIA1 2 N-acetylserine +P47120 YJR070C LIA1 126 Phosphoserine +P47120 YJR070C LIA1 187 Phosphothreonine +P47120 YJR070C LIA1 281 Phosphoserine +P27344 YBR278W DPB3 186 Phosphoserine +P27344 YBR278W DPB3 188 Phosphoserine +P27344 YBR278W DPB3 189 Phosphoserine +P40487 YIL103W DPH1 44 Phosphoserine +P47013 YJL134W LCB3 16 Phosphothreonine +P47013 YJL134W LCB3 18 Phosphoserine +P38844 YHR143W DSE2 308 GPI-anchor +P43616 YFR044C DUG1 451 Phosphoserine +P32528 YBR208C DUR1,2 803 Phosphoserine +P32528 YBR208C DUR1,2 1798 N6-biotinyllysine +P53759 YML080W DUS1 2 N-acetylthreonine +P53063 YGL246C RAI1 198 Phosphoserine +Q06337 YDR359C EAF1 841 Phosphoserine +Q06337 YDR359C EAF1 971 Phosphothreonine +P53911 YNL136W EAF7 200 Phosphoserine +P53911 YNL136W EAF7 225 Phosphoserine +Q03212 YMR171C EAR1 519 Phosphoserine +Q03212 YMR171C EAR1 538 Phosphoserine +Q03212 YMR171C EAR1 110 N-linked +Q03212 YMR171C EAR1 203 N-linked +Q03212 YMR171C EAR1 210 N-linked +Q03212 YMR171C EAR1 256 N-linked +Q03212 YMR171C EAR1 295 N-linked +P38167 YBL101C ECM21 18 Phosphoserine +P38167 YBL101C ECM21 115 Phosphoserine +P38167 YBL101C ECM21 140 Phosphoserine +P38167 YBL101C ECM21 286 Phosphoserine +P38167 YBL101C ECM21 527 Phosphoserine +P38167 YBL101C ECM21 550 Phosphoserine +P38167 YBL101C ECM21 775 Phosphoserine +P38167 YBL101C ECM21 1035 Phosphoserine +P38167 YBL101C ECM21 191 Glycyl +P38167 YBL101C ECM21 577 Glycyl +P38167 YBL101C ECM21 651 Glycyl +P38167 YBL101C ECM21 712 Glycyl +P38167 YBL101C ECM21 794 Glycyl +P38167 YBL101C ECM21 807 Glycyl +P38167 YBL101C ECM21 1024 Glycyl +P38737 YHL030W ECM29 2 N-acetylserine +P38737 YHL030W ECM29 1692 Phosphoserine +P32497 YMR309C NIP1 98 Phosphoserine +P32497 YMR309C NIP1 99 Phosphoserine +P32497 YMR309C NIP1 103 Phosphoserine +Q12050 YOR144C ELG1 6 Phosphoserine +P25574 YCL045C EMC1 73 N-linked +P25574 YCL045C EMC1 106 N-linked +P25574 YCL045C EMC1 192 N-linked +P25574 YCL045C EMC1 202 N-linked +P25574 YCL045C EMC1 420 N-linked +P25574 YCL045C EMC1 443 N-linked +P25574 YCL045C EMC1 574 N-linked +P25574 YCL045C EMC1 578 N-linked +P40077 YER124C DSE1 553 Glycyl +Q12432 YPR023C EAF3 201 Phosphoserine +P32471 YAL003W EFB1 2 N-acetylalanine +P32471 YAL003W EFB1 31 Phosphoserine +P32471 YAL003W EFB1 86 Phosphoserine +P32471 YAL003W EFB1 13 Glycyl +P29547 YPL048W CAM1 2 N-acetylserine +P29547 YPL048W CAM1 32 Phosphothreonine +P32324 YOR133W; YDR385W 509 N6%2CN6%2CN6-trimethyllysine%3B +P32324 YOR133W; YDR385W 509 N6%2CN6-dimethyllysine%3B +P32324 YOR133W; YDR385W 509 N6-methyllysine%3B +P32324 YOR133W; YDR385W 579 Phosphoserine +P32324 YOR133W; YDR385W 613 N6%2CN6-dimethyllysine%3B +P32324 YOR133W; YDR385W 613 N6-methyllysine%3B +P32324 YOR133W; YDR385W 699 Diphthamide +P32324 YOR133W; YDR385W 713 Phosphothreonine +P32324 YOR133W; YDR385W 763 Phosphothreonine +P32324 YOR133W; YDR385W 841 Glycyl +P47163 YJR129C EFM3 177 Phosphothreonine +P24482 YPR175W DPB2 122 Phosphoserine +P24482 YPR175W DPB2 141 Phosphoserine%3B +P24482 YPR175W DPB2 613 Phosphoserine +P39985 YEL055C POL5 789 Phosphoserine +Q06673 YLR436C ECM30 635 Phosphoserine +Q06673 YLR436C ECM30 1065 Phosphoserine +P38728 YHL043W ECM34 45 N-linked +Q05902 YLR299W ECM38 119 N-linked +Q05902 YLR299W ECM38 191 N-linked +Q05902 YLR299W ECM38 270 N-linked +Q05902 YLR299W ECM38 298 N-linked +Q05902 YLR299W ECM38 454 N-linked +Q05902 YLR299W ECM38 517 N-linked +P47138 YJR097W JJJ3 2 N-acetylserine +P14020 YPR183W DPM1 2 N-acetylserine +P14020 YPR183W DPM1 141 Phosphoserine%3B +P15436 YDL102W POL3 30 Phosphoserine +P15436 YDL102W POL3 37 Phosphoserine +P39009 YDL101C DUN1 10 Phosphoserine +P39009 YDL101C DUN1 139 Phosphoserine +P39009 YDL101C DUN1 380 Phosphothreonine +Q04067 YDR429C TIF35 2 N-acetylserine +Q04067 YDR429C TIF35 131 Phosphoserine +Q03764 YDR147W EKI1 23 Phosphoserine +Q02884 YPL101W ELP4 222 Phosphoserine +Q04409 YDR516C EMI2 2 N-acetylserine +Q04409 YDR516C EMI2 2 Phosphoserine +Q04409 YDR516C EMI2 470 Phosphoserine +P38333 YBR247C ENP1 172 Phosphoserine%3B +P38333 YBR247C ENP1 190 Phosphoserine +P38333 YBR247C ENP1 404 Phosphoserine +P54781 YMR015C ERG5 164 Glycyl +P54781 YMR015C ERG5 198 Glycyl +P53080 YGL222C EDC1 2 N-acetylserine +P53080 YGL222C EDC1 82 Phosphoserine +P39998 YEL015W EDC3 257 Phosphoserine +P39998 YEL015W EDC3 261 Phosphoserine +P14741 YKR026C GCN3 2 N-acetylserine +P14741 YKR026C GCN3 291 Phosphothreonine +P32501 YDR211W GCD6 478 Phosphoserine +P32501 YDR211W GCD6 481 Phosphoserine +P32501 YDR211W GCD6 507 Phosphoserine +P32501 YDR211W GCD6 525 Phosphoserine +P32501 YDR211W GCD6 538 Phosphoserine +P32501 YDR211W GCD6 707 Phosphoserine +Q05775 YLR192C HCR1 75 Phosphothreonine +Q05775 YLR192C HCR1 92 Phosphoserine +P36053 YKL160W ELF1 55 Phosphoserine +P36053 YKL160W ELF1 117 Phosphoserine +P36053 YKL160W ELF1 124 Phosphoserine +P36053 YKL160W ELF1 142 Phosphoserine +P25358 YCR034W ELO2 334 Phosphothreonine +P25358 YCR034W ELO2 336 Phosphoserine +P25358 YCR034W ELO2 338 Phosphoserine +P25358 YCR034W ELO2 32 N-linked +P39013 YNL084C END3 276 Phosphoserine +Q05785 YLR206W ENT2 165 Phosphothreonine +Q05785 YLR206W ENT2 167 Phosphoserine +Q05785 YLR206W ENT2 430 Phosphothreonine +Q05785 YLR206W ENT2 434 Phosphoserine +Q05785 YLR206W ENT2 450 Phosphothreonine +Q05785 YLR206W ENT2 468 Phosphothreonine +Q05785 YLR206W ENT2 470 Phosphothreonine +Q05785 YLR206W ENT2 426 Glycyl +Q12003 YPL236C ENV7 13 S-palmitoyl +Q12003 YPL236C ENV7 14 S-palmitoyl +Q12003 YPL236C ENV7 15 S-palmitoyl +O13529 YHR021W-A ECM12 2 N-linked +O13529 YHR021W-A ECM12 132 N-linked +O13529 YHR021W-A ECM12 137 N-linked +P39715 YAL059W ECM1 188 Phosphoserine +P34216 YBL047C EDE1 238 Phosphothreonine +P34216 YBL047C EDE1 241 Phosphoserine +P34216 YBL047C EDE1 244 Phosphoserine +P34216 YBL047C EDE1 245 Phosphothreonine +P34216 YBL047C EDE1 248 Phosphoserine +P34216 YBL047C EDE1 249 Phosphoserine +P34216 YBL047C EDE1 251 Phosphothreonine +P34216 YBL047C EDE1 265 Phosphoserine +P34216 YBL047C EDE1 419 Phosphoserine +P34216 YBL047C EDE1 450 Phosphothreonine +P34216 YBL047C EDE1 477 Phosphothreonine +P34216 YBL047C EDE1 487 Phosphothreonine +P34216 YBL047C EDE1 495 Phosphoserine +P34216 YBL047C EDE1 848 Phosphoserine +P34216 YBL047C EDE1 931 Phosphoserine +P34216 YBL047C EDE1 950 Phosphoserine +P34216 YBL047C EDE1 964 Phosphoserine +P34216 YBL047C EDE1 1008 Phosphoserine +P34216 YBL047C EDE1 1012 Phosphoserine +P34216 YBL047C EDE1 1020 Phosphoserine +P34216 YBL047C EDE1 1046 Phosphothreonine +P34216 YBL047C EDE1 1069 Phosphoserine +P34216 YBL047C EDE1 1087 Phosphoserine +P34216 YBL047C EDE1 1093 Phosphoserine +P34216 YBL047C EDE1 1095 Phosphoserine +P34216 YBL047C EDE1 1096 Phosphoserine +P34216 YBL047C EDE1 1100 Phosphoserine +P34216 YBL047C EDE1 1111 Phosphothreonine +P34216 YBL047C EDE1 1181 Phosphoserine +P34216 YBL047C EDE1 1187 Phosphoserine +P34216 YBL047C EDE1 1307 Phosphothreonine +P34216 YBL047C EDE1 1343 Phosphoserine +P34216 YBL047C EDE1 674 Glycyl +P34216 YBL047C EDE1 1329 Glycyl +P36008 YKL081W TEF4 2 N-acetylserine +P53978 YNL014W HEF3 2 N-acetylserine +P53978 YNL014W HEF3 187 N6%2CN6%2CN6-trimethyllysine +P53978 YNL014W HEF3 196 N6%2CN6%2CN6-trimethyllysine +P53978 YNL014W HEF3 789 N6%2CN6%2CN6-trimethyllysine +P53978 YNL014W HEF3 972 Phosphothreonine +P53978 YNL014W HEF3 974 Phosphoserine +P53978 YNL014W HEF3 1039 Phosphoserine +P53978 YNL014W HEF3 1040 Phosphoserine +P12754 YGR083C GCD2 2 N-acetylserine +P12754 YGR083C GCD2 106 Phosphoserine +P12754 YGR083C GCD2 121 Phosphothreonine +P32801 YKL048C ELM1 152 Phosphoserine +P32801 YKL048C ELM1 516 Phosphoserine +P32801 YKL048C ELM1 519 Phosphoserine +P32476 YGR175C ERG1 284 Glycyl +P32476 YGR175C ERG1 289 Glycyl +P32476 YGR175C ERG1 311 Glycyl +P38819 YHR110W ERP5 171 N-linked +Q08649 YOR244W ESA1 17 Phosphoserine +Q08649 YOR244W ESA1 262 N6-acetyllysine%3B +Q06340 YDR363W ESC2 90 Phosphoserine +Q06340 YDR363W ESC2 125 Phosphoserine +Q06340 YDR363W ESC2 126 Phosphoserine +Q06344 YDR365C ESF1 86 Phosphoserine +Q06344 YDR365C ESF1 220 Phosphothreonine +Q06344 YDR365C ESF1 223 Phosphoserine +Q06344 YDR365C ESF1 225 Phosphoserine +Q06344 YDR365C ESF1 367 Phosphoserine +Q06344 YDR365C ESF1 369 Phosphoserine +Q06344 YDR365C ESF1 372 Phosphoserine +Q06344 YDR365C ESF1 542 Phosphothreonine +P22696 YJR017C ESS1 161 Phosphoserine +P32474 YDR518W EUG1 159 N-linked +P32474 YDR518W EUG1 174 N-linked +P32474 YDR518W EUG1 207 N-linked +P32474 YDR518W EUG1 293 N-linked +P32474 YDR518W EUG1 462 N-linked +Q02908 YPL086C ELP3 453 Glycyl +P00925 YHR174W ENO2 138 Phosphoserine +P00925 YHR174W ENO2 188 Phosphoserine +P00925 YHR174W ENO2 313 Phosphothreonine +P00925 YHR174W ENO2 324 Phosphothreonine +P00925 YHR174W ENO2 60 Glycyl +P00925 YHR174W ENO2 243 Glycyl +P00925 YHR174W ENO2 358 Glycyl +Q12518 YDL161W ENT1 160 Phosphothreonine +Q12518 YDL161W ENT1 163 Phosphoserine +Q12518 YDL161W ENT1 180 Phosphothreonine +Q12518 YDL161W ENT1 328 Phosphoserine +Q12518 YDL161W ENT1 364 Phosphothreonine +Q12518 YDL161W ENT1 366 Phosphothreonine +Q12518 YDL161W ENT1 384 Phosphothreonine +Q12518 YDL161W ENT1 386 Phosphothreonine +Q12518 YDL161W ENT1 388 Phosphothreonine +Q12518 YDL161W ENT1 395 Phosphothreonine%3B +Q12518 YDL161W ENT1 415 Phosphothreonine%3B +Q12518 YDL161W ENT1 357 Glycyl +P47160 YJR125C ENT3 2 N-acetylserine +P47160 YJR125C ENT3 196 Phosphoserine +P47160 YJR125C ENT3 198 Phosphoserine +P47160 YJR125C ENT3 203 Phosphoserine +P47160 YJR125C ENT3 212 Phosphoserine +P47160 YJR125C ENT3 223 Phosphoserine +Q03769 YDR153C ENT5 1 N-acetylmethionine +Q03769 YDR153C ENT5 322 Phosphoserine +Q03769 YDR153C ENT5 324 Phosphoserine +Q03769 YDR153C ENT5 363 Phosphoserine +Q03769 YDR153C ENT5 368 Phosphothreonine +Q03769 YDR153C ENT5 394 Phosphoserine +Q03769 YDR153C ENT5 401 Phosphoserine +Q08651 YOR246C ENV9 282 N-linked +P25087 YML008C ERG6 2 N-acetylserine +P25087 YML008C ERG6 99 Phosphoserine +P40456 YIL151C ESL1 170 Phosphoserine +P40456 YIL151C ESL1 190 Phosphoserine +Q07872 YLL038C ENT4 195 Phosphoserine +P40557 YIL005W EPS1 85 N-linked +P40557 YIL005W EPS1 264 N-linked +P40557 YIL005W EPS1 299 N-linked +P40557 YIL005W EPS1 370 N-linked +P38604 YHR072W ERG7 2 N-acetylthreonine +P38836 YHR132C ECM14 41 N-linked +P38836 YHR132C ECM14 295 N-linked +Q05958 YLR228C ECM22 431 Phosphoserine +Q05958 YLR228C ECM22 445 Phosphoserine +Q05958 YLR228C ECM22 464 Phosphoserine +P32644 YER176W ECM32 227 Phosphoserine +P32644 YER176W ECM32 392 Phosphoserine +P32644 YER176W ECM32 465 Phosphothreonine +P38248 YBR078W ECM33 339 Phosphoserine +P38248 YBR078W ECM33 406 GPI-anchor +P38248 YBR078W ECM33 21 N-linked +P38248 YBR078W ECM33 56 N-linked +P38248 YBR078W ECM33 82 N-linked +P38248 YBR078W ECM33 196 N-linked +P38248 YBR078W ECM33 209 N-linked +P38248 YBR078W ECM33 227 N-linked +P38248 YBR078W ECM33 234 N-linked +P38248 YBR078W ECM33 241 N-linked +P38248 YBR078W ECM33 267 N-linked +P38248 YBR078W ECM33 279 N-linked +P38248 YBR078W ECM33 304 N-linked +P38248 YBR078W ECM33 328 N-linked +P38248 YBR078W ECM33 389 N-linked +P43605 YFR027W ECO1 223 N6-acetyllysine%3B +P38249 YBR079C RPG1 508 Phosphoserine +P38249 YBR079C RPG1 691 Phosphoserine +P38249 YBR079C RPG1 935 Phosphothreonine +P40217 YMR146C TIF34 302 Phosphoserine +Q05050 YMR031C EIS1 2 N-acetylserine +Q05050 YMR031C EIS1 2 Phosphoserine +Q05050 YMR031C EIS1 88 Phosphoserine +Q05050 YMR031C EIS1 130 Phosphoserine +Q05050 YMR031C EIS1 182 Phosphoserine +Q05050 YMR031C EIS1 401 Phosphoserine +Q05050 YMR031C EIS1 584 Phosphoserine +Q05050 YMR031C EIS1 710 Phosphoserine +Q05050 YMR031C EIS1 720 Phosphothreonine +Q05050 YMR031C EIS1 763 Phosphoserine +Q05050 YMR031C EIS1 775 Phosphoserine +Q05050 YMR031C EIS1 816 Phosphoserine +Q05050 YMR031C EIS1 828 Phosphoserine +Q05050 YMR031C EIS1 829 Phosphoserine +Q05050 YMR031C EIS1 838 Phosphoserine +P40319 YLR372W ELO3 2 N-linked +P40319 YLR372W ELO3 20 N-linked +P40319 YLR372W ELO3 66 N-linked +P53861 YNL230C ELA1 235 Phosphoserine +P53861 YNL230C ELA1 278 Phosphoserine +P53753 YNR067C DSE4 138 N-linked +P53753 YNR067C DSE4 186 N-linked +P53753 YNR067C DSE4 223 N-linked +P53753 YNR067C DSE4 259 N-linked +P53753 YNR067C DSE4 280 N-linked +P53753 YNR067C DSE4 303 N-linked +P53753 YNR067C DSE4 307 N-linked +P53753 YNR067C DSE4 393 N-linked +P53753 YNR067C DSE4 533 N-linked +P53753 YNR067C DSE4 886 N-linked +P06103 YOR361C PRT1 61 Phosphoserine +P06103 YOR361C PRT1 67 Phosphotyrosine +P06103 YOR361C PRT1 669 Phosphoserine +P00924 YGR254W ENO1 119 Phosphoserine +P00924 YGR254W ENO1 138 Phosphoserine +P00924 YGR254W ENO1 188 Phosphoserine +P00924 YGR254W ENO1 313 Phosphothreonine +P00924 YGR254W ENO1 324 Phosphothreonine +P00924 YGR254W ENO1 60 Glycyl +P00924 YGR254W ENO1 243 Glycyl +P00924 YGR254W ENO1 358 Glycyl +P32353 YLR056W ERG3 324 Glycyl +P32353 YLR056W ERG3 344 Glycyl +Q03071 YPL046C ELC1 2 N-acetylserine +Q03071 YPL046C ELC1 2 Phosphoserine +P53938 YNL080C EOS1 103 N-linked +P53938 YNL080C EOS1 104 N-linked +Q12452 YLR100W ERG27 345 Phosphothreonine +P38748 YHL010C ETP1 376 Phosphoserine +P38748 YHL010C ETP1 369 Glycyl +P38748 YHL010C ETP1 410 Glycyl +P38748 YHL010C ETP1 450 Glycyl +P38071 YBR026C ETR1 339 Phosphoserine +P23776 YLR300W EXG1 165 N-linked +P23776 YLR300W EXG1 325 N-linked +P52911 YDR261C EXG2 50 N-linked +P52911 YDR261C EXG2 77 N-linked +P52911 YDR261C EXG2 86 N-linked +P52911 YDR261C EXG2 90 N-linked +P52911 YDR261C EXG2 106 N-linked +P52911 YDR261C EXG2 157 N-linked +P52911 YDR261C EXG2 220 N-linked +P52911 YDR261C EXG2 281 N-linked +P52911 YDR261C EXG2 285 N-linked +P52911 YDR261C EXG2 310 N-linked +P52911 YDR261C EXG2 317 N-linked +P52911 YDR261C EXG2 322 N-linked +P52911 YDR261C EXG2 401 N-linked +P52911 YDR261C EXG2 480 N-linked +P52911 YDR261C EXG2 539 N-linked +Q04660 YMR049C ERB1 23 Phosphoserine +Q04660 YMR049C ERB1 72 Phosphoserine +Q04660 YMR049C ERB1 76 Phosphoserine +Q04660 YMR049C ERB1 146 Phosphoserine +Q04660 YMR049C ERB1 149 Phosphoserine +Q04660 YMR049C ERB1 418 Phosphoserine +Q04660 YMR049C ERB1 127 Glycyl +P05453 YDR172W SUP35 2 N-acetylserine +P05453 YDR172W SUP35 571 Phosphoserine +P19097 YPL231W FAS2 50 Phosphoserine +P19097 YPL231W FAS2 180 O-(pantetheine +P19097 YPL231W FAS2 523 Phosphoserine +P19097 YPL231W FAS2 958 Phosphoserine +P19097 YPL231W FAS2 1440 Phosphoserine +P19097 YPL231W FAS2 37 Glycyl +P53917 YNL127W FAR11 18 Phosphoserine +P53917 YNL127W FAR11 81 Phosphoserine +P53917 YNL127W FAR11 524 Phosphoserine +P53917 YNL127W FAR11 527 Phosphoserine +P53917 YNL127W FAR11 528 Phosphoserine +P21268 YJL157C FAR1 87 Phosphoserine%3B +P21268 YJL157C FAR1 110 Phosphoserine +P21268 YJL157C FAR1 114 Phosphoserine +P21268 YJL157C FAR1 306 Phosphothreonine +P15646 YDL014W NOP1 16 Asymmetric +P15646 YDL014W NOP1 16 Omega-N-methylarginine%3B +P15646 YDL014W NOP1 22 Omega-N-methylarginine%3B +P15646 YDL014W NOP1 30 Asymmetric +P15646 YDL014W NOP1 34 Asymmetric +P15646 YDL014W NOP1 34 Omega-N-methylarginine%3B +P15646 YDL014W NOP1 40 Omega-N-methylarginine%3B +P15646 YDL014W NOP1 48 Asymmetric +P15646 YDL014W NOP1 52 Asymmetric +P15646 YDL014W NOP1 52 Omega-N-methylarginine%3B +P15646 YDL014W NOP1 58 Omega-N-methylarginine%3B +P15646 YDL014W NOP1 70 Asymmetric +P15646 YDL014W NOP1 70 Omega-N-methylarginine%3B +P15646 YDL014W NOP1 73 Asymmetric +P15646 YDL014W NOP1 73 Omega-N-methylarginine%3B +P15646 YDL014W NOP1 81 Asymmetric +P15646 YDL014W NOP1 81 Omega-N-methylarginine%3B +P15646 YDL014W NOP1 150 Glycyl +P40988 YMR319C FET4 48 Phosphoserine +P40988 YMR319C FET4 50 Phosphoserine +P40988 YMR319C FET4 39 Glycyl +P53918 YNL125C ESBP6 57 Phosphoserine +P53918 YNL125C ESBP6 112 Phosphoserine +P53918 YNL125C ESBP6 172 Phosphoserine +P53918 YNL125C ESBP6 637 Phosphoserine +P53918 YNL125C ESBP6 230 N-linked +P53918 YNL125C ESBP6 471 N-linked +P53918 YNL125C ESBP6 492 N-linked +P38224 YBR040W FIG1 288 Phosphoserine +P38224 YBR040W FIG1 293 Phosphothreonine +P38224 YBR040W FIG1 296 Phosphoserine +P40020 YER032W FIR1 81 Phosphoserine +P40020 YER032W FIR1 172 Phosphoserine +P40020 YER032W FIR1 225 Phosphoserine +Q08906 YOR382W FIT2 130 GPI-anchor +Q08906 YOR382W FIT2 92 N-linked +P12385 YBR143C SUP45 182 N5-methylglutamine +P12385 YBR143C SUP45 421 Phosphoserine +P12385 YBR143C SUP45 331 Glycyl +Q03103 YML130C ERO1 21 N-linked +Q03103 YML130C ERO1 35 N-linked +Q03103 YML130C ERO1 53 N-linked +Q03103 YML130C ERO1 130 N-linked +Q03103 YML130C ERO1 342 N-linked +Q03103 YML130C ERO1 425 N-linked +Q03103 YML130C ERO1 458 N-linked +Q03103 YML130C ERO1 468 N-linked +Q03103 YML130C ERO1 491 N-linked +P17261 YCR075C ERS1 177 N-linked +Q03661 YMR219W ESC1 500 Phosphothreonine +Q03661 YMR219W ESC1 532 Phosphoserine +Q03661 YMR219W ESC1 579 Phosphoserine +Q03661 YMR219W ESC1 583 Phosphoserine +Q03661 YMR219W ESC1 608 Phosphoserine +Q03661 YMR219W ESC1 662 Phosphoserine +Q03661 YMR219W ESC1 865 Phosphoserine +Q03661 YMR219W ESC1 866 Phosphoserine +Q03661 YMR219W ESC1 888 Phosphoserine +Q03661 YMR219W ESC1 911 Phosphoserine +Q03661 YMR219W ESC1 937 Phosphoserine +Q03661 YMR219W ESC1 1092 Phosphoserine +Q03661 YMR219W ESC1 1096 Phosphoserine +Q03661 YMR219W ESC1 1098 Phosphoserine +Q03661 YMR219W ESC1 1166 Phosphoserine +Q03661 YMR219W ESC1 1176 Phosphoserine +Q03661 YMR219W ESC1 1178 Phosphoserine +Q03661 YMR219W ESC1 1214 Phosphoserine +Q03661 YMR219W ESC1 1254 Phosphoserine +Q03661 YMR219W ESC1 1290 Phosphoserine +Q03661 YMR219W ESC1 1326 Phosphoserine +Q03661 YMR219W ESC1 1332 Phosphoserine +Q03661 YMR219W ESC1 1403 Phosphoserine +Q03661 YMR219W ESC1 1409 Phosphoserine +Q03661 YMR219W ESC1 1450 Phosphoserine +Q03661 YMR219W ESC1 1454 Phosphoserine +Q03661 YMR219W ESC1 1539 Phosphoserine +Q03661 YMR219W ESC1 1590 Phosphoserine +Q03661 YMR219W ESC1 1591 Phosphoserine +P53743 YNR054C ESF2 7 Phosphoserine +P53743 YNR054C ESF2 13 Phosphoserine +P53743 YNR054C ESF2 14 Phosphoserine +P42940 YGR207C CIR1 2 N-acetylserine +Q08421 YOR051C ETT1 30 Phosphoserine +P39875 YOR033C EXO1 372 Phosphoserine +P38261 YBR102C EXO84 58 Phosphothreonine +P38261 YBR102C EXO84 139 Phosphoserine +P38261 YBR102C EXO84 482 Phosphoserine +P38261 YBR102C EXO84 219 Glycyl +P09201 YLR377C FBP1 12 Phosphoserine +P34756 YFR019W FAB1 2 N-acetylserine +P34756 YFR019W FAB1 186 Phosphoserine +P34756 YFR019W FAB1 1627 Phosphoserine +P34756 YFR019W FAB1 1630 Phosphoserine +P34756 YFR019W FAB1 1938 Phosphoserine +P34756 YFR019W FAB1 1953 Phosphothreonine +P32604 YJL155C FBP26 435 Phosphoserine +P32604 YJL155C FBP26 446 Phosphoserine +Q04952 YMR306W FKS3 844 N-linked +Q04952 YMR306W FKS3 874 N-linked +Q04952 YMR306W FKS3 955 N-linked +Q04952 YMR306W FKS3 1002 N-linked +Q04952 YMR306W FKS3 1170 N-linked +Q04952 YMR306W FKS3 1360 N-linked +Q04952 YMR306W FKS3 1579 N-linked +Q04952 YMR306W FKS3 1761 N-linked +P36170 YKR102W FLO10 1146 GPI-anchor +P36170 YKR102W FLO10 122 N-linked +P36170 YKR102W FLO10 157 N-linked +P36170 YKR102W FLO10 279 N-linked +P36170 YKR102W FLO10 389 N-linked +P36170 YKR102W FLO10 452 N-linked +P36170 YKR102W FLO10 515 N-linked +P36170 YKR102W FLO10 578 N-linked +P36170 YKR102W FLO10 656 N-linked +P36170 YKR102W FLO10 686 N-linked +P36170 YKR102W FLO10 879 N-linked +P36170 YKR102W FLO10 1092 N-linked +P36170 YKR102W FLO10 1099 N-linked +P08640 YIR019C FLO11 1346 GPI-anchor +P08640 YIR019C FLO11 817 N-linked +P08640 YIR019C FLO11 874 N-linked +P32768 YAR050W FLO1 1514 GPI-anchor +P32768 YAR050W FLO1 135 N-linked +P32768 YAR050W FLO1 187 N-linked +P32768 YAR050W FLO1 262 N-linked +P32768 YAR050W FLO1 329 N-linked +P32768 YAR050W FLO1 374 N-linked +P32768 YAR050W FLO1 419 N-linked +P32768 YAR050W FLO1 464 N-linked +P32768 YAR050W FLO1 509 N-linked +P32768 YAR050W FLO1 554 N-linked +P32768 YAR050W FLO1 599 N-linked +P32768 YAR050W FLO1 644 N-linked +P32768 YAR050W FLO1 689 N-linked +P32768 YAR050W FLO1 734 N-linked +P32768 YAR050W FLO1 1114 N-linked +Q05040 YMR029C FAR8 115 Phosphoserine +Q05040 YMR029C FAR8 132 Phosphothreonine +Q08907 YOR383C FIT3 182 GPI-anchor +P53971 YNL023C FAP1 951 Phosphothreonine +P53971 YNL023C FAP1 958 Phosphoserine +Q03254 YMR277W FCP1 701 Phosphoserine +Q03254 YMR277W FCP1 718 Phosphoserine +Q03254 YMR277W FCP1 720 Phosphoserine +Q03254 YMR277W FCP1 74 Glycyl +Q12119 YER060W-A FCY22 46 Phosphothreonine +P17064 YER056C FCY2 18 Phosphoserine +P17064 YER056C FCY2 16 Glycyl +P39676 YGR234W YHB1 22 Phosphothreonine +P07149 YKL182W FAS1 1 N-acetylmethionine +P07149 YKL182W FAS1 733 Phosphothreonine +P07149 YKL182W FAS1 1121 Phosphoserine +P07149 YKL182W FAS1 1364 Glycyl +P40039 YER060W FCY21 43 Phosphoserine +P40039 YER060W FCY21 46 Phosphothreonine +Q08991 YPL279C FEX2 109 N-linked +Q08991 YPL279C FEX2 117 N-linked +Q08991 YPL279C FEX2 235 N-linked +P25653 YCR089W FIG2 1588 GPI-anchor +P25653 YCR089W FIG2 29 N-linked +P25653 YCR089W FIG2 231 N-linked +P25653 YCR089W FIG2 298 N-linked +P25653 YCR089W FIG2 347 N-linked +P25653 YCR089W FIG2 386 N-linked +P25653 YCR089W FIG2 426 N-linked +P25653 YCR089W FIG2 495 N-linked +P25653 YCR089W FIG2 535 N-linked +P25653 YCR089W FIG2 661 N-linked +P25653 YCR089W FIG2 674 N-linked +P25653 YCR089W FIG2 713 N-linked +P25653 YCR089W FIG2 889 N-linked +P25653 YCR089W FIG2 907 N-linked +P25653 YCR089W FIG2 1079 N-linked +P25653 YCR089W FIG2 1400 N-linked +P42837 YNL325C FIG4 829 Phosphoserine +P38911 YML074C FPR3 2 N-acetylserine +P38911 YML074C FPR3 80 Phosphoserine +P38911 YML074C FPR3 81 Phosphoserine +P38911 YML074C FPR3 89 Phosphothreonine +P38911 YML074C FPR3 184 Phosphotyrosine%3B +P38911 YML074C FPR3 186 Phosphoserine%3B +P20081 YNL135C FPR1 2 N-acetylserine +P20081 YNL135C FPR1 51 Phosphoserine +P38631 YLR342W FKS1 269 Phosphothreonine +P38631 YLR342W FKS1 272 Phosphothreonine +P38631 YLR342W FKS1 259 Glycyl +P38631 YLR342W FKS1 275 Glycyl +P38631 YLR342W FKS1 386 Glycyl +P38631 YLR342W FKS1 910 Glycyl +P38631 YLR342W FKS1 915 Glycyl +P38631 YLR342W FKS1 1539 Glycyl +P38631 YLR342W FKS1 1547 Glycyl +Q07825 YLL029W FRA1 69 Phosphoserine +Q07825 YLL029W FRA1 92 Phosphoserine +Q07825 YLL029W FRA1 95 Phosphoserine +P32791 YLR214W FRE1 69 N-linked +P32791 YLR214W FRE1 100 N-linked +P32791 YLR214W FRE1 124 N-linked +P53746 YNR060W FRE4 51 N-linked +P53746 YNR060W FRE4 80 N-linked +P53746 YNR060W FRE4 101 N-linked +P53746 YNR060W FRE4 113 N-linked +P53746 YNR060W FRE4 127 N-linked +P53746 YNR060W FRE4 135 N-linked +P08417 YPL262W FUM1 428 Phosphothreonine +P28003 YAL034C FUN19 194 Phosphothreonine +P28003 YAL034C FUN19 207 Phosphoserine +P28003 YAL034C FUN19 211 Phosphoserine +P11412 YNL241C ZWF1 2 N-acetylserine +P11412 YNL241C ZWF1 142 Phosphoserine +P11412 YNL241C ZWF1 145 Phosphotyrosine +P04385 YBR020W GAL1 381 Phosphoserine +P04386 YPL248C GAL4 694 Phosphotyrosine +P04386 YPL248C GAL4 696 Phosphoserine +P04386 YPL248C GAL4 699 Phosphoserine +P04386 YPL248C GAL4 703 Phosphoserine +P04386 YPL248C GAL4 712 Phosphoserine +Q04739 YER027C GAL83 12 Phosphoserine +Q04739 YER027C GAL83 21 Phosphoserine +Q04739 YER027C GAL83 44 Phosphoserine +Q04739 YER027C GAL83 135 Phosphoserine +Q04739 YER027C GAL83 276 Phosphoserine +Q04739 YER027C GAL83 279 Phosphoserine +P39719 YAL053W FLC2 28 N-linked +P39719 YAL053W FLC2 65 N-linked +P39719 YAL053W FLC2 81 N-linked +P39719 YAL053W FLC2 156 N-linked +P39719 YAL053W FLC2 323 N-linked +P36033 YKL220C FRE2 85 N-linked +P36033 YKL220C FRE2 108 N-linked +P36033 YKL220C FRE2 120 N-linked +P36033 YKL220C FRE2 134 N-linked +P36033 YKL220C FRE2 341 N-linked +Q12473 YLL051C FRE6 89 N-linked +Q12473 YLL051C FRE6 112 N-linked +Q12473 YLL051C FRE6 124 N-linked +P12709 YBR196C PGI1 2 N-acetylserine +P12709 YBR196C PGI1 53 Phosphothreonine +P12709 YBR196C PGI1 220 Phosphothreonine +P17649 YGR019W UGA1 326 N6-(pyridoxal +P38225 YBR041W FAT1 184 N-linked +P38225 YBR041W FAT1 289 N-linked +P38225 YBR041W FAT1 534 N-linked +P38225 YBR041W FAT1 591 N-linked +P38993 YMR058W FET3 27 N-linked +P38993 YMR058W FET3 74 N-linked +P38993 YMR058W FET3 77 N-linked +P38993 YMR058W FET3 88 N-linked +P38993 YMR058W FET3 113 N-linked +P38993 YMR058W FET3 194 N-linked +P38993 YMR058W FET3 198 N-linked +P38993 YMR058W FET3 244 N-linked +P38993 YMR058W FET3 265 N-linked +P38993 YMR058W FET3 292 N-linked +P38993 YMR058W FET3 300 N-linked +P38993 YMR058W FET3 359 N-linked +P38993 YMR058W FET3 381 N-linked +Q08913 YOR390W FEX1 109 N-linked +Q08913 YOR390W FEX1 117 N-linked +Q08913 YOR390W FEX1 235 N-linked +P39521 YPR104C FHL1 44 Phosphoserine +P39521 YPR104C FHL1 228 Phosphoserine +P39521 YPR104C FHL1 230 Phosphothreonine +P39521 YPR104C FHL1 247 Phosphothreonine +P39521 YPR104C FHL1 264 Phosphoserine +P53121 YGL139W FLC3 616 Phosphoserine +P53121 YGL139W FLC3 635 Phosphoserine +P53121 YGL139W FLC3 779 Phosphoserine +P53121 YGL139W FLC3 782 Phosphoserine +P53121 YGL139W FLC3 149 N-linked +P53121 YGL139W FLC3 321 N-linked +P53121 YGL139W FLC3 547 N-linked +Q08967 YPL221W FLC1 610 Phosphoserine +Q08967 YPL221W FLC1 626 Phosphothreonine +Q08967 YPL221W FLC1 771 Phosphoserine +Q08967 YPL221W FLC1 774 Phosphoserine +Q08967 YPL221W FLC1 143 N-linked +Q08967 YPL221W FLC1 281 N-linked +P53739 YNR047W FPK1 140 Phosphoserine +P53739 YNR047W FPK1 144 Phosphoserine +P53739 YNR047W FPK1 171 Phosphoserine +P53739 YNR047W FPK1 175 Phosphoserine +P53739 YNR047W FPK1 185 Phosphoserine +P53739 YNR047W FPK1 300 Phosphoserine +P53739 YNR047W FPK1 414 Phosphoserine +P53739 YNR047W FPK1 462 Phosphoserine +P23900 YLL043W FPS1 150 Phosphoserine +P23900 YLL043W FPS1 168 Phosphothreonine +P23900 YLL043W FPS1 209 Phosphoserine +P23900 YLL043W FPS1 212 Phosphoserine +P38310 YBR207W FTH1 449 Phosphoserine +P38310 YBR207W FTH1 453 Phosphoserine +P00358 YJR009C TDH2 302 Phosphoserine +P00358 YJR009C TDH2 46 Glycyl +P00358 YJR009C TDH2 63 Glycyl +P00359 YGR192C TDH3 302 Phosphoserine +P00359 YGR192C TDH3 46 Glycyl +P00359 YGR192C TDH3 63 Glycyl +P38260 YBR101C FES1 12 Phosphoserine +P43561 YFL041W FET5 24 N-linked +P43561 YFL041W FET5 86 N-linked +P43561 YFL041W FET5 115 N-linked +P43561 YFL041W FET5 196 N-linked +P43561 YFL041W FET5 200 N-linked +P43561 YFL041W FET5 246 N-linked +P43561 YFL041W FET5 295 N-linked +P43561 YFL041W FET5 364 N-linked +P43561 YFL041W FET5 455 N-linked +P41813 YNL068C FKH2 708 Phosphoserine +P41813 YNL068C FKH2 832 Phosphoserine +P41813 YNL068C FKH2 833 Phosphoserine +P40989 YGR032W GSC2 288 Phosphothreonine +P40989 YGR032W GSC2 291 Phosphothreonine +P40989 YGR032W GSC2 278 Glycyl +P40989 YGR032W GSC2 405 Glycyl +P40989 YGR032W GSC2 929 Glycyl +P40989 YGR032W GSC2 934 Glycyl +P40989 YGR032W GSC2 1558 Glycyl +P40989 YGR032W GSC2 1566 Glycyl +Q08905 YOR381W FRE3 85 N-linked +Q08905 YOR381W FRE3 108 N-linked +Q08905 YOR381W FRE3 120 N-linked +Q08905 YOR381W FRE3 134 N-linked +Q08908 YOR384W FRE5 117 N-linked +Q12209 YLR047C FRE8 371 N-linked +Q12209 YLR047C FRE8 383 N-linked +Q12209 YLR047C FRE8 384 N-linked +Q03002 YPL141C FRK1 441 Phosphoserine +Q03898 YDR130C FIN1 54 Phosphoserine +Q03898 YDR130C FIN1 68 Phosphothreonine +Q03898 YDR130C FIN1 74 Phosphoserine +Q03898 YDR130C FIN1 88 Phosphoserine +Q04433 YDR534C FIT1 506 GPI-anchor +Q04433 YDR534C FIT1 412 N-linked +Q04433 YDR534C FIT1 464 N-linked +Q04433 YDR534C FIT1 503 N-linked +P39712 YAL063C FLO9 1299 GPI-anchor +P39712 YAL063C FLO9 135 N-linked +P39712 YAL063C FLO9 187 N-linked +P39712 YAL063C FLO9 203 N-linked +P39712 YAL063C FLO9 257 N-linked +P39712 YAL063C FLO9 262 N-linked +P39712 YAL063C FLO9 270 N-linked +P39712 YAL063C FLO9 329 N-linked +P39712 YAL063C FLO9 419 N-linked +P39712 YAL063C FLO9 464 N-linked +P39712 YAL063C FLO9 509 N-linked +P39712 YAL063C FLO9 554 N-linked +P39712 YAL063C FLO9 599 N-linked +P39712 YAL063C FLO9 644 N-linked +P39712 YAL063C FLO9 689 N-linked +P39712 YAL063C FLO9 734 N-linked +P39712 YAL063C FLO9 888 N-linked +Q07651 YDL222C FMP45 230 Phosphoserine +Q07651 YDL222C FMP45 232 Phosphoserine +Q07651 YDL222C FMP45 235 Phosphothreonine +Q07651 YDL222C FMP45 73 N-linked +P31380 YAL019W FUN30 232 Phosphoserine +P31380 YAL019W FUN30 369 Phosphoserine +P31380 YAL019W FUN30 451 Phosphoserine +Q12035 YLR051C FCF2 1 N-acetylmethionine +Q06205 YLR449W FPR4 80 Phosphoserine +Q06205 YLR449W FPR4 82 Phosphoserine +Q04991 YMR221C FMP42 238 Phosphoserine +Q04991 YMR221C FMP42 249 Phosphoserine +Q04991 YMR221C FMP42 269 Phosphoserine +P53848 YNL256W FOL1 2 N-acetylserine +P53848 YNL256W FOL1 286 Phosphoserine +P38894 YHR211W FLO5 1052 GPI-anchor +P38894 YHR211W FLO5 135 N-linked +P38894 YHR211W FLO5 187 N-linked +P38894 YHR211W FLO5 203 N-linked +P38894 YHR211W FLO5 262 N-linked +P38894 YHR211W FLO5 663 N-linked +P38894 YHR211W FLO5 749 N-linked +Q12029 YOR271C FSF1 2 N-acetylalanine +P16892 YBL016W FUS3 180 Phosphothreonine +P16892 YBL016W FUS3 182 Phosphotyrosine +P16892 YBL016W FUS3 345 Glycyl +P53913 YNL133C FYV6 2 N-acetylserine +P45976 YJR093C FIP1 50 Phosphoserine +P04397 YBR019C GAL10 562 Phosphoserine +P13181 YLR081W GAL2 32 Phosphoserine +P13181 YLR081W GAL2 35 Phosphoserine +P13181 YLR081W GAL2 39 Phosphoserine +P13181 YLR081W GAL2 48 Phosphoserine +P13181 YLR081W GAL2 50 Phosphoserine +P13181 YLR081W GAL2 53 Phosphoserine +P13181 YLR081W GAL2 55 Phosphoserine +P13045 YDR009W GAL3 1 N-acetylmethionine +P43574 YFL021W GAT1 167 Phosphoserine +P43574 YFL021W GAT1 262 Phosphoserine +P43574 YFL021W GAT1 270 Phosphoserine +P43574 YFL021W GAT1 369 Phosphothreonine +P43574 YFL021W GAT1 399 Phosphoserine +P43574 YFL021W GAT1 418 Phosphoserine +P39012 YLR088W GAA1 87 N-linked +P28006 YOR178C GAC1 415 Phosphoserine +P28006 YOR178C GAC1 424 Phosphoserine +P40056 YER083C GET2 2 N-acetylserine +P40056 YER083C GET2 45 Phosphoserine +P40056 YER083C GET2 173 N-linked +P40056 YER083C GET2 196 N-linked +P14742 YKL104C GFA1 253 Phosphoserine +P14742 YKL104C GFA1 334 Phosphothreonine +P14742 YKL104C GFA1 336 Phosphoserine +P40036 YER054C GIP2 51 Phosphoserine +P40036 YER054C GIP2 52 Phosphothreonine +P40036 YER054C GIP2 155 Phosphoserine +P40036 YER054C GIP2 221 Phosphoserine +P40036 YER054C GIP2 238 Phosphoserine +P39732 YAL031C GIP4 497 Phosphoserine +P39732 YAL031C GIP4 501 Phosphoserine +P39732 YAL031C GIP4 609 Phosphoserine +P25346 YCR098C GIT1 80 N-linked +P36143 YKR058W GLG1 230 O-linked +P36143 YKR058W GLG1 598 O-linked +Q05670 YMR232W FUS2 20 Phosphothreonine +Q05670 YMR232W FUS2 67 Phosphoserine +Q05670 YMR232W FUS2 72 Phosphoserine +Q05670 YMR232W FUS2 84 Phosphoserine +Q05670 YMR232W FUS2 88 Phosphothreonine +Q05670 YMR232W FUS2 100 Phosphoserine +Q05670 YMR232W FUS2 106 Phosphoserine +Q08559 YOR183W FYV12 91 N-linked +P46949 YGR196C FYV8 92 Phosphoserine +P46949 YGR196C FYV8 100 Phosphoserine +P46949 YGR196C FYV8 134 Phosphoserine +P46949 YGR196C FYV8 163 Phosphoserine +P46949 YGR196C FYV8 180 Phosphoserine +P46949 YGR196C FYV8 182 Phosphoserine +P46949 YGR196C FYV8 237 Phosphoserine +P46949 YGR196C FYV8 238 Phosphoserine +P46949 YGR196C FYV8 532 Phosphoserine +P08431 YBR018C GAL7 27 Phosphoserine +P04387 YML051W GAL80 1 N-acetylmethionine +P25555 YCL011C GBP2 130 Phosphothreonine +P51601 YGR267C FOL2 15 Phosphothreonine +P51601 YGR267C FOL2 23 Phosphoserine +P43535 YFR009W GCN20 2 N-acetylalanine +Q04839 YMR255W GFD1 87 Phosphoserine +Q04839 YMR255W GFD1 106 Phosphoserine +Q04839 YMR255W GFD1 111 Phosphoserine +P22146 YMR307W GAS1 528 GPI-anchor +P22146 YMR307W GAS1 40 N-linked +P22146 YMR307W GAS1 57 N-linked +P22146 YMR307W GAS1 95 N-linked +P22146 YMR307W GAS1 149 N-linked +P22146 YMR307W GAS1 165 N-linked +P22146 YMR307W GAS1 253 N-linked +P22146 YMR307W GAS1 283 N-linked +P22146 YMR307W GAS1 321 N-linked +P22146 YMR307W GAS1 409 N-linked +P22146 YMR307W GAS1 495 N-linked +Q06135 YLR343W GAS2 531 GPI-anchor +Q06135 YLR343W GAS2 498 N-linked +P39993 YEL022W GEA2 46 Phosphoserine +P39993 YEL022W GEA2 284 Phosphoserine +Q06648 YDR309C GIC2 254 Phosphoserine +Q06648 YDR309C GIC2 258 Phosphoserine +Q06648 YDR309C GIC2 337 Phosphoserine +Q06648 YDR309C GIC2 345 Phosphoserine +Q06648 YDR309C GIC2 367 Phosphoserine +Q03833 YDR096W GIS1 70 Phosphoserine +Q03833 YDR096W GIS1 343 Phosphoserine +Q03833 YDR096W GIS1 690 Phosphoserine +Q03833 YDR096W GIS1 694 Phosphoserine +Q03833 YDR096W GIS1 696 Phosphoserine +Q03833 YDR096W GIS1 734 Phosphoserine +Q03833 YDR096W GIS1 747 Phosphoserine +P38196 YBL042C FUI1 54 Phosphothreonine +P38196 YBL042C FUI1 56 Phosphoserine +P38196 YBL042C FUI1 635 Glycyl +P11710 YCL027W FUS1 178 Phosphothreonine +P11710 YCL027W FUS1 190 Phosphoserine +P11710 YCL027W FUS1 256 Phosphoserine +P11710 YCL027W FUS1 281 Phosphothreonine +P11710 YCL027W FUS1 424 Phosphothreonine +P38297 YBR179C FZO1 398 Glycyl +P38297 YBR179C FZO1 464 Glycyl +P18852 YJR086W STE18 107 Cysteine +P18852 YJR086W STE18 106 S-palmitoyl +P18852 YJR086W STE18 107 S-farnesyl +P47102 YJR031C GEA1 49 Phosphoserine +Q04233 YML006C GIS4 165 Phosphoserine +Q04233 YML006C GIS4 304 Phosphoserine +Q04233 YML006C GIS4 616 Phosphoserine +Q04233 YML006C GIS4 622 Phosphoserine +Q04233 YML006C GIS4 707 Phosphoserine +Q04233 YML006C GIS4 720 Phosphoserine +P32614 YEL047C FRD1 66 Phosphoserine +P31381 YAL022C FUN26 45 Phosphoserine +P31381 YAL022C FUN26 58 Phosphoserine +P19145 YKR039W GAP1 76 Glycyl +P28007 YHR089C GAR1 4 Asymmetric +P28007 YHR089C GAR1 8 Asymmetric +P28007 YHR089C GAR1 11 Asymmetric +P28007 YHR089C GAR1 15 Asymmetric +P28007 YHR089C GAR1 19 Asymmetric +P28007 YHR089C GAR1 147 Asymmetric +P28007 YHR089C GAR1 154 Asymmetric +P28007 YHR089C GAR1 158 Asymmetric +P28007 YHR089C GAR1 162 Asymmetric +P28007 YHR089C GAR1 165 Asymmetric +P28007 YHR089C GAR1 171 Asymmetric +P28007 YHR089C GAR1 174 Asymmetric +P28007 YHR089C GAR1 180 Asymmetric +P28007 YHR089C GAR1 184 Asymmetric +P28007 YHR089C GAR1 189 Asymmetric +P28007 YHR089C GAR1 193 Asymmetric +P28007 YHR089C GAR1 197 Asymmetric +P28007 YHR089C GAR1 201 Asymmetric +P28007 YHR089C GAR1 77 Glycyl +Q03655 YMR215W GAS3 498 GPI-anchor +Q03655 YMR215W GAS3 201 N-linked +Q03655 YMR215W GAS3 269 N-linked +Q03655 YMR215W GAS3 350 N-linked +Q03655 YMR215W GAS3 385 N-linked +Q03655 YMR215W GAS3 404 N-linked +Q03655 YMR215W GAS3 422 N-linked +P39726 YAL044C GCV3 102 N6-lipoyllysine +Q08271 YOL132W GAS4 447 GPI-anchor +Q08271 YOL132W GAS4 151 N-linked +Q08271 YOL132W GAS4 398 N-linked +Q08193 YOL030W GAS5 462 GPI-anchor +Q08193 YOL030W GAS5 24 N-linked +Q08193 YOL030W GAS5 60 N-linked +Q08193 YOL030W GAS5 166 N-linked +Q08193 YOL030W GAS5 299 N-linked +Q08193 YOL030W GAS5 344 N-linked +Q08193 YOL030W GAS5 359 N-linked +P38011 YMR116C ASC1 2 N-acetylalanine +P38011 YMR116C ASC1 96 Phosphothreonine +P38011 YMR116C ASC1 168 Phosphothreonine +P38011 YMR116C ASC1 46 Glycyl +P38011 YMR116C ASC1 53 Glycyl +P38011 YMR116C ASC1 107 Glycyl +P38011 YMR116C ASC1 137 Glycyl +P38011 YMR116C ASC1 161 Glycyl +P07261 YPL075W GCR1 447 Phosphothreonine +P07261 YPL075W GCR1 449 Phosphoserine +P07261 YPL075W GCR1 482 Phosphoserine +P07261 YPL075W GCR1 489 Phosphoserine +P07261 YPL075W GCR1 538 Phosphoserine +P14065 YOR120W GCY1 306 Phosphoserine +P32775 YEL011W GLC3 190 Phosphoserine +P17695 YDR513W GRX2 37 Phosphoserine +P17695 YDR513W GRX2 61 S-glutathionyl +P17695 YDR513W GRX2 91 Phosphoserine +P37303 YEL046C GLY1 213 N6-(pyridoxal +P37303 YEL046C GLY1 367 Phosphoserine +P37303 YEL046C GLY1 369 Phosphoserine +P37303 YEL046C GLY1 370 Phosphothreonine +P37303 YEL046C GLY1 228 Glycyl +P38875 YHR188C GPI16 184 N-linked +P40106 YER062C GPP2 90 Phosphoserine +P40106 YER062C GPP2 64 Glycyl +P40106 YER062C GPP2 144 Glycyl +P35197 YDL226C GCS1 151 Phosphothreonine +P35197 YDL226C GCS1 157 Phosphoserine +P35197 YDL226C GCS1 161 Phosphothreonine +P35197 YDL226C GCS1 168 Phosphoserine +P35197 YDL226C GCS1 170 Phosphothreonine +P35197 YDL226C GCS1 260 Phosphoserine +Q03016 YPL137C GIP3 68 Phosphoserine +Q03016 YPL137C GIP3 99 Phosphothreonine +Q03016 YPL137C GIP3 103 Phosphoserine +Q03016 YPL137C GIP3 143 Phosphoserine +Q03016 YPL137C GIP3 260 Phosphoserine +Q03016 YPL137C GIP3 264 Phosphothreonine +Q03016 YPL137C GIP3 269 Phosphoserine +P03069 YEL009C GCN4 17 Phosphoserine +P03069 YEL009C GCN4 165 Phosphothreonine%3B +P03069 YEL009C GCN4 218 Phosphoserine +Q01722 YNL199C GCR2 151 Phosphoserine +Q01722 YNL199C GCR2 406 Phosphoserine +Q01722 YNL199C GCR2 409 Phosphoserine +P32621 YEL042W GDA1 41 N-linked +P32621 YEL042W GDA1 280 N-linked +P32621 YEL042W GDA1 335 N-linked +Q02979 YPL110C GDE1 653 Phosphoserine +Q02979 YPL110C GDE1 983 Phosphoserine +P37291 YLR058C SHM2 20 Phosphothreonine +P37291 YLR058C SHM2 26 Phosphoserine +P37291 YLR058C SHM2 248 N6-(pyridoxal +P37291 YLR058C SHM2 429 Phosphoserine +P37291 YLR058C SHM2 456 Glycyl +P40107 YGL225W VRG4 119 N-linked +P40107 YGL225W VRG4 242 N-linked +P40107 YGL225W VRG4 246 N-linked +P40107 YGL225W VRG4 249 N-linked +P0CE11 YER039C HVG1 149 N-linked +P0CE11 YER039C HVG1 153 N-linked +P43577 YFL017C GNA1 2 N-acetylserine +P10823 YER020W GPA2 2 N-myristoyl +P10823 YER020W GPA2 4 S-palmitoyl +Q08886 YOR371C GPB1 91 Phosphoserine +Q08886 YOR371C GPB1 161 Phosphothreonine +Q05584 YDR272W GLO2 257 Phosphoserine +P38682 YER122C GLO3 170 Phosphoserine +P38682 YER122C GLO3 306 Phosphoserine +P38682 YER122C GLO3 389 Phosphoserine +P38682 YER122C GLO3 398 Phosphoserine +P48813 YDR508C GNP1 29 Phosphoserine +P48813 YDR508C GNP1 113 Phosphoserine +P48813 YDR508C GNP1 124 Phosphoserine +P48813 YDR508C GNP1 127 Phosphothreonine +P48813 YDR508C GNP1 34 Glycyl +P48813 YDR508C GNP1 39 Glycyl +P48813 YDR508C GNP1 41 Glycyl +P48813 YDR508C GNP1 61 Glycyl +P48813 YDR508C GNP1 132 Glycyl +P53839 YNL274C GOR1 31 Phosphothreonine +Q00055 YDL022W GPD1 2 N-acetylserine +Q00055 YDL022W GPD1 24 Phosphoserine +Q00055 YDL022W GPD1 27 Phosphoserine +Q06636 YDR302W GPI11 16 Phosphoserine +P49095 YMR189W GCV2 773 N6-(pyridoxal +Q06336 YDR358W GGA1 348 Phosphothreonine +Q06336 YDR358W GGA1 353 Phosphoserine +Q06336 YDR358W GGA1 357 Phosphoserine +Q06336 YDR358W GGA1 378 Phosphoserine +Q06336 YDR358W GGA1 394 Phosphoserine +P38817 YHR108W GGA2 180 Glycyl +P38817 YHR108W GGA2 287 Glycyl +P38138 YBR229C ROT2 114 N-linked +P38138 YBR229C ROT2 126 N-linked +P38138 YBR229C ROT2 142 N-linked +P38138 YBR229C ROT2 173 N-linked +P38138 YBR229C ROT2 345 N-linked +P38138 YBR229C ROT2 783 N-linked +P38138 YBR229C ROT2 791 N-linked +P38138 YBR229C ROT2 867 N-linked +P38138 YBR229C ROT2 880 N-linked +P38138 YBR229C ROT2 907 N-linked +P38138 YBR229C ROT2 941 N-linked +Q04924 YDR221W GTB1 145 N-linked +Q04924 YDR221W GTB1 240 N-linked +Q04924 YDR221W GTB1 358 N-linked +Q04924 YDR221W GTB1 520 N-linked +Q04924 YDR221W GTB1 525 N-linked +Q04924 YDR221W GTB1 688 N-linked +Q04924 YDR221W GTB1 699 N-linked +Q12434 YDL135C RDI1 2 N-acetylalanine +Q12434 YDL135C RDI1 27 Phosphothreonine +Q12434 YDL135C RDI1 40 Phosphoserine +P41818 YMR311C GLC8 12 Phosphoserine +P41818 YMR311C GLC8 118 Phosphothreonine%3B +P41818 YMR311C GLC8 158 Phosphoserine +P41818 YMR311C GLC8 184 Phosphoserine +P47011 YJL137C GLG2 230 O-linked +P47011 YJL137C GLG2 232 O-linked +P47011 YJL137C GLG2 367 O-linked +P38263 YBR105C VID24 27 Phosphoserine +P38263 YBR105C VID24 20 Glycyl +Q12263 YDR507C GIN4 406 Phosphoserine +Q12263 YDR507C GIN4 465 Phosphoserine +Q12263 YDR507C GIN4 471 Phosphoserine +Q12263 YDR507C GIN4 617 Phosphoserine +Q12263 YDR507C GIN4 689 Phosphoserine +Q12263 YDR507C GIN4 719 Phosphoserine +Q12263 YDR507C GIN4 805 Phosphoserine +Q12263 YDR507C GIN4 807 Phosphoserine +Q12263 YDR507C GIN4 883 Phosphoserine +Q12263 YDR507C GIN4 884 Phosphothreonine +Q12263 YDR507C GIN4 930 Phosphoserine +P32288 YPR035W GLN1 2 N-acetylalanine +P32288 YPR035W GLN1 5 Phosphoserine +P32288 YPR035W GLN1 283 Glycyl +P32288 YPR035W GLN1 324 Glycyl +P32288 YPR035W GLN1 363 Glycyl +P25373 YCL035C GRX1 27 S-glutathionyl +P25373 YCL035C GRX1 11 Glycyl +Q12680 YDL171C GLT1 2070 Phosphothreonine +P37292 YBR263W SHM1 265 N6-(pyridoxal +Q07830 YLL031C GPI13 66 N-linked +Q07830 YLL031C GPI13 71 N-linked +Q07830 YLL031C GPI13 100 N-linked +Q07830 YLL031C GPI13 182 N-linked +Q07830 YLL031C GPI13 203 N-linked +Q07830 YLL031C GPI13 411 N-linked +Q07830 YLL031C GPI13 681 N-linked +Q07830 YLL031C GPI13 682 N-linked +Q07830 YLL031C GPI13 707 N-linked +Q07830 YLL031C GPI13 742 N-linked +P41277 YIL053W GPP1 90 Phosphoserine +P41277 YIL053W GPP1 64 Glycyl +P41277 YIL053W GPP1 64 Glycyl +P41277 YIL053W GPP1 144 Glycyl +P18494 YER040W GLN3 251 Phosphoserine +P18494 YER040W GLN3 267 Phosphoserine +P18494 YER040W GLN3 285 Phosphoserine +P18494 YER040W GLN3 469 Phosphoserine +P18494 YER040W GLN3 552 Phosphoserine +P18494 YER040W GLN3 562 Phosphoserine +P36148 YKR067W GPT2 632 Phosphoserine +P36148 YKR067W GPT2 637 Phosphoserine +P36148 YKR067W GPT2 647 Phosphoserine +P36148 YKR067W GPT2 651 Phosphoserine +P36148 YKR067W GPT2 654 Phosphoserine +P36148 YKR067W GPT2 657 Phosphoserine +P36148 YKR067W GPT2 664 Phosphoserine +P36148 YKR067W GPT2 668 Phosphoserine +P36148 YKR067W GPT2 671 Phosphoserine +P36148 YKR067W GPT2 673 Phosphothreonine +P36148 YKR067W GPT2 688 Phosphoserine +P36148 YKR067W GPT2 692 Phosphothreonine +P36148 YKR067W GPT2 693 Phosphoserine +Q04410 YDR517W GRH1 1 N-acetylmethionine +Q04410 YDR517W GRH1 155 Phosphoserine +Q04322 YMR192W GYL1 1 N-acetylmethionine +Q04322 YMR192W GYL1 17 Phosphothreonine +Q04322 YMR192W GYL1 37 Phosphoserine +Q04322 YMR192W GYL1 73 Phosphoserine +Q04322 YMR192W GYL1 139 Phosphoserine +Q04322 YMR192W GYL1 498 Glycyl +P48365 YDL234C GYP7 265 Phosphoserine +P48365 YDL234C GYP7 339 Phosphoserine +P23337 YFR015C GSY1 159 Phosphoserine +P23337 YFR015C GSY1 363 Phosphoserine +P23337 YFR015C GSY1 560 Phosphoserine +P23337 YFR015C GSY1 651 Phosphoserine +P23337 YFR015C GSY1 655 Phosphoserine +P23337 YFR015C GSY1 660 Phosphoserine%3B +P23337 YFR015C GSY1 662 Phosphoserine%3B +P23337 YFR015C GSY1 667 Phosphothreonine +P04911 YDR225W HTA1 2 N-acetylserine +P04911 YDR225W HTA1 5 N6-acetyllysine +P04911 YDR225W HTA1 8 N6-acetyllysine +P04911 YDR225W HTA1 106 N5-methylglutamine +P04911 YDR225W HTA1 129 Phosphoserine +P04911 YDR225W HTA1 127 Glycyl +P02294 YBL002W HTB2 7 N6-acetyllysine%3B +P02294 YBL002W HTB2 8 N6-acetyllysine%3B +P02294 YBL002W HTB2 11 Phosphoserine +P02294 YBL002W HTB2 12 N6-acetyllysine +P02294 YBL002W HTB2 17 N6-acetyllysine%3B +P02294 YBL002W HTB2 7 Glycyl +P02294 YBL002W HTB2 8 Glycyl +P02294 YBL002W HTB2 17 Glycyl +P02294 YBL002W HTB2 18 Glycyl +P02294 YBL002W HTB2 124 Glycyl +P38736 YHL031C GOS1 2 N-acetylserine +P38736 YHL031C GOS1 164 Phosphoserine +P39717 YAL056W GPB2 24 Phosphoserine +P40531 YIL041W GVP36 2 N-acetylserine +P40531 YIL041W GVP36 2 Phosphoserine +P40531 YIL041W GVP36 319 Phosphoserine +P40531 YIL041W GVP36 13 Glycyl +P40531 YIL041W GVP36 305 Glycyl +P40531 YIL041W GVP36 313 Glycyl +Q08484 YOR070C GYP1 69 Phosphoserine +Q08484 YOR070C GYP1 250 Phosphoserine +P48566 YNL293W MSB3 147 Phosphoserine +P48566 YNL293W MSB3 484 Phosphoserine +Q12753 YPR008W HAA1 125 Phosphoserine +Q12753 YPR008W HAA1 231 Phosphoserine +Q12753 YPR008W HAA1 241 Phosphoserine +Q12753 YPR008W HAA1 291 Phosphoserine +P32835 YLR293C GSP1 2 N-acetylserine +P32835 YLR293C GSP1 2 Phosphoserine +P53551 YPL127C HHO1 174 Phosphoserine +Q12341 YPL001W HAT1 354 Phosphoserine +P41921 YPL091W GLR1 1 N-acetylmethionine +P32836 YOR185C GSP2 2 N-acetylserine +P32836 YOR185C GSP2 2 Phosphoserine +P39996 YEL017W GTT3 66 Phosphoserine +P39996 YEL017W GTT3 72 Phosphoserine +P39996 YEL017W GTT3 99 Phosphoserine +P39996 YEL017W GTT3 116 Phosphoserine +P38970 YJL165C HAL5 17 Phosphoserine +P38970 YJL165C HAL5 19 Phosphoserine +P38970 YJL165C HAL5 68 Phosphoserine +P38970 YJL165C HAL5 72 Phosphoserine +P38970 YJL165C HAL5 160 Phosphoserine +P38970 YJL165C HAL5 273 Phosphoserine +P38970 YJL165C HAL5 277 Phosphoserine +P38970 YJL165C HAL5 324 Phosphoserine +P38970 YJL165C HAL5 333 Phosphoserine +P38970 YJL165C HAL5 336 Phosphoserine +P38970 YJL165C HAL5 358 Phosphoserine +P38970 YJL165C HAL5 391 Phosphoserine +P38970 YJL165C HAL5 395 Phosphoserine +P38199 YBL032W HEK2 358 Phosphoserine +P38199 YBL032W HEK2 360 Phosphoserine +P38199 YBL032W HEK2 362 Phosphoserine +Q12361 YDL035C GPR1 373 Phosphoserine +Q12361 YDL035C GPR1 903 Phosphoserine +P24814 YJR090C GRR1 199 Phosphoserine +P24814 YJR090C GRR1 300 Phosphoserine +Q04697 YML048W GSF2 89 N-linked +Q04697 YML048W GSF2 173 N-linked +P32806 YJL044C GYP6 436 Phosphoserine +Q96VH4 YCL026C-B HBN1 2 N-acetylserine +Q12096 YOR320C GNT1 136 N-linked +Q12096 YOR320C GNT1 177 N-linked +Q12096 YOR320C GNT1 187 N-linked +Q12096 YOR320C GNT1 425 N-linked +Q04080 YDR434W GPI17 100 N-linked +Q04080 YDR434W GPI17 170 N-linked +Q04080 YDR434W GPI17 228 N-linked +Q04080 YDR434W GPI17 247 N-linked +Q04080 YDR434W GPI17 299 N-linked +P38211 YBR004C GPI18 69 N-linked +P38211 YBR004C GPI18 101 N-linked +P40367 YJL062W LAS21 145 N-linked +P40367 YJL062W LAS21 185 N-linked +P40367 YJL062W LAS21 298 N-linked +P40367 YJL062W LAS21 506 N-linked +P47122 YJR072C NPA3 304 Phosphoserine +P47122 YJR072C NPA3 308 Phosphoserine +P47122 YJR072C NPA3 313 Phosphoserine +P47122 YJR072C NPA3 352 Phosphoserine +P47122 YJR072C NPA3 369 Glycyl +Q12068 YOL151W GRE2 333 Phosphoserine +P40956 YGL181W GTS1 153 Phosphoserine +P40956 YGL181W GTS1 181 Phosphotyrosine +P40956 YGL181W GTS1 184 Phosphoserine +P40956 YGL181W GTS1 187 Phosphoserine +P40956 YGL181W GTS1 240 Phosphoserine +P40956 YGL181W GTS1 249 Phosphothreonine +P38625 YMR217W GUA1 241 Glycyl +P38625 YMR217W GUA1 426 Glycyl +Q12180 YOL089C HAL9 221 Phosphoserine +Q12180 YOL089C HAL9 937 Phosphoserine +Q05580 YDR266C HEL2 2 N-acetylserine +Q05580 YDR266C HEL2 57 Phosphothreonine +Q05580 YDR266C HEL2 354 Phosphoserine +P53258 YGR100W MDR1 2 N-acetylserine +P53258 YGR100W MDR1 764 Phosphoserine +P53258 YGR100W MDR1 871 Phosphoserine +Q12344 YPL249C GYP5 25 Phosphoserine +Q12344 YPL249C GYP5 30 Phosphoserine +Q12344 YPL249C GYP5 89 Phosphothreonine +Q12344 YPL249C GYP5 389 Phosphoserine +P27472 YLR258W GSY2 159 Phosphoserine +P27472 YLR258W GSY2 363 Phosphoserine +P27472 YLR258W GSY2 467 Phosphoserine +P27472 YLR258W GSY2 651 Phosphoserine +P27472 YLR258W GSY2 655 Phosphoserine%3B +P27472 YLR258W GSY2 661 Phosphoserine%3B +P27472 YLR258W GSY2 663 Phosphoserine%3B +P27472 YLR258W GSY2 668 Phosphothreonine%3B +P36125 YKR030W GMH1 2 N-acetylserine +P41911 YOL059W GPD2 70 Phosphoserine +P41911 YOL059W GPD2 72 Phosphoserine +P41911 YOL059W GPD2 75 Phosphoserine +P49018 YDR331W GPI8 256 N-linked +P49018 YDR331W GPI8 346 N-linked +Q12214 YPR068C HOS1 110 Phosphoserine +Q01448 YBR215W HPC2 47 Phosphoserine +Q01448 YBR215W HPC2 49 Phosphoserine +Q01448 YBR215W HPC2 435 Phosphoserine +Q05905 YLR301W HRI1 143 Phosphoserine +P09950 YDR232W HEM1 337 N6-(pyridoxal +P28789 YDL205C HEM3 251 S-(dipyrrolylmethanemethyl)cysteine +Q12276 YOR227W HER1 102 Phosphoserine +Q12276 YOR227W HER1 128 Phosphothreonine +Q12276 YOR227W HER1 277 Phosphoserine +Q12276 YOR227W HER1 1013 Phosphoserine +Q12276 YOR227W HER1 1130 Phosphothreonine +Q12276 YOR227W HER1 1200 Phosphoserine +Q12276 YOR227W HER1 1204 Phosphoserine +Q12276 YOR227W HER1 1207 Phosphoserine +P41809 YDR420W HKR1 24 N-linked +P41809 YDR420W HKR1 1252 N-linked +P41809 YDR420W HKR1 1293 N-linked +P41809 YDR420W HKR1 1342 N-linked +P41809 YDR420W HKR1 1400 N-linked +P54839 YML126C ERG13 276 Phosphoserine +P40480 YIL112W HOS4 14 Phosphoserine +P40480 YIL112W HOS4 16 Phosphoserine +P40480 YIL112W HOS4 37 Phosphothreonine +P40480 YIL112W HOS4 67 Phosphoserine +P40480 YIL112W HOS4 290 Phosphoserine +P40480 YIL112W HOS4 507 Phosphoserine +P40480 YIL112W HOS4 698 Phosphoserine +P40480 YIL112W HOS4 700 Phosphothreonine +P40480 YIL112W HOS4 778 Phosphoserine +P48570 YDL182W LYS20 385 Phosphoserine +P48570 YDL182W LYS20 396 Phosphothreonine +P48570 YDL182W LYS20 401 Phosphoserine +P48570 YDL182W LYS20 410 Phosphoserine +Q99332 YOR324C FRT1 167 Phosphoserine +Q99332 YOR324C FRT1 342 Phosphoserine +P17629 YDR138W HPR1 234 Phosphoserine +P47171 YJR140C HIR3 302 Phosphothreonine +P47171 YJR140C HIR3 304 Phosphoserine +P48353 YMR161W HLJ1 109 Phosphoserine +P12683 YML075C HMG1 552 Phosphothreonine +P12683 YML075C HMG1 115 N-linked +P12683 YML075C HMG1 181 N-linked +P12683 YML075C HMG1 452 N-linked +P12683 YML075C HMG1 490 N-linked +P02293 YDR224C HTB1 7 N6-acetyllysine%3B +P02293 YDR224C HTB1 8 N6-acetyllysine%3B +P02293 YDR224C HTB1 11 Phosphoserine +P02293 YDR224C HTB1 12 N6-acetyllysine +P02293 YDR224C HTB1 17 N6-acetyllysine%3B +P02293 YDR224C HTB1 7 Glycyl +P02293 YDR224C HTB1 8 Glycyl +P02293 YDR224C HTB1 17 Glycyl +P02293 YDR224C HTB1 18 Glycyl +P02293 YDR224C HTB1 124 Glycyl +P32769 YKR084C HBS1 124 Phosphoserine +Q07653 YDL223C HBT1 41 Phosphoserine +Q07653 YDL223C HBT1 303 Phosphoserine +Q07653 YDL223C HBT1 363 Phosphoserine +Q07653 YDL223C HBT1 491 Phosphoserine +Q07653 YDL223C HBT1 561 Phosphoserine +Q07653 YDL223C HBT1 671 Phosphoserine +Q07653 YDL223C HBT1 855 Phosphotyrosine +Q07653 YDL223C HBT1 857 Phosphoserine +Q07653 YDL223C HBT1 1005 Phosphoserine +Q07653 YDL223C HBT1 1034 Phosphoserine +P25364 YCR065W HCM1 342 Phosphothreonine +P25364 YCR065W HCM1 496 Phosphoserine +Q12373 YLL022C HIF1 174 Phosphoserine +Q03281 YDR458C HEH2 123 Phosphoserine +P05373 YGL040C HEM2 254 Phosphoserine +P04912 YBL003C HTA2 2 N-acetylserine +P04912 YBL003C HTA2 5 N6-acetyllysine +P04912 YBL003C HTA2 8 N6-acetyllysine +P04912 YBL003C HTA2 106 N5-methylglutamine +P04912 YBL003C HTA2 129 Phosphoserine +P04912 YBL003C HTA2 127 Glycyl +Q12692 YOL012C HTZ1 2 N-acetylserine +Q12692 YOL012C HTZ1 4 N6-acetyllysine +Q12692 YOL012C HTZ1 9 N6-acetyllysine +Q12692 YOL012C HTZ1 11 N6-acetyllysine +Q12692 YOL012C HTZ1 15 N6-acetyllysine +P61830 YBR010W; YNL031C 5 N6%2CN6%2CN6-trimethyllysine%3B +P61830 YBR010W; YNL031C 5 N6%2CN6-dimethyllysine%3B +P61830 YBR010W; YNL031C 5 N6-methyllysine%3B +P61830 YBR010W; YNL031C 10 N6-acetyllysine%3B +P61830 YBR010W; YNL031C 10 N6-methyllysine%3B +P61830 YBR010W; YNL031C 11 Phosphoserine +P61830 YBR010W; YNL031C 15 N6%2CN6-dimethyllysine%3B +P61830 YBR010W; YNL031C 15 N6-acetyllysine%3B +P61830 YBR010W; YNL031C 19 N6-acetyllysine%3B +P61830 YBR010W; YNL031C 19 N6-methyllysine%3B +P61830 YBR010W; YNL031C 24 N6-acetyllysine%3B +P61830 YBR010W; YNL031C 24 N6-methyllysine%3B +P61830 YBR010W; YNL031C 28 N6%2CN6%2CN6-trimethyllysine%3B +P61830 YBR010W; YNL031C 28 N6%2CN6-dimethyllysine%3B +P61830 YBR010W; YNL031C 28 N6-acetyllysine%3B +P61830 YBR010W; YNL031C 28 N6-methyllysine%3B +P61830 YBR010W; YNL031C 37 N6%2CN6%2CN6-trimethyllysine%3B +P61830 YBR010W; YNL031C 37 N6%2CN6-dimethyllysine%3B +P61830 YBR010W; YNL031C 37 N6-acetyllysine%3B +P61830 YBR010W; YNL031C 37 N6-methyllysine%3B +P61830 YBR010W; YNL031C 57 N6-acetyllysine +P61830 YBR010W; YNL031C 65 N6-acetyllysine +P61830 YBR010W; YNL031C 80 N6%2CN6%2CN6-trimethyllysine%3B +P61830 YBR010W; YNL031C 80 N6%2CN6-dimethyllysine%3B +P61830 YBR010W; YNL031C 80 N6-methyllysine%3B +P02309 YBR009C; YNL030W 6 N6-acetyllysine +P02309 YBR009C; YNL030W 13 N6-acetyllysine +P02309 YBR009C; YNL030W 17 N6-acetyllysine +P02309 YBR009C; YNL030W 61 Phosphoserine +P02309 YBR009C; YNL030W 65 Phosphoserine +P02309 YBR009C; YNL030W 80 N6-acetyllysine +Q01766 YPR005C HAL1 266 Phosphoserine +P06774 YGL237C HAP2 2 N-acetylserine +P06774 YGL237C HAP2 52 Phosphoserine +P06774 YGL237C HAP2 265 Phosphothreonine +Q02516 YOR358W HAP5 7 Phosphoserine +Q03532 YMR290C HAS1 12 Phosphoserine +Q04458 YMR110C HFD1 111 Phosphoserine +P32480 YOR038C HIR2 713 Phosphoserine +P00498 YER055C HIS1 1 N-acetylmethionine +Q05787 YLR207W HRD3 101 N-linked +Q05787 YLR207W HRD3 123 N-linked +Q05787 YLR207W HRD3 142 N-linked +Q05787 YLR207W HRD3 429 N-linked +Q05787 YLR207W HRD3 611 N-linked +Q99383 YOL123W HRP1 2 Phosphoserine +Q99383 YOL123W HRP1 3 Phosphoserine +Q99383 YOL123W HRP1 206 Phosphoserine +Q99383 YOL123W HRP1 458 Phosphothreonine +Q99383 YOL123W HRP1 462 Phosphoserine +P29295 YPL204W HRR25 143 Phosphoserine +P32479 YBL008W HIR1 610 Phosphoserine +P07172 YIL116W HIS5 230 N6-(pyridoxal +P40037 YER057C HMF1 52 Glycyl +P19807 YGL077C HNM1 22 Phosphoserine +P19807 YGL077C HNM1 42 Phosphoserine +P19807 YGL077C HNM1 7 N-linked +P19807 YGL077C HNM1 20 N-linked +P19807 YGL077C HNM1 248 N-linked +P19807 YGL077C HNM1 341 N-linked +P47124 YJR075W HOC1 37 N-linked +Q9URQ5 YCR020W-B HTL1 2 N-acetylserine +P32874 YMR207C HFA1 804 N6-biotinyllysine +Q02959 YPL116W HOS3 582 Phosphoserine +Q02959 YPL116W HOS3 583 Phosphoserine +Q02959 YPL116W HOS3 613 Phosphoserine +Q02959 YPL116W HOS3 629 Phosphoserine +P34244 YKL101W HSL1 511 Phosphoserine +P34244 YKL101W HSL1 629 Phosphoserine +P34244 YKL101W HSL1 685 Phosphoserine +P34244 YKL101W HSL1 837 Phosphoserine +P34244 YKL101W HSL1 866 Phosphoserine +P34244 YKL101W HSL1 1220 Phosphoserine +P34244 YKL101W HSL1 1250 Phosphoserine +P34244 YKL101W HSL1 1284 Phosphoserine +P34244 YKL101W HSL1 1287 Phosphoserine +P34244 YKL101W HSL1 1325 Phosphoserine +P48362 YGR187C HGH1 2 N-acetylthreonine +P06775 YGR191W HIP1 76 Phosphothreonine +P12684 YLR450W HMG2 565 Phosphothreonine +P12684 YLR450W HMG2 115 N-linked +P12684 YLR450W HMG2 150 N-linked +P12684 YLR450W HMG2 158 N-linked +P12684 YLR450W HMG2 179 N-linked +P12684 YLR450W HMG2 428 N-linked +P12684 YLR450W HMG2 455 N-linked +Q05164 YOL155C HPF1 946 GPI-anchor +Q05164 YOL155C HPF1 28 N-linked +Q05164 YOL155C HPF1 35 N-linked +Q05164 YOL155C HPF1 493 N-linked +Q05164 YOL155C HPF1 601 N-linked +Q05164 YOL155C HPF1 638 N-linked +P38753 YHL002W HSE1 2 N-acetylserine +P38753 YHL002W HSE1 162 Phosphoserine +P10961 YGL073W HSF1 1 N-acetylmethionine +P10961 YGL073W HSF1 97 Phosphothreonine +P10961 YGL073W HSF1 450 Phosphoserine +P10961 YGL073W HSF1 458 Phosphoserine +P10961 YGL073W HSF1 471 Phosphoserine +P10961 YGL073W HSF1 478 Phosphoserine +P10961 YGL073W HSF1 528 Phosphoserine +P22943 YFL014W HSP12 21 Phosphoserine%3B +P22943 YFL014W HSP12 24 Phosphoserine +P22943 YFL014W HSP12 59 Phosphoserine +P22943 YFL014W HSP12 73 Phosphoserine +P22943 YFL014W HSP12 97 Phosphoserine +P32485 YLR113W HOG1 2 N-acetylthreonine +P32485 YLR113W HOG1 174 Phosphothreonine +P32485 YLR113W HOG1 176 Phosphotyrosine +Q12122 YDL131W LYS21 399 Phosphoserine +Q12122 YDL131W LYS21 410 Phosphothreonine +Q03213 YMR172W HOT1 146 Phosphoserine +Q03213 YMR172W HOT1 153 Phosphoserine +P15992 YBR072W HSP26 2 N-acetylserine +P15992 YBR072W HSP26 42 Phosphothreonine +P15992 YBR072W HSP26 90 Phosphoserine +P15992 YBR072W HSP26 163 Phosphothreonine +P15992 YBR072W HSP26 208 Phosphoserine +P15992 YBR072W HSP26 211 Phosphoserine +P25619 YCR021C HSP30 308 Phosphoserine +P25619 YCR021C HSP30 331 Phosphothreonine +P40325 YGR268C HUA1 2 N-acetylserine +P40325 YGR268C HUA1 3 Glycyl +P40325 YGR268C HUA1 18 Glycyl +Q12345 YLR052W IES3 157 Phosphoserine +Q12345 YLR052W IES3 211 Phosphoserine +P39730 YAL035W FUN12 405 Phosphoserine +Q04432 YDR533C HSP31 138 Cysteine +Q12329 YDR171W HSP42 182 Phosphoserine +Q12329 YDR171W HSP42 213 Phosphoserine +Q12329 YDR171W HSP42 214 Phosphoserine +Q12329 YDR171W HSP42 215 Phosphoserine +Q12329 YDR171W HSP42 223 Phosphoserine +P53119 YGL141W HUL5 1 N-acetylmethionine +P32465 YHR094C HXT1 23 Phosphoserine +P32465 YHR094C HXT1 38 Phosphoserine +P32465 YHR094C HXT1 44 Phosphoserine +P32465 YHR094C HXT1 228 N-linked +P32466 YDR345C HXT3 23 Phosphoserine +P32466 YDR345C HXT3 225 N-linked +P32466 YDR345C HXT3 416 N-linked +P38695 YHR096C HXT5 126 N-linked +P38695 YHR096C HXT5 249 N-linked +P38695 YHR096C HXT5 61 Glycyl +P39004 YDR342C HXT7 556 Phosphothreonine +P39004 YDR342C HXT7 91 N-linked +P39004 YDR342C HXT7 228 N-linked +P39004 YDR342C HXT7 560 Glycyl +P46958 YJL146W IDS2 1 N-acetylmethionine +P46958 YJL146W IDS2 13 Phosphothreonine +P46958 YJL146W IDS2 23 Phosphoserine +P46958 YJL146W IDS2 27 Phosphoserine +P46958 YJL146W IDS2 39 Phosphoserine +P46958 YJL146W IDS2 122 Phosphoserine +P46958 YJL146W IDS2 130 Phosphoserine +P46958 YJL146W IDS2 136 Phosphoserine +P46958 YJL146W IDS2 147 Phosphoserine +P46958 YJL146W IDS2 148 Phosphoserine +P40060 YER092W IES5 124 Phosphothreonine +P20459 YJR007W SUI2 52 Phosphoserine%3B +P20459 YJR007W SUI2 292 Phosphoserine +P20459 YJR007W SUI2 294 Phosphoserine +P28817 YDR036C EHD3 326 Phosphothreonine +P0CY09 YCL067C HMLALPHA2 1 N-acetylmethionine +Q04178 YDR399W HPT1 2 N-acetylserine +P38922 YNL004W HRB1 343 Phosphoserine +P38922 YNL004W HRB1 355 Phosphoserine +Q08732 YOR267C HRK1 37 Phosphoserine +Q08732 YOR267C HRK1 382 Phosphoserine +Q08732 YOR267C HRK1 472 Phosphoserine +Q08732 YOR267C HRK1 495 Phosphothreonine +Q08732 YOR267C HRK1 498 Phosphoserine +P50079 YGR223C HSV2 61 N-linked +P50079 YGR223C HSV2 155 N-linked +P50079 YGR223C HSV2 256 N-linked +P50079 YGR223C HSV2 280 N-linked +P50079 YGR223C HSV2 315 N-linked +P50079 YGR223C HSV2 421 N-linked +P04806 YFR053C HXK1 245 Phosphoserine +P04806 YFR053C HXK1 272 Phosphoserine +P04807 YGL253W HXK2 15 Phosphoserine +P04807 YGL253W HXK2 38 Phosphothreonine +P04807 YGL253W HXK2 158 Phosphoserine +P04807 YGL253W HXK2 245 Phosphoserine +P04807 YGL253W HXK2 272 Phosphoserine +Q12520 YPL244C HUT1 165 N-linked +P15496 YPL117C IDI1 7 Phosphoserine +P09064 YPL237W SUI3 40 Phosphoserine +P09064 YPL237W SUI3 69 Phosphothreonine +P09064 YPL237W SUI3 80 Phosphoserine +P09064 YPL237W SUI3 92 Phosphoserine +P09064 YPL237W SUI3 112 Phosphoserine +P09064 YPL237W SUI3 116 Phosphothreonine +P09064 YPL237W SUI3 118 Phosphoserine +P10081 YKR059W; YJL138C 2 N-acetylserine +P10081 YKR059W; YJL138C 73 Phosphothreonine +P10081 YKR059W; YJL138C 77 Phosphoserine +P10081 YKR059W; YJL138C 129 Phosphoserine +P10081 YKR059W; YJL138C 146 Phosphothreonine +P39936 YGL049C TIF4632 74 Phosphoserine +P39936 YGL049C TIF4632 196 Phosphothreonine +P39936 YGL049C TIF4632 301 Phosphothreonine +P39936 YGL049C TIF4632 503 Phosphoserine +P39936 YGL049C TIF4632 913 Phosphoserine +P39979 YEL066W HPA3 2 N-acetylserine +P19882 YLR259C HSP60 102 Phosphothreonine +P19882 YLR259C HSP60 485 Phosphoserine +P22202 YER103W SSA4 552 Phosphoserine +P53686 YPL015C HST2 2 N-acetylserine +P53686 YPL015C HST2 340 Phosphoserine +P54862 YOL156W HXT11 87 N-linked +P54862 YOL156W HXT11 227 N-linked +P40886 YJL214W HXT8 92 N-linked +P40886 YJL214W HXT8 102 N-linked +P40886 YJL214W HXT8 429 N-linked +P53892 YNL164C IBD2 100 Phosphoserine +P53892 YNL164C IBD2 106 Phosphoserine +P53892 YNL164C IBD2 211 Phosphothreonine +P38284 YBR157C ICS2 217 Phosphoserine +P38274 YBR133C HSL7 317 Phosphoserine +P38274 YBR133C HSL7 614 Phosphothreonine +P0CS90 YJR045C SSC1 330 Phosphothreonine +P19211 YJR047C ANB1 2 Phosphoserine +P19211 YJR047C ANB1 7 Phosphothreonine +P19211 YJR047C ANB1 51 Hypusine +Q12522 YPR016C TIF6 174 Phosphoserine%3B +Q12522 YPR016C TIF6 175 Phosphoserine%3B +Q12522 YPR016C TIF6 231 Phosphoserine +P06168 YLR355C ILV5 355 Phosphoserine +Q03824 YMR163C INP2 275 N-linked +Q03824 YMR163C INP2 343 N-linked +Q03824 YMR163C INP2 344 N-linked +Q03824 YMR163C INP2 379 N-linked +Q03824 YMR163C INP2 517 N-linked +Q03824 YMR163C INP2 569 N-linked +Q03824 YMR163C INP2 574 N-linked +Q12271 YOR109W INP53 497 Phosphoserine +Q12271 YOR109W INP53 986 Phosphoserine +Q12271 YOR109W INP53 1035 Phosphoserine +Q12271 YOR109W INP53 1105 Phosphothreonine +P00724 YIL162W SUC2 23 N-linked +P00724 YIL162W SUC2 64 N-linked +P00724 YIL162W SUC2 97 N-linked +P00724 YIL162W SUC2 111 N-linked +P00724 YIL162W SUC2 118 N-linked +P00724 YIL162W SUC2 165 N-linked +P00724 YIL162W SUC2 266 N-linked +P00724 YIL162W SUC2 275 N-linked +P00724 YIL162W SUC2 356 N-linked +P00724 YIL162W SUC2 369 N-linked +P00724 YIL162W SUC2 384 N-linked +P00724 YIL162W SUC2 398 N-linked +P00724 YIL162W SUC2 512 N-linked +P32589 YPL106C SSE1 2 N-acetylserine +P32589 YPL106C SSE1 242 Phosphothreonine +P32589 YPL106C SSE1 660 Phosphoserine +P32589 YPL106C SSE1 195 Glycyl +P17709 YCL040W GLK1 2 N-acetylserine +P17709 YCL040W GLK1 2 Phosphoserine +P17709 YCL040W GLK1 470 Phosphoserine +P43581 YFL011W HXT10 75 N-linked +P40441 YIL170W HXT12 194 N-linked +P23585 YMR011W HXT2 2 N-acetylserine +P23585 YMR011W HXT2 11 Phosphoserine +P23585 YMR011W HXT2 13 Phosphoserine +P23585 YMR011W HXT2 17 Phosphoserine +P23585 YMR011W HXT2 20 Phosphoserine +P23585 YMR011W HXT2 29 Phosphothreonine +P23585 YMR011W HXT2 32 Phosphoserine +P23585 YMR011W HXT2 266 Phosphoserine%3B +P23585 YMR011W HXT2 539 Phosphoserine%3B +P23585 YMR011W HXT2 82 N-linked +P32467 YHR092C HXT4 425 N-linked +P32467 YHR092C HXT4 45 Glycyl +P39003 YDR343C HXT6 91 N-linked +P39003 YDR343C HXT6 228 N-linked +P39003 YDR343C HXT6 560 Glycyl +P40885 YJL219W HXT9 87 N-linked +P40885 YJL219W HXT9 227 N-linked +P43598 YFR017C IGD1 64 Phosphoserine +P43598 YFR017C IGD1 65 Phosphothreonine +P43598 YFR017C IGD1 95 Phosphoserine +P43598 YFR017C IGD1 96 Phosphoserine +P43598 YFR017C IGD1 132 Phosphothreonine +P43598 YFR017C IGD1 164 Phosphoserine +Q02821 YNL189W SRP1 1 N-acetylmethionine +P40069 YER110C KAP123 646 Phosphoserine +Q03694 YMR204C INP1 273 Phosphoserine +P47046 YJL051W IRC8 690 Phosphoserine +P28241 YOR136W IDH2 105 Phosphothreonine +P28241 YOR136W IDH2 153 Phosphothreonine +P28241 YOR136W IDH2 327 Phosphothreonine +P28241 YOR136W IDH2 349 Phosphothreonine +P40154 YNL215W IES2 67 Phosphoserine +P40154 YNL215W IES2 129 Phosphoserine +P47170 YJR138W IML1 680 Phosphoserine +P47170 YJR138W IML1 737 Phosphoserine +P53901 YNL152W INN1 392 Phosphoserine +P50942 YNL106C INP52 152 Phosphoserine +P50942 YNL106C INP52 522 Phosphoserine +P50942 YNL106C INP52 1005 Phosphoserine +P50942 YNL106C INP52 1016 Phosphoserine +P50942 YNL106C INP52 1032 Phosphothreonine +P50942 YNL106C INP52 1095 Phosphoserine +Q04213 YMR044W IOC4 2 Phosphoserine +Q04213 YMR044W IOC4 9 Phosphothreonine +Q04213 YMR044W IOC4 65 Phosphoserine +Q04213 YMR044W IOC4 73 Phosphoserine +Q04213 YMR044W IOC4 242 Phosphoserine +P07250 YDR173C ARG82 1 N-acetylmethionine +P07250 YDR173C ARG82 97 Phosphoserine +P07260 YOL139C CDC33 2 Phosphoserine%3B +P07260 YOL139C CDC33 15 Phosphoserine%3B +P07260 YOL139C CDC33 22 Phosphothreonine +P07260 YOL139C CDC33 28 Phosphoserine +P07260 YOL139C CDC33 30 Phosphoserine +P07260 YOL139C CDC33 114 Glycyl +P39520 YLR223C IFH1 208 Phosphoserine +P39520 YLR223C IFH1 1041 Phosphoserine +P43579 YFL013C IES1 27 Phosphoserine +P43579 YFL013C IES1 487 Phosphoserine +P43579 YFL013C IES1 493 Phosphoserine +P43579 YFL013C IES1 504 Phosphoserine +P43579 YFL013C IES1 507 Phosphothreonine +P32481 YER025W GCD11 60 Phosphothreonine +P32481 YER025W GCD11 258 Phosphoserine +P39935 YGR162W TIF4631 181 Phosphothreonine +P39935 YGR162W TIF4631 883 Phosphoserine +P39935 YGR162W TIF4631 888 Phosphothreonine +P39935 YGR162W TIF4631 908 Phosphoserine +P39935 YGR162W TIF4631 948 Phosphoserine +P23301 YEL034W HYP2 2 N-acetylserine +P23301 YEL034W HYP2 2 Phosphoserine +P23301 YEL034W HYP2 10 Phosphothreonine +P23301 YEL034W HYP2 51 Hypusine +P23301 YEL034W HYP2 74 Phosphoserine +P23301 YEL034W HYP2 86 Glycyl +Q9P305 YHR132W-A IGO2 2 N-acetylserine +Q9P305 YHR132W-A IGO2 6 Phosphoserine +Q9P305 YHR132W-A IGO2 63 Phosphoserine +Q9P305 YHR132W-A IGO2 108 Phosphoserine +Q9P305 YHR132W-A IGO2 119 Phosphoserine +P47042 YJL057C IKS1 96 Phosphoserine +P47169 YJR137C MET5 903 Phosphoserine +P05694 YER091C MET6 89 Phosphoserine +P05694 YER091C MET6 242 Phosphoserine +P05694 YER091C MET6 566 Phosphothreonine +P05694 YER091C MET6 629 Phosphoserine +P05694 YER091C MET6 706 Phosphoserine +P38920 YMR167W MLH1 441 Phosphoserine%3B +P40457 YIL149C MLP2 1512 Phosphoserine +P40457 YIL149C MLP2 1670 Phosphoserine +P53152 YGL087C MMS2 71 Phosphoserine +P38888 YHR204W MNL1 86 N-linked +P38888 YHR204W MNL1 517 N-linked +P38888 YHR204W MNL1 672 N-linked +P38888 YHR204W MNL1 762 N-linked +P41821 YNL291C MID1 32 N-linked +P41821 YNL291C MID1 70 N-linked +P41821 YNL291C MID1 112 N-linked +P41821 YNL291C MID1 125 N-linked +P41821 YNL291C MID1 159 N-linked +P41821 YNL291C MID1 175 N-linked +P41821 YNL291C MID1 228 N-linked +P41821 YNL291C MID1 238 N-linked +P41821 YNL291C MID1 265 N-linked +P41821 YNL291C MID1 282 N-linked +P41821 YNL291C MID1 285 N-linked +P41821 YNL291C MID1 291 N-linked +P41821 YNL291C MID1 324 N-linked +P34072 YNL076W MKS1 25 Phosphothreonine +P34072 YNL076W MKS1 247 Phosphoserine +P34072 YNL076W MKS1 276 Phosphoserine +P34072 YNL076W MKS1 442 Phosphoserine +P34072 YNL076W MKS1 518 Phosphoserine%3B +P32047 YNL074C MLF3 8 Phosphoserine +P32047 YNL074C MLF3 11 Phosphoserine +P32047 YNL074C MLF3 14 Phosphoserine +P32047 YNL074C MLF3 56 Phosphoserine +P32047 YNL074C MLF3 74 Phosphoserine +P32047 YNL074C MLF3 79 Phosphoserine +P32047 YNL074C MLF3 121 Phosphothreonine +P32047 YNL074C MLF3 145 Phosphoserine +P32047 YNL074C MLF3 156 Phosphoserine +P32047 YNL074C MLF3 160 Phosphoserine +P32047 YNL074C MLF3 169 Phosphothreonine +P32047 YNL074C MLF3 171 Phosphoserine +P32047 YNL074C MLF3 173 Phosphothreonine +P32047 YNL074C MLF3 183 Phosphoserine +P32047 YNL074C MLF3 189 Phosphoserine +P32047 YNL074C MLF3 227 Phosphotyrosine +P32047 YNL074C MLF3 228 Phosphoserine +P32047 YNL074C MLF3 257 Phosphoserine +P32047 YNL074C MLF3 265 Phosphoserine +P32047 YNL074C MLF3 295 Phosphotyrosine +P32047 YNL074C MLF3 297 Phosphoserine +P32047 YNL074C MLF3 320 Phosphoserine +P32047 YNL074C MLF3 353 Phosphoserine +P32047 YNL074C MLF3 439 Phosphoserine +Q12372 YLL061W MMP1 6 Phosphoserine +Q12372 YLL061W MMP1 21 Phosphothreonine +Q12372 YLL061W MMP1 23 Phosphoserine +Q06324 YLR190W MMR1 12 Phosphothreonine +Q06324 YLR190W MMR1 16 Phosphoserine +Q06324 YLR190W MMR1 37 Phosphoserine +P46982 YJL186W MNN5 113 N-linked +P46982 YJL186W MNN5 136 N-linked +P46982 YJL186W MNN5 259 N-linked +P46982 YJL186W MNN5 264 N-linked +P40549 YIL014W MNT3 34 N-linked +P40549 YIL014W MNT3 168 N-linked +P53745 YNR059W MNT4 132 N-linked +P53745 YNR059W MNT4 167 N-linked +P53745 YNR059W MNT4 223 N-linked +P53745 YNR059W MNT4 349 N-linked +P43563 YFL034C-B MOB2 33 Phosphotyrosine +P43563 YFL034C-B MOB2 59 Phosphoserine +P43563 YFL034C-B MOB2 76 Phosphothreonine +P23641 YJR077C MIR1 2 N-acetylserine%3B +P23641 YJR077C MIR1 4 Phosphoserine +P23641 YJR077C MIR1 145 Phosphoserine +P47083 YJR002W MPP10 2 N-acetylserine +P47083 YJR002W MPP10 176 Phosphoserine +P47083 YJR002W MPP10 177 Phosphoserine +P47083 YJR002W MPP10 181 Phosphotyrosine +Q06211 YPR164W MMS1 1294 Phosphothreonine +Q12205 YLR057W MNL2 45 N-linked +P38069 YBR015C MNN2 34 N-linked +P38069 YBR015C MNN2 363 N-linked +P38069 YBR015C MNN2 473 N-linked +P53129 YGL124C MON1 22 Phosphoserine +P53129 YGL124C MON1 71 Phosphoserine +P53379 YDR144C MKC7 575 GPI-anchor +P53379 YDR144C MKC7 180 N-linked +P53379 YDR144C MKC7 190 N-linked +P53379 YDR144C MKC7 219 N-linked +P53379 YDR144C MKC7 229 N-linked +P53379 YDR144C MKC7 232 N-linked +P53379 YDR144C MKC7 286 N-linked +P53379 YDR144C MKC7 346 N-linked +P53379 YDR144C MKC7 471 N-linked +P53379 YDR144C MKC7 517 N-linked +P40577 YIR025W MND2 293 Phosphoserine +P39106 YER001W MNN1 50 N-linked +P39106 YER001W MNN1 225 N-linked +P39106 YER001W MNN1 254 N-linked +P39106 YER001W MNN1 383 N-linked +P35724 YKL064W MNR2 114 Phosphoserine +P35724 YKL064W MNR2 175 Phosphoserine +P35724 YKL064W MNR2 177 Phosphothreonine +P35724 YKL064W MNR2 182 Phosphoserine +P35724 YKL064W MNR2 383 Phosphoserine +P35724 YKL064W MNR2 571 Phosphothreonine +P35724 YKL064W MNR2 576 Phosphoserine +P35724 YKL064W MNR2 582 Phosphoserine +P53059 YGL257C MNT2 187 N-linked +P38257 YBR098W MMS4 2 N-acetylserine +P38257 YBR098W MMS4 48 Phosphoserine +P38257 YBR098W MMS4 49 Phosphoserine +P38257 YBR098W MMS4 61 Phosphoserine +P40484 YIL106W MOB1 34 Phosphoserine +P40484 YIL106W MOB1 36 Phosphoserine +P40484 YIL106W MOB1 80 Phosphoserine +P40484 YIL106W MOB1 229 Phosphoserine +P54785 YMR070W MOT3 1 N-acetylmethionine +P41940 YDL055C PSA1 153 Phosphothreonine +P41940 YDL055C PSA1 244 Glycyl +P53725 YNR024W MPP6 2 N-acetylserine +P53725 YNR024W MPP6 42 Phosphoserine +P53725 YNR024W MPP6 150 Phosphoserine +Q08471 YOR066W MSA1 268 Phosphoserine +P32333 YPL082C MOT1 93 Phosphoserine +P32333 YPL082C MOT1 677 Phosphoserine +P53163 YGL068W MNP1 34 N-linked +P32906 YJR131W MNS1 96 N-linked +P32906 YJR131W MNS1 155 N-linked +P32906 YJR131W MNS1 224 N-linked +Q12404 YOR288C MPD1 47 N-linked +Q12404 YOR288C MPD1 307 N-linked +P35728 YKL059C MPE1 221 Phosphoserine +P39016 YGL178W MPT5 662 Phosphoserine +P39016 YGL178W MPT5 834 Phosphoserine +P39016 YGL178W MPT5 838 Phosphoserine +P53045 YGR060W ERG25 96 Glycyl +P33748 YMR037C MSN2 288 Phosphoserine +P33748 YMR037C MSN2 304 Phosphoserine +P33748 YMR037C MSN2 451 Phosphoserine +P33748 YMR037C MSN2 582 Phosphoserine +P33748 YMR037C MSN2 633 Phosphoserine +P40029 YER042W MXR1 58 Phosphoserine +P40850 YNL085W MKT1 358 Phosphoserine +P40850 YNL085W MKT1 362 Phosphoserine +P40850 YNL085W MKT1 371 Phosphoserine +P40850 YNL085W MKT1 4 Glycyl +P53604 YNR049C MSO1 1 N-acetylmethionine +P53604 YNR049C MSO1 102 Phosphoserine +P20676 YOR098C NUP1 2 N-acetylserine +P20676 YOR098C NUP1 54 Phosphoserine +P20676 YOR098C NUP1 161 Phosphoserine +P20676 YOR098C NUP1 381 Phosphothreonine +P20676 YOR098C NUP1 383 Phosphoserine +P20676 YOR098C NUP1 637 Phosphoserine +Q12454 YDR067C OCA6 2 Phosphothreonine +P31755 YGL038C OCH1 203 N-linked +P31755 YGL038C OCH1 281 N-linked +P31755 YGL038C OCH1 341 N-linked +P31755 YGL038C OCH1 393 N-linked +P38325 YBR230C OM14 12 Phosphoserine +P38325 YBR230C OM14 15 Phosphoserine +Q06593 YPR194C OPT2 374 N-linked +Q06593 YPR194C OPT2 860 N-linked +Q06144 YLR350W ORM2 9 Phosphoserine +Q06144 YLR350W ORM2 15 Phosphoserine +Q06144 YLR350W ORM2 18 Phosphothreonine +Q06144 YLR350W ORM2 22 Phosphoserine +Q06144 YLR350W ORM2 29 Phosphoserine +Q06144 YLR350W ORM2 51 Phosphoserine +P43558 YFL044C OTU1 160 Glycyl +P32336 YOR373W NUD1 388 Phosphothreonine +P32336 YOR373W NUD1 392 Phosphothreonine +P32336 YOR373W NUD1 417 Phosphoserine +P32336 YOR373W NUD1 419 Phosphoserine +P32336 YOR373W NUD1 357 Glycyl +P16387 YER178W PDA1 313 Phosphoserine%3B +Q06810 YPR075C OPY2 285 Phosphoserine +Q06810 YPR075C OPY2 348 Phosphoserine +Q06810 YPR075C OPY2 172 N-linked +Q06810 YPR075C OPY2 185 N-linked +P54784 YML065W ORC1 237 Phosphoserine +P07991 YLR438W CAR2 272 N6-(pyridoxal +P07991 YLR438W CAR2 390 Glycyl +P16451 YGR193C PDX1 73 N6-lipoyllysine +Q02630 YMR047C NUP116 886 Phosphoserine +P19262 YDR148C KGD2 114 N6-lipoyllysine +P19262 YDR148C KGD2 340 Phosphothreonine +P12695 YNL071W LAT1 75 N6-lipoyllysine +P54790 YLL004W ORC3 2 N-acetylserine +P05150 YJL088W ARG3 2 N-acetylserine +P52593 YML103C NUP188 340 Phosphoserine +P52593 YML103C NUP188 406 Glycyl +P21957 YHL020C OPI1 10 Phosphoserine +P54791 YPR162C ORC4 9 Phosphoserine +P38351 YBR279W PAF1 147 Phosphoserine +P38351 YBR279W PAF1 422 Phosphothreonine +Q12033 YOR275C RIM20 2 N-acetylserine +P37304 YDR251W PAM1 659 Phosphoserine +P37304 YDR251W PAM1 732 Phosphoserine +P37304 YDR251W PAM1 767 Phosphoserine +P36102 YKL025C PAN3 57 Phosphothreonine +P36102 YKL025C PAN3 252 Phosphoserine +P53298 YGR179C OKP1 70 Phosphoserine +P28273 YKL215C OXP1 930 Phosphoserine +P28273 YKL215C OXP1 1077 Phosphoserine +P40897 YJL212C OPT1 48 Phosphothreonine +P40897 YJL212C OPT1 50 Phosphothreonine +P40897 YJL212C OPT1 51 Phosphothreonine +P40897 YJL212C OPT1 46 N-linked +P40897 YJL212C OPT1 640 N-linked +P32833 YBR060C ORC2 60 Phosphothreonine +P32833 YBR060C ORC2 187 Phosphothreonine +P32833 YBR060C ORC2 188 Phosphoserine +P32567 YMR165C PAH1 110 Phosphoserine +P32567 YMR165C PAH1 114 Phosphoserine +P32567 YMR165C PAH1 168 Phosphoserine +P32567 YMR165C PAH1 511 Phosphoserine +P32567 YMR165C PAH1 602 Phosphoserine%3B +P32567 YMR165C PAH1 723 Phosphothreonine%3B +P32567 YMR165C PAH1 744 Phosphoserine%3B +P32567 YMR165C PAH1 748 Phosphoserine +P32567 YMR165C PAH1 773 Phosphoserine +P32567 YMR165C PAH1 774 Phosphoserine +P32567 YMR165C PAH1 810 Phosphoserine +P32567 YMR165C PAH1 814 Phosphoserine +P32567 YMR165C PAH1 816 Phosphothreonine +P32567 YMR165C PAH1 844 Phosphoserine +P32567 YMR165C PAH1 847 Phosphoserine +P38826 YHR118C ORC6 146 Phosphothreonine +Q05518 YDR348C PAL1 14 Phosphoserine +Q05518 YDR348C PAL1 45 Phosphoserine +Q05518 YDR348C PAL1 47 Phosphothreonine +Q05518 YDR348C PAL1 49 Phosphoserine +Q05518 YDR348C PAL1 64 Phosphoserine +Q05518 YDR348C PAL1 114 Phosphoserine +Q05518 YDR348C PAL1 121 Phosphoserine +Q05518 YDR348C PAL1 153 Phosphothreonine +Q05518 YDR348C PAL1 304 Phosphothreonine +Q05518 YDR348C PAL1 307 Phosphoserine +Q05518 YDR348C PAL1 135 Glycyl +Q05518 YDR348C PAL1 138 Glycyl +Q05518 YDR348C PAL1 292 Glycyl +Q05518 YDR348C PAL1 328 Glycyl +Q05518 YDR348C PAL1 445 Glycyl +P53179 YGL045W RIM8 521 Glycyl +P48565 YNL294C RIM21 409 Phosphoserine +P32521 YIR006C PAN1 241 Phosphothreonine +P32521 YIR006C PAN1 570 Phosphothreonine +P32521 YIR006C PAN1 747 Phosphoserine +P32521 YIR006C PAN1 757 Phosphoserine +P32521 YIR006C PAN1 993 Phosphothreonine +P32521 YIR006C PAN1 995 Phosphothreonine +P32521 YIR006C PAN1 1003 Phosphoserine +P32521 YIR006C PAN1 1180 Phosphoserine +P32521 YIR006C PAN1 1250 Phosphoserine +P32521 YIR006C PAN1 1253 Phosphoserine +P32521 YIR006C PAN1 1281 Phosphoserine +P32521 YIR006C PAN1 1321 Phosphothreonine +Q12451 YDL019C OSH2 2 N-acetylserine +Q12451 YDL019C OSH2 7 Phosphoserine +Q12451 YDL019C OSH2 422 Phosphoserine +Q12451 YDL019C OSH2 445 Phosphoserine +Q12451 YDL019C OSH2 451 Phosphoserine +Q12451 YDL019C OSH2 455 Phosphoserine +Q12451 YDL019C OSH2 458 Phosphoserine +Q12451 YDL019C OSH2 459 Phosphoserine +Q12451 YDL019C OSH2 486 Phosphoserine +Q12451 YDL019C OSH2 488 Phosphothreonine +Q12451 YDL019C OSH2 512 Phosphoserine +Q12451 YDL019C OSH2 515 Phosphoserine +Q12451 YDL019C OSH2 717 Phosphoserine +Q12451 YDL019C OSH2 783 Phosphothreonine +Q12451 YDL019C OSH2 787 Phosphoserine +Q12451 YDL019C OSH2 825 Phosphoserine +Q12451 YDL019C OSH2 1151 Phosphoserine +Q02201 YKR003W OSH6 16 Phosphoserine +P50946 YNL099C OCA1 2 N-acetylthreonine +P50946 YNL099C OCA1 24 Phosphoserine +P33767 YEL002C WBP1 60 N-linked +P33767 YEL002C WBP1 332 N-linked +P43611 YFR039C OSW7 354 Phosphotyrosine +P32263 YER023W PRO3 246 Phosphothreonine +P32263 YER023W PRO3 279 Phosphoserine +P32263 YER023W PRO3 171 Glycyl +P41543 YJL002C OST1 18 N-linked +P41543 YJL002C OST1 99 N-linked +P41543 YJL002C OST1 217 N-linked +P41543 YJL002C OST1 336 N-linked +P41543 YJL002C OST1 400 N-linked +Q08952 YPL196W OXR1 1 N-acetylmethionine +Q08952 YPL196W OXR1 178 Phosphoserine +P40091 YER149C PEA2 230 Phosphoserine +P40219 YMR148W OSW5 102 Phosphoserine +Q03558 YHR179W OYE2 353 Phosphoserine +Q03558 YHR179W OYE2 379 Phosphoserine +P25644 YCR077C PAT1 2 N-acetylserine +P25644 YCR077C PAT1 456 Phosphoserine +P25644 YCR077C PAT1 457 Phosphoserine +P24867 YNL289W PCL1 39 Phosphothreonine%3B +P24867 YNL289W PCL1 43 Phosphoserine%3B +P24867 YNL289W PCL1 82 Glycyl +P24867 YNL289W PCL1 121 Glycyl +Q08966 YPL219W PCL8 32 Phosphoserine +P15873 YBR088C POL30 127 Glycyl +P15873 YBR088C POL30 164 Glycyl +P15873 YBR088C POL30 164 Glycyl +P26263 YGR087C PDC6 2 N-acetylserine +P26263 YGR087C PDC6 223 Phosphoserine +P26263 YGR087C PDC6 266 Phosphothreonine +P26263 YGR087C PDC6 353 Phosphothreonine +P26263 YGR087C PDC6 522 Phosphothreonine +P26263 YGR087C PDC6 212 Glycyl +P26263 YGR087C PDC6 233 Glycyl +P26263 YGR087C PDC6 269 Glycyl +P26263 YGR087C PDC6 505 Glycyl +P29468 YKR002W PAP1 452 Phosphoserine +P29468 YKR002W PAP1 550 Phosphoserine +Q12515 YDL173W PAR32 2 N-acetylalanine +Q12515 YDL173W PAR32 36 Phosphoserine +Q12515 YDL173W PAR32 39 Phosphoserine +Q12515 YDL173W PAR32 47 Phosphoserine +Q12515 YDL173W PAR32 123 Phosphoserine +Q12515 YDL173W PAR32 138 Phosphoserine +Q12515 YDL173W PAR32 141 Phosphoserine +Q12515 YDL173W PAR32 147 Phosphoserine +Q12515 YDL173W PAR32 246 Phosphoserine +P40186 YIL050W PCL7 69 Phosphoserine +P17967 YCL043C PDI1 82 N-linked +P17967 YCL043C PDI1 117 N-linked +P17967 YCL043C PDI1 155 N-linked +P17967 YCL043C PDI1 174 N-linked +P17967 YCL043C PDI1 425 N-linked +P40530 YIL042C PKP1 148 Phosphohistidine%3B +P12383 YGL013C PDR1 21 Phosphoserine +P12383 YGL013C PDR1 930 Phosphoserine +P12383 YGL013C PDR1 942 Phosphoserine +P12383 YGL013C PDR1 948 Phosphoserine +P33302 YOR153W PDR5 22 Phosphoserine +P33302 YOR153W PDR5 49 Phosphothreonine +P33302 YOR153W PDR5 51 Phosphothreonine +P33302 YOR153W PDR5 54 Phosphoserine +P33302 YOR153W PDR5 58 Phosphoserine +P33302 YOR153W PDR5 61 Phosphoserine +P33302 YOR153W PDR5 837 Phosphoserine +P33302 YOR153W PDR5 840 Phosphoserine +P33302 YOR153W PDR5 841 Phosphoserine +P33302 YOR153W PDR5 849 Phosphoserine +P33302 YOR153W PDR5 850 Phosphoserine +P33302 YOR153W PDR5 854 Phosphoserine +P33302 YOR153W PDR5 734 N-linked +P33302 YOR153W PDR5 1447 N-linked +P33302 YOR153W PDR5 825 Glycyl +P53224 YGR038W ORM1 29 Phosphoserine +P53224 YGR038W ORM1 32 Phosphoserine +P53224 YGR038W ORM1 56 Phosphoserine +P35845 YAR042W SWH1 394 Phosphoserine +P35845 YAR042W SWH1 490 Phosphoserine +P35845 YAR042W SWH1 500 Phosphoserine +P35845 YAR042W SWH1 678 Phosphoserine +P35845 YAR042W SWH1 683 Phosphoserine +P35845 YAR042W SWH1 691 Phosphoserine +P35845 YAR042W SWH1 692 Phosphothreonine +P35845 YAR042W SWH1 694 Phosphothreonine +P35845 YAR042W SWH1 708 Phosphoserine +P35845 YAR042W SWH1 712 Phosphoserine +P38713 YHR073W OSH3 190 Phosphoserine +P38713 YHR073W OSH3 193 Phosphoserine +P38713 YHR073W OSH3 210 Phosphothreonine +P38713 YHR073W OSH3 323 Phosphothreonine +P38713 YHR073W OSH3 324 Phosphoserine +P38713 YHR073W OSH3 325 Phosphothreonine +P38713 YHR073W OSH3 352 Phosphothreonine +P38713 YHR073W OSH3 605 Phosphoserine +P38755 YHR001W OSH7 276 Glycyl +P08018 YJL128C PBS2 68 Phosphoserine +P08018 YJL128C PBS2 269 Phosphoserine +P08018 YJL128C PBS2 514 Phosphoserine +P08018 YJL128C PBS2 518 Phosphothreonine +P13259 YGR202C PCT1 16 Phosphoserine +P13259 YGR202C PCT1 59 Phosphothreonine +P13259 YGR202C PCT1 346 Phosphoserine +P13259 YGR202C PCT1 401 Phosphoserine%3B +Q99220 YDR057W YOS9 52 N-linked +Q99220 YDR057W YOS9 74 N-linked +Q99220 YDR057W YOS9 380 N-linked +P04147 YER165W PAB1 2 N-acetylalanine +P04147 YER165W PAB1 107 Omega-N-methylarginine +P04147 YER165W PAB1 249 Phosphoserine +P04147 YER165W PAB1 332 Phosphoserine +P04147 YER165W PAB1 405 Phosphoserine +P04147 YER165W PAB1 7 Glycyl +P04147 YER165W PAB1 337 Glycyl +P25580 YCL052C PBN1 24 N-linked +P25580 YCL052C PBN1 85 N-linked +P25580 YCL052C PBN1 120 N-linked +P25580 YCL052C PBN1 212 N-linked +P25580 YCL052C PBN1 365 N-linked +P40038 YER059W PCL6 61 Phosphoserine +P40038 YER059W PCL6 281 Phosphoserine +P40038 YER059W PCL6 312 Phosphoserine +P40038 YER059W PCL6 317 Phosphothreonine +P40550 YIL013C PDR11 595 N-linked +P40550 YIL013C PDR11 1289 N-linked +P40550 YIL013C PDR11 1324 N-linked +P40550 YIL013C PDR11 1346 N-linked +Q04182 YDR406W PDR15 558 N-linked +Q04182 YDR406W PDR15 744 N-linked +P53756 YNR070W PDR18 48 N-linked +P53756 YNR070W PDR18 144 N-linked +P53756 YNR070W PDR18 205 N-linked +P53756 YNR070W PDR18 350 N-linked +P53756 YNR070W PDR18 697 N-linked +P53756 YNR070W PDR18 733 N-linked +P53756 YNR070W PDR18 958 N-linked +P53756 YNR070W PDR18 1320 N-linked +Q04264 YMR076C PDS5 1231 Phosphoserine +Q04264 YMR076C PDS5 1233 Phosphoserine +P36139 YKR046C PET10 2 N-acetylserine +P53112 YGL153W PEX14 2 N-acetylserine +P53112 YGL153W PEX14 313 Phosphoserine +P48363 YGR078C PAC10 1 N-acetylmethionine +P38075 YBR035C PDX3 29 Glycyl +P47116 YJR059W PTK2 56 Phosphothreonine +P47116 YJR059W PTK2 59 Phosphoserine +P47116 YJR059W PTK2 80 Phosphoserine +P47116 YJR059W PTK2 623 Phosphoserine +P47116 YJR059W PTK2 632 Phosphoserine +P47116 YJR059W PTK2 694 Phosphoserine +P47116 YJR059W PTK2 700 Phosphothreonine +P47116 YJR059W PTK2 711 Phosphoserine +P47116 YJR059W PTK2 737 Phosphothreonine +P47116 YJR059W PTK2 752 Phosphoserine +P47116 YJR059W PTK2 755 Phosphoserine +P47116 YJR059W PTK2 778 Phosphoserine +P47116 YJR059W PTK2 781 Phosphoserine +P29461 YOR208W PTP2 258 Phosphoserine +P29461 YOR208W PTP2 430 Phosphoserine +P07244 YGL234W ADE5,7 455 Phosphoserine +P07244 YGL234W ADE5,7 458 Phosphoserine +P03962 YEL021W URA3 2 N-acetylserine +P03962 YEL021W URA3 93 Glycyl +P03962 YEL021W URA3 209 Glycyl +P03962 YEL021W URA3 253 Glycyl +P25339 YGL014W PUF4 205 Phosphothreonine +P25339 YGL014W PUF4 212 Phosphothreonine +P25339 YGL014W PUF4 252 Phosphothreonine +P25339 YGL014W PUF4 256 Phosphoserine +Q06991 YLR414C PUN1 100 N-linked +Q06991 YLR414C PUN1 209 N-linked +Q06991 YLR414C PUN1 260 Glycyl +P38972 YGR061C ADE6 2 N-acetylthreonine +P11154 YGL062W PYC1 734 N6-carboxylysine +P11154 YGL062W PYC1 1135 N6-biotinyllysine +P28272 YKL216W URA1 46 Glycyl +Q12355 YDR055W PST1 419 GPI-anchor +Q12355 YDR055W PST1 57 N-linked +Q12355 YDR055W PST1 76 N-linked +Q12355 YDR055W PST1 83 N-linked +Q12355 YDR055W PST1 86 N-linked +Q12355 YDR055W PST1 196 N-linked +Q12355 YDR055W PST1 210 N-linked +Q12355 YDR055W PST1 228 N-linked +Q12355 YDR055W PST1 235 N-linked +Q12355 YDR055W PST1 242 N-linked +Q12355 YDR055W PST1 263 N-linked +Q12355 YDR055W PST1 268 N-linked +Q12355 YDR055W PST1 280 N-linked +Q12355 YDR055W PST1 292 N-linked +Q12355 YDR055W PST1 305 N-linked +Q12355 YDR055W PST1 329 N-linked +P39927 YGR156W PTI1 272 Phosphoserine +P27616 YAR015W ADE1 2 N-acetylserine +Q05911 YLR359W ADE13 196 Glycyl +P32641 YER173W RAD24 652 Phosphoserine +P32641 YER173W RAD24 654 Phosphoserine +Q00578 YIL143C SSL2 752 Phosphoserine +Q04231 YML011C RAD33 2 N-acetylserine +Q04231 YML011C RAD33 19 Glycyl +P22216 YPL153C RAD53 24 Phosphoserine +P22216 YPL153C RAD53 175 Phosphoserine +P22216 YPL153C RAD53 547 Phosphoserine +P22216 YPL153C RAD53 560 Phosphoserine +P22216 YPL153C RAD53 774 Phosphoserine +P22216 YPL153C RAD53 793 Phosphoserine +P06779 YJR052W RAD7 64 Phosphoserine +P06779 YJR052W RAD7 85 Phosphoserine +P32864 YOR370C MRS6 470 Phosphoserine +P25635 YCR057C PWP2 225 Phosphoserine +P25635 YCR057C PWP2 232 Phosphoserine +P25635 YCR057C PWP2 651 Phosphoserine +P25635 YCR057C PWP2 664 Phosphoserine +P25635 YCR057C PWP2 912 Phosphoserine +P25635 YCR057C PWP2 913 Phosphoserine +P34230 YKL188C PXA2 33 N-linked +P34230 YKL188C PXA2 39 N-linked +P34230 YKL188C PXA2 162 N-linked +P34230 YKL188C PXA2 230 N-linked +P34230 YKL188C PXA2 241 N-linked +P34230 YKL188C PXA2 267 N-linked +P34230 YKL188C PXA2 295 N-linked +P34230 YKL188C PXA2 560 N-linked +P34230 YKL188C PXA2 608 N-linked +P34230 YKL188C PXA2 620 N-linked +P34230 YKL188C PXA2 647 N-linked +P34230 YKL188C PXA2 836 N-linked +P32327 YBR218C PYC2 2 N-acetylserine +P32327 YBR218C PYC2 735 N6-carboxylysine +P32327 YBR218C PYC2 1136 N6-biotinyllysine +P13298 YML106W URA5 213 Phosphoserine +P13298 YML106W URA5 225 Phosphoserine +P06777 YPL022W RAD1 613 Phosphoserine +P06777 YPL022W RAD1 1071 Phosphoserine +P06777 YPL022W RAD1 1072 Phosphothreonine +P32628 YEL037C RAD23 94 Phosphothreonine +P32628 YEL037C RAD23 121 Phosphoserine +P32628 YEL037C RAD23 139 Phosphothreonine +P32628 YEL037C RAD23 49 Glycyl +P53037 YGR170W PSD2 1043 Pyruvic +P31374 YAL017W PSK1 10 Phosphoserine +P31374 YAL017W PSK1 192 Phosphoserine +P31374 YAL017W PSK1 202 Phosphoserine +P31374 YAL017W PSK1 255 Phosphoserine +P31374 YAL017W PSK1 286 Phosphoserine +P31374 YAL017W PSK1 327 Phosphoserine +P31374 YAL017W PSK1 926 Phosphoserine +P31374 YAL017W PSK1 1018 Phosphoserine +P31374 YAL017W PSK1 1023 Phosphoserine +P31374 YAL017W PSK1 1035 Phosphoserine +P31374 YAL017W PSK1 1055 Phosphoserine +P31374 YAL017W PSK1 1079 Phosphothreonine +Q01329 YAL043C PTA1 500 Phosphoserine +Q04373 YDR496C PUF6 31 Phosphoserine%3B +Q04373 YDR496C PUF6 34 Phosphoserine +Q04373 YDR496C PUF6 34 Phosphoserine%3B +Q04373 YDR496C PUF6 35 Phosphoserine +Q04373 YDR496C PUF6 35 Phosphoserine%3B +Q02256 YIR026C YVH1 196 Phosphoserine +P21304 YLR196W PWP1 52 Phosphoserine +P21304 YLR196W PWP1 131 Phosphoserine +P50896 YDR505C PSP1 31 Phosphoserine +P50896 YDR505C PSP1 34 Phosphoserine +P50896 YDR505C PSP1 36 Phosphoserine +P50896 YDR505C PSP1 237 Phosphoserine +P50896 YDR505C PSP1 334 Phosphothreonine +P50896 YDR505C PSP1 520 Phosphoserine +P34222 YBL057C PTH2 152 Glycyl +Q08647 YOR243C PUS7 2 N-acetylserine +P39006 YNL169C PSD1 463 Pyruvic +P25044 YDL230W PTP1 83 Phosphoserine%3B +P40048 YER075C PTP3 75 Phosphothreonine +P40048 YER075C PTP3 248 Phosphoserine +P40048 YER075C PTP3 297 Phosphoserine +P40048 YER075C PTP3 368 Phosphoserine +P40454 YIL153W RRD1 341 Phosphoserine +P32588 YNL016W PUB1 2 N-acetylserine +Q12221 YPR042C PUF2 72 Phosphoserine +Q12221 YPR042C PUF2 198 Phosphoserine +Q12221 YPR042C PUF2 872 Phosphoserine +Q12221 YPR042C PUF2 876 Phosphoserine +Q07807 YLL013C PUF3 83 Phosphothreonine +Q07807 YLL013C PUF3 207 Phosphoserine +Q07807 YLL013C PUF3 210 Phosphoserine +P21264 YOR128C ADE2 37 Phosphoserine +P41909 YPL147W PXA1 142 N-linked +P41909 YPL147W PXA1 281 N-linked +P41909 YPL147W PXA1 403 N-linked +P36166 YKR090W PXL1 43 Phosphoserine +P36166 YKR090W PXL1 63 Phosphoserine +P53335 YGR280C PXR1 230 Phosphoserine +P10622 YDL130W RPP1B 2 N-acetylserine +P10622 YDL130W RPP1B 96 Phosphoserine +P36159 YKR079C TRZ1 824 Phosphoserine +P51862 YLR371W ROM2 2 N-acetylserine +P51862 YLR371W ROM2 76 Phosphoserine +P51862 YLR371W ROM2 193 Phosphoserine +P51862 YLR371W ROM2 223 Phosphoserine +P51862 YLR371W ROM2 566 Phosphoserine +P51862 YLR371W ROM2 628 Phosphoserine +Q01080 YNL248C RPA49 34 Phosphoserine +Q01080 YNL248C RPA49 151 Phosphoserine +P27999 YGL070C RPB9 40 Phosphoserine +Q02933 YPL123C RNY1 37 N-linked +Q02933 YPL123C RNY1 70 N-linked +Q02933 YPL123C RNY1 103 N-linked +Q02933 YPL123C RNY1 123 N-linked +P10964 YOR341W RPA190 889 Phosphoserine +P10964 YOR341W RPA190 1636 Phosphoserine +P07703 YPR110C RPC40 2 N-acetylserine +P07703 YPR110C RPC40 17 Phosphoserine +P16370 YIL021W RPB3 2 N-acetylserine +Q12250 YDL147W RPN5 2 N-acetylserine +Q06103 YPR108W RPN7 8 Phosphoserine +Q06103 YPR108W RPN7 77 Phosphoserine +P38061 YBL092W RPL32 40 Phosphoserine +P05319 YOL039W RPP2A 16 Phosphothreonine +P05319 YOL039W RPP2A 40 Phosphoserine +P05319 YOL039W RPP2A 43 Phosphoserine +P05319 YOL039W RPP2A 49 Phosphoserine +P05319 YOL039W RPP2A 96 Phosphoserine +P05319 YOL039W RPP2A 2 Glycyl +P05319 YOL039W RPP2A 48 Glycyl +P02400 YDR382W RPP2B 29 Phosphoserine +P02400 YDR382W RPP2B 100 Phosphoserine +P02400 YDR382W RPP2B 49 Glycyl +Q12495 YPR018W RLF2 78 Phosphothreonine +Q12495 YPR018W RLF2 94 Phosphoserine +Q12495 YPR018W RLF2 509 Phosphothreonine +Q03195 YDR091C RLI1 349 Phosphoserine +Q12224 YPL089C RLM1 120 Phosphoserine +Q12224 YPL089C RLM1 164 Phosphoserine +Q12224 YPL089C RLM1 374 Phosphoserine +Q12224 YPL089C RLM1 377 Phosphoserine +P36534 YPL173W MRPL40 2 N-acetylserine +P43620 YFR048W RMD8 2 N-acetylserine +P0CX26 YJR094W-A RPL43B 40 Phosphoserine +P0CX28 YHR141C RPL42B 40 N6-methyllysine%3B +P0CX28 YHR141C RPL42B 55 N6-methyllysine%3B +Q02326 YML073C RPL6A 2 N-acetylserine +Q02326 YML073C RPL6A 12 Phosphoserine +Q02326 YML073C RPL6A 128 Glycyl +P05317 YLR340W RPP0 68 Phosphoserine +P05317 YLR340W RPP0 302 Phosphoserine%3B +P05317 YLR340W RPP0 14 Glycyl +P05317 YLR340W RPP0 97 Glycyl +P05317 YLR340W RPP0 144 Glycyl +Q07915 YLR009W RLP24 172 Phosphoserine +P11745 YMR235C RNA1 360 Phosphoserine +P05747 YFR032C-A RPL29 52 Glycyl +P0CX27 YNL162W RPL42A 40 N6-methyllysine%3B +P0CX27 YNL162W RPL42A 55 N6-methyllysine%3B +P02406 YGL103W RPL28 96 Glycyl +P0CX85 YDL136W RPL35B 13 Phosphoserine +P0CX85 YDL136W RPL35B 50 Phosphoserine +P14126 YOR063W RPL3 24 Phosphoserine +P14126 YOR063W RPL3 103 Phosphothreonine +P14126 YOR063W RPL3 156 Phosphoserine +P14126 YOR063W RPL3 243 Pros-methylhistidine +P14126 YOR063W RPL3 297 Phosphoserine +P14126 YOR063W RPL3 39 Glycyl +P14126 YOR063W RPL3 136 Glycyl +P0CH09 YKR094C RPL40B 76 Glycyl +P0CH09 YKR094C RPL40B 93 Glycyl +P10664 YBR031W RPL4A 2 N-acetylserine +Q12487 YOR150W MRPL23 2 N-acetylserine +P0CX42 YER117W RPL23B 2 N-acetylserine +P0CX42 YER117W RPL23B 106 N6%2CN6-dimethyllysine%3B +P0CX42 YER117W RPL23B 110 N6%2CN6-dimethyllysine%3B +P04456 YOL127W RPL25 61 Glycyl +P05318 YDL081C RPP1A 2 N-acetylserine +P05318 YDL081C RPP1A 96 Phosphoserine +P0CH08 YIL148W RPL40A 76 Glycyl +P0CH08 YIL148W RPL40A 93 Glycyl +P0CX25 YPR043W RPL43A 40 Phosphoserine +P26321 YPL131W RPL5 167 Phosphoserine +P26321 YPL131W RPL5 176 Phosphoserine +P26321 YPL131W RPL5 235 Phosphoserine +P26321 YPL131W RPL5 164 Glycyl +P05739 YLR448W RPL6B 12 Phosphoserine +P05739 YLR448W RPL6B 128 Glycyl +P38144 YBR245C ISW1 694 Phosphothreonine +P38144 YBR245C ISW1 846 Phosphoserine +Q08773 YOR304W ISW2 17 Phosphoserine +Q08773 YOR304W ISW2 19 Phosphoserine +Q08773 YOR304W ISW2 831 Phosphoserine +Q08773 YOR304W ISW2 1079 Phosphothreonine +Q08773 YOR304W ISW2 1082 Phosphoserine +Q03419 YDR492W IZH1 79 N-linked +Q03419 YDR492W IZH1 207 N-linked +P36224 YMR294W JNM1 91 Phosphoserine +P07170 YDR226W ADK1 2 N-acetylserine +P07170 YDR226W ADK1 3 N-acetylserine +Q12055 YDL166C FAP7 183 Phosphotyrosine +Q12055 YDL166C FAP7 188 Phosphoserine +Q12055 YDL166C FAP7 196 Phosphoserine +P06245 YPL203W TPK2 1 N-acetylmethionine +P06245 YPL203W TPK2 224 Phosphothreonine +Q04746 YMR065W KAR5 159 N-linked +Q04746 YMR065W KAR5 206 N-linked +Q04746 YMR065W KAR5 313 N-linked +Q04746 YMR065W KAR5 404 N-linked +P39962 YER123W YCK3 517 S-palmitoyl +P39962 YER123W YCK3 518 S-palmitoyl +P39962 YER123W YCK3 519 S-palmitoyl +P39962 YER123W YCK3 520 S-palmitoyl +P39962 YER123W YCK3 522 S-palmitoyl +P39962 YER123W YCK3 523 S-palmitoyl +P39962 YER123W YCK3 524 S-palmitoyl +P27466 YFR014C CMK1 343 Phosphotyrosine +P27466 YFR014C CMK1 357 Phosphoserine +P27466 YFR014C CMK1 417 Phosphoserine +P27466 YFR014C CMK1 418 Phosphoserine +P27466 YFR014C CMK1 420 Phosphoserine +P27466 YFR014C CMK1 429 Phosphoserine +P34167 YPR163C TIF3 65 Phosphoserine +P34167 YPR163C TIF3 71 Phosphoserine +P38431 YPR041W TIF5 170 Phosphoserine +P38431 YPR041W TIF5 172 Phosphoserine +P38431 YPR041W TIF5 191 Phosphothreonine +P38431 YPR041W TIF5 228 Phosphoserine +P38431 YPR041W TIF5 317 Phosphothreonine +P38431 YPR041W TIF5 397 Phosphoserine +P53897 YNL157W IGO1 32 Phosphoserine +P53897 YNL157W IGO1 64 Phosphoserine +P50094 YML056C IMD4 125 Phosphoserine +Q06704 YLR309C IMH1 308 Phosphoserine +Q06704 YLR309C IMH1 660 Phosphoserine +Q06704 YLR309C IMH1 827 Phosphoserine +Q06704 YLR309C IMH1 830 Phosphothreonine +P47031 YJL082W IML2 265 Phosphoserine +P47031 YJL082W IML2 268 Phosphoserine +P47031 YJL082W IML2 378 Phosphoserine +P47031 YJL082W IML2 380 Phosphothreonine +P47031 YJL082W IML2 383 Phosphoserine +P47031 YJL082W IML2 392 Phosphoserine +P32351 YIL154C IMP2' 24 Phosphothreonine +P11986 YJL153C INO1 368 Phosphoserine +P53115 YGL150C INO80 65 Phosphoserine +P53115 YGL150C INO80 115 Phosphoserine +P53115 YGL150C INO80 133 Phosphoserine +P53115 YGL150C INO80 610 Phosphoserine +P07278 YIL033C BCY1 3 Phosphoserine +P07278 YIL033C BCY1 4 Phosphoserine +P07278 YIL033C BCY1 9 Phosphoserine +P07278 YIL033C BCY1 68 Phosphoserine +P07278 YIL033C BCY1 70 Phosphoserine +P07278 YIL033C BCY1 74 Phosphoserine +P07278 YIL033C BCY1 77 Phosphoserine +P07278 YIL033C BCY1 79 Phosphoserine +P07278 YIL033C BCY1 81 Phosphoserine +P07278 YIL033C BCY1 83 Phosphoserine +P07278 YIL033C BCY1 84 Phosphoserine +P07278 YIL033C BCY1 129 Phosphothreonine +P07278 YIL033C BCY1 130 Phosphoserine +P07278 YIL033C BCY1 131 Phosphothreonine +P07278 YIL033C BCY1 144 Phosphothreonine +P07278 YIL033C BCY1 145 Phosphoserine%3B +P07278 YIL033C BCY1 147 Phosphoserine +P07278 YIL033C BCY1 150 Phosphothreonine +P07278 YIL033C BCY1 160 Phosphothreonine +P23292 YNL154C YCK2 2 N-acetylserine +P23292 YNL154C YCK2 455 Phosphoserine +P23292 YNL154C YCK2 545 S-palmitoyl +P23292 YNL154C YCK2 546 S-palmitoyl +P23292 YNL154C YCK2 465 Glycyl +P19158 YOL081W IRA2 635 Phosphothreonine +P30605 YDR497C ITR1 12 Phosphothreonine +P30605 YDR497C ITR1 26 Phosphoserine +P30605 YDR497C ITR1 31 Phosphoserine +P30605 YDR497C ITR1 35 Phosphoserine +P30605 YDR497C ITR1 37 Phosphoserine +P30605 YDR497C ITR1 46 Phosphoserine +P30605 YDR497C ITR1 371 N-linked +P30605 YDR497C ITR1 573 Glycyl +Q07959 YLR023C IZH3 45 N-linked +Q07959 YLR023C IZH3 123 N-linked +Q07959 YLR023C IZH3 153 N-linked +Q07959 YLR023C IZH3 256 N-linked +Q07959 YLR023C IZH3 319 N-linked +P53863 YNL227C JJJ1 393 Phosphoserine +P53863 YNL227C JJJ1 504 Phosphothreonine +P22517 YOL016C CMK2 316 Phosphothreonine%3B +P22517 YOL016C CMK2 353 Phosphotyrosine +P22517 YOL016C CMK2 354 Phosphoserine +P22517 YOL016C CMK2 367 Phosphoserine +P22517 YOL016C CMK2 371 Phosphoserine +P22517 YOL016C CMK2 387 Phosphoserine%3B +P22517 YOL016C CMK2 443 Phosphoserine +Q12494 YDR017C KCS1 150 Phosphoserine +Q12494 YDR017C KCS1 396 Phosphoserine +Q12494 YDR017C KCS1 469 Phosphoserine +Q12494 YDR017C KCS1 537 Phosphoserine +Q12494 YDR017C KCS1 539 Phosphoserine +Q12494 YDR017C KCS1 566 Phosphoserine +Q12494 YDR017C KCS1 583 Phosphoserine +Q12494 YDR017C KCS1 589 Phosphoserine +Q12494 YDR017C KCS1 646 Phosphoserine +Q12494 YDR017C KCS1 664 Phosphoserine +Q12494 YDR017C KCS1 670 Phosphoserine +Q06142 YLR347C KAP95 2 N-acetylserine +Q06142 YLR347C KAP95 836 Phosphoserine +P32337 YMR308C PSE1 2 N-acetylserine +P32337 YMR308C PSE1 830 Phosphothreonine +P53067 YGL241W KAP114 1 N-acetylmethionine +P47135 YJR091C JSN1 129 Phosphoserine +P47135 YJR091C JSN1 131 Phosphothreonine +P47135 YJR091C JSN1 160 Phosphoserine +P47135 YJR091C JSN1 168 Phosphoserine +P47135 YJR091C JSN1 913 Phosphoserine +Q02932 YPL125W KAP120 2 N-acetylalanine +P01094 YMR174C PAI3 1 N-acetylmethionine +P53877 YNL182C IPI3 388 Phosphoserine +P18963 YBR140C IRA1 497 Phosphoserine +P18963 YBR140C IRA1 915 Phosphoserine +P18963 YBR140C IRA1 1342 Phosphoserine +P18963 YBR140C IRA1 1753 Phosphoserine%3B +P18963 YBR140C IRA1 3004 Phosphoserine%3B +P47056 YJL037W IRC18 74 N-linked +P47056 YJL037W IRC18 104 N-linked +P00817 YBR011C IPP1 65 Phosphothreonine +P00817 YBR011C IPP1 251 Phosphothreonine +P00817 YBR011C IPP1 266 Phosphoserine +P00817 YBR011C IPP1 286 Phosphoserine +P00817 YBR011C IPP1 239 Glycyl +P00817 YBR011C IPP1 279 Glycyl +Q12280 YPL242C IQG1 264 Phosphothreonine +Q12280 YPL242C IQG1 268 Phosphoserine +Q12280 YPL242C IQG1 299 Phosphothreonine +P32488 YMR081C ISF1 119 Phosphoserine +Q07532 YDL115C IWR1 2 N-acetylserine +P33417 YKL032C IXR1 532 Phosphoserine +P0CT04 YNL015W PBI2 74 Phosphothreonine +P36115 YKR019C IRS4 180 Phosphoserine +Q12358 YLL057C JLP1 52 Phosphoserine +P05986 YKL166C TPK3 15 Phosphoserine +P05986 YKL166C TPK3 55 Phosphoserine +P11927 YNL188W KAR1 233 Phosphothreonine +P32526 YPL269W KAR9 496 Phosphoserine +P23291 YHR135C YCK1 522 Phosphoserine +P23291 YHR135C YCK1 523 Phosphoserine +P23291 YHR135C YCK1 527 Phosphoserine +P23291 YHR135C YCK1 537 S-palmitoyl +P23291 YHR135C YCK1 538 S-palmitoyl +P35844 YPL145C KES1 370 Phosphothreonine +P35844 YPL145C KES1 389 Phosphoserine +P13134 YNL238W KEX2 42 N-linked +P13134 YNL238W KEX2 163 N-linked +P13134 YNL238W KEX2 404 N-linked +P13134 YNL238W KEX2 480 N-linked +P38692 YHR102W KIC1 735 Phosphoserine +P38991 YPL209C IPL1 5 Phosphoserine%3B +P38991 YPL209C IPL1 76 Phosphoserine +P38991 YPL209C IPL1 260 Phosphothreonine%3B +P38250 YBR086C IST2 638 Phosphoserine +P38250 YBR086C IST2 701 Phosphothreonine +P38250 YBR086C IST2 704 Phosphoserine +P38250 YBR086C IST2 720 Phosphoserine +P38250 YBR086C IST2 726 Phosphothreonine +P38250 YBR086C IST2 729 Phosphoserine +P38250 YBR086C IST2 730 Phosphotyrosine +P38250 YBR086C IST2 757 Phosphoserine +P38250 YBR086C IST2 793 Phosphoserine +P38250 YBR086C IST2 844 Phosphoserine +P38250 YBR086C IST2 847 Phosphoserine +P38250 YBR086C IST2 850 Phosphothreonine +P25389 YCL024W KCC4 396 Phosphoserine +P25389 YCL024W KCC4 675 Phosphoserine +P25389 YCL024W KCC4 707 Phosphoserine +P25389 YCL024W KCC4 777 Phosphoserine +P25389 YCL024W KCC4 822 Phosphoserine +P25389 YCL024W KCC4 825 Phosphoserine +P25389 YCL024W KCC4 871 Phosphoserine +P17423 YHR025W THR1 133 Glycyl +P13185 YDR122W KIN1 534 Phosphoserine +P13185 YDR122W KIN1 593 Phosphoserine +P13185 YDR122W KIN1 646 Phosphoserine +P13185 YDR122W KIN1 764 Phosphoserine +P13185 YDR122W KIN1 986 Phosphoserine +P06242 YDL108W KIN28 162 Phosphothreonine%3B +P24583 YBL105C PKC1 226 Phosphoserine +P24583 YBL105C PKC1 761 Phosphoserine +Q06505 YPR133C SPN1 15 Phosphothreonine +Q06505 YPR133C SPN1 23 Phosphoserine%3B +Q06505 YPR133C SPN1 40 Phosphoserine +Q06505 YPR133C SPN1 85 Phosphoserine +Q06505 YPR133C SPN1 86 Phosphothreonine +Q06505 YPR133C SPN1 89 Phosphoserine +Q03361 YDR475C JIP4 48 Phosphoserine +Q03361 YDR475C JIP4 51 Phosphoserine +Q03361 YDR475C JIP4 360 Phosphoserine +Q03361 YDR475C JIP4 510 Phosphoserine +Q03361 YDR475C JIP4 552 Phosphoserine +Q03361 YDR475C JIP4 577 Phosphoserine +Q03361 YDR475C JIP4 775 Phosphoserine +P00549 YAL038W CDC19 2 N-acetylserine +P00549 YAL038W CDC19 9 Phosphoserine +P00549 YAL038W CDC19 16 Phosphoserine +P00549 YAL038W CDC19 31 Phosphothreonine +P00549 YAL038W CDC19 70 Phosphoserine +P00549 YAL038W CDC19 184 Phosphothreonine +P00549 YAL038W CDC19 213 Phosphoserine +P00549 YAL038W CDC19 316 Phosphoserine +P00549 YAL038W CDC19 450 Phosphoserine +P00549 YAL038W CDC19 478 Phosphothreonine +P00549 YAL038W CDC19 204 Glycyl +P00549 YAL038W CDC19 255 Glycyl +P00549 YAL038W CDC19 446 Glycyl +P14681 YGR040W KSS1 183 Phosphothreonine +P14681 YGR040W KSS1 185 Phosphotyrosine +P50090 YGR238C KEL2 455 Phosphothreonine +P50090 YGR238C KEL2 509 Phosphoserine +P13186 YLR096W KIN2 22 Phosphoserine +P13186 YLR096W KIN2 146 Phosphoserine +P13186 YLR096W KIN2 549 Phosphoserine +P13186 YLR096W KIN2 609 Phosphoserine +P13186 YLR096W KIN2 888 Phosphoserine +Q01919 YOR233W KIN4 365 Phosphoserine +Q01919 YOR233W KIN4 388 Phosphoserine +Q01919 YOR233W KIN4 521 Phosphoserine +Q01919 YOR233W KIN4 748 Phosphoserine +P52489 YOR347C PYK2 24 Phosphoserine +P42846 YNL308C KRI1 177 Phosphoserine +P42846 YNL308C KRI1 184 Phosphoserine +P42846 YNL308C KRI1 185 Phosphoserine +P42846 YNL308C KRI1 486 Phosphoserine +P54070 YPL053C KTR6 82 N-linked +P54070 YPL053C KTR6 98 N-linked +Q06554 YLR247C IRC20 2 N-acetylserine +Q06554 YLR247C IRC20 810 Phosphoserine +P32361 YHR079C IRE1 840 Phosphoserine%3B +P32361 YHR079C IRE1 841 Phosphoserine%3B +P32361 YHR079C IRE1 111 N-linked +P32361 YHR079C IRE1 213 N-linked +P32361 YHR079C IRE1 298 N-linked +P32361 YHR079C IRE1 397 N-linked +P30606 YOL103W ITR2 394 N-linked +Q04934 YDR229W IVY1 59 Phosphoserine +Q04934 YDR229W IVY1 84 Phosphoserine +Q04934 YDR229W IVY1 85 Phosphoserine +Q04934 YDR229W IVY1 335 Phosphoserine +P36035 YKL217W JEN1 2 N-acetylserine +P36035 YKL217W JEN1 4 Phosphoserine +P36035 YKL217W JEN1 11 Phosphoserine +P36035 YKL217W JEN1 61 Phosphoserine +P36035 YKL217W JEN1 66 Phosphoserine +P36035 YKL217W JEN1 70 Phosphothreonine +P36035 YKL217W JEN1 584 Phosphoserine +P36035 YKL217W JEN1 603 Phosphoserine +P36035 YKL217W JEN1 606 Phosphoserine +P36035 YKL217W JEN1 9 Glycyl +P36035 YKL217W JEN1 338 Glycyl +P46997 YJL162C JJJ2 229 Phosphoserine +P06244 YJL164C TPK1 2 N-acetylserine +Q08979 YPL263C KEL3 47 Phosphoserine +Q04066 YDR428C BNA7 9 Phosphoserine +P38853 YHR158C KEL1 20 Phosphoserine +P38853 YHR158C KEL1 23 Phosphoserine +P38853 YHR158C KEL1 25 Phosphoserine +P38853 YHR158C KEL1 94 Phosphoserine +P38853 YHR158C KEL1 467 Phosphothreonine +P38853 YHR158C KEL1 477 Phosphothreonine +P38853 YHR158C KEL1 503 Phosphoserine +P38853 YHR158C KEL1 604 Phosphothreonine +P38853 YHR158C KEL1 613 Phosphoserine +P38853 YHR158C KEL1 626 Phosphothreonine +P38853 YHR158C KEL1 689 Phosphoserine +P38853 YHR158C KEL1 691 Phosphoserine +P38853 YHR158C KEL1 717 Phosphoserine +P38853 YHR158C KEL1 748 Phosphoserine +P38853 YHR158C KEL1 837 Phosphoserine +P38853 YHR158C KEL1 848 Phosphoserine +P38853 YHR158C KEL1 958 Phosphoserine +P38853 YHR158C KEL1 997 Phosphoserine +P38853 YHR158C KEL1 1003 Phosphoserine +P38853 YHR158C KEL1 1022 Phosphoserine +P40309 YJL094C KHA1 557 Phosphoserine +P40309 YJL094C KHA1 562 Glycyl +P25341 YCR091W KIN82 203 Phosphoserine +P40504 YIL085C KTR7 89 N-linked +P40504 YIL085C KTR7 144 N-linked +P09620 YGL203C KEX1 660 Phosphoserine +P09620 YGL203C KEX1 81 N-linked +P09620 YGL203C KEX1 459 N-linked +P09620 YGL203C KEX1 467 N-linked +P15454 YDR454C GUK1 2 N-acetylserine +P15454 YDR454C GUK1 149 Phosphoserine +P15454 YDR454C GUK1 157 Phosphotyrosine +P17260 YNL322C KRE1 288 GPI-anchor +P38691 YHR082C KSP1 416 Phosphoserine +P38691 YHR082C KSP1 419 Phosphoserine +P38691 YHR082C KSP1 501 Phosphothreonine +P38691 YHR082C KSP1 504 Phosphothreonine +P38691 YHR082C KSP1 526 Phosphothreonine +P38691 YHR082C KSP1 529 Phosphoserine +P38691 YHR082C KSP1 646 Phosphoserine +P38691 YHR082C KSP1 845 Phosphoserine +P38691 YHR082C KSP1 884 Phosphoserine +P38691 YHR082C KSP1 1005 Phosphothreonine +P38691 YHR082C KSP1 1014 Phosphoserine +P38800 YHR080C LAM4 66 Phosphothreonine +P38800 YHR080C LAM4 747 Phosphoserine +P20485 YLR133W CKI1 30 Phosphoserine%3B +P20485 YLR133W CKI1 48 Phosphoserine +P20485 YLR133W CKI1 51 Phosphoserine +P20485 YLR133W CKI1 54 Phosphothreonine +P20485 YLR133W CKI1 85 Phosphoserine%3B +P22023 YOR336W KRE5 115 N-linked +P22023 YOR336W KRE5 228 N-linked +P22023 YOR336W KRE5 293 N-linked +P22023 YOR336W KRE5 457 N-linked +P22023 YOR336W KRE5 519 N-linked +P22023 YOR336W KRE5 523 N-linked +P22023 YOR336W KRE5 644 N-linked +P22023 YOR336W KRE5 870 N-linked +P22023 YOR336W KRE5 1091 N-linked +P22023 YOR336W KRE5 1150 N-linked +P22023 YOR336W KRE5 1195 N-linked +P33550 YKR061W KTR2 65 N-linked +P33550 YKR061W KTR2 81 N-linked +P33550 YKR061W KTR2 92 N-linked +P33550 YKR061W KTR2 167 N-linked +P43560 YFL042C LAM5 110 Phosphothreonine +P43560 YFL042C LAM5 113 Phosphoserine +P43560 YFL042C LAM5 140 Phosphoserine +P43560 YFL042C LAM5 143 Phosphothreonine +P43560 YFL042C LAM5 149 Phosphoserine +P36004 YKL168C KKQ8 19 Phosphoserine +P36004 YKL168C KKQ8 232 Phosphoserine +P36004 YKL168C KKQ8 238 Phosphoserine +P36004 YKL168C KKQ8 241 Phosphoserine +P32350 YLL019C KNS1 562 Phosphothreonine +P32895 YKL181W PRS1 199 Phosphoserine +P32895 YKL181W PRS1 218 Phosphoserine +P32895 YKL181W PRS1 271 Phosphoserine +P32895 YKL181W PRS1 295 Phosphoserine +P40970 YDR062W LCB2 366 N6-(pyridoxal +P39002 YIL009W FAA3 2 N-acetylserine +P40079 YER127W LCP5 2 N-acetylserine +P25587 YCL005W LDB16 180 Phosphothreonine +P25587 YCL005W LDB16 184 Phosphothreonine +P25587 YCL005W LDB16 241 Phosphoserine +Q02799 YPL054W LEE1 21 Phosphoserine +Q02799 YPL054W LEE1 30 Phosphoserine +Q02799 YPL054W LEE1 282 Phosphoserine +P53281 YGR136W LSB1 2 N-acetylserine +P53281 YGR136W LSB1 48 Phosphoserine +P53281 YGR136W LSB1 114 Phosphoserine +P53281 YGR136W LSB1 116 Phosphoserine +P53281 YGR136W LSB1 41 Glycyl +P53281 YGR136W LSB1 79 Glycyl +P53281 YGR136W LSB1 118 Glycyl +P53281 YGR136W LSB1 219 Glycyl +P42838 YNL323W LEM3 36 Phosphoserine +P42838 YNL323W LEM3 113 N-linked +P42838 YNL323W LEM3 240 N-linked +P42838 YNL323W LEM3 256 N-linked +P42838 YNL323W LEM3 279 N-linked +P42838 YNL323W LEM3 298 N-linked +P42838 YNL323W LEM3 332 N-linked +Q12265 YOL061W PRS5 119 Phosphotyrosine +Q12265 YOL061W PRS5 120 Phosphothreonine +Q12265 YOL061W PRS5 123 Phosphoserine +Q12265 YOL061W PRS5 127 Phosphothreonine +Q12265 YOL061W PRS5 183 Phosphoserine +Q12265 YOL061W PRS5 332 Phosphoserine +P27810 YOR099W KTR1 120 N-linked +Q92325 YOL025W LAG2 16 Glycyl +Q12446 YOR181W LAS17 334 Phosphothreonine +Q12446 YOR181W LAS17 337 Phosphoserine +Q12446 YOR181W LAS17 588 Phosphoserine +P07264 YGL009C LEU1 488 Phosphoserine +P07264 YGL009C LEU1 494 Phosphothreonine +P07264 YGL009C LEU1 495 Phosphoserine +P53966 YNL029C KTR5 86 N-linked +P32807 YMR284W YKU70 370 Phosphoserine +P32807 YMR284W YKU70 371 Phosphoserine +P32807 YMR284W YKU70 372 Phosphoserine +P25045 YMR296C LCB1 121 Phosphothreonine +Q06147 YLR260W LCB5 91 S-palmitoyl +Q06147 YLR260W LCB5 94 S-palmitoyl +P36016 YKL073W LHS1 128 N-linked +P36016 YKL073W LHS1 458 N-linked +P36016 YKL073W LHS1 474 N-linked +P36016 YKL073W LHS1 481 N-linked +P36016 YKL073W LHS1 489 N-linked +P36016 YKL073W LHS1 527 N-linked +P36016 YKL073W LHS1 844 N-linked +P40026 YER038C KRE29 81 Phosphoserine +P40026 YER038C KRE29 101 Phosphoserine +P27809 YDR483W KRE2 197 N-linked +P30624 YOR317W FAA1 189 Glycyl +P32486 YPR159W KRE6 81 Phosphoserine +P32486 YPR159W KRE6 116 Phosphoserine +P32486 YPR159W KRE6 133 Phosphoserine +P32486 YPR159W KRE6 134 Phosphoserine +P32486 YPR159W KRE6 136 Phosphoserine +P32486 YPR159W KRE6 139 Phosphoserine +P32486 YPR159W KRE6 374 N-linked +P32486 YPR159W KRE6 461 N-linked +P32486 YPR159W KRE6 538 N-linked +P32486 YPR159W KRE6 563 N-linked +P32486 YPR159W KRE6 691 N-linked +P33399 YDL051W LHP1 2 N-acetylserine +P33399 YDL051W LHP1 15 Phosphoserine +P33399 YDL051W LHP1 19 Phosphoserine +P33399 YDL051W LHP1 104 Omega-N-methylarginine +P33399 YDL051W LHP1 230 Phosphoserine +P33399 YDL051W LHP1 233 Phosphoserine +P33399 YDL051W LHP1 235 Phosphoserine +Q05979 YLR231C BNA5 252 N6-(pyridoxal +P28496 YKL008C LAC1 2 N-acetylserine +P28496 YKL008C LAC1 23 Phosphoserine +P28496 YKL008C LAC1 24 Phosphoserine +P28496 YKL008C LAC1 103 N-linked +P38703 YHL003C LAG1 23 Phosphoserine +P38703 YHL003C LAG1 24 Phosphoserine +P38703 YHL003C LAG1 103 N-linked +P38851 YHR155W LAM1 1205 N-linked +Q08001 YLR072W LAM6 343 Phosphothreonine +Q08001 YLR072W LAM6 591 Phosphoserine +Q08001 YLR072W LAM6 593 Phosphothreonine +Q08001 YLR072W LAM6 594 Phosphoserine +Q08001 YLR072W LAM6 597 Phosphoserine +Q04377 YDR499W LCD1 10 Phosphoserine +Q04377 YDR499W LCD1 11 Phosphoserine +Q04377 YDR499W LCD1 76 Phosphoserine +Q02786 YPL056C LCL1 81 GPI-anchor +P38439 YOR123C LEO1 105 Phosphoserine +P38439 YOR123C LEO1 132 Phosphoserine +P38439 YOR123C LEO1 188 Phosphoserine +P38439 YOR123C LEO1 358 Phosphoserine +P38439 YOR123C LEO1 372 Phosphoserine +Q12342 YDL146W LDB17 7 Phosphoserine +Q12342 YDL146W LDB17 463 Phosphoserine +Q12342 YDL146W LDB17 466 Phosphoserine +P47055 YJL038C LOH1 42 N-linked +P47055 YJL038C LOH1 62 N-linked +P47055 YJL038C LOH1 136 N-linked +P25579 YCL051W LRE1 393 Phosphoserine +P25579 YCL051W LRE1 398 Phosphoserine +P25579 YCL051W LRE1 516 Phosphoserine +P25579 YCL051W LRE1 552 Phosphoserine +P43586 YFR001W LOC1 24 Phosphoserine +P35688 YDL240W LRG1 1 N-acetylmethionine +P35688 YDL240W LRG1 562 Phosphoserine +P40495 YIL094C LYS12 98 Phosphoserine +Q04087 YDR439W LRS4 168 Phosphoserine +Q04087 YDR439W LRS4 230 Phosphoserine +P43603 YFR024C-A LSB3 227 Phosphoserine +P43603 YFR024C-A LSB3 298 Phosphothreonine +P43603 YFR024C-A LSB3 300 Phosphoserine +P43603 YFR024C-A LSB3 303 Phosphoserine +P43603 YFR024C-A LSB3 393 Phosphothreonine +P43603 YFR024C-A LSB3 397 Phosphoserine +P43603 YFR024C-A LSB3 402 Phosphoserine +P43603 YFR024C-A LSB3 416 Phosphoserine +Q12230 YPL004C LSP1 233 Phosphothreonine +P22134 YER142C MAG1 110 Phosphoserine +Q12176 YDR060W MAK21 2 N-acetylserine +Q12176 YDR060W MAK21 62 Phosphoserine +Q12176 YDR060W MAK21 73 Phosphoserine +Q12176 YDR060W MAK21 80 Phosphoserine +Q12176 YDR060W MAK21 275 Phosphoserine +Q12176 YDR060W MAK21 708 Phosphotyrosine +Q12176 YDR060W MAK21 710 Phosphoserine +Q12176 YDR060W MAK21 874 Phosphoserine +Q12176 YDR060W MAK21 878 Phosphoserine +Q12176 YDR060W MAK21 977 Phosphoserine +Q12176 YDR060W MAK21 978 Phosphoserine +Q12176 YDR060W MAK21 1024 Phosphoserine +Q12246 YOR171C LCB4 111 Phosphoserine +Q12246 YOR171C LCB4 120 Phosphoserine +Q12246 YOR171C LCB4 154 Phosphoserine +Q12246 YOR171C LCB4 160 Phosphoserine +Q12246 YOR171C LCB4 451 Phosphoserine%3B +Q12246 YOR171C LCB4 454 Phosphoserine +Q12246 YOR171C LCB4 455 Phosphoserine%3B +Q12246 YOR171C LCB4 460 Phosphoserine +Q12246 YOR171C LCB4 43 S-palmitoyl +Q12246 YOR171C LCB4 46 S-palmitoyl +Q12246 YOR171C LCB4 148 Glycyl +Q12502 YOR322C LDB19 93 Phosphothreonine +Q12502 YOR322C LDB19 384 Phosphoserine +Q12502 YOR322C LDB19 619 Phosphothreonine +Q12502 YOR322C LDB19 808 Phosphoserine +Q12502 YOR322C LDB19 486 Glycyl +Q02783 YPL060W MFM1 202 N-linked +P32487 YNL268W LYP1 64 Phosphoserine +P32487 YNL268W LYP1 75 Phosphoserine +P32487 YNL268W LYP1 77 Phosphothreonine +P32487 YNL268W LYP1 79 Phosphoserine +P32487 YNL268W LYP1 87 Phosphoserine +P32487 YNL268W LYP1 90 Phosphothreonine +P32487 YNL268W LYP1 54 Glycyl +P38828 YHR121W LSM12 2 N-acetylserine +P53048 YGR289C MAL11 523 N-linked +Q01662 YLR244C MAP1 2 N-acetylserine +P38174 YBL091C MAP2 35 Phosphoserine +P34239 YKL176C LST4 401 Phosphoserine +P07866 YAL024C LTE1 271 Phosphoserine +P07866 YAL024C LTE1 559 Phosphoserine +P07866 YAL024C LTE1 689 Phosphoserine +P07866 YAL024C LTE1 691 Phosphothreonine +P07866 YAL024C LTE1 808 Phosphoserine +P07866 YAL024C LTE1 810 Phosphoserine +P07866 YAL024C LTE1 1028 Phosphoserine +P07866 YAL024C LTE1 1109 Phosphoserine +Q07508 YDL087C LUC7 2 N-acetylserine +P35192 YMR021C MAC1 143 Phosphoserine +P47074 YJL013C MAD3 268 Phosphoserine +P41910 YDR005C MAF1 90 Phosphoserine +P41910 YDR005C MAF1 209 Phosphoserine +P41910 YDR005C MAF1 210 Phosphoserine +P41910 YDR005C MAF1 347 Phosphothreonine +Q07376 YDL054C MCH1 255 Phosphoserine +Q07376 YDL054C MCH1 60 N-linked +Q07376 YDL054C MCH1 131 N-linked +Q07376 YDL054C MCH1 194 N-linked +P36032 YKL221W MCH2 72 N-linked +Q08777 YOR306C MCH5 125 N-linked +Q08777 YOR306C MCH5 194 N-linked +Q08777 YOR306C MCH5 419 N-linked +Q06675 YDR318W MCM21 88 Phosphothreonine +P11746 YMR043W MCM1 2 N-acetylserine +P11746 YMR043W MCM1 2 Phosphoserine +P11746 YMR043W MCM1 144 Phosphoserine +P17505 YKL085W MDH1 177 Phosphoserine +P17505 YKL085W MDH1 199 Phosphothreonine +P53145 YGL099W LSG1 103 Phosphoserine +P34078 YKL143W LTV1 2 N-acetylserine +P34078 YKL143W LTV1 288 Phosphoserine +P34078 YKL143W LTV1 293 Phosphoserine +P34078 YKL143W LTV1 299 Phosphoserine +P34078 YKL143W LTV1 303 Phosphoserine +P40957 YGL086W MAD1 502 Phosphothreonine +P20484 YKL021C MAK11 2 N-acetylserine +P20484 YKL021C MAK11 376 Phosphoserine +P20484 YKL021C MAK11 380 Phosphoserine +P20484 YKL021C MAK11 382 Phosphothreonine +P38112 YBR142W MAK5 135 Phosphothreonine +P38112 YBR142W MAK5 138 Phosphoserine +P38112 YBR142W MAK5 678 Phosphoserine +P36007 YKL218C SRY1 53 N6-(pyridoxal +P22855 YGL156W AMS1 2 N-acetylserine +Q92328 YOL009C MDM12 49 Glycyl +P38295 YBR177C EHT1 114 Glycyl +P29469 YBL023C MCM2 14 Phosphoserine +P29469 YBL023C MCM2 16 Phosphoserine +P29469 YBL023C MCM2 23 Phosphoserine +P29469 YBL023C MCM2 164 Phosphoserine +P29469 YBL023C MCM2 170 Phosphoserine +P30665 YPR019W MCM4 52 Phosphoserine +P30665 YPR019W MCM4 56 Phosphoserine +P30665 YPR019W MCM4 69 Phosphoserine +P53091 YGL201C MCM6 78 Phosphoserine +P53091 YGL201C MCM6 249 Phosphoserine +P53091 YGL201C MCM6 372 Phosphoserine +P53091 YGL201C MCM6 766 Phosphothreonine +P38132 YBR202W MCM7 811 Phosphothreonine +P38132 YBR202W MCM7 819 Phosphoserine +P38132 YBR202W MCM7 838 Phosphoserine +Q99257 YPL169C MEX67 2 N-acetylserine +P34166 YNL145W MFA2 35 Cysteine +P34166 YNL145W MFA2 35 S-farnesyl +P40578 YIR033W MGA2 255 Phosphoserine +P40578 YIR033W MGA2 467 Phosphoserine +P43638 YJL042W MHP1 1 N-acetylmethionine +P43638 YJL042W MHP1 81 Phosphoserine +P43638 YJL042W MHP1 222 Phosphothreonine +P43638 YJL042W MHP1 309 Phosphoserine +P43638 YJL042W MHP1 311 Phosphoserine +P43638 YJL042W MHP1 354 Phosphoserine +P43638 YJL042W MHP1 357 Phosphoserine +P43638 YJL042W MHP1 577 Phosphothreonine +P43638 YJL042W MHP1 221 Glycyl +Q12019 YLR106C MDN1 1026 Phosphothreonine +Q12019 YLR106C MDN1 2971 Phosphoserine +Q12019 YLR106C MDN1 4353 Phosphoserine +Q12019 YLR106C MDN1 4388 Phosphothreonine +Q12019 YLR106C MDN1 4555 Phosphoserine +P34165 YDR461W MFA1 33 Cysteine +P34165 YDR461W MFA1 33 S-farnesyl +P40002 YEL007W MIT1 152 Phosphoserine +P32490 YOR231W MKK1 192 Phosphoserine +P53141 YGL106W MLC1 116 Glycyl +P38998 YIR034C LYS1 2 N-acetylalanine%3B +P07702 YBR115C LYS2 880 O-(pantetheine +P07702 YBR115C LYS2 541 Glycyl +P07702 YBR115C LYS2 1276 Glycyl +O14467 YOR298C-A MBF1 143 Phosphoserine +P19659 YOL051W GAL11 2 N-acetylserine +P19659 YOL051W GAL11 335 Phosphoserine +P19659 YOL051W GAL11 736 Phosphoserine +P19659 YOL051W GAL11 752 Phosphoserine +P19659 YOL051W GAL11 783 Phosphoserine +P19659 YOL051W GAL11 785 Phosphoserine +P19659 YOL051W GAL11 789 Phosphoserine +P19659 YOL051W GAL11 793 Phosphothreonine +P19659 YOL051W GAL11 831 Phosphoserine +P19659 YOL051W GAL11 1003 Phosphoserine +P19659 YOL051W GAL11 1008 Phosphoserine +P19659 YOL051W GAL11 1018 Phosphoserine +P19659 YOL051W GAL11 1034 Phosphoserine +Q02205 YKR007W MEH1 146 Phosphoserine +Q02205 YKR007W MEH1 149 Phosphoserine +Q02205 YKR007W MEH1 2 N-myristoyl +Q02205 YKR007W MEH1 7 S-palmitoyl +Q02205 YKR007W MEH1 8 S-palmitoyl +P33441 YML062C MFT1 266 Phosphoserine +P35201 YKL089W MIF2 325 Phosphoserine +P27705 YGL035C MIG1 278 Phosphoserine +P27705 YGL035C MIG1 302 Phosphoserine +P27705 YGL035C MIG1 310 Phosphoserine +P27705 YGL035C MIG1 311 Phosphoserine +P27705 YGL035C MIG1 314 Phosphoserine +P27705 YGL035C MIG1 377 Phosphoserine +Q06820 YPR083W MDM36 42 Phosphoserine +Q02574 YLR288C MEC3 452 Phosphoserine +Q12321 YPR070W MED1 155 Phosphoserine +Q12321 YPR070W MED1 423 Phosphoserine +P32570 YBR253W SRB6 2 N-acetylserine +P43623 YFR055W IRC7 208 N6-(pyridoxal +P36027 YLR332W MID2 260 Phosphoserine +P36027 YLR332W MID2 327 Phosphoserine +P36027 YLR332W MID2 329 Phosphoserine +P36027 YLR332W MID2 355 Phosphoserine +P36027 YLR332W MID2 35 N-linked +P36027 YLR332W MID2 211 N-linked +Q02455 YKR095W MLP1 2 N-acetylserine +Q02455 YKR095W MLP1 337 Phosphothreonine +Q02455 YKR095W MLP1 379 Phosphoserine +Q02455 YKR095W MLP1 1670 Phosphoserine +Q02455 YKR095W MLP1 1710 Phosphoserine +Q02455 YKR095W MLP1 1733 Phosphoserine +Q02455 YKR095W MLP1 1803 Phosphoserine +P32354 YIL150C MCM10 17 Phosphothreonine +P32354 YIL150C MCM10 18 Phosphoserine +P32354 YIL150C MCM10 453 Phosphoserine +P32354 YIL150C MCM10 454 Phosphoserine +P22133 YOL126C MDH2 6 Phosphothreonine +P53094 YGL197W MDS3 472 Phosphoserine +P53094 YGL197W MDS3 475 Phosphoserine +P53094 YGL197W MDS3 621 Phosphoserine +P53094 YGL197W MDS3 639 Phosphoserine +P53094 YGL197W MDS3 693 Phosphoserine +P53094 YGL197W MDS3 698 Phosphoserine +P53094 YGL197W MDS3 744 Phosphoserine +P53094 YGL197W MDS3 747 Phosphoserine +P53094 YGL197W MDS3 756 Phosphoserine +P53094 YGL197W MDS3 757 Phosphoserine +P53094 YGL197W MDS3 781 Phosphoserine +P53094 YGL197W MDS3 785 Phosphothreonine +P53094 YGL197W MDS3 787 Phosphoserine +P53094 YGL197W MDS3 900 Phosphoserine +P53094 YGL197W MDS3 904 Phosphoserine +P53094 YGL197W MDS3 930 Phosphothreonine +P53094 YGL197W MDS3 1187 Phosphoserine +P47025 YJL112W MDV1 376 Phosphoserine +P19263 YLR071C RGR1 2 N-acetylthreonine +P19263 YLR071C RGR1 7 Phosphoserine +P19263 YLR071C RGR1 1036 Phosphothreonine +P39014 YIL046W MET30 67 Phosphoserine +P47164 YJR130C STR2 443 N6-(pyridoxal +P19358 YDR502C SAM2 2 N-acetylserine +P36051 YKL165C MCD4 90 N-linked +P36051 YKL165C MCD4 138 N-linked +P36051 YKL165C MCD4 198 N-linked +P36051 YKL165C MCD4 202 N-linked +P36051 YKL165C MCD4 286 N-linked +P36051 YKL165C MCD4 312 N-linked +P21965 YNL307C MCK1 2 N-acetylserine +P21965 YNL307C MCK1 198 Phosphoserine +P21965 YNL307C MCK1 199 Phosphotyrosine +P21965 YNL307C MCK1 202 Phosphoserine +P24279 YEL032W MCM3 761 Phosphoserine +P24279 YEL032W MCM3 777 Phosphoserine +P24279 YEL032W MCM3 781 Phosphoserine +P24279 YEL032W MCM3 868 Phosphothreonine +Q12343 YOR174W MED4 2 N-acetylserine +Q12343 YOR174W MED4 237 Phosphothreonine%3B +Q12343 YOR174W MED4 242 Phosphoserine +P40513 YIL070C MAM33 91 Phosphothreonine +Q12296 YOL060C MAM3 439 Phosphoserine +Q12296 YOL060C MAM3 447 Phosphoserine +Q12296 YOL060C MAM3 527 Phosphoserine +Q12296 YOL060C MAM3 603 Phosphoserine +Q12296 YOL060C MAM3 604 Phosphotyrosine +Q12296 YOL060C MAM3 607 Phosphothreonine +Q12296 YOL060C MAM3 614 Phosphoserine +P39678 YDL056W MBP1 110 Phosphoserine +P39678 YDL056W MBP1 325 Phosphothreonine +P39678 YDL056W MBP1 326 Phosphoserine +P39678 YDL056W MBP1 330 Phosphoserine +P39678 YDL056W MBP1 827 Phosphoserine +P23493 YKL093W MBR1 159 Phosphothreonine +P23493 YKL093W MBR1 177 Phosphoserine +P23493 YKL093W MBR1 224 Phosphoserine +P23493 YKL093W MBR1 227 Phosphoserine +P36060 YKL150W MCR1 278 Phosphoserine +P53885 YNL173C MDG1 160 Phosphoserine +P53885 YNL173C MDG1 216 Phosphothreonine +P53885 YNL173C MDG1 288 Phosphoserine +P53885 YNL173C MDG1 314 Glycyl +Q12124 YDL005C MED2 6 Phosphoserine +Q12124 YDL005C MED2 208 Phosphoserine%3B +P40260 YGR121C MEP1 442 Phosphoserine +P40260 YGR121C MEP1 445 Phosphoserine +P32389 YNL103W MET4 416 Phosphoserine +P32389 YNL103W MET4 564 Phosphoserine +Q08268 YOL119C MCH4 131 N-linked +Q08268 YOL119C MCH4 54 Glycyl +Q01846 YML104C MDM1 670 Phosphoserine +Q01846 YML104C MDM1 673 Phosphoserine +Q01846 YML104C MDM1 692 Phosphoserine +P40356 YGL025C PGD1 1 N-acetylmethionine +P38782 YHR058C MED6 225 Phosphoserine +P41948 YNL142W MEP2 4 N-linked +P38849 YHR151C MTC6 32 N-linked +P38849 YHR151C MTC6 60 N-linked +P38849 YHR151C MTC6 80 N-linked +P38849 YHR151C MTC6 89 N-linked +P38849 YHR151C MTC6 156 N-linked +P38849 YHR151C MTC6 171 N-linked +P38849 YHR151C MTC6 175 N-linked +P38849 YHR151C MTC6 202 N-linked +P38849 YHR151C MTC6 240 N-linked +P38849 YHR151C MTC6 259 N-linked +P38849 YHR151C MTC6 311 N-linked +P38849 YHR151C MTC6 362 N-linked +P38849 YHR151C MTC6 433 N-linked +P0CX81 YHR055C CUP1-2 30 Glycyl +P36006 YKL129C MYO3 357 Phosphoserine +P47018 YJL123C MTC1 273 Phosphoserine +P47018 YJL123C MTC1 436 Phosphoserine +P53176 YGL051W MST27 3 Phosphothreonine +P36084 YKL074C MUD2 49 Phosphoserine +P39552 YAR033W MST28 3 Phosphothreonine +P0CY08 YCR039C MATALPHA2 1 N-acetylmethionine +P38335 YBR255W MTC4 85 Phosphoserine +P38335 YBR255W MTC4 263 Phosphothreonine +P38335 YBR255W MTC4 481 Phosphoserine +P38335 YBR255W MTC4 491 Phosphoserine +P38335 YBR255W MTC4 493 Phosphotyrosine +P46151 YPL023C MET12 120 Phosphoserine +P46151 YPL023C MET12 301 Phosphoserine +P46151 YPL023C MET12 358 Phosphoserine +Q06489 YPR118W MRI1 2 N-acetylserine +Q06489 YPR118W MRI1 351 Phosphoserine +Q06106 YPR112C MRD1 220 Phosphoserine +Q06106 YPR112C MRD1 264 Phosphoserine +Q12117 YDR033W MRH1 289 Phosphoserine +Q12117 YDR033W MRH1 295 Phosphothreonine +Q12117 YDR033W MRH1 299 Phosphoserine +P50873 YDL079C MRK1 13 Phosphoserine +P35719 YKL142W MRP8 23 Phosphoserine +P35719 YKL142W MRP8 137 Glycyl +P50276 YGR055W MUP1 552 Phosphothreonine +P50276 YGR055W MUP1 573 Phosphoserine +P50276 YGR055W MUP1 28 Glycyl +P38994 YDR208W MSS4 207 Phosphoserine +P38994 YDR208W MSS4 222 Phosphothreonine +P38994 YDR208W MSS4 225 Phosphoserine +P38994 YDR208W MSS4 659 Phosphothreonine +P38994 YDR208W MSS4 661 Phosphoserine +Q02642 YPL037C EGD1 151 Phosphothreonine +P25588 YCL061C MRC1 144 Phosphoserine +P25588 YCL061C MRC1 409 Phosphoserine +P25588 YCL061C MRC1 411 Phosphoserine +P25588 YCL061C MRC1 434 Phosphoserine +P25588 YCL061C MRC1 605 Phosphoserine +P25588 YCL061C MRC1 607 Phosphoserine +P25588 YCL061C MRC1 609 Phosphothreonine +P25588 YCL061C MRC1 801 Phosphoserine +P25588 YCL061C MRC1 807 Phosphoserine +P25588 YCL061C MRC1 911 Phosphoserine +Q06815 YPR079W MRL1 335 Phosphoserine +Q06815 YPR079W MRL1 339 Phosphoserine +Q06815 YPR079W MRL1 342 Phosphoserine +Q06815 YPR079W MRL1 371 Phosphoserine +Q06815 YPR079W MRL1 380 Phosphoserine +Q06815 YPR079W MRL1 116 N-linked +Q06815 YPR079W MRL1 136 N-linked +Q06815 YPR079W MRL1 178 N-linked +Q06815 YPR079W MRL1 215 N-linked +P36157 YKR077W MSA2 157 Phosphoserine +P36157 YKR077W MSA2 292 Phosphoserine +P32334 YGR014W MSB2 1300 Phosphoserine +P32334 YGR014W MSB2 30 N-linked +P32334 YGR014W MSB2 859 N-linked +P32334 YGR014W MSB2 885 N-linked +P32334 YGR014W MSB2 945 N-linked +P32334 YGR014W MSB2 1049 N-linked +P32334 YGR014W MSB2 1088 N-linked +P32334 YGR014W MSB2 1175 N-linked +P38694 YHR039C MSC7 15 N-linked +P38694 YHR039C MSC7 565 N-linked +P38694 YHR039C MSC7 627 N-linked +P34232 YKL186C MTR2 125 Phosphothreonine +P48563 YNL297C MON2 2 N-acetylalanine +P48563 YNL297C MON2 564 Phosphoserine +P48563 YNL297C MON2 567 Phosphoserine +P48563 YNL297C MON2 571 Phosphoserine +Q05812 YLR219W MSC3 57 Phosphoserine +Q05812 YLR219W MSC3 64 Phosphoserine +Q05812 YLR219W MSC3 127 Phosphoserine +Q05812 YLR219W MSC3 151 Phosphoserine +Q05812 YLR219W MSC3 155 Phosphoserine +Q05812 YLR219W MSC3 363 Phosphoserine +Q05812 YLR219W MSC3 646 Phosphothreonine +Q05812 YLR219W MSC3 660 Phosphoserine +P53214 YGR023W MTL1 481 Phosphoserine +P53214 YGR023W MTL1 482 Phosphoserine +P29952 YER003C PMI40 2 N-acetylserine +P29952 YER003C PMI40 107 Phosphoserine +P10507 YLR163C MAS1 243 Phosphoserine +P21339 YOR188W MSB1 538 Phosphoserine +P21339 YOR188W MSB1 776 Phosphoserine +P21339 YOR188W MSB1 816 Phosphoserine +Q03104 YML128C MSC1 237 Phosphothreonine +Q03104 YML128C MSC1 243 Phosphoserine +P38590 YNL053W MSG5 22 Phosphoserine +P38590 YNL053W MSG5 98 Phosphoserine +P38590 YNL053W MSG5 151 Phosphoserine +P38590 YNL053W MSG5 178 Phosphothreonine +Q03834 YDR097C MSH6 102 Phosphoserine +Q03834 YDR097C MSH6 145 Phosphoserine +Q03834 YDR097C MSH6 150 Phosphoserine +Q03834 YDR097C MSH6 201 Phosphoserine +Q03834 YDR097C MSH6 451 Phosphothreonine +P33749 YKL062W MSN4 1 N-acetylmethionine +P33749 YKL062W MSN4 178 Phosphoserine +P33749 YKL062W MSN4 263 Phosphoserine +P33749 YKL062W MSN4 316 Phosphoserine +P33749 YKL062W MSN4 319 Phosphoserine +P33749 YKL062W MSN4 479 Phosphothreonine +P33749 YKL062W MSN4 558 Phosphoserine +P47047 YJL050W MTR4 34 Phosphothreonine +P47047 YJL050W MTR4 84 Phosphoserine +P47047 YJL050W MTR4 843 Phosphoserine +Q08750 YOR298W MUM3 285 N-linked +P19524 YOR326W MYO2 2 N-acetylserine +P19524 YOR326W MYO2 1097 Phosphothreonine +P19524 YOR326W MYO2 1121 Phosphoserine +P16603 YHR042W NCP1 666 Glycyl +Q06389 YDR373W FRQ1 2 N-myristoyl +P0CX80 YHR053C CUP1-1 30 Glycyl +Q04439 YMR109W MYO5 357 Phosphoserine +Q04439 YMR109W MYO5 359 Phosphotyrosine +Q04439 YMR109W MYO5 777 Phosphoserine +Q04439 YMR109W MYO5 992 Phosphoserine +Q04439 YMR109W MYO5 1205 Phosphoserine +Q12387 YOL076W MDM20 2 N-acetylserine +P12945 YDL040C NAT1 2 N-acetylserine +P12945 YDL040C NAT1 674 Phosphoserine +P52919 YLR457C NBP1 251 Phosphoserine +P52919 YLR457C NBP1 260 Phosphoserine +Q12163 YDR162C NBP2 102 Phosphoserine +Q12163 YDR162C NBP2 196 Phosphoserine +Q12163 YDR162C NBP2 235 Phosphoserine +Q12374 YPR155C NCA2 29 Phosphoserine +Q02866 YPL070W MUK1 67 Phosphoserine +Q02866 YPL070W MUK1 163 Phosphoserine +Q02866 YPL070W MUK1 185 Phosphoserine +Q02866 YPL070W MUK1 245 Phosphoserine +P25293 YKR048C NAP1 20 Phosphothreonine +P25293 YKR048C NAP1 24 Phosphothreonine +P25293 YKR048C NAP1 27 Phosphoserine +P25293 YKR048C NAP1 53 Phosphothreonine +P25293 YKR048C NAP1 69 Phosphoserine +P25293 YKR048C NAP1 76 Phosphoserine +P25293 YKR048C NAP1 82 Phosphoserine +P25293 YKR048C NAP1 98 Phosphoserine +P25293 YKR048C NAP1 104 Phosphoserine +P25293 YKR048C NAP1 140 Phosphoserine +P25293 YKR048C NAP1 159 Phosphoserine%3B +P25293 YKR048C NAP1 177 Phosphoserine%3B +P25293 YKR048C NAP1 397 Phosphoserine%3B +P25293 YKR048C NAP1 50 Glycyl +P42939 YGR206W MVB12 1 N-acetylmethionine +P42939 YGR206W MVB12 94 Phosphoserine +Q03735 YML117W NAB6 2 N-acetylserine +Q03735 YML117W NAB6 464 Phosphoserine +Q03735 YML117W NAB6 467 Phosphoserine +P53919 YNL124W NAF1 255 Phosphoserine +P30771 YMR080C NAM7 56 Phosphoserine +P30771 YMR080C NAM7 869 Phosphoserine +Q08229 YOL070C NBA1 138 Phosphoserine +Q08229 YOL070C NBA1 208 Phosphoserine +Q08229 YOL070C NBA1 403 Phosphothreonine +P38205 YBL024W NCL1 426 Phosphothreonine +P38205 YBL024W NCL1 431 Phosphoserine +P38205 YBL024W NCL1 667 Phosphoserine +P38996 YPL190C NAB3 86 Phosphothreonine +P38996 YPL190C NAB3 451 Phosphothreonine +P38879 YHR193C EGD2 2 N-acetylserine +P38879 YHR193C EGD2 93 Phosphoserine +Q08887 YOR372C NDD1 319 Phosphothreonine%3B +P36010 YKL067W YNK1 95 Phosphothreonine +P25374 YCL017C NFS1 299 N6-(pyridoxal +Q99271 YLR138W NHA1 568 Phosphoserine +Q99271 YLR138W NHA1 765 Phosphothreonine +Q99271 YLR138W NHA1 768 Phosphoserine +Q99271 YLR138W NHA1 774 Phosphoserine +P53914 YNL132W KRE33 1001 Phosphoserine +P53914 YNL132W KRE33 1007 Phosphoserine +P53914 YNL132W KRE33 1010 Phosphoserine +P40096 YER159C BUR6 27 Phosphoserine +P40096 YER159C BUR6 141 Phosphoserine +P32500 YML031W NDC1 401 Phosphoserine +P32500 YML031W NDC1 412 Phosphoserine +P40460 YIL144W NDC80 38 Phosphothreonine +P40460 YIL144W NDC80 248 Phosphothreonine +P32831 YBR212W NGR1 1 N-acetylmethionine +P32831 YBR212W NGR1 524 Phosphoserine +P39744 YOR206W NOC2 70 Phosphoserine +P39744 YOR206W NOC2 149 Phosphoserine +P39744 YOR206W NOC2 160 Phosphoserine +P39744 YOR206W NOC2 166 Phosphoserine +P39744 YOR206W NOC2 698 Phosphoserine +P39744 YOR206W NOC2 708 Phosphoserine +P25353 YCR026C NPP1 161 N-linked +P25353 YCR026C NPP1 204 N-linked +P25353 YCR026C NPP1 264 N-linked +P25353 YCR026C NPP1 296 N-linked +P25353 YCR026C NPP1 403 N-linked +P53718 YNR009W NRM1 145 Phosphoserine +Q08485 YOR071C NRT1 560 Phosphoserine +Q08485 YOR071C NRT1 572 Phosphoserine +P53898 YNL156C NSG2 90 Phosphoserine +Q12457 YDR026C NSI1 64 Phosphothreonine +P48234 YGR145W ENP2 529 Phosphoserine +P48234 YGR145W ENP2 550 Phosphoserine +P48234 YGR145W ENP2 555 Phosphoserine +Q07623 YDL213C NOP6 45 Phosphoserine +Q07623 YDL213C NOP6 160 Phosphoserine +P27476 YGR159C NSR1 353 Asymmetric +P27476 YGR159C NSR1 362 Asymmetric +P27476 YGR159C NSR1 366 Asymmetric +P27476 YGR159C NSR1 375 Asymmetric +P27476 YGR159C NSR1 379 Asymmetric +P27476 YGR159C NSR1 382 Asymmetric +Q08214 YOL043C NTG2 194 Glycyl +Q03210 YML118W NGL3 62 Phosphoserine +Q04121 YDR456W NHX1 490 Phosphothreonine +Q04121 YDR456W NHX1 494 Phosphoserine +Q04121 YDR456W NHX1 498 Phosphothreonine +Q04121 YDR456W NHX1 499 Phosphoserine +Q04121 YDR456W NHX1 569 Phosphoserine +Q04121 YDR456W NHX1 420 N-linked +Q04121 YDR456W NHX1 515 N-linked +Q04121 YDR456W NHX1 550 N-linked +Q04121 YDR456W NHX1 563 N-linked +P32770 YDL167C NRP1 345 Phosphoserine +P32770 YDL167C NRP1 455 Phosphoserine +P32770 YDL167C NRP1 630 Phosphoserine +P37838 YPL043W NOP4 247 Phosphoserine +P37838 YPL043W NOP4 379 Phosphothreonine +Q12080 YPL146C NOP53 31 Phosphoserine +P22211 YNL183C NPR1 47 Phosphoserine%3B +P22211 YNL183C NPR1 85 Phosphoserine +P22211 YNL183C NPR1 90 Phosphoserine +P22211 YNL183C NPR1 100 Phosphoserine +P22211 YNL183C NPR1 111 Phosphoserine +P22211 YNL183C NPR1 116 Phosphoserine +P22211 YNL183C NPR1 125 Phosphoserine +P22211 YNL183C NPR1 137 Phosphoserine +P22211 YNL183C NPR1 141 Phosphoserine +P22211 YNL183C NPR1 257 Phosphoserine%3B +P22211 YNL183C NPR1 259 Phosphoserine +P22211 YNL183C NPR1 260 Phosphoserine +P22211 YNL183C NPR1 288 Phosphoserine +P22211 YNL183C NPR1 292 Phosphoserine +P22211 YNL183C NPR1 317 Phosphoserine +P22211 YNL183C NPR1 320 Phosphoserine +P22211 YNL183C NPR1 328 Phosphoserine +P22211 YNL183C NPR1 334 Phosphotyrosine +P22211 YNL183C NPR1 336 Phosphoserine +P22211 YNL183C NPR1 353 Phosphoserine +P22211 YNL183C NPR1 356 Phosphoserine +P22211 YNL183C NPR1 357 Phosphoserine%3B +P22211 YNL183C NPR1 385 Phosphoserine +P53935 YNL091W NST1 266 Phosphoserine +Q12311 YPR031W NTO1 728 Phosphoserine +Q02629 YKL068W NUP100 763 Phosphoserine +Q02629 YKL068W NUP100 783 Phosphoserine +Q92317 YDR397C NCB2 135 Phosphoserine +Q92317 YDR397C NCB2 137 Phosphoserine +Q92317 YDR397C NCB2 142 Phosphoserine +P49954 YLR351C NIT3 34 Phosphothreonine +Q06178 YLR328W NMA1 91 Phosphoserine +Q06178 YLR328W NMA1 95 Phosphoserine +Q06178 YLR328W NMA1 96 Phosphoserine +Q06178 YLR328W NMA1 111 Phosphoserine +P46970 YJR132W NMD5 977 Phosphoserine +P53939 YNL078W NIS1 260 Phosphoserine +P53939 YNL078W NIS1 264 Phosphoserine +P53939 YNL078W NIS1 300 Phosphoserine +P53939 YNL078W NIS1 302 Phosphoserine +P34909 YER068W MOT2 310 Phosphothreonine +P34909 YER068W MOT2 312 Phosphoserine +P34909 YER068W MOT2 326 Phosphothreonine +P34909 YER068W MOT2 360 Phosphoserine +P34909 YER068W MOT2 270 Glycyl +P32494 YDR176W NGG1 134 Phosphoserine +P32494 YDR176W NGG1 407 Phosphoserine +P32494 YDR176W NGG1 464 Phosphothreonine +Q6Q547 YHR072W-A NOP10 36 Phosphoserine +Q6Q547 YHR072W-A NOP10 28 Glycyl +Q01560 YDR432W NPL3 182 Phosphoserine +Q01560 YDR432W NPL3 224 Phosphoserine +Q12499 YOR310C NOP58 281 Glycyl +P39923 YEL062W NPR2 362 Phosphoserine +Q08972 YPL226W NEW1 443 Phosphoserine +Q08972 YPL226W NEW1 1191 Phosphothreonine +P0CE68 YKR103W NFT1 4 N-linked +Q03435 YDL002C NHP10 2 N-acetylserine +P53253 YGR089W NNF2 10 Glycyl +Q08208 YOL041C NOP12 70 Phosphoserine +Q08208 YOL041C NOP12 181 Phosphothreonine +Q08208 YOL041C NOP12 184 Phosphoserine +Q12460 YLR197W NOP56 321 Phosphoserine +P47035 YJL076W NET1 60 Phosphoserine +P47035 YJL076W NET1 166 Phosphoserine +P47035 YJL076W NET1 231 Phosphoserine +P47035 YJL076W NET1 252 Phosphoserine +P47035 YJL076W NET1 437 Phosphoserine +P47035 YJL076W NET1 439 Phosphoserine +P47035 YJL076W NET1 447 Phosphoserine +P47035 YJL076W NET1 452 Phosphoserine +P47035 YJL076W NET1 497 Phosphoserine +P47035 YJL076W NET1 676 Phosphothreonine +P47035 YJL076W NET1 830 Phosphoserine +P47035 YJL076W NET1 1042 Phosphothreonine +P47035 YJL076W NET1 1056 Phosphoserine +P47035 YJL076W NET1 1059 Phosphoserine +Q07896 YLR002C NOC3 395 Phosphoserine +Q03790 YMR153W NUP53 2 N-acetylalanine +Q03790 YMR153W NUP53 101 Phosphoserine +Q03790 YMR153W NUP53 297 Phosphoserine +Q03790 YMR153W NUP53 438 Phosphoserine +Q12493 YDR383C NKP1 222 Phosphoserine +P36003 YKL171W NNK1 178 Phosphoserine +P36003 YKL171W NNK1 179 Phosphoserine +P36003 YKL171W NNK1 405 Phosphoserine +P36003 YKL171W NNK1 426 Phosphoserine +P36003 YKL171W NNK1 737 Phosphoserine +P36003 YKL171W NNK1 739 Phosphotyrosine +Q02892 YPL093W NOG1 563 Phosphoserine +Q12514 YPR072W NOT5 306 Phosphothreonine +Q12514 YPR072W NOT5 377 Phosphoserine +Q12514 YPR072W NOT5 338 Glycyl +P38742 YHL023C NPR3 76 Phosphoserine +P38742 YHL023C NPR3 486 Phosphoserine +P38742 YHL023C NPR3 987 Phosphoserine +P32499 YLR335W NUP2 17 Phosphoserine +P32499 YLR335W NUP2 20 Phosphoserine +P32499 YLR335W NUP2 137 Phosphoserine +P32499 YLR335W NUP2 165 Phosphoserine +P32499 YLR335W NUP2 203 Phosphoserine +P32499 YLR335W NUP2 205 Phosphoserine +P32499 YLR335W NUP2 348 Phosphoserine +P32499 YLR335W NUP2 351 Phosphoserine +P32499 YLR335W NUP2 361 Phosphothreonine +P32499 YLR335W NUP2 581 Phosphoserine +P32499 YLR335W NUP2 590 Phosphothreonine +P49686 YDR192C NUP42 137 Phosphoserine +P49686 YDR192C NUP42 298 Phosphoserine +Q05166 YDL088C ASM4 458 Phosphoserine +Q05166 YDL088C ASM4 464 Phosphoserine +Q12066 YDL089W NUR1 3 Phosphoserine +Q12066 YDL089W NUR1 417 Phosphoserine +Q12066 YDL089W NUR1 474 Phosphoserine +P39720 YAL051W OAF1 155 Phosphoserine +P53949 YNL056W OCA2 181 Phosphoserine +P38837 YHR133C NSG1 39 Phosphoserine +P38837 YHR133C NSG1 76 Phosphoserine +Q12143 YPL233W NSL1 2 N-acetylserine +P14907 YJL041W NSP1 238 Phosphoserine +P14907 YJL041W NSP1 361 Phosphoserine +P14907 YJL041W NSP1 456 Phosphoserine +P14907 YJL041W NSP1 631 Phosphoserine +P35729 YKL057C NUP120 417 Phosphothreonine +P40064 YER105C NUP157 1 N-acetylmethionine +P40064 YER105C NUP157 1034 Phosphoserine +P40477 YIL115C NUP159 404 Phosphoserine +P40477 YIL115C NUP159 657 Phosphoserine +P40477 YIL115C NUP159 724 Phosphoserine +P40477 YIL115C NUP159 735 Phosphoserine +P40477 YIL115C NUP159 745 Phosphoserine +P40477 YIL115C NUP159 803 Phosphothreonine +P40477 YIL115C NUP159 805 Phosphoserine +P40477 YIL115C NUP159 819 Phosphoserine +P40477 YIL115C NUP159 889 Phosphoserine +P40477 YIL115C NUP159 940 Phosphoserine +P40010 YER006W NUG1 337 Phosphoserine +Q00402 YDR150W NUM1 611 Phosphoserine +Q00402 YDR150W NUM1 675 Phosphoserine +Q00402 YDR150W NUM1 746 Phosphoserine +Q00402 YDR150W NUM1 881 Phosphoserine +Q00402 YDR150W NUM1 945 Phosphoserine +Q00402 YDR150W NUM1 1009 Phosphoserine +Q00402 YDR150W NUM1 1201 Phosphoserine +Q00402 YDR150W NUM1 1265 Phosphoserine +Q00402 YDR150W NUM1 1329 Phosphoserine +Q00402 YDR150W NUM1 2162 Phosphoserine +Q00402 YDR150W NUM1 2164 Phosphoserine +Q00402 YDR150W NUM1 2197 Phosphoserine +Q00402 YDR150W NUM1 2217 Phosphoserine +Q00402 YDR150W NUM1 2220 Phosphoserine +Q00402 YDR150W NUM1 2221 Phosphoserine +Q00402 YDR150W NUM1 2360 Phosphoserine +Q00402 YDR150W NUM1 2424 Phosphoserine +Q00402 YDR150W NUM1 2494 Phosphoserine +Q00402 YDR150W NUM1 2545 Phosphoserine +P39705 YAR002W NUP60 10 Phosphoserine +P39705 YAR002W NUP60 49 Phosphoserine +P39705 YAR002W NUP60 81 Phosphoserine +P39705 YAR002W NUP60 89 Phosphoserine +P39705 YAR002W NUP60 162 Phosphoserine +P39705 YAR002W NUP60 171 Phosphoserine +P39705 YAR002W NUP60 214 Phosphoserine +P39705 YAR002W NUP60 222 Phosphoserine +P39705 YAR002W NUP60 352 Phosphoserine +P39705 YAR002W NUP60 360 Phosphoserine +P39705 YAR002W NUP60 374 Phosphoserine +P39705 YAR002W NUP60 382 Phosphoserine +P39705 YAR002W NUP60 460 Phosphothreonine +P39705 YAR002W NUP60 480 Phosphoserine +P39705 YAR002W NUP60 483 Phosphoserine +P38881 YHR195W NVJ1 156 Phosphoserine +P38881 YHR195W NVJ1 199 Phosphoserine +P38881 YHR195W NVJ1 285 Phosphoserine +P38881 YHR195W NVJ1 298 Phosphoserine +P38302 YBR188C NTC20 139 Phosphoserine +P31378 YAL015C NTG1 194 Glycyl +P49687 YGL092W NUP145 273 Phosphoserine +P49687 YGL092W NUP145 403 Phosphoserine +P49687 YGL092W NUP145 404 Phosphoserine +P49687 YGL092W NUP145 414 Phosphoserine +P49687 YGL092W NUP145 667 Phosphoserine +P49687 YGL092W NUP145 679 Phosphoserine +P49687 YGL092W NUP145 689 Phosphoserine +P49687 YGL092W NUP145 751 Phosphothreonine +P38219 YBR025C OLA1 89 Phosphothreonine +P38219 YBR025C OLA1 116 Phosphoserine +P38219 YBR025C OLA1 119 Phosphoserine +P38219 YBR025C OLA1 98 Glycyl +P53204 YGR010W NMA2 85 Phosphoserine +P53204 YGR010W NMA2 89 Phosphoserine +P53204 YGR010W NMA2 90 Phosphoserine +P53883 YNL175C NOP13 2 N-acetylserine +P53883 YNL175C NOP13 2 Phosphoserine +P53883 YNL175C NOP13 105 Phosphothreonine +P53883 YNL175C NOP13 335 Phosphoserine +P25655 YCR093W CDC39 2102 Phosphothreonine +P06102 YIL038C NOT3 303 Phosphoserine +P06102 YIL038C NOT3 307 Phosphoserine +P06102 YIL038C NOT3 322 Phosphoserine +P06102 YIL038C NOT3 446 Phosphoserine +P06102 YIL038C NOT3 450 Phosphoserine +P06102 YIL038C NOT3 565 Phosphoserine +P06102 YIL038C NOT3 569 Phosphoserine +P06102 YIL038C NOT3 571 Phosphothreonine +P06102 YIL038C NOT3 657 Phosphoserine +P06102 YIL038C NOT3 535 Glycyl +P39997 YEL016C NPP2 62 N-linked +P39997 YEL016C NPP2 69 N-linked +P39997 YEL016C NPP2 112 N-linked +P39997 YEL016C NPP2 153 N-linked +P39997 YEL016C NPP2 441 N-linked +P53617 YNL251C NRD1 263 Phosphoserine +P53617 YNL251C NRD1 265 Phosphoserine +P53617 YNL251C NRD1 271 Phosphoserine +P40007 YER002W NOP16 176 Phosphoserine +P40007 YER002W NOP16 178 Phosphoserine +P40991 YNL061W NOP2 580 Phosphoserine +Q08287 YOL144W NOP8 234 Phosphoserine +Q08287 YOL144W NOP8 239 Phosphoserine +Q08287 YOL144W NOP8 268 Phosphoserine +Q08287 YOL144W NOP8 370 Phosphoserine +Q04958 YML059C NTE1 300 Phosphoserine +Q04958 YML059C NTE1 312 Phosphoserine +Q04958 YML059C NTE1 632 Phosphoserine +Q04958 YML059C NTE1 634 Phosphoserine +Q04958 YML059C NTE1 653 Phosphoserine +Q04958 YML059C NTE1 661 Phosphoserine +Q04958 YML059C NTE1 670 Phosphoserine +Q04958 YML059C NTE1 680 Phosphoserine +Q04958 YML059C NTE1 739 Phosphoserine +Q04958 YML059C NTE1 803 Phosphothreonine +P33331 YER009W NTF2 2 N-acetylserine +P33331 YER009W NTF2 53 Glycyl +P36118 YKR022C NTR2 40 Phosphoserine +P36118 YKR022C NTR2 153 Phosphoserine +P36118 YKR022C NTR2 197 Phosphoserine +P36161 YKR082W NUP133 2 N-acetylserine +P38181 YBL079W NUP170 1247 Phosphoserine +P53742 YNR053C NOG2 60 Phosphoserine +P53742 YNR053C NOG2 85 Phosphoserine +P53742 YNR053C NOG2 155 Phosphoserine +Q12200 YPL006W NCR1 123 N-linked +Q12200 YPL006W NCR1 145 N-linked +Q12200 YPL006W NCR1 178 N-linked +Q12200 YPL006W NCR1 314 N-linked +Q12200 YPL006W NCR1 401 N-linked +Q12200 YPL006W NCR1 513 N-linked +Q12200 YPL006W NCR1 900 N-linked +Q12200 YPL006W NCR1 940 N-linked +Q03125 YDR043C NRG1 163 Phosphoserine +P51533 YOR328W PDR10 754 N-linked +Q02785 YPL058C PDR12 2 N-acetylserine +Q02785 YPL058C PDR12 32 Phosphoserine +Q02785 YPL058C PDR12 52 Phosphoserine +Q02785 YPL058C PDR12 56 Phosphoserine +Q02785 YPL058C PDR12 1405 N-linked +Q02785 YPL058C PDR12 426 Glycyl +Q07418 YDL065C PEX19 62 Phosphoserine +Q07418 YDL065C PEX19 304 Phosphoserine +Q07418 YDL065C PEX19 339 Cysteine +Q07418 YDL065C PEX19 339 S-farnesyl +Q06169 YLR324W PEX30 2 N-acetylserine +Q06169 YLR324W PEX30 52 Phosphoserine +Q06169 YLR324W PEX30 420 Phosphoserine +Q06169 YLR324W PEX30 424 Phosphoserine +P07269 YDL106C PHO2 542 Phosphothreonine +P17442 YGR233C PHO81 956 Phosphoserine +P25360 YCR037C PHO87 162 N-linked +P25360 YCR037C PHO87 202 N-linked +P25360 YCR037C PHO87 274 N-linked +P25360 YCR037C PHO87 102 Glycyl +Q12057 YOR104W PIN2 141 Phosphothreonine +Q12057 YOR104W PIN2 91 N-linked +Q12057 YOR104W PIN2 132 N-linked +Q12057 YOR104W PIN2 276 N-linked +Q03407 YDR490C PKH1 294 Phosphoserine +Q03407 YDR490C PKH1 296 Phosphoserine +P39105 YMR008C PLB1 634 GPI-anchor +P39105 YMR008C PLB1 26 N-linked +P39105 YMR008C PLB1 33 N-linked +P39105 YMR008C PLB1 52 N-linked +P39105 YMR008C PLB1 78 N-linked +P39105 YMR008C PLB1 92 N-linked +P39105 YMR008C PLB1 123 N-linked +P39105 YMR008C PLB1 160 N-linked +P39105 YMR008C PLB1 170 N-linked +P39105 YMR008C PLB1 215 N-linked +P39105 YMR008C PLB1 277 N-linked +P39105 YMR008C PLB1 307 N-linked +P39105 YMR008C PLB1 345 N-linked +P39105 YMR008C PLB1 388 N-linked +P39105 YMR008C PLB1 459 N-linked +P39105 YMR008C PLB1 489 N-linked +P39105 YMR008C PLB1 513 N-linked +P39105 YMR008C PLB1 541 N-linked +P39105 YMR008C PLB1 565 N-linked +P39105 YMR008C PLB1 582 N-linked +Q03674 YMR006C PLB2 680 GPI-anchor +Q03674 YMR006C PLB2 47 N-linked +Q03674 YMR006C PLB2 80 N-linked +Q03674 YMR006C PLB2 94 N-linked +Q03674 YMR006C PLB2 125 N-linked +Q03674 YMR006C PLB2 162 N-linked +Q03674 YMR006C PLB2 181 N-linked +Q03674 YMR006C PLB2 193 N-linked +Q03674 YMR006C PLB2 217 N-linked +Q03674 YMR006C PLB2 279 N-linked +Q03674 YMR006C PLB2 309 N-linked +Q03674 YMR006C PLB2 365 N-linked +Q03674 YMR006C PLB2 390 N-linked +Q03674 YMR006C PLB2 491 N-linked +Q03674 YMR006C PLB2 515 N-linked +Q03674 YMR006C PLB2 524 N-linked +Q03674 YMR006C PLB2 543 N-linked +Q03674 YMR006C PLB2 567 N-linked +Q03674 YMR006C PLB2 584 N-linked +Q03674 YMR006C PLB2 598 N-linked +Q03674 YMR006C PLB2 630 N-linked +Q03674 YMR006C PLB2 634 N-linked +Q03674 YMR006C PLB2 642 N-linked +Q03674 YMR006C PLB2 648 N-linked +Q03674 YMR006C PLB2 652 N-linked +Q03674 YMR006C PLB2 658 N-linked +P27801 YLR148W PEP3 907 Phosphoserine +P40335 YJL053W PEP8 216 Phosphoserine +P53203 YGR004W PEX31 432 Phosphoserine +P53203 YGR004W PEX31 435 Phosphothreonine +P46988 YJL179W PFD1 2 N-acetylserine +P52553 YLR200W YKE2 2 N-acetylserine +P07270 YFR034C PHO4 100 Phosphoserine%3B +P07270 YFR034C PHO4 114 Phosphoserine%3B +P07270 YFR034C PHO4 128 Phosphoserine%3B +P07270 YFR034C PHO4 152 Phosphoserine%3B +P07270 YFR034C PHO4 204 Phosphoserine +P07270 YFR034C PHO4 223 Phosphoserine%3B +P07270 YFR034C PHO4 242 Phosphoserine +P07270 YFR034C PHO4 243 Phosphoserine +P20052 YOL001W PHO80 234 Phosphoserine%3B +P20052 YOL001W PHO80 267 Phosphoserine%3B +P06738 YPR160W GPH1 31 Phosphothreonine +P06738 YPR160W GPH1 333 Phosphoserine +P06738 YPR160W GPH1 751 N6-(pyridoxal +P40187 YIL045W PIG2 162 Phosphoserine +P40187 YIL045W PIG2 196 Phosphoserine +P40187 YIL045W PIG2 296 Phosphoserine +P40187 YIL045W PIG2 304 Phosphoserine +Q12252 YOL084W PHM7 115 N-linked +Q12252 YOL084W PHM7 132 N-linked +P53297 YGR178C PBP1 106 Phosphoserine +P53297 YGR178C PBP1 193 Phosphothreonine +P53297 YGR178C PBP1 215 Phosphoserine +P53297 YGR178C PBP1 436 Phosphoserine +P53297 YGR178C PBP1 344 Glycyl +P06169 YLR044C PDC1 2 N-acetylserine +P06169 YLR044C PDC1 223 Phosphoserine +P06169 YLR044C PDC1 266 Phosphothreonine +P06169 YLR044C PDC1 336 Phosphothreonine +P06169 YLR044C PDC1 353 Phosphothreonine +P06169 YLR044C PDC1 522 Phosphothreonine +P06169 YLR044C PDC1 526 Phosphoserine +P06169 YLR044C PDC1 212 Glycyl +P06169 YLR044C PDC1 233 Glycyl +P06169 YLR044C PDC1 269 Glycyl +P06169 YLR044C PDC1 332 Glycyl +P06169 YLR044C PDC1 484 Glycyl +P06169 YLR044C PDC1 505 Glycyl +P06169 YLR044C PDC1 520 Glycyl +P38848 YHR150W PEX28 361 N-linked +P35056 YDR244W PEX5 1 N-acetylmethionine +P35056 YDR244W PEX5 61 Phosphoserine +P35056 YDR244W PEX5 6 Glycyl +P35056 YDR244W PEX5 18 Glycyl +P35056 YDR244W PEX5 24 Glycyl +P53900 YNL153C GIM3 1 N-acetylmethionine +P53896 YNL158W PGA1 72 N-linked +P53896 YNL158W PGA1 80 N-linked +P32854 YOR036W PEP12 2 Phosphoserine +P32854 YOR036W PEP12 23 Phosphoserine +Q02969 YPL112C PEX25 58 Phosphoserine +Q02969 YPL112C PEX25 63 Phosphoserine +Q02969 YPL112C PEX25 289 Phosphoserine +P53903 YNL149C PGA2 2 N-acetylserine +P53903 YNL149C PGA2 119 Phosphoserine +P07271 YML061C PIF1 70 Phosphoserine +P07271 YML061C PIF1 72 Phosphoserine +P07271 YML061C PIF1 169 Phosphoserine +P07271 YML061C PIF1 584 Phosphoserine +P14242 YNL082W PMS1 393 Phosphoserine +P14242 YNL082W PMS1 566 Phosphoserine +P47190 YOR321W PMT3 124 N-linked +P47190 YOR321W PMT3 324 N-linked +P47190 YOR321W PMT3 398 N-linked +P52867 YDL093W PMT5 33 N-linked +P52867 YDL093W PMT5 213 N-linked +P52867 YDL093W PMT5 380 N-linked +P52867 YDL093W PMT5 386 N-linked +P42934 YGR199W PMT6 2 N-acetylserine +P42934 YGR199W PMT6 156 N-linked +P42934 YGR199W PMT6 404 N-linked +P42934 YGR199W PMT6 481 N-linked +Q05788 YLR209C PNP1 2 N-acetylserine +Q05788 YLR209C PNP1 275 Phosphoserine +P47180 YJR153W PGU1 318 N-linked +P47180 YJR153W PGU1 330 N-linked +P37012 YMR105C PGM2 2 N-acetylserine +P37012 YMR105C PGM2 111 Phosphothreonine +P37012 YMR105C PGM2 117 Phosphothreonine +P37012 YMR105C PGM2 119 Phosphoserine +Q03262 YMR278W PRM15 158 Phosphoserine +P25297 YML123C PHO84 302 Phosphothreonine +P25297 YML123C PHO84 303 Phosphoserine +P25297 YML123C PHO84 316 Phosphoserine +P25297 YML123C PHO84 317 Phosphothreonine +P25297 YML123C PHO84 321 Phosphoserine +P25297 YML123C PHO84 577 Phosphoserine +P25297 YML123C PHO84 579 Phosphoserine +P25297 YML123C PHO84 581 Phosphoserine +P25297 YML123C PHO84 6 Glycyl +P25297 YML123C PHO84 298 Glycyl +P38264 YBR106W PHO88 157 Phosphoserine +P27514 YNR013C PHO91 295 Phosphoserine +P27514 YNR013C PHO91 311 Phosphoserine +P27514 YNR013C PHO91 312 Phosphoserine +Q03306 YDR466W PKH3 696 Phosphoserine +Q03306 YDR466W PKH3 753 Phosphoserine +Q03306 YDR466W PKH3 871 Phosphoserine +P05030 YGL008C PMA1 61 Phosphoserine +P05030 YGL008C PMA1 175 Phosphothreonine +P05030 YGL008C PMA1 911 Phosphoserine +P05030 YGL008C PMA1 912 Phosphothreonine +P05030 YGL008C PMA1 918 Phosphothreonine +P05030 YGL008C PMA1 252 Glycyl +P05030 YGL008C PMA1 555 Glycyl +P53261 YGR103W NOP7 288 Phosphoserine +P53261 YGR103W NOP7 308 Phosphothreonine +P16861 YGR240C PFK1 3 Phosphoserine +P16861 YGR240C PFK1 166 Phosphoserine +P16861 YGR240C PFK1 179 Phosphoserine +P16861 YGR240C PFK1 185 Phosphoserine +P16861 YGR240C PFK1 189 Phosphoserine +P16861 YGR240C PFK1 192 Phosphoserine +P16861 YGR240C PFK1 217 Phosphoserine +P16861 YGR240C PFK1 450 Phosphothreonine +P16861 YGR240C PFK1 89 Glycyl +P16861 YGR240C PFK1 625 Glycyl +P16862 YMR205C PFK2 152 Phosphothreonine +P16862 YMR205C PFK2 163 Phosphoserine +P16862 YMR205C PFK2 171 Phosphoserine +P16862 YMR205C PFK2 803 Phosphoserine +P00560 YCR012W PGK1 2 N-acetylserine +P00560 YCR012W PGK1 93 Phosphothreonine +P00560 YCR012W PGK1 110 Phosphoserine +P00560 YCR012W PGK1 130 Phosphoserine +P00560 YCR012W PGK1 154 Phosphoserine +P00560 YCR012W PGK1 172 Phosphoserine +P00560 YCR012W PGK1 203 Phosphothreonine +P00560 YCR012W PGK1 241 Phosphothreonine +P00560 YCR012W PGK1 298 Phosphothreonine +P00560 YCR012W PGK1 318 Phosphoserine +P00560 YCR012W PGK1 331 Phosphothreonine +P00560 YCR012W PGK1 392 Phosphothreonine +P00560 YCR012W PGK1 82 Glycyl +P00560 YCR012W PGK1 197 Glycyl +P00560 YCR012W PGK1 258 Glycyl +P00560 YCR012W PGK1 274 Glycyl +P00560 YCR012W PGK1 302 Glycyl +P33401 YKL127W PGM1 2 N-acetylserine +P33401 YKL127W PGM1 120 Phosphoserine +P38244 YBR074W PFF1 96 N-linked +P38244 YBR074W PFF1 121 N-linked +P38244 YBR074W PFF1 189 N-linked +P38244 YBR074W PFF1 217 N-linked +P38244 YBR074W PFF1 656 N-linked +P38244 YBR074W PFF1 768 N-linked +P38244 YBR074W PFF1 796 N-linked +P38244 YBR074W PFF1 811 N-linked +P38244 YBR074W PFF1 866 N-linked +P38244 YBR074W PFF1 937 N-linked +P39104 YNL267W PIK1 10 Phosphoserine +P39104 YNL267W PIK1 236 Phosphoserine +P39104 YNL267W PIK1 384 Phosphoserine +P39104 YNL267W PIK1 394 Phosphothreonine +P39104 YNL267W PIK1 396 Phosphoserine +P39104 YNL267W PIK1 592 Phosphoserine +P53252 YGR086C PIL1 14 Phosphothreonine +P53252 YGR086C PIL1 16 Phosphoserine +P53252 YGR086C PIL1 45 Phosphoserine +P53252 YGR086C PIL1 98 Phosphoserine +P53252 YGR086C PIL1 163 Phosphoserine +P53252 YGR086C PIL1 230 Phosphoserine +P53252 YGR086C PIL1 233 Phosphothreonine +P53252 YGR086C PIL1 299 Phosphoserine +P53252 YGR086C PIL1 29 Glycyl +Q12236 YOL100W PKH2 138 Phosphoserine +Q12236 YOL100W PKH2 619 Phosphoserine +Q12236 YOL100W PKH2 1009 Phosphoserine +Q04383 YDR501W PLM2 281 Phosphoserine +Q04383 YDR501W PLM2 295 Phosphoserine +Q04383 YDR501W PLM2 302 Phosphoserine +Q04383 YDR501W PLM2 384 Phosphoserine +Q12412 YOR161C PNS1 259 N-linked +Q12445 YLR018C POM34 270 Phosphoserine +Q12445 YLR018C POM34 273 Phosphothreonine +Q12445 YLR018C POM34 292 Phosphoserine +Q12445 YLR018C POM34 294 Phosphoserine +P23287 YLR433C CNA1 2 N-acetylserine +P39966 YER089C PTC2 376 Phosphothreonine +P39966 YER089C PTC2 380 Phosphothreonine +P11491 YDR481C PHO8 123 Phosphoserine +P11491 YDR481C PHO8 268 N-linked +P11491 YDR481C PHO8 401 N-linked +Q04004 YDR183W PLP1 1 N-acetylmethionine +P32634 YER132C PMD1 298 Phosphothreonine +P32634 YER132C PMD1 838 Phosphoserine +P32634 YER132C PMD1 1289 Phosphoserine +P32634 YER132C PMD1 1307 Phosphoserine +P32634 YER132C PMD1 1356 Phosphoserine +P32634 YER132C PMD1 1664 Phosphoserine +Q06644 YDR307W PMT7 347 N-linked +Q99216 YOR145C PNO1 47 Phosphoserine +Q99216 YOR145C PNO1 51 Phosphothreonine +P38693 YHR215W PHO12 97 N-linked +P38693 YHR215W PHO12 162 N-linked +P38693 YHR215W PHO12 192 N-linked +P38693 YHR215W PHO12 250 N-linked +P38693 YHR215W PHO12 315 N-linked +P38693 YHR215W PHO12 356 N-linked +P38693 YHR215W PHO12 390 N-linked +P38693 YHR215W PHO12 439 N-linked +P38693 YHR215W PHO12 445 N-linked +P38693 YHR215W PHO12 461 N-linked +Q08108 YOL011W PLB3 659 GPI-anchor +Q08108 YOL011W PLB3 56 N-linked +Q08108 YOL011W PLB3 82 N-linked +Q08108 YOL011W PLB3 129 N-linked +Q08108 YOL011W PLB3 166 N-linked +Q08108 YOL011W PLB3 221 N-linked +Q08108 YOL011W PLB3 283 N-linked +Q08108 YOL011W PLB3 313 N-linked +Q08108 YOL011W PLB3 351 N-linked +Q08108 YOL011W PLB3 495 N-linked +Q08108 YOL011W PLB3 519 N-linked +Q08108 YOL011W PLB3 547 N-linked +Q08108 YOL011W PLB3 571 N-linked +Q08108 YOL011W PLB3 588 N-linked +Q08108 YOL011W PLB3 614 N-linked +P41812 YNL221C POP1 524 Phosphothreonine +P00950 YKL152C GPM1 12 Phosphoserine +P00950 YKL152C GPM1 49 Phosphotyrosine +P00950 YKL152C GPM1 116 Phosphoserine +P00950 YKL152C GPM1 127 Phosphoserine +P00950 YKL152C GPM1 128 Phosphoserine +P00950 YKL152C GPM1 185 Phosphoserine +P00950 YKL152C GPM1 197 Phosphoserine +P00950 YKL152C GPM1 31 Glycyl +P00950 YKL152C GPM1 57 Glycyl +P00950 YKL152C GPM1 71 Glycyl +P00950 YKL152C GPM1 139 Glycyl +P00950 YKL152C GPM1 175 Glycyl +P00950 YKL152C GPM1 191 Glycyl +P33775 YDL095W PMT1 2 N-acetylserine +P33775 YDL095W PMT1 390 N-linked +P33775 YDL095W PMT1 513 N-linked +P33775 YDL095W PMT1 743 N-linked +P31382 YAL023C PMT2 2 N-acetylserine +P31382 YAL023C PMT2 32 Phosphoserine +P31382 YAL023C PMT2 38 Phosphoserine +P31382 YAL023C PMT2 39 Phosphoserine +P31382 YAL023C PMT2 131 N-linked +P31382 YAL023C PMT2 155 N-linked +P31382 YAL023C PMT2 403 N-linked +P46971 YJR143C PMT4 759 N-linked +P39685 YMR129W POM152 45 Phosphoserine +P39685 YMR129W POM152 60 Phosphoserine +P39685 YMR129W POM152 280 N-linked +P23594 YDL134C PPH21 369 Leucine +P00635 YBR093C PHO5 97 N-linked +P00635 YBR093C PHO5 103 N-linked +P00635 YBR093C PHO5 162 N-linked +P00635 YBR093C PHO5 192 N-linked +P00635 YBR093C PHO5 250 N-linked +P00635 YBR093C PHO5 315 N-linked +P00635 YBR093C PHO5 356 N-linked +P00635 YBR093C PHO5 390 N-linked +P00635 YBR093C PHO5 439 N-linked +P00635 YBR093C PHO5 445 N-linked +P00635 YBR093C PHO5 456 N-linked +P00635 YBR093C PHO5 461 N-linked +P40035 YER053C PIC2 1 N-acetylmethionine +P40473 YIL122W POG1 152 Phosphoserine +P40473 YIL122W POG1 168 Phosphoserine +P40473 YIL122W POG1 314 Phosphoserine +P39008 YNR052C POP2 1 N-acetylmethionine +P39008 YNR052C POP2 97 Phosphothreonine%3B +P17157 YPL031C PHO85 18 Phosphotyrosine +P17157 YPL031C PHO85 289 Glycyl +P53191 YGL023C PIB2 46 Phosphoserine +P53191 YGL023C PIB2 53 Phosphoserine +P53191 YGL023C PIB2 56 Phosphothreonine +P53191 YGL023C PIB2 73 Phosphoserine +P53191 YGL023C PIB2 113 Phosphoserine +P53191 YGL023C PIB2 124 Phosphoserine +P53191 YGL023C PIB2 148 Phosphoserine +P53191 YGL023C PIB2 165 Phosphoserine +P53191 YGL023C PIB2 174 Phosphoserine +P53191 YGL023C PIB2 300 Phosphoserine +P53191 YGL023C PIB2 309 Phosphoserine +P53191 YGL023C PIB2 381 Phosphoserine +P07283 YFL045C SEC53 240 Phosphoserine +P38336 YBR257W POP4 64 Phosphoserine +P38291 YBR167C POP7 115 Phosphoserine +P23595 YDL188C PPH22 38 Phosphoserine +P23595 YDL188C PPH22 43 Phosphothreonine +P23595 YDL188C PPH22 377 Leucine +P34221 YBL056W PTC3 324 Phosphoserine +P34221 YBL056W PTC3 332 Phosphoserine +P35842 YAR071W PHO11 97 N-linked +P35842 YAR071W PHO11 162 N-linked +P35842 YAR071W PHO11 192 N-linked +P35842 YAR071W PHO11 250 N-linked +P35842 YAR071W PHO11 315 N-linked +P35842 YAR071W PHO11 356 N-linked +P35842 YAR071W PHO11 390 N-linked +P35842 YAR071W PHO11 439 N-linked +P35842 YAR071W PHO11 445 N-linked +P35842 YAR071W PHO11 461 N-linked +P53549 YOR259C RPT4 2 N-acetylserine +Q01939 YGL048C RPT6 2 N-acetylthreonine +P25375 YCL057W PRD1 73 Phosphoserine +Q04119 YDR452W PPN1 58 N-linked +Q04119 YDR452W PPN1 505 N-linked +Q04119 YDR452W PPN1 511 N-linked +Q04119 YDR452W PPN1 6 Glycyl +Q06449 YPR154W PIN3 2 N-acetylserine +Q06449 YPR154W PIN3 52 Phosphoserine +Q06449 YPR154W PIN3 55 Phosphoserine +Q06449 YPR154W PIN3 80 Glycyl +P34217 YBL051C PIN4 56 Phosphoserine +P34217 YBL051C PIN4 189 Phosphoserine +P34217 YBL051C PIN4 191 Phosphoserine +P34217 YBL051C PIN4 194 Phosphoserine +P34217 YBL051C PIN4 197 Phosphoserine +P34217 YBL051C PIN4 305 Phosphothreonine +P34217 YBL051C PIN4 393 Phosphoserine +P34217 YBL051C PIN4 466 Phosphoserine +P34217 YBL051C PIN4 541 Phosphoserine +P34217 YBL051C PIN4 636 Phosphoserine +P34217 YBL051C PIN4 638 Phosphoserine +P34217 YBL051C PIN4 640 Phosphoserine +P34217 YBL051C PIN4 653 Phosphoserine +P34217 YBL051C PIN4 655 Phosphoserine +Q12017 YOR281C PLP2 35 Phosphoserine +Q12017 YOR281C PLP2 62 Phosphoserine +Q12161 YOL054W PSH1 143 Phosphoserine +Q12161 YOL054W PSH1 191 Phosphoserine +Q12161 YOL054W PSH1 310 Phosphothreonine +Q12161 YOL054W PSH1 403 Phosphoserine +P08456 YER026C CHO1 4 Phosphoserine +P08456 YER026C CHO1 34 Phosphoserine +P08456 YER026C CHO1 42 Phosphoserine +P08456 YER026C CHO1 46 Phosphoserine +P08456 YER026C CHO1 47 Phosphoserine +P08456 YER026C CHO1 50 Phosphoserine +P28708 YKL116C PRR1 1 N-acetylmethionine +P28708 YKL116C PRR1 132 Phosphoserine +P23639 YML092C PRE8 108 Glycyl +P50109 YML017W PSP2 238 Phosphoserine +P50109 YML017W PSP2 340 Phosphoserine +Q07949 YLR019W PSR2 9 S-palmitoyl +Q07949 YLR019W PSR2 10 S-palmitoyl +P32901 YKR093W PTR2 37 Phosphotyrosine +P32901 YKR093W PTR2 39 Phosphoserine +P32901 YKR093W PTR2 45 Phosphoserine +P32901 YKR093W PTR2 594 Phosphoserine +P38193 YBL046W PSY4 347 Phosphothreonine +P32857 YKL039W PTM1 480 Phosphoserine +P32857 YKL039W PTM1 483 Phosphothreonine +P32857 YKL039W PTM1 498 Phosphothreonine +P32857 YKL039W PTM1 132 N-linked +P23394 YDR243C PRP28 69 Phosphoserine +P22141 YER012W PRE1 1 N-acetylmethionine +P22141 YER012W PRE1 76 Phosphoserine +P33329 YDR436W PPZ2 55 Phosphoserine +P33329 YDR436W PPZ2 71 Phosphoserine +P33329 YDR436W PPZ2 161 Phosphothreonine +P33329 YDR436W PPZ2 203 Phosphoserine +P33329 YDR436W PPZ2 224 Phosphoserine +P33329 YDR436W PPZ2 271 Phosphothreonine +P33329 YDR436W PPZ2 275 Phosphoserine +P33329 YDR436W PPZ2 310 Phosphoserine +P33329 YDR436W PPZ2 2 N-myristoyl +P40494 YIL095W PRK1 402 Phosphoserine +P40494 YIL095W PRK1 428 Phosphoserine +P40494 YIL095W PRK1 484 Phosphoserine +P40494 YIL095W PRK1 553 Phosphothreonine +P40494 YIL095W PRK1 556 Phosphoserine +P53835 YNL279W PRM1 135 N-linked +P53835 YNL279W PRM1 145 N-linked +P53835 YNL279W PRM1 188 N-linked +P53835 YNL279W PRM1 197 N-linked +P53835 YNL279W PRM1 231 N-linked +P53835 YNL279W PRM1 252 N-linked +P53835 YNL279W PRM1 272 N-linked +P53835 YNL279W PRM1 280 N-linked +P53835 YNL279W PRM1 490 N-linked +P53835 YNL279W PRM1 505 N-linked +P53835 YNL279W PRM1 512 N-linked +P53835 YNL279W PRM1 531 N-linked +P53835 YNL279W PRM1 573 N-linked +P53835 YNL279W PRM1 587 N-linked +P21243 YGL011C SCL1 2 N-acetylserine +P21243 YGL011C SCL1 237 Phosphoserine +P21243 YGL011C SCL1 232 Glycyl +P21242 YOR362C PRE10 2 N-acetylthreonine +P26570 YML016C PPZ1 49 Phosphoserine +P26570 YML016C PPZ1 171 Phosphothreonine +P26570 YML016C PPZ1 209 Phosphoserine +P26570 YML016C PPZ1 222 Phosphoserine +P26570 YML016C PPZ1 261 Phosphothreonine +P26570 YML016C PPZ1 265 Phosphoserine +P26570 YML016C PPZ1 690 Phosphoserine +P26570 YML016C PPZ1 2 N-myristoyl +P49960 YMR268C PRP24 19 Phosphoserine +P33203 YKL012W PRP40 576 Phosphothreonine +P40303 YOL038W PRE6 60 Phosphothreonine +P38624 YJL001W PRE3 1 N-acetylmethionine +P25451 YER094C PUP3 31 Phosphoserine +P25451 YER094C PUP3 70 Glycyl +Q08217 YOL045W PSK2 118 Phosphothreonine +P14747 YML057W CMP2 31 Phosphothreonine +P14747 YML057W CMP2 489 Phosphoserine +P14747 YML057W CMP2 520 Phosphoserine +P24031 YBR092C PHO3 97 N-linked +P24031 YBR092C PHO3 103 N-linked +P24031 YBR092C PHO3 162 N-linked +P24031 YBR092C PHO3 192 N-linked +P24031 YBR092C PHO3 250 N-linked +P24031 YBR092C PHO3 315 N-linked +P24031 YBR092C PHO3 356 N-linked +P24031 YBR092C PHO3 390 N-linked +P24031 YBR092C PHO3 439 N-linked +P24031 YBR092C PHO3 445 N-linked +P24031 YBR092C PHO3 456 N-linked +P24031 YBR092C PHO3 461 N-linked +P52290 YDL024C DIA3 98 N-linked +P52290 YDL024C DIA3 163 N-linked +P52290 YDL024C DIA3 193 N-linked +P52290 YDL024C DIA3 202 N-linked +P52290 YDL024C DIA3 238 N-linked +P52290 YDL024C DIA3 251 N-linked +P52290 YDL024C DIA3 316 N-linked +P52290 YDL024C DIA3 357 N-linked +P52290 YDL024C DIA3 391 N-linked +P52290 YDL024C DIA3 457 N-linked +P52290 YDL024C DIA3 462 N-linked +P40347 YPR073C LTP1 57 Phosphoserine +P40476 YIL117C PRM5 129 Phosphoserine +P40476 YIL117C PRM5 279 Phosphoserine +P40476 YIL117C PRM5 282 Phosphoserine +P40476 YIL117C PRM5 288 Phosphoserine +P40476 YIL117C PRM5 314 Glycyl +P53131 YGL120C PRP43 8 Phosphoserine +P53131 YGL120C PRP43 9 Phosphoserine +P40327 YDL007W RPT2 2 N-myristoyl +P40327 YDL007W RPT2 234 Glycyl +P40327 YDL007W RPT2 255 Glycyl +P40327 YDL007W RPT2 290 Glycyl +P33297 YOR117W RPT5 2 N-acetylalanine +P33297 YOR117W RPT5 180 Phosphotyrosine +P33298 YDR394W RPT3 1 N-acetylmethionine +P33298 YDR394W RPT3 280 Glycyl +P09232 YEL060C PRB1 594 N-linked +P23638 YGR135W PRE9 100 Glycyl +P23638 YGR135W PRE9 199 Glycyl +P23638 YGR135W PRE9 231 Glycyl +P53633 YNL044W YIP3 1 N-acetylmethionine +P53633 YNL044W YIP3 18 Phosphoserine +P54885 YOR323C PRO2 2 N-acetylserine +P20095 YNR011C PRP2 2 N-acetylserine +P33299 YKL145W RPT1 164 Phosphoserine +P33299 YKL145W RPT1 231 Phosphoserine +P34227 YBL064C PRX1 53 Phosphoserine +P47033 YJL078C PRY3 853 GPI-anchor +P47033 YJL078C PRY3 101 N-linked +P47033 YJL078C PRY3 360 N-linked +P47033 YJL078C PRY3 488 N-linked +P47033 YJL078C PRY3 535 N-linked +P47033 YJL078C PRY3 547 N-linked +P47033 YJL078C PRY3 569 N-linked +P47033 YJL078C PRY3 625 N-linked +P32379 YGR253C PUP2 55 Phosphothreonine +P32379 YGR253C PUP2 56 Phosphoserine +P32379 YGR253C PUP2 251 Phosphoserine +P40302 YMR314W PRE5 14 Phosphoserine +P40302 YMR314W PRE5 191 Glycyl +Q07800 YLL010C PSR1 110 Phosphoserine +Q07800 YLL010C PSR1 9 S-palmitoyl +Q07800 YLL010C PSR1 10 S-palmitoyl +Q07800 YLL010C PSR1 154 Glycyl +P15380 YOR348C PUT4 72 N-linked +P15380 YOR348C PUT4 78 N-linked +P07259 YJL130C URA2 2 N-acetylalanine +P07259 YJL130C URA2 1857 Phosphoserine%3B +P07259 YJL130C URA2 1853 Glycyl +P32849 YLR032W RAD5 2 N-acetylserine +P32849 YLR032W RAD5 20 Phosphoserine +P32849 YLR032W RAD5 23 Phosphoserine +P32849 YLR032W RAD5 129 Phosphoserine +P32849 YLR032W RAD5 130 Phosphoserine +P14737 YDR217C RAD9 26 Phosphoserine +P14737 YDR217C RAD9 56 Phosphoserine +P14737 YDR217C RAD9 205 Phosphoserine +P14737 YDR217C RAD9 218 Phosphothreonine +P14737 YDR217C RAD9 248 Phosphoserine +P14737 YDR217C RAD9 312 Phosphoserine +P14737 YDR217C RAD9 315 Phosphoserine +P14737 YDR217C RAD9 462 Phosphoserine +P14737 YDR217C RAD9 471 Phosphothreonine +P14737 YDR217C RAD9 474 Phosphothreonine +P14737 YDR217C RAD9 568 Phosphoserine +P14737 YDR217C RAD9 729 Phosphoserine +P20051 YLR420W URA4 98 N6-carboxylysine +P07257 YPR191W QCR2 141 Phosphoserine +P07257 YPR191W QCR2 168 Phosphoserine +P40474 YIL121W QDR2 21 Phosphoserine +P40474 YIL121W QDR2 38 Phosphothreonine +P40474 YIL121W QDR2 40 Phosphoserine +P38227 YBR043C QDR3 436 Phosphoserine +P48581 YOR368W RAD17 383 Phosphoserine +P40352 YJR035W RAD26 30 Phosphoserine +P21827 YGL097W SRM1 135 Phosphoserine +P21827 YGL097W SRM1 136 Phosphoserine +P07276 YGR258C RAD2 118 Phosphoserine +P07276 YGR258C RAD2 367 Phosphoserine +P07276 YGR258C RAD2 583 Phosphoserine +Q12465 YLR084C RAX2 41 N-linked +Q12465 YLR084C RAX2 45 N-linked +Q12465 YLR084C RAX2 69 N-linked +Q12465 YLR084C RAX2 88 N-linked +Q12465 YLR084C RAX2 124 N-linked +Q12465 YLR084C RAX2 134 N-linked +Q12465 YLR084C RAX2 145 N-linked +Q12465 YLR084C RAX2 158 N-linked +Q12465 YLR084C RAX2 166 N-linked +Q12465 YLR084C RAX2 171 N-linked +Q12465 YLR084C RAX2 187 N-linked +Q12465 YLR084C RAX2 200 N-linked +Q12465 YLR084C RAX2 235 N-linked +Q12465 YLR084C RAX2 238 N-linked +Q12465 YLR084C RAX2 244 N-linked +Q12465 YLR084C RAX2 333 N-linked +Q12465 YLR084C RAX2 365 N-linked +Q12465 YLR084C RAX2 379 N-linked +Q12465 YLR084C RAX2 432 N-linked +Q12465 YLR084C RAX2 445 N-linked +Q12465 YLR084C RAX2 516 N-linked +Q12465 YLR084C RAX2 524 N-linked +Q12465 YLR084C RAX2 613 N-linked +Q12465 YLR084C RAX2 620 N-linked +Q12465 YLR084C RAX2 626 N-linked +Q12465 YLR084C RAX2 640 N-linked +Q12465 YLR084C RAX2 677 N-linked +Q12465 YLR084C RAX2 705 N-linked +Q12465 YLR084C RAX2 713 N-linked +Q12465 YLR084C RAX2 721 N-linked +Q12465 YLR084C RAX2 731 N-linked +Q12465 YLR084C RAX2 749 N-linked +Q12465 YLR084C RAX2 758 N-linked +Q12465 YLR084C RAX2 792 N-linked +Q12465 YLR084C RAX2 821 N-linked +Q12465 YLR084C RAX2 848 N-linked +Q12465 YLR084C RAX2 861 N-linked +Q12465 YLR084C RAX2 884 N-linked +Q12465 YLR084C RAX2 890 N-linked +Q12465 YLR084C RAX2 908 N-linked +Q12465 YLR084C RAX2 923 N-linked +Q12465 YLR084C RAX2 942 N-linked +Q12465 YLR084C RAX2 956 N-linked +Q12465 YLR084C RAX2 980 N-linked +Q12465 YLR084C RAX2 983 N-linked +Q12465 YLR084C RAX2 1011 N-linked +Q12465 YLR084C RAX2 1024 N-linked +Q12465 YLR084C RAX2 1031 N-linked +Q12465 YLR084C RAX2 1060 N-linked +Q12465 YLR084C RAX2 1071 N-linked +Q12465 YLR084C RAX2 1098 N-linked +Q12465 YLR084C RAX2 1126 N-linked +P31244 YBR114W RAD16 25 Phosphoserine +P31244 YBR114W RAD16 109 Phosphoserine +P11938 YNL216W RAP1 486 Phosphothreonine +P11938 YNL216W RAP1 731 Phosphoserine +P53295 YGR173W RBG2 364 Phosphoserine +Q08096 YOL010W RCL1 2 N-acetylserine +Q03446 YDR003W RCR2 161 Phosphoserine +Q03446 YDR003W RCR2 191 Phosphothreonine +P39531 YJL204C RCY1 409 Phosphoserine +P03872 R0040C REP2 1 N-acetylmethionine +P06780 YPR165W RHO1 2 N-acetylserine +P06780 YPR165W RHO1 206 Cysteine +P06780 YPR165W RHO1 206 S-geranylgeranyl +Q05672 YDL189W RBS1 198 Phosphoserine +Q05672 YDL189W RBS1 435 Phosphoserine +Q05672 YDL189W RBS1 439 Phosphoserine +Q05672 YDL189W RBS1 447 Phosphoserine +Q08273 YOL133W HRT1 15 Phosphoserine +P21538 YBR049C REB1 355 Phosphoserine +P21538 YBR049C REB1 807 Glycyl +P10862 YCR066W RAD18 155 Phosphothreonine +P10862 YCR066W RAD18 174 Phosphoserine +P10862 YCR066W RAD18 204 Glycyl +P12753 YNL250W RAD50 469 Phosphoserine +P12753 YNL250W RAD50 568 Phosphothreonine +Q08760 YOR301W RAX1 167 Phosphoserine +Q12044 YOR220W RCN2 104 Phosphoserine +Q12044 YOR220W RCN2 110 Phosphoserine +Q12044 YOR220W RCN2 132 Phosphothreonine +Q12044 YOR220W RCN2 152 Phosphoserine +Q12044 YOR220W RCN2 157 Phosphoserine +Q12044 YOR220W RCN2 160 Phosphoserine +Q12044 YOR220W RCN2 183 Phosphoserine +Q12044 YOR220W RCN2 187 Phosphoserine +Q12044 YOR220W RCN2 193 Phosphoserine +Q12044 YOR220W RCN2 201 Phosphoserine +Q12044 YOR220W RCN2 255 Phosphoserine +Q04779 YMR075W RCO1 1 N-acetylmethionine +Q04779 YMR075W RCO1 68 Phosphoserine +Q04779 YMR075W RCO1 683 Phosphoserine +P19541 YPL133C RDS2 102 Phosphoserine +P19541 YPL133C RDS2 231 Phosphothreonine +Q00816 YDR028C REG1 2 N-acetylserine +Q00816 YDR028C REG1 73 Phosphothreonine +Q00816 YDR028C REG1 75 Phosphoserine +Q00816 YDR028C REG1 242 Phosphoserine +Q00816 YDR028C REG1 254 Phosphoserine +Q00816 YDR028C REG1 311 Phosphoserine +Q00816 YDR028C REG1 421 Phosphoserine +Q00816 YDR028C REG1 480 Phosphotyrosine +Q00816 YDR028C REG1 490 Phosphoserine +Q00816 YDR028C REG1 570 Phosphoserine +Q00816 YDR028C REG1 572 Phosphoserine +Q00816 YDR028C REG1 576 Phosphoserine +Q00816 YDR028C REG1 610 Phosphoserine +Q00816 YDR028C REG1 614 Phosphoserine +Q00816 YDR028C REG1 680 Phosphoserine +Q00816 YDR028C REG1 896 Phosphothreonine +Q00816 YDR028C REG1 898 Phosphoserine +Q00816 YDR028C REG1 980 Phosphoserine +P38344 YBR267W REI1 140 Phosphothreonine +P39729 YAL036C RBG1 2 N-acetylserine +P38623 YLR248W RCK2 46 Phosphoserine +P38623 YLR248W RCK2 50 Phosphoserine +P38623 YLR248W RCK2 187 Phosphoserine +P38623 YLR248W RCK2 350 Phosphothreonine +P38623 YLR248W RCK2 520 Phosphoserine +P36054 YKL159C RCN1 113 Phosphoserine +P36054 YKL159C RCN1 117 Phosphoserine +P36054 YKL159C RCN1 182 Phosphothreonine +P38086 YBR073W RDH54 649 Glycyl +P01119 YOR101W RAS1 306 Cysteine +P01119 YOR101W RAS1 305 S-palmitoyl +P01119 YOR101W RAS1 306 S-farnesyl +P01120 YNL098C RAS2 198 Phosphoserine +P01120 YNL098C RAS2 202 Phosphoserine +P01120 YNL098C RAS2 207 Phosphoserine +P01120 YNL098C RAS2 214 Phosphoserine +P01120 YNL098C RAS2 235 Phosphoserine +P01120 YNL098C RAS2 238 Phosphoserine +P01120 YNL098C RAS2 319 Cysteine +P01120 YNL098C RAS2 318 S-palmitoyl +P01120 YNL098C RAS2 319 S-farnesyl +P01120 YNL098C RAS2 131 Glycyl +P47104 YJR033C RAV1 1244 Phosphoserine +P47104 YJR033C RAV1 1248 Phosphoserine +Q12192 YOR279C RFM1 215 Phosphoserine +P40043 YER067W RGI1 68 Glycyl +P32862 YKL038W RGT1 202 Phosphoserine +P32862 YKL038W RGT1 205 Phosphoserine +P32862 YKL038W RGT1 208 Phosphoserine +P32862 YKL038W RGT1 229 Phosphoserine +P32862 YKL038W RGT1 283 Phosphoserine +P32862 YKL038W RGT1 284 Phosphoserine +P32862 YKL038W RGT1 410 Phosphoserine +P32862 YKL038W RGT1 414 Phosphoserine +P32862 YKL038W RGT1 1130 Phosphoserine +P25378 YCR027C RHB1 1 N-acetylmethionine +P25378 YCR027C RHB1 206 Cysteine +P25378 YCR027C RHB1 206 S-farnesyl +Q12305 YOR285W RDL1 26 Phosphoserine +P53331 YGR276C RNH70 24 Phosphoserine +P38630 YOR217W RFC1 38 Phosphothreonine +P38630 YOR217W RFC1 40 Phosphoserine +P38630 YOR217W RFC1 63 Phosphothreonine +P38629 YNL290W RFC3 2 N-acetylserine +Q06624 YPR180W AOS1 9 Phosphoserine +Q06624 YPR180W AOS1 35 Glycyl +P43565 YFL033C RIM15 380 Phosphoserine +P43565 YFL033C RIM15 476 Phosphoserine +P43565 YFL033C RIM15 704 Phosphothreonine +P43565 YFL033C RIM15 709 Phosphoserine +P43565 YFL033C RIM15 733 Phosphoserine +P43565 YFL033C RIM15 736 Phosphoserine +P43565 YFL033C RIM15 737 Phosphoserine +P43565 YFL033C RIM15 747 Phosphothreonine +P43565 YFL033C RIM15 1044 Phosphoserine +P43565 YFL033C RIM15 1048 Phosphoserine +P43565 YFL033C RIM15 1064 Phosphoserine +P43565 YFL033C RIM15 1075 Phosphothreonine%3B +P43565 YFL033C RIM15 1421 Phosphoserine +P43565 YFL033C RIM15 1531 Phosphoserine +P43565 YFL033C RIM15 1538 Phosphoserine +P43565 YFL033C RIM15 1542 Phosphoserine +P43565 YFL033C RIM15 1565 Phosphoserine +P43565 YFL033C RIM15 1764 Phosphoserine +P39083 YOR127W RGA1 278 Phosphothreonine +P39083 YOR127W RGA1 291 Phosphoserine +P39083 YOR127W RGA1 532 Phosphothreonine +Q06108 YPR115W RGC1 136 Phosphoserine +Q06108 YPR115W RGC1 249 Phosphoserine +Q06108 YPR115W RGC1 252 Phosphoserine +Q06108 YPR115W RGC1 481 Phosphoserine +Q06108 YPR115W RGC1 537 Phosphoserine +Q06108 YPR115W RGC1 652 Phosphoserine +Q06108 YPR115W RGC1 765 Phosphoserine +Q06108 YPR115W RGC1 813 Phosphoserine +Q06108 YPR115W RGC1 817 Phosphothreonine +Q06108 YPR115W RGC1 857 Phosphothreonine +Q06108 YPR115W RGC1 866 Phosphoserine +Q06108 YPR115W RGC1 879 Phosphoserine +Q06108 YPR115W RGC1 918 Phosphoserine +Q06108 YPR115W RGC1 966 Phosphoserine +Q06108 YPR115W RGC1 969 Phosphoserine +Q06108 YPR115W RGC1 975 Phosphoserine +Q06108 YPR115W RGC1 1059 Phosphoserine +Q06108 YPR115W RGC1 1081 Phosphoserine +Q06108 YPR115W RGC1 1082 Phosphoserine +P16664 YDR137W RGP1 351 Phosphoserine +P16664 YDR137W RGP1 354 Phosphoserine +P16664 YDR137W RGP1 357 Phosphoserine +P16664 YDR137W RGP1 363 Phosphoserine +P16664 YDR137W RGP1 364 Phosphoserine +P16664 YDR137W RGP1 370 Phosphoserine +Q12300 YDL138W RGT2 136 N-linked +Q12300 YDL138W RGT2 385 N-linked +P21524 YER070W RNR1 227 Phosphoserine +P21524 YER070W RNR1 816 Phosphoserine +P21524 YER070W RNR1 837 Phosphoserine +P21524 YER070W RNR1 887 Phosphoserine +P21524 YER070W RNR1 387 Glycyl +P21524 YER070W RNR1 853 Glycyl +Q07844 YLL034C RIX7 42 Phosphoserine +P26785 YNL069C RPL16B 2 N-acetylserine%3B +P26785 YNL069C RPL16B 43 Phosphoserine +P26785 YNL069C RPL16B 181 Phosphoserine +P26785 YNL069C RPL16B 185 Phosphoserine +P26785 YNL069C RPL16B 187 Phosphoserine +P26785 YNL069C RPL16B 176 Glycyl +P46990 YJL177W RPL17B 70 Phosphothreonine +P46990 YJL177W RPL17B 46 Glycyl +P36105 YKL006W RPL14A 2 N-acetylserine +P0CX49 YOL120C RPL18A 50 N6%2CN6%2CN6-trimethyllysine +P0CX49 YOL120C RPL18A 116 Glycyl +P0CX24 YOR312C RPL20B 32 Phosphoserine +P0CX24 YOR312C RPL20B 125 Glycyl +P0CX24 YOR312C RPL20B 131 Glycyl +P0CX24 YOR312C RPL20B 149 Glycyl +Q12672 YPL079W RPL21B 32 Glycyl +P0CX41 YBL087C RPL23A 2 N-acetylserine +P0CX41 YBL087C RPL23A 106 N6%2CN6-dimethyllysine%3B +P0CX41 YBL087C RPL23A 110 N6%2CN6-dimethyllysine%3B +P30775 YGL143C MRF1 287 N5-methylglutamine +P53893 YNL163C RIA1 431 Phosphoserine +P22336 YAR007C RFA1 2 N-acetylserine +P22336 YAR007C RFA1 178 Phosphoserine%3B +P26754 YNL312W RFA2 27 Phosphoserine +P26754 YNL312W RFA2 122 Phosphoserine +P40348 YJR068W RFC2 1 N-acetylmethionine +P06781 YNL090W RHO2 189 Cysteine +P06781 YNL090W RHO2 188 S-palmitoyl +P06781 YNL090W RHO2 189 S-geranylgeranyl +Q3E757 YGR085C RPL11B 2 N-acetylserine +Q3E757 YGR085C RPL11B 75 N6%2CN6%2CN6-trimethyllysine +P48743 YLR176C RFX1 173 Phosphoserine +Q06407 YDR379W RGA2 763 Phosphoserine +P38339 YBR260C RGD1 386 Phosphothreonine +P40160 YNL207W RIO2 346 Phosphoserine +P49723 YGR180C RNR4 1 N-acetylmethionine +P49723 YGR180C RNR4 169 Phosphoserine +P49723 YGR180C RNR4 332 Phosphoserine +P49723 YGR180C RNR4 334 Phosphothreonine +P49723 YGR180C RNR4 336 Phosphoserine +P49723 YGR180C RNR4 337 Glycyl +P38145 YBR256C RIB5 95 Phosphoserine +Q00245 YIL118W RHO3 228 Cysteine +Q00245 YIL118W RHO3 228 S-farnesyl +P53879 YNL180C RHO5 223 Phosphoserine +P53879 YNL180C RHO5 228 Phosphoserine +P53879 YNL180C RHO5 232 Phosphothreonine +P53879 YNL180C RHO5 244 Phosphothreonine +P53879 YNL180C RHO5 328 Cysteine +P53879 YNL180C RHO5 328 S-geranylgeranyl +P53879 YNL180C RHO5 276 Glycyl +P09938 YJL026W RNR2 15 Phosphoserine +P09938 YJL026W RNR2 24 Phosphoserine +P09938 YJL026W RNR2 41 Phosphoserine +P21672 YIL066C RNR3 227 Phosphoserine +P21672 YIL066C RNR3 806 Phosphoserine +P21672 YIL066C RNR3 827 Phosphoserine +P21672 YIL066C RNR3 868 Phosphoserine +P21672 YIL066C RNR3 387 Glycyl +P26784 YIL133C RPL16A 2 N-acetylserine +P26784 YIL133C RPL16A 44 Phosphoserine +P26784 YIL133C RPL16A 188 Phosphoserine +P26784 YIL133C RPL16A 177 Glycyl +Q99258 YDR487C RIB3 3 Phosphothreonine +P29539 YBR275C RIF1 97 Phosphoserine +P29539 YBR275C RIF1 1637 Phosphoserine +P29539 YBR275C RIF1 1795 Phosphoserine +P29539 YBR275C RIF1 1852 Phosphoserine +P38883 YHR197W RIX1 2 N-acetylserine +P0CX53 YEL054C RPL12A 2 N%2CN-dimethylproline%3B +P0CX53 YEL054C RPL12A 4 N6%2CN6%2CN6-trimethyllysine%3B +P0CX53 YEL054C RPL12A 11 N6%2CN6%2CN6-trimethyllysine%3B +P0CX53 YEL054C RPL12A 25 Phosphoserine +P0CX53 YEL054C RPL12A 38 Phosphoserine +P0CX53 YEL054C RPL12A 67 N5-methylarginine%3B +P0CX53 YEL054C RPL12A 130 Glycyl +P0CX53 YEL054C RPL12A 146 Glycyl +Q12690 YDL082W RPL13A 144 Phosphothreonine +Q12690 YDL082W RPL13A 152 Phosphothreonine +Q00246 YKR055W RHO4 264 Phosphoserine +Q00246 YKR055W RHO4 268 Phosphoserine +Q00246 YKR055W RHO4 276 Phosphoserine +Q00246 YKR055W RHO4 288 Cysteine +Q00246 YKR055W RHO4 288 S-farnesyl +P38615 YMR139W RIM11 199 Phosphotyrosine +Q12196 YOR119C RIO1 402 Phosphoserine%3B +Q12196 YOR119C RIO1 403 Phosphoserine%3B +Q12196 YOR119C RIO1 409 Phosphoserine%3B +Q12196 YOR119C RIO1 416 Phosphoserine%3B +Q12196 YOR119C RIO1 417 Phosphoserine%3B +Q12196 YOR119C RIO1 419 Phosphoserine%3B +P41805 YLR075W RPL10 143 Phosphoserine +P41805 YLR075W RPL10 205 Phosphoserine +P41805 YLR075W RPL10 40 Glycyl +P41805 YLR075W RPL10 101 Glycyl +P38741 YHL024W RIM4 525 Phosphoserine +P0C0W9 YPR102C RPL11A 2 N-acetylserine +P0C0W9 YPR102C RPL11A 75 N6%2CN6%2CN6-trimethyllysine +P0CX54 YDR418W RPL12B 2 N%2CN-dimethylproline%3B +P0CX54 YDR418W RPL12B 4 N6%2CN6%2CN6-trimethyllysine%3B +P0CX54 YDR418W RPL12B 11 N6%2CN6%2CN6-trimethyllysine%3B +P0CX54 YDR418W RPL12B 25 Phosphoserine +P0CX54 YDR418W RPL12B 38 Phosphoserine +P0CX54 YDR418W RPL12B 67 N5-methylarginine%3B +P0CX54 YDR418W RPL12B 130 Glycyl +P0CX54 YDR418W RPL12B 146 Glycyl +P0CX44 YGL135W RPL1B 2 N-acetylserine +P0CX44 YGL135W RPL1B 47 N6-methyllysine%3B +P0CX44 YGL135W RPL1B 79 Phosphoserine +P0CX44 YGL135W RPL1B 86 Phosphoserine +P0CX23 YMR242C RPL20A 32 Phosphoserine +P0CX23 YMR242C RPL20A 125 Glycyl +P0CX23 YMR242C RPL20A 131 Glycyl +P0CX23 YMR242C RPL20A 149 Glycyl +P24000 YGR148C RPL24B 7 Phosphoserine +P0CX46 YIL018W RPL2B 52 Phosphoserine +P0CX46 YIL018W RPL2B 95 Phosphoserine +P0CX46 YIL018W RPL2B 159 Phosphoserine +P0CX46 YIL018W RPL2B 160 Phosphoserine +P0CX46 YIL018W RPL2B 249 Phosphoserine +P0CX46 YIL018W RPL2B 46 Glycyl +P0CX46 YIL018W RPL2B 93 Glycyl +P0CX46 YIL018W RPL2B 119 Glycyl +P0CX46 YIL018W RPL2B 145 Glycyl +P0CX45 YFR031C-A RPL2A 52 Phosphoserine +P0CX45 YFR031C-A RPL2A 95 Phosphoserine +P0CX45 YFR031C-A RPL2A 159 Phosphoserine +P0CX45 YFR031C-A RPL2A 160 Phosphoserine +P0CX45 YFR031C-A RPL2A 249 Phosphoserine +P0CX45 YFR031C-A RPL2A 46 Glycyl +P0CX45 YFR031C-A RPL2A 93 Glycyl +P0CX45 YFR031C-A RPL2A 119 Glycyl +P0CX45 YFR031C-A RPL2A 145 Glycyl +P14120 YGL030W RPL30 22 Glycyl +P14120 YGL030W RPL30 53 Glycyl +P14120 YGL030W RPL30 83 Glycyl +P05744 YPL143W RPL33A 2 N-acetylalanine%3B +P05744 YPL143W RPL33A 47 Glycyl +P0CX84 YDL191W RPL35A 13 Phosphoserine +P0CX84 YDL191W RPL35A 50 Phosphoserine +P05745 YMR194W RPL36A 2 N-acetylthreonine +P49626 YDR012W RPL4B 2 N-acetylserine +Q02753 YBR191W RPL21A 32 Glycyl +P0CX82 YBR084C-A RPL19A 30 Phosphoserine +P0CX82 YBR084C-A RPL19A 37 Phosphoserine +P0CX82 YBR084C-A RPL19A 91 Phosphoserine +P0CX82 YBR084C-A RPL19A 21 Glycyl +P0CX82 YBR084C-A RPL19A 53 Glycyl +P0CX82 YBR084C-A RPL19A 60 Glycyl +P0CX82 YBR084C-A RPL19A 146 Glycyl +P0CX82 YBR084C-A RPL19A 186 Glycyl +P0CX83 YBL027W RPL19B 30 Phosphoserine +P0CX83 YBL027W RPL19B 37 Phosphoserine +P0CX83 YBL027W RPL19B 91 Phosphoserine +P0CX83 YBL027W RPL19B 21 Glycyl +P0CX83 YBL027W RPL19B 53 Glycyl +P0CX83 YBL027W RPL19B 60 Glycyl +P0CX83 YBL027W RPL19B 146 Glycyl +P0CX83 YBL027W RPL19B 186 Glycyl +P40212 YMR142C RPL13B 144 Phosphothreonine +P40212 YMR142C RPL13B 152 Phosphothreonine +P38754 YHL001W RPL14B 2 N-acetylserine +P05740 YKL180W RPL17A 70 Phosphothreonine +P05740 YKL180W RPL17A 46 Glycyl +P0CX50 YNL301C RPL18B 50 N6%2CN6%2CN6-trimethyllysine +P0CX50 YNL301C RPL18B 116 Glycyl +P0CX43 YPL220W RPL1A 2 N-acetylserine +P0CX43 YPL220W RPL1A 47 N6-methyllysine%3B +P0CX43 YPL220W RPL1A 79 Phosphoserine +P0CX43 YPL220W RPL1A 86 Phosphoserine +P04449 YGL031C RPL24A 7 Phosphoserine +P41056 YOR234C RPL33B 2 N-acetylalanine%3B +P41056 YOR234C RPL33B 47 Glycyl +P25367 YCL028W RNQ1 143 Phosphoserine +P25367 YCL028W RNQ1 5 Glycyl +P25367 YCL028W RNQ1 84 Glycyl +P39956 YER169W RPH1 399 Phosphothreonine +P39956 YER169W RPH1 430 Phosphoserine +P39956 YER169W RPH1 459 Phosphoserine +P39956 YER169W RPH1 557 Phosphoserine +P39956 YER169W RPH1 561 Phosphoserine +P39956 YER169W RPH1 575 Phosphoserine +P39956 YER169W RPH1 584 Phosphoserine +P39956 YER169W RPH1 652 Phosphoserine +P39956 YER169W RPH1 689 Phosphoserine +P35178 YDR087C RRP1 1 N-acetylmethionine +P35178 YDR087C RRP1 267 Phosphoserine +Q05022 YMR229C RRP5 47 Phosphothreonine +Q05022 YMR229C RRP5 187 Phosphoserine +Q05022 YMR229C RRP5 188 Phosphoserine +Q05022 YMR229C RRP5 1724 Phosphoserine +P25381 YCR045C RRT12 38 N-linked +P25381 YCR045C RRT12 64 N-linked +P25381 YCR045C RRT12 106 N-linked +P25381 YCR045C RRT12 121 N-linked +P25381 YCR045C RRT12 268 N-linked +P25381 YCR045C RRT12 356 N-linked +P25381 YCR045C RRT12 449 N-linked +P36121 YKR025W RPC37 61 Phosphothreonine +P32565 YIL075C RPN2 2 N-acetylserine +P32565 YIL075C RPN2 801 Phosphothreonine +P32565 YIL075C RPN2 932 Phosphothreonine +Q03305 YDR465C RMT2 181 Phosphoserine +Q03305 YDR465C RMT2 184 Phosphoserine +P22138 YPR010C RPA135 2 N-acetylserine +P22138 YPR010C RPA135 81 Phosphoserine +P22138 YPR010C RPA135 1156 Phosphoserine +P20435 YPR187W RPO26 24 Phosphoserine +P28000 YNL113W RPC19 15 Phosphothreonine +P28000 YNL113W RPC19 33 Phosphothreonine +P28000 YNL113W RPC19 134 Glycyl +P04050 YDL140C RPO21 1471 Phosphothreonine +P04050 YDL140C RPO21 695 Glycyl +P04050 YDL140C RPO21 1246 Glycyl +P04050 YDL140C RPO21 1350 Glycyl +P20433 YJL140W RPB4 1 N-acetylmethionine +P20433 YJL140W RPB4 91 Phosphothreonine +P20433 YJL140W RPB4 92 Phosphothreonine +P50106 YDR156W RPA14 121 Phosphoserine +P32349 YPR190C RPC82 27 Phosphothreonine +P32349 YPR190C RPC82 392 Phosphoserine +P32349 YPR190C RPC82 394 Phosphoserine +P17890 YNL151C RPC31 189 Phosphoserine +P35718 YKL144C RPC25 162 Phosphoserine +Q12377 YDL097C RPN6 2 N-acetylserine +Q06506 YPR137W RRP9 2 N-acetylserine +Q06506 YPR137W RRP9 50 Phosphoserine +P0CX48 YBR048W RPS11B 2 N-acetylserine +P0CX48 YBR048W RPS11B 15 Glycyl +P0CX48 YBR048W RPS11B 46 Glycyl +P0CX48 YBR048W RPS11B 56 Glycyl +P0CX48 YBR048W RPS11B 57 Glycyl +P0CX48 YBR048W RPS11B 79 Glycyl +P0CX48 YBR048W RPS11B 96 Glycyl +P0CX48 YBR048W RPS11B 105 Glycyl +P0CX48 YBR048W RPS11B 133 Glycyl +P0CX48 YBR048W RPS11B 141 Glycyl +P0CX48 YBR048W RPS11B 148 Glycyl +P40693 YNL002C RLP7 2 N-acetylserine +P40693 YNL002C RLP7 14 Phosphoserine +P40693 YNL002C RLP7 120 Phosphothreonine +P40693 YNL002C RLP7 278 Phosphoserine +Q02805 YOR018W ROD1 138 Phosphoserine +Q02805 YOR018W ROD1 141 Phosphoserine +Q02805 YOR018W ROD1 436 Phosphoserine +Q02805 YOR018W ROD1 536 Phosphoserine +Q02805 YOR018W ROD1 720 Phosphoserine +Q02805 YOR018W ROD1 725 Phosphoserine +Q02805 YOR018W ROD1 401 Glycyl +P53046 YGR070W ROM1 1 N-acetylmethionine +P53046 YGR070W ROM1 154 Phosphoserine +P53046 YGR070W ROM1 155 Phosphoserine +P53046 YGR070W ROM1 180 Phosphothreonine +P53046 YGR070W ROM1 433 Phosphoserine +Q03691 YMR200W ROT1 103 N-linked +Q03691 YMR200W ROT1 107 N-linked +Q03691 YMR200W ROT1 139 N-linked +P47006 YJL148W RPA34 10 Phosphoserine +P47006 YJL148W RPA34 12 Phosphoserine +P47006 YJL148W RPA34 14 Phosphoserine +P47006 YJL148W RPA34 60 Phosphoserine +P46669 YOR340C RPA43 244 Phosphoserine +P46669 YOR340C RPA43 251 Phosphoserine +P46669 YOR340C RPA43 265 Phosphoserine +P46669 YOR340C RPA43 269 Phosphoserine +P46669 YOR340C RPA43 285 Phosphoserine +P20436 YOR224C RPB8 2 N-acetylserine +P20436 YOR224C RPB8 68 Phosphothreonine +P22139 YOR210W RPB10 59 Glycyl +P25441 YDL150W RPC53 137 Phosphoserine +P25441 YDL150W RPC53 138 Phosphoserine +P25441 YDL150W RPC53 178 Phosphoserine +P25441 YDL150W RPC53 182 Phosphoserine +P25441 YDL150W RPC53 224 Phosphoserine +P25441 YDL150W RPC53 228 Phosphothreonine +P25441 YDL150W RPC53 232 Phosphothreonine +Q12754 YPL012W RRP12 1059 Phosphoserine +Q12754 YPL012W RRP12 1067 Phosphoserine +Q06511 YPR143W RRP15 69 Phosphoserine +P25359 YCR035C RRP43 2 N-acetylalanine +P25359 YCR035C RRP43 26 Phosphoserine +Q01855 YOL040C RPS15 2 N-acetylserine +Q01855 YOL040C RPS15 24 Glycyl +Q01855 YOL040C RPS15 35 Glycyl +Q01855 YOL040C RPS15 64 Glycyl +P38701 YHL015W RPS20 2 N-acetylserine +P38701 YHL015W RPS20 6 Glycyl +P38701 YHL015W RPS20 8 Glycyl +P38701 YHL015W RPS20 21 Glycyl +P38701 YHL015W RPS20 32 Glycyl +P38701 YHL015W RPS20 101 Glycyl +P0C0V8 YKR057W RPS21A 1 N-acetylmethionine +P08518 YOR151C RPB2 919 Phosphoserine +P32561 YNL330C RPD3 394 Phosphothreonine +P32561 YNL330C RPD3 408 Phosphoserine +P43588 YFR004W RPN11 1 N-acetylmethionine +P38764 YHR027C RPN1 16 Phosphoserine +P38764 YHR027C RPN1 19 Phosphoserine +P38764 YHR027C RPN1 24 Phosphothreonine +P38764 YHR027C RPN1 178 Phosphoserine +P38764 YHR027C RPN1 187 Phosphoserine +P38764 YHR027C RPN1 695 Phosphoserine +P40016 YER021W RPN3 2 N-acetylalanine +P40016 YER021W RPN3 454 Phosphoserine +P0CX47 YDR025W RPS11A 2 N-acetylserine +P0CX47 YDR025W RPS11A 15 Glycyl +P0CX47 YDR025W RPS11A 46 Glycyl +P0CX47 YDR025W RPS11A 56 Glycyl +P0CX47 YDR025W RPS11A 57 Glycyl +P0CX47 YDR025W RPS11A 79 Glycyl +P0CX47 YDR025W RPS11A 96 Glycyl +P0CX47 YDR025W RPS11A 105 Glycyl +P0CX47 YDR025W RPS11A 133 Glycyl +P0CX47 YDR025W RPS11A 141 Glycyl +P0CX47 YDR025W RPS11A 148 Glycyl +P36160 YKR081C RPF2 73 Phosphoserine +O13563 YLR421C RPN13 2 N-acetylserine +O13563 YLR421C RPN13 133 Phosphoserine +O13563 YLR421C RPN13 135 Phosphoserine +O13563 YLR421C RPN13 140 Phosphoserine +Q08723 YOR261C RPN8 2 N-acetylserine +Q08723 YOR261C RPN8 314 Phosphoserine +Q08723 YOR261C RPN8 317 Phosphoserine +Q08723 YOR261C RPN8 319 Phosphoserine +Q08723 YOR261C RPN8 327 Phosphothreonine +Q12532 YPL009C RQC2 797 Phosphoserine +Q04031 YDR412W RRP17 113 Phosphoserine +Q04031 YDR412W RRP17 116 Phosphoserine +Q04031 YDR412W RRP17 122 Phosphoserine +P38961 YDR083W RRP8 62 Phosphoserine +P36080 YKL082C RRP14 2 N-acetylserine +P40470 YIL127C RRT14 197 Phosphoserine +P40470 YIL127C RRT14 202 Phosphoserine +P40470 YIL127C RRT14 203 Phosphoserine +Q3E792 YGR027C RPS25A 2 N%2CN-dimethylproline%3B +P41058 YDL061C RPS29B 25 Phosphoserine +P26783 YJR123W RPS5 2 N-acetylserine +P26783 YJR123W RPS5 27 Phosphothreonine +P26783 YJR123W RPS5 45 Glycyl +P26783 YJR123W RPS5 203 Glycyl +P48164 YNL096C RPS7B 2 N-acetylserine +P48164 YNL096C RPS7B 10 Phosphoserine +P48164 YNL096C RPS7B 31 Phosphoserine +Q06488 YLR357W RSC2 612 Phosphotyrosine +Q06488 YLR357W RSC2 682 Phosphoserine +P43609 YFR037C RSC8 485 Phosphoserine +Q02950 YPL118W MRP51 327 Phosphoserine +Q03919 YDR139C RUB1 76 Glycyl +Q3E754 YJL136C RPS21B 1 N-acetylmethionine +P0CX31 YER074W RPS24A 2 N-acetylserine +P0CX31 YER074W RPS24A 14 Phosphoserine +P0CX31 YER074W RPS24A 56 Phosphoserine +P0CX31 YER074W RPS24A 21 Glycyl +Q08932 YPL193W RSA1 1 N-acetylmethionine +Q08932 YPL193W RSA1 172 Phosphoserine +P38781 YHR056C RSC30 150 Phosphoserine +Q03201 YDR041W RSM10 193 Phosphoserine +Q05468 YDR333C RQC1 119 Phosphoserine +Q05468 YDR333C RQC1 158 Phosphothreonine +Q05468 YDR333C RQC1 160 Phosphoserine +Q04225 YMR131C RRB1 5 Phosphoserine +P38766 YHR031C RRM3 64 Phosphoserine +P38712 YHR065C RRP3 43 Phosphoserine +P38712 YHR065C RRP3 45 Phosphoserine +P38712 YHR065C RRP3 47 Phosphoserine +P48589 YOR369C RPS12 85 Glycyl +P48589 YOR369C RPS12 95 Glycyl +P48589 YOR369C RPS12 114 Glycyl +P23248 YML063W RPS1B 2 N-acetylalanine%3B +P23248 YML063W RPS1B 245 Phosphoserine +P23248 YML063W RPS1B 254 Phosphothreonine +P23248 YML063W RPS1B 248 Glycyl +P0CX52 YDL083C RPS16B 2 N-acetylserine +P0CX52 YDL083C RPS16B 34 Phosphoserine +P0CX52 YDL083C RPS16B 61 Phosphoserine +P0CX52 YDL083C RPS16B 70 Phosphothreonine +P0CX52 YDL083C RPS16B 76 Phosphoserine +P0CX52 YDL083C RPS16B 30 Glycyl +P0CX52 YDL083C RPS16B 47 Glycyl +P0CX52 YDL083C RPS16B 59 Glycyl +P0CX56 YML026C RPS18B 2 N-acetylserine +P0CX56 YML026C RPS18B 48 N6-methyllysine%3B +P0CX56 YML026C RPS18B 36 Glycyl +P0CX56 YML026C RPS18B 49 Glycyl +P0CX56 YML026C RPS18B 80 Glycyl +P0CX56 YML026C RPS18B 96 Glycyl +P0CX29 YGR118W RPS23A 64 3%2C4-dihydroxyproline +P0CX29 YGR118W RPS23A 56 Glycyl +P0CX32 YIL069C RPS24B 2 N-acetylserine +P0CX32 YIL069C RPS24B 14 Phosphoserine +P0CX32 YIL069C RPS24B 56 Phosphoserine +P0CX32 YIL069C RPS24B 21 Glycyl +P0C0T4 YLR333C RPS25B 2 N%2CN-dimethylproline%3B +P0CX35 YJR145C RPS4A 32 Phosphoserine +P0CX35 YJR145C RPS4A 115 Phosphothreonine +P0CX35 YJR145C RPS4A 247 Phosphoserine +P0CX35 YJR145C RPS4A 62 Glycyl +P0CX35 YJR145C RPS4A 134 Glycyl +P0CX35 YJR145C RPS4A 161 Glycyl +P0CX35 YJR145C RPS4A 168 Glycyl +P0CX35 YJR145C RPS4A 174 Glycyl +P0CX35 YJR145C RPS4A 179 Glycyl +P0CX35 YJR145C RPS4A 211 Glycyl +P0CX35 YJR145C RPS4A 233 Glycyl +P32832 YMR091C NPL6 86 Phosphoserine +Q03124 YML127W RSC9 44 Phosphoserine +P38792 YHR069C RRP4 2 N-acetylserine +P38792 YHR069C RRP4 28 Phosphoserine +P38792 YHR069C RRP4 268 Phosphoserine +Q12149 YOR001W RRP6 138 Phosphoserine +Q12149 YOR001W RRP6 520 Phosphothreonine +Q12149 YOR001W RRP6 640 Phosphoserine +Q12149 YOR001W RRP6 645 Phosphoserine +P35997 YKL156W RPS27A 40 S-methylcysteine +P0C0X0 YLR264W RPS28B 1 N-acetylmethionine +P25443 YGL123W RPS2 2 N-acetylserine +P25443 YGL123W RPS2 11 Asymmetric +P25443 YGL123W RPS2 11 Omega-N-methylarginine%3B +P25443 YGL123W RPS2 33 Glycyl +P0CX34 YOR182C RPS30B 16 Phosphoserine +P0CX34 YOR182C RPS30B 48 Phosphothreonine +Q05942 YLR221C RSA3 83 Phosphoserine +Q05942 YLR221C RSA3 88 Phosphothreonine +Q05942 YLR221C RSA3 99 Phosphoserine +P53236 YGR056W RSC1 670 Phosphoserine +Q02206 YKR008W RSC4 199 Phosphoserine +Q02206 YKR008W RSC4 545 Phosphoserine +P33442 YLR441C RPS1A 2 N-acetylalanine%3B +P33442 YLR441C RPS1A 245 Phosphothreonine +P33442 YLR441C RPS1A 254 Phosphothreonine +P33442 YLR441C RPS1A 248 Glycyl +P0CX37 YPL090C RPS6A 163 Phosphothreonine +P0CX37 YPL090C RPS6A 116 Glycyl +P0CX37 YPL090C RPS6A 131 Glycyl +P0CX37 YPL090C RPS6A 149 Glycyl +P0CX37 YPL090C RPS6A 214 Glycyl +P0CX40 YER102W RPS8B 62 Phosphothreonine +P0CX40 YER102W RPS8B 66 Phosphoserine +P0CX40 YER102W RPS8B 69 Phosphoserine +P0CX40 YER102W RPS8B 73 Phosphoserine +P0CX40 YER102W RPS8B 86 Phosphoserine +P0CX40 YER102W RPS8B 107 Phosphothreonine +P0CX40 YER102W RPS8B 154 Phosphoserine +P0CX40 YER102W RPS8B 155 Phosphoserine +P0CX40 YER102W RPS8B 158 Phosphoserine +P0CX40 YER102W RPS8B 161 Phosphoserine +Q08417 YOR049C RSB1 3 N-linked +Q08417 YOR049C RSB1 6 N-linked +P46974 YJR127C RSF2 231 Phosphoserine +P46974 YJR127C RSF2 322 Phosphoserine +P46974 YJR127C RSF2 544 Phosphoserine +P46974 YJR127C RSF2 632 Phosphoserine +Q03516 YMR266W RSN1 949 Phosphoserine +P32905 YGR214W RPS0A 2 N-acetylserine +P40161 YNL206C RTT106 2 N-acetylserine +P40161 YNL206C RTT106 408 Phosphoserine +P40161 YNL206C RTT106 411 Phosphoserine +P40161 YNL206C RTT106 450 Phosphoserine +P53064 YGL244W RTF1 17 Phosphoserine +P53064 YGL244W RTF1 69 Phosphotyrosine +P53064 YGL244W RTF1 71 Phosphoserine +P53064 YGL244W RTF1 477 Phosphoserine +P0CX30 YPR132W RPS23B 64 3%2C4-dihydroxyproline +P0CX30 YPR132W RPS23B 56 Glycyl +P41057 YLR388W RPS29A 25 Phosphoserine +P05750 YNL178W RPS3 44 Phosphothreonine +P05750 YNL178W RPS3 70 Phosphothreonine +P05750 YNL178W RPS3 97 Phosphoserine +P05750 YNL178W RPS3 129 Phosphoserine +P05750 YNL178W RPS3 146 Omega-N-methylarginine%3B +P05750 YNL178W RPS3 221 Phosphoserine +P05750 YNL178W RPS3 231 Phosphothreonine +P05750 YNL178W RPS3 106 Glycyl +P05750 YNL178W RPS3 132 Glycyl +P05750 YNL178W RPS3 141 Glycyl +P05750 YNL178W RPS3 151 Glycyl +P05750 YNL178W RPS3 200 Glycyl +P05750 YNL178W RPS3 212 Glycyl +O13516 YPL081W RPS9A 184 Phosphoserine +O13516 YPL081W RPS9A 180 Glycyl +Q12481 YOR287C RRP36 14 Phosphoserine +Q12481 YOR287C RRP36 41 Phosphoserine +Q12481 YOR287C RRP36 42 Phosphoserine +P05756 YDR064W RPS13 32 Phosphoserine +P05756 YDR064W RPS13 39 Glycyl +P05756 YDR064W RPS13 43 Glycyl +P06367 YCR031C RPS14A 2 N-acetylserine +P05759 YLR167W RPS31 122 Phosphoserine +P05759 YLR167W RPS31 76 Glycyl +P0CX51 YMR143W RPS16A 2 N-acetylserine +P0CX51 YMR143W RPS16A 34 Phosphoserine +P0CX51 YMR143W RPS16A 61 Phosphoserine +P0CX51 YMR143W RPS16A 70 Phosphothreonine +P0CX51 YMR143W RPS16A 76 Phosphoserine +P0CX51 YMR143W RPS16A 30 Glycyl +P0CX51 YMR143W RPS16A 47 Glycyl +P0CX51 YMR143W RPS16A 59 Glycyl +P0CX55 YDR450W RPS18A 2 N-acetylserine +P0CX55 YDR450W RPS18A 48 N6-methyllysine%3B +P0CX55 YDR450W RPS18A 36 Glycyl +P0CX55 YDR450W RPS18A 49 Glycyl +P0CX55 YDR450W RPS18A 80 Glycyl +P0CX55 YDR450W RPS18A 96 Glycyl +Q3E7X9 YOR167C RPS28A 1 N-acetylmethionine +P0CX33 YLR287C-A RPS30A 16 Phosphoserine +P0CX33 YLR287C-A RPS30A 48 Phosphothreonine +P0CX36 YHR203C RPS4B 32 Phosphoserine +P0CX36 YHR203C RPS4B 115 Phosphothreonine +P0CX36 YHR203C RPS4B 247 Phosphoserine +P0CX36 YHR203C RPS4B 62 Glycyl +P0CX36 YHR203C RPS4B 134 Glycyl +P0CX36 YHR203C RPS4B 161 Glycyl +P0CX36 YHR203C RPS4B 168 Glycyl +P0CX36 YHR203C RPS4B 174 Glycyl +P0CX36 YHR203C RPS4B 179 Glycyl +P0CX36 YHR203C RPS4B 211 Glycyl +P0CX36 YHR203C RPS4B 233 Glycyl +P0CX38 YBR181C RPS6B 163 Phosphothreonine +P0CX38 YBR181C RPS6B 116 Glycyl +P0CX38 YBR181C RPS6B 131 Glycyl +P0CX38 YBR181C RPS6B 149 Glycyl +P0CX38 YBR181C RPS6B 214 Glycyl +P0CX39 YBL072C RPS8A 62 Phosphothreonine +P0CX39 YBL072C RPS8A 66 Phosphoserine +P0CX39 YBL072C RPS8A 69 Phosphoserine +P0CX39 YBL072C RPS8A 73 Phosphoserine +P0CX39 YBL072C RPS8A 86 Phosphoserine +P0CX39 YBL072C RPS8A 107 Phosphothreonine +P0CX39 YBL072C RPS8A 154 Phosphoserine +P0CX39 YBL072C RPS8A 155 Phosphoserine +P0CX39 YBL072C RPS8A 158 Phosphoserine +P0CX39 YBL072C RPS8A 161 Phosphoserine +P05755 YBR189W RPS9B 184 Phosphoserine +P05755 YBR189W RPS9B 180 Glycyl +Q06639 YDR303C RSC3 95 Phosphoserine +Q06639 YDR303C RSC3 236 Phosphoserine +P38165 YBL103C RTG3 81 Phosphoserine +P38165 YBL103C RTG3 123 Phosphoserine +P38165 YBL103C RTG3 142 Phosphoserine +P38165 YBL103C RTG3 150 Phosphothreonine +P38165 YBL103C RTG3 227 Phosphoserine +P38165 YBL103C RTG3 236 Phosphoserine +P38165 YBL103C RTG3 241 Phosphoserine +P38165 YBL103C RTG3 269 Phosphoserine +Q12443 YDL204W RTN2 278 Phosphoserine +Q12443 YDL204W RTN2 137 N-linked +P26786 YOR096W RPS7A 2 N-acetylserine +P26786 YOR096W RPS7A 124 Glycyl +P38850 YHR154W RTT107 304 Phosphoserine +P38850 YHR154W RTT107 532 Phosphothreonine +P38850 YHR154W RTT107 591 Phosphoserine +P38850 YHR154W RTT107 593 Phosphoserine +P38850 YHR154W RTT107 720 Phosphoserine +P38850 YHR154W RTT107 800 Phosphoserine +P38850 YHR154W RTT107 806 Phosphoserine +Q08281 YOL138C RTC1 1036 Phosphoserine +Q08281 YOL138C RTC1 1080 Phosphoserine +Q08281 YOL138C RTC1 1087 Phosphoserine +Q08281 YOL138C RTC1 1089 Phosphoserine +Q08281 YOL138C RTC1 1123 Phosphoserine +Q08281 YOL138C RTC1 1133 Phosphoserine +P53330 YGR275W RTT102 77 Phosphoserine +P53330 YGR275W RTT102 122 Phosphoserine +P53850 YNL254C RTC4 23 Phosphoserine +Q04947 YDR233C RTN1 186 Phosphothreonine +Q04947 YDR233C RTN1 219 Phosphothreonine +Q04947 YDR233C RTN1 232 Phosphoserine +P20606 YPL218W SAR1 155 Phosphothreonine +P20606 YPL218W SAR1 157 Phosphoserine +P20606 YPL218W SAR1 133 Glycyl +P28707 YKL117W SBA1 2 N-acetylserine +P06105 YJL080C SCP160 50 Phosphothreonine +P06105 YJL080C SCP160 54 Phosphoserine +P06105 YJL080C SCP160 63 Phosphoserine +P06105 YJL080C SCP160 85 Phosphoserine +P06105 YJL080C SCP160 87 Phosphoserine +P06105 YJL080C SCP160 89 Phosphoserine +P06105 YJL080C SCP160 630 Phosphoserine +P06105 YJL080C SCP160 1112 Phosphoserine +P40541 YIL026C IRR1 28 Phosphoserine +P40541 YIL026C IRR1 628 Phosphoserine +P11792 YHR205W SCH9 570 Phosphothreonine%3B +P11792 YHR205W SCH9 711 Phosphoserine%3B +P11792 YHR205W SCH9 723 Phosphothreonine%3B +P11792 YHR205W SCH9 726 Phosphoserine%3B +P11792 YHR205W SCH9 737 Phosphothreonine%3B +P11792 YHR205W SCH9 758 Phosphoserine%3B +P11792 YHR205W SCH9 765 Phosphoserine%3B +P32607 YOL067C RTG1 50 Phosphoserine +P32607 YOL067C RTG1 52 Phosphoserine +P32607 YOL067C RTG1 60 Phosphothreonine +Q03940 YDR190C RVB1 2 N-acetylvaline +Q12158 YDL003W MCD1 161 Phosphoserine +Q12158 YDL003W MCD1 175 Phosphoserine%3B +Q12158 YDL003W MCD1 210 N6-acetyllysine%3B +Q12158 YDL003W MCD1 263 Phosphoserine%3B +Q12158 YDL003W MCD1 307 Phosphoserine +Q12158 YDL003W MCD1 354 Phosphothreonine +P34758 YOR329C SCD5 564 Phosphoserine +P43612 YFR040W SAP155 58 Phosphoserine +P43612 YFR040W SAP155 255 Phosphoserine +P43612 YFR040W SAP155 613 Phosphothreonine +P43612 YFR040W SAP155 618 Phosphothreonine +P17121 YDR389W SAC7 37 Phosphoserine +P17121 YDR389W SAC7 46 Phosphoserine +P17121 YDR389W SAC7 435 Phosphoserine +P17121 YDR389W SAC7 491 Phosphoserine +P17121 YDR389W SAC7 632 Phosphoserine +Q12136 YDL153C SAS10 12 Phosphoserine +Q12136 YDL153C SAS10 314 Phosphoserine +Q12136 YDL153C SAS10 316 Phosphoserine +Q12136 YDL153C SAS10 336 Phosphoserine +Q12136 YDL153C SAS10 339 Phosphoserine +Q12136 YDL153C SAS10 477 Phosphoserine +Q04002 YDR180W SCC2 43 Phosphoserine%3B +Q04002 YDR180W SCC2 67 Phosphothreonine +Q04002 YDR180W SCC2 74 Phosphoserine%3B +Q04002 YDR180W SCC2 127 Phosphoserine +Q04002 YDR180W SCC2 157 Phosphoserine +Q04002 YDR180W SCC2 162 Phosphoserine%3B +Q04002 YDR180W SCC2 163 Phosphoserine +Q04002 YDR180W SCC2 231 Phosphothreonine +Q04002 YDR180W SCC2 236 Phosphothreonine +Q04002 YDR180W SCC2 305 Phosphoserine +Q04002 YDR180W SCC2 320 Phosphoserine +Q04002 YDR180W SCC2 360 Phosphothreonine%3B +Q04002 YDR180W SCC2 753 Phosphoserine +Q04002 YDR180W SCC2 1179 Phosphoserine%3B +Q04002 YDR180W SCC2 1182 Phosphoserine +Q04002 YDR180W SCC2 1183 Phosphoserine%3B +Q04002 YDR180W SCC2 1185 Phosphoserine +P45978 YPR129W SCD6 2 N-acetylserine +Q04951 YMR305C SCW10 279 N-linked +P13856 YGR152C RSR1 269 Cysteine +P13856 YGR152C RSR1 269 S-geranylgeranyl +P46654 YLR048W RPS0B 2 N-acetylserine +Q12100 YDL025C RTK1 58 Phosphothreonine +Q12100 YDL025C RTK1 60 Phosphoserine +Q12100 YDL025C RTK1 216 Phosphoserine +Q12100 YDL025C RTK1 334 Glycyl +P53289 YGR161C RTS3 172 Phosphoserine +P53289 YGR161C RTS3 192 Phosphoserine +P53289 YGR161C RTS3 214 Phosphoserine +P53289 YGR161C RTS3 238 Phosphoserine +Q12242 YOR138C RUP1 56 Phosphoserine +P39743 YDR388W RVS167 2 N-acetylserine +P39743 YDR388W RVS167 299 Phosphoserine%3B +P39743 YDR388W RVS167 321 Phosphoserine%3B +P39743 YDR388W RVS167 379 Phosphoserine%3B +P39743 YDR388W RVS167 242 Glycyl +P39743 YDR388W RVS167 481 Glycyl +P40856 YJL098W SAP185 20 Glycyl +P38352 YBR280C SAF1 16 Phosphoserine +P38352 YBR280C SAF1 266 Phosphoserine +P20840 YJR004C SAG1 627 GPI-anchor +P20840 YJR004C SAG1 79 N-linked +P20840 YJR004C SAG1 109 N-linked +P20840 YJR004C SAG1 135 N-linked +P20840 YJR004C SAG1 248 N-linked +P20840 YJR004C SAG1 282 O-linked +P20840 YJR004C SAG1 289 O-linked +P20840 YJR004C SAG1 299 O-linked +P20840 YJR004C SAG1 303 O-linked +P20840 YJR004C SAG1 306 N-linked +P20840 YJR004C SAG1 307 O-linked +P20840 YJR004C SAG1 308 O-linked +P20840 YJR004C SAG1 311 O-linked +P20840 YJR004C SAG1 314 O-linked +P20840 YJR004C SAG1 315 O-linked +P20840 YJR004C SAG1 316 O-linked +P20840 YJR004C SAG1 329 O-linked +P20840 YJR004C SAG1 331 O-linked +P20840 YJR004C SAG1 334 O-linked +P20840 YJR004C SAG1 335 O-linked +P20840 YJR004C SAG1 338 O-linked +P20840 YJR004C SAG1 339 O-linked +P20840 YJR004C SAG1 340 O-linked +P20840 YJR004C SAG1 341 O-linked +P20840 YJR004C SAG1 342 O-linked +P20840 YJR004C SAG1 345 O-linked +P20840 YJR004C SAG1 346 O-linked +P20840 YJR004C SAG1 349 O-linked +P20840 YJR004C SAG1 350 O-linked +P20840 YJR004C SAG1 364 N-linked +P20840 YJR004C SAG1 402 N-linked +P20840 YJR004C SAG1 460 N-linked +P20840 YJR004C SAG1 485 N-linked +P20840 YJR004C SAG1 501 N-linked +P20840 YJR004C SAG1 614 N-linked +P39954 YER043C SAH1 2 N-acetylserine +P39954 YER043C SAH1 393 Phosphothreonine +P39954 YER043C SAH1 21 Glycyl +P39954 YER043C SAH1 413 Glycyl +Q08985 YPL273W SAM4 138 Phosphothreonine +Q08873 YOR367W SCP1 2 N-acetylserine +Q08873 YOR367W SCP1 11 Phosphoserine +P40075 YER120W SCS2 2 N-acetylserine +P40075 YER120W SCS2 106 Phosphoserine +P40357 YGR009C SEC9 79 Phosphoserine +P40357 YGR009C SEC9 92 Phosphoserine +P40357 YGR009C SEC9 186 Phosphoserine +P40357 YGR009C SEC9 190 Phosphoserine +P40357 YGR009C SEC9 213 Phosphoserine +P40357 YGR009C SEC9 271 Phosphoserine +P40357 YGR009C SEC9 273 Phosphoserine +P40357 YGR009C SEC9 315 Phosphoserine +P40357 YGR009C SEC9 355 Phosphothreonine +P40357 YGR009C SEC9 359 Phosphoserine +Q01589 YDR077W SED1 318 GPI-anchor +Q01589 YDR077W SED1 22 N-linked +Q01589 YDR077W SED1 56 N-linked +Q01589 YDR077W SED1 78 N-linked +Q01589 YDR077W SED1 92 N-linked +Q01589 YDR077W SED1 114 N-linked +Q01589 YDR077W SED1 136 N-linked +Q01589 YDR077W SED1 152 N-linked +P34228 YBL066C SEF1 8 Phosphoserine +P34228 YBL066C SEF1 263 Phosphoserine +P34228 YBL066C SEF1 806 Phosphoserine +P36123 YKR028W SAP190 774 Phosphoserine +P36123 YKR028W SAP190 857 Phosphoserine +P36123 YKR028W SAP190 862 Phosphoserine +P36123 YKR028W SAP190 892 Phosphoserine +P36123 YKR028W SAP190 990 Phosphothreonine +P36123 YKR028W SAP190 991 Phosphoserine +P32368 YKL212W SAC1 246 Glycyl +P32368 YKL212W SAC1 358 Glycyl +P46674 YDR159W SAC3 568 Phosphoserine +P46674 YDR159W SAC3 748 N6-acetyllysine +P46674 YDR159W SAC3 866 Phosphoserine +P43589 YFR005C SAD1 1 N-acetylmethionine +Q08986 YPL274W SAM3 10 Phosphoserine +Q08986 YPL274W SAM3 27 Phosphoserine +Q08986 YPL274W SAM3 44 Phosphoserine +Q08986 YPL274W SAM3 184 N-linked +Q08986 YPL274W SAM3 243 N-linked +P53324 YGR263C SAY1 2 N-acetylalanine +P53324 YGR263C SAY1 85 N-linked +P53324 YGR263C SAY1 283 N-linked +P53324 YGR263C SAY1 401 N-linked +P38814 YHR103W SBE22 72 Phosphoserine +P38814 YHR103W SBE22 201 Phosphoserine +P38814 YHR103W SBE22 459 Phosphoserine +P38814 YHR103W SBE22 517 Phosphoserine +P38814 YHR103W SBE22 520 Phosphoserine +P42223 YDR351W SBE2 82 Phosphoserine +P42223 YDR351W SBE2 83 Phosphoserine +P42223 YDR351W SBE2 450 Phosphoserine +P42223 YDR351W SBE2 532 Phosphoserine +P36047 YKL193C SDS22 56 Phosphoserine +Q06245 YLR166C SEC10 142 Phosphoserine +Q06245 YLR166C SEC10 485 Phosphoserine +Q06245 YLR166C SEC10 507 Phosphoserine +P48415 YPL085W SEC16 28 Phosphoserine +P48415 YPL085W SEC16 73 Phosphoserine +P48415 YPL085W SEC16 144 Phosphoserine +P48415 YPL085W SEC16 313 Phosphoserine +P48415 YPL085W SEC16 472 Phosphoserine +P48415 YPL085W SEC16 483 Phosphoserine +P48415 YPL085W SEC16 595 Phosphothreonine +P48415 YPL085W SEC16 607 Phosphoserine +P48415 YPL085W SEC16 660 Phosphoserine +P48415 YPL085W SEC16 663 Phosphoserine +P48415 YPL085W SEC16 665 Phosphoserine +P48415 YPL085W SEC16 674 Phosphoserine +P48415 YPL085W SEC16 678 Phosphoserine +P48415 YPL085W SEC16 681 Phosphoserine +P48415 YPL085W SEC16 701 Phosphoserine +P48415 YPL085W SEC16 704 Phosphoserine +P48415 YPL085W SEC16 706 Phosphoserine +P48415 YPL085W SEC16 759 Phosphoserine +P48415 YPL085W SEC16 762 Phosphoserine +P48415 YPL085W SEC16 765 Phosphoserine +P48415 YPL085W SEC16 768 Phosphoserine +P48415 YPL085W SEC16 843 Phosphoserine +P48415 YPL085W SEC16 1511 Phosphoserine +P48415 YPL085W SEC16 1515 Phosphoserine +P48415 YPL085W SEC16 1578 Phosphoserine +P48415 YPL085W SEC16 1602 Phosphoserine +P48415 YPL085W SEC16 1603 Phosphoserine +P48415 YPL085W SEC16 1611 Phosphoserine +P48415 YPL085W SEC16 1617 Phosphoserine +P48415 YPL085W SEC16 1778 Phosphoserine +P48415 YPL085W SEC16 1875 Phosphoserine +P48415 YPL085W SEC16 1973 Phosphoserine +P48415 YPL085W SEC16 1986 Phosphoserine +P48415 YPL085W SEC16 1992 Phosphoserine +P48415 YPL085W SEC16 2049 Phosphothreonine +P48415 YPL085W SEC16 2130 Phosphoserine +P18759 YBR080C SEC18 226 Phosphoserine +P15303 YPR181C SEC23 1 N-acetylmethionine +P17065 YNL272C SEC2 1 N-acetylmethionine +P17065 YNL272C SEC2 168 Phosphothreonine +P17065 YNL272C SEC2 171 Phosphoserine +P17065 YNL272C SEC2 515 Phosphoserine +P38968 YDL195W SEC31 349 Phosphoserine +P38968 YDL195W SEC31 836 Phosphoserine +P38968 YDL195W SEC31 974 Phosphoserine +P38968 YDL195W SEC31 977 Phosphoserine +P38968 YDL195W SEC31 980 Phosphoserine +P38968 YDL195W SEC31 988 Phosphoserine +P38968 YDL195W SEC31 992 Phosphoserine +P38968 YDL195W SEC31 999 Phosphoserine +P38968 YDL195W SEC31 1050 Phosphothreonine +P38968 YDL195W SEC31 1053 Phosphoserine +P21825 YPL094C SEC62 2 N-acetylserine +P33754 YBR171W SEC66 5 N-linked +P33754 YBR171W SEC66 12 N-linked +Q05567 YDR294C DPL1 380 N6-(pyridoxal +Q07657 YDL225W SHS1 2 N-acetylserine +Q07657 YDL225W SHS1 400 Phosphotyrosine +Q07657 YDL225W SHS1 408 Phosphoserine +Q07657 YDL225W SHS1 416 Phosphoserine +Q07657 YDL225W SHS1 447 Phosphoserine +Q07657 YDL225W SHS1 460 Phosphoserine +Q07657 YDL225W SHS1 519 Phosphoserine +Q07657 YDL225W SHS1 520 Phosphoserine +Q07657 YDL225W SHS1 522 Phosphoserine +Q07657 YDL225W SHS1 525 Phosphoserine +Q07657 YDL225W SHS1 539 Phosphothreonine +Q07657 YDL225W SHS1 545 Phosphoserine +Q07657 YDL225W SHS1 548 Phosphoserine +Q07657 YDL225W SHS1 426 Glycyl +Q07657 YDL225W SHS1 437 Glycyl +P38717 YNL257C SIP3 1206 N-linked +P32900 YHR149C SKG6 137 Phosphoserine +P32900 YHR149C SKG6 169 Phosphothreonine +P32900 YHR149C SKG6 191 Phosphoserine +P32900 YHR149C SKG6 193 Phosphoserine +P32900 YHR149C SKG6 219 Phosphoserine +P32900 YHR149C SKG6 221 Phosphothreonine +P32900 YHR149C SKG6 222 Phosphoserine +P32900 YHR149C SKG6 251 Phosphoserine +P32900 YHR149C SKG6 369 Phosphoserine +P32900 YHR149C SKG6 672 Phosphoserine +P32900 YHR149C SKG6 717 Phosphoserine +P35207 YLR398C SKI2 209 Phosphoserine +Q08491 YOR076C SKI7 88 Phosphoserine +Q08491 YOR076C SKI7 90 Phosphoserine +P42843 YNL311C SKP2 594 Phosphothreonine +Q00772 YHR030C SLT2 190 Phosphothreonine +Q00772 YHR030C SLT2 192 Phosphotyrosine +P32566 YGR229C SMI1 202 Phosphoserine +P32566 YGR229C SMI1 203 Phosphoserine +P32566 YGR229C SMI1 376 Phosphothreonine +P32566 YGR229C SMI1 381 Phosphoserine +P32566 YGR229C SMI1 394 Phosphoserine +P32566 YGR229C SMI1 400 Phosphoserine +P32566 YGR229C SMI1 453 Glycyl +Q04174 YOR149C SMP3 403 N-linked +Q04174 YOR149C SMP3 452 N-linked +P38990 YER129W SAK1 43 Phosphothreonine +P38990 YER129W SAK1 964 Phosphoserine +P38990 YER129W SAK1 1126 Phosphoserine +P39955 YER047C SAP1 536 Phosphoserine +Q99314 YOR213C SAS5 144 Phosphoserine +Q00711 YKL148C SDH1 90 Tele-8alpha-FAD +P24280 YMR079W SEC14 302 Phosphoserine +P24280 YMR079W SEC14 42 Glycyl +P24280 YMR079W SEC14 84 Glycyl +P40510 YIL074C SER33 2 N-acetylserine +P40510 YIL074C SER33 22 Phosphoserine +P40510 YIL074C SER33 29 Phosphoserine +P40510 YIL074C SER33 33 Phosphoserine +P46995 YJL168C SET2 10 Phosphoserine +P46995 YJL168C SET2 522 Phosphoserine +Q08446 YOR057W SGT1 168 Phosphoserine +Q08446 YOR057W SGT1 171 Phosphoserine +Q08446 YOR057W SGT1 32 Glycyl +P38634 YLR079W SIC1 5 Phosphothreonine%3B +P38634 YLR079W SIC1 33 Phosphothreonine +P38634 YLR079W SIC1 76 Phosphoserine +P38634 YLR079W SIC1 173 Phosphothreonine +P38634 YLR079W SIC1 198 Phosphoserine +P38634 YLR079W SIC1 201 Phosphoserine +P38634 YLR079W SIC1 268 Lysine +P38634 YLR079W SIC1 272 Lysine +P38634 YLR079W SIC1 274 Lysine +P38262 YBR103W SIF2 137 Phosphoserine +Q06315 YLR187W SKG3 10 Phosphoserine +Q06315 YLR187W SKG3 31 Phosphoserine +Q06315 YLR187W SKG3 578 Phosphothreonine +Q06315 YLR187W SKG3 580 Phosphoserine +Q06315 YLR187W SKG3 592 Phosphoserine +Q06315 YLR187W SKG3 701 Phosphoserine +Q06315 YLR187W SKG3 954 Phosphoserine +P38314 YBR214W SDS24 94 Phosphoserine +P38314 YBR214W SDS24 458 Phosphoserine +P38314 YBR214W SDS24 524 Phosphoserine +P38164 YBL104C SEA4 123 Phosphoserine +P38164 YBL104C SEA4 136 Phosphoserine +P33332 YER008C SEC3 290 Phosphothreonine +P33332 YER008C SEC3 606 Phosphoserine +P89102 YDR166C SEC5 184 Phosphoserine +P38890 YHR207C SET5 517 Phosphoserine +P47166 YJR134C SGM1 2 N-acetylserine +P47166 YJR134C SGM1 151 Phosphoserine +P47166 YJR134C SGM1 538 Phosphoserine +P47166 YJR134C SGM1 549 Phosphoserine +P47166 YJR134C SGM1 568 Phosphoserine +P47166 YJR134C SGM1 571 Phosphoserine +P47166 YJR134C SGM1 576 Phosphoserine +P47166 YJR134C SGM1 589 Phosphoserine +P32578 YDR422C SIP1 33 Phosphoserine +P32578 YDR422C SIP1 181 Phosphoserine +P32578 YDR422C SIP1 198 Phosphoserine +P32578 YDR422C SIP1 200 Phosphoserine +P32578 YDR422C SIP1 206 Phosphoserine +P32578 YDR422C SIP1 209 Phosphoserine +P32578 YDR422C SIP1 220 Phosphoserine +P32578 YDR422C SIP1 331 Phosphoserine +P32578 YDR422C SIP1 494 Phosphoserine +P32578 YDR422C SIP1 497 Phosphoserine +P32578 YDR422C SIP1 643 Phosphoserine +P32578 YDR422C SIP1 2 N-myristoyl +P33336 YGR143W SKN1 56 Phosphoserine +P33336 YGR143W SKN1 65 Phosphoserine +P33336 YGR143W SKN1 67 Phosphoserine +P33336 YGR143W SKN1 92 Phosphoserine +P33336 YGR143W SKN1 103 Phosphoserine +P33336 YGR143W SKN1 142 Phosphoserine +P33336 YGR143W SKN1 162 Phosphoserine +P33336 YGR143W SKN1 165 Phosphoserine +P33336 YGR143W SKN1 170 Phosphoserine +P33336 YGR143W SKN1 176 Phosphoserine +P33336 YGR143W SKN1 337 N-linked +P33336 YGR143W SKN1 426 N-linked +P33336 YGR143W SKN1 513 N-linked +P33336 YGR143W SKN1 590 N-linked +P33336 YGR143W SKN1 615 N-linked +P33336 YGR143W SKN1 743 N-linked +Q03656 YMR216C SKY1 383 Phosphothreonine +Q03656 YMR216C SKY1 386 Phosphothreonine +Q03656 YMR216C SKY1 388 Phosphoserine +Q03656 YMR216C SKY1 393 Phosphoserine +Q03656 YMR216C SKY1 410 Phosphoserine +Q03656 YMR216C SKY1 427 Phosphoserine +Q03656 YMR216C SKY1 432 Phosphoserine +Q03656 YMR216C SKY1 445 Phosphoserine +Q03656 YMR216C SKY1 449 Phosphoserine +Q03656 YMR216C SKY1 453 Phosphoserine +P38283 YBR156C SLI15 268 Phosphoserine +P38283 YBR156C SLI15 489 Phosphoserine +P14906 YOR254C SEC63 512 Phosphoserine +Q04279 YMR086W SEG1 48 Phosphoserine +Q04279 YMR086W SEG1 220 Phosphoserine +Q04279 YMR086W SEG1 235 Phosphoserine +Q04279 YMR086W SEG1 238 Phosphoserine +Q04279 YMR086W SEG1 319 Phosphoserine +Q04279 YMR086W SEG1 339 Phosphoserine +Q04279 YMR086W SEG1 352 Phosphoserine +Q04279 YMR086W SEG1 434 Phosphoserine +Q04279 YMR086W SEG1 461 Phosphoserine +Q04279 YMR086W SEG1 467 Phosphothreonine +Q04279 YMR086W SEG1 630 Phosphoserine +Q04279 YMR086W SEG1 675 Phosphothreonine +Q04279 YMR086W SEG1 758 Phosphoserine +Q04279 YMR086W SEG1 816 Phosphoserine +Q04279 YMR086W SEG1 818 Phosphoserine +Q04279 YMR086W SEG1 855 Phosphoserine +P53011 YGL100W SEH1 257 Phosphoserine +O94742 YDR363W-A SEM1 2 N-acetylserine +O94742 YDR363W-A SEM1 12 Phosphoserine +P53953 YNL049C SFB2 51 Phosphoserine +P38166 YBL102W SFT2 2 N-acetylserine +P38166 YBL102W SFT2 60 Phosphoserine +P53965 YNL032W SIW14 94 Phosphoserine +Q04195 YDR409W SIZ1 132 Phosphoserine +Q04195 YDR409W SIZ1 794 Phosphoserine +Q3E784 YER180C-A SLO1 2 N-acetylserine +Q3E784 YER180C-A SLO1 10 Phosphoserine +Q02775 YDR088C SLU7 120 Phosphoserine +Q02775 YDR088C SLU7 212 Phosphothreonine +P40072 YER116C SLX8 50 Phosphoserine +P40072 YER116C SLX8 66 Phosphothreonine +P40072 YER116C SLX8 67 Phosphoserine +P11655 YNR026C SEC12 439 N-linked +P11655 YNR026C SEC12 462 N-linked +P22224 YGL233W SEC15 286 Phosphoserine +P22214 YLR268W SEC22 160 Phosphoserine +P07560 YFL005W SEC4 201 Phosphoserine +P07560 YFL005W SEC4 204 Phosphoserine +P07560 YFL005W SEC4 214 S-geranylgeranyl +P07560 YFL005W SEC4 215 S-geranylgeranyl +P11075 YDR170C SEC7 212 Phosphoserine +P11075 YDR170C SEC7 215 Phosphoserine +P11075 YDR170C SEC7 334 Phosphothreonine +P11075 YDR170C SEC7 447 Phosphoserine +P11075 YDR170C SEC7 452 Phosphoserine +P11075 YDR170C SEC7 455 Phosphoserine +P11075 YDR170C SEC7 807 Phosphoserine +P11075 YDR170C SEC7 1226 Phosphoserine +P11075 YDR170C SEC7 1240 Phosphothreonine +P11075 YDR170C SEC7 1741 Phosphoserine +P11075 YDR170C SEC7 1752 Phosphoserine +P11075 YDR170C SEC7 797 Glycyl +P32855 YPR055W SEC8 16 Phosphoserine +P32855 YPR055W SEC8 19 Phosphoserine +P40316 YDR113C PDS1 185 Phosphoserine +P40316 YDR113C PDS1 186 Phosphoserine +P40316 YDR113C PDS1 212 Phosphoserine +P40316 YDR113C PDS1 213 Phosphoserine +P40316 YDR113C PDS1 277 Phosphoserine +P40316 YDR113C PDS1 292 Phosphoserine%3B +P25365 YCR067C SED4 65 Phosphoserine +P25365 YCR067C SED4 388 N-linked +P25365 YCR067C SED4 620 N-linked +P25365 YCR067C SED4 1039 N-linked +P40054 YER081W SER3 22 Phosphoserine +P40054 YER081W SER3 29 Phosphoserine +P40054 YER081W SER3 33 Phosphoserine +P36124 YKR029C SET3 236 Phosphoserine +P36124 YKR029C SET3 684 Phosphoserine +P36124 YKR029C SET3 718 Phosphoserine +P36124 YKR029C SET3 719 Phosphothreonine +P36124 YKR029C SET3 741 Phosphoserine +Q12314 YOR021C SFM1 204 Phosphoserine +Q12314 YOR021C SFM1 207 Phosphoserine +P53313 YGR245C SDA1 278 Phosphoserine +P32602 YBL050W SEC17 2 N-acetylserine +P32602 YBL050W SEC17 261 Glycyl +P40482 YIL109C SEC24 178 Phosphoserine +P32844 YIL068C SEC6 2 N-acetylserine +P34250 YKL105C SEG2 137 Phosphoserine +P34250 YKL105C SEG2 280 Phosphoserine +P34250 YKL105C SEG2 504 Phosphoserine +P34250 YKL105C SEG2 507 Phosphoserine +P34250 YKL105C SEG2 556 Phosphoserine +P34250 YKL105C SEG2 980 Phosphoserine +P34250 YKL105C SEG2 1022 Phosphoserine +P34250 YKL105C SEG2 526 Glycyl +P34250 YKL105C SEG2 743 Glycyl +P38272 YBR130C SHE3 343 Phosphoserine +P38272 YBR130C SHE3 394 Phosphoserine +P53334 YGR279C SCW4 89 N-linked +P33330 YOR184W SER1 20 Phosphothreonine +P33330 YOR184W SER1 112 Phosphoserine +P33330 YOR184W SER1 218 N6-(pyridoxal +P38827 YHR119W SET1 625 Phosphoserine +P38827 YHR119W SET1 875 Phosphothreonine +Q12369 YLL003W SFI1 10 Phosphoserine +Q12369 YLL003W SFI1 855 Phosphoserine +P35735 YKL051W SFK1 208 Phosphoserine +P20134 YOR140W SFL1 220 Phosphoserine +P20134 YOR140W SFL1 556 Phosphoserine +P20134 YOR140W SFL1 733 Phosphoserine +Q12234 YOR216C RUD3 55 Phosphoserine +Q12234 YOR216C RUD3 64 Phosphoserine +Q12234 YOR216C RUD3 468 Phosphoserine +Q07458 YDL076C RXT3 2 N-acetylserine +P34218 YBL052C SAS3 367 N6-acetyllysine%3B +P40963 YMR127C SAS2 168 N6-acetyllysine%3B +P36048 YKL173W SNU114 85 Phosphoserine +P36048 YKL173W SNU114 88 Phosphothreonine +P10870 YDL194W SNF3 383 N-linked +P18888 YHL025W SNF6 165 Phosphothreonine +P39929 YLR025W SNF7 72 Phosphothreonine +P39929 YLR025W SNF7 119 Phosphoserine +P39929 YLR025W SNF7 193 Phosphoserine +P39929 YLR025W SNF7 229 Glycyl +P00445 YJR104C SOD1 26 Phosphoserine +P00445 YJR104C SOD1 39 Phosphoserine +P00445 YJR104C SOD1 99 Phosphoserine +P00445 YJR104C SOD1 117 Phosphoserine +P00445 YJR104C SOD1 132 Phosphothreonine +P00445 YJR104C SOD1 138 Phosphothreonine +P00445 YJR104C SOD1 19 Glycyl +P00445 YJR104C SOD1 70 Glycyl +Q03954 YDR201W SPC19 107 Phosphoserine +Q03954 YDR201W SPC19 116 Phosphoserine +Q12455 YLR146C SPE4 5 Phosphoserine +P06843 YER161C SPT2 2 N-acetylserine +P06843 YER161C SPT2 126 Phosphoserine +P35177 YBR081C SPT7 78 Phosphothreonine%3B +P35177 YBR081C SPT7 88 Phosphoserine +P35177 YBR081C SPT7 1293 Phosphoserine +P38985 YDL092W SRP14 8 Phosphoserine +P32342 YKL122C SRP21 2 N-acetylserine +P40505 YIL084C SDS3 166 Phosphoserine +P40505 YIL084C SDS3 211 Phosphoserine +P15367 YIR022W SEC11 121 N-linked +P38810 YHR098C SFB3 15 Phosphoserine +P38810 YHR098C SFB3 72 Phosphothreonine +P38810 YHR098C SFB3 83 Phosphoserine +P38810 YHR098C SFB3 85 Phosphoserine +P38810 YHR098C SFB3 94 Phosphoserine +P38810 YHR098C SFB3 101 Phosphoserine +P38810 YHR098C SFB3 110 Phosphoserine +P38810 YHR098C SFB3 216 Phosphothreonine +P51534 YOR035C SHE4 18 Phosphoserine +P40073 YER118C SHO1 166 Phosphoserine +P40073 YER118C SHO1 59 N-linked +P25294 YNL007C SIS1 275 Phosphoserine +P52286 YDR328C SKP1 177 Phosphothreonine +P33338 YNL243W SLA2 294 Phosphothreonine +P33338 YNL243W SLA2 298 Phosphothreonine +P33338 YNL243W SLA2 308 Phosphoserine +P33338 YNL243W SLA2 555 Phosphoserine +Q12078 YLR034C SMF3 87 N-linked +P25357 YCR033W SNT1 187 Phosphoserine +P25357 YCR033W SNT1 395 Phosphoserine +P25357 YCR033W SNT1 796 Phosphothreonine +P25357 YCR033W SNT1 1037 Phosphoserine +P50278 YNR034W SOL1 65 Phosphoserine +P50278 YNR034W SOL1 68 Phosphoserine +P50278 YNR034W SOL1 320 Phosphothreonine +Q08199 YOL031C SIL1 105 N-linked +Q08199 YOL031C SIL1 181 N-linked +Q08199 YOL031C SIL1 215 N-linked +Q08199 YOL031C SIL1 233 N-linked +Q08199 YOL031C SIL1 315 N-linked +Q08199 YOL031C SIL1 333 N-linked +P40472 YIL123W SIM1 423 N-linked +P11978 YDR227W SIR4 692 Phosphoserine +P11978 YDR227W SIR4 1128 Glycyl +P36169 YKR100C SKG1 142 Phosphoserine +P36169 YKR100C SKG1 273 Phosphothreonine +P32790 YBL007C SLA1 447 Phosphoserine +P32790 YBL007C SLA1 449 Phosphoserine +P32790 YBL007C SLA1 454 Phosphoserine +P32790 YBL007C SLA1 799 Phosphoserine +P32790 YBL007C SLA1 831 Phosphothreonine +P32790 YBL007C SLA1 858 Phosphothreonine +P32790 YBL007C SLA1 887 Phosphothreonine +P32790 YBL007C SLA1 904 Phosphothreonine +P32790 YBL007C SLA1 984 Phosphothreonine +P32790 YBL007C SLA1 993 Phosphothreonine +P32790 YBL007C SLA1 996 Phosphoserine +P32790 YBL007C SLA1 1075 Phosphothreonine +P32790 YBL007C SLA1 471 Glycyl +P32790 YBL007C SLA1 548 Glycyl +P47037 YJL074C SMC3 112 N6-acetyllysine +P47037 YJL074C SMC3 113 N6-acetyllysine +P38925 YOL122C SMF1 24 Phosphoserine +P38925 YOL122C SMF1 33 Glycyl +P38925 YOL122C SMF1 34 Glycyl +Q04007 YDR186C SND1 309 Phosphoserine +Q04007 YDR186C SND1 310 Phosphoserine +Q04007 YDR186C SND1 311 Phosphoserine +Q04007 YDR186C SND1 332 Phosphoserine +Q04007 YDR186C SND1 334 Phosphoserine +Q04007 YDR186C SND1 692 Phosphoserine +Q04007 YDR186C SND1 694 Phosphoserine +Q04007 YDR186C SND1 706 Phosphoserine +Q04007 YDR186C SND1 841 Phosphoserine +Q04007 YDR186C SND1 668 Glycyl +Q04007 YDR186C SND1 670 Glycyl +P38956 YDR073W SNF11 2 N-acetylserine +P22082 YOR290C SNF2 358 Phosphoserine +P22082 YOR290C SNF2 383 Phosphothreonine +P22082 YOR290C SNF2 716 Phosphoserine +P22082 YOR290C SNF2 1340 Phosphoserine +P22082 YOR290C SNF2 543 Glycyl +P46950 YGR197C SNG1 91 Phosphothreonine +P53438 YMR016C SOK2 771 Phosphoserine +P37262 YCR073W-A SOL2 42 Phosphoserine +P37262 YCR073W-A SOL2 64 Phosphoserine +P31109 YAL030W SNC1 95 S-palmitoyl +P31109 YAL030W SNC1 63 Glycyl +P33328 YOR327C SNC2 58 Phosphoserine +P33328 YOR327C SNC2 94 S-palmitoyl +P33328 YOR327C SNC2 62 Glycyl +Q12420 YOR308C SNU66 268 Phosphoserine +P40317 YDR006C SOK1 40 Phosphoserine +P40317 YDR006C SOK1 53 Phosphoserine +P40317 YDR006C SOK1 191 Phosphoserine +P40317 YDR006C SOK1 193 Phosphoserine +P40317 YDR006C SOK1 245 Phosphoserine +P25808 YFL002C SPB4 254 Phosphoserine +P46965 YJR010C-A SPC1 2 N-acetylserine +P38915 YLR055C SPT8 85 Phosphothreonine +P38915 YLR055C SPT8 108 Phosphoserine +P38915 YLR055C SPT8 123 Phosphoserine +P38915 YLR055C SPT8 131 Phosphoserine +P38915 YLR055C SPT8 451 Phosphoserine +Q03707 YML034W SRC1 78 Phosphoserine +Q03707 YML034W SRC1 80 Phosphoserine +Q03707 YML034W SRC1 85 Phosphoserine +Q03707 YML034W SRC1 181 Phosphoserine +Q03707 YML034W SRC1 203 Phosphoserine +Q03707 YML034W SRC1 204 Phosphoserine +Q03707 YML034W SRC1 206 Phosphoserine +Q03707 YML034W SRC1 301 Phosphoserine +Q03707 YML034W SRC1 394 Phosphothreonine +Q03707 YML034W SRC1 427 Phosphoserine +P39931 YLR250W SSP120 212 Phosphothreonine +P53172 YGL056C SDS23 9 Phosphoserine +P53172 YGL056C SDS23 42 Phosphoserine +P53172 YGL056C SDS23 46 Phosphoserine +P53172 YGL056C SDS23 430 Phosphoserine +Q12118 YOR007C SGT2 308 Phosphothreonine +P38200 YBL031W SHE1 165 Phosphoserine +P36024 YKR072C SIS2 47 Phosphoserine +P36024 YKR072C SIS2 50 Phosphoserine +P36024 YKR072C SIS2 54 Phosphoserine +P36024 YKR072C SIS2 56 Phosphoserine +P36024 YKR072C SIS2 155 Phosphoserine +P38889 YHR206W SKN7 427 4-aspartylphosphate +Q02100 YNL167C SKO1 94 Phosphoserine +Q02100 YNL167C SKO1 113 Phosphothreonine +Q02100 YNL167C SKO1 399 Phosphoserine +Q02100 YNL167C SKO1 558 Phosphoserine +P34252 YKL108W SLD2 84 Phosphothreonine%3B +Q04964 YML058W SML1 1 N-acetylmethionine +Q04964 YML058W SML1 56 Phosphoserine%3B +Q04964 YML058W SML1 58 Phosphoserine%3B +Q04964 YML058W SML1 60 Phosphoserine%3B +Q12306 YDR510W SMT3 2 N-acetylserine +Q12306 YDR510W SMT3 2 Phosphoserine +Q12306 YDR510W SMT3 4 Phosphoserine +Q12306 YDR510W SMT3 98 Glycyl +P32364 YKL079W SMY1 583 Phosphothreonine +P32909 YBR172C SMY2 12 Phosphoserine +P32909 YBR172C SMY2 96 Phosphoserine +P32909 YBR172C SMY2 129 Phosphothreonine +P32909 YBR172C SMY2 311 Phosphothreonine +P32909 YBR172C SMY2 545 Phosphoserine +P32909 YBR172C SMY2 602 Phosphoserine +P56508 YDR525W-A SNA2 71 Phosphoserine +P56508 YDR525W-A SNA2 77 Phosphoserine +P00447 YHR008C SOD2 147 Phosphothreonine +P00447 YHR008C SOD2 149 Phosphothreonine +P23201 YLL021W SPA2 182 Phosphoserine +P23201 YLL021W SPA2 183 Phosphoserine +P23201 YLL021W SPA2 220 Phosphothreonine +P23201 YLL021W SPA2 254 Phosphoserine +P23201 YLL021W SPA2 274 Phosphoserine +P23201 YLL021W SPA2 301 Phosphoserine +P23201 YLL021W SPA2 585 Phosphoserine +P23201 YLL021W SPA2 599 Phosphoserine +P23201 YLL021W SPA2 646 Phosphoserine +P23201 YLL021W SPA2 817 Phosphoserine +P23201 YLL021W SPA2 820 Phosphoserine +P23201 YLL021W SPA2 865 Phosphoserine +P23201 YLL021W SPA2 883 Phosphoserine +P23201 YLL021W SPA2 910 Phosphoserine +P23201 YLL021W SPA2 937 Phosphoserine +P23201 YLL021W SPA2 961 Phosphoserine +P23201 YLL021W SPA2 979 Phosphoserine +P23201 YLL021W SPA2 1053 Phosphoserine +P23201 YLL021W SPA2 1056 Phosphoserine +P23201 YLL021W SPA2 1080 Phosphoserine +P23201 YLL021W SPA2 1173 Phosphoserine +P23201 YLL021W SPA2 1179 Phosphothreonine +P23201 YLL021W SPA2 1180 Phosphoserine +P23201 YLL021W SPA2 1251 Phosphothreonine +P23201 YLL021W SPA2 1263 Phosphoserine +P36131 YKR037C SPC34 199 Phosphothreonine%3B +P53540 YNL126W SPC98 124 Phosphoserine +P53540 YNL126W SPC98 136 Phosphoserine +P40092 YER150W SPI1 127 GPI-anchor +P40092 YER150W SPI1 41 N-linked +P40092 YER150W SPI1 59 N-linked +P53541 YNL012W SPO1 233 N-linked +P53541 YNL012W SPO1 293 N-linked +P53541 YNL012W SPO1 303 N-linked +P53541 YNL012W SPO1 500 N-linked +P53541 YNL012W SPO1 536 N-linked +P53541 YNL012W SPO1 560 N-linked +P53541 YNL012W SPO1 563 N-linked +P53541 YNL012W SPO1 572 N-linked +P35209 YMR179W SPT21 454 Phosphoserine +Q06168 YLR321C SFH1 78 Phosphoserine +P25554 YCL010C SGF29 139 Phosphoserine +P22579 YOL004W SIN3 137 Phosphoserine +P22579 YOL004W SIN3 303 Phosphothreonine +P22579 YOL004W SIN3 304 Phosphothreonine +P22579 YOL004W SIN3 316 Phosphoserine +P22579 YOL004W SIN3 1046 Phosphoserine +P34164 YGL208W SIP2 66 Phosphoserine +P34164 YGL208W SIP2 298 Phosphoserine +P34164 YGL208W SIP2 2 N-myristoyl +P40210 YMR140W SIP5 13 Phosphoserine +P40210 YMR140W SIP5 183 Phosphothreonine +P40210 YMR140W SIP5 433 Phosphothreonine +P40210 YMR140W SIP5 436 Phosphoserine +P40210 YMR140W SIP5 438 Phosphothreonine +P53955 YNL047C SLM2 626 Phosphoserine +P53955 YNL047C SLM2 649 Phosphoserine +P53955 YNL047C SLM2 653 Phosphoserine +Q12098 YLR135W SLX4 72 Phosphothreonine%3B +Q12098 YLR135W SLX4 113 Phosphothreonine%3B +Q12098 YLR135W SLX4 289 Phosphoserine%3B +Q12098 YLR135W SLX4 319 Phosphothreonine%3B +Q12098 YLR135W SLX4 329 Phosphoserine%3B +Q12098 YLR135W SLX4 355 Phosphoserine%3B +P54867 YOR008C SLG1 331 Phosphoserine +P54867 YOR008C SLG1 353 Phosphoserine +P54867 YOR008C SLG1 65 N-linked +P40485 YIL105C SLM1 145 Phosphoserine +P40485 YIL105C SLM1 150 Phosphoserine +P40485 YIL105C SLM1 153 Phosphoserine +P39928 YIL147C SLN1 502 Phosphoserine +P39928 YIL147C SLN1 576 Phosphohistidine%3B +P39928 YIL147C SLN1 758 Phosphoserine +P39928 YIL147C SLN1 833 Phosphoserine +P39928 YIL147C SLN1 1041 Phosphoserine +P39928 YIL147C SLN1 1044 Phosphoserine +P39928 YIL147C SLN1 1144 4-aspartylphosphate +P39928 YIL147C SLN1 100 N-linked +P39928 YIL147C SLN1 138 N-linked +P39928 YIL147C SLN1 142 N-linked +P39928 YIL147C SLN1 181 N-linked +P39928 YIL147C SLN1 224 N-linked +P39928 YIL147C SLN1 272 N-linked +Q12267 YLR086W SMC4 2 N-acetylserine +Q12267 YLR086W SMC4 43 Phosphothreonine +Q12267 YLR086W SMC4 113 Phosphoserine +P18480 YBR289W SNF5 818 Phosphoserine +P32568 YDR011W SNQ2 2 N-acetylserine +P32568 YDR011W SNQ2 26 Phosphoserine +P32568 YDR011W SNQ2 29 Phosphoserine +P32568 YDR011W SNQ2 64 Phosphoserine +P32568 YDR011W SNQ2 80 Phosphoserine +P32568 YDR011W SNQ2 86 Phosphoserine +P32568 YDR011W SNQ2 1153 Phosphothreonine +P32568 YDR011W SNQ2 273 N-linked +P32568 YDR011W SNQ2 334 N-linked +P32568 YDR011W SNQ2 518 N-linked +P32568 YDR011W SNQ2 730 N-linked +P32568 YDR011W SNQ2 874 N-linked +P32568 YDR011W SNQ2 1401 N-linked +P53207 YGR013W SNU71 512 Phosphoserine +P53207 YGR013W SNU71 514 Phosphoserine +Q12133 YLR066W SPC3 102 N-linked +Q12133 YLR066W SPC3 173 N-linked +P36094 YKL042W SPC42 213 Phosphoserine +P36094 YKL042W SPC42 217 Phosphoserine +P36094 YKL042W SPC42 284 Phosphoserine +P36094 YKL042W SPC42 329 Phosphoserine +P17123 YHR152W SPO12 2 N-acetylserine +P17123 YHR152W SPO12 118 Phosphoserine +P17123 YHR152W SPO12 125 Phosphoserine +P50875 YOL148C SPT20 446 Phosphoserine +P50875 YOL148C SPT20 516 Phosphothreonine +Q06132 YLR336C SGD1 736 Phosphoserine +P06701 YLR442C SIR3 2 N-acetylalanine +P34226 YBL061C SKT5 148 Phosphoserine +P34226 YBL061C SKT5 561 Phosphoserine +P34226 YBL061C SKT5 563 Phosphoserine +P34226 YBL061C SKT5 564 Phosphothreonine +P34226 YBL061C SKT5 693 Cysteine +P34226 YBL061C SKT5 693 S-farnesyl +Q08581 YOR195W SLK19 7 Phosphothreonine%3B +Q08581 YOR195W SLK19 188 Phosphoserine +Q08581 YOR195W SLK19 189 Phosphoserine +Q08581 YOR195W SLK19 201 Phosphoserine%3B +Q08581 YOR195W SLK19 216 Phosphoserine +Q08581 YOR195W SLK19 273 Phosphothreonine +Q08581 YOR195W SLK19 283 Phosphoserine +Q12232 YOR154W SLP1 25 N-linked +Q12232 YOR154W SLP1 378 N-linked +Q12232 YOR154W SLP1 381 N-linked +Q12232 YOR154W SLP1 408 N-linked +Q12232 YOR154W SLP1 448 N-linked +Q12232 YOR154W SLP1 486 N-linked +P32380 YDR356W SPC110 18 Phosphothreonine +P32380 YDR356W SPC110 60 Phosphoserine%3B +P32380 YDR356W SPC110 64 Phosphothreonine%3B +P32380 YDR356W SPC110 68 Phosphothreonine%3B +P32380 YDR356W SPC110 80 Phosphoserine +P32380 YDR356W SPC110 529 Phosphoserine +P25582 YCL054W SPB1 455 Phosphoserine +P25582 YCL054W SPB1 464 Phosphoserine +P25582 YCL054W SPB1 529 Phosphoserine +Q04398 YDR504C SPG3 86 N-linked +P33419 YPL124W SPC29 18 Phosphothreonine +P33419 YPL124W SPC29 65 Phosphoserine +P33419 YPL124W SPC29 240 Phosphothreonine%3B +Q03029 YPL130W SPO19 198 GPI-anchor +P38904 YDR464W SPP41 1014 Phosphoserine +P38904 YDR464W SPP41 1067 Phosphoserine +P38904 YDR464W SPP41 981 Glycyl +P38904 YDR464W SPP41 1154 Glycyl +P32603 YOR190W SPR1 201 N-linked +P32573 YNL202W SPS19 188 Glycyl +P32558 YGL207W SPT16 526 Phosphoserine +P32558 YGL207W SPT16 765 Phosphoserine +P35210 YKL020C SPT23 468 Phosphoserine +P53866 YNL224C SQS1 105 Phosphoserine +P53866 YNL224C SQS1 217 Phosphoserine +P53866 YNL224C SQS1 255 Phosphoserine +P53866 YNL224C SQS1 334 Phosphoserine +P53866 YNL224C SQS1 343 Phosphoserine +P53866 YNL224C SQS1 345 Phosphoserine +P24276 YDR293C SSD1 2 N-acetylserine +P24276 YDR293C SSD1 40 Phosphoserine +P24276 YDR293C SSD1 164 Phosphoserine +P24276 YDR293C SSD1 183 Phosphoserine +P24276 YDR293C SSD1 227 Phosphothreonine +P24276 YDR293C SSD1 286 Phosphoserine +P24276 YDR293C SSD1 322 Phosphoserine +P24276 YDR293C SSD1 491 Phosphoserine +P24276 YDR293C SSD1 492 Phosphoserine +P24276 YDR293C SSD1 688 Phosphotyrosine +P32343 YKL124W SSH4 358 Phosphoserine +P32343 YKL124W SSH4 212 N-linked +P32343 YKL124W SSH4 356 N-linked +P32343 YKL124W SSH4 430 N-linked +P32343 YKL124W SSH4 507 N-linked +P32343 YKL124W SSH4 557 N-linked +P32343 YKL124W SSH4 575 N-linked +P32343 YKL124W SSH4 367 Glycyl +P15705 YOR027W STI1 227 Phosphoserine +P15705 YOR027W STI1 99 Glycyl +P15705 YOR027W STI1 168 Glycyl +P15705 YOR027W STI1 384 Glycyl +P14359 YJL151C SNA3 125 Glycyl +P38839 YHR136C SPL2 59 Phosphoserine +P38839 YHR136C SPL2 86 Phosphoserine +Q12516 YDL133W SRF1 45 Phosphoserine +Q12516 YDL133W SRF1 167 Phosphoserine +Q12516 YDL133W SRF1 297 N-linked +Q12516 YDL133W SRF1 385 N-linked +Q12020 YLR082C SRL2 11 Phosphoserine +Q12020 YLR082C SRL2 139 Phosphoserine +P36167 YKR091W SRL3 212 Phosphoserine +P25567 YCL037C SRO9 55 Phosphoserine +P25567 YCL037C SRO9 148 Phosphoserine +P25567 YCL037C SRO9 422 Phosphoserine +P25567 YCL037C SRO9 156 Glycyl +P25567 YCL037C SRO9 301 Glycyl +P25567 YCL037C SRO9 342 Glycyl +P25567 YCL037C SRO9 352 Glycyl +P42845 YNL309W STB1 2 N-acetylserine +P42845 YNL309W STB1 7 Phosphoserine +P42845 YNL309W STB1 72 Phosphoserine +P42845 YNL309W STB1 99 Phosphothreonine +P42845 YNL309W STB1 102 Phosphoserine +P42845 YNL309W STB1 419 Phosphothreonine +Q03497 YHL007C STE20 2 N-acetylserine +Q03497 YHL007C STE20 87 Phosphoserine +Q03497 YHL007C STE20 165 Phosphoserine +Q03497 YHL007C STE20 167 Phosphothreonine +Q03497 YHL007C STE20 169 Phosphoserine +Q03497 YHL007C STE20 203 Phosphothreonine +Q03497 YHL007C STE20 418 Phosphoserine +Q03497 YHL007C STE20 502 Phosphoserine +Q03497 YHL007C STE20 547 Phosphoserine +Q03497 YHL007C STE20 562 Phosphoserine +Q03497 YHL007C STE20 573 Phosphothreonine +Q03497 YHL007C STE20 585 Phosphoserine +Q03497 YHL007C STE20 773 Phosphothreonine +Q03497 YHL007C STE20 924 Phosphoserine +Q03497 YHL007C STE20 927 Phosphothreonine +P32917 YDR103W STE5 329 Phosphoserine +P12866 YKL209C STE6 61 N-linked +P12866 YKL209C STE6 1022 Glycyl +P06784 YDL159W STE7 359 Phosphoserine +P06784 YDL159W STE7 363 Phosphothreonine +P39932 YDR536W STL1 197 N-linked +P39932 YDR536W STL1 319 N-linked +P09959 YLR182W SWI6 149 Phosphoserine +P09959 YLR182W SWI6 160 Phosphoserine%3B +P09959 YLR182W SWI6 176 Phosphoserine +P09959 YLR182W SWI6 179 Phosphothreonine +P09959 YLR182W SWI6 182 Phosphothreonine +P09959 YLR182W SWI6 547 Phosphoserine +P46655 YGL245W GUS1 300 Phosphothreonine +P53277 YGR129W SYF2 45 Phosphoserine +P53277 YGR129W SYF2 124 Phosphoserine +P53277 YGR129W SYF2 125 Phosphoserine +P11972 YLR452C SST2 252 Phosphoserine +P11972 YLR452C SST2 408 Phosphoserine +P11972 YLR452C SST2 539 Phosphoserine%3B +P11972 YLR452C SST2 587 Phosphoserine +P41930 YPL092W SSU1 444 Phosphoserine +P41930 YPL092W SSU1 448 Phosphoserine +P41930 YPL092W SSU1 450 Phosphoserine +P08153 YDR146C SWI5 225 Phosphoserine +P08153 YDR146C SWI5 278 Phosphoserine +P08153 YDR146C SWI5 300 Phosphoserine +P08153 YDR146C SWI5 339 Phosphothreonine +P08153 YDR146C SWI5 376 Phosphoserine +P08153 YDR146C SWI5 488 Phosphoserine +P08153 YDR146C SWI5 492 Phosphoserine +P08153 YDR146C SWI5 505 Phosphoserine +P08153 YDR146C SWI5 522 Phosphoserine%3B +P08153 YDR146C SWI5 646 Phosphoserine%3B +P08153 YDR146C SWI5 664 Phosphoserine%3B +P23615 YGR116W SPT6 94 Phosphoserine +P23615 YGR116W SPT6 134 Phosphoserine +P23615 YGR116W SPT6 136 Phosphoserine +P23615 YGR116W SPT6 148 Phosphoserine +P23615 YGR116W SPT6 155 Phosphoserine +P23615 YGR116W SPT6 206 Phosphoserine +P23615 YGR116W SPT6 295 Phosphoserine +Q08673 YOR247W SRL1 23 N-linked +Q08673 YOR247W SRL1 174 N-linked +Q08673 YOR247W SRL1 200 N-linked +Q08673 YOR247W SRL1 206 N-linked +P10080 YHL034C SBP1 2 N-acetylserine +P10080 YHL034C SBP1 91 Phosphothreonine +P10080 YHL034C SBP1 119 Phosphothreonine +P10080 YHL034C SBP1 242 Phosphothreonine +P10080 YHL034C SBP1 244 Phosphoserine +P53599 YNR031C SSK2 57 Phosphoserine +P53599 YNR031C SSK2 62 Phosphoserine +P53599 YNR031C SSK2 78 Phosphoserine +P53599 YNR031C SSK2 118 Phosphoserine +P53599 YNR031C SSK2 290 Phosphoserine +P53599 YNR031C SSK2 1424 Phosphoserine +Q07084 YLR006C SSK1 110 Phosphoserine +Q07084 YLR006C SSK1 195 Phosphoserine +Q07084 YLR006C SSK1 327 Phosphoserine +Q07084 YLR006C SSK1 351 Phosphoserine +Q07084 YLR006C SSK1 368 Phosphoserine +Q07084 YLR006C SSK1 380 Phosphoserine +Q07084 YLR006C SSK1 554 4-aspartylphosphate +Q07084 YLR006C SSK1 673 Phosphoserine +Q07084 YLR006C SSK1 693 Phosphothreonine +Q07084 YLR006C SSK1 703 Phosphoserine +Q07084 YLR006C SSK1 706 Phosphoserine +Q12427 YDR169C STB3 254 Phosphoserine +P36085 YKL072W STB6 514 Phosphoserine +D6VTK4 YFL026W STE2 310 Phosphoserine +D6VTK4 YFL026W STE2 315 Phosphoserine +D6VTK4 YFL026W STE2 329 Phosphothreonine +D6VTK4 YFL026W STE2 331 Phosphoserine +D6VTK4 YFL026W STE2 360 Phosphoserine +D6VTK4 YFL026W STE2 363 Phosphothreonine +D6VTK4 YFL026W STE2 366 Phosphoserine +D6VTK4 YFL026W STE2 382 Phosphothreonine +D6VTK4 YFL026W STE2 385 Phosphoserine +D6VTK4 YFL026W STE2 386 Phosphoserine +D6VTK4 YFL026W STE2 411 Phosphothreonine +D6VTK4 YFL026W STE2 414 Phosphothreonine +D6VTK4 YFL026W STE2 25 N-linked +D6VTK4 YFL026W STE2 32 N-linked +D6VTK4 YFL026W STE2 374 Glycyl +D6VTK4 YFL026W STE2 400 Glycyl +D6VTK4 YFL026W STE2 422 Glycyl +P25344 YCL032W STE50 202 Phosphoserine +P25344 YCL032W STE50 244 Phosphothreonine +P25344 YCL032W STE50 248 Phosphoserine +P16965 YGR008C STF2 28 Phosphoserine +P16965 YGR008C STF2 69 Phosphoserine +P53312 YGR244C LSC2 102 Phosphoserine +P53312 YGR244C LSC2 263 Phosphoserine +P53312 YGR244C LSC2 276 Phosphoserine +P38359 YBR294W SUL1 51 N-linked +P38359 YBR294W SUL1 93 N-linked +P38359 YBR294W SUL1 358 N-linked +P38359 YBR294W SUL1 391 N-linked +P38359 YBR294W SUL1 630 N-linked +P38359 YBR294W SUL1 653 N-linked +P38359 YBR294W SUL1 718 N-linked +Q03088 YPL032C SVL3 471 Phosphoserine +Q03088 YPL032C SVL3 496 Phosphothreonine +Q03088 YPL032C SVL3 551 Phosphoserine +Q03088 YPL032C SVL3 662 Phosphoserine +Q03088 YPL032C SVL3 739 Phosphothreonine +Q03088 YPL032C SVL3 756 Phosphothreonine +Q03088 YPL032C SVL3 757 Phosphoserine +Q06677 YDR320C SWA2 52 Phosphoserine +Q06677 YDR320C SWA2 64 Phosphoserine +Q06677 YDR320C SWA2 264 Phosphoserine +Q06677 YDR320C SWA2 308 Phosphoserine +Q06677 YDR320C SWA2 312 Phosphoserine +P32828 YDL013W SLX5 14 Phosphoserine +P32828 YDL013W SLX5 29 Phosphoserine +Q08817 YOR353C SOG2 214 Phosphothreonine +P39543 YJL192C SOP4 35 N-linked +P39543 YJL192C SOP4 53 N-linked +P39543 YJL192C SOP4 85 N-linked +P39543 YJL192C SOP4 115 N-linked +P39543 YJL192C SOP4 170 N-linked +P53148 YGL093W SPC105 77 Phosphoserine +P53148 YGL093W SPC105 356 Phosphothreonine +P53148 YGL093W SPC105 380 Phosphoserine +P06844 YDR392W SPT3 270 Phosphoserine +P32916 YDR292C SRP101 239 Phosphoserine +P32916 YDR292C SRP101 523 Phosphoserine +P12954 YJL092W SRS2 833 Phosphoserine +P13130 YHR139C SPS100 26 N-linked +P13130 YHR139C SPS100 50 N-linked +P13130 YHR139C SPS100 58 N-linked +P13130 YHR139C SPS100 64 N-linked +P13130 YHR139C SPS100 76 N-linked +P13130 YHR139C SPS100 108 N-linked +P13130 YHR139C SPS100 181 N-linked +P13130 YHR139C SPS100 190 N-linked +P13130 YHR139C SPS100 199 N-linked +P13130 YHR139C SPS100 205 N-linked +P13130 YHR139C SPS100 248 N-linked +P13130 YHR139C SPS100 281 N-linked +Q07549 YDL123W SNA4 134 Phosphoserine +Q07549 YDL123W SNA4 2 S-palmitoyl +Q07549 YDL123W SNA4 3 S-palmitoyl +Q07549 YDL123W SNA4 5 S-palmitoyl +Q07549 YDL123W SNA4 7 S-palmitoyl +Q07549 YDL123W SNA4 8 S-palmitoyl +Q07549 YDL123W SNA4 128 Glycyl +Q04477 YMR117C SPC24 2 N-acetylserine +P40014 YER018C SPC25 2 N-acetylalanine +Q03012 YPL138C SPP1 87 Phosphoserine +P25380 YCL048W SPS22 440 GPI-anchor +P25380 YCL048W SPS22 256 N-linked +P25380 YCL048W SPS22 314 N-linked +P25380 YCL048W SPS22 327 N-linked +P27692 YML010W SPT5 35 Phosphothreonine +P27692 YML010W SPT5 133 Phosphothreonine +P27692 YML010W SPT5 136 Phosphoserine +P27692 YML010W SPT5 188 Phosphoserine +P27692 YML010W SPT5 219 Phosphoserine +P39015 YLR150W STM1 2 N-acetylserine +P39015 YLR150W STM1 55 Phosphoserine +P39015 YLR150W STM1 118 Phosphoserine +P39015 YLR150W STM1 229 Phosphoserine +P39015 YLR150W STM1 46 Glycyl +P39015 YLR150W STM1 121 Glycyl +P39015 YLR150W STM1 171 Glycyl +P39015 YLR150W STM1 184 Glycyl +Q05937 YLR375W STP3 71 Phosphoserine +Q05937 YLR375W STP3 111 Phosphoserine +Q07351 YDL048C STP4 153 Phosphoserine +Q07351 YDL048C STP4 155 Phosphoserine +Q12038 YPR032W SRO7 591 Phosphoserine +Q12038 YPR032W SRO7 602 Phosphoserine +P32583 YKR092C SRP40 133 Phosphoserine +P32583 YKR092C SRP40 289 Phosphothreonine +P32583 YKR092C SRP40 293 Phosphoserine +P32583 YKR092C SRP40 394 Phosphoserine +P38931 YDR443C SSN2 370 Phosphoserine +P38931 YDR443C SSN2 375 Phosphoserine +P38931 YDR443C SSN2 425 Phosphoserine +P38931 YDR443C SSN2 601 Phosphothreonine +P38931 YDR443C SSN2 608 Phosphoserine%3B +P38931 YDR443C SSN2 636 Phosphoserine +P38931 YDR443C SSN2 748 Phosphoserine +P37296 YMR054W STV1 1 N-acetylmethionine +P37296 YMR054W STV1 223 Phosphoserine +P37296 YMR054W STV1 228 Phosphoserine +P31377 YAL014C SYN8 238 S-palmitoyl +P36126 YKR031C SPO14 2 N-acetylserine +P36126 YKR031C SPO14 8 Phosphoserine +P36126 YKR031C SPO14 30 Phosphoserine +P36126 YKR031C SPO14 145 Phosphoserine +P36126 YKR031C SPO14 1461 Phosphoserine +P36126 YKR031C SPO14 1462 Phosphothreonine +Q07798 YLL005C SPO75 2 N-linked +Q07798 YLL005C SPO75 184 N-linked +Q07798 YLL005C SPO75 503 N-linked +P08459 YDR522C SPS2 475 GPI-anchor +P08459 YDR522C SPS2 77 N-linked +P08459 YDR522C SPS2 135 N-linked +P08459 YDR522C SPS2 285 N-linked +P08459 YDR522C SPS2 303 N-linked +P08459 YDR522C SPS2 340 N-linked +P08459 YDR522C SPS2 343 N-linked +P08459 YDR522C SPS2 355 N-linked +P38789 YHR066W SSF1 301 Phosphothreonine +P39926 YMR183C SSO2 31 Phosphoserine +P39926 YMR183C SSO2 34 Phosphoserine +P38788 YHR064C SSZ1 477 Phosphoserine +P38788 YHR064C SSZ1 480 Phosphoserine +P25379 YCL064C CHA1 2 N-acetylserine +P25379 YCL064C CHA1 37 N6-(pyridoxal +P33894 YOR219C STE13 377 N-linked +P33894 YOR219C STE13 814 N-linked +P53101 YGL184C STR3 213 N6-(pyridoxal +P46676 YDR310C SUM1 2 N-acetylserine +P46676 YDR310C SUM1 378 Phosphoserine +P46676 YDR310C SUM1 379 Phosphoserine +P46676 YDR310C SUM1 628 Phosphoserine +P46676 YDR310C SUM1 681 Phosphoserine +P46676 YDR310C SUM1 697 Phosphothreonine +P46676 YDR310C SUM1 712 Phosphoserine%3B +P46676 YDR310C SUM1 738 Phosphoserine +P46676 YDR310C SUM1 817 Phosphothreonine +P53616 YNL066W SUN4 395 N-linked +P33300 YPL057C SUR1 349 Phosphoserine +P54003 YML052W SUR7 293 Phosphoserine +P54003 YML052W SUR7 301 Phosphoserine +P54003 YML052W SUR7 47 N-linked +P04802 YLL018C DPS1 2 N-acetylserine +P04802 YLL018C DPS1 14 Phosphoserine +P04802 YLL018C DPS1 301 Phosphoserine +P04802 YLL018C DPS1 502 Phosphoserine +P04802 YLL018C DPS1 546 Phosphoserine +Q02875 YPL105C SYH1 350 Phosphothreonine +P54000 YMR039C SUB1 119 Phosphoserine +P54000 YMR039C SUB1 268 Phosphoserine +P54000 YMR039C SUB1 269 Phosphoserine +P54000 YMR039C SUB1 289 Phosphoserine +Q07478 YDL084W SUB2 2 N-acetylserine +Q07478 YDL084W SUB2 13 Phosphoserine +Q07478 YDL084W SUB2 37 Phosphoserine +Q07478 YDL084W SUB2 169 Phosphothreonine +P53201 YGR002C SWC4 2 N-acetylserine +P38326 YBR231C SWC5 209 Phosphoserine +P38088 YBR121C GRS1 25 N-acetylserine +P38088 YBR121C GRS1 226 Phosphoserine +P38088 YBR121C GRS1 476 Phosphoserine +P38088 YBR121C GRS1 528 Phosphoserine +P38088 YBR121C GRS1 689 Phosphothreonine +Q6WNK7 YBR111W-A SUS1 68 Glycyl +P38869 YHR181W SVP26 115 N-linked +P32591 YJL176C SWI3 88 Phosphoserine +P32591 YJL176C SWI3 185 Phosphoserine +P32591 YJL176C SWI3 235 Phosphothreonine +P32591 YJL176C SWI3 657 Phosphoserine +P40825 YOR335C ALA1 504 Phosphoserine +P40825 YOR335C ALA1 975 Phosphoserine +P40528 YIL047C SYG1 172 Phosphoserine +P40528 YIL047C SYG1 179 Phosphoserine +P40528 YIL047C SYG1 859 Phosphoserine +P40528 YIL047C SYG1 860 Phosphoserine +P46679 YMR053C STB2 594 Phosphoserine +P46679 YMR053C STB2 625 Phosphoserine +P23561 YLR362W STE11 323 Phosphoserine +P23561 YLR362W STE11 465 Phosphoserine +P01098 YDL130W-A STF1 24 Phosphoserine +P39007 YGL022W STT3 60 N-linked +P39007 YGL022W STT3 535 N-linked +P39007 YGL022W STT3 539 N-linked +P38198 YBL034C STU1 997 Phosphoserine +P38198 YBL034C STU1 1018 Phosphoserine +P38198 YBL034C STU1 1047 Phosphothreonine +P38198 YBL034C STU1 1063 Phosphoserine +P38198 YBL034C STU1 1167 Phosphoserine +P46675 YLR045C STU2 2 Phosphoserine +P46675 YLR045C STU2 277 Phosphoserine +P46675 YLR045C STU2 813 Phosphoserine +P32911 YNL244C SUI1 2 N-acetylserine +Q12254 YPL163C SVS1 23 N-linked +Q12254 YPL163C SVS1 249 N-linked +Q12254 YPL163C SVS1 256 N-linked +P15180 YDR037W KRS1 2 N-acetylserine +P15180 YDR037W KRS1 30 Phosphoserine +P15180 YDR037W KRS1 62 Phosphothreonine +P15180 YDR037W KRS1 308 Glycyl +P15180 YDR037W KRS1 577 Glycyl +P40150 YNL209W SSB2 2 N-acetylalanine +P40150 YNL209W SSB2 47 Phosphothreonine +P40150 YNL209W SSB2 431 Phosphothreonine +P13574 YHR084W STE12 29 Phosphothreonine +P13574 YHR084W STE12 214 Phosphoserine +P13574 YHR084W STE12 226 Phosphoserine +P13574 YHR084W STE12 289 Phosphothreonine +P13574 YHR084W STE12 400 Phosphoserine +P32597 YIL126W STH1 38 Phosphoserine +P37297 YLR305C STT4 459 Phosphoserine +P32944 YJL187C SWE1 36 Phosphoserine%3B +P32944 YJL187C SWE1 45 Phosphothreonine%3B +P32944 YJL187C SWE1 56 Phosphoserine%3B +P32944 YJL187C SWE1 63 Phosphoserine%3B +P32944 YJL187C SWE1 70 Phosphoserine +P32944 YJL187C SWE1 74 Phosphothreonine%3B +P32944 YJL187C SWE1 102 Phosphoserine%3B +P32944 YJL187C SWE1 105 Phosphoserine%3B +P32944 YJL187C SWE1 111 Phosphoserine%3B +P32944 YJL187C SWE1 118 Phosphoserine%3B +P32944 YJL187C SWE1 121 Phosphothreonine%3B +P32944 YJL187C SWE1 124 Phosphothreonine%3B +P32944 YJL187C SWE1 127 Phosphoserine%3B +P32944 YJL187C SWE1 131 Phosphothreonine%3B +P32944 YJL187C SWE1 133 Phosphoserine%3B +P32944 YJL187C SWE1 136 Phosphoserine%3B +P32944 YJL187C SWE1 156 Phosphoserine%3B +P32944 YJL187C SWE1 169 Phosphoserine%3B +P32944 YJL187C SWE1 196 Phosphothreonine%3B +P32944 YJL187C SWE1 201 Phosphoserine%3B +P32944 YJL187C SWE1 225 Phosphoserine%3B +P32944 YJL187C SWE1 254 Phosphoserine%3B +P32944 YJL187C SWE1 262 Phosphoserine +P32944 YJL187C SWE1 263 Phosphoserine%3B +P32944 YJL187C SWE1 266 Phosphoserine%3B +P32944 YJL187C SWE1 280 Phosphothreonine%3B +P32944 YJL187C SWE1 284 Phosphoserine +P32944 YJL187C SWE1 294 Phosphoserine +P32944 YJL187C SWE1 312 Phosphoserine%3B +P32944 YJL187C SWE1 345 Phosphoserine +P32944 YJL187C SWE1 367 Phosphothreonine%3B +P32944 YJL187C SWE1 373 Phosphothreonine%3B +P32944 YJL187C SWE1 379 Phosphoserine%3B +P32944 YJL187C SWE1 384 Phosphothreonine%3B +P32944 YJL187C SWE1 395 Phosphoserine%3B +P32944 YJL187C SWE1 438 Phosphoserine%3B +P32944 YJL187C SWE1 610 Phosphoserine%3B +P32944 YJL187C SWE1 629 Phosphothreonine%3B +P32944 YJL187C SWE1 688 Phosphothreonine%3B +P32944 YJL187C SWE1 692 Phosphothreonine +P32944 YJL187C SWE1 741 Glycyl +P25302 YER111C SWI4 255 Phosphoserine +P25302 YER111C SWI4 806 Phosphoserine +P15625 YFL022C FRS2 2 N-acetylserine +P07806 YGR094W VAS1 73 Phosphoserine +P07806 YGR094W VAS1 294 Phosphoserine +P07806 YGR094W VAS1 332 Phosphoserine +P07806 YGR094W VAS1 707 Phosphoserine +P07806 YGR094W VAS1 1003 Phosphothreonine +P41895 YGR186W TFG1 198 Phosphoserine +P41895 YGR186W TFG1 200 Phosphothreonine +P41895 YGR186W TFG1 515 Phosphoserine +P41895 YGR186W TFG1 560 Phosphoserine +P41895 YGR186W TFG1 562 Phosphoserine +P41895 YGR186W TFG1 571 Phosphoserine +P41895 YGR186W TFG1 655 Phosphoserine +Q12030 YDR167W TAF10 58 Phosphoserine +Q12030 YDR167W TAF10 146 Phosphoserine +P35189 YPL129W TAF14 181 Glycyl +P23255 YCR042C TAF2 158 Phosphothreonine +P23255 YCR042C TAF2 161 Phosphothreonine +P23255 YCR042C TAF2 163 Phosphoserine +P23255 YCR042C TAF2 318 Phosphoserine +Q12297 YPL011C TAF3 237 Phosphothreonine +Q12297 YPL011C TAF3 310 Phosphoserine +Q12297 YPL011C TAF3 346 Phosphoserine +P09436 YBL076C ILS1 829 Phosphoserine +P09436 YBL076C ILS1 1059 Phosphoserine +P09436 YBL076C ILS1 486 Glycyl +Q06836 YPR095C SYT1 277 Phosphothreonine +Q06836 YPR095C SYT1 369 Phosphoserine +P25638 YCR060W TAH1 2 N-acetylserine +P15019 YLR354C TAL1 2 N-acetylserine +P13188 YOR168W GLN4 378 Phosphoserine +P32774 YKL058W TOA2 95 Phosphoserine +P32774 YKL058W TOA2 102 Phosphoserine +P36421 YGR185C TYS1 2 N-acetylserine +P36421 YGR185C TYS1 235 Phosphoserine +P36421 YGR185C TYS1 359 Phosphothreonine +Q04226 YML015C TAF11 236 Phosphoserine +Q04226 YML015C TAF11 238 Phosphoserine +P38129 YBR198C TAF5 299 Phosphoserine +P38129 YBR198C TAF5 411 Phosphoserine +P38129 YBR198C TAF5 415 Phosphoserine +P38129 YBR198C TAF5 787 Phosphoserine +Q03750 YML114C TAF8 269 Phosphoserine +Q04545 YML081W TDA9 527 Phosphoserine +Q04545 YML081W TDA9 603 Phosphoserine +P34163 YKL140W TGL1 462 Phosphoserine +P34163 YKL140W TGL1 466 Phosphoserine +P34163 YKL140W TGL1 521 Phosphoserine +P34163 YKL140W TGL1 538 Phosphoserine +P34163 YKL140W TGL1 539 Phosphothreonine +P34163 YKL140W TGL1 246 Glycyl +Q12043 YOR081C TGL5 645 Phosphoserine +Q12043 YOR081C TGL5 270 N-linked +Q12043 YOR081C TGL5 289 N-linked +Q12043 YOR081C TGL5 297 N-linked +Q12043 YOR081C TGL5 304 N-linked +Q12043 YOR081C TGL5 321 N-linked +Q12043 YOR081C TGL5 474 N-linked +Q12043 YOR081C TGL5 589 N-linked +Q12043 YOR081C TGL5 680 N-linked +Q12043 YOR081C TGL5 714 N-linked +Q12043 YOR081C TGL5 742 N-linked +P04801 YIL078W THS1 195 Phosphoserine +P04801 YIL078W THS1 289 Phosphoserine +P04801 YIL078W THS1 297 Phosphothreonine +P04801 YIL078W THS1 381 Phosphothreonine +P04801 YIL078W THS1 453 Phosphoserine +P04801 YIL078W THS1 457 Phosphoserine +P04801 YIL078W THS1 460 Phosphothreonine +P04801 YIL078W THS1 605 Phosphoserine +P38854 YHR159W TDA11 236 Phosphothreonine +P38854 YHR159W TDA11 244 Phosphoserine +P38854 YHR159W TDA11 286 Phosphoserine +Q03533 YMR291W TDA1 504 Phosphothreonine +Q03533 YMR291W TDA1 509 Phosphoserine +Q03533 YMR291W TDA1 518 Phosphoserine +Q03533 YMR291W TDA1 538 Phosphothreonine +Q03533 YMR291W TDA1 578 Phosphoserine +P40045 YER071C TDA2 2 N-acetylserine +P02557 YFL037W TUB2 278 Phosphoserine +P02557 YFL037W TUB2 280 Phosphoserine +Q12466 YOR086C TCB1 1000 Phosphoserine +Q03640 YML072C TCB3 67 Phosphoserine +Q03640 YML072C TCB3 112 Phosphoserine +Q03640 YML072C TCB3 1340 Phosphoserine +Q03640 YML072C TCB3 1342 Phosphoserine +Q03640 YML072C TCB3 1346 Phosphoserine +Q03640 YML072C TCB3 1350 Phosphothreonine +Q03640 YML072C TCB3 1354 Phosphoserine +Q03640 YML072C TCB3 1400 Phosphoserine +P40533 YIL039W TED1 38 N-linked +P40533 YIL039W TED1 147 N-linked +P40533 YIL039W TED1 229 N-linked +P40533 YIL039W TED1 266 N-linked +P40533 YIL039W TED1 307 N-linked +Q03761 YDR145W TAF12 2 N-acetylserine +Q03761 YDR145W TAF12 129 Phosphoserine +Q03761 YDR145W TAF12 286 Phosphoserine +P50105 YMR005W TAF4 36 Phosphoserine +P50105 YMR005W TAF4 49 Phosphoserine +P50105 YMR005W TAF4 80 Phosphoserine +P53072 YGL232W TAN1 72 Phosphoserine +P39076 YIL142W CCT2 2 N-acetylserine +P39079 YDR188W CCT6 2 N-acetylserine +P39079 YDR188W CCT6 249 Phosphoserine +P38758 YHR009C TDA3 189 Phosphoserine +P38758 YHR009C TDA3 204 Phosphoserine +P38758 YHR009C TDA3 306 Phosphoserine +P53882 YNL176C TDA7 628 Phosphoserine +P53882 YNL176C TDA7 4 N-linked +P53882 YNL176C TDA7 257 N-linked +P53882 YNL176C TDA7 492 N-linked +P53882 YNL176C TDA7 557 N-linked +P53882 YNL176C TDA7 562 N-linked +P53882 YNL176C TDA7 626 N-linked +P53882 YNL176C TDA7 512 Glycyl +Q12004 YPR056W TFB4 1 N-acetylmethionine +P34111 YAL001C TFC3 546 Phosphoserine +P40085 YER140W EMP65 22 Phosphoserine +P40085 YER140W EMP65 318 N-linked +P38756 YHR003C TCD1 259 Phosphoserine +Q06466 YPR157W TDA6 61 N-linked +Q06466 YPR157W TDA6 124 N-linked +Q06466 YPR157W TDA6 141 N-linked +P47988 YOR337W TEA1 22 Phosphothreonine +P47988 YOR337W TEA1 755 Phosphothreonine +P18412 YBR083W TEC1 2 N-acetylserine +P18412 YBR083W TEC1 325 Phosphoserine +P53038 YGR099W TEL2 417 Phosphoserine +P53038 YGR099W TEL2 419 Phosphoserine +P32367 YBR123C TFC1 617 Phosphoserine +P53215 YGR024C THG1 2 N-acetylalanine +Q07748 YDL244W THI13 62 N6-(pyridoxal +Q08579 YOR192C THI72 560 Phosphoserine +Q08579 YOR192C THI72 572 Phosphoserine +P41544 YJL004C SYS1 192 Phosphoserine +P41544 YJL004C SYS1 15 Glycyl +P41896 YGR005C TFG2 28 Phosphoserine +P41896 YGR005C TFG2 34 Phosphoserine +P41896 YGR005C TFG2 56 Phosphoserine +Q05021 YMR227C TAF7 99 Phosphotyrosine +Q05021 YMR227C TAF7 101 Phosphoserine +Q05021 YMR227C TAF7 104 Phosphoserine +P40468 YIL129C TAO3 141 Phosphoserine +P40468 YIL129C TAO3 1144 Phosphoserine +P40468 YIL129C TAO3 2264 Phosphothreonine +P40468 YIL129C TAO3 2267 Phosphoserine +P40468 YIL129C TAO3 2355 Phosphoserine +P26637 YPL160W CDC60 2 N-acetylserine +P26637 YPL160W CDC60 142 Phosphothreonine +P00958 YGR264C MES1 2 N-acetylserine +P36145 YKR062W TFA2 52 Phosphoserine +P36145 YKR062W TFA2 97 Phosphoserine +P36145 YKR062W TFA2 106 Phosphoserine +P11747 YML098W TAF13 131 Phosphothreonine +P38085 YBR069C TAT1 13 Phosphoserine +P38085 YBR069C TAT1 80 Phosphoserine +P38085 YBR069C TAT1 84 Phosphoserine +P38085 YBR069C TAT1 39 Glycyl +P48606 YOR265W RBL2 94 Phosphoserine +P48231 YNL087W TCB2 991 Phosphoserine +P12612 YDR212W TCP1 2 N-acetylserine +P47079 YJL008C CCT8 505 Phosphoserine +P47079 YJL008C CCT8 15 Glycyl +Q07793 YDR261C-D TY1B-DR4 416 Phosphoserine +Q03856 YDR098C-A TY1A-DR1 416 Phosphoserine +O74302 YDR261C-C TY1A-DR4 416 Phosphoserine +P0CX70 YDR365W-A TY1A-DR6 416 Phosphoserine +P14680 YJL141C YAK1 38 Phosphoserine +P14680 YJL141C YAK1 115 Phosphoserine +P14680 YJL141C YAK1 118 Phosphoserine +P14680 YJL141C YAK1 127 Phosphoserine +P14680 YJL141C YAK1 206 Phosphoserine +P14680 YJL141C YAK1 240 Phosphoserine +P14680 YJL141C YAK1 245 Phosphoserine +P14680 YJL141C YAK1 247 Phosphoserine +P14680 YJL141C YAK1 288 Phosphothreonine +P14680 YJL141C YAK1 295 Phosphoserine +P14680 YJL141C YAK1 530 Phosphotyrosine +P46683 YPL239W YAR1 78 Phosphoserine +P40917 YOR028C CIN5 85 Phosphoserine +P40917 YOR028C CIN5 89 Phosphoserine +P40917 YOR028C CIN5 196 Phosphoserine +Q03612 YER138C TY1B-ER1 416 Phosphoserine diff --git a/test_files/PTMs.txt b/test_files/PTMs.txt new file mode 100644 index 0000000..51e681e --- /dev/null +++ b/test_files/PTMs.txt @@ -0,0 +1,9881 @@ +P12688 57 Phosphothreonine +P12688 61 Phosphoserine +P12688 64 Phosphoserine +P12688 71 Phosphoserine +P12688 170 Phosphoserine +P12688 502 Phosphothreonine +P12688 504 Phosphothreonine%3B +P12688 644 Phosphoserine +P12688 653 Phosphoserine +P12688 662 Phosphothreonine%3B +P12688 671 Phosphoserine +P25491 406 Cysteine +P25491 406 S-farnesyl +P25491 198 Glycyl +P16521 2 N-acetylserine +P16521 187 N6%2CN6%2CN6-trimethyllysine +P16521 196 N6%2CN6%2CN6-trimethyllysine +P16521 642 Phosphoserine +P16521 789 N6%2CN6%2CN6-trimethyllysine +P16521 972 Phosphothreonine +P16521 974 Phosphoserine +P16521 1039 Phosphoserine +P16521 1040 Phosphoserine +P16521 350 Glycyl +P16521 636 Glycyl +P11484 2 N-acetylalanine +P11484 47 Phosphothreonine +P11484 431 Phosphothreonine +P39940 258 Glycyl +Q06224 517 Phosphoserine%3B +P02829 657 Phosphoserine +P10591 2 N-acetylserine +P10591 62 Phosphoserine +P10591 551 Phosphoserine +P10591 603 Phosphoserine +P10591 556 Glycyl +P41800 6 N-linked +P41800 50 N-linked +P41800 55 N-linked +P41800 59 N-linked +P00546 2 N-acetylserine +P00546 19 Phosphotyrosine +P00546 169 Phosphothreonine +P15108 653 Phosphoserine +P31539 1 N-acetylmethionine +P31539 206 Phosphoserine +P31539 306 Phosphoserine +P31539 499 Phosphothreonine +P31539 535 Phosphoserine +P31539 442 Glycyl +P31539 620 Glycyl +P25623 264 Phosphoserine +P25623 331 Phosphoserine +P25623 416 Phosphothreonine +P25623 496 Phosphoserine +P25623 500 Phosphoserine +P25623 577 Phosphothreonine +P25623 256 Glycyl +P08539 2 N-myristoyl +P08539 3 S-palmitoyl +P08539 165 Glycyl +P15442 761 Phosphoserine +P15442 882 Phosphothreonine%3B +P15442 887 Phosphothreonine%3B +P10592 2 N-acetylserine +P10592 20 Phosphoserine +P10592 551 Phosphoserine +P10592 603 Phosphoserine +P10592 556 Glycyl +P06782 210 Phosphothreonine%3B +P06782 413 Phosphoserine +P06782 487 Phosphoserine +P06782 632 Phosphoserine +P06782 461 Glycyl +P06782 549 Glycyl +P22147 1506 Phosphothreonine +P22147 1510 Phosphoserine +P32598 1 N-acetylmethionine +P32598 22 Glycyl +P32598 47 Glycyl +P35202 2 N-acetylserine +P16120 124 N6-(pyridoxal +P16120 467 Phosphoserine +P40328 255 Phosphoserine +P39077 1 N-acetylmethionine +P39077 257 Phosphoserine +P35691 9 Phosphoserine +P35691 15 Phosphoserine +P29056 381 Phosphoserine +P29056 384 Phosphoserine +P32318 205 2%2C3-didehydroalanine +Q08144 109 Phosphoserine +P07273 116 Phosphoserine +P00927 109 N6-(pyridoxal +P41338 2 N-acetylserine +O74700 1 N-acetylmethionine +Q12218 465 GPI-anchor +Q12218 327 N-linked +Q12218 348 N-linked +Q12218 368 N-linked +Q12218 403 N-linked +Q12218 404 N-linked +Q05998 560 Phosphoserine +P40040 22 Phosphoserine +P40040 58 Phosphoserine +P40040 68 Phosphoserine +P27654 186 GPI-anchor +P10863 233 GPI-anchor +P32802 61 N-linked +P32802 282 N-linked +Q03290 157 Phosphoserine +Q03290 258 Phosphothreonine +P46678 49 Phosphoserine +P46678 178 Phosphoserine +Q12415 365 Phosphoserine +P42883 62 N6-(pyridoxal +P40340 2 N-acetylalanine +P40340 11 Phosphoserine +P40340 17 Phosphoserine +P40340 94 Phosphoserine +P40340 212 Phosphothreonine +P40340 229 Phosphothreonine +P40340 241 Phosphoserine +P40340 259 Phosphoserine +P40340 285 Phosphoserine +P40340 367 Phosphoserine +P40340 369 Phosphoserine +P40340 370 Phosphoserine +P40340 735 Phosphoserine +P40340 1142 Phosphoserine +P40340 1256 Phosphoserine +Q08921 52 Phosphothreonine +Q08921 82 Phosphothreonine +Q08921 84 Phosphoserine +Q08921 104 Phosphoserine +Q08921 107 Phosphoserine +Q08921 115 Phosphoserine +Q08921 144 Phosphoserine +Q08921 203 Phosphoserine +Q08921 215 Phosphoserine +Q08921 290 Phosphoserine +Q08921 397 Phosphoserine +Q08921 575 Phosphoserine +Q08921 707 Phosphoserine +P32776 150 Phosphothreonine +P33339 311 Phosphoserine +Q08686 201 Phosphoserine +Q08686 264 Phosphoserine +P33315 286 Phosphoserine +P33315 648 Glycyl +Q12239 114 N-linked +P36165 55 Phosphoserine +P36165 737 Phosphoserine +P36165 749 Phosphoserine +P36165 751 Phosphoserine +P36165 836 Phosphoserine +P47183 62 N6-(pyridoxal +P43534 62 N6-(pyridoxal +P89886 1 N-acetylmethionine +Q12049 1 N-acetylmethionine +P40462 2 N-acetylserine +Q12513 24 Phosphoserine +Q12513 68 Phosphoserine +P53840 626 Phosphoserine +P53840 654 Phosphoserine +P53840 1056 Phosphoserine +P53840 1058 Phosphoserine +P53840 1213 Phosphoserine +P40310 119 Phosphoserine +Q03280 1890 Phosphoserine +Q03280 2096 Phosphothreonine +Q03280 2119 Phosphoserine +Q03280 2376 Phosphoserine +Q03280 2406 Phosphoserine +Q03280 2418 Phosphoserine +P35180 172 Phosphoserine +P38825 55 Phosphoserine +P32830 2 N-acetylserine +P33890 231 GPI-anchor +Q08422 2 N-acetylserine +Q08422 43 Phosphoserine +Q08422 54 Phosphoserine +P04786 14 Phosphoserine +P04786 15 Phosphoserine +P04786 24 Phosphoserine +P04786 49 Phosphoserine +P04786 76 Phosphoserine +P06786 1086 Phosphothreonine%3B +P06786 1087 Phosphoserine%3B +P06786 1252 Phosphoserine +P06786 1258 Phosphothreonine%3B +P06786 1266 Phosphoserine%3B +P06786 1269 Phosphoserine%3B +P06786 1272 Phosphoserine%3B +P06786 1353 Phosphoserine%3B +P06786 1356 Phosphoserine%3B +P06786 1408 Phosphoserine%3B +P06786 1423 Phosphoserine%3B +Q06177 28 Phosphoserine +Q06177 79 Phosphoserine +P49334 44 Phosphoserine +P49334 46 Phosphoserine +P38288 236 N-linked +P38288 417 N-linked +P12685 15 Phosphoserine +P12685 414 Phosphoserine +P12685 534 Phosphoserine +P12685 100 N-linked +P12685 169 N-linked +P12685 222 N-linked +P12685 227 N-linked +P12685 251 N-linked +P12685 369 N-linked +P12685 383 N-linked +P12685 497 N-linked +P12685 501 N-linked +P12685 532 N-linked +P12685 580 N-linked +P12685 677 N-linked +P12685 919 N-linked +P12685 1030 N-linked +P12685 1135 N-linked +Q12400 16 Phosphothreonine +Q12400 283 Phosphoserine +Q02648 107 Phosphoserine +P32643 2 N-acetylserine +P32600 10 Phosphothreonine +P17536 195 Phosphoserine +P17536 39 Glycyl +P17536 59 Glycyl +P17536 187 Glycyl +P53283 50 Phosphoserine +Q12256 589 Phosphothreonine +Q12256 606 Phosphothreonine +Q12256 608 Phosphothreonine +Q12256 633 Phosphoserine +Q12256 646 Phosphoserine +Q05024 113 Phosphoserine +Q05024 225 Phosphoserine +Q05024 201 Glycyl +Q05024 215 Glycyl +P33753 92 Phosphoserine +P33753 93 Phosphoserine +P22217 54 Glycyl +P22217 66 Glycyl +P22217 96 Glycyl +P34760 174 Phosphothreonine +P34760 14 Glycyl +P34760 89 Glycyl +P34760 132 Glycyl +P40061 19 Phosphoserine +P40061 81 Phosphoserine +P40061 84 Phosphoserine +P40061 87 Phosphoserine +P40061 141 Phosphoserine +P40552 245 GPI-anchor +P40552 234 N-linked +Q12000 301 Phosphoserine +Q06266 40 Phosphoserine +Q06266 100 Phosphoserine +Q07824 19 Phosphoserine%3B +Q07824 52 Phosphothreonine%3B +Q07824 72 Phosphoserine +Q07824 76 Phosphoserine +Q07824 89 Phosphothreonine +Q07824 91 Phosphoserine +Q07824 342 Phosphoserine%3B +Q12199 55 Phosphothreonine +P23254 286 Phosphoserine +P23254 335 Phosphoserine +P23254 402 Phosphoserine +P23254 492 Phosphoserine +P23254 647 Glycyl +Q03322 31 Phosphothreonine%3B +Q03322 205 S-palmitoyl +Q03322 206 S-palmitoyl +Q03322 183 Glycyl +P53322 27 Phosphoserine +P53322 283 Glycyl +Q08919 139 N-linked +Q08919 213 N-linked +Q08919 529 N-linked +Q03774 93 Phosphoserine +P32893 393 Phosphoserine +P32893 398 Phosphoserine +Q02208 397 Phosphoserine +Q02208 405 Phosphothreonine +P07213 174 Phosphoserine +P48560 80 GPI-anchor +P48560 69 N-linked +P00942 4 Phosphothreonine +P00942 71 Phosphoserine +P00942 215 Phosphoserine +P00942 223 Glycyl +P40414 55 Phosphoserine +P40414 116 Phosphoserine +P40414 157 Phosphoserine +Q06451 55 Phosphoserine +Q06451 98 Phosphothreonine +Q06451 101 Phosphoserine +Q06451 132 Phosphoserine +P36029 569 Phosphoserine +Q04183 379 Phosphoserine +Q04183 387 Phosphoserine +P38427 49 Phosphoserine +P38427 53 Phosphoserine +P38427 56 Phosphoserine +P38427 71 Phosphoserine +P38427 77 Phosphoserine +P38427 135 Phosphoserine +P38427 147 Phosphoserine +P38427 161 Phosphoserine +P38427 229 Phosphoserine +P38427 251 Phosphothreonine +P38427 303 Phosphoserine +P38427 815 Phosphothreonine +P35172 52 Phosphoserine +P35172 53 Phosphoserine +P35172 88 Phosphothreonine +P35172 112 Phosphoserine +P34219 280 Phosphoserine +P34219 333 Phosphoserine +P34219 341 Phosphoserine +P34219 366 Phosphoserine +P33448 1 N-acetylmethionine +P38811 2 N-acetylserine +P38811 172 Phosphoserine +P38811 542 Phosphoserine +Q08693 228 N-linked +Q08693 669 N-linked +Q08693 736 N-linked +P48561 596 Phosphoserine +P48561 602 Phosphoserine +P28584 216 N-linked +P28584 233 N-linked +P28584 265 N-linked +P33122 104 Phosphoserine +P33122 237 Phosphothreonine +P21734 93 Glycyl +P33296 139 Phosphoserine +P33296 178 Phosphothreonine +P32571 443 Phosphoserine +P19812 296 Phosphoserine +P19812 300 Phosphoserine +P19812 1938 Phosphoserine +Q07963 1218 Phosphoserine +Q07963 1222 Phosphoserine +Q07963 709 Glycyl +Q06682 139 Phosphoserine +P29509 303 Phosphoserine +P38962 63 N-linked +P38962 86 N-linked +P38962 185 N-linked +P22803 62 Phosphoserine +P22803 67 Glycyl +P22803 97 Glycyl +Q12094 286 Phosphoserine +Q12094 289 Phosphoserine +Q08747 218 Phosphoserine +Q08747 220 Phosphoserine +Q08747 223 Phosphoserine +P14682 186 Phosphoserine +P14682 282 Phosphoserine +P14682 292 Phosphoserine +P40032 607 Phosphoserine +P38426 148 Phosphoserine +P38426 150 Phosphoserine +P38426 181 Phosphoserine +P38426 265 Phosphothreonine +P38426 267 Phosphoserine +P38426 273 Phosphoserine +P38426 960 Phosphoserine +P46959 302 Phosphoserine +Q12009 7 Phosphoserine%3B +Q12009 59 Phosphoserine +P53250 167 Phosphoserine +P53250 172 Phosphoserine +P00899 81 Phosphoserine +P00899 223 Phosphothreonine +P00937 2 Phosphoserine +P00931 384 N6-(pyridoxal +P00931 540 Phosphoserine +P00931 683 Phosphoserine +Q04767 146 Phosphothreonine +Q04767 153 Phosphothreonine +Q04767 22 N-linked +Q99394 2 N-acetylserine +Q04120 174 Phosphothreonine +Q04120 14 Glycyl +Q04120 89 Glycyl +Q04120 132 Glycyl +P36097 817 Phosphoserine +P16649 439 Phosphoserine +P32356 2 N-acetylserine +P32356 20 Phosphoserine +P32356 21 Phosphoserine +P32356 23 Phosphoserine +P32356 58 Phosphothreonine +P32356 60 Phosphoserine +P32356 66 Phosphoserine +P32356 83 Phosphoserine +P53044 354 Phosphoserine +P33202 87 Phosphothreonine +P33202 349 Glycyl +Q02724 2 N-acetylserine +Q02724 21 Phosphoserine +Q02724 25 Phosphoserine +Q02724 179 Phosphothreonine +Q02724 264 Phosphoserine +P28274 422 Glycyl +P40362 182 Phosphoserine +P40362 184 Phosphoserine +P40498 53 Phosphoserine +P40498 63 Phosphoserine +P40498 196 Phosphoserine +P16140 4 Phosphoserine +P16140 137 Phosphoserine +P16140 503 Phosphoserine +P16140 504 Phosphoserine +P16140 511 Phosphoserine%3B +P16140 515 Phosphoserine +P16140 14 Glycyl +P16140 508 Glycyl +P38358 420 N-linked +Q04602 62 Phosphoserine +Q04602 99 Phosphoserine +Q04602 106 Phosphoserine +Q04602 160 Phosphoserine +Q04602 192 Phosphoserine +Q04602 480 N-linked +Q04602 553 N-linked +P39538 84 Phosphoserine +P39538 1160 Phosphoserine +P47049 369 Phosphoserine +P40554 99 1-thioglycine +P40554 99 Glycyl +Q04500 34 Phosphoserine +Q04500 35 Phosphoserine +Q04500 151 Phosphoserine +Q04500 423 Phosphoserine +Q04500 424 Phosphoserine +Q04500 488 Phosphoserine +Q04500 500 Phosphoserine +Q04500 562 Phosphoserine +Q04500 668 Phosphoserine +Q04500 738 Phosphoserine +Q12339 182 Phosphoserine +P43123 218 Phosphoserine +P43123 461 Phosphoserine +P52490 92 Glycyl +Q02159 89 Glycyl +Q08562 121 Phosphoserine +P25386 1770 Phosphoserine +P42945 2 N-acetylserine +Q06078 2 N-acetylserine +Q06078 772 Phosphoserine +P53254 10 Phosphoserine +P53254 58 Phosphoserine +P53254 60 Phosphothreonine +P53254 64 Phosphoserine +P53276 95 Phosphothreonine +P53276 148 Phosphoserine +P53276 150 Phosphoserine +P21373 499 Phosphoserine +P21373 503 Phosphoserine +Q01476 907 Phosphoserine +P43593 389 Phosphothreonine +P43593 470 Phosphoserine +P38882 547 Phosphoserine +P38882 564 Phosphoserine +P25591 2 N-acetylalanine +P25591 119 Phosphoserine +P25591 149 Phosphothreonine +P25591 178 Phosphoserine +P25591 248 Phosphothreonine +P25591 269 Phosphoserine +P17255 2 N-acetylalanine +P17255 131 Phosphothreonine +P17255 858 Phosphoserine +P17255 928 Phosphoserine +P06104 120 Phosphoserine%3B +P38349 388 Phosphoserine +P38349 19 Glycyl +P53177 26 Phosphoserine +P53177 238 Phosphoserine +P22515 2 N-acetylserine +P22515 265 Phosphoserine +P22515 914 Phosphoserine +P22515 595 Glycyl +P22515 608 Glycyl +P52491 1 N-acetylmethionine +P15732 12 Phosphoserine +P15732 91 Glycyl +P38187 198 Phosphoserine +P25037 530 Phosphoserine +P25037 531 Phosphoserine +P25037 555 Phosphoserine +P25037 618 Phosphoserine +P25037 638 Phosphoserine +P25037 652 Phosphothreonine +P25037 653 Phosphoserine +P25037 654 Phosphoserine +P25037 670 Phosphoserine +P25037 755 Phosphoserine +P32861 2 N-acetylserine +P32861 17 Phosphoserine +P32861 19 Phosphothreonine +P32861 21 Phosphoserine +P32861 79 Phosphoserine +P32861 369 Omega-N-methylarginine +Q08960 496 Glycyl +P38820 1 N-acetylmethionine +P38820 326 Phosphoserine +P15731 12 Phosphoserine +P15731 91 Glycyl +P34223 128 Phosphoserine +P34223 210 Phosphoserine +P34223 224 Phosphoserine +P34223 315 Phosphoserine +P34223 321 Phosphoserine +P34223 322 Phosphoserine +P34223 331 Phosphothreonine +P34223 241 Glycyl +Q04511 511 Phosphoserine +Q04511 514 Phosphothreonine +P40537 788 Phosphoserine +P40537 903 Phosphoserine +P40537 983 Phosphoserine +P40537 984 Phosphoserine +Q12151 122 Phosphothreonine +Q12151 519 Phosphoserine +P50623 2 N-acetylserine +P0CG63 76 Glycyl +Q03327 1 N-acetylmethionine +P39547 11 Glycyl +P39547 218 Glycyl +P18562 82 Phosphoserine +P27515 17 Phosphoserine +P27515 276 Phosphoserine +P32366 1 N-acetylmethionine +Q06708 767 Phosphoserine +Q06708 805 Phosphoserine +Q06708 867 Phosphoserine +Q99385 1 N-acetylmethionine +Q99385 13 Phosphoserine +P53058 26 N-linked +P53058 48 N-linked +P53058 91 N-linked +P53058 139 N-linked +P53058 152 N-linked +Q08926 140 Phosphoserine +Q08926 185 Phosphoserine +Q08926 205 Phosphoserine +P39001 114 Phosphoserine +P39001 141 Phosphoserine +P39001 150 Phosphoserine +P39001 228 Phosphoserine +P39001 316 Phosphoserine +P39001 318 Phosphoserine +P39001 645 Phosphoserine +P23202 2 N-acetylmethionine +Q03714 374 Phosphoserine +Q03714 376 Phosphoserine +Q03714 379 Phosphoserine +P36172 70 N-linked +P36172 423 N-linked +P04840 109 Phosphoserine +P04840 117 Phosphothreonine +P40157 170 Phosphoserine +P40157 195 Phosphoserine +P40157 196 Phosphoserine +P40157 222 Phosphoserine +P40157 486 Phosphothreonine +Q06685 31 Phosphoserine +Q06685 54 Phosphoserine +Q06685 77 Phosphoserine +Q06685 895 Phosphoserine +Q06685 1107 Phosphoserine +P39968 11 Phosphoserine +P39968 16 Phosphoserine +P39968 2 N-myristoyl +P39968 4 S-palmitoyl +P39968 5 S-palmitoyl +P39968 7 S-palmitoyl +P39968 77 Glycyl +P39968 515 Glycyl +Q05934 21 N-linked +Q05934 242 N-linked +Q05934 291 N-linked +Q05934 540 N-linked +Q05934 645 N-linked +Q05934 649 N-linked +Q05934 652 N-linked +Q05934 662 N-linked +Q05934 669 N-linked +Q05934 673 N-linked +Q05934 688 N-linked +Q05934 722 N-linked +P23642 25 Phosphoserine +P23642 215 N-linked +P23642 251 N-linked +P48836 2 N-acetylserine +P32319 96 N-linked +P32319 170 N-linked +P32319 447 N-linked +P32319 793 N-linked +P32319 1010 N-linked +P32319 1303 N-linked +P32913 544 Phosphoserine +Q04272 2 N-myristoyl +P39702 1 N-acetylmethionine +P38329 34 Phosphoserine +P38329 654 Phosphoserine +P38329 915 Phosphoserine +P38329 918 Phosphoserine +P40522 409 Phosphoserine +Q08438 90 Phosphothreonine +P53285 74 N-linked +P53285 145 N-linked +Q06525 150 Phosphoserine +Q12132 162 Phosphoserine +Q12132 163 Phosphoserine +P53950 164 Phosphoserine +P53950 1020 N-linked +P53950 1099 N-linked +P47161 55 N-linked +P47161 237 N-linked +P47161 568 N-linked +P47161 599 N-linked +P47161 670 N-linked +P37370 519 Phosphoserine +P37370 762 Phosphoserine +P37370 109 N-linked +P37370 212 N-linked +P37370 337 N-linked +P37370 383 N-linked +P37370 784 N-linked +P37370 796 N-linked +Q03631 128 Phosphothreonine +P31412 2 N-acetylalanine +P22203 2 N-acetylserine +Q04301 123 N-linked +Q04301 324 N-linked +Q04301 504 N-linked +P25594 195 N-linked +P53262 69 N-linked +P53262 104 N-linked +P53262 172 N-linked +P32563 2 N-acetylalanine +P38959 26 Phosphoserine +P38959 53 Phosphoserine +Q12071 69 Phosphoserine +Q12071 72 Phosphoserine +Q12071 74 Phosphothreonine +P47111 137 Phosphoserine +Q12016 1 N-acetylmethionine +Q12016 8 Phosphoserine +Q12016 52 N-linked +Q06385 14 Phosphoserine +Q06385 19 Phosphoserine +Q07655 22 Phosphoserine +Q07655 206 Phosphoserine +Q07655 258 Phosphoserine +Q07655 283 Phosphoserine +P42839 26 Phosphothreonine +P42839 32 Phosphoserine +P42839 33 Phosphothreonine +P42839 110 Phosphoserine +P42839 118 Phosphothreonine +P42839 121 Phosphoserine +P42839 361 N-linked +P39904 602 Phosphoserine +P54787 375 Phosphoserine +Q06263 183 Phosphoserine +Q06263 195 Phosphothreonine +Q06263 233 Phosphoserine +P47165 79 Phosphoserine +P53076 2 N-acetylserine +P53076 147 Phosphoserine +P53076 246 Phosphoserine +P53076 248 Phosphoserine +P53076 277 Phosphoserine +P22219 2 N-myristoyl +P21576 579 Phosphoserine +P21576 599 Phosphoserine +Q04338 2 N-acetylserine +Q04338 110 Phosphoserine +Q04338 149 Phosphoserine +P40438 479 N-linked +P40438 769 N-linked +P40438 986 N-linked +P40890 479 N-linked +P40890 769 N-linked +P40890 986 N-linked +P34761 231 Phosphoserine +P40463 53 Phosphoserine +P40463 61 Phosphoserine +P40463 102 Phosphoserine +P40463 172 Phosphoserine +P40463 299 Phosphoserine +P40463 301 Phosphoserine +P40463 303 Phosphoserine +P40463 325 Phosphoserine +Q07878 1364 Phosphoserine +Q07878 1382 Phosphoserine +Q07878 1715 Phosphoserine +Q07878 1729 Phosphoserine +Q07878 1731 Phosphoserine +Q03390 12 Phosphoserine +P53853 3 Phosphoserine +Q12215 84 N-linked +Q12215 367 N-linked +Q12215 370 N-linked +P38739 340 N-linked +P38739 386 N-linked +P38739 389 N-linked +P38739 398 N-linked +P38739 479 N-linked +P38739 553 N-linked +P38739 583 N-linked +P43582 75 Phosphoserine +P43582 78 Phosphothreonine +P43582 50 Glycyl +P43582 60 Glycyl +P53241 32 Phosphoserine +P53241 33 Phosphoserine +P53241 43 Phosphoserine +P40547 226 Phosphoserine +P38735 11 N-linked +P38735 370 N-linked +P20795 626 Phosphoserine +P34110 846 Phosphoserine +P34110 848 Phosphoserine +P34110 868 Phosphoserine +Q02725 43 Phosphoserine +Q02725 45 Phosphoserine +Q02725 50 Phosphoserine +Q02725 183 Phosphothreonine +Q02725 195 Phosphoserine +Q02725 198 Phosphoserine +Q02725 270 Phosphoserine +Q02725 274 Phosphoserine +Q02725 589 Phosphoserine +Q02725 592 Phosphoserine +Q02725 621 Phosphoserine +Q02725 622 Phosphoserine +P47075 75 Glycyl +Q12416 47 Phosphothreonine +Q12416 57 Phosphothreonine +Q12416 59 Phosphoserine +Q12416 62 Phosphoserine +Q12416 88 Phosphoserine +Q12416 113 Phosphoserine +Q12416 115 Phosphoserine +Q12416 154 Phosphoserine +Q12416 156 Phosphoserine +Q12416 161 Phosphoserine +Q12416 262 Phosphoserine +Q12416 288 Phosphoserine +Q12416 290 Phosphothreonine +Q12363 187 Phosphothreonine +Q12363 200 Phosphoserine +Q12363 370 Phosphothreonine +Q12363 406 Phosphothreonine +P36095 203 Glycyl +P40343 157 Phosphoserine +P40343 495 Phosphoserine +P40343 613 Phosphoserine +P40343 294 Glycyl +P36116 2 N-acetylalanine +Q03388 425 Phosphoserine +P40046 2 N-acetylserine +P43585 182 Phosphoserine +P43585 187 Phosphoserine +P43585 196 Phosphoserine +P43585 264 Phosphoserine +P43585 583 Phosphoserine +P43585 615 Phosphoserine +P43585 616 Phosphoserine +P43585 620 Phosphothreonine +P43585 626 Phosphoserine +P43585 657 Phosphoserine +P53832 402 Phosphothreonine +P53832 455 Phosphoserine +P53832 458 Phosphoserine +P42826 244 Phosphoserine +P33301 349 Phosphoserine +P33301 533 Phosphoserine +P33301 534 Phosphoserine +P33301 553 Phosphoserine +P33301 555 Phosphothreonine +Q02792 574 Phosphoserine +P30822 1080 Phosphoserine +P36017 188 Phosphoserine +P36017 210 Cysteine +P36017 208 S-geranylgeranyl +P36017 210 S-geranylgeranyl +Q03897 759 Phosphoserine +P38216 2 N-acetylserine +P38216 32 Glycyl +P38239 2 N-acetylserine +P38243 182 Phosphoserine +P38243 184 Phosphothreonine +P38243 186 Phosphoserine +P32386 936 Phosphoserine +P32386 940 Phosphoserine +P32386 955 Phosphoserine +P32386 6 N-linked +P32386 97 N-linked +P25349 244 Cysteine +P25349 243 S-palmitoyl +P25349 244 S-farnesyl +P25351 313 Phosphoserine +P25351 603 Phosphoserine +P25639 219 Phosphoserine +P25639 87 N-linked +P25639 98 N-linked +P25639 250 Glycyl +Q12489 2 N-acetylserine +Q12489 13 Glycyl +Q03193 229 Phosphoserine +Q03193 251 N-linked +Q03193 259 N-linked +Q03780 1 N-acetylmethionine +Q03780 63 Phosphoserine +Q03780 254 Phosphoserine +Q03780 313 Phosphoserine +Q03780 342 Phosphoserine +Q03780 345 Phosphoserine +Q03780 390 Phosphoserine +Q03780 477 Phosphoserine +Q03780 492 Phosphoserine +Q03780 546 Phosphoserine +Q03780 683 Phosphoserine +Q03780 699 Phosphoserine +P34225 290 Phosphothreonine +P34225 293 Phosphoserine +P34225 299 Phosphoserine +P43590 50 Glycyl +P53273 42 Phosphoserine +P53273 127 Phosphoserine +P53273 130 Phosphothreonine +P53273 140 Phosphoserine +P53273 144 Phosphoserine +P53273 149 Phosphoserine +P53273 152 Phosphoserine +P53273 153 Phosphoserine +P53273 842 Phosphoserine +P53273 847 Phosphothreonine +P48236 78 Phosphoserine +P38750 305 Phosphothreonine +P38750 546 Phosphoserine +P38750 588 Phosphothreonine +P38708 149 Phosphoserine +P38708 170 Phosphothreonine +P38708 655 Phosphoserine +P38716 198 N6-(pyridoxal +P34231 675 Phosphoserine +P34231 678 Phosphoserine +P34231 61 N-linked +P34231 84 N-linked +P34231 115 N-linked +P34231 154 N-linked +P34231 176 N-linked +P34231 197 N-linked +P34231 207 N-linked +P34231 228 N-linked +P34231 241 N-linked +P34231 267 N-linked +P34231 293 N-linked +P34231 299 N-linked +P34231 312 N-linked +P34231 335 N-linked +P34231 351 N-linked +P34231 373 N-linked +P34231 389 N-linked +P34231 519 N-linked +P34231 709 N-linked +P34231 714 N-linked +P34231 724 N-linked +P34231 697 Glycyl +Q07988 203 GPI-anchor +Q07988 148 N-linked +Q07988 181 N-linked +Q07988 191 N-linked +Q05131 425 Phosphoserine +Q03177 528 Phosphoserine +Q03177 771 Phosphothreonine +P53964 270 N-linked +Q99247 668 Phosphoserine +Q99247 693 Phosphothreonine +Q92393 416 Phosphoserine +Q08844 28 N-linked +Q08844 43 N-linked +Q08844 87 N-linked +Q08844 103 N-linked +P53049 10 Phosphoserine +P53049 24 Phosphoserine +P53049 53 Phosphothreonine +P53049 661 N-linked +P53049 759 N-linked +P53049 799 N-linked +Q12079 155 N-linked +Q12079 265 N-linked +Q02864 21 Phosphoserine +Q06537 27 N-linked +P18961 63 Phosphothreonine +P18961 66 Phosphothreonine +P18961 72 Phosphoserine +P18961 499 Phosphothreonine +P18961 501 Phosphothreonine%3B +P18961 641 Phosphoserine%3B +P18961 650 Phosphoserine +P18961 659 Phosphothreonine%3B +P18961 669 Phosphoserine +P32939 208 Cysteine +P32939 206 S-geranylgeranyl +P32939 208 S-geranylgeranyl +P32939 147 Glycyl +P36036 1 N-acetylmethionine +P38079 293 Phosphoserine +P38079 341 Phosphothreonine +P38079 343 Phosphoserine +P38079 286 Glycyl +Q2V2Q2 55 GPI-anchor +Q2V2Q2 25 N-linked +Q2V2Q2 30 N-linked +Q2V2Q2 35 N-linked +Q2V2Q2 40 N-linked +P39109 251 Phosphoserine +P39109 873 Phosphoserine +P39109 903 Phosphoserine +P39109 908 Phosphoserine +P39109 911 Phosphothreonine +P39109 914 Phosphoserine +Q12316 416 Phosphoserine +Q12222 211 Phosphoserine +P38733 111 N-linked +Q99219 2 N-acetylserine +P53845 2 N-acetylserine +P40440 87 N-linked +P47098 416 Phosphoserine +P47072 514 Phosphoserine +P36015 158 Phosphothreonine +P36015 197 Cysteine +P36015 196 S-palmitoyl +P36015 197 S-farnesyl +P53925 22 Phosphoserine +P53925 56 Phosphoserine +P53925 63 Phosphoserine +P53925 244 Phosphoserine +Q08234 41 N-linked +Q08234 86 N-linked +Q08234 101 N-linked +Q08234 151 N-linked +Q08234 341 N-linked +Q08234 349 N-linked +Q08234 371 N-linked +Q08234 528 N-linked +Q08234 983 N-linked +Q12275 99 Phosphoserine +Q12275 751 Phosphoserine +Q12275 28 N-linked +Q12275 71 N-linked +Q12275 98 N-linked +Q12275 128 N-linked +Q12275 151 N-linked +Q12275 209 N-linked +Q12275 288 N-linked +Q12275 328 N-linked +Q12275 575 N-linked +Q12275 644 N-linked +Q12275 730 N-linked +Q12275 881 N-linked +Q12275 917 N-linked +Q12275 995 N-linked +Q12275 1009 N-linked +Q12275 1198 N-linked +Q12275 1301 N-linked +Q12275 1302 N-linked +Q12275 1447 N-linked +Q12275 1472 N-linked +Q12275 1488 N-linked +Q12275 1565 N-linked +Q12275 1597 N-linked +Q12275 1634 N-linked +Q12282 212 GPI-anchor +Q12282 155 N-linked +Q12282 160 N-linked +Q12282 203 N-linked +Q12282 212 N-linked +Q06328 136 Phosphoserine +P40583 515 GPI-anchor +P40583 57 N-linked +P40583 149 N-linked +P40583 156 N-linked +P40583 161 N-linked +P40583 183 N-linked +P40583 195 N-linked +P40583 311 N-linked +P40583 363 N-linked +P40583 375 N-linked +P40583 379 N-linked +P40583 472 N-linked +P48559 415 S-geranylgeranyl +P48559 416 S-geranylgeranyl +P51996 2 N-acetylserine +P51996 221 S-geranylgeranyl +P51996 222 S-geranylgeranyl +P40517 31 Phosphothreonine +P40517 179 Phosphoserine +P50111 229 Phosphoserine +Q07555 267 Phosphoserine +P0CX65 416 Phosphoserine +Q12301 225 Phosphoserine +Q99315 2 N-acetylserine +P53278 286 Phosphoserine +P53278 343 Phosphoserine +P53278 347 Phosphoserine +P53278 809 Phosphothreonine +P38809 69 Phosphoserine +P38809 76 Phosphothreonine +P38809 189 Phosphothreonine +P38809 288 Phosphoserine +P38809 294 Phosphoserine +P38809 359 Phosphoserine +P38809 78 Glycyl +P38809 187 Glycyl +P38809 242 Glycyl +P38841 41 Phosphoserine +P40566 594 Phosphothreonine +P47100 416 Phosphoserine +P47139 39 Phosphoserine +Q07895 68 N-linked +Q07895 112 N-linked +Q07895 152 N-linked +Q07895 200 N-linked +Q07895 291 N-linked +Q07895 333 N-linked +Q07895 450 N-linked +Q07895 521 N-linked +Q07895 542 N-linked +Q07895 569 N-linked +Q07895 663 N-linked +Q07895 679 N-linked +Q07895 688 N-linked +Q07834 762 Phosphoserine +Q12110 127 Phosphoserine +P0CX68 416 Phosphoserine +Q05948 22 Glycyl +Q06146 2 N-acetylvaline +Q06146 44 Phosphothreonine +Q06146 49 Phosphoserine +Q06146 69 Phosphoserine +Q06146 121 Phosphoserine +Q06146 126 Phosphoserine +Q06146 129 Phosphoserine +Q06146 137 Phosphoserine +Q06146 139 Phosphoserine +Q06146 159 Phosphothreonine +Q06146 238 Phosphoserine +Q06146 240 Phosphoserine +Q06146 242 Phosphoserine +Q06146 270 Phosphoserine +Q06137 6 Phosphoserine +P53751 35 N-linked +P53751 336 N-linked +P53751 553 N-linked +P53751 846 N-linked +P53751 985 N-linked +P53962 351 Phosphoserine +P0CX59 416 Phosphoserine +Q06839 310 Phosphoserine +Q06839 451 Phosphoserine +P0C2I9 416 Phosphoserine +P0C2J1 416 Phosphoserine +Q12523 47 Phosphoserine +Q12523 65 Phosphoserine +P43587 2 N-acetylserine +P43587 22 Phosphoserine +P43587 133 Phosphoserine +P36019 220 Cysteine +P36019 218 S-geranylgeranyl +P36019 220 S-geranylgeranyl +P0CX57 416 Phosphoserine +P38749 135 Phosphoserine +O43137 22 Phosphoserine +Q12217 416 Phosphoserine +Q12193 416 Phosphoserine +P38355 199 Phosphothreonine +P38355 234 Phosphoserine +P38142 63 N-linked +Q8J0M4 71 Phosphoserine +Q8J0M4 74 Phosphoserine +Q8J0M4 86 Glycyl +Q12235 500 Phosphoserine +Q12235 501 Phosphoserine +Q12235 146 N-linked +Q03855 416 Phosphoserine +Q12407 90 Phosphoserine +P0CX66 416 Phosphoserine +P40028 730 Phosphoserine +P40028 731 Phosphoserine +Q12141 416 Phosphoserine +P53274 106 Phosphoserine +P53316 29 Phosphoserine +P53316 433 Phosphoserine +P53316 435 Phosphoserine +P53316 482 Phosphoserine +P53316 485 Phosphoserine +P53316 486 Phosphothreonine +P53316 501 Phosphoserine +P53110 1 N-acetylmethionine +P38833 96 Phosphoserine +P38870 2 N-acetylserine +P36134 17 Glycyl +P0CX72 416 Phosphoserine +Q3E760 4 N-linked +P53740 78 N-linked +P53740 123 N-linked +P53740 187 N-linked +P53740 202 N-linked +P53740 213 N-linked +P53740 240 N-linked +P53740 291 N-linked +Q08560 14 N-linked +Q08560 15 N-linked +Q12441 416 Phosphoserine +Q99231 416 Phosphoserine +Q03362 10 N-linked +Q03362 70 N-linked +Q03362 74 N-linked +P0CX71 416 Phosphoserine +P43562 52 N-linked +P43562 374 N-linked +P53249 59 N-linked +P53249 98 N-linked +P53249 126 N-linked +P53249 171 N-linked +P53249 221 N-linked +P53249 230 N-linked +P53249 262 N-linked +P38887 305 N-linked +P38887 497 N-linked +P38887 577 N-linked +P0CF21 39 N6-(pyridoxal +P40520 68 N-linked +P40520 84 N-linked +P0C2I7 416 Phosphoserine +Q12402 2 N-acetylserine +Q02831 59 Phosphoserine +Q02831 95 Phosphoserine +Q6Q5H1 416 Phosphoserine +Q99395 68 Phosphoserine +Q07688 64 Phosphohistidine +P40049 65 N-linked +P40049 86 N-linked +P40049 93 N-linked +P40049 220 N-linked +P40049 231 N-linked +P43564 435 Phosphoserine +P43564 1037 Phosphoserine +P53066 1 N-acetylmethionine +P53066 172 Phosphoserine +P0CX19 184 GPI-anchor +P0CX19 28 N-linked +P0CX19 138 N-linked +P38745 497 Phosphoserine +P38745 152 N-linked +P38745 253 N-linked +Q04116 315 Phosphoserine +P40543 107 Phosphoserine +P40543 172 Phosphoserine +P40508 230 Phosphoserine +P40017 2 N-acetylserine +P40017 783 Phosphoserine +Q3E776 114 N-linked +P42937 1 N-acetylmethionine +Q3E7B7 37 Phosphoserine +P0CX67 416 Phosphoserine +P53139 2 N-myristoyl +P53139 4 S-palmitoyl +P0CX74 416 Phosphoserine +P47121 15 N-linked +P40361 9 Phosphoserine +P40361 41 Phosphoserine +P40361 178 Phosphoserine +P40361 180 Phosphoserine +P36138 21 Glycyl +P40544 184 N-linked +P40544 274 N-linked +P40544 285 N-linked +P0C2I3 416 Phosphoserine +P40095 63 N-linked +P40095 123 N-linked +P40095 236 N-linked +P40095 437 N-linked +P40095 442 N-linked +P40095 498 N-linked +P40095 535 N-linked +P40095 541 N-linked +Q12085 416 Phosphoserine +Q12485 416 Phosphoserine +Q12269 416 Phosphoserine +P40442 28 N-linked +P40442 35 N-linked +P40442 468 N-linked +P40442 664 N-linked +P36114 196 Phosphothreonine +P36114 246 Phosphoserine +P36114 377 Phosphoserine +P36114 380 Phosphoserine +P0C2I6 416 Phosphoserine +Q06251 1 N-acetylmethionine +Q06251 31 Phosphoserine +Q06251 34 Phosphoserine +Q06251 84 Phosphoserine +Q06251 235 Phosphothreonine +Q05777 232 GPI-anchor +Q05777 229 N-linked +P0CX76 416 Phosphoserine +Q04835 40 Glycyl +Q03730 93 Phosphoserine +Q03161 88 Phosphoserine +P53826 99 N-linked +P53826 106 N-linked +P53947 148 Phosphoserine +P53947 256 Phosphoserine +P53947 276 Phosphoserine +P38806 183 Phosphoserine +P38806 185 Phosphothreonine +P38806 188 Phosphoserine +P53862 118 N-linked +Q08206 1 N-acetylmethionine +P0CX73 416 Phosphoserine +P0CX58 416 Phosphoserine +Q06522 95 N-linked +Q12152 456 Phosphoserine +Q12152 533 Phosphoserine +P32618 154 Phosphothreonine +P32618 501 Phosphoserine +P32618 520 Phosphoserine +P32618 802 Phosphoserine +P32618 842 Phosphoserine +P32618 895 Phosphoserine +Q07950 73 Phosphoserine +Q07950 107 Phosphoserine +P43597 180 Phosphoserine +P43597 462 Phosphoserine +P43597 523 Phosphoserine +P43597 861 Phosphothreonine +P43597 975 Phosphoserine +P43597 1037 Phosphoserine +P43597 1046 Phosphoserine +P53120 1167 Phosphoserine +P53120 1191 Phosphotyrosine +P53120 1198 Phosphoserine +P53120 1199 Phosphoserine +P25637 187 Glycyl +P40483 361 Phosphoserine +P40483 245 Glycyl +P40483 478 Glycyl +P40483 518 Glycyl +P40483 579 Glycyl +P40483 590 Glycyl +P40483 596 Glycyl +P53108 60 Phosphoserine +P47078 33 N-linked +P36119 426 Phosphoserine +P36119 431 Phosphoserine +P36119 434 Phosphoserine +P36119 457 Phosphoserine +P36119 509 Glycyl +Q06698 9 Phosphoserine +Q06698 816 Phosphoserine +Q03434 416 Phosphoserine +Q04336 299 Phosphoserine +Q04336 984 Phosphoserine +Q04336 1013 Phosphothreonine +Q04336 1081 Phosphoserine +Q03559 11 Phosphoserine +Q03559 23 Phosphoserine +Q03559 26 Glycyl +Q03559 32 Glycyl +Q04869 2 Phosphoserine +P39523 1 N-acetylmethionine +P39523 553 Phosphoserine +P39523 586 Phosphoserine +P39523 619 Phosphoserine +P39523 649 Phosphoserine +P39523 681 Phosphoserine +P39523 766 Phosphoserine +P39523 771 Phosphoserine +Q03795 237 Phosphoserine +Q05016 260 Phosphoserine +Q03759 2 N-acetylserine +P53723 2 N-acetylserine +P53723 44 N-linked +P53723 98 N-linked +Q08910 26 N-linked +Q08910 48 N-linked +Q08910 91 N-linked +Q08910 139 N-linked +Q08910 152 N-linked +Q08910 183 N-linked +Q08157 224 Phosphoserine +Q08157 232 Phosphoserine +Q08157 363 Phosphoserine +P38070 90 Phosphoserine +P38070 105 Phosphoserine +P38070 107 Phosphothreonine +P38070 321 Phosphoserine%3B +P38070 490 Phosphothreonine%3B +P38070 513 Phosphoserine%3B +P53057 57 N-linked +P38815 65 Phosphoserine +P38815 66 Phosphoserine +Q99260 215 Cysteine +Q99260 213 S-geranylgeranyl +Q99260 215 S-geranylgeranyl +P31111 481 Phosphoserine +P40021 275 Phosphoserine +P40021 354 Phosphoserine +P40021 403 Phosphoserine +P40021 407 Phosphoserine +P40021 632 Phosphoserine +P40021 676 Phosphoserine +Q12512 28 N-linked +Q12512 57 N-linked +Q12512 98 N-linked +Q12512 217 N-linked +Q06325 26 N-linked +Q06325 59 N-linked +Q06325 106 N-linked +Q06325 131 N-linked +Q06325 140 N-linked +Q06325 143 N-linked +Q06325 148 N-linked +Q06325 175 N-linked +Q06325 308 N-linked +Q06325 391 N-linked +Q06325 455 N-linked +Q06325 478 N-linked +Q06325 484 N-linked +Q06325 549 N-linked +Q06325 552 N-linked +P38146 199 Cysteine +P38146 197 S-geranylgeranyl +P38146 199 S-geranylgeranyl +P38555 2 N-acetylserine +P38555 222 S-geranylgeranyl +P38555 223 S-geranylgeranyl +P36018 139 Phosphoserine +P36018 142 Phosphoserine +P36018 232 S-geranylgeranyl +P36018 233 S-geranylgeranyl +P36018 151 Glycyl +P38280 159 Phosphoserine +P38280 160 Phosphoserine +Q12324 636 Phosphothreonine +P53303 23 Phosphoserine +P53303 407 Phosphothreonine +P0C2I5 416 Phosphoserine +Q06689 654 Phosphoserine +Q06689 665 Phosphoserine +Q06689 49 N-linked +Q06689 72 N-linked +Q06689 103 N-linked +Q06689 142 N-linked +Q06689 160 N-linked +Q06689 194 N-linked +Q06689 215 N-linked +Q06689 228 N-linked +Q06689 252 N-linked +Q06689 286 N-linked +Q06689 299 N-linked +Q06689 318 N-linked +Q06689 322 N-linked +Q06689 358 N-linked +Q06689 375 N-linked +Q06689 405 N-linked +Q06689 429 N-linked +Q06689 468 N-linked +Q06689 671 Glycyl +Q04461 17 Phosphoserine +Q04461 23 Phosphoserine +Q04461 237 Phosphoserine +Q04461 249 Phosphoserine +Q04461 254 Phosphothreonine +Q04471 338 Phosphoserine +Q04670 416 Phosphoserine +Q03823 76 Phosphoserine +Q03823 79 Phosphoserine +Q03231 47 Phosphoserine +Q04867 190 Phosphoserine +Q03208 72 Phosphoserine +Q04773 1 N-acetylmethionine +Q04773 121 Phosphoserine +Q04773 126 Phosphoserine +Q12470 416 Phosphoserine +P53719 136 Phosphoserine +P40159 2 N-acetylserine +P40159 53 Phosphoserine +P40159 70 Phosphoserine +Q92392 416 Phosphoserine +Q12015 11 N-linked +Q12015 41 N-linked +Q12015 77 N-linked +Q12015 99 N-linked +Q12015 145 N-linked +Q08743 19 N-linked +Q08743 121 N-linked +Q08912 68 N-linked +Q08912 150 N-linked +Q08912 219 N-linked +Q08912 366 N-linked +Q08912 441 N-linked +Q08912 447 N-linked +Q08912 464 N-linked +Q08912 528 N-linked +Q12160 36 N-linked +Q06116 2254 Phosphoserine +Q06116 2278 Phosphoserine +Q06116 191 N-linked +Q06116 210 N-linked +Q06116 311 N-linked +Q06116 452 N-linked +Q06116 468 N-linked +Q06116 605 N-linked +Q06116 638 N-linked +Q06116 663 N-linked +Q06116 698 N-linked +Q06116 789 N-linked +Q06116 835 N-linked +Q06116 981 N-linked +Q06116 1255 N-linked +Q06116 1404 N-linked +Q06116 1476 N-linked +Q06116 1978 N-linked +Q06116 2189 N-linked +Q06116 2279 N-linked +P0CX60 416 Phosphoserine +Q06523 47 Phosphoserine +Q12159 2 N-acetylserine +Q12159 8 Phosphoserine +Q12159 100 Phosphoserine +P53107 272 Phosphothreonine +Q12436 148 Phosphoserine +Q12436 149 Phosphoserine +Q12436 162 Phosphoserine +Q12436 170 Phosphoserine +Q12436 188 Phosphothreonine +P32527 50 Phosphoserine +P40523 559 Phosphoserine +P47114 291 Phosphoserine +P47114 319 Phosphoserine +P46992 368 GPI-anchor +P46992 51 N-linked +P46992 99 N-linked +P46992 122 N-linked +P46992 146 N-linked +P46992 174 N-linked +P46992 219 N-linked +P46992 249 N-linked +P46992 267 N-linked +P46992 300 N-linked +P46992 328 N-linked +P46992 346 N-linked +P47087 176 Phosphoserine +Q07990 139 GPI-anchor +Q07990 77 N-linked +Q07990 104 N-linked +Q07990 120 N-linked +P0CX75 416 Phosphoserine +Q99296 82 Phosphoserine +Q99296 89 Phosphoserine +Q99296 483 Phosphoserine +Q99296 651 Phosphoserine +Q05854 1143 Phosphoserine +Q04706 416 Phosphoserine +Q3E842 45 N-linked +P0CX69 416 Phosphoserine +Q03219 263 Phosphoserine +Q03649 82 Glycyl +Q03697 209 Phosphoserine +Q03697 99 N-linked +Q12273 416 Phosphoserine +Q3E752 24 Phosphoserine +Q3E752 32 Phosphoserine +Q06833 640 Phosphoserine +Q06833 669 Phosphoserine +Q06833 717 Phosphoserine +Q06833 720 Phosphoserine +Q06833 723 Phosphoserine +Q06833 228 N-linked +Q06833 263 N-linked +Q06833 279 N-linked +Q06833 300 N-linked +Q06833 391 N-linked +Q06833 528 N-linked +Q06833 529 N-linked +Q06833 595 N-linked +Q06833 620 N-linked +Q06833 700 N-linked +Q06833 718 N-linked +Q06616 158 Phosphoserine +Q06616 170 Phosphoserine +Q06616 175 Phosphoserine +Q12697 1 N-acetylmethionine +Q12697 95 Phosphothreonine +Q12697 108 Phosphoserine +Q12697 1117 Phosphoserine +Q12697 1120 Phosphoserine +Q12303 483 GPI-anchor +Q12303 75 N-linked +Q12303 120 N-linked +Q12303 160 N-linked +Q12303 163 N-linked +Q12303 275 N-linked +Q12303 309 N-linked +Q12303 328 N-linked +Q12303 367 N-linked +Q12303 422 N-linked +Q12303 445 N-linked +Q12303 462 N-linked +P41920 60 Phosphoserine +Q08245 2 N-acetylserine +Q08245 2 Phosphoserine +Q08245 25 Phosphoserine +Q08245 40 Phosphoserine +Q08245 49 Phosphothreonine +Q08245 18 Glycyl +Q08245 23 Glycyl +Q08245 29 Glycyl +Q08245 34 Glycyl +Q08245 45 Glycyl +Q08245 57 Glycyl +Q08245 82 Glycyl +P53752 157 N-linked +P53975 270 N-linked +Q3E824 44 N-linked +P32329 548 GPI-anchor +P32329 95 N-linked +P32329 203 N-linked +P32329 232 N-linked +P32329 242 N-linked +P32329 245 N-linked +P32329 299 N-linked +P32329 358 N-linked +P32329 480 N-linked +P32329 522 N-linked +P32329 532 N-linked +P01123 1 N-acetylmethionine +P01123 172 Phosphoserine +P01123 174 Phosphoserine +P01123 23 S-palmitoyl +P01123 123 S-palmitoyl +P01123 205 S-geranylgeranyl +P01123 206 S-geranylgeranyl +P01123 144 Glycyl +P47043 156 Phosphoserine +P47043 166 Phosphoserine +P47043 515 Phosphoserine +P54786 50 Phosphoserine +Q12025 47 N-linked +P38966 238 Phosphoserine +P38966 241 Phosphoserine +P38966 316 Phosphoserine +P38966 324 Phosphoserine +P38966 327 Phosphoserine +P38966 609 Phosphoserine +P38966 612 Phosphoserine +P38966 668 Phosphoserine +P38966 760 Phosphoserine +Q12121 329 Phosphoserine +P40022 1 N-acetylmethionine +P35723 190 Glycyl +Q12173 2 N-acetylserine +P50089 215 Phosphoserine +P50089 667 Phosphoserine +P53183 339 Phosphoserine +P53133 223 Phosphoserine +P38616 40 N-linked +P38616 50 N-linked +P38616 53 N-linked +P38616 58 N-linked +P38616 61 N-linked +P38616 65 N-linked +P38616 87 N-linked +P38616 94 N-linked +P38616 100 N-linked +P38616 106 N-linked +P38616 118 N-linked +P38616 172 N-linked +P38616 239 N-linked +P38616 286 N-linked +P38829 2 N-acetylserine +P40449 16 Glycyl +P40449 35 Glycyl +P47099 416 Phosphoserine +P47115 221 Phosphoserine +P0C2I8 416 Phosphoserine +Q06247 24 Phosphothreonine +Q06247 27 Phosphoserine +Q06247 115 N-linked +Q06247 141 N-linked +Q06247 169 N-linked +Q06247 407 N-linked +Q06247 425 N-linked +Q06247 449 N-linked +Q06247 453 N-linked +Q06247 527 N-linked +Q06247 580 N-linked +Q08989 40 N-linked +Q08989 68 N-linked +Q08989 150 N-linked +Q08989 220 N-linked +Q08989 304 N-linked +Q08989 367 N-linked +Q08989 442 N-linked +Q08989 448 N-linked +Q08816 69 Phosphotyrosine +Q08816 105 Phosphoserine +Q08816 108 Phosphoserine +Q08816 342 Phosphoserine +Q12414 416 Phosphoserine +Q12010 9 N-linked +Q12010 189 N-linked +Q12010 275 N-linked +P32793 301 Phosphoserine +P32793 311 Phosphoserine +P26725 77 N-linked +P26725 82 N-linked +P26725 92 N-linked +P26725 167 N-linked +P26725 414 N-linked +P53735 16 Phosphoserine +P53735 131 Phosphoserine +P53735 498 Phosphoserine +P20107 387 Phosphoserine +P20107 393 Phosphoserine +P20107 397 Phosphoserine +P20107 357 Glycyl +P34240 178 Phosphoserine +P34240 188 Phosphoserine +Q06681 13 Phosphoserine +Q06681 411 Phosphoserine +Q06681 596 Phosphoserine +Q06681 1032 Phosphoserine +Q06681 1306 N-linked +Q06681 1373 N-linked +Q06681 1430 N-linked +P15891 2 N-acetylalanine +P15891 165 Phosphothreonine +P15891 167 Phosphoserine +P15891 169 Phosphoserine +P15891 181 Phosphothreonine +P15891 183 Phosphoserine +P15891 313 Phosphoserine +P15891 365 Phosphoserine +P15891 389 Phosphoserine +P15891 458 Phosphoserine +P15891 481 Phosphoserine +P15891 464 Glycyl +P32316 2 N-acetylthreonine +P32316 350 Phosphoserine +Q00362 124 Phosphoserine +P47096 176 Phosphoserine +P32357 253 Phosphoserine +P32357 274 Phosphothreonine +P32357 328 Phosphotyrosine +P32357 331 Phosphoserine +P32357 345 Phosphothreonine +P07248 54 Phosphoserine +P07248 188 Phosphothreonine +P07248 193 Phosphothreonine +P07248 230 Phosphoserine%3B +P07248 258 Phosphoserine +P07248 259 Phosphothreonine +P07248 299 Phosphoserine +P07248 323 Phosphoserine +P07248 325 Phosphoserine +P07248 327 Phosphothreonine +P38903 242 Phosphothreonine +P38903 257 Phosphothreonine +P47129 44 Phosphoserine +P47129 71 Phosphoserine +P47129 74 Phosphoserine +P47129 78 Phosphoserine +P47129 165 Phosphoserine +P47129 288 Phosphoserine +P14164 189 Phosphothreonine +P14164 193 Phosphoserine +P14164 467 Phosphoserine +P14164 554 Phosphoserine +P14164 618 Phosphoserine +P14164 624 Phosphoserine%3B +P14164 720 Phosphoserine%3B +P14164 18 Glycyl +P40535 171 Phosphoserine +P40535 179 Phosphoserine +P40535 399 Phosphoserine +P40535 557 Phosphoserine +P40535 559 Phosphothreonine +P31787 51 Glycyl +P31787 72 Glycyl +P32323 699 GPI-anchor +Q12471 55 Glycyl +P23542 2 N-acetylserine +P23542 255 N6-(pyridoxal +P23542 389 Phosphoserine +Q07622 184 Glycyl +Q07622 191 Glycyl +Q03771 2 N-acetylserine +P21192 80 Phosphoserine +P21192 122 Phosphoserine +P21192 247 Phosphoserine +P21192 249 Phosphoserine +P21192 253 Phosphoserine +P21192 259 Phosphothreonine +P21192 385 Phosphoserine +P21192 392 Phosphoserine +P21192 483 Phosphoserine +P21192 486 Phosphothreonine +P21192 501 Phosphothreonine +P21192 564 Phosphoserine +P21192 709 Phosphoserine +P21192 714 Phosphoserine +P28240 53 Phosphothreonine +P38720 50 Phosphoserine +Q01802 286 N6-(pyridoxal +Q08641 93 Phosphoserine +Q08641 150 Phosphothreonine +Q08641 321 Phosphoserine +Q08641 326 Phosphoserine +Q08641 347 Phosphothreonine +P40433 92 Phosphoserine +P40433 157 Phosphothreonine +P40433 644 Phosphoserine +P40433 652 Phosphoserine +P40433 659 Phosphoserine +P40433 667 Phosphoserine +Q00955 2 N-acetylserine +Q00955 2 Phosphoserine +Q00955 735 N6-biotinyllysine +Q00955 790 Phosphoserine +Q00955 1148 Phosphoserine +Q00955 1157 Phosphoserine +Q00955 1162 Phosphoserine +P40529 2 N-acetylserine +P40529 180 Phosphoserine +P40529 183 Phosphoserine +P40529 207 Phosphoserine +P46680 2 N-acetylserine +P52893 77 Phosphoserine +P52893 412 N6-(pyridoxal +P38065 727 Phosphothreonine +P38065 733 Phosphoserine +P53886 1462 Phosphoserine +P36154 78 Phosphoserine +P46367 96 Phosphoserine +P46367 216 Phosphothreonine +P46367 500 Phosphoserine +P40350 83 N-linked +P40350 119 N-linked +P43633 76 Phosphoserine +P43633 79 Phosphoserine +Q08269 2 N-acetylserine +Q08269 77 Phosphotyrosine +Q08269 85 Phosphoserine +Q08269 185 Phosphoserine +Q08269 188 Phosphoserine +Q08269 220 Phosphoserine +Q08269 221 Phosphoserine +Q08269 236 Phosphoserine +Q08269 242 Phosphothreonine +Q08269 850 Phosphoserine +P14904 356 Phosphoserine +P14904 107 N-linked +P14904 110 N-linked +P14904 448 N-linked +P60010 1 N-acetylmethionine +P60010 191 Glycyl +P25371 659 Phosphoserine +P25371 702 Phosphoserine +P25371 50 N-linked +P25371 114 N-linked +P25371 165 N-linked +P25371 221 N-linked +P25371 935 N-linked +P33304 472 Phosphoserine +P33304 526 Phosphoserine +P43636 170 N-linked +P43636 303 N-linked +P43636 371 N-linked +P43636 400 N-linked +P47029 155 Phosphoserine +P47029 162 Phosphoserine +P47029 213 Phosphoserine +P47029 586 Phosphoserine +P47029 826 Phosphoserine +P47029 838 Phosphoserine +P47029 900 Phosphoserine +P47029 1022 Phosphoserine +P47029 1023 Phosphoserine +P40502 2 N-acetylserine +P40563 18 Phosphothreonine +P40563 36 Phosphoserine +P40563 58 Phosphothreonine +P40563 70 Phosphoserine +P40563 85 Phosphothreonine +P40563 104 Phosphoserine +P40563 183 Phosphoserine +P40563 206 Phosphoserine +P40563 231 Phosphoserine +P40563 277 Phosphothreonine +P40563 284 Phosphoserine +P40563 324 Phosphoserine +P40563 552 Phosphothreonine +P40563 576 Phosphoserine +P40563 620 Phosphoserine +P40563 623 Phosphoserine +P40563 625 Phosphoserine +P40563 627 Phosphoserine +P40563 667 Phosphoserine +P40563 671 Phosphoserine +P40563 675 Phosphoserine +P40563 678 Phosphoserine +P16550 60 Phosphothreonine +P00330 2 N-acetylserine +P00330 213 Phosphoserine +P00330 223 Phosphothreonine +P00330 279 Phosphoserine +P00330 316 Phosphoserine +P00330 226 Glycyl +P00330 234 Glycyl +P00330 287 Glycyl +P00330 319 Glycyl +P00331 2 N-acetylserine +P00331 213 Phosphoserine +P00331 223 Phosphothreonine +P00331 279 Phosphoserine +P00331 316 Phosphoserine +P00331 226 Glycyl +P00331 234 Glycyl +P00331 287 Glycyl +P00331 319 Glycyl +Q04894 131 Phosphoserine +Q04894 315 Phosphoserine +Q04894 359 Phosphoserine +P38266 57 Phosphoserine +P38266 58 Phosphoserine +P38266 64 Phosphoserine +P38266 476 Phosphoserine +P38266 729 Phosphothreonine +P38266 861 Phosphothreonine +Q99299 25 Phosphoserine +P53954 262 N-linked +P53954 393 N-linked +P53954 480 N-linked +P53954 490 N-linked +P38313 41 Phosphoserine +P38313 45 Phosphoserine +P38313 53 Phosphoserine +P38313 59 Phosphoserine +P38313 101 Phosphoserine +P52910 679 Phosphoserine +P52910 506 Glycyl +P25376 6 Phosphoserine +P25376 633 S-palmitoyl +P25376 11 Glycyl +P10869 333 Phosphothreonine +Q08548 513 Phosphoserine +Q08548 605 Phosphoserine +Q08548 610 Phosphoserine +Q08548 615 Phosphoserine +P36117 220 Phosphoserine +P38113 226 Phosphothreonine +P38113 282 Phosphoserine +P38113 319 Phosphoserine +P38113 229 Glycyl +P38113 237 Glycyl +P38113 290 Glycyl +Q12013 534 N-linked +P52892 327 N6-(pyridoxal +P14540 11 Phosphothreonine +P14540 56 Phosphoserine +P14540 63 Phosphoserine +P14540 76 Phosphoserine +P14540 83 Phosphoserine +P14540 96 Phosphoserine +P14540 147 Phosphoserine +P14540 150 Phosphothreonine +P14540 179 Phosphothreonine +P14540 268 Phosphoserine +P14540 290 Phosphothreonine +P14540 310 Phosphotyrosine +P14540 313 Phosphoserine +P14540 27 Glycyl +P14540 73 Glycyl +P14540 85 Glycyl +P14540 308 Glycyl +P50076 31 N-linked +P50076 278 N-linked +P50076 372 N-linked +P32375 157 N6-carboxylysine +P54783 56 Pros-8alpha-FAD +P38971 39 Phosphothreonine +Q08981 48 Phosphoserine +Q08981 161 Phosphothreonine +Q08981 202 Phosphoserine +P32463 82 O-(pantetheine +P25377 132 Phosphoserine +P25377 316 Phosphoserine +P32781 22 O-linked +P32781 30 O-linked +P32781 32 O-linked +P32781 39 O-linked +P32781 63 O-linked +P32781 66 O-linked +P32781 75 O-linked +P38628 67 Phosphoserine +P43567 201 N6-(pyridoxal +Q12476 31 Phosphoserine +Q12476 49 Phosphoserine +P19414 391 Phosphoserine +P19414 409 Phosphothreonine +P19414 556 Phosphoserine +Q03233 79 Phosphoserine +Q12433 282 Phosphoserine +Q12433 505 Phosphoserine +P38013 2 N-acetylserine +P38013 28 Phosphoserine +P38013 59 Phosphoserine +P38013 116 Phosphoserine +P38013 32 Glycyl +P38013 48 Glycyl +P38013 113 Glycyl +Q12156 2 N-acetylserine +Q12156 137 Phosphoserine +P40507 37 Phosphoserine +P39010 51 Phosphoserine +P39010 57 Phosphoserine +P38840 90 Phosphoserine +P38840 92 Phosphoserine +P80428 349 Phosphoserine +P40467 166 Phosphoserine%3B +P40467 186 Phosphoserine +P40467 963 Phosphoserine +P34233 56 Phosphoserine +P34233 465 Phosphoserine +P49435 68 Phosphoserine +P18544 276 N6-(pyridoxal +P53974 478 Phosphoserine +P53974 522 Phosphoserine +P53974 535 Phosphoserine +P38116 2 N-myristoyl +P40994 2 N-myristoyl +P53090 100 Phosphoserine +P32449 2 N-acetylserine +P53946 7 Phosphoserine +P53946 24 Phosphothreonine +P53946 383 Phosphoserine +P53946 12 Glycyl +Q12386 65 Phosphoserine +Q12386 70 Phosphoserine +P53731 155 Phosphothreonine +P53731 324 Phosphoserine +P38986 350 Phosphoserine +P40024 43 Phosphoserine +P40024 65 Phosphoserine +P40024 196 Phosphoserine +P40024 446 Phosphothreonine +P11076 2 N-myristoyl +P11076 127 Glycyl +P00812 1 N-acetylmethionine +P00812 16 Phosphoserine +P00812 77 Phosphothreonine +P00812 270 Phosphothreonine +P15274 19 Phosphoserine +P15274 58 Phosphoserine +P15274 61 Phosphoserine +P15274 138 Phosphoserine +Q08951 2 N-acetylthreonine +Q08951 700 Phosphoserine +Q08951 727 Phosphoserine +Q08951 767 Phosphothreonine +Q08951 770 Phosphoserine +Q08951 773 Phosphoserine +Q08951 798 Phosphoserine +Q08951 888 Phosphoserine +Q08951 918 Phosphoserine +P36973 2 N-acetylserine +P25628 21 Phosphoserine +P25628 45 Phosphoserine +P36090 511 S-palmitoyl +P36090 516 S-palmitoyl +P46682 693 Phosphoserine +P46682 698 Phosphoserine +P46682 724 Phosphoserine +P46682 726 Phosphoserine +P04076 27 Phosphoserine +P38832 137 GPI-anchor +P37302 85 N-linked +P37302 96 N-linked +P37302 115 N-linked +P37302 150 N-linked +P37302 162 N-linked +P37302 371 N-linked +P37302 427 N-linked +P37302 480 N-linked +P22936 356 Phosphoserine +Q06408 588 Glycyl +P38080 2 N-acetylserine +P38080 10 Phosphoserine +P38080 407 Phosphoserine +P38080 471 Phosphothreonine +P38080 504 Phosphoserine +P38080 541 Phosphoserine +P38080 574 Phosphoserine +P38080 801 Phosphoserine +P38080 846 Phosphoserine +P38080 953 Phosphoserine +P38080 960 Phosphoserine +P38080 1048 Phosphoserine +P38080 1072 Phosphoserine +P38080 1008 Glycyl +P38080 1046 Glycyl +P54115 3 Glycyl +P54115 142 Glycyl +P54115 196 Glycyl +P16661 88 N-linked +P16661 199 N-linked +P16661 425 N-linked +P19880 9 Phosphoserine +P19880 14 Phosphoserine +P19880 17 Phosphoserine +P19880 165 Phosphothreonine +P19880 204 Phosphoserine +P19880 372 Phosphoserine +P19880 528 Phosphoserine +P27351 649 Phosphoserine +P27351 652 Phosphothreonine +P27351 683 Phosphoserine +Q99186 179 Phosphoserine +Q99186 180 Phosphoserine +Q99186 181 Phosphoserine +P38115 151 Phosphothreonine +P53309 449 Phosphothreonine +P53309 282 Glycyl +P13586 2 N-acetylserine +P13586 227 Phosphoserine +Q12675 70 Phosphothreonine +Q12675 85 Phosphoserine +Q12675 389 Phosphoserine +Q12675 392 Phosphoserine +Q12675 396 Phosphoserine +Q12675 403 Phosphoserine +Q12675 406 Phosphotyrosine +Q12675 782 Phosphothreonine +Q12675 1542 Phosphoserine +Q12675 1592 Phosphoserine +Q12675 938 Glycyl +P40527 102 Phosphoserine +P40527 551 Phosphoserine +P38316 186 Glycyl +Q06628 344 Phosphoserine%3B +Q06628 348 Phosphoserine%3B +Q06628 355 Phosphoserine +Q06628 437 Phosphoserine%3B +Q06628 438 Phosphoserine%3B +Q06628 461 Phosphoserine +Q06628 496 Phosphoserine%3B +Q06628 535 Phosphoserine%3B +Q06628 541 Phosphoserine%3B +Q06628 554 Phosphoserine +Q06628 581 Phosphoserine%3B +Q06628 646 Phosphoserine%3B +Q06628 649 Phosphoserine%3B +P21306 52 Phosphothreonine +P00830 112 Phosphothreonine +P00830 237 Phosphothreonine +P00830 373 Phosphoserine +P05626 144 Phosphoserine +Q07528 2 N-acetylserine +Q07528 361 Phosphoserine +Q07528 363 Phosphoserine +P48016 28 N-linked +P48016 32 N-linked +P48016 98 N-linked +P48016 207 N-linked +P48016 238 N-linked +P48016 247 N-linked +P48016 255 N-linked +P48016 259 N-linked +P48016 325 N-linked +P48016 370 N-linked +P48016 376 N-linked +P48016 488 N-linked +P48016 539 N-linked +P48016 568 N-linked +P48016 628 N-linked +P48016 638 N-linked +P48016 696 N-linked +P48016 705 N-linked +P48016 879 N-linked +P48016 897 N-linked +P48016 910 N-linked +P48016 972 N-linked +P48016 990 N-linked +P48016 1031 N-linked +P48016 1049 N-linked +P48016 1064 N-linked +P48016 1147 N-linked +P48016 1157 N-linked +Q12233 1 N-acetylmethionine +Q12233 3 Phosphoserine +Q12233 62 Phosphoserine +Q12500 519 Phosphoserine +Q12500 524 Phosphoserine +Q05933 29 Glycyl +P0CX79 29 N-linked +P0CX79 93 N-linked +P0CX79 239 N-linked +P25641 173 N-linked +P25641 202 N-linked +P25641 208 N-linked +P35193 136 Phosphoserine +P35193 141 Phosphoserine +P35193 243 Phosphoserine +P35193 213 Glycyl +P35193 216 Glycyl +P53104 34 Phosphoserine +P53104 129 Phosphothreonine +P53104 226 Phosphothreonine%3B +P53104 304 Phosphoserine +P53104 365 Phosphoserine +P53104 390 Phosphoserine +P53104 508 Phosphoserine%3B +P53104 515 Phosphoserine%3B +P53104 533 Phosphoserine +P53104 551 Phosphoserine +P53104 552 Phosphoserine +P53104 590 Phosphothreonine +P53104 621 Phosphoserine +P53104 635 Phosphoserine +P53104 638 Phosphoserine +P53104 647 Phosphoserine +P53104 677 Phosphoserine +P53104 680 Phosphoserine +P53104 683 Phosphoserine +P53104 769 Phosphoserine +P53104 783 Phosphoserine +P53867 488 Phosphoserine +Q12380 149 Glycyl +Q12092 106 Phosphoserine +Q12092 187 Phosphoserine +Q12092 188 Phosphoserine +P40458 114 Phosphoserine +P40458 119 Phosphoserine +P38182 116 Phosphatidylethanolamine +P32453 109 Phosphoserine +P40851 262 Phosphoserine +Q06541 296 N-linked +P46993 121 Phosphoserine +P46993 123 Phosphoserine +P46993 125 Phosphoserine +P46993 153 Phosphothreonine +P54074 2 N-linked +P54074 19 N-linked +P54074 29 N-linked +P48361 344 Phosphoserine +P48361 793 Phosphoserine +P48361 808 Phosphothreonine +P48361 944 Phosphoserine +P48361 969 Phosphoserine +P48361 1017 Phosphothreonine +P48361 1070 Phosphoserine +P48361 1095 Phosphoserine +P48361 1098 Phosphoserine +P32660 53 Phosphoserine +P32660 70 Phosphothreonine +P32660 81 Phosphoserine +P32660 85 Phosphothreonine +P32660 92 Phosphoserine +P32660 94 Phosphothreonine +P32660 104 Phosphoserine +P32660 109 Phosphothreonine +P32660 351 Phosphoserine +P32660 354 Phosphoserine +P32660 358 Phosphoserine +P32660 365 Phosphoserine +P32660 368 Phosphotyrosine +P32660 1506 Phosphoserine +P32660 1551 Phosphothreonine +P32660 1552 Phosphoserine +P32660 1563 Phosphoserine +P32660 895 Glycyl +Q12674 627 Phosphoserine +P30902 2 N-acetylserine +P40518 142 Phosphothreonine +Q06598 201 N-linked +Q06598 365 N-linked +P35734 26 Phosphoserine +P35734 118 Phosphoserine +P35734 134 Phosphoserine +P35734 140 Phosphothreonine +P35734 155 Phosphoserine +P35734 156 Phosphoserine +P35734 200 Phosphoserine%3B +P35734 216 Phosphoserine +P35734 250 Phosphoserine%3B +P53855 236 Phosphoserine +Q05789 2 N-acetylserine +P36107 392 Phosphoserine +P36107 395 Phosphoserine +P36107 132 N-linked +P36062 59 Phosphoserine +P36062 119 Phosphoserine +P36062 121 Phosphoserine +P36062 165 Phosphoserine +P53629 175 Phosphoserine +P53629 176 Phosphoserine +P19146 2 N-myristoyl +P19146 127 Glycyl +P49089 265 Phosphoserine +P49089 509 Phosphoserine +P43601 354 Phosphoserine +Q02887 213 Phosphothreonine +Q02887 237 Phosphoserine +P25568 278 Phosphoserine +Q06485 127 Phosphoserine +Q06485 129 Phosphoserine +P40344 19 N6-acetyllysine%3B +P40344 48 N6-acetyllysine%3B +P32907 2 N-acetylserine +P32907 2 Phosphoserine +P32907 7 Phosphoserine +P32907 21 Phosphoserine +P32907 22 Phosphoserine +P32907 28 Phosphoserine +P32907 40 Phosphoserine +P32454 381 N-linked +P32454 713 N-linked +P32381 1 N-acetylmethionine +P53244 364 Glycyl +P53983 24 N-linked +P53983 34 N-linked +P53983 46 N-linked +P53983 66 N-linked +P0CZ17 29 N-linked +P0CZ17 93 N-linked +P0CZ17 239 N-linked +P39524 102 Phosphoserine +P39986 324 Phosphoserine +P39986 936 Phosphoserine +Q01217 359 Phosphoserine +Q02804 1 N-acetylmethionine +Q02804 50 Glycyl +P28777 2 N-acetylserine +P18634 118 Glycyl +P50275 17 Phosphoserine +P0CX77 29 N-linked +P0CX77 93 N-linked +P0CX77 239 N-linked +P0CX78 29 N-linked +P0CX78 93 N-linked +P0CX78 239 N-linked +Q06321 76 Phosphoserine +Q06321 693 Phosphoserine +Q12142 143 Phosphoserine +Q12142 144 Phosphoserine +Q12142 787 Phosphoserine +Q12359 4 Phosphoserine +P61829 1 N-formylmethionine +P35817 270 Phosphoserine +P35817 429 Phosphoserine +P35817 615 Phosphoserine +P35817 659 Phosphoserine +P39714 63 Phosphoserine +P07251 57 Phosphoserine +P07251 178 Phosphoserine +P13090 394 N-linked +P13090 471 N-linked +Q01389 407 Phosphothreonine +Q01389 411 Phosphoserine +Q01389 491 Phosphoserine +Q01389 747 Phosphoserine +Q01389 816 Phosphoserine +Q01389 1058 Phosphoserine +Q01389 1061 Phosphoserine +Q01389 1134 Phosphoserine%3B +P39713 63 Phosphoserine +Q08347 1 N-acetylmethionine +P81449 2 N-acetylserine +P41815 14 Phosphoserine +P41815 79 Phosphoserine +P47068 103 Phosphoserine +P47068 158 Phosphoserine +P47068 166 Phosphoserine +P47068 565 Phosphoserine +P47068 621 Phosphoserine +P47068 631 Phosphoserine +P47068 634 Phosphoserine +P47068 636 Phosphothreonine +P47068 638 Phosphoserine +P47068 647 Phosphoserine +P47068 850 Phosphothreonine +P47068 889 Phosphoserine +P47068 894 Phosphothreonine +P47068 895 Phosphothreonine +P47068 1012 Glycyl +Q08236 1 N-acetylmethionine +Q08236 140 Phosphoserine +Q08236 144 Phosphoserine +Q08236 400 Phosphoserine +Q08236 509 Phosphoserine +Q08236 510 Phosphothreonine +Q08236 552 Phosphoserine +P47082 8 Phosphoserine +P47082 15 Phosphoserine +P47082 35 Phosphoserine +P47082 181 Phosphothreonine +P47082 187 Phosphoserine +P38084 3 Phosphoserine +P38084 15 Phosphothreonine +P38084 16 Phosphoserine +P38084 19 Phosphoserine +P38084 21 Phosphoserine +P38084 24 Phosphoserine +P38084 76 Phosphoserine +P38084 84 Phosphoserine +P39960 129 Phosphoserine +P39960 283 Phosphoserine +P39960 1012 Phosphoserine +P39960 1016 Phosphoserine +P39960 1038 Phosphothreonine +P39960 1046 Phosphoserine +P39960 1054 Phosphoserine +P39960 1128 Phosphoserine +P39960 27 Glycyl +P36149 80 S-palmitoyl +P47134 477 Phosphoserine +P47134 508 Phosphoserine +P47134 552 Phosphoserine +P47134 587 Phosphoserine +P47134 751 Phosphoserine +P47134 765 Phosphoserine +P47041 58 Phosphotyrosine +P47041 59 Phosphoserine +P47041 139 Phosphoserine +P47041 144 Phosphoserine +Q08235 285 Phosphoserine +Q05611 177 Phosphoserine +Q08280 37 Phosphoserine +Q08280 41 Phosphoserine +Q08280 49 N-linked +P47176 202 N6-(pyridoxal +P15703 202 N-linked +P15703 284 N-linked +P50277 314 N6-(pyridoxal +Q08965 438 Phosphoserine +Q08965 478 Phosphoserine +Q08965 492 Phosphoserine +Q08965 504 Phosphothreonine +Q08965 516 Phosphothreonine +Q08965 518 Phosphoserine +Q08965 523 Phosphoserine +Q08965 574 Phosphoserine +Q08965 578 Phosphoserine +P47039 271 N6-(pyridoxal +P40450 621 Phosphoserine +P40450 751 Phosphoserine +Q07660 830 N-linked +P53755 111 Phosphoserine +P53755 350 Phosphoserine +Q06604 46 Phosphoserine +Q06604 79 Phosphoserine +Q06604 88 Phosphoserine +Q06604 185 Phosphoserine +Q06604 220 Phosphoserine +Q06604 309 Phosphoserine +Q06604 320 Phosphoserine +P50944 88 Phosphoserine +P50944 130 Phosphoserine +P50944 165 Phosphoserine +P41696 61 Phosphoserine +P41696 286 Phosphoserine +P41696 325 Phosphoserine +Q12365 29 Phosphoserine +Q12365 73 Phosphoserine +Q12365 115 Phosphoserine +P38928 642 Phosphoserine +P38928 673 Phosphoserine +P38928 676 Phosphoserine +P38928 41 N-linked +P38928 50 N-linked +P38928 96 N-linked +P38928 117 N-linked +P38928 163 N-linked +P38928 260 N-linked +P38928 266 N-linked +P38928 304 N-linked +P38928 324 N-linked +P38928 359 N-linked +P38928 382 N-linked +P38928 389 N-linked +P38928 403 N-linked +P38928 447 N-linked +P38928 451 N-linked +P38928 495 N-linked +P33306 334 Phosphoserine +P33306 757 Phosphoserine +P33306 761 Phosphoserine +Q07442 264 Phosphoserine +P53858 43 Phosphoserine +P53858 133 Phosphoserine +P53858 281 Phosphoserine +P53858 364 Phosphoserine +P53858 394 Phosphoserine +P53858 410 Phosphothreonine +P53858 476 Phosphoserine +P53858 500 Phosphoserine +P53858 503 Phosphoserine +P53858 618 Phosphoserine +P53858 703 Phosphothreonine +P53858 746 Phosphoserine +P53858 825 Phosphoserine +Q06338 205 Phosphothreonine +Q06338 209 Phosphothreonine +P47113 317 Phosphoserine +P40013 2 N-acetylserine +P40013 157 Phosphoserine +P29366 1 N-acetylmethionine +P29366 47 Phosphoserine +P29366 255 Phosphoserine +P29366 258 Phosphoserine +P29366 458 Phosphoserine +P29366 461 Phosphoserine +P38813 24 N-linked +P38813 144 N-linked +P43583 11 Phosphoserine +P43583 29 Phosphoserine +P43583 56 Phosphoserine +P43583 62 Phosphoserine +P43583 64 Phosphothreonine +P43583 66 Phosphothreonine +P43583 1041 Phosphoserine +Q04347 257 Phosphothreonine +Q04347 367 Phosphoserine +Q04347 371 Phosphothreonine +Q04347 375 Phosphoserine +P33314 2 N-acetylserine +P33314 854 Phosphoserine +P47136 10 Phosphoserine +P47136 78 Phosphoserine +P47136 81 Phosphoserine +P47136 91 Phosphoserine +P47136 96 Phosphoserine +P47136 167 Phosphoserine +P47136 365 Phosphothreonine +P47136 367 Phosphoserine +P47136 511 Phosphoserine +P47136 616 Phosphoserine +P47136 805 Phosphoserine +P47136 811 Phosphoserine +P41697 12 Phosphothreonine +P41697 233 Phosphoserine +P41697 327 Phosphoserine +P41697 342 Phosphoserine +P38822 327 Phosphoserine +P38822 463 Phosphoserine +P38822 472 Phosphoserine +P38822 476 Phosphoserine +Q04749 315 Phosphoserine +Q04749 350 Phosphoserine +P40074 344 Phosphoserine +P12630 84 N-linked +P12630 90 N-linked +P12630 268 N-linked +P12630 308 N-linked +P12630 366 N-linked +P12630 398 N-linked +P12630 468 N-linked +P12630 503 N-linked +P12630 551 N-linked +Q12186 93 Phosphoserine +Q12186 95 Phosphoserine +Q12186 100 Phosphotyrosine +Q12186 382 Phosphoserine +P38891 219 N6-(pyridoxal +P38891 315 Phosphothreonine +P38772 330 Phosphoserine +P32873 254 Phosphoserine +Q06631 41 Phosphoserine +Q06631 44 Phosphoserine +Q06631 366 Phosphoserine +Q06631 372 Phosphoserine +Q06631 379 Phosphoserine +P11709 95 Phosphoserine +P11709 110 Phosphoserine +Q08492 16 Phosphoserine +Q08492 45 Phosphoserine +Q08492 65 Phosphoserine +Q08492 144 Phosphoserine +Q05949 24 Phosphoserine +P0C155 54 N-linked +P0C155 76 N-linked +P0C155 335 N-linked +P0C155 428 N-linked +P0C155 17 Glycyl +P27614 88 N-linked +P27614 176 N-linked +P27614 228 N-linked +P27614 381 N-linked +P27614 525 N-linked +P27614 8 Glycyl +P00729 124 N-linked +P00729 198 N-linked +P00729 279 N-linked +P00729 479 N-linked +P34730 2 N-acetylserine +P38041 104 Phosphoserine +P38041 106 Phosphoserine +P38041 128 Phosphoserine +P38041 151 Phosphothreonine +P38041 158 Phosphothreonine +P38041 209 Phosphoserine +P38041 393 Phosphoserine +P38041 412 Phosphoserine +P38041 525 Phosphoserine +P38041 528 Phosphoserine +P38041 589 Phosphoserine +P38041 590 Phosphoserine +P38041 593 Phosphoserine +P38041 644 Phosphoserine +P38041 655 Phosphoserine +P38041 735 Phosphoserine +P38041 919 Phosphothreonine +P53836 491 Phosphoserine +P53836 510 Phosphoserine +P53836 518 Phosphoserine +P53836 538 Phosphoserine +P53836 556 Phosphoserine +P53836 871 Phosphoserine +P53836 885 Phosphoserine +P39101 132 Glycyl +P17555 454 Phosphoserine +P06787 82 Phosphoserine +P06787 102 Phosphoserine +P27825 25 N-linked +P27825 104 N-linked +P27825 296 N-linked +P27825 416 N-linked +P27825 425 N-linked +P04817 54 Phosphoserine +P04817 66 Phosphoserine +P28495 2 N-acetylserine +P28495 17 Phosphoserine +P34237 364 Phosphoserine +P34237 450 Phosphoserine +P34237 453 Phosphoserine +P34237 555 Phosphoserine +P15202 2 N-acetylserine +Q06071 33 Phosphoserine +P29311 2 N-acetylserine +P29311 89 Phosphoserine +P29311 76 Glycyl +P48582 740 Phosphoserine +P32639 403 Phosphoserine +P25558 766 Phosphoserine +P25558 1045 Phosphothreonine +P25558 1063 Phosphoserine +P25558 1075 Phosphoserine +P25558 1134 Phosphoserine +P25558 1149 Phosphoserine +P25558 1157 Phosphothreonine +P25558 1160 Phosphoserine +P25558 1228 Phosphoserine +P25558 1254 Phosphoserine +P25558 1257 Phosphoserine +P25558 1390 Phosphoserine +P25558 1412 Phosphoserine +P25558 1429 Phosphothreonine +P25558 1440 Phosphothreonine +P25558 1443 Phosphoserine +P25558 1501 Phosphoserine +P25558 1549 Phosphoserine +P25558 1589 Phosphoserine +P25558 1614 Phosphoserine +P25558 792 Glycyl +P25558 963 Glycyl +Q12191 2 N-acetylserine +Q12191 87 Phosphoserine +Q12191 170 Phosphoserine +Q12191 292 Phosphothreonine +Q03758 22 Phosphothreonine +Q03758 557 Phosphoserine +P12962 78 Phosphoserine +P12962 91 Phosphoserine +P12962 99 Phosphothreonine +P12962 101 Phosphothreonine +P12962 102 Phosphothreonine +P12962 154 Phosphoserine +P53890 70 Phosphoserine +P53890 179 Phosphoserine +P53890 194 Phosphoserine +P53890 257 Phosphothreonine +P53890 270 Phosphoserine +P53890 273 Phosphoserine +P53890 274 Phosphothreonine +P53890 332 Phosphoserine +P53890 340 Phosphoserine +P53890 344 Phosphotyrosine +P53890 346 Phosphoserine +P53890 350 Phosphoserine +P39969 18 Phosphoserine +P39969 24 Phosphoserine +P39969 28 Phosphoserine +P39969 450 Phosphoserine +P39969 519 Phosphoserine +P39969 523 Phosphoserine +P39969 546 Phosphoserine +P39969 652 Phosphoserine +P43132 227 Phosphoserine +P38356 312 Glycyl +P43573 580 Phosphoserine +P53323 187 Phosphoserine%3B +P53323 189 Phosphoserine%3B +P41698 92 N-linked +P41698 110 N-linked +P41698 211 N-linked +P41698 240 N-linked +P41698 271 N-linked +P41698 333 N-linked +P41698 396 N-linked +P41698 423 N-linked +P53226 112 Phosphoserine +P53226 189 Phosphoserine +P53226 83 N-linked +P53226 139 N-linked +P53226 142 N-linked +P53226 221 N-linked +P53226 259 N-linked +P53226 263 N-linked +P53226 289 N-linked +P53226 299 N-linked +P53226 340 N-linked +P48524 58 Phosphoserine +P48524 70 Phosphoserine +P07245 176 Phosphoserine +P07245 318 Phosphothreonine +P07245 322 Phosphoserine +P36076 42 Phosphoserine +P36076 116 Phosphoserine +P36076 121 Phosphoserine +P36076 124 Phosphoserine +P36076 264 Phosphoserine +P13517 2 N-acetylserine +P13517 85 Phosphoserine +P13517 92 Phosphoserine +Q02948 142 Phosphothreonine +P38934 260 Phosphoserine +P38934 336 Phosphothreonine +P38934 369 Phosphoserine +Q06150 383 Phosphoserine +P53741 187 Phosphoserine +P53741 282 Phosphoserine +P53741 336 Phosphothreonine +P53741 340 Phosphoserine +P53741 398 Phosphoserine +P43571 19 N-linked +P43571 295 N-linked +P43571 302 N-linked +P43571 447 N-linked +P43571 456 N-linked +P43571 485 N-linked +P43571 565 N-linked +P43571 651 N-linked +P43571 668 N-linked +P43571 694 N-linked +P43571 918 N-linked +P41832 311 Phosphoserine +P41832 325 Phosphoserine +P41832 1085 Phosphoserine +P41832 1170 Phosphoserine +P41832 1338 Phosphoserine +P41832 1344 Phosphoserine +P41832 1918 Phosphothreonine +P25385 1 N-acetylmethionine +P14772 645 Phosphoserine +P14772 885 Phosphoserine +P14772 889 Phosphothreonine +P14772 893 Phosphoserine +P14772 895 Phosphoserine +P14772 916 Phosphothreonine +P14772 927 Phosphoserine +P14772 931 Phosphoserine +P14772 934 Phosphothreonine +P14772 1011 N-linked +P23293 240 Phosphothreonine%3B +P23293 400 Phosphoserine +P23293 405 Phosphothreonine +P23293 417 Phosphoserine +P23293 634 Phosphoserine +P36106 177 Phosphoserine +P32797 306 Phosphoserine +P32797 308 Phosphothreonine +P32797 333 Phosphoserine +P25656 199 N-linked +P25656 216 N-linked +P25656 237 N-linked +P25656 288 N-linked +P25656 329 N-linked +P09119 368 Phosphothreonine +P53197 213 Phosphoserine +Q12453 754 Phosphoserine +P07267 144 N-linked +P07267 345 N-linked +P32582 53 N6-(pyridoxal +P32582 134 Phosphoserine +P32582 350 Phosphoserine +P32582 424 Phosphoserine +Q06703 142 N-linked +Q06703 181 N-linked +Q06703 199 N-linked +Q06703 246 N-linked +Q06703 263 N-linked +P27636 561 Phosphoserine +P27636 567 Phosphoserine +P27636 870 Phosphothreonine +P04821 151 Phosphoserine +P04821 154 Phosphoserine +P04821 423 Phosphoserine +P04821 580 Phosphoserine +P04821 596 Phosphoserine +P04821 632 Phosphoserine +P04821 635 Phosphothreonine +P04821 649 Phosphoserine +P25694 472 Phosphoserine +P25694 519 Phosphoserine +P25694 735 Phosphothreonine +P25694 770 Phosphoserine +P25694 305 Glycyl +P25694 322 Glycyl +P25694 346 Glycyl +P25694 522 Glycyl +P25694 539 Glycyl +P25694 594 Glycyl +P25694 673 Glycyl +P40969 575 Phosphoserine +P53894 109 Phosphothreonine +P24869 2 N-acetylserine +P80235 517 Phosphoserine +P25296 2 N-myristoyl +P07253 2 N-acetylserine +P07253 97 Phosphothreonine +P31384 33 Phosphothreonine +P31384 278 Phosphoserine +P31384 285 Phosphothreonine +Q12127 112 GPI-anchor +Q12127 21 N-linked +Q12127 23 O-linked +Q12127 24 O-linked +Q12127 26 O-linked +Q12127 28 O-linked +Q12127 31 O-linked +Q12127 32 O-linked +Q12127 33 O-linked +Q12127 36 O-linked +Q12127 38 O-linked +Q12127 39 O-linked +Q12127 46 O-linked +Q12127 48 O-linked +Q12127 81 N-linked +Q12127 97 N-linked +Q12127 80 Glycyl +P32457 2 N-acetylserine +P32457 2 Phosphoserine +P32457 9 Phosphoserine +P32457 47 Phosphothreonine +P32457 60 Phosphoserine +P32457 77 Phosphoserine +P32457 175 Phosphoserine +P32457 468 Phosphothreonine +P32457 509 Phosphoserine +P32457 4 Glycyl +P32457 11 Glycyl +P32457 30 Glycyl +P32457 63 Glycyl +P32457 287 Glycyl +Q06697 114 Phosphoserine +Q06697 150 Phosphoserine +P17106 1 N-acetylmethionine +P17106 45 Phosphoserine%3B +P17106 48 Phosphoserine +P17106 84 Phosphoserine +P17106 138 Phosphothreonine +Q06702 26 N-linked +Q06702 50 N-linked +Q06702 68 N-linked +Q06702 189 N-linked +P25342 1 N-acetylmethionine +P25342 216 Phosphothreonine +P32468 2 N-acetylserine +P16522 59 Phosphoserine%3B +P06704 130 Phosphothreonine +P25356 1667 Glycyl +P27637 2 N-acetylserine +P27637 159 Phosphotyrosine +P27637 160 Phosphoserine +P27637 162 Phosphoserine +P27637 177 Phosphothreonine +P27637 212 Phosphoserine +P27637 222 Phosphoserine +P27637 376 Phosphoserine +P27637 378 Phosphoserine +P27637 401 Phosphoserine +P27637 507 Phosphoserine +P27637 655 Phosphoserine +P27637 658 Phosphoserine +P27637 670 Phosphoserine +P32504 566 Phosphoserine +P32504 706 Phosphotyrosine +P33322 47 Phosphoserine +P33322 378 Phosphothreonine +P33322 9 Glycyl +P33322 267 Glycyl +P50077 284 Phosphoserine +P00431 220 Phosphotyrosine +Q7LHD1 115 GPI-anchor +Q7LHD1 21 N-linked +Q7LHD1 82 N-linked +P19073 188 Cysteine +P19073 188 S-geranylgeranyl +P32458 2 N-acetylserine +P32458 2 Phosphoserine +P32458 305 Phosphoserine +P32458 327 Phosphothreonine +P32458 412 Glycyl +P14724 12 Phosphoserine +P06101 14 Phosphoserine +P06101 17 Phosphoserine +P06101 367 Phosphoserine +P06101 466 Phosphoserine +P06101 484 Phosphoserine +Q12018 760 Glycyl +P38910 2 N-acetylserine +P38910 31 Phosphoserine +P47818 29 Phosphoserine +P47818 53 Phosphoserine +P47818 68 Phosphoserine +P47818 71 Phosphoserine +P47818 83 Phosphoserine +O13547 217 GPI-anchor +O13547 87 N-linked +O13547 161 Glycyl +Q00684 467 Phosphoserine +O13297 2 N-acetylserine +O13297 15 Phosphoserine +O13297 124 Phosphoserine +P29029 553 N-linked +Q12114 305 Phosphothreonine +Q12114 338 Phosphoserine +Q12114 362 Phosphoserine +Q12114 365 Phosphoserine +Q12114 383 Phosphoserine +Q12114 384 Phosphoserine +Q12114 573 Phosphoserine +Q12114 579 Phosphoserine +Q12114 590 Phosphoserine +Q12114 584 Glycyl +P43634 164 Phosphoserine +P43634 166 Phosphoserine +P22516 86 Phosphoserine +P22516 172 Phosphoserine +Q08032 453 Phosphothreonine +P07834 104 Phosphoserine +P32562 23 Phosphothreonine +P32562 419 Phosphoserine +P40558 291 Phosphoserine +P53280 1042 Phosphoserine +P08004 34 Phosphoserine +P08004 35 Phosphoserine +P08004 270 Phosphoserine +P08004 299 Phosphoserine +P08004 318 Phosphoserine +P08004 328 Phosphothreonine +P08004 358 Phosphoserine +P14180 40 Phosphoserine +P14180 82 Phosphoserine +P14180 86 Phosphoserine +P14180 100 Phosphoserine +P14180 133 Phosphoserine +P14180 217 Phosphoserine +P14180 22 N-linked +P14180 197 N-linked +P14180 447 N-linked +P32657 36 Phosphoserine +P32657 72 Phosphoserine +P32657 987 Phosphoserine +P32657 989 Phosphoserine +P32657 1336 Phosphoserine +P32657 1364 Phosphoserine +P32657 1372 Phosphoserine +P32657 1144 Glycyl +Q06350 147 N-linked +Q06350 228 N-linked +Q06350 456 N-linked +Q06350 472 N-linked +P05374 2 N-acetylserine +P29465 537 Phosphoserine +P29465 538 Phosphothreonine +P29465 82 N-linked +P29465 114 N-linked +P29465 152 N-linked +P29465 163 N-linked +P29465 303 N-linked +P29465 332 N-linked +P29465 371 N-linked +P29465 136 Glycyl +P40019 2 N-acetylserine +P40019 68 Phosphoserine +P40019 70 Phosphoserine +Q07897 59 Phosphoserine +P27895 972 Phosphoserine +P48562 29 Phosphoserine +P48562 46 Phosphoserine +P48562 351 Phosphoserine +P48562 367 Phosphoserine +P48562 425 Phosphoserine +P22137 1107 Glycyl +Q06156 464 Phosphoserine +Q06156 475 Phosphoserine +P53079 1 N-acetylmethionine +P53079 305 Phosphoserine +Q12510 64 Phosphoserine +Q12510 69 Phosphothreonine +Q12510 224 Phosphoserine +Q06680 198 Phosphoserine +Q06680 933 Phosphoserine +Q06680 981 Phosphoserine +Q06680 1008 Phosphoserine +P47001 68 O-linked +P47001 78 O-linked +P47001 105 O-linked +P47001 106 O-linked +P47001 107 O-linked +P47001 109 O-linked +P47001 111 O-linked +P47001 112 O-linked +P47001 113 O-linked +P47001 114 N-linked +P47001 116 O-linked +P47001 117 O-linked +P47001 118 O-linked +Q03690 1247 Phosphoserine +P53865 17 Phosphoserine +P53865 20 Phosphoserine +P53865 72 Phosphoserine +P53865 85 Phosphoserine +P53865 89 Phosphoserine +P53865 151 Phosphoserine +P41810 181 Phosphoserine +P41810 540 Phosphoserine +Q01519 82 Phosphoserine +Q03048 4 Phosphoserine +P00401 245 1'-histidyl-3'-tyrosine +P38287 354 Phosphoserine +P43639 2 N-acetylserine +P43639 2 Phosphoserine +P46946 143 Phosphoserine +P46946 267 Phosphoserine%3B +P32074 638 Phosphothreonine +P32074 643 Phosphoserine +P32074 653 Phosphoserine +P32074 647 Glycyl +P32798 225 Phosphoserine +P32798 301 Glycyl +P04037 55 Phosphothreonine +P10614 458 Phosphoserine +P10614 116 Glycyl +P10614 353 Glycyl +P10614 454 Glycyl +P08679 21 Phosphoserine +P08679 218 Glycyl +P08679 239 Glycyl +P08679 354 Glycyl +P08679 385 Glycyl +P17891 49 Phosphothreonine +P17891 52 Phosphoserine +P41811 326 Phosphoserine +P38170 245 Phosphoserine +P38170 548 Phosphoserine +P43621 277 Phosphothreonine +Q06705 2 N-acetylserine +Q06705 2 Phosphoserine +Q03957 14 Phosphoserine%3B +Q03957 338 Phosphothreonine +P40094 507 Phosphoserine +P40094 647 Phosphoserine +Q06440 441 Phosphoserine +Q06440 454 Phosphoserine +Q06440 456 Phosphoserine +Q06440 517 Phosphothreonine +Q06440 529 Phosphothreonine +Q06440 573 Phosphoserine +Q06440 579 Phosphoserine +Q12150 82 N-linked +Q12150 117 N-linked +Q12150 144 N-linked +Q12150 271 N-linked +Q12150 478 N-linked +Q12150 530 N-linked +Q12150 816 N-linked +Q12150 821 N-linked +Q12150 839 N-linked +Q12150 892 N-linked +Q12150 1309 N-linked +Q12150 1368 N-linked +Q12150 1453 N-linked +Q12150 1785 N-linked +Q12150 1921 N-linked +Q12150 2130 N-linked +Q12150 2146 N-linked +Q12150 2280 N-linked +Q12150 2337 N-linked +Q12150 2520 N-linked +Q12150 2578 N-linked +Q12150 2719 N-linked +Q12150 2869 N-linked +Q12748 2 N-acetylserine +Q08923 174 Phosphothreonine +Q08923 175 Phosphoserine +Q08923 177 Phosphothreonine +Q08923 216 Phosphoserine +Q08923 267 Phosphoserine +Q12734 23 Phosphoserine +Q12734 46 Phosphoserine +Q12734 127 Phosphoserine +Q12734 327 Phosphoserine +Q12734 987 Phosphoserine +Q12734 841 Glycyl +P25618 419 N-linked +P25618 490 N-linked +P25618 767 N-linked +P25618 792 N-linked +P25618 825 N-linked +Q04632 410 Phosphoserine +P38845 153 Phosphoserine +P38845 156 Phosphoserine +P38845 182 Phosphothreonine +P38845 271 Phosphoserine +P38845 295 Phosphothreonine +P38845 319 Phosphoserine +P38845 343 Phosphoserine +P38845 366 Phosphothreonine +P38845 394 Phosphoserine +P38845 440 Phosphoserine +P43497 71 GPI-anchor +P53968 170 Phosphothreonine +P53968 175 Phosphoserine +P53968 245 Phosphoserine +P53968 385 Phosphoserine +P14306 1 N-acetylmethionine +P53301 482 GPI-anchor +P53301 117 N-linked +P53301 177 N-linked +P53301 201 N-linked +Q06538 171 N-linked +P35206 35 N-linked +P35206 49 N-linked +P25355 433 Phosphothreonine +P25355 559 Phosphoserine +P53923 489 Phosphoserine +P53830 163 Phosphoserine +P00044 78 N6%2CN6%2CN6-trimethyllysine%3B +P00044 79 N6%2CN6%2CN6-trimethyllysine +P32898 920 Phosphoserine +P32623 445 GPI-anchor +P32623 28 N-linked +P32623 96 N-linked +P32623 190 N-linked +P32623 196 N-linked +P32623 233 N-linked +P32623 237 N-linked +P32623 261 N-linked +P32623 297 N-linked +P32623 310 N-linked +P49573 344 Phosphoserine +P49573 349 Phosphoserine +P49573 356 Phosphothreonine +P49573 369 Phosphoserine +P49573 113 N-linked +P49573 148 N-linked +P49573 345 Glycyl +P89105 1015 Phosphoserine +P89105 1017 Phosphoserine +Q04201 48 Phosphoserine +Q04201 37 Glycyl +Q08412 21 Phosphoserine +Q08412 36 Phosphoserine +Q08412 70 Phosphothreonine +Q08412 91 Phosphoserine +Q08412 167 Phosphothreonine +Q08412 220 Phosphoserine +Q08412 309 Phosphoserine +Q08412 318 Phosphoserine +Q08412 346 Phosphothreonine +Q08412 348 Phosphoserine +Q08412 352 Phosphothreonine +Q08412 364 Phosphothreonine +Q08412 367 Phosphothreonine +Q08412 407 Phosphoserine +Q08412 15 Glycyl +Q08412 59 Glycyl +Q08412 76 Glycyl +Q08412 156 Glycyl +Q08412 354 Glycyl +Q08412 396 Glycyl +P47050 791 Glycyl +P53854 129 Phosphoserine +Q12046 335 Phosphoserine +Q12046 336 Phosphoserine +P53008 42 N-linked +P53008 122 N-linked +P53008 135 N-linked +P53008 787 N-linked +P28319 217 GPI-anchor +Q08226 704 Phosphoserine +P53859 94 Phosphoserine +P21657 833 Phosphoserine +P47179 1137 GPI-anchor +P22204 17 Phosphoserine +P22204 20 Phosphoserine +P22204 74 Phosphoserine +P22204 374 Phosphoserine%3B +P22204 544 Phosphothreonine%3B +P24309 269 Phosphoserine +P36091 428 GPI-anchor +P36091 34 N-linked +P36091 84 N-linked +P36091 109 N-linked +P36091 133 N-linked +P36091 203 N-linked +P36091 225 N-linked +P36091 240 N-linked +P36091 265 N-linked +P36091 281 N-linked +P36091 337 N-linked +P36091 362 N-linked +P36091 420 N-linked +P53899 273 Phosphoserine +P08678 2 N-acetylserine +P08678 376 Phosphothreonine +P08678 389 Phosphothreonine +P08678 433 Phosphoserine +P08678 487 Phosphoserine +P08678 497 Phosphoserine +P08678 562 Phosphoserine +P53206 86 N6-(pyridoxal +P47178 275 GPI-anchor +P18962 63 N-linked +P18962 79 N-linked +P18962 110 N-linked +P18962 139 N-linked +P18962 372 N-linked +P18962 392 N-linked +P18962 421 N-linked +P18962 738 N-linked +Q12123 341 Phosphoserine +P46963 35 Phosphothreonine +P53137 377 Phosphoserine +Q12389 101 Phosphoserine +Q12389 398 Phosphoserine +Q12389 400 Phosphoserine +P24783 88 Phosphoserine +P24783 90 Phosphoserine +P24783 474 Glycyl +P20449 86 Phosphoserine +P20449 93 Phosphoserine +P20449 162 Phosphoserine +P53734 73 Phosphoserine +P53734 77 Phosphoserine +P53734 78 Phosphoserine +P21182 88 Pyruvic +P08432 116 N6-(pyridoxal +P06634 2 N-acetylalanine +P06634 62 Dimethylated +P06634 215 Phosphoserine +P06634 218 Phosphoserine +P06634 263 Phosphoserine +P06634 535 Phosphoserine +P06634 539 Phosphoserine +P06634 543 Phosphoserine +P06634 572 Phosphoserine +P06634 576 Phosphoserine +P06634 598 Phosphoserine +P06634 158 Glycyl +P38307 1 N-acetylmethionine +Q01454 377 Phosphoserine +Q01454 379 Phosphoserine +Q01454 398 Phosphoserine +Q01454 401 Phosphothreonine +Q01454 411 Phosphothreonine +Q01454 463 Phosphoserine +P53769 33 Phosphoserine +P53769 105 Phosphoserine +P35176 139 N-linked +P14832 2 N-acetylserine +P14832 71 Phosphothreonine +P14832 142 Phosphoserine +P14832 145 Phosphoserine +P14832 29 Glycyl +P14832 42 Glycyl +P14832 123 Glycyl +P14832 139 Glycyl +P14832 151 Glycyl +P14832 158 Glycyl +P31373 204 N6-(pyridoxal +P31373 362 Phosphoserine +Q12248 91 Phosphoserine +P25334 166 N-linked +P06106 44 Phosphoserine +P06106 209 N6-(pyridoxal +P06106 160 Glycyl +Q99288 248 Phosphoserine +Q05080 337 Phosphoserine +Q05080 366 Phosphoserine +Q05080 421 Phosphoserine +P20448 692 Phosphoserine +P20448 710 Phosphoserine +P20448 714 Phosphoserine +P20448 743 Phosphoserine +P40087 171 Glycyl +P40087 257 Glycyl +P69851 1 N-acetylmethionine +P32328 17 Phosphoserine +P32328 366 Phosphoserine +P32328 536 Phosphothreonine +P53550 116 Phosphoserine +P53550 439 Phosphoserine +P53550 677 Phosphothreonine +P53550 679 Phosphoserine +P53550 682 Phosphoserine +P53550 751 Phosphoserine +P53550 771 Phosphoserine +P53550 773 Phosphoserine +P53550 778 Phosphoserine +P18899 183 Phosphoserine +P18899 191 Phosphoserine +P18899 314 Phosphoserine +P18899 322 Phosphoserine +P31385 56 Phosphoserine +P31385 120 Phosphoserine +P31385 370 Phosphoserine +P14922 429 Phosphoserine +P14922 475 Phosphothreonine +P14922 710 Phosphoserine +P14922 741 Phosphoserine +P14922 768 Phosphoserine +P14922 815 Phosphoserine +P14922 817 Phosphoserine +P14922 866 Phosphoserine +P14922 943 Phosphoserine +Q07533 209 Phosphoserine +Q07533 292 Phosphoserine +Q07533 313 Phosphoserine +Q07533 354 Phosphoserine +Q07533 391 Phosphothreonine +P36162 1 N-acetylmethionine +P53267 2 N-acetylserine +P53267 20 Phosphoserine%3B +P53267 31 Phosphoserine +P53267 257 Phosphoserine%3B +P53267 265 Phosphoserine%3B +P53267 292 Phosphoserine%3B +P53202 688 Glycyl +Q02554 104 Phosphothreonine +Q02554 112 Phosphothreonine +Q02554 114 Phosphoserine +P54838 2 N-acetylserine +P54838 2 Phosphoserine +P54838 5 Phosphoserine +P54838 365 Phosphoserine +P54838 512 Phosphoserine +Q12382 44 Phosphoserine +Q12382 45 Phosphoserine +Q12382 46 Phosphoserine +Q12382 11 N-linked +Q12382 197 N-linked +Q12382 270 N-linked +P54861 629 Phosphoserine +P40059 245 Phosphoserine +P40059 247 Phosphoserine +P40059 487 Phosphoserine +P40059 489 Phosphothreonine +P40059 491 Phosphoserine +P32469 172 Phosphoserine +P32469 298 Phosphoserine +P32892 208 Phosphoserine +P23501 62 N-linked +P07262 2 N-acetylserine +P07262 325 Glycyl +P07262 371 Glycyl +P07262 433 Glycyl +Q08496 393 Phosphoserine +P04819 58 Phosphoserine +P04819 75 Phosphoserine +P04819 119 Phosphoserine +P04819 123 Phosphoserine +Q03921 244 Phosphoserine +P46957 1 N-acetylmethionine +P46957 20 Phosphoserine +P36152 206 Phosphoserine +Q04792 318 N6-(pyridoxal +P35732 260 Phosphoserine +P35732 273 Phosphoserine +P35732 307 Phosphoserine +P35732 338 Phosphothreonine +P35732 646 Phosphoserine +P32330 716 Phosphoserine +P39708 326 Glycyl +P39708 372 Glycyl +P39708 436 Glycyl +Q04603 183 Phosphoserine%3B +Q04217 181 Phosphoserine +P40318 1 N-acetylmethionine +P47110 223 Phosphothreonine +P47110 230 Phosphoserine +P53255 242 Phosphoserine +P32325 59 Phosphoserine +P32325 84 Phosphoserine +P32325 235 Phosphoserine +P32325 623 Phosphoserine +Q03373 34 Phosphoserine +Q03373 225 Phosphoserine +Q03373 266 Phosphoserine +Q03373 270 Phosphoserine +P40366 17 Phosphoserine +Q06819 2 N-acetylalanine +P39976 17 Glycyl +P31116 290 Glycyl +P36037 332 Phosphoserine +Q12395 12 Phosphoserine +Q06151 2 N-acetylserine +Q06151 60 Phosphoserine +Q06151 66 Phosphothreonine +Q06151 66 Phosphothreonine%3B +Q06151 70 Phosphotyrosine +Q06151 120 Phosphothreonine +P89113 24 N-linked +P89113 27 N-linked +P69771 5 Phosphoserine +P38823 150 Glycyl +P38823 204 Glycyl +P38823 217 Glycyl +P38823 237 Glycyl +P38823 240 Glycyl +P38823 260 Glycyl +P38823 300 Glycyl +P38823 306 Glycyl +P38823 313 Glycyl +P38823 317 Glycyl +Q08949 436 Phosphoserine +Q05031 437 GPI-anchor +Q05031 89 N-linked +Q05031 114 N-linked +Q05031 138 N-linked +Q05031 208 N-linked +Q05031 231 N-linked +Q05031 245 N-linked +Q05031 270 N-linked +Q05031 273 N-linked +Q05031 417 N-linked +Q08650 17 Phosphoserine +P13663 13 Phosphothreonine +P13663 318 Phosphoserine +P13663 323 Phosphoserine +Q03063 45 Phosphoserine +Q03063 126 Phosphoserine +Q03063 142 Phosphoserine +Q03063 272 Phosphoserine +Q03063 275 Phosphoserine +Q03063 330 Phosphoserine +Q03063 379 Phosphothreonine +Q03063 395 Phosphoserine +Q03063 428 Phosphoserine +P53388 22 Phosphoserine +P53388 76 Glycyl +P53924 206 Phosphoserine +P53924 211 Glycyl +P53924 256 Glycyl +P53924 258 Glycyl +P53924 288 Glycyl +P53924 310 Glycyl +P53924 333 Glycyl +P53924 343 Glycyl +P53924 346 Glycyl +P53924 366 Glycyl +P53924 406 Glycyl +P53924 412 Glycyl +P53924 423 Glycyl +P38859 4 Phosphothreonine +P38859 17 Phosphoserine%3B +P38859 237 Phosphoserine%3B +P38859 962 Phosphothreonine +P02994 2 N%2CN%2CN-trimethylglycine%3B +P02994 3 N6%2CN6-dimethyllysine%3B +P02994 3 N6-methyllysine%3B +P02994 18 Phosphoserine +P02994 30 N6-methyllysine%3B +P02994 72 Phosphothreonine +P02994 79 N6%2CN6%2CN6-trimethyllysine%3B +P02994 82 Phosphothreonine +P02994 163 Phosphoserine +P02994 259 Phosphothreonine +P02994 289 Phosphoserine +P02994 316 N6%2CN6-dimethyllysine%3B +P02994 316 N6-methyllysine%3B +P02994 390 N6-methyllysine%3B +P02994 414 Phosphoserine +P02994 430 Phosphothreonine +P02994 458 Lysine +P02994 224 Glycyl +P02994 242 Glycyl +P02994 253 Glycyl +P02994 271 Glycyl +P02994 393 Glycyl +P02994 437 Glycyl +Q03653 227 Phosphoserine +Q03653 231 Phosphothreonine +Q03653 564 Phosphoserine +Q03653 625 Phosphoserine +Q03653 632 Phosphoserine +Q03653 643 Phosphoserine +Q03653 675 Phosphoserine +Q03653 687 Phosphothreonine +Q03653 690 Phosphothreonine +Q03653 735 Phosphoserine +Q03653 771 Phosphoserine +Q03653 774 Phosphoserine +P09032 296 Phosphoserine +P09032 300 Phosphoserine +P09032 306 Phosphothreonine +P38121 126 Phosphoserine +P13382 2 N-acetylserine +P13382 31 Phosphoserine +P13382 82 Phosphoserine +P13382 83 Phosphoserine +P13382 84 Phosphoserine +P13382 169 Phosphoserine +P13382 170 Phosphoserine +P13382 172 Phosphothreonine +P13382 240 Phosphoserine +P13382 274 Phosphoserine +P13382 309 Phosphothreonine +P13382 313 Phosphothreonine +Q05521 285 Phosphoserine +Q08729 395 Phosphoserine +P48510 13 Glycyl +P48510 76 Glycyl +P40568 250 Phosphoserine +P36049 104 Phosphoserine +P36049 177 Phosphoserine +P36049 183 Phosphoserine +Q99252 291 Phosphoserine +Q99252 338 Phosphoserine +P53168 2 N-acetylserine +P36041 30 Phosphoserine +P36041 281 Phosphoserine +P36041 282 Phosphoserine +P36041 327 Phosphoserine +P36041 344 Phosphoserine +P36041 387 Phosphoserine +P42835 1020 GPI-anchor +P42835 65 N-linked +P42835 103 N-linked +P42835 161 N-linked +P42835 175 N-linked +P42835 249 N-linked +P42835 332 N-linked +P42835 401 N-linked +P42835 435 N-linked +P42835 465 N-linked +P42835 485 N-linked +P42835 506 N-linked +P42835 526 N-linked +P42835 544 N-linked +P42835 556 N-linked +P42835 635 N-linked +P42835 636 N-linked +P42835 657 N-linked +P42835 709 N-linked +P42835 756 N-linked +P47120 2 N-acetylserine +P47120 126 Phosphoserine +P47120 187 Phosphothreonine +P47120 281 Phosphoserine +P27344 186 Phosphoserine +P27344 188 Phosphoserine +P27344 189 Phosphoserine +P40487 44 Phosphoserine +P47013 16 Phosphothreonine +P47013 18 Phosphoserine +P38844 308 GPI-anchor +P43616 451 Phosphoserine +P32528 803 Phosphoserine +P32528 1798 N6-biotinyllysine +P53759 2 N-acetylthreonine +P53063 198 Phosphoserine +Q06337 841 Phosphoserine +Q06337 971 Phosphothreonine +P53911 200 Phosphoserine +P53911 225 Phosphoserine +Q03212 519 Phosphoserine +Q03212 538 Phosphoserine +Q03212 110 N-linked +Q03212 203 N-linked +Q03212 210 N-linked +Q03212 256 N-linked +Q03212 295 N-linked +P38167 18 Phosphoserine +P38167 115 Phosphoserine +P38167 140 Phosphoserine +P38167 286 Phosphoserine +P38167 527 Phosphoserine +P38167 550 Phosphoserine +P38167 775 Phosphoserine +P38167 1035 Phosphoserine +P38167 191 Glycyl +P38167 577 Glycyl +P38167 651 Glycyl +P38167 712 Glycyl +P38167 794 Glycyl +P38167 807 Glycyl +P38167 1024 Glycyl +P38737 2 N-acetylserine +P38737 1692 Phosphoserine +P53235 564 Phosphoserine +P53235 567 Phosphoserine +P53235 572 Phosphoserine +P32497 98 Phosphoserine +P32497 99 Phosphoserine +P32497 103 Phosphoserine +Q12050 6 Phosphoserine +P25574 73 N-linked +P25574 106 N-linked +P25574 192 N-linked +P25574 202 N-linked +P25574 420 N-linked +P25574 443 N-linked +P25574 574 N-linked +P25574 578 N-linked +P40077 553 Glycyl +Q12432 201 Phosphoserine +P32471 2 N-acetylalanine +P32471 31 Phosphoserine +P32471 86 Phosphoserine +P32471 13 Glycyl +P29547 2 N-acetylserine +P29547 32 Phosphothreonine +P32324 509 N6%2CN6%2CN6-trimethyllysine%3B +P32324 509 N6%2CN6-dimethyllysine%3B +P32324 509 N6-methyllysine%3B +P32324 579 Phosphoserine +P32324 613 N6%2CN6-dimethyllysine%3B +P32324 613 N6-methyllysine%3B +P32324 699 Diphthamide +P32324 713 Phosphothreonine +P32324 763 Phosphothreonine +P32324 841 Glycyl +P47163 177 Phosphothreonine +P24482 122 Phosphoserine +P24482 141 Phosphoserine%3B +P24482 613 Phosphoserine +P39985 789 Phosphoserine +Q06673 635 Phosphoserine +Q06673 1065 Phosphoserine +P38728 45 N-linked +Q05902 119 N-linked +Q05902 191 N-linked +Q05902 270 N-linked +Q05902 298 N-linked +Q05902 454 N-linked +Q05902 517 N-linked +P47138 2 N-acetylserine +P14020 2 N-acetylserine +P14020 141 Phosphoserine%3B +P15436 30 Phosphoserine +P15436 37 Phosphoserine +P39009 10 Phosphoserine +P39009 139 Phosphoserine +P39009 380 Phosphothreonine +Q04067 2 N-acetylserine +Q04067 131 Phosphoserine +Q03764 23 Phosphoserine +Q02884 222 Phosphoserine +Q04409 2 N-acetylserine +Q04409 2 Phosphoserine +Q04409 470 Phosphoserine +P38333 172 Phosphoserine%3B +P38333 190 Phosphoserine +P38333 404 Phosphoserine +P54781 164 Glycyl +P54781 198 Glycyl +P53080 2 N-acetylserine +P53080 82 Phosphoserine +P39998 257 Phosphoserine +P39998 261 Phosphoserine +P14741 2 N-acetylserine +P14741 291 Phosphothreonine +P32501 478 Phosphoserine +P32501 481 Phosphoserine +P32501 507 Phosphoserine +P32501 525 Phosphoserine +P32501 538 Phosphoserine +P32501 707 Phosphoserine +Q05775 75 Phosphothreonine +Q05775 92 Phosphoserine +P36053 55 Phosphoserine +P36053 117 Phosphoserine +P36053 124 Phosphoserine +P36053 142 Phosphoserine +P25358 334 Phosphothreonine +P25358 336 Phosphoserine +P25358 338 Phosphoserine +P25358 32 N-linked +P39013 276 Phosphoserine +Q05785 165 Phosphothreonine +Q05785 167 Phosphoserine +Q05785 430 Phosphothreonine +Q05785 434 Phosphoserine +Q05785 450 Phosphothreonine +Q05785 468 Phosphothreonine +Q05785 470 Phosphothreonine +Q05785 426 Glycyl +Q12003 13 S-palmitoyl +Q12003 14 S-palmitoyl +Q12003 15 S-palmitoyl +O13529 2 N-linked +O13529 132 N-linked +O13529 137 N-linked +P39715 188 Phosphoserine +P34216 238 Phosphothreonine +P34216 241 Phosphoserine +P34216 244 Phosphoserine +P34216 245 Phosphothreonine +P34216 248 Phosphoserine +P34216 249 Phosphoserine +P34216 251 Phosphothreonine +P34216 265 Phosphoserine +P34216 419 Phosphoserine +P34216 450 Phosphothreonine +P34216 477 Phosphothreonine +P34216 487 Phosphothreonine +P34216 495 Phosphoserine +P34216 848 Phosphoserine +P34216 931 Phosphoserine +P34216 950 Phosphoserine +P34216 964 Phosphoserine +P34216 1008 Phosphoserine +P34216 1012 Phosphoserine +P34216 1020 Phosphoserine +P34216 1046 Phosphothreonine +P34216 1069 Phosphoserine +P34216 1087 Phosphoserine +P34216 1093 Phosphoserine +P34216 1095 Phosphoserine +P34216 1096 Phosphoserine +P34216 1100 Phosphoserine +P34216 1111 Phosphothreonine +P34216 1181 Phosphoserine +P34216 1187 Phosphoserine +P34216 1307 Phosphothreonine +P34216 1343 Phosphoserine +P34216 674 Glycyl +P34216 1329 Glycyl +P36008 2 N-acetylserine +P53978 2 N-acetylserine +P53978 187 N6%2CN6%2CN6-trimethyllysine +P53978 196 N6%2CN6%2CN6-trimethyllysine +P53978 789 N6%2CN6%2CN6-trimethyllysine +P53978 972 Phosphothreonine +P53978 974 Phosphoserine +P53978 1039 Phosphoserine +P53978 1040 Phosphoserine +P12754 2 N-acetylserine +P12754 106 Phosphoserine +P12754 121 Phosphothreonine +P32801 152 Phosphoserine +P32801 516 Phosphoserine +P32801 519 Phosphoserine +P32476 284 Glycyl +P32476 289 Glycyl +P32476 311 Glycyl +P38819 171 N-linked +Q08649 17 Phosphoserine +Q08649 262 N6-acetyllysine%3B +Q06340 90 Phosphoserine +Q06340 125 Phosphoserine +Q06340 126 Phosphoserine +Q06344 86 Phosphoserine +Q06344 220 Phosphothreonine +Q06344 223 Phosphoserine +Q06344 225 Phosphoserine +Q06344 367 Phosphoserine +Q06344 369 Phosphoserine +Q06344 372 Phosphoserine +Q06344 542 Phosphothreonine +P22696 161 Phosphoserine +P32474 159 N-linked +P32474 174 N-linked +P32474 207 N-linked +P32474 293 N-linked +P32474 462 N-linked +Q02908 453 Glycyl +P00925 138 Phosphoserine +P00925 188 Phosphoserine +P00925 313 Phosphothreonine +P00925 324 Phosphothreonine +P00925 60 Glycyl +P00925 243 Glycyl +P00925 358 Glycyl +Q12518 160 Phosphothreonine +Q12518 163 Phosphoserine +Q12518 180 Phosphothreonine +Q12518 328 Phosphoserine +Q12518 364 Phosphothreonine +Q12518 366 Phosphothreonine +Q12518 384 Phosphothreonine +Q12518 386 Phosphothreonine +Q12518 388 Phosphothreonine +Q12518 395 Phosphothreonine%3B +Q12518 415 Phosphothreonine%3B +Q12518 357 Glycyl +P47160 2 N-acetylserine +P47160 196 Phosphoserine +P47160 198 Phosphoserine +P47160 203 Phosphoserine +P47160 212 Phosphoserine +P47160 223 Phosphoserine +Q03769 1 N-acetylmethionine +Q03769 322 Phosphoserine +Q03769 324 Phosphoserine +Q03769 363 Phosphoserine +Q03769 368 Phosphothreonine +Q03769 394 Phosphoserine +Q03769 401 Phosphoserine +Q08651 282 N-linked +P25087 2 N-acetylserine +P25087 99 Phosphoserine +P40456 170 Phosphoserine +P40456 190 Phosphoserine +Q07872 195 Phosphoserine +P40557 85 N-linked +P40557 264 N-linked +P40557 299 N-linked +P40557 370 N-linked +P38604 2 N-acetylthreonine +P38836 41 N-linked +P38836 295 N-linked +Q05958 431 Phosphoserine +Q05958 445 Phosphoserine +Q05958 464 Phosphoserine +P32644 227 Phosphoserine +P32644 392 Phosphoserine +P32644 465 Phosphothreonine +P38248 339 Phosphoserine +P38248 406 GPI-anchor +P38248 21 N-linked +P38248 56 N-linked +P38248 82 N-linked +P38248 196 N-linked +P38248 209 N-linked +P38248 227 N-linked +P38248 234 N-linked +P38248 241 N-linked +P38248 267 N-linked +P38248 279 N-linked +P38248 304 N-linked +P38248 328 N-linked +P38248 389 N-linked +P43605 223 N6-acetyllysine%3B +P38249 508 Phosphoserine +P38249 691 Phosphoserine +P38249 935 Phosphothreonine +P40217 302 Phosphoserine +Q05050 2 N-acetylserine +Q05050 2 Phosphoserine +Q05050 88 Phosphoserine +Q05050 130 Phosphoserine +Q05050 182 Phosphoserine +Q05050 401 Phosphoserine +Q05050 584 Phosphoserine +Q05050 710 Phosphoserine +Q05050 720 Phosphothreonine +Q05050 763 Phosphoserine +Q05050 775 Phosphoserine +Q05050 816 Phosphoserine +Q05050 828 Phosphoserine +Q05050 829 Phosphoserine +Q05050 838 Phosphoserine +P40319 2 N-linked +P40319 20 N-linked +P40319 66 N-linked +P53861 235 Phosphoserine +P53861 278 Phosphoserine +P53753 138 N-linked +P53753 186 N-linked +P53753 223 N-linked +P53753 259 N-linked +P53753 280 N-linked +P53753 303 N-linked +P53753 307 N-linked +P53753 393 N-linked +P53753 533 N-linked +P53753 886 N-linked +P06103 61 Phosphoserine +P06103 67 Phosphotyrosine +P06103 669 Phosphoserine +P00924 119 Phosphoserine +P00924 138 Phosphoserine +P00924 188 Phosphoserine +P00924 313 Phosphothreonine +P00924 324 Phosphothreonine +P00924 60 Glycyl +P00924 243 Glycyl +P00924 358 Glycyl +P32353 324 Glycyl +P32353 344 Glycyl +Q03071 2 N-acetylserine +Q03071 2 Phosphoserine +P53938 103 N-linked +P53938 104 N-linked +Q12452 345 Phosphothreonine +P38748 376 Phosphoserine +P38748 369 Glycyl +P38748 410 Glycyl +P38748 450 Glycyl +P38071 339 Phosphoserine +P23776 165 N-linked +P23776 325 N-linked +P52911 50 N-linked +P52911 77 N-linked +P52911 86 N-linked +P52911 90 N-linked +P52911 106 N-linked +P52911 157 N-linked +P52911 220 N-linked +P52911 281 N-linked +P52911 285 N-linked +P52911 310 N-linked +P52911 317 N-linked +P52911 322 N-linked +P52911 401 N-linked +P52911 480 N-linked +P52911 539 N-linked +Q04660 23 Phosphoserine +Q04660 72 Phosphoserine +Q04660 76 Phosphoserine +Q04660 146 Phosphoserine +Q04660 149 Phosphoserine +Q04660 418 Phosphoserine +Q04660 127 Glycyl +P05453 2 N-acetylserine +P05453 571 Phosphoserine +P19097 50 Phosphoserine +P19097 180 O-(pantetheine +P19097 523 Phosphoserine +P19097 958 Phosphoserine +P19097 1440 Phosphoserine +P19097 37 Glycyl +P53917 18 Phosphoserine +P53917 81 Phosphoserine +P53917 524 Phosphoserine +P53917 527 Phosphoserine +P53917 528 Phosphoserine +P21268 87 Phosphoserine%3B +P21268 110 Phosphoserine +P21268 114 Phosphoserine +P21268 306 Phosphothreonine +P15646 16 Asymmetric +P15646 16 Omega-N-methylarginine%3B +P15646 22 Omega-N-methylarginine%3B +P15646 30 Asymmetric +P15646 34 Asymmetric +P15646 34 Omega-N-methylarginine%3B +P15646 40 Omega-N-methylarginine%3B +P15646 48 Asymmetric +P15646 52 Asymmetric +P15646 52 Omega-N-methylarginine%3B +P15646 58 Omega-N-methylarginine%3B +P15646 70 Asymmetric +P15646 70 Omega-N-methylarginine%3B +P15646 73 Asymmetric +P15646 73 Omega-N-methylarginine%3B +P15646 81 Asymmetric +P15646 81 Omega-N-methylarginine%3B +P15646 150 Glycyl +P40988 48 Phosphoserine +P40988 50 Phosphoserine +P40988 39 Glycyl +P53918 57 Phosphoserine +P53918 112 Phosphoserine +P53918 172 Phosphoserine +P53918 637 Phosphoserine +P53918 230 N-linked +P53918 471 N-linked +P53918 492 N-linked +P38224 288 Phosphoserine +P38224 293 Phosphothreonine +P38224 296 Phosphoserine +P40020 81 Phosphoserine +P40020 172 Phosphoserine +P40020 225 Phosphoserine +Q08906 130 GPI-anchor +Q08906 92 N-linked +P12385 182 N5-methylglutamine +P12385 421 Phosphoserine +P12385 331 Glycyl +Q03103 21 N-linked +Q03103 35 N-linked +Q03103 53 N-linked +Q03103 130 N-linked +Q03103 342 N-linked +Q03103 425 N-linked +Q03103 458 N-linked +Q03103 468 N-linked +Q03103 491 N-linked +P17261 177 N-linked +Q03661 500 Phosphothreonine +Q03661 532 Phosphoserine +Q03661 579 Phosphoserine +Q03661 583 Phosphoserine +Q03661 608 Phosphoserine +Q03661 662 Phosphoserine +Q03661 865 Phosphoserine +Q03661 866 Phosphoserine +Q03661 888 Phosphoserine +Q03661 911 Phosphoserine +Q03661 937 Phosphoserine +Q03661 1092 Phosphoserine +Q03661 1096 Phosphoserine +Q03661 1098 Phosphoserine +Q03661 1166 Phosphoserine +Q03661 1176 Phosphoserine +Q03661 1178 Phosphoserine +Q03661 1214 Phosphoserine +Q03661 1254 Phosphoserine +Q03661 1290 Phosphoserine +Q03661 1326 Phosphoserine +Q03661 1332 Phosphoserine +Q03661 1403 Phosphoserine +Q03661 1409 Phosphoserine +Q03661 1450 Phosphoserine +Q03661 1454 Phosphoserine +Q03661 1539 Phosphoserine +Q03661 1590 Phosphoserine +Q03661 1591 Phosphoserine +P53743 7 Phosphoserine +P53743 13 Phosphoserine +P53743 14 Phosphoserine +P42940 2 N-acetylserine +Q08421 30 Phosphoserine +P39875 372 Phosphoserine +P38261 58 Phosphothreonine +P38261 139 Phosphoserine +P38261 482 Phosphoserine +P38261 219 Glycyl +P09201 12 Phosphoserine +P34756 2 N-acetylserine +P34756 186 Phosphoserine +P34756 1627 Phosphoserine +P34756 1630 Phosphoserine +P34756 1938 Phosphoserine +P34756 1953 Phosphothreonine +P32604 435 Phosphoserine +P32604 446 Phosphoserine +Q04952 844 N-linked +Q04952 874 N-linked +Q04952 955 N-linked +Q04952 1002 N-linked +Q04952 1170 N-linked +Q04952 1360 N-linked +Q04952 1579 N-linked +Q04952 1761 N-linked +P36170 1146 GPI-anchor +P36170 122 N-linked +P36170 157 N-linked +P36170 279 N-linked +P36170 389 N-linked +P36170 452 N-linked +P36170 515 N-linked +P36170 578 N-linked +P36170 656 N-linked +P36170 686 N-linked +P36170 879 N-linked +P36170 1092 N-linked +P36170 1099 N-linked +P08640 1346 GPI-anchor +P08640 817 N-linked +P08640 874 N-linked +P32768 1514 GPI-anchor +P32768 135 N-linked +P32768 187 N-linked +P32768 262 N-linked +P32768 329 N-linked +P32768 374 N-linked +P32768 419 N-linked +P32768 464 N-linked +P32768 509 N-linked +P32768 554 N-linked +P32768 599 N-linked +P32768 644 N-linked +P32768 689 N-linked +P32768 734 N-linked +P32768 1114 N-linked +Q05040 115 Phosphoserine +Q05040 132 Phosphothreonine +Q08907 182 GPI-anchor +P53971 951 Phosphothreonine +P53971 958 Phosphoserine +Q03254 701 Phosphoserine +Q03254 718 Phosphoserine +Q03254 720 Phosphoserine +Q03254 74 Glycyl +Q12119 46 Phosphothreonine +P17064 18 Phosphoserine +P17064 16 Glycyl +P39676 22 Phosphothreonine +P07149 1 N-acetylmethionine +P07149 733 Phosphothreonine +P07149 1121 Phosphoserine +P07149 1364 Glycyl +P40039 43 Phosphoserine +P40039 46 Phosphothreonine +Q08991 109 N-linked +Q08991 117 N-linked +Q08991 235 N-linked +P25653 1588 GPI-anchor +P25653 29 N-linked +P25653 231 N-linked +P25653 298 N-linked +P25653 347 N-linked +P25653 386 N-linked +P25653 426 N-linked +P25653 495 N-linked +P25653 535 N-linked +P25653 661 N-linked +P25653 674 N-linked +P25653 713 N-linked +P25653 889 N-linked +P25653 907 N-linked +P25653 1079 N-linked +P25653 1400 N-linked +P42837 829 Phosphoserine +P38911 2 N-acetylserine +P38911 80 Phosphoserine +P38911 81 Phosphoserine +P38911 89 Phosphothreonine +P38911 184 Phosphotyrosine%3B +P38911 186 Phosphoserine%3B +P20081 2 N-acetylserine +P20081 51 Phosphoserine +P38631 269 Phosphothreonine +P38631 272 Phosphothreonine +P38631 259 Glycyl +P38631 275 Glycyl +P38631 386 Glycyl +P38631 910 Glycyl +P38631 915 Glycyl +P38631 1539 Glycyl +P38631 1547 Glycyl +Q07825 69 Phosphoserine +Q07825 92 Phosphoserine +Q07825 95 Phosphoserine +P32791 69 N-linked +P32791 100 N-linked +P32791 124 N-linked +P53746 51 N-linked +P53746 80 N-linked +P53746 101 N-linked +P53746 113 N-linked +P53746 127 N-linked +P53746 135 N-linked +P08417 428 Phosphothreonine +P28003 194 Phosphothreonine +P28003 207 Phosphoserine +P28003 211 Phosphoserine +P11412 2 N-acetylserine +P11412 142 Phosphoserine +P11412 145 Phosphotyrosine +P04385 381 Phosphoserine +P04386 694 Phosphotyrosine +P04386 696 Phosphoserine +P04386 699 Phosphoserine +P04386 703 Phosphoserine +P04386 712 Phosphoserine +Q04739 12 Phosphoserine +Q04739 21 Phosphoserine +Q04739 44 Phosphoserine +Q04739 135 Phosphoserine +Q04739 276 Phosphoserine +Q04739 279 Phosphoserine +P39719 28 N-linked +P39719 65 N-linked +P39719 81 N-linked +P39719 156 N-linked +P39719 323 N-linked +P36033 85 N-linked +P36033 108 N-linked +P36033 120 N-linked +P36033 134 N-linked +P36033 341 N-linked +Q12473 89 N-linked +Q12473 112 N-linked +Q12473 124 N-linked +P12709 2 N-acetylserine +P12709 53 Phosphothreonine +P12709 220 Phosphothreonine +P17649 326 N6-(pyridoxal +P38225 184 N-linked +P38225 289 N-linked +P38225 534 N-linked +P38225 591 N-linked +P38993 27 N-linked +P38993 74 N-linked +P38993 77 N-linked +P38993 88 N-linked +P38993 113 N-linked +P38993 194 N-linked +P38993 198 N-linked +P38993 244 N-linked +P38993 265 N-linked +P38993 292 N-linked +P38993 300 N-linked +P38993 359 N-linked +P38993 381 N-linked +Q08913 109 N-linked +Q08913 117 N-linked +Q08913 235 N-linked +P39521 44 Phosphoserine +P39521 228 Phosphoserine +P39521 230 Phosphothreonine +P39521 247 Phosphothreonine +P39521 264 Phosphoserine +P53121 616 Phosphoserine +P53121 635 Phosphoserine +P53121 779 Phosphoserine +P53121 782 Phosphoserine +P53121 149 N-linked +P53121 321 N-linked +P53121 547 N-linked +Q08967 610 Phosphoserine +Q08967 626 Phosphothreonine +Q08967 771 Phosphoserine +Q08967 774 Phosphoserine +Q08967 143 N-linked +Q08967 281 N-linked +P53739 140 Phosphoserine +P53739 144 Phosphoserine +P53739 171 Phosphoserine +P53739 175 Phosphoserine +P53739 185 Phosphoserine +P53739 300 Phosphoserine +P53739 414 Phosphoserine +P53739 462 Phosphoserine +P23900 150 Phosphoserine +P23900 168 Phosphothreonine +P23900 209 Phosphoserine +P23900 212 Phosphoserine +P38310 449 Phosphoserine +P38310 453 Phosphoserine +P00358 302 Phosphoserine +P00358 46 Glycyl +P00358 63 Glycyl +P00359 302 Phosphoserine +P00359 46 Glycyl +P00359 63 Glycyl +P38260 12 Phosphoserine +P43561 24 N-linked +P43561 86 N-linked +P43561 115 N-linked +P43561 196 N-linked +P43561 200 N-linked +P43561 246 N-linked +P43561 295 N-linked +P43561 364 N-linked +P43561 455 N-linked +P41813 708 Phosphoserine +P41813 832 Phosphoserine +P41813 833 Phosphoserine +P40989 288 Phosphothreonine +P40989 291 Phosphothreonine +P40989 278 Glycyl +P40989 405 Glycyl +P40989 929 Glycyl +P40989 934 Glycyl +P40989 1558 Glycyl +P40989 1566 Glycyl +Q08905 85 N-linked +Q08905 108 N-linked +Q08905 120 N-linked +Q08905 134 N-linked +Q08908 117 N-linked +Q12209 371 N-linked +Q12209 383 N-linked +Q12209 384 N-linked +Q03002 441 Phosphoserine +Q03898 54 Phosphoserine +Q03898 68 Phosphothreonine +Q03898 74 Phosphoserine +Q03898 88 Phosphoserine +Q04433 506 GPI-anchor +Q04433 412 N-linked +Q04433 464 N-linked +Q04433 503 N-linked +P39712 1299 GPI-anchor +P39712 135 N-linked +P39712 187 N-linked +P39712 203 N-linked +P39712 257 N-linked +P39712 262 N-linked +P39712 270 N-linked +P39712 329 N-linked +P39712 419 N-linked +P39712 464 N-linked +P39712 509 N-linked +P39712 554 N-linked +P39712 599 N-linked +P39712 644 N-linked +P39712 689 N-linked +P39712 734 N-linked +P39712 888 N-linked +Q07651 230 Phosphoserine +Q07651 232 Phosphoserine +Q07651 235 Phosphothreonine +Q07651 73 N-linked +P31380 232 Phosphoserine +P31380 369 Phosphoserine +P31380 451 Phosphoserine +Q12035 1 N-acetylmethionine +Q06205 80 Phosphoserine +Q06205 82 Phosphoserine +Q04991 238 Phosphoserine +Q04991 249 Phosphoserine +Q04991 269 Phosphoserine +P53848 2 N-acetylserine +P53848 286 Phosphoserine +P38894 1052 GPI-anchor +P38894 135 N-linked +P38894 187 N-linked +P38894 203 N-linked +P38894 262 N-linked +P38894 663 N-linked +P38894 749 N-linked +Q12029 2 N-acetylalanine +P16892 180 Phosphothreonine +P16892 182 Phosphotyrosine +P16892 345 Glycyl +P53913 2 N-acetylserine +P45976 50 Phosphoserine +P04397 562 Phosphoserine +P13181 32 Phosphoserine +P13181 35 Phosphoserine +P13181 39 Phosphoserine +P13181 48 Phosphoserine +P13181 50 Phosphoserine +P13181 53 Phosphoserine +P13181 55 Phosphoserine +P13045 1 N-acetylmethionine +P43574 167 Phosphoserine +P43574 262 Phosphoserine +P43574 270 Phosphoserine +P43574 369 Phosphothreonine +P43574 399 Phosphoserine +P43574 418 Phosphoserine +P39012 87 N-linked +P28006 415 Phosphoserine +P28006 424 Phosphoserine +P40056 2 N-acetylserine +P40056 45 Phosphoserine +P40056 173 N-linked +P40056 196 N-linked +P14742 253 Phosphoserine +P14742 334 Phosphothreonine +P14742 336 Phosphoserine +P40036 51 Phosphoserine +P40036 52 Phosphothreonine +P40036 155 Phosphoserine +P40036 221 Phosphoserine +P40036 238 Phosphoserine +P39732 497 Phosphoserine +P39732 501 Phosphoserine +P39732 609 Phosphoserine +P25346 80 N-linked +P36143 230 O-linked +P36143 598 O-linked +Q05670 20 Phosphothreonine +Q05670 67 Phosphoserine +Q05670 72 Phosphoserine +Q05670 84 Phosphoserine +Q05670 88 Phosphothreonine +Q05670 100 Phosphoserine +Q05670 106 Phosphoserine +Q08559 91 N-linked +P46949 92 Phosphoserine +P46949 100 Phosphoserine +P46949 134 Phosphoserine +P46949 163 Phosphoserine +P46949 180 Phosphoserine +P46949 182 Phosphoserine +P46949 237 Phosphoserine +P46949 238 Phosphoserine +P46949 532 Phosphoserine +P08431 27 Phosphoserine +P04387 1 N-acetylmethionine +P25555 130 Phosphothreonine +P51601 15 Phosphothreonine +P51601 23 Phosphoserine +P43535 2 N-acetylalanine +Q04839 87 Phosphoserine +Q04839 106 Phosphoserine +Q04839 111 Phosphoserine +P22146 528 GPI-anchor +P22146 40 N-linked +P22146 57 N-linked +P22146 95 N-linked +P22146 149 N-linked +P22146 165 N-linked +P22146 253 N-linked +P22146 283 N-linked +P22146 321 N-linked +P22146 409 N-linked +P22146 495 N-linked +Q06135 531 GPI-anchor +Q06135 498 N-linked +P39993 46 Phosphoserine +P39993 284 Phosphoserine +Q06648 254 Phosphoserine +Q06648 258 Phosphoserine +Q06648 337 Phosphoserine +Q06648 345 Phosphoserine +Q06648 367 Phosphoserine +Q03833 70 Phosphoserine +Q03833 343 Phosphoserine +Q03833 690 Phosphoserine +Q03833 694 Phosphoserine +Q03833 696 Phosphoserine +Q03833 734 Phosphoserine +Q03833 747 Phosphoserine +P38196 54 Phosphothreonine +P38196 56 Phosphoserine +P38196 635 Glycyl +P11710 178 Phosphothreonine +P11710 190 Phosphoserine +P11710 256 Phosphoserine +P11710 281 Phosphothreonine +P11710 424 Phosphothreonine +P38297 398 Glycyl +P38297 464 Glycyl +P18852 107 Cysteine +P18852 106 S-palmitoyl +P18852 107 S-farnesyl +P47102 49 Phosphoserine +Q04233 165 Phosphoserine +Q04233 304 Phosphoserine +Q04233 616 Phosphoserine +Q04233 622 Phosphoserine +Q04233 707 Phosphoserine +Q04233 720 Phosphoserine +P32614 66 Phosphoserine +P31381 45 Phosphoserine +P31381 58 Phosphoserine +P19145 76 Glycyl +P28007 4 Asymmetric +P28007 8 Asymmetric +P28007 11 Asymmetric +P28007 15 Asymmetric +P28007 19 Asymmetric +P28007 147 Asymmetric +P28007 154 Asymmetric +P28007 158 Asymmetric +P28007 162 Asymmetric +P28007 165 Asymmetric +P28007 171 Asymmetric +P28007 174 Asymmetric +P28007 180 Asymmetric +P28007 184 Asymmetric +P28007 189 Asymmetric +P28007 193 Asymmetric +P28007 197 Asymmetric +P28007 201 Asymmetric +P28007 77 Glycyl +Q03655 498 GPI-anchor +Q03655 201 N-linked +Q03655 269 N-linked +Q03655 350 N-linked +Q03655 385 N-linked +Q03655 404 N-linked +Q03655 422 N-linked +P39726 102 N6-lipoyllysine +Q08271 447 GPI-anchor +Q08271 151 N-linked +Q08271 398 N-linked +Q08193 462 GPI-anchor +Q08193 24 N-linked +Q08193 60 N-linked +Q08193 166 N-linked +Q08193 299 N-linked +Q08193 344 N-linked +Q08193 359 N-linked +P38011 2 N-acetylalanine +P38011 96 Phosphothreonine +P38011 168 Phosphothreonine +P38011 46 Glycyl +P38011 53 Glycyl +P38011 107 Glycyl +P38011 137 Glycyl +P38011 161 Glycyl +P07261 447 Phosphothreonine +P07261 449 Phosphoserine +P07261 482 Phosphoserine +P07261 489 Phosphoserine +P07261 538 Phosphoserine +P14065 306 Phosphoserine +P32775 190 Phosphoserine +P17695 37 Phosphoserine +P17695 61 S-glutathionyl +P17695 91 Phosphoserine +P37303 213 N6-(pyridoxal +P37303 367 Phosphoserine +P37303 369 Phosphoserine +P37303 370 Phosphothreonine +P37303 228 Glycyl +P38875 184 N-linked +P40106 90 Phosphoserine +P40106 64 Glycyl +P40106 144 Glycyl +P35197 151 Phosphothreonine +P35197 157 Phosphoserine +P35197 161 Phosphothreonine +P35197 168 Phosphoserine +P35197 170 Phosphothreonine +P35197 260 Phosphoserine +Q03016 68 Phosphoserine +Q03016 99 Phosphothreonine +Q03016 103 Phosphoserine +Q03016 143 Phosphoserine +Q03016 260 Phosphoserine +Q03016 264 Phosphothreonine +Q03016 269 Phosphoserine +P03069 17 Phosphoserine +P03069 165 Phosphothreonine%3B +P03069 218 Phosphoserine +Q01722 151 Phosphoserine +Q01722 406 Phosphoserine +Q01722 409 Phosphoserine +P32621 41 N-linked +P32621 280 N-linked +P32621 335 N-linked +Q02979 653 Phosphoserine +Q02979 983 Phosphoserine +P37291 20 Phosphothreonine +P37291 26 Phosphoserine +P37291 248 N6-(pyridoxal +P37291 429 Phosphoserine +P37291 456 Glycyl +P40107 119 N-linked +P40107 242 N-linked +P40107 246 N-linked +P40107 249 N-linked +P0CE11 149 N-linked +P0CE11 153 N-linked +P43577 2 N-acetylserine +P10823 2 N-myristoyl +P10823 4 S-palmitoyl +Q08886 91 Phosphoserine +Q08886 161 Phosphothreonine +Q05584 257 Phosphoserine +P38682 170 Phosphoserine +P38682 306 Phosphoserine +P38682 389 Phosphoserine +P38682 398 Phosphoserine +P48813 29 Phosphoserine +P48813 113 Phosphoserine +P48813 124 Phosphoserine +P48813 127 Phosphothreonine +P48813 34 Glycyl +P48813 39 Glycyl +P48813 41 Glycyl +P48813 61 Glycyl +P48813 132 Glycyl +P53839 31 Phosphothreonine +Q00055 2 N-acetylserine +Q00055 24 Phosphoserine +Q00055 27 Phosphoserine +Q06636 16 Phosphoserine +P49095 773 N6-(pyridoxal +Q06336 348 Phosphothreonine +Q06336 353 Phosphoserine +Q06336 357 Phosphoserine +Q06336 378 Phosphoserine +Q06336 394 Phosphoserine +P38817 180 Glycyl +P38817 287 Glycyl +P38138 114 N-linked +P38138 126 N-linked +P38138 142 N-linked +P38138 173 N-linked +P38138 345 N-linked +P38138 783 N-linked +P38138 791 N-linked +P38138 867 N-linked +P38138 880 N-linked +P38138 907 N-linked +P38138 941 N-linked +Q04924 145 N-linked +Q04924 240 N-linked +Q04924 358 N-linked +Q04924 520 N-linked +Q04924 525 N-linked +Q04924 688 N-linked +Q04924 699 N-linked +Q12434 2 N-acetylalanine +Q12434 27 Phosphothreonine +Q12434 40 Phosphoserine +P41818 12 Phosphoserine +P41818 118 Phosphothreonine%3B +P41818 158 Phosphoserine +P41818 184 Phosphoserine +P47011 230 O-linked +P47011 232 O-linked +P47011 367 O-linked +P38263 27 Phosphoserine +P38263 20 Glycyl +Q12263 406 Phosphoserine +Q12263 465 Phosphoserine +Q12263 471 Phosphoserine +Q12263 617 Phosphoserine +Q12263 689 Phosphoserine +Q12263 719 Phosphoserine +Q12263 805 Phosphoserine +Q12263 807 Phosphoserine +Q12263 883 Phosphoserine +Q12263 884 Phosphothreonine +Q12263 930 Phosphoserine +P32288 2 N-acetylalanine +P32288 5 Phosphoserine +P32288 283 Glycyl +P32288 324 Glycyl +P32288 363 Glycyl +P25373 27 S-glutathionyl +P25373 11 Glycyl +Q12680 2070 Phosphothreonine +P37292 265 N6-(pyridoxal +Q07830 66 N-linked +Q07830 71 N-linked +Q07830 100 N-linked +Q07830 182 N-linked +Q07830 203 N-linked +Q07830 411 N-linked +Q07830 681 N-linked +Q07830 682 N-linked +Q07830 707 N-linked +Q07830 742 N-linked +P41277 90 Phosphoserine +P41277 64 Glycyl +P41277 64 Glycyl +P41277 144 Glycyl +P18494 251 Phosphoserine +P18494 267 Phosphoserine +P18494 285 Phosphoserine +P18494 469 Phosphoserine +P18494 552 Phosphoserine +P18494 562 Phosphoserine +P36148 632 Phosphoserine +P36148 637 Phosphoserine +P36148 647 Phosphoserine +P36148 651 Phosphoserine +P36148 654 Phosphoserine +P36148 657 Phosphoserine +P36148 664 Phosphoserine +P36148 668 Phosphoserine +P36148 671 Phosphoserine +P36148 673 Phosphothreonine +P36148 688 Phosphoserine +P36148 692 Phosphothreonine +P36148 693 Phosphoserine +Q04410 1 N-acetylmethionine +Q04410 155 Phosphoserine +Q04322 1 N-acetylmethionine +Q04322 17 Phosphothreonine +Q04322 37 Phosphoserine +Q04322 73 Phosphoserine +Q04322 139 Phosphoserine +Q04322 498 Glycyl +P48365 265 Phosphoserine +P48365 339 Phosphoserine +P23337 159 Phosphoserine +P23337 363 Phosphoserine +P23337 560 Phosphoserine +P23337 651 Phosphoserine +P23337 655 Phosphoserine +P23337 660 Phosphoserine%3B +P23337 662 Phosphoserine%3B +P23337 667 Phosphothreonine +P04911 2 N-acetylserine +P04911 5 N6-acetyllysine +P04911 8 N6-acetyllysine +P04911 106 N5-methylglutamine +P04911 129 Phosphoserine +P04911 127 Glycyl +P02294 7 N6-acetyllysine%3B +P02294 8 N6-acetyllysine%3B +P02294 11 Phosphoserine +P02294 12 N6-acetyllysine +P02294 17 N6-acetyllysine%3B +P02294 7 Glycyl +P02294 8 Glycyl +P02294 17 Glycyl +P02294 18 Glycyl +P02294 124 Glycyl +P38736 2 N-acetylserine +P38736 164 Phosphoserine +P39717 24 Phosphoserine +P40531 2 N-acetylserine +P40531 2 Phosphoserine +P40531 319 Phosphoserine +P40531 13 Glycyl +P40531 305 Glycyl +P40531 313 Glycyl +Q08484 69 Phosphoserine +Q08484 250 Phosphoserine +P48566 147 Phosphoserine +P48566 484 Phosphoserine +Q12753 125 Phosphoserine +Q12753 231 Phosphoserine +Q12753 241 Phosphoserine +Q12753 291 Phosphoserine +P32835 2 N-acetylserine +P32835 2 Phosphoserine +P53551 174 Phosphoserine +Q12341 354 Phosphoserine +P41921 1 N-acetylmethionine +P32836 2 N-acetylserine +P32836 2 Phosphoserine +P39996 66 Phosphoserine +P39996 72 Phosphoserine +P39996 99 Phosphoserine +P39996 116 Phosphoserine +P38970 17 Phosphoserine +P38970 19 Phosphoserine +P38970 68 Phosphoserine +P38970 72 Phosphoserine +P38970 160 Phosphoserine +P38970 273 Phosphoserine +P38970 277 Phosphoserine +P38970 324 Phosphoserine +P38970 333 Phosphoserine +P38970 336 Phosphoserine +P38970 358 Phosphoserine +P38970 391 Phosphoserine +P38970 395 Phosphoserine +P38199 358 Phosphoserine +P38199 360 Phosphoserine +P38199 362 Phosphoserine +Q12361 373 Phosphoserine +Q12361 903 Phosphoserine +P24814 199 Phosphoserine +P24814 300 Phosphoserine +Q04697 89 N-linked +Q04697 173 N-linked +P32806 436 Phosphoserine +Q96VH4 2 N-acetylserine +Q12096 136 N-linked +Q12096 177 N-linked +Q12096 187 N-linked +Q12096 425 N-linked +Q04080 100 N-linked +Q04080 170 N-linked +Q04080 228 N-linked +Q04080 247 N-linked +Q04080 299 N-linked +P38211 69 N-linked +P38211 101 N-linked +P40367 145 N-linked +P40367 185 N-linked +P40367 298 N-linked +P40367 506 N-linked +P47122 304 Phosphoserine +P47122 308 Phosphoserine +P47122 313 Phosphoserine +P47122 352 Phosphoserine +P47122 369 Glycyl +Q12068 333 Phosphoserine +P40956 153 Phosphoserine +P40956 181 Phosphotyrosine +P40956 184 Phosphoserine +P40956 187 Phosphoserine +P40956 240 Phosphoserine +P40956 249 Phosphothreonine +P38625 241 Glycyl +P38625 426 Glycyl +Q12180 221 Phosphoserine +Q12180 937 Phosphoserine +Q05580 2 N-acetylserine +Q05580 57 Phosphothreonine +Q05580 354 Phosphoserine +P53258 2 N-acetylserine +P53258 764 Phosphoserine +P53258 871 Phosphoserine +Q12344 25 Phosphoserine +Q12344 30 Phosphoserine +Q12344 89 Phosphothreonine +Q12344 389 Phosphoserine +P27472 159 Phosphoserine +P27472 363 Phosphoserine +P27472 467 Phosphoserine +P27472 651 Phosphoserine +P27472 655 Phosphoserine%3B +P27472 661 Phosphoserine%3B +P27472 663 Phosphoserine%3B +P27472 668 Phosphothreonine%3B +P36125 2 N-acetylserine +P41911 70 Phosphoserine +P41911 72 Phosphoserine +P41911 75 Phosphoserine +P49018 256 N-linked +P49018 346 N-linked +Q12214 110 Phosphoserine +Q01448 47 Phosphoserine +Q01448 49 Phosphoserine +Q01448 435 Phosphoserine +Q05905 143 Phosphoserine +P09950 337 N6-(pyridoxal +P28789 251 S-(dipyrrolylmethanemethyl)cysteine +Q12276 102 Phosphoserine +Q12276 128 Phosphothreonine +Q12276 277 Phosphoserine +Q12276 1013 Phosphoserine +Q12276 1130 Phosphothreonine +Q12276 1200 Phosphoserine +Q12276 1204 Phosphoserine +Q12276 1207 Phosphoserine +P41809 24 N-linked +P41809 1252 N-linked +P41809 1293 N-linked +P41809 1342 N-linked +P41809 1400 N-linked +P54839 276 Phosphoserine +P40480 14 Phosphoserine +P40480 16 Phosphoserine +P40480 37 Phosphothreonine +P40480 67 Phosphoserine +P40480 290 Phosphoserine +P40480 507 Phosphoserine +P40480 698 Phosphoserine +P40480 700 Phosphothreonine +P40480 778 Phosphoserine +P48570 385 Phosphoserine +P48570 396 Phosphothreonine +P48570 401 Phosphoserine +P48570 410 Phosphoserine +Q99332 167 Phosphoserine +Q99332 342 Phosphoserine +P17629 234 Phosphoserine +P47171 302 Phosphothreonine +P47171 304 Phosphoserine +P48353 109 Phosphoserine +P12683 552 Phosphothreonine +P12683 115 N-linked +P12683 181 N-linked +P12683 452 N-linked +P12683 490 N-linked +P02293 7 N6-acetyllysine%3B +P02293 8 N6-acetyllysine%3B +P02293 11 Phosphoserine +P02293 12 N6-acetyllysine +P02293 17 N6-acetyllysine%3B +P02293 7 Glycyl +P02293 8 Glycyl +P02293 17 Glycyl +P02293 18 Glycyl +P02293 124 Glycyl +P32769 124 Phosphoserine +Q07653 41 Phosphoserine +Q07653 303 Phosphoserine +Q07653 363 Phosphoserine +Q07653 491 Phosphoserine +Q07653 561 Phosphoserine +Q07653 671 Phosphoserine +Q07653 855 Phosphotyrosine +Q07653 857 Phosphoserine +Q07653 1005 Phosphoserine +Q07653 1034 Phosphoserine +P25364 342 Phosphothreonine +P25364 496 Phosphoserine +Q12373 174 Phosphoserine +Q03281 123 Phosphoserine +P05373 254 Phosphoserine +P04912 2 N-acetylserine +P04912 5 N6-acetyllysine +P04912 8 N6-acetyllysine +P04912 106 N5-methylglutamine +P04912 129 Phosphoserine +P04912 127 Glycyl +Q12692 2 N-acetylserine +Q12692 4 N6-acetyllysine +Q12692 9 N6-acetyllysine +Q12692 11 N6-acetyllysine +Q12692 15 N6-acetyllysine +P61830 5 N6%2CN6%2CN6-trimethyllysine%3B +P61830 5 N6%2CN6-dimethyllysine%3B +P61830 5 N6-methyllysine%3B +P61830 10 N6-acetyllysine%3B +P61830 10 N6-methyllysine%3B +P61830 11 Phosphoserine +P61830 15 N6%2CN6-dimethyllysine%3B +P61830 15 N6-acetyllysine%3B +P61830 19 N6-acetyllysine%3B +P61830 19 N6-methyllysine%3B +P61830 24 N6-acetyllysine%3B +P61830 24 N6-methyllysine%3B +P61830 28 N6%2CN6%2CN6-trimethyllysine%3B +P61830 28 N6%2CN6-dimethyllysine%3B +P61830 28 N6-acetyllysine%3B +P61830 28 N6-methyllysine%3B +P61830 37 N6%2CN6%2CN6-trimethyllysine%3B +P61830 37 N6%2CN6-dimethyllysine%3B +P61830 37 N6-acetyllysine%3B +P61830 37 N6-methyllysine%3B +P61830 57 N6-acetyllysine +P61830 65 N6-acetyllysine +P61830 80 N6%2CN6%2CN6-trimethyllysine%3B +P61830 80 N6%2CN6-dimethyllysine%3B +P61830 80 N6-methyllysine%3B +P02309 6 N6-acetyllysine +P02309 13 N6-acetyllysine +P02309 17 N6-acetyllysine +P02309 61 Phosphoserine +P02309 65 Phosphoserine +P02309 80 N6-acetyllysine +Q01766 266 Phosphoserine +P06774 2 N-acetylserine +P06774 52 Phosphoserine +P06774 265 Phosphothreonine +Q02516 7 Phosphoserine +Q03532 12 Phosphoserine +Q04458 111 Phosphoserine +P32480 713 Phosphoserine +P00498 1 N-acetylmethionine +Q05787 101 N-linked +Q05787 123 N-linked +Q05787 142 N-linked +Q05787 429 N-linked +Q05787 611 N-linked +Q99383 2 Phosphoserine +Q99383 3 Phosphoserine +Q99383 206 Phosphoserine +Q99383 458 Phosphothreonine +Q99383 462 Phosphoserine +P29295 143 Phosphoserine +P32479 610 Phosphoserine +P07172 230 N6-(pyridoxal +P40037 52 Glycyl +P19807 22 Phosphoserine +P19807 42 Phosphoserine +P19807 7 N-linked +P19807 20 N-linked +P19807 248 N-linked +P19807 341 N-linked +P47124 37 N-linked +Q9URQ5 2 N-acetylserine +P32874 804 N6-biotinyllysine +Q02959 582 Phosphoserine +Q02959 583 Phosphoserine +Q02959 613 Phosphoserine +Q02959 629 Phosphoserine +P34244 511 Phosphoserine +P34244 629 Phosphoserine +P34244 685 Phosphoserine +P34244 837 Phosphoserine +P34244 866 Phosphoserine +P34244 1220 Phosphoserine +P34244 1250 Phosphoserine +P34244 1284 Phosphoserine +P34244 1287 Phosphoserine +P34244 1325 Phosphoserine +P48362 2 N-acetylthreonine +P06775 76 Phosphothreonine +P12684 565 Phosphothreonine +P12684 115 N-linked +P12684 150 N-linked +P12684 158 N-linked +P12684 179 N-linked +P12684 428 N-linked +P12684 455 N-linked +Q05164 946 GPI-anchor +Q05164 28 N-linked +Q05164 35 N-linked +Q05164 493 N-linked +Q05164 601 N-linked +Q05164 638 N-linked +P38753 2 N-acetylserine +P38753 162 Phosphoserine +P10961 1 N-acetylmethionine +P10961 97 Phosphothreonine +P10961 450 Phosphoserine +P10961 458 Phosphoserine +P10961 471 Phosphoserine +P10961 478 Phosphoserine +P10961 528 Phosphoserine +P22943 21 Phosphoserine%3B +P22943 24 Phosphoserine +P22943 59 Phosphoserine +P22943 73 Phosphoserine +P22943 97 Phosphoserine +P32485 2 N-acetylthreonine +P32485 174 Phosphothreonine +P32485 176 Phosphotyrosine +Q12122 399 Phosphoserine +Q12122 410 Phosphothreonine +Q03213 146 Phosphoserine +Q03213 153 Phosphoserine +P15992 2 N-acetylserine +P15992 42 Phosphothreonine +P15992 90 Phosphoserine +P15992 163 Phosphothreonine +P15992 208 Phosphoserine +P15992 211 Phosphoserine +P25619 308 Phosphoserine +P25619 331 Phosphothreonine +P40325 2 N-acetylserine +P40325 3 Glycyl +P40325 18 Glycyl +Q12345 157 Phosphoserine +Q12345 211 Phosphoserine +P39730 405 Phosphoserine +Q04432 138 Cysteine +Q12329 182 Phosphoserine +Q12329 213 Phosphoserine +Q12329 214 Phosphoserine +Q12329 215 Phosphoserine +Q12329 223 Phosphoserine +P53119 1 N-acetylmethionine +P32465 23 Phosphoserine +P32465 38 Phosphoserine +P32465 44 Phosphoserine +P32465 228 N-linked +P32466 23 Phosphoserine +P32466 225 N-linked +P32466 416 N-linked +P38695 126 N-linked +P38695 249 N-linked +P38695 61 Glycyl +P39004 556 Phosphothreonine +P39004 91 N-linked +P39004 228 N-linked +P39004 560 Glycyl +P46958 1 N-acetylmethionine +P46958 13 Phosphothreonine +P46958 23 Phosphoserine +P46958 27 Phosphoserine +P46958 39 Phosphoserine +P46958 122 Phosphoserine +P46958 130 Phosphoserine +P46958 136 Phosphoserine +P46958 147 Phosphoserine +P46958 148 Phosphoserine +P40060 124 Phosphothreonine +P20459 52 Phosphoserine%3B +P20459 292 Phosphoserine +P20459 294 Phosphoserine +P28817 326 Phosphothreonine +P0CY09 1 N-acetylmethionine +Q04178 2 N-acetylserine +P38922 343 Phosphoserine +P38922 355 Phosphoserine +Q08732 37 Phosphoserine +Q08732 382 Phosphoserine +Q08732 472 Phosphoserine +Q08732 495 Phosphothreonine +Q08732 498 Phosphoserine +P50079 61 N-linked +P50079 155 N-linked +P50079 256 N-linked +P50079 280 N-linked +P50079 315 N-linked +P50079 421 N-linked +P04806 245 Phosphoserine +P04806 272 Phosphoserine +P04807 15 Phosphoserine +P04807 38 Phosphothreonine +P04807 158 Phosphoserine +P04807 245 Phosphoserine +P04807 272 Phosphoserine +Q12520 165 N-linked +P15496 7 Phosphoserine +P09064 40 Phosphoserine +P09064 69 Phosphothreonine +P09064 80 Phosphoserine +P09064 92 Phosphoserine +P09064 112 Phosphoserine +P09064 116 Phosphothreonine +P09064 118 Phosphoserine +P10081 2 N-acetylserine +P10081 73 Phosphothreonine +P10081 77 Phosphoserine +P10081 129 Phosphoserine +P10081 146 Phosphothreonine +P39936 74 Phosphoserine +P39936 196 Phosphothreonine +P39936 301 Phosphothreonine +P39936 503 Phosphoserine +P39936 913 Phosphoserine +P39979 2 N-acetylserine +P19882 102 Phosphothreonine +P19882 485 Phosphoserine +P22202 552 Phosphoserine +P53686 2 N-acetylserine +P53686 340 Phosphoserine +P54862 87 N-linked +P54862 227 N-linked +P40886 92 N-linked +P40886 102 N-linked +P40886 429 N-linked +P53892 100 Phosphoserine +P53892 106 Phosphoserine +P53892 211 Phosphothreonine +P38284 217 Phosphoserine +P38274 317 Phosphoserine +P38274 614 Phosphothreonine +P0CS90 330 Phosphothreonine +P19211 2 Phosphoserine +P19211 7 Phosphothreonine +P19211 51 Hypusine +Q12522 174 Phosphoserine%3B +Q12522 175 Phosphoserine%3B +Q12522 231 Phosphoserine +P06168 355 Phosphoserine +Q03824 275 N-linked +Q03824 343 N-linked +Q03824 344 N-linked +Q03824 379 N-linked +Q03824 517 N-linked +Q03824 569 N-linked +Q03824 574 N-linked +Q12271 497 Phosphoserine +Q12271 986 Phosphoserine +Q12271 1035 Phosphoserine +Q12271 1105 Phosphothreonine +P00724 23 N-linked +P00724 64 N-linked +P00724 97 N-linked +P00724 111 N-linked +P00724 118 N-linked +P00724 165 N-linked +P00724 266 N-linked +P00724 275 N-linked +P00724 356 N-linked +P00724 369 N-linked +P00724 384 N-linked +P00724 398 N-linked +P00724 512 N-linked +P32589 2 N-acetylserine +P32589 242 Phosphothreonine +P32589 660 Phosphoserine +P32589 195 Glycyl +P17709 2 N-acetylserine +P17709 2 Phosphoserine +P17709 470 Phosphoserine +P43581 75 N-linked +P40441 194 N-linked +P23585 2 N-acetylserine +P23585 11 Phosphoserine +P23585 13 Phosphoserine +P23585 17 Phosphoserine +P23585 20 Phosphoserine +P23585 29 Phosphothreonine +P23585 32 Phosphoserine +P23585 266 Phosphoserine%3B +P23585 539 Phosphoserine%3B +P23585 82 N-linked +P32467 425 N-linked +P32467 45 Glycyl +P39003 91 N-linked +P39003 228 N-linked +P39003 560 Glycyl +P40885 87 N-linked +P40885 227 N-linked +P43598 64 Phosphoserine +P43598 65 Phosphothreonine +P43598 95 Phosphoserine +P43598 96 Phosphoserine +P43598 132 Phosphothreonine +P43598 164 Phosphoserine +Q02821 1 N-acetylmethionine +P40069 646 Phosphoserine +Q03694 273 Phosphoserine +P47046 690 Phosphoserine +P28241 105 Phosphothreonine +P28241 153 Phosphothreonine +P28241 327 Phosphothreonine +P28241 349 Phosphothreonine +P40154 67 Phosphoserine +P40154 129 Phosphoserine +P47170 680 Phosphoserine +P47170 737 Phosphoserine +P53901 392 Phosphoserine +P50942 152 Phosphoserine +P50942 522 Phosphoserine +P50942 1005 Phosphoserine +P50942 1016 Phosphoserine +P50942 1032 Phosphothreonine +P50942 1095 Phosphoserine +Q04213 2 Phosphoserine +Q04213 9 Phosphothreonine +Q04213 65 Phosphoserine +Q04213 73 Phosphoserine +Q04213 242 Phosphoserine +P07250 1 N-acetylmethionine +P07250 97 Phosphoserine +P07260 2 Phosphoserine%3B +P07260 15 Phosphoserine%3B +P07260 22 Phosphothreonine +P07260 28 Phosphoserine +P07260 30 Phosphoserine +P07260 114 Glycyl +P39520 208 Phosphoserine +P39520 1041 Phosphoserine +P43579 27 Phosphoserine +P43579 487 Phosphoserine +P43579 493 Phosphoserine +P43579 504 Phosphoserine +P43579 507 Phosphothreonine +P32481 60 Phosphothreonine +P32481 258 Phosphoserine +P39935 181 Phosphothreonine +P39935 883 Phosphoserine +P39935 888 Phosphothreonine +P39935 908 Phosphoserine +P39935 948 Phosphoserine +P23301 2 N-acetylserine +P23301 2 Phosphoserine +P23301 10 Phosphothreonine +P23301 51 Hypusine +P23301 74 Phosphoserine +P23301 86 Glycyl +Q9P305 2 N-acetylserine +Q9P305 6 Phosphoserine +Q9P305 63 Phosphoserine +Q9P305 108 Phosphoserine +Q9P305 119 Phosphoserine +P47042 96 Phosphoserine +P47169 903 Phosphoserine +P05694 89 Phosphoserine +P05694 242 Phosphoserine +P05694 566 Phosphothreonine +P05694 629 Phosphoserine +P05694 706 Phosphoserine +P38920 441 Phosphoserine%3B +P40457 1512 Phosphoserine +P40457 1670 Phosphoserine +P53152 71 Phosphoserine +P38888 86 N-linked +P38888 517 N-linked +P38888 672 N-linked +P38888 762 N-linked +P41821 32 N-linked +P41821 70 N-linked +P41821 112 N-linked +P41821 125 N-linked +P41821 159 N-linked +P41821 175 N-linked +P41821 228 N-linked +P41821 238 N-linked +P41821 265 N-linked +P41821 282 N-linked +P41821 285 N-linked +P41821 291 N-linked +P41821 324 N-linked +P34072 25 Phosphothreonine +P34072 247 Phosphoserine +P34072 276 Phosphoserine +P34072 442 Phosphoserine +P34072 518 Phosphoserine%3B +P32047 8 Phosphoserine +P32047 11 Phosphoserine +P32047 14 Phosphoserine +P32047 56 Phosphoserine +P32047 74 Phosphoserine +P32047 79 Phosphoserine +P32047 121 Phosphothreonine +P32047 145 Phosphoserine +P32047 156 Phosphoserine +P32047 160 Phosphoserine +P32047 169 Phosphothreonine +P32047 171 Phosphoserine +P32047 173 Phosphothreonine +P32047 183 Phosphoserine +P32047 189 Phosphoserine +P32047 227 Phosphotyrosine +P32047 228 Phosphoserine +P32047 257 Phosphoserine +P32047 265 Phosphoserine +P32047 295 Phosphotyrosine +P32047 297 Phosphoserine +P32047 320 Phosphoserine +P32047 353 Phosphoserine +P32047 439 Phosphoserine +Q12372 6 Phosphoserine +Q12372 21 Phosphothreonine +Q12372 23 Phosphoserine +Q06324 12 Phosphothreonine +Q06324 16 Phosphoserine +Q06324 37 Phosphoserine +P46982 113 N-linked +P46982 136 N-linked +P46982 259 N-linked +P46982 264 N-linked +P40549 34 N-linked +P40549 168 N-linked +P53745 132 N-linked +P53745 167 N-linked +P53745 223 N-linked +P53745 349 N-linked +P43563 33 Phosphotyrosine +P43563 59 Phosphoserine +P43563 76 Phosphothreonine +P23641 2 N-acetylserine%3B +P23641 4 Phosphoserine +P23641 145 Phosphoserine +P47083 2 N-acetylserine +P47083 176 Phosphoserine +P47083 177 Phosphoserine +P47083 181 Phosphotyrosine +Q06211 1294 Phosphothreonine +Q12205 45 N-linked +P38069 34 N-linked +P38069 363 N-linked +P38069 473 N-linked +P53129 22 Phosphoserine +P53129 71 Phosphoserine +P53379 575 GPI-anchor +P53379 180 N-linked +P53379 190 N-linked +P53379 219 N-linked +P53379 229 N-linked +P53379 232 N-linked +P53379 286 N-linked +P53379 346 N-linked +P53379 471 N-linked +P53379 517 N-linked +P40577 293 Phosphoserine +P39106 50 N-linked +P39106 225 N-linked +P39106 254 N-linked +P39106 383 N-linked +P35724 114 Phosphoserine +P35724 175 Phosphoserine +P35724 177 Phosphothreonine +P35724 182 Phosphoserine +P35724 383 Phosphoserine +P35724 571 Phosphothreonine +P35724 576 Phosphoserine +P35724 582 Phosphoserine +P53059 187 N-linked +P38257 2 N-acetylserine +P38257 48 Phosphoserine +P38257 49 Phosphoserine +P38257 61 Phosphoserine +P40484 34 Phosphoserine +P40484 36 Phosphoserine +P40484 80 Phosphoserine +P40484 229 Phosphoserine +P54785 1 N-acetylmethionine +P41940 153 Phosphothreonine +P41940 244 Glycyl +P53725 2 N-acetylserine +P53725 42 Phosphoserine +P53725 150 Phosphoserine +Q08471 268 Phosphoserine +P32333 93 Phosphoserine +P32333 677 Phosphoserine +P53163 34 N-linked +P32906 96 N-linked +P32906 155 N-linked +P32906 224 N-linked +Q12404 47 N-linked +Q12404 307 N-linked +P35728 221 Phosphoserine +P39016 662 Phosphoserine +P39016 834 Phosphoserine +P39016 838 Phosphoserine +P53045 96 Glycyl +P33748 288 Phosphoserine +P33748 304 Phosphoserine +P33748 451 Phosphoserine +P33748 582 Phosphoserine +P33748 633 Phosphoserine +P40029 58 Phosphoserine +P40850 358 Phosphoserine +P40850 362 Phosphoserine +P40850 371 Phosphoserine +P40850 4 Glycyl +P53604 1 N-acetylmethionine +P53604 102 Phosphoserine +P20676 2 N-acetylserine +P20676 54 Phosphoserine +P20676 161 Phosphoserine +P20676 381 Phosphothreonine +P20676 383 Phosphoserine +P20676 637 Phosphoserine +Q12454 2 Phosphothreonine +P31755 203 N-linked +P31755 281 N-linked +P31755 341 N-linked +P31755 393 N-linked +P38325 12 Phosphoserine +P38325 15 Phosphoserine +Q06593 374 N-linked +Q06593 860 N-linked +Q06144 9 Phosphoserine +Q06144 15 Phosphoserine +Q06144 18 Phosphothreonine +Q06144 22 Phosphoserine +Q06144 29 Phosphoserine +Q06144 51 Phosphoserine +P43558 160 Glycyl +P32336 388 Phosphothreonine +P32336 392 Phosphothreonine +P32336 417 Phosphoserine +P32336 419 Phosphoserine +P32336 357 Glycyl +P16387 313 Phosphoserine%3B +Q06810 285 Phosphoserine +Q06810 348 Phosphoserine +Q06810 172 N-linked +Q06810 185 N-linked +P54784 237 Phosphoserine +P07991 272 N6-(pyridoxal +P07991 390 Glycyl +P16451 73 N6-lipoyllysine +Q02630 886 Phosphoserine +P19262 114 N6-lipoyllysine +P19262 340 Phosphothreonine +P12695 75 N6-lipoyllysine +P54790 2 N-acetylserine +P05150 2 N-acetylserine +P52593 340 Phosphoserine +P52593 406 Glycyl +P21957 10 Phosphoserine +P54791 9 Phosphoserine +P38351 147 Phosphoserine +P38351 422 Phosphothreonine +Q12033 2 N-acetylserine +P37304 659 Phosphoserine +P37304 732 Phosphoserine +P37304 767 Phosphoserine +P36102 57 Phosphothreonine +P36102 252 Phosphoserine +P53298 70 Phosphoserine +P28273 930 Phosphoserine +P28273 1077 Phosphoserine +P40897 48 Phosphothreonine +P40897 50 Phosphothreonine +P40897 51 Phosphothreonine +P40897 46 N-linked +P40897 640 N-linked +P32833 60 Phosphothreonine +P32833 187 Phosphothreonine +P32833 188 Phosphoserine +P32567 110 Phosphoserine +P32567 114 Phosphoserine +P32567 168 Phosphoserine +P32567 511 Phosphoserine +P32567 602 Phosphoserine%3B +P32567 723 Phosphothreonine%3B +P32567 744 Phosphoserine%3B +P32567 748 Phosphoserine +P32567 773 Phosphoserine +P32567 774 Phosphoserine +P32567 810 Phosphoserine +P32567 814 Phosphoserine +P32567 816 Phosphothreonine +P32567 844 Phosphoserine +P32567 847 Phosphoserine +P38826 146 Phosphothreonine +Q05518 14 Phosphoserine +Q05518 45 Phosphoserine +Q05518 47 Phosphothreonine +Q05518 49 Phosphoserine +Q05518 64 Phosphoserine +Q05518 114 Phosphoserine +Q05518 121 Phosphoserine +Q05518 153 Phosphothreonine +Q05518 304 Phosphothreonine +Q05518 307 Phosphoserine +Q05518 135 Glycyl +Q05518 138 Glycyl +Q05518 292 Glycyl +Q05518 328 Glycyl +Q05518 445 Glycyl +P53179 521 Glycyl +P48565 409 Phosphoserine +P32521 241 Phosphothreonine +P32521 570 Phosphothreonine +P32521 747 Phosphoserine +P32521 757 Phosphoserine +P32521 993 Phosphothreonine +P32521 995 Phosphothreonine +P32521 1003 Phosphoserine +P32521 1180 Phosphoserine +P32521 1250 Phosphoserine +P32521 1253 Phosphoserine +P32521 1281 Phosphoserine +P32521 1321 Phosphothreonine +Q12451 2 N-acetylserine +Q12451 7 Phosphoserine +Q12451 422 Phosphoserine +Q12451 445 Phosphoserine +Q12451 451 Phosphoserine +Q12451 455 Phosphoserine +Q12451 458 Phosphoserine +Q12451 459 Phosphoserine +Q12451 486 Phosphoserine +Q12451 488 Phosphothreonine +Q12451 512 Phosphoserine +Q12451 515 Phosphoserine +Q12451 717 Phosphoserine +Q12451 783 Phosphothreonine +Q12451 787 Phosphoserine +Q12451 825 Phosphoserine +Q12451 1151 Phosphoserine +Q02201 16 Phosphoserine +P50946 2 N-acetylthreonine +P50946 24 Phosphoserine +P33767 60 N-linked +P33767 332 N-linked +P43611 354 Phosphotyrosine +P32263 246 Phosphothreonine +P32263 279 Phosphoserine +P32263 171 Glycyl +P41543 18 N-linked +P41543 99 N-linked +P41543 217 N-linked +P41543 336 N-linked +P41543 400 N-linked +Q08952 1 N-acetylmethionine +Q08952 178 Phosphoserine +P40091 230 Phosphoserine +P40219 102 Phosphoserine +Q03558 353 Phosphoserine +Q03558 379 Phosphoserine +P25644 2 N-acetylserine +P25644 456 Phosphoserine +P25644 457 Phosphoserine +P24867 39 Phosphothreonine%3B +P24867 43 Phosphoserine%3B +P24867 82 Glycyl +P24867 121 Glycyl +Q08966 32 Phosphoserine +P15873 127 Glycyl +P15873 164 Glycyl +P15873 164 Glycyl +P26263 2 N-acetylserine +P26263 223 Phosphoserine +P26263 266 Phosphothreonine +P26263 353 Phosphothreonine +P26263 522 Phosphothreonine +P26263 212 Glycyl +P26263 233 Glycyl +P26263 269 Glycyl +P26263 505 Glycyl +P29468 452 Phosphoserine +P29468 550 Phosphoserine +Q12515 2 N-acetylalanine +Q12515 36 Phosphoserine +Q12515 39 Phosphoserine +Q12515 47 Phosphoserine +Q12515 123 Phosphoserine +Q12515 138 Phosphoserine +Q12515 141 Phosphoserine +Q12515 147 Phosphoserine +Q12515 246 Phosphoserine +P40186 69 Phosphoserine +P17967 82 N-linked +P17967 117 N-linked +P17967 155 N-linked +P17967 174 N-linked +P17967 425 N-linked +P40530 148 Phosphohistidine%3B +P12383 21 Phosphoserine +P12383 930 Phosphoserine +P12383 942 Phosphoserine +P12383 948 Phosphoserine +P33302 22 Phosphoserine +P33302 49 Phosphothreonine +P33302 51 Phosphothreonine +P33302 54 Phosphoserine +P33302 58 Phosphoserine +P33302 61 Phosphoserine +P33302 837 Phosphoserine +P33302 840 Phosphoserine +P33302 841 Phosphoserine +P33302 849 Phosphoserine +P33302 850 Phosphoserine +P33302 854 Phosphoserine +P33302 734 N-linked +P33302 1447 N-linked +P33302 825 Glycyl +P53224 29 Phosphoserine +P53224 32 Phosphoserine +P53224 56 Phosphoserine +P35845 394 Phosphoserine +P35845 490 Phosphoserine +P35845 500 Phosphoserine +P35845 678 Phosphoserine +P35845 683 Phosphoserine +P35845 691 Phosphoserine +P35845 692 Phosphothreonine +P35845 694 Phosphothreonine +P35845 708 Phosphoserine +P35845 712 Phosphoserine +P38713 190 Phosphoserine +P38713 193 Phosphoserine +P38713 210 Phosphothreonine +P38713 323 Phosphothreonine +P38713 324 Phosphoserine +P38713 325 Phosphothreonine +P38713 352 Phosphothreonine +P38713 605 Phosphoserine +P38755 276 Glycyl +P08018 68 Phosphoserine +P08018 269 Phosphoserine +P08018 514 Phosphoserine +P08018 518 Phosphothreonine +P13259 16 Phosphoserine +P13259 59 Phosphothreonine +P13259 346 Phosphoserine +P13259 401 Phosphoserine%3B +Q99220 52 N-linked +Q99220 74 N-linked +Q99220 380 N-linked +P04147 2 N-acetylalanine +P04147 107 Omega-N-methylarginine +P04147 249 Phosphoserine +P04147 332 Phosphoserine +P04147 405 Phosphoserine +P04147 7 Glycyl +P04147 337 Glycyl +P25580 24 N-linked +P25580 85 N-linked +P25580 120 N-linked +P25580 212 N-linked +P25580 365 N-linked +P40038 61 Phosphoserine +P40038 281 Phosphoserine +P40038 312 Phosphoserine +P40038 317 Phosphothreonine +P40550 595 N-linked +P40550 1289 N-linked +P40550 1324 N-linked +P40550 1346 N-linked +Q04182 558 N-linked +Q04182 744 N-linked +P53756 48 N-linked +P53756 144 N-linked +P53756 205 N-linked +P53756 350 N-linked +P53756 697 N-linked +P53756 733 N-linked +P53756 958 N-linked +P53756 1320 N-linked +Q04264 1231 Phosphoserine +Q04264 1233 Phosphoserine +P36139 2 N-acetylserine +P53112 2 N-acetylserine +P53112 313 Phosphoserine +P48363 1 N-acetylmethionine +P38075 29 Glycyl +P47116 56 Phosphothreonine +P47116 59 Phosphoserine +P47116 80 Phosphoserine +P47116 623 Phosphoserine +P47116 632 Phosphoserine +P47116 694 Phosphoserine +P47116 700 Phosphothreonine +P47116 711 Phosphoserine +P47116 737 Phosphothreonine +P47116 752 Phosphoserine +P47116 755 Phosphoserine +P47116 778 Phosphoserine +P47116 781 Phosphoserine +P29461 258 Phosphoserine +P29461 430 Phosphoserine +P07244 455 Phosphoserine +P07244 458 Phosphoserine +P03962 2 N-acetylserine +P03962 93 Glycyl +P03962 209 Glycyl +P03962 253 Glycyl +P25339 205 Phosphothreonine +P25339 212 Phosphothreonine +P25339 252 Phosphothreonine +P25339 256 Phosphoserine +Q06991 100 N-linked +Q06991 209 N-linked +Q06991 260 Glycyl +P38972 2 N-acetylthreonine +P11154 734 N6-carboxylysine +P11154 1135 N6-biotinyllysine +P28272 46 Glycyl +Q12355 419 GPI-anchor +Q12355 57 N-linked +Q12355 76 N-linked +Q12355 83 N-linked +Q12355 86 N-linked +Q12355 196 N-linked +Q12355 210 N-linked +Q12355 228 N-linked +Q12355 235 N-linked +Q12355 242 N-linked +Q12355 263 N-linked +Q12355 268 N-linked +Q12355 280 N-linked +Q12355 292 N-linked +Q12355 305 N-linked +Q12355 329 N-linked +P39927 272 Phosphoserine +P27616 2 N-acetylserine +Q05911 196 Glycyl +P32641 652 Phosphoserine +P32641 654 Phosphoserine +Q00578 752 Phosphoserine +Q04231 2 N-acetylserine +Q04231 19 Glycyl +P22216 24 Phosphoserine +P22216 175 Phosphoserine +P22216 547 Phosphoserine +P22216 560 Phosphoserine +P22216 774 Phosphoserine +P22216 793 Phosphoserine +P06779 64 Phosphoserine +P06779 85 Phosphoserine +P32864 470 Phosphoserine +P25635 225 Phosphoserine +P25635 232 Phosphoserine +P25635 651 Phosphoserine +P25635 664 Phosphoserine +P25635 912 Phosphoserine +P25635 913 Phosphoserine +P34230 33 N-linked +P34230 39 N-linked +P34230 162 N-linked +P34230 230 N-linked +P34230 241 N-linked +P34230 267 N-linked +P34230 295 N-linked +P34230 560 N-linked +P34230 608 N-linked +P34230 620 N-linked +P34230 647 N-linked +P34230 836 N-linked +P32327 2 N-acetylserine +P32327 735 N6-carboxylysine +P32327 1136 N6-biotinyllysine +P13298 213 Phosphoserine +P13298 225 Phosphoserine +P06777 613 Phosphoserine +P06777 1071 Phosphoserine +P06777 1072 Phosphothreonine +P32628 94 Phosphothreonine +P32628 121 Phosphoserine +P32628 139 Phosphothreonine +P32628 49 Glycyl +P53037 1043 Pyruvic +P31374 10 Phosphoserine +P31374 192 Phosphoserine +P31374 202 Phosphoserine +P31374 255 Phosphoserine +P31374 286 Phosphoserine +P31374 327 Phosphoserine +P31374 926 Phosphoserine +P31374 1018 Phosphoserine +P31374 1023 Phosphoserine +P31374 1035 Phosphoserine +P31374 1055 Phosphoserine +P31374 1079 Phosphothreonine +Q01329 500 Phosphoserine +Q04373 31 Phosphoserine%3B +Q04373 34 Phosphoserine +Q04373 34 Phosphoserine%3B +Q04373 35 Phosphoserine +Q04373 35 Phosphoserine%3B +Q02256 196 Phosphoserine +P21304 52 Phosphoserine +P21304 131 Phosphoserine +P50896 31 Phosphoserine +P50896 34 Phosphoserine +P50896 36 Phosphoserine +P50896 237 Phosphoserine +P50896 334 Phosphothreonine +P50896 520 Phosphoserine +P34222 152 Glycyl +Q08647 2 N-acetylserine +P39006 463 Pyruvic +P25044 83 Phosphoserine%3B +P40048 75 Phosphothreonine +P40048 248 Phosphoserine +P40048 297 Phosphoserine +P40048 368 Phosphoserine +P40454 341 Phosphoserine +P32588 2 N-acetylserine +Q12221 72 Phosphoserine +Q12221 198 Phosphoserine +Q12221 872 Phosphoserine +Q12221 876 Phosphoserine +Q07807 83 Phosphothreonine +Q07807 207 Phosphoserine +Q07807 210 Phosphoserine +P21264 37 Phosphoserine +P41909 142 N-linked +P41909 281 N-linked +P41909 403 N-linked +P36166 43 Phosphoserine +P36166 63 Phosphoserine +P53335 230 Phosphoserine +P10622 2 N-acetylserine +P10622 96 Phosphoserine +P36159 824 Phosphoserine +P51862 2 N-acetylserine +P51862 76 Phosphoserine +P51862 193 Phosphoserine +P51862 223 Phosphoserine +P51862 566 Phosphoserine +P51862 628 Phosphoserine +Q01080 34 Phosphoserine +Q01080 151 Phosphoserine +P27999 40 Phosphoserine +Q02933 37 N-linked +Q02933 70 N-linked +Q02933 103 N-linked +Q02933 123 N-linked +P10964 889 Phosphoserine +P10964 1636 Phosphoserine +P07703 2 N-acetylserine +P07703 17 Phosphoserine +P16370 2 N-acetylserine +Q12250 2 N-acetylserine +Q06103 8 Phosphoserine +Q06103 77 Phosphoserine +P38061 40 Phosphoserine +P05319 16 Phosphothreonine +P05319 40 Phosphoserine +P05319 43 Phosphoserine +P05319 49 Phosphoserine +P05319 96 Phosphoserine +P05319 2 Glycyl +P05319 48 Glycyl +P02400 29 Phosphoserine +P02400 100 Phosphoserine +P02400 49 Glycyl +Q12495 78 Phosphothreonine +Q12495 94 Phosphoserine +Q12495 509 Phosphothreonine +Q03195 349 Phosphoserine +Q12224 120 Phosphoserine +Q12224 164 Phosphoserine +Q12224 374 Phosphoserine +Q12224 377 Phosphoserine +P36534 2 N-acetylserine +P43620 2 N-acetylserine +P0CX26 40 Phosphoserine +P0CX28 40 N6-methyllysine%3B +P0CX28 55 N6-methyllysine%3B +Q02326 2 N-acetylserine +Q02326 12 Phosphoserine +Q02326 128 Glycyl +P05317 68 Phosphoserine +P05317 302 Phosphoserine%3B +P05317 14 Glycyl +P05317 97 Glycyl +P05317 144 Glycyl +Q07915 172 Phosphoserine +P38330 132 Phosphoserine +P11745 360 Phosphoserine +P05747 52 Glycyl +P0CX27 40 N6-methyllysine%3B +P0CX27 55 N6-methyllysine%3B +P02406 96 Glycyl +P0CX85 13 Phosphoserine +P0CX85 50 Phosphoserine +P14126 24 Phosphoserine +P14126 103 Phosphothreonine +P14126 156 Phosphoserine +P14126 243 Pros-methylhistidine +P14126 297 Phosphoserine +P14126 39 Glycyl +P14126 136 Glycyl +P0CH09 76 Glycyl +P0CH09 93 Glycyl +P10664 2 N-acetylserine +Q12487 2 N-acetylserine +P0CX42 2 N-acetylserine +P0CX42 106 N6%2CN6-dimethyllysine%3B +P0CX42 110 N6%2CN6-dimethyllysine%3B +P04456 61 Glycyl +P05318 2 N-acetylserine +P05318 96 Phosphoserine +P0CH08 76 Glycyl +P0CH08 93 Glycyl +P0CX25 40 Phosphoserine +P26321 167 Phosphoserine +P26321 176 Phosphoserine +P26321 235 Phosphoserine +P26321 164 Glycyl +P05739 12 Phosphoserine +P05739 128 Glycyl +P38144 694 Phosphothreonine +P38144 846 Phosphoserine +Q08773 17 Phosphoserine +Q08773 19 Phosphoserine +Q08773 831 Phosphoserine +Q08773 1079 Phosphothreonine +Q08773 1082 Phosphoserine +Q03419 79 N-linked +Q03419 207 N-linked +P36224 91 Phosphoserine +P07170 2 N-acetylserine +P07170 3 N-acetylserine +Q12055 183 Phosphotyrosine +Q12055 188 Phosphoserine +Q12055 196 Phosphoserine +P06245 1 N-acetylmethionine +P06245 224 Phosphothreonine +Q04746 159 N-linked +Q04746 206 N-linked +Q04746 313 N-linked +Q04746 404 N-linked +P39962 517 S-palmitoyl +P39962 518 S-palmitoyl +P39962 519 S-palmitoyl +P39962 520 S-palmitoyl +P39962 522 S-palmitoyl +P39962 523 S-palmitoyl +P39962 524 S-palmitoyl +P27466 343 Phosphotyrosine +P27466 357 Phosphoserine +P27466 417 Phosphoserine +P27466 418 Phosphoserine +P27466 420 Phosphoserine +P27466 429 Phosphoserine +P34167 65 Phosphoserine +P34167 71 Phosphoserine +P38431 170 Phosphoserine +P38431 172 Phosphoserine +P38431 191 Phosphothreonine +P38431 228 Phosphoserine +P38431 317 Phosphothreonine +P38431 397 Phosphoserine +P53897 32 Phosphoserine +P53897 64 Phosphoserine +P50094 125 Phosphoserine +Q06704 308 Phosphoserine +Q06704 660 Phosphoserine +Q06704 827 Phosphoserine +Q06704 830 Phosphothreonine +P47031 265 Phosphoserine +P47031 268 Phosphoserine +P47031 378 Phosphoserine +P47031 380 Phosphothreonine +P47031 383 Phosphoserine +P47031 392 Phosphoserine +P32351 24 Phosphothreonine +P11986 368 Phosphoserine +P53115 65 Phosphoserine +P53115 115 Phosphoserine +P53115 133 Phosphoserine +P53115 610 Phosphoserine +P07278 3 Phosphoserine +P07278 4 Phosphoserine +P07278 9 Phosphoserine +P07278 68 Phosphoserine +P07278 70 Phosphoserine +P07278 74 Phosphoserine +P07278 77 Phosphoserine +P07278 79 Phosphoserine +P07278 81 Phosphoserine +P07278 83 Phosphoserine +P07278 84 Phosphoserine +P07278 129 Phosphothreonine +P07278 130 Phosphoserine +P07278 131 Phosphothreonine +P07278 144 Phosphothreonine +P07278 145 Phosphoserine%3B +P07278 147 Phosphoserine +P07278 150 Phosphothreonine +P07278 160 Phosphothreonine +P23292 2 N-acetylserine +P23292 455 Phosphoserine +P23292 545 S-palmitoyl +P23292 546 S-palmitoyl +P23292 465 Glycyl +P19158 635 Phosphothreonine +P30605 12 Phosphothreonine +P30605 26 Phosphoserine +P30605 31 Phosphoserine +P30605 35 Phosphoserine +P30605 37 Phosphoserine +P30605 46 Phosphoserine +P30605 371 N-linked +P30605 573 Glycyl +Q07959 45 N-linked +Q07959 123 N-linked +Q07959 153 N-linked +Q07959 256 N-linked +Q07959 319 N-linked +P53863 393 Phosphoserine +P53863 504 Phosphothreonine +P22517 316 Phosphothreonine%3B +P22517 353 Phosphotyrosine +P22517 354 Phosphoserine +P22517 367 Phosphoserine +P22517 371 Phosphoserine +P22517 387 Phosphoserine%3B +P22517 443 Phosphoserine +Q12494 150 Phosphoserine +Q12494 396 Phosphoserine +Q12494 469 Phosphoserine +Q12494 537 Phosphoserine +Q12494 539 Phosphoserine +Q12494 566 Phosphoserine +Q12494 583 Phosphoserine +Q12494 589 Phosphoserine +Q12494 646 Phosphoserine +Q12494 664 Phosphoserine +Q12494 670 Phosphoserine +Q06142 2 N-acetylserine +Q06142 836 Phosphoserine +P32337 2 N-acetylserine +P32337 830 Phosphothreonine +P53067 1 N-acetylmethionine +P47135 129 Phosphoserine +P47135 131 Phosphothreonine +P47135 160 Phosphoserine +P47135 168 Phosphoserine +P47135 913 Phosphoserine +Q02932 2 N-acetylalanine +P01094 1 N-acetylmethionine +P53877 388 Phosphoserine +P18963 497 Phosphoserine +P18963 915 Phosphoserine +P18963 1342 Phosphoserine +P18963 1753 Phosphoserine%3B +P18963 3004 Phosphoserine%3B +P47056 74 N-linked +P47056 104 N-linked +P00817 65 Phosphothreonine +P00817 251 Phosphothreonine +P00817 266 Phosphoserine +P00817 286 Phosphoserine +P00817 239 Glycyl +P00817 279 Glycyl +Q12280 264 Phosphothreonine +Q12280 268 Phosphoserine +Q12280 299 Phosphothreonine +P32488 119 Phosphoserine +Q07532 2 N-acetylserine +P33417 532 Phosphoserine +P0CT04 74 Phosphothreonine +P36115 180 Phosphoserine +Q12358 52 Phosphoserine +P05986 15 Phosphoserine +P05986 55 Phosphoserine +P11927 233 Phosphothreonine +P32526 496 Phosphoserine +P23291 522 Phosphoserine +P23291 523 Phosphoserine +P23291 527 Phosphoserine +P23291 537 S-palmitoyl +P23291 538 S-palmitoyl +P35844 370 Phosphothreonine +P35844 389 Phosphoserine +P13134 42 N-linked +P13134 163 N-linked +P13134 404 N-linked +P13134 480 N-linked +P38692 735 Phosphoserine +P38991 5 Phosphoserine%3B +P38991 76 Phosphoserine +P38991 260 Phosphothreonine%3B +P38250 638 Phosphoserine +P38250 701 Phosphothreonine +P38250 704 Phosphoserine +P38250 720 Phosphoserine +P38250 726 Phosphothreonine +P38250 729 Phosphoserine +P38250 730 Phosphotyrosine +P38250 757 Phosphoserine +P38250 793 Phosphoserine +P38250 844 Phosphoserine +P38250 847 Phosphoserine +P38250 850 Phosphothreonine +P25389 396 Phosphoserine +P25389 675 Phosphoserine +P25389 707 Phosphoserine +P25389 777 Phosphoserine +P25389 822 Phosphoserine +P25389 825 Phosphoserine +P25389 871 Phosphoserine +P17423 133 Glycyl +P13185 534 Phosphoserine +P13185 593 Phosphoserine +P13185 646 Phosphoserine +P13185 764 Phosphoserine +P13185 986 Phosphoserine +P06242 162 Phosphothreonine%3B +P24583 226 Phosphoserine +P24583 761 Phosphoserine +Q06505 15 Phosphothreonine +Q06505 23 Phosphoserine%3B +Q06505 40 Phosphoserine +Q06505 85 Phosphoserine +Q06505 86 Phosphothreonine +Q06505 89 Phosphoserine +Q03361 48 Phosphoserine +Q03361 51 Phosphoserine +Q03361 360 Phosphoserine +Q03361 510 Phosphoserine +Q03361 552 Phosphoserine +Q03361 577 Phosphoserine +Q03361 775 Phosphoserine +P00549 2 N-acetylserine +P00549 9 Phosphoserine +P00549 16 Phosphoserine +P00549 31 Phosphothreonine +P00549 70 Phosphoserine +P00549 184 Phosphothreonine +P00549 213 Phosphoserine +P00549 316 Phosphoserine +P00549 450 Phosphoserine +P00549 478 Phosphothreonine +P00549 204 Glycyl +P00549 255 Glycyl +P00549 446 Glycyl +P14681 183 Phosphothreonine +P14681 185 Phosphotyrosine +P50090 455 Phosphothreonine +P50090 509 Phosphoserine +P13186 22 Phosphoserine +P13186 146 Phosphoserine +P13186 549 Phosphoserine +P13186 609 Phosphoserine +P13186 888 Phosphoserine +Q01919 365 Phosphoserine +Q01919 388 Phosphoserine +Q01919 521 Phosphoserine +Q01919 748 Phosphoserine +P52489 24 Phosphoserine +P42846 177 Phosphoserine +P42846 184 Phosphoserine +P42846 185 Phosphoserine +P42846 486 Phosphoserine +P54070 82 N-linked +P54070 98 N-linked +Q06554 2 N-acetylserine +Q06554 810 Phosphoserine +P32361 840 Phosphoserine%3B +P32361 841 Phosphoserine%3B +P32361 111 N-linked +P32361 213 N-linked +P32361 298 N-linked +P32361 397 N-linked +P30606 394 N-linked +Q04934 59 Phosphoserine +Q04934 84 Phosphoserine +Q04934 85 Phosphoserine +Q04934 335 Phosphoserine +P36035 2 N-acetylserine +P36035 4 Phosphoserine +P36035 11 Phosphoserine +P36035 61 Phosphoserine +P36035 66 Phosphoserine +P36035 70 Phosphothreonine +P36035 584 Phosphoserine +P36035 603 Phosphoserine +P36035 606 Phosphoserine +P36035 9 Glycyl +P36035 338 Glycyl +P46997 229 Phosphoserine +P06244 2 N-acetylserine +Q07551 123 Phosphoserine +Q08979 47 Phosphoserine +Q04066 9 Phosphoserine +P38853 20 Phosphoserine +P38853 23 Phosphoserine +P38853 25 Phosphoserine +P38853 94 Phosphoserine +P38853 467 Phosphothreonine +P38853 477 Phosphothreonine +P38853 503 Phosphoserine +P38853 604 Phosphothreonine +P38853 613 Phosphoserine +P38853 626 Phosphothreonine +P38853 689 Phosphoserine +P38853 691 Phosphoserine +P38853 717 Phosphoserine +P38853 748 Phosphoserine +P38853 837 Phosphoserine +P38853 848 Phosphoserine +P38853 958 Phosphoserine +P38853 997 Phosphoserine +P38853 1003 Phosphoserine +P38853 1022 Phosphoserine +P40309 557 Phosphoserine +P40309 562 Glycyl +P25341 203 Phosphoserine +P40504 89 N-linked +P40504 144 N-linked +P09620 660 Phosphoserine +P09620 81 N-linked +P09620 459 N-linked +P09620 467 N-linked +P15454 2 N-acetylserine +P15454 149 Phosphoserine +P15454 157 Phosphotyrosine +P17260 288 GPI-anchor +P38691 416 Phosphoserine +P38691 419 Phosphoserine +P38691 501 Phosphothreonine +P38691 504 Phosphothreonine +P38691 526 Phosphothreonine +P38691 529 Phosphoserine +P38691 646 Phosphoserine +P38691 845 Phosphoserine +P38691 884 Phosphoserine +P38691 1005 Phosphothreonine +P38691 1014 Phosphoserine +P38800 66 Phosphothreonine +P38800 747 Phosphoserine +P20485 30 Phosphoserine%3B +P20485 48 Phosphoserine +P20485 51 Phosphoserine +P20485 54 Phosphothreonine +P20485 85 Phosphoserine%3B +P22023 115 N-linked +P22023 228 N-linked +P22023 293 N-linked +P22023 457 N-linked +P22023 519 N-linked +P22023 523 N-linked +P22023 644 N-linked +P22023 870 N-linked +P22023 1091 N-linked +P22023 1150 N-linked +P22023 1195 N-linked +P33550 65 N-linked +P33550 81 N-linked +P33550 92 N-linked +P33550 167 N-linked +P43560 110 Phosphothreonine +P43560 113 Phosphoserine +P43560 140 Phosphoserine +P43560 143 Phosphothreonine +P43560 149 Phosphoserine +P36004 19 Phosphoserine +P36004 232 Phosphoserine +P36004 238 Phosphoserine +P36004 241 Phosphoserine +P32350 562 Phosphothreonine +P32895 199 Phosphoserine +P32895 218 Phosphoserine +P32895 271 Phosphoserine +P32895 295 Phosphoserine +P40970 366 N6-(pyridoxal +P39002 2 N-acetylserine +P40079 2 N-acetylserine +P25587 180 Phosphothreonine +P25587 184 Phosphothreonine +P25587 241 Phosphoserine +Q02799 21 Phosphoserine +Q02799 30 Phosphoserine +Q02799 282 Phosphoserine +P53281 2 N-acetylserine +P53281 48 Phosphoserine +P53281 114 Phosphoserine +P53281 116 Phosphoserine +P53281 41 Glycyl +P53281 79 Glycyl +P53281 118 Glycyl +P53281 219 Glycyl +P42838 36 Phosphoserine +P42838 113 N-linked +P42838 240 N-linked +P42838 256 N-linked +P42838 279 N-linked +P42838 298 N-linked +P42838 332 N-linked +Q12265 119 Phosphotyrosine +Q12265 120 Phosphothreonine +Q12265 123 Phosphoserine +Q12265 127 Phosphothreonine +Q12265 183 Phosphoserine +Q12265 332 Phosphoserine +P27810 120 N-linked +Q92325 16 Glycyl +Q12446 334 Phosphothreonine +Q12446 337 Phosphoserine +Q12446 588 Phosphoserine +P07264 488 Phosphoserine +P07264 494 Phosphothreonine +P07264 495 Phosphoserine +P53966 86 N-linked +P32807 370 Phosphoserine +P32807 371 Phosphoserine +P32807 372 Phosphoserine +P25045 121 Phosphothreonine +Q06147 91 S-palmitoyl +Q06147 94 S-palmitoyl +P36016 128 N-linked +P36016 458 N-linked +P36016 474 N-linked +P36016 481 N-linked +P36016 489 N-linked +P36016 527 N-linked +P36016 844 N-linked +P40026 81 Phosphoserine +P40026 101 Phosphoserine +P27809 197 N-linked +P30624 189 Glycyl +P32486 81 Phosphoserine +P32486 116 Phosphoserine +P32486 133 Phosphoserine +P32486 134 Phosphoserine +P32486 136 Phosphoserine +P32486 139 Phosphoserine +P32486 374 N-linked +P32486 461 N-linked +P32486 538 N-linked +P32486 563 N-linked +P32486 691 N-linked +P33399 2 N-acetylserine +P33399 15 Phosphoserine +P33399 19 Phosphoserine +P33399 104 Omega-N-methylarginine +P33399 230 Phosphoserine +P33399 233 Phosphoserine +P33399 235 Phosphoserine +Q05979 252 N6-(pyridoxal +P28496 2 N-acetylserine +P28496 23 Phosphoserine +P28496 24 Phosphoserine +P28496 103 N-linked +P38703 23 Phosphoserine +P38703 24 Phosphoserine +P38703 103 N-linked +P38851 1205 N-linked +Q08001 343 Phosphothreonine +Q08001 591 Phosphoserine +Q08001 593 Phosphothreonine +Q08001 594 Phosphoserine +Q08001 597 Phosphoserine +Q04377 10 Phosphoserine +Q04377 11 Phosphoserine +Q04377 76 Phosphoserine +Q02786 81 GPI-anchor +P38439 105 Phosphoserine +P38439 132 Phosphoserine +P38439 188 Phosphoserine +P38439 358 Phosphoserine +P38439 372 Phosphoserine +Q12342 7 Phosphoserine +Q12342 463 Phosphoserine +Q12342 466 Phosphoserine +P47055 42 N-linked +P47055 62 N-linked +P47055 136 N-linked +P25579 393 Phosphoserine +P25579 398 Phosphoserine +P25579 516 Phosphoserine +P25579 552 Phosphoserine +P43586 24 Phosphoserine +P35688 1 N-acetylmethionine +P35688 562 Phosphoserine +P40495 98 Phosphoserine +Q04087 168 Phosphoserine +Q04087 230 Phosphoserine +P43603 227 Phosphoserine +P43603 298 Phosphothreonine +P43603 300 Phosphoserine +P43603 303 Phosphoserine +P43603 393 Phosphothreonine +P43603 397 Phosphoserine +P43603 402 Phosphoserine +P43603 416 Phosphoserine +Q12230 233 Phosphothreonine +P22134 110 Phosphoserine +Q12176 2 N-acetylserine +Q12176 62 Phosphoserine +Q12176 73 Phosphoserine +Q12176 80 Phosphoserine +Q12176 275 Phosphoserine +Q12176 708 Phosphotyrosine +Q12176 710 Phosphoserine +Q12176 874 Phosphoserine +Q12176 878 Phosphoserine +Q12176 977 Phosphoserine +Q12176 978 Phosphoserine +Q12176 1024 Phosphoserine +Q12246 111 Phosphoserine +Q12246 120 Phosphoserine +Q12246 154 Phosphoserine +Q12246 160 Phosphoserine +Q12246 451 Phosphoserine%3B +Q12246 454 Phosphoserine +Q12246 455 Phosphoserine%3B +Q12246 460 Phosphoserine +Q12246 43 S-palmitoyl +Q12246 46 S-palmitoyl +Q12246 148 Glycyl +Q12502 93 Phosphothreonine +Q12502 384 Phosphoserine +Q12502 619 Phosphothreonine +Q12502 808 Phosphoserine +Q12502 486 Glycyl +Q02783 202 N-linked +P32487 64 Phosphoserine +P32487 75 Phosphoserine +P32487 77 Phosphothreonine +P32487 79 Phosphoserine +P32487 87 Phosphoserine +P32487 90 Phosphothreonine +P32487 54 Glycyl +P38828 2 N-acetylserine +P53048 523 N-linked +Q01662 2 N-acetylserine +P38174 35 Phosphoserine +P34239 401 Phosphoserine +P07866 271 Phosphoserine +P07866 559 Phosphoserine +P07866 689 Phosphoserine +P07866 691 Phosphothreonine +P07866 808 Phosphoserine +P07866 810 Phosphoserine +P07866 1028 Phosphoserine +P07866 1109 Phosphoserine +Q07508 2 N-acetylserine +P35192 143 Phosphoserine +P47074 268 Phosphoserine +P41910 90 Phosphoserine +P41910 209 Phosphoserine +P41910 210 Phosphoserine +P41910 347 Phosphothreonine +Q07376 255 Phosphoserine +Q07376 60 N-linked +Q07376 131 N-linked +Q07376 194 N-linked +P36032 72 N-linked +Q08777 125 N-linked +Q08777 194 N-linked +Q08777 419 N-linked +Q06675 88 Phosphothreonine +P11746 2 N-acetylserine +P11746 2 Phosphoserine +P11746 144 Phosphoserine +P17505 177 Phosphoserine +P17505 199 Phosphothreonine +P53145 103 Phosphoserine +P34078 2 N-acetylserine +P34078 288 Phosphoserine +P34078 293 Phosphoserine +P34078 299 Phosphoserine +P34078 303 Phosphoserine +P40957 502 Phosphothreonine +P20484 2 N-acetylserine +P20484 376 Phosphoserine +P20484 380 Phosphoserine +P20484 382 Phosphothreonine +P38112 135 Phosphothreonine +P38112 138 Phosphoserine +P38112 678 Phosphoserine +P36007 53 N6-(pyridoxal +P22855 2 N-acetylserine +Q92328 49 Glycyl +P38295 114 Glycyl +P29469 14 Phosphoserine +P29469 16 Phosphoserine +P29469 23 Phosphoserine +P29469 164 Phosphoserine +P29469 170 Phosphoserine +P30665 52 Phosphoserine +P30665 56 Phosphoserine +P30665 69 Phosphoserine +P53091 78 Phosphoserine +P53091 249 Phosphoserine +P53091 372 Phosphoserine +P53091 766 Phosphothreonine +P38132 811 Phosphothreonine +P38132 819 Phosphoserine +P38132 838 Phosphoserine +Q12198 376 N6-(pyridoxal +Q99257 2 N-acetylserine +P34166 35 Cysteine +P34166 35 S-farnesyl +P40578 255 Phosphoserine +P40578 467 Phosphoserine +P43638 1 N-acetylmethionine +P43638 81 Phosphoserine +P43638 222 Phosphothreonine +P43638 309 Phosphoserine +P43638 311 Phosphoserine +P43638 354 Phosphoserine +P43638 357 Phosphoserine +P43638 577 Phosphothreonine +P43638 221 Glycyl +Q12019 1026 Phosphothreonine +Q12019 2971 Phosphoserine +Q12019 4353 Phosphoserine +Q12019 4388 Phosphothreonine +Q12019 4555 Phosphoserine +P34165 33 Cysteine +P34165 33 S-farnesyl +P40002 152 Phosphoserine +P32490 192 Phosphoserine +P53141 116 Glycyl +P38998 2 N-acetylalanine%3B +P07702 880 O-(pantetheine +P07702 541 Glycyl +P07702 1276 Glycyl +O14467 143 Phosphoserine +P19659 2 N-acetylserine +P19659 335 Phosphoserine +P19659 736 Phosphoserine +P19659 752 Phosphoserine +P19659 783 Phosphoserine +P19659 785 Phosphoserine +P19659 789 Phosphoserine +P19659 793 Phosphothreonine +P19659 831 Phosphoserine +P19659 1003 Phosphoserine +P19659 1008 Phosphoserine +P19659 1018 Phosphoserine +P19659 1034 Phosphoserine +Q02205 146 Phosphoserine +Q02205 149 Phosphoserine +Q02205 2 N-myristoyl +Q02205 7 S-palmitoyl +Q02205 8 S-palmitoyl +P33441 266 Phosphoserine +P35201 325 Phosphoserine +P27705 278 Phosphoserine +P27705 302 Phosphoserine +P27705 310 Phosphoserine +P27705 311 Phosphoserine +P27705 314 Phosphoserine +P27705 377 Phosphoserine +Q06820 42 Phosphoserine +Q02574 452 Phosphoserine +Q12321 155 Phosphoserine +Q12321 423 Phosphoserine +P32570 2 N-acetylserine +P43623 208 N6-(pyridoxal +Q04533 287 Phosphoserine +Q04533 451 N6-(pyridoxal +P36027 260 Phosphoserine +P36027 327 Phosphoserine +P36027 329 Phosphoserine +P36027 355 Phosphoserine +P36027 35 N-linked +P36027 211 N-linked +Q02455 2 N-acetylserine +Q02455 337 Phosphothreonine +Q02455 379 Phosphoserine +Q02455 1670 Phosphoserine +Q02455 1710 Phosphoserine +Q02455 1733 Phosphoserine +Q02455 1803 Phosphoserine +P32354 17 Phosphothreonine +P32354 18 Phosphoserine +P32354 453 Phosphoserine +P32354 454 Phosphoserine +P22133 6 Phosphothreonine +P53094 472 Phosphoserine +P53094 475 Phosphoserine +P53094 621 Phosphoserine +P53094 639 Phosphoserine +P53094 693 Phosphoserine +P53094 698 Phosphoserine +P53094 744 Phosphoserine +P53094 747 Phosphoserine +P53094 756 Phosphoserine +P53094 757 Phosphoserine +P53094 781 Phosphoserine +P53094 785 Phosphothreonine +P53094 787 Phosphoserine +P53094 900 Phosphoserine +P53094 904 Phosphoserine +P53094 930 Phosphothreonine +P53094 1187 Phosphoserine +P47025 376 Phosphoserine +P19263 2 N-acetylthreonine +P19263 7 Phosphoserine +P19263 1036 Phosphothreonine +P39014 67 Phosphoserine +P47164 443 N6-(pyridoxal +P19358 2 N-acetylserine +P36051 90 N-linked +P36051 138 N-linked +P36051 198 N-linked +P36051 202 N-linked +P36051 286 N-linked +P36051 312 N-linked +P21965 2 N-acetylserine +P21965 198 Phosphoserine +P21965 199 Phosphotyrosine +P21965 202 Phosphoserine +P24279 761 Phosphoserine +P24279 777 Phosphoserine +P24279 781 Phosphoserine +P24279 868 Phosphothreonine +Q12343 2 N-acetylserine +Q12343 237 Phosphothreonine%3B +Q12343 242 Phosphoserine +P40513 91 Phosphothreonine +Q12296 439 Phosphoserine +Q12296 447 Phosphoserine +Q12296 527 Phosphoserine +Q12296 603 Phosphoserine +Q12296 604 Phosphotyrosine +Q12296 607 Phosphothreonine +Q12296 614 Phosphoserine +P39678 110 Phosphoserine +P39678 325 Phosphothreonine +P39678 326 Phosphoserine +P39678 330 Phosphoserine +P39678 827 Phosphoserine +P23493 159 Phosphothreonine +P23493 177 Phosphoserine +P23493 224 Phosphoserine +P23493 227 Phosphoserine +P36060 278 Phosphoserine +P53885 160 Phosphoserine +P53885 216 Phosphothreonine +P53885 288 Phosphoserine +P53885 314 Glycyl +Q12124 6 Phosphoserine +Q12124 208 Phosphoserine%3B +P40260 442 Phosphoserine +P40260 445 Phosphoserine +P32389 416 Phosphoserine +P32389 564 Phosphoserine +Q08268 131 N-linked +Q08268 54 Glycyl +Q01846 670 Phosphoserine +Q01846 673 Phosphoserine +Q01846 692 Phosphoserine +P40356 1 N-acetylmethionine +P38782 225 Phosphoserine +P41948 4 N-linked +P38849 32 N-linked +P38849 60 N-linked +P38849 80 N-linked +P38849 89 N-linked +P38849 156 N-linked +P38849 171 N-linked +P38849 175 N-linked +P38849 202 N-linked +P38849 240 N-linked +P38849 259 N-linked +P38849 311 N-linked +P38849 362 N-linked +P38849 433 N-linked +P0CX81 30 Glycyl +P36006 357 Phosphoserine +P47018 273 Phosphoserine +P47018 436 Phosphoserine +P53176 3 Phosphothreonine +P36084 49 Phosphoserine +P39552 3 Phosphothreonine +P0CY08 1 N-acetylmethionine +P38335 85 Phosphoserine +P38335 263 Phosphothreonine +P38335 481 Phosphoserine +P38335 491 Phosphoserine +P38335 493 Phosphotyrosine +P46151 120 Phosphoserine +P46151 301 Phosphoserine +P46151 358 Phosphoserine +Q06489 2 N-acetylserine +Q06489 351 Phosphoserine +Q06106 220 Phosphoserine +Q06106 264 Phosphoserine +Q12117 289 Phosphoserine +Q12117 295 Phosphothreonine +Q12117 299 Phosphoserine +P50873 13 Phosphoserine +P35719 23 Phosphoserine +P35719 137 Glycyl +P50276 552 Phosphothreonine +P50276 573 Phosphoserine +P50276 28 Glycyl +P38994 207 Phosphoserine +P38994 222 Phosphothreonine +P38994 225 Phosphoserine +P38994 659 Phosphothreonine +P38994 661 Phosphoserine +Q02642 151 Phosphothreonine +P25588 144 Phosphoserine +P25588 409 Phosphoserine +P25588 411 Phosphoserine +P25588 434 Phosphoserine +P25588 605 Phosphoserine +P25588 607 Phosphoserine +P25588 609 Phosphothreonine +P25588 801 Phosphoserine +P25588 807 Phosphoserine +P25588 911 Phosphoserine +Q06815 335 Phosphoserine +Q06815 339 Phosphoserine +Q06815 342 Phosphoserine +Q06815 371 Phosphoserine +Q06815 380 Phosphoserine +Q06815 116 N-linked +Q06815 136 N-linked +Q06815 178 N-linked +Q06815 215 N-linked +P36157 157 Phosphoserine +P36157 292 Phosphoserine +P32334 1300 Phosphoserine +P32334 30 N-linked +P32334 859 N-linked +P32334 885 N-linked +P32334 945 N-linked +P32334 1049 N-linked +P32334 1088 N-linked +P32334 1175 N-linked +P38694 15 N-linked +P38694 565 N-linked +P38694 627 N-linked +P34232 125 Phosphothreonine +P48563 2 N-acetylalanine +P48563 564 Phosphoserine +P48563 567 Phosphoserine +P48563 571 Phosphoserine +Q05812 57 Phosphoserine +Q05812 64 Phosphoserine +Q05812 127 Phosphoserine +Q05812 151 Phosphoserine +Q05812 155 Phosphoserine +Q05812 363 Phosphoserine +Q05812 646 Phosphothreonine +Q05812 660 Phosphoserine +P53214 481 Phosphoserine +P53214 482 Phosphoserine +P29952 2 N-acetylserine +P29952 107 Phosphoserine +P10507 243 Phosphoserine +P21339 538 Phosphoserine +P21339 776 Phosphoserine +P21339 816 Phosphoserine +Q03104 237 Phosphothreonine +Q03104 243 Phosphoserine +P38590 22 Phosphoserine +P38590 98 Phosphoserine +P38590 151 Phosphoserine +P38590 178 Phosphothreonine +Q03834 102 Phosphoserine +Q03834 145 Phosphoserine +Q03834 150 Phosphoserine +Q03834 201 Phosphoserine +Q03834 451 Phosphothreonine +P33749 1 N-acetylmethionine +P33749 178 Phosphoserine +P33749 263 Phosphoserine +P33749 316 Phosphoserine +P33749 319 Phosphoserine +P33749 479 Phosphothreonine +P33749 558 Phosphoserine +P47047 34 Phosphothreonine +P47047 84 Phosphoserine +P47047 843 Phosphoserine +Q08750 285 N-linked +P19524 2 N-acetylserine +P19524 1097 Phosphothreonine +P19524 1121 Phosphoserine +P16603 666 Glycyl +Q06389 2 N-myristoyl +P0CX80 30 Glycyl +Q04439 357 Phosphoserine +Q04439 359 Phosphotyrosine +Q04439 777 Phosphoserine +Q04439 992 Phosphoserine +Q04439 1205 Phosphoserine +Q12387 2 N-acetylserine +P12945 2 N-acetylserine +P12945 674 Phosphoserine +P52919 251 Phosphoserine +P52919 260 Phosphoserine +Q12163 102 Phosphoserine +Q12163 196 Phosphoserine +Q12163 235 Phosphoserine +Q12374 29 Phosphoserine +Q02866 67 Phosphoserine +Q02866 163 Phosphoserine +Q02866 185 Phosphoserine +Q02866 245 Phosphoserine +P25293 20 Phosphothreonine +P25293 24 Phosphothreonine +P25293 27 Phosphoserine +P25293 53 Phosphothreonine +P25293 69 Phosphoserine +P25293 76 Phosphoserine +P25293 82 Phosphoserine +P25293 98 Phosphoserine +P25293 104 Phosphoserine +P25293 140 Phosphoserine +P25293 159 Phosphoserine%3B +P25293 177 Phosphoserine%3B +P25293 397 Phosphoserine%3B +P25293 50 Glycyl +P42939 1 N-acetylmethionine +P42939 94 Phosphoserine +Q03735 2 N-acetylserine +Q03735 464 Phosphoserine +Q03735 467 Phosphoserine +P53919 255 Phosphoserine +P30771 56 Phosphoserine +P30771 869 Phosphoserine +Q08229 138 Phosphoserine +Q08229 208 Phosphoserine +Q08229 403 Phosphothreonine +P38205 426 Phosphothreonine +P38205 431 Phosphoserine +P38205 667 Phosphoserine +P38996 86 Phosphothreonine +P38996 451 Phosphothreonine +P38879 2 N-acetylserine +P38879 93 Phosphoserine +Q08887 319 Phosphothreonine%3B +P36010 95 Phosphothreonine +P25374 299 N6-(pyridoxal +Q99271 568 Phosphoserine +Q99271 765 Phosphothreonine +Q99271 768 Phosphoserine +Q99271 774 Phosphoserine +P53914 1001 Phosphoserine +P53914 1007 Phosphoserine +P53914 1010 Phosphoserine +P40096 27 Phosphoserine +P40096 141 Phosphoserine +P32500 401 Phosphoserine +P32500 412 Phosphoserine +P40460 38 Phosphothreonine +P40460 248 Phosphothreonine +P32831 1 N-acetylmethionine +P32831 524 Phosphoserine +P39744 70 Phosphoserine +P39744 149 Phosphoserine +P39744 160 Phosphoserine +P39744 166 Phosphoserine +P39744 698 Phosphoserine +P39744 708 Phosphoserine +P25353 161 N-linked +P25353 204 N-linked +P25353 264 N-linked +P25353 296 N-linked +P25353 403 N-linked +P53718 145 Phosphoserine +Q08485 560 Phosphoserine +Q08485 572 Phosphoserine +P53898 90 Phosphoserine +Q12457 64 Phosphothreonine +P36059 6 Phosphoserine +P48234 529 Phosphoserine +P48234 550 Phosphoserine +P48234 555 Phosphoserine +Q07623 45 Phosphoserine +Q07623 160 Phosphoserine +P27476 353 Asymmetric +P27476 362 Asymmetric +P27476 366 Asymmetric +P27476 375 Asymmetric +P27476 379 Asymmetric +P27476 382 Asymmetric +Q08214 194 Glycyl +Q03210 62 Phosphoserine +Q04121 490 Phosphothreonine +Q04121 494 Phosphoserine +Q04121 498 Phosphothreonine +Q04121 499 Phosphoserine +Q04121 569 Phosphoserine +Q04121 420 N-linked +Q04121 515 N-linked +Q04121 550 N-linked +Q04121 563 N-linked +P32770 345 Phosphoserine +P32770 455 Phosphoserine +P32770 630 Phosphoserine +P37838 247 Phosphoserine +P37838 379 Phosphothreonine +Q12080 31 Phosphoserine +P22211 47 Phosphoserine%3B +P22211 85 Phosphoserine +P22211 90 Phosphoserine +P22211 100 Phosphoserine +P22211 111 Phosphoserine +P22211 116 Phosphoserine +P22211 125 Phosphoserine +P22211 137 Phosphoserine +P22211 141 Phosphoserine +P22211 257 Phosphoserine%3B +P22211 259 Phosphoserine +P22211 260 Phosphoserine +P22211 288 Phosphoserine +P22211 292 Phosphoserine +P22211 317 Phosphoserine +P22211 320 Phosphoserine +P22211 328 Phosphoserine +P22211 334 Phosphotyrosine +P22211 336 Phosphoserine +P22211 353 Phosphoserine +P22211 356 Phosphoserine +P22211 357 Phosphoserine%3B +P22211 385 Phosphoserine +P53935 266 Phosphoserine +Q12311 728 Phosphoserine +Q02629 763 Phosphoserine +Q02629 783 Phosphoserine +Q92317 135 Phosphoserine +Q92317 137 Phosphoserine +Q92317 142 Phosphoserine +P49954 34 Phosphothreonine +Q06178 91 Phosphoserine +Q06178 95 Phosphoserine +Q06178 96 Phosphoserine +Q06178 111 Phosphoserine +P46970 977 Phosphoserine +P53939 260 Phosphoserine +P53939 264 Phosphoserine +P53939 300 Phosphoserine +P53939 302 Phosphoserine +P34909 310 Phosphothreonine +P34909 312 Phosphoserine +P34909 326 Phosphothreonine +P34909 360 Phosphoserine +P34909 270 Glycyl +P32494 134 Phosphoserine +P32494 407 Phosphoserine +P32494 464 Phosphothreonine +Q6Q547 36 Phosphoserine +Q6Q547 28 Glycyl +Q01560 182 Phosphoserine +Q01560 224 Phosphoserine +Q12499 281 Glycyl +P39923 362 Phosphoserine +Q08972 443 Phosphoserine +Q08972 1191 Phosphothreonine +P0CE68 4 N-linked +Q03435 2 N-acetylserine +P53253 10 Glycyl +Q08208 70 Phosphoserine +Q08208 181 Phosphothreonine +Q08208 184 Phosphoserine +Q12460 321 Phosphoserine +P47035 60 Phosphoserine +P47035 166 Phosphoserine +P47035 231 Phosphoserine +P47035 252 Phosphoserine +P47035 437 Phosphoserine +P47035 439 Phosphoserine +P47035 447 Phosphoserine +P47035 452 Phosphoserine +P47035 497 Phosphoserine +P47035 676 Phosphothreonine +P47035 830 Phosphoserine +P47035 1042 Phosphothreonine +P47035 1056 Phosphoserine +P47035 1059 Phosphoserine +Q07896 395 Phosphoserine +Q03790 2 N-acetylalanine +Q03790 101 Phosphoserine +Q03790 297 Phosphoserine +Q03790 438 Phosphoserine +Q12493 222 Phosphoserine +P36003 178 Phosphoserine +P36003 179 Phosphoserine +P36003 405 Phosphoserine +P36003 426 Phosphoserine +P36003 737 Phosphoserine +P36003 739 Phosphotyrosine +Q02892 563 Phosphoserine +Q12514 306 Phosphothreonine +Q12514 377 Phosphoserine +Q12514 338 Glycyl +P38742 76 Phosphoserine +P38742 486 Phosphoserine +P38742 987 Phosphoserine +P32499 17 Phosphoserine +P32499 20 Phosphoserine +P32499 137 Phosphoserine +P32499 165 Phosphoserine +P32499 203 Phosphoserine +P32499 205 Phosphoserine +P32499 348 Phosphoserine +P32499 351 Phosphoserine +P32499 361 Phosphothreonine +P32499 581 Phosphoserine +P32499 590 Phosphothreonine +P49686 137 Phosphoserine +P49686 298 Phosphoserine +Q05166 458 Phosphoserine +Q05166 464 Phosphoserine +Q12066 3 Phosphoserine +Q12066 417 Phosphoserine +Q12066 474 Phosphoserine +P39720 155 Phosphoserine +P53949 181 Phosphoserine +P38837 39 Phosphoserine +P38837 76 Phosphoserine +Q12143 2 N-acetylserine +P14907 238 Phosphoserine +P14907 361 Phosphoserine +P14907 456 Phosphoserine +P14907 631 Phosphoserine +P35729 417 Phosphothreonine +P40064 1 N-acetylmethionine +P40064 1034 Phosphoserine +P40477 404 Phosphoserine +P40477 657 Phosphoserine +P40477 724 Phosphoserine +P40477 735 Phosphoserine +P40477 745 Phosphoserine +P40477 803 Phosphothreonine +P40477 805 Phosphoserine +P40477 819 Phosphoserine +P40477 889 Phosphoserine +P40477 940 Phosphoserine +P40010 337 Phosphoserine +Q00402 611 Phosphoserine +Q00402 675 Phosphoserine +Q00402 746 Phosphoserine +Q00402 881 Phosphoserine +Q00402 945 Phosphoserine +Q00402 1009 Phosphoserine +Q00402 1201 Phosphoserine +Q00402 1265 Phosphoserine +Q00402 1329 Phosphoserine +Q00402 2162 Phosphoserine +Q00402 2164 Phosphoserine +Q00402 2197 Phosphoserine +Q00402 2217 Phosphoserine +Q00402 2220 Phosphoserine +Q00402 2221 Phosphoserine +Q00402 2360 Phosphoserine +Q00402 2424 Phosphoserine +Q00402 2494 Phosphoserine +Q00402 2545 Phosphoserine +P39705 10 Phosphoserine +P39705 49 Phosphoserine +P39705 81 Phosphoserine +P39705 89 Phosphoserine +P39705 162 Phosphoserine +P39705 171 Phosphoserine +P39705 214 Phosphoserine +P39705 222 Phosphoserine +P39705 352 Phosphoserine +P39705 360 Phosphoserine +P39705 374 Phosphoserine +P39705 382 Phosphoserine +P39705 460 Phosphothreonine +P39705 480 Phosphoserine +P39705 483 Phosphoserine +P38881 156 Phosphoserine +P38881 199 Phosphoserine +P38881 285 Phosphoserine +P38881 298 Phosphoserine +P38302 139 Phosphoserine +P31378 194 Glycyl +P49687 273 Phosphoserine +P49687 403 Phosphoserine +P49687 404 Phosphoserine +P49687 414 Phosphoserine +P49687 667 Phosphoserine +P49687 679 Phosphoserine +P49687 689 Phosphoserine +P49687 751 Phosphothreonine +P38219 89 Phosphothreonine +P38219 116 Phosphoserine +P38219 119 Phosphoserine +P38219 98 Glycyl +P53204 85 Phosphoserine +P53204 89 Phosphoserine +P53204 90 Phosphoserine +P53883 2 N-acetylserine +P53883 2 Phosphoserine +P53883 105 Phosphothreonine +P53883 335 Phosphoserine +P25655 2102 Phosphothreonine +P06102 303 Phosphoserine +P06102 307 Phosphoserine +P06102 322 Phosphoserine +P06102 446 Phosphoserine +P06102 450 Phosphoserine +P06102 565 Phosphoserine +P06102 569 Phosphoserine +P06102 571 Phosphothreonine +P06102 657 Phosphoserine +P06102 535 Glycyl +P39997 62 N-linked +P39997 69 N-linked +P39997 112 N-linked +P39997 153 N-linked +P39997 441 N-linked +P53617 263 Phosphoserine +P53617 265 Phosphoserine +P53617 271 Phosphoserine +P40007 176 Phosphoserine +P40007 178 Phosphoserine +P40991 580 Phosphoserine +Q08287 234 Phosphoserine +Q08287 239 Phosphoserine +Q08287 268 Phosphoserine +Q08287 370 Phosphoserine +Q04958 300 Phosphoserine +Q04958 312 Phosphoserine +Q04958 632 Phosphoserine +Q04958 634 Phosphoserine +Q04958 653 Phosphoserine +Q04958 661 Phosphoserine +Q04958 670 Phosphoserine +Q04958 680 Phosphoserine +Q04958 739 Phosphoserine +Q04958 803 Phosphothreonine +P33331 2 N-acetylserine +P33331 53 Glycyl +P36118 40 Phosphoserine +P36118 153 Phosphoserine +P36118 197 Phosphoserine +P36161 2 N-acetylserine +P38181 1247 Phosphoserine +P53742 60 Phosphoserine +P53742 85 Phosphoserine +P53742 155 Phosphoserine +Q12200 123 N-linked +Q12200 145 N-linked +Q12200 178 N-linked +Q12200 314 N-linked +Q12200 401 N-linked +Q12200 513 N-linked +Q12200 900 N-linked +Q12200 940 N-linked +Q03125 163 Phosphoserine +P51533 754 N-linked +Q02785 2 N-acetylserine +Q02785 32 Phosphoserine +Q02785 52 Phosphoserine +Q02785 56 Phosphoserine +Q02785 1405 N-linked +Q02785 426 Glycyl +Q07418 62 Phosphoserine +Q07418 304 Phosphoserine +Q07418 339 Cysteine +Q07418 339 S-farnesyl +Q06169 2 N-acetylserine +Q06169 52 Phosphoserine +Q06169 420 Phosphoserine +Q06169 424 Phosphoserine +P07269 542 Phosphothreonine +P17442 956 Phosphoserine +P25360 162 N-linked +P25360 202 N-linked +P25360 274 N-linked +P25360 102 Glycyl +Q12057 141 Phosphothreonine +Q12057 91 N-linked +Q12057 132 N-linked +Q12057 276 N-linked +Q03407 294 Phosphoserine +Q03407 296 Phosphoserine +P39105 634 GPI-anchor +P39105 26 N-linked +P39105 33 N-linked +P39105 52 N-linked +P39105 78 N-linked +P39105 92 N-linked +P39105 123 N-linked +P39105 160 N-linked +P39105 170 N-linked +P39105 215 N-linked +P39105 277 N-linked +P39105 307 N-linked +P39105 345 N-linked +P39105 388 N-linked +P39105 459 N-linked +P39105 489 N-linked +P39105 513 N-linked +P39105 541 N-linked +P39105 565 N-linked +P39105 582 N-linked +Q03674 680 GPI-anchor +Q03674 47 N-linked +Q03674 80 N-linked +Q03674 94 N-linked +Q03674 125 N-linked +Q03674 162 N-linked +Q03674 181 N-linked +Q03674 193 N-linked +Q03674 217 N-linked +Q03674 279 N-linked +Q03674 309 N-linked +Q03674 365 N-linked +Q03674 390 N-linked +Q03674 491 N-linked +Q03674 515 N-linked +Q03674 524 N-linked +Q03674 543 N-linked +Q03674 567 N-linked +Q03674 584 N-linked +Q03674 598 N-linked +Q03674 630 N-linked +Q03674 634 N-linked +Q03674 642 N-linked +Q03674 648 N-linked +Q03674 652 N-linked +Q03674 658 N-linked +P27801 907 Phosphoserine +P40335 216 Phosphoserine +P53203 432 Phosphoserine +P53203 435 Phosphothreonine +P46988 2 N-acetylserine +P52553 2 N-acetylserine +P07270 100 Phosphoserine%3B +P07270 114 Phosphoserine%3B +P07270 128 Phosphoserine%3B +P07270 152 Phosphoserine%3B +P07270 204 Phosphoserine +P07270 223 Phosphoserine%3B +P07270 242 Phosphoserine +P07270 243 Phosphoserine +P20052 234 Phosphoserine%3B +P20052 267 Phosphoserine%3B +P06738 31 Phosphothreonine +P06738 333 Phosphoserine +P06738 751 N6-(pyridoxal +P40187 162 Phosphoserine +P40187 196 Phosphoserine +P40187 296 Phosphoserine +P40187 304 Phosphoserine +Q12252 115 N-linked +Q12252 132 N-linked +P53297 106 Phosphoserine +P53297 193 Phosphothreonine +P53297 215 Phosphoserine +P53297 436 Phosphoserine +P53297 344 Glycyl +P06169 2 N-acetylserine +P06169 223 Phosphoserine +P06169 266 Phosphothreonine +P06169 336 Phosphothreonine +P06169 353 Phosphothreonine +P06169 522 Phosphothreonine +P06169 526 Phosphoserine +P06169 212 Glycyl +P06169 233 Glycyl +P06169 269 Glycyl +P06169 332 Glycyl +P06169 484 Glycyl +P06169 505 Glycyl +P06169 520 Glycyl +P38848 361 N-linked +P35056 1 N-acetylmethionine +P35056 61 Phosphoserine +P35056 6 Glycyl +P35056 18 Glycyl +P35056 24 Glycyl +P53900 1 N-acetylmethionine +P53872 174 GPI-anchor +P53872 55 N-linked +P53872 64 N-linked +P53872 75 N-linked +P53872 84 N-linked +P53872 95 N-linked +P53872 104 N-linked +P53872 115 N-linked +P53872 124 N-linked +P53872 135 N-linked +P53872 144 N-linked +P53872 155 N-linked +P53896 72 N-linked +P53896 80 N-linked +P32854 2 Phosphoserine +P32854 23 Phosphoserine +Q02969 58 Phosphoserine +Q02969 63 Phosphoserine +Q02969 289 Phosphoserine +P53903 2 N-acetylserine +P53903 119 Phosphoserine +P07271 70 Phosphoserine +P07271 72 Phosphoserine +P07271 169 Phosphoserine +P07271 584 Phosphoserine +P14242 393 Phosphoserine +P14242 566 Phosphoserine +P47190 124 N-linked +P47190 324 N-linked +P47190 398 N-linked +P52867 33 N-linked +P52867 213 N-linked +P52867 380 N-linked +P52867 386 N-linked +P42934 2 N-acetylserine +P42934 156 N-linked +P42934 404 N-linked +P42934 481 N-linked +Q05788 2 N-acetylserine +Q05788 275 Phosphoserine +P47180 318 N-linked +P47180 330 N-linked +P37012 2 N-acetylserine +P37012 111 Phosphothreonine +P37012 117 Phosphothreonine +P37012 119 Phosphoserine +Q03262 158 Phosphoserine +P25297 302 Phosphothreonine +P25297 303 Phosphoserine +P25297 316 Phosphoserine +P25297 317 Phosphothreonine +P25297 321 Phosphoserine +P25297 577 Phosphoserine +P25297 579 Phosphoserine +P25297 581 Phosphoserine +P25297 6 Glycyl +P25297 298 Glycyl +P38264 157 Phosphoserine +P27514 295 Phosphoserine +P27514 311 Phosphoserine +P27514 312 Phosphoserine +Q03306 696 Phosphoserine +Q03306 753 Phosphoserine +Q03306 871 Phosphoserine +P05030 61 Phosphoserine +P05030 175 Phosphothreonine +P05030 911 Phosphoserine +P05030 912 Phosphothreonine +P05030 918 Phosphothreonine +P05030 252 Glycyl +P05030 555 Glycyl +P53261 288 Phosphoserine +P53261 308 Phosphothreonine +P16861 3 Phosphoserine +P16861 166 Phosphoserine +P16861 179 Phosphoserine +P16861 185 Phosphoserine +P16861 189 Phosphoserine +P16861 192 Phosphoserine +P16861 217 Phosphoserine +P16861 450 Phosphothreonine +P16861 89 Glycyl +P16861 625 Glycyl +P16862 152 Phosphothreonine +P16862 163 Phosphoserine +P16862 171 Phosphoserine +P16862 803 Phosphoserine +P00560 2 N-acetylserine +P00560 93 Phosphothreonine +P00560 110 Phosphoserine +P00560 130 Phosphoserine +P00560 154 Phosphoserine +P00560 172 Phosphoserine +P00560 203 Phosphothreonine +P00560 241 Phosphothreonine +P00560 298 Phosphothreonine +P00560 318 Phosphoserine +P00560 331 Phosphothreonine +P00560 392 Phosphothreonine +P00560 82 Glycyl +P00560 197 Glycyl +P00560 258 Glycyl +P00560 274 Glycyl +P00560 302 Glycyl +P33401 2 N-acetylserine +P33401 120 Phosphoserine +P38244 96 N-linked +P38244 121 N-linked +P38244 189 N-linked +P38244 217 N-linked +P38244 656 N-linked +P38244 768 N-linked +P38244 796 N-linked +P38244 811 N-linked +P38244 866 N-linked +P38244 937 N-linked +P39104 10 Phosphoserine +P39104 236 Phosphoserine +P39104 384 Phosphoserine +P39104 394 Phosphothreonine +P39104 396 Phosphoserine +P39104 592 Phosphoserine +P53252 14 Phosphothreonine +P53252 16 Phosphoserine +P53252 45 Phosphoserine +P53252 98 Phosphoserine +P53252 163 Phosphoserine +P53252 230 Phosphoserine +P53252 233 Phosphothreonine +P53252 299 Phosphoserine +P53252 29 Glycyl +Q12236 138 Phosphoserine +Q12236 619 Phosphoserine +Q12236 1009 Phosphoserine +Q04383 281 Phosphoserine +Q04383 295 Phosphoserine +Q04383 302 Phosphoserine +Q04383 384 Phosphoserine +P38197 2 N-acetylserine +P38197 49 N6-(pyridoxal +Q12412 259 N-linked +Q12445 270 Phosphoserine +Q12445 273 Phosphothreonine +Q12445 292 Phosphoserine +Q12445 294 Phosphoserine +P23287 2 N-acetylserine +P39966 376 Phosphothreonine +P39966 380 Phosphothreonine +P11491 123 Phosphoserine +P11491 268 N-linked +P11491 401 N-linked +Q04004 1 N-acetylmethionine +P32634 298 Phosphothreonine +P32634 838 Phosphoserine +P32634 1289 Phosphoserine +P32634 1307 Phosphoserine +P32634 1356 Phosphoserine +P32634 1664 Phosphoserine +Q06644 347 N-linked +Q99216 47 Phosphoserine +Q99216 51 Phosphothreonine +P38693 97 N-linked +P38693 162 N-linked +P38693 192 N-linked +P38693 250 N-linked +P38693 315 N-linked +P38693 356 N-linked +P38693 390 N-linked +P38693 439 N-linked +P38693 445 N-linked +P38693 461 N-linked +Q08108 659 GPI-anchor +Q08108 56 N-linked +Q08108 82 N-linked +Q08108 129 N-linked +Q08108 166 N-linked +Q08108 221 N-linked +Q08108 283 N-linked +Q08108 313 N-linked +Q08108 351 N-linked +Q08108 495 N-linked +Q08108 519 N-linked +Q08108 547 N-linked +Q08108 571 N-linked +Q08108 588 N-linked +Q08108 614 N-linked +P41812 524 Phosphothreonine +P00950 12 Phosphoserine +P00950 49 Phosphotyrosine +P00950 116 Phosphoserine +P00950 127 Phosphoserine +P00950 128 Phosphoserine +P00950 185 Phosphoserine +P00950 197 Phosphoserine +P00950 31 Glycyl +P00950 57 Glycyl +P00950 71 Glycyl +P00950 139 Glycyl +P00950 175 Glycyl +P00950 191 Glycyl +P33775 2 N-acetylserine +P33775 390 N-linked +P33775 513 N-linked +P33775 743 N-linked +P31382 2 N-acetylserine +P31382 32 Phosphoserine +P31382 38 Phosphoserine +P31382 39 Phosphoserine +P31382 131 N-linked +P31382 155 N-linked +P31382 403 N-linked +P46971 759 N-linked +P39685 45 Phosphoserine +P39685 60 Phosphoserine +P39685 280 N-linked +P23594 369 Leucine +P00635 97 N-linked +P00635 103 N-linked +P00635 162 N-linked +P00635 192 N-linked +P00635 250 N-linked +P00635 315 N-linked +P00635 356 N-linked +P00635 390 N-linked +P00635 439 N-linked +P00635 445 N-linked +P00635 456 N-linked +P00635 461 N-linked +P40035 1 N-acetylmethionine +P40473 152 Phosphoserine +P40473 168 Phosphoserine +P40473 314 Phosphoserine +P39008 1 N-acetylmethionine +P39008 97 Phosphothreonine%3B +P17157 18 Phosphotyrosine +P17157 289 Glycyl +P53191 46 Phosphoserine +P53191 53 Phosphoserine +P53191 56 Phosphothreonine +P53191 73 Phosphoserine +P53191 113 Phosphoserine +P53191 124 Phosphoserine +P53191 148 Phosphoserine +P53191 165 Phosphoserine +P53191 174 Phosphoserine +P53191 300 Phosphoserine +P53191 309 Phosphoserine +P53191 381 Phosphoserine +P07283 240 Phosphoserine +P38336 64 Phosphoserine +P38291 115 Phosphoserine +P23595 38 Phosphoserine +P23595 43 Phosphothreonine +P23595 377 Leucine +P34221 324 Phosphoserine +P34221 332 Phosphoserine +P35842 97 N-linked +P35842 162 N-linked +P35842 192 N-linked +P35842 250 N-linked +P35842 315 N-linked +P35842 356 N-linked +P35842 390 N-linked +P35842 439 N-linked +P35842 445 N-linked +P35842 461 N-linked +P53549 2 N-acetylserine +Q01939 2 N-acetylthreonine +P25375 73 Phosphoserine +Q04119 58 N-linked +Q04119 505 N-linked +Q04119 511 N-linked +Q04119 6 Glycyl +Q06449 2 N-acetylserine +Q06449 52 Phosphoserine +Q06449 55 Phosphoserine +Q06449 80 Glycyl +P34217 56 Phosphoserine +P34217 189 Phosphoserine +P34217 191 Phosphoserine +P34217 194 Phosphoserine +P34217 197 Phosphoserine +P34217 305 Phosphothreonine +P34217 393 Phosphoserine +P34217 466 Phosphoserine +P34217 541 Phosphoserine +P34217 636 Phosphoserine +P34217 638 Phosphoserine +P34217 640 Phosphoserine +P34217 653 Phosphoserine +P34217 655 Phosphoserine +Q12017 35 Phosphoserine +Q12017 62 Phosphoserine +Q12161 143 Phosphoserine +Q12161 191 Phosphoserine +Q12161 310 Phosphothreonine +Q12161 403 Phosphoserine +P08456 4 Phosphoserine +P08456 34 Phosphoserine +P08456 42 Phosphoserine +P08456 46 Phosphoserine +P08456 47 Phosphoserine +P08456 50 Phosphoserine +P28708 1 N-acetylmethionine +P28708 132 Phosphoserine +P23639 108 Glycyl +P50109 238 Phosphoserine +P50109 340 Phosphoserine +Q07949 9 S-palmitoyl +Q07949 10 S-palmitoyl +P32901 37 Phosphotyrosine +P32901 39 Phosphoserine +P32901 45 Phosphoserine +P32901 594 Phosphoserine +P38193 347 Phosphothreonine +P32857 480 Phosphoserine +P32857 483 Phosphothreonine +P32857 498 Phosphothreonine +P32857 132 N-linked +P23394 69 Phosphoserine +P22141 1 N-acetylmethionine +P22141 76 Phosphoserine +P33329 55 Phosphoserine +P33329 71 Phosphoserine +P33329 161 Phosphothreonine +P33329 203 Phosphoserine +P33329 224 Phosphoserine +P33329 271 Phosphothreonine +P33329 275 Phosphoserine +P33329 310 Phosphoserine +P33329 2 N-myristoyl +P40494 402 Phosphoserine +P40494 428 Phosphoserine +P40494 484 Phosphoserine +P40494 553 Phosphothreonine +P40494 556 Phosphoserine +P53835 135 N-linked +P53835 145 N-linked +P53835 188 N-linked +P53835 197 N-linked +P53835 231 N-linked +P53835 252 N-linked +P53835 272 N-linked +P53835 280 N-linked +P53835 490 N-linked +P53835 505 N-linked +P53835 512 N-linked +P53835 531 N-linked +P53835 573 N-linked +P53835 587 N-linked +P21243 2 N-acetylserine +P21243 237 Phosphoserine +P21243 232 Glycyl +P21242 2 N-acetylthreonine +P26570 49 Phosphoserine +P26570 171 Phosphothreonine +P26570 209 Phosphoserine +P26570 222 Phosphoserine +P26570 261 Phosphothreonine +P26570 265 Phosphoserine +P26570 690 Phosphoserine +P26570 2 N-myristoyl +P49960 19 Phosphoserine +P33203 576 Phosphothreonine +P40303 60 Phosphothreonine +P38624 1 N-acetylmethionine +P25451 31 Phosphoserine +P25451 70 Glycyl +Q08217 118 Phosphothreonine +P14747 31 Phosphothreonine +P14747 489 Phosphoserine +P14747 520 Phosphoserine +P24031 97 N-linked +P24031 103 N-linked +P24031 162 N-linked +P24031 192 N-linked +P24031 250 N-linked +P24031 315 N-linked +P24031 356 N-linked +P24031 390 N-linked +P24031 439 N-linked +P24031 445 N-linked +P24031 456 N-linked +P24031 461 N-linked +P52290 98 N-linked +P52290 163 N-linked +P52290 193 N-linked +P52290 202 N-linked +P52290 238 N-linked +P52290 251 N-linked +P52290 316 N-linked +P52290 357 N-linked +P52290 391 N-linked +P52290 457 N-linked +P52290 462 N-linked +P40347 57 Phosphoserine +P40476 129 Phosphoserine +P40476 279 Phosphoserine +P40476 282 Phosphoserine +P40476 288 Phosphoserine +P40476 314 Glycyl +P53131 8 Phosphoserine +P53131 9 Phosphoserine +P40327 2 N-myristoyl +P40327 234 Glycyl +P40327 255 Glycyl +P40327 290 Glycyl +P33297 2 N-acetylalanine +P33297 180 Phosphotyrosine +P33298 1 N-acetylmethionine +P33298 280 Glycyl +P09232 594 N-linked +P23638 100 Glycyl +P23638 199 Glycyl +P23638 231 Glycyl +P53633 1 N-acetylmethionine +P53633 18 Phosphoserine +P54885 2 N-acetylserine +P20095 2 N-acetylserine +P33299 164 Phosphoserine +P33299 231 Phosphoserine +P34227 53 Phosphoserine +P47033 853 GPI-anchor +P47033 101 N-linked +P47033 360 N-linked +P47033 488 N-linked +P47033 535 N-linked +P47033 547 N-linked +P47033 569 N-linked +P47033 625 N-linked +P32379 55 Phosphothreonine +P32379 56 Phosphoserine +P32379 251 Phosphoserine +P40302 14 Phosphoserine +P40302 191 Glycyl +Q07800 110 Phosphoserine +Q07800 9 S-palmitoyl +Q07800 10 S-palmitoyl +Q07800 154 Glycyl +P15380 72 N-linked +P15380 78 N-linked +P07259 2 N-acetylalanine +P07259 1857 Phosphoserine%3B +P07259 1853 Glycyl +P32849 2 N-acetylserine +P32849 20 Phosphoserine +P32849 23 Phosphoserine +P32849 129 Phosphoserine +P32849 130 Phosphoserine +P14737 26 Phosphoserine +P14737 56 Phosphoserine +P14737 205 Phosphoserine +P14737 218 Phosphothreonine +P14737 248 Phosphoserine +P14737 312 Phosphoserine +P14737 315 Phosphoserine +P14737 462 Phosphoserine +P14737 471 Phosphothreonine +P14737 474 Phosphothreonine +P14737 568 Phosphoserine +P14737 729 Phosphoserine +P20051 98 N6-carboxylysine +P07257 141 Phosphoserine +P07257 168 Phosphoserine +P40474 21 Phosphoserine +P40474 38 Phosphothreonine +P40474 40 Phosphoserine +P38227 436 Phosphoserine +P48581 383 Phosphoserine +P40352 30 Phosphoserine +P21827 135 Phosphoserine +P21827 136 Phosphoserine +P07276 118 Phosphoserine +P07276 367 Phosphoserine +P07276 583 Phosphoserine +Q12465 41 N-linked +Q12465 45 N-linked +Q12465 69 N-linked +Q12465 88 N-linked +Q12465 124 N-linked +Q12465 134 N-linked +Q12465 145 N-linked +Q12465 158 N-linked +Q12465 166 N-linked +Q12465 171 N-linked +Q12465 187 N-linked +Q12465 200 N-linked +Q12465 235 N-linked +Q12465 238 N-linked +Q12465 244 N-linked +Q12465 333 N-linked +Q12465 365 N-linked +Q12465 379 N-linked +Q12465 432 N-linked +Q12465 445 N-linked +Q12465 516 N-linked +Q12465 524 N-linked +Q12465 613 N-linked +Q12465 620 N-linked +Q12465 626 N-linked +Q12465 640 N-linked +Q12465 677 N-linked +Q12465 705 N-linked +Q12465 713 N-linked +Q12465 721 N-linked +Q12465 731 N-linked +Q12465 749 N-linked +Q12465 758 N-linked +Q12465 792 N-linked +Q12465 821 N-linked +Q12465 848 N-linked +Q12465 861 N-linked +Q12465 884 N-linked +Q12465 890 N-linked +Q12465 908 N-linked +Q12465 923 N-linked +Q12465 942 N-linked +Q12465 956 N-linked +Q12465 980 N-linked +Q12465 983 N-linked +Q12465 1011 N-linked +Q12465 1024 N-linked +Q12465 1031 N-linked +Q12465 1060 N-linked +Q12465 1071 N-linked +Q12465 1098 N-linked +Q12465 1126 N-linked +P31244 25 Phosphoserine +P31244 109 Phosphoserine +P11938 486 Phosphothreonine +P11938 731 Phosphoserine +P53295 364 Phosphoserine +Q08096 2 N-acetylserine +Q03446 161 Phosphoserine +Q03446 191 Phosphothreonine +P39531 409 Phosphoserine +P03872 1 N-acetylmethionine +P06780 2 N-acetylserine +P06780 206 Cysteine +P06780 206 S-geranylgeranyl +Q05672 198 Phosphoserine +Q05672 435 Phosphoserine +Q05672 439 Phosphoserine +Q05672 447 Phosphoserine +Q08273 15 Phosphoserine +P21538 355 Phosphoserine +P21538 807 Glycyl +P10862 155 Phosphothreonine +P10862 174 Phosphoserine +P10862 204 Glycyl +P12753 469 Phosphoserine +P12753 568 Phosphothreonine +Q08760 167 Phosphoserine +Q12044 104 Phosphoserine +Q12044 110 Phosphoserine +Q12044 132 Phosphothreonine +Q12044 152 Phosphoserine +Q12044 157 Phosphoserine +Q12044 160 Phosphoserine +Q12044 183 Phosphoserine +Q12044 187 Phosphoserine +Q12044 193 Phosphoserine +Q12044 201 Phosphoserine +Q12044 255 Phosphoserine +Q04779 1 N-acetylmethionine +Q04779 68 Phosphoserine +Q04779 683 Phosphoserine +P19541 102 Phosphoserine +P19541 231 Phosphothreonine +Q00816 2 N-acetylserine +Q00816 73 Phosphothreonine +Q00816 75 Phosphoserine +Q00816 242 Phosphoserine +Q00816 254 Phosphoserine +Q00816 311 Phosphoserine +Q00816 421 Phosphoserine +Q00816 480 Phosphotyrosine +Q00816 490 Phosphoserine +Q00816 570 Phosphoserine +Q00816 572 Phosphoserine +Q00816 576 Phosphoserine +Q00816 610 Phosphoserine +Q00816 614 Phosphoserine +Q00816 680 Phosphoserine +Q00816 896 Phosphothreonine +Q00816 898 Phosphoserine +Q00816 980 Phosphoserine +P38344 140 Phosphothreonine +P39729 2 N-acetylserine +P38623 46 Phosphoserine +P38623 50 Phosphoserine +P38623 187 Phosphoserine +P38623 350 Phosphothreonine +P38623 520 Phosphoserine +P36054 113 Phosphoserine +P36054 117 Phosphoserine +P36054 182 Phosphothreonine +P38086 649 Glycyl +P01119 306 Cysteine +P01119 305 S-palmitoyl +P01119 306 S-farnesyl +P01120 198 Phosphoserine +P01120 202 Phosphoserine +P01120 207 Phosphoserine +P01120 214 Phosphoserine +P01120 235 Phosphoserine +P01120 238 Phosphoserine +P01120 319 Cysteine +P01120 318 S-palmitoyl +P01120 319 S-farnesyl +P01120 131 Glycyl +P47104 1244 Phosphoserine +P47104 1248 Phosphoserine +Q12192 215 Phosphoserine +P40043 68 Glycyl +P32862 202 Phosphoserine +P32862 205 Phosphoserine +P32862 208 Phosphoserine +P32862 229 Phosphoserine +P32862 283 Phosphoserine +P32862 284 Phosphoserine +P32862 410 Phosphoserine +P32862 414 Phosphoserine +P32862 1130 Phosphoserine +P25378 1 N-acetylmethionine +P25378 206 Cysteine +P25378 206 S-farnesyl +Q12305 26 Phosphoserine +P53331 24 Phosphoserine +P38630 38 Phosphothreonine +P38630 40 Phosphoserine +P38630 63 Phosphothreonine +P38629 2 N-acetylserine +Q06624 9 Phosphoserine +Q06624 35 Glycyl +P43565 380 Phosphoserine +P43565 476 Phosphoserine +P43565 704 Phosphothreonine +P43565 709 Phosphoserine +P43565 733 Phosphoserine +P43565 736 Phosphoserine +P43565 737 Phosphoserine +P43565 747 Phosphothreonine +P43565 1044 Phosphoserine +P43565 1048 Phosphoserine +P43565 1064 Phosphoserine +P43565 1075 Phosphothreonine%3B +P43565 1421 Phosphoserine +P43565 1531 Phosphoserine +P43565 1538 Phosphoserine +P43565 1542 Phosphoserine +P43565 1565 Phosphoserine +P43565 1764 Phosphoserine +P39083 278 Phosphothreonine +P39083 291 Phosphoserine +P39083 532 Phosphothreonine +Q06108 136 Phosphoserine +Q06108 249 Phosphoserine +Q06108 252 Phosphoserine +Q06108 481 Phosphoserine +Q06108 537 Phosphoserine +Q06108 652 Phosphoserine +Q06108 765 Phosphoserine +Q06108 813 Phosphoserine +Q06108 817 Phosphothreonine +Q06108 857 Phosphothreonine +Q06108 866 Phosphoserine +Q06108 879 Phosphoserine +Q06108 918 Phosphoserine +Q06108 966 Phosphoserine +Q06108 969 Phosphoserine +Q06108 975 Phosphoserine +Q06108 1059 Phosphoserine +Q06108 1081 Phosphoserine +Q06108 1082 Phosphoserine +P16664 351 Phosphoserine +P16664 354 Phosphoserine +P16664 357 Phosphoserine +P16664 363 Phosphoserine +P16664 364 Phosphoserine +P16664 370 Phosphoserine +Q12300 136 N-linked +Q12300 385 N-linked +P21524 227 Phosphoserine +P21524 816 Phosphoserine +P21524 837 Phosphoserine +P21524 887 Phosphoserine +P21524 387 Glycyl +P21524 853 Glycyl +Q07844 42 Phosphoserine +P26785 2 N-acetylserine%3B +P26785 43 Phosphoserine +P26785 181 Phosphoserine +P26785 185 Phosphoserine +P26785 187 Phosphoserine +P26785 176 Glycyl +P46990 70 Phosphothreonine +P46990 46 Glycyl +P36105 2 N-acetylserine +P0CX49 50 N6%2CN6%2CN6-trimethyllysine +P0CX49 116 Glycyl +P0CX24 32 Phosphoserine +P0CX24 125 Glycyl +P0CX24 131 Glycyl +P0CX24 149 Glycyl +Q12672 32 Glycyl +P0CX41 2 N-acetylserine +P0CX41 106 N6%2CN6-dimethyllysine%3B +P0CX41 110 N6%2CN6-dimethyllysine%3B +P30775 287 N5-methylglutamine +P53893 431 Phosphoserine +P22336 2 N-acetylserine +P22336 178 Phosphoserine%3B +P26754 27 Phosphoserine +P26754 122 Phosphoserine +P40348 1 N-acetylmethionine +P06781 189 Cysteine +P06781 188 S-palmitoyl +P06781 189 S-geranylgeranyl +Q3E757 2 N-acetylserine +Q3E757 75 N6%2CN6%2CN6-trimethyllysine +P48743 173 Phosphoserine +Q06407 763 Phosphoserine +P38339 386 Phosphothreonine +P40160 346 Phosphoserine +P49723 1 N-acetylmethionine +P49723 169 Phosphoserine +P49723 332 Phosphoserine +P49723 334 Phosphothreonine +P49723 336 Phosphoserine +P49723 337 Glycyl +P38145 95 Phosphoserine +Q00245 228 Cysteine +Q00245 228 S-farnesyl +P53879 223 Phosphoserine +P53879 228 Phosphoserine +P53879 232 Phosphothreonine +P53879 244 Phosphothreonine +P53879 328 Cysteine +P53879 328 S-geranylgeranyl +P53879 276 Glycyl +P09938 15 Phosphoserine +P09938 24 Phosphoserine +P09938 41 Phosphoserine +P21672 227 Phosphoserine +P21672 806 Phosphoserine +P21672 827 Phosphoserine +P21672 868 Phosphoserine +P21672 387 Glycyl +P26784 2 N-acetylserine +P26784 44 Phosphoserine +P26784 188 Phosphoserine +P26784 177 Glycyl +Q99258 3 Phosphothreonine +P29539 97 Phosphoserine +P29539 1637 Phosphoserine +P29539 1795 Phosphoserine +P29539 1852 Phosphoserine +P38883 2 N-acetylserine +P0CX53 2 N%2CN-dimethylproline%3B +P0CX53 4 N6%2CN6%2CN6-trimethyllysine%3B +P0CX53 11 N6%2CN6%2CN6-trimethyllysine%3B +P0CX53 25 Phosphoserine +P0CX53 38 Phosphoserine +P0CX53 67 N5-methylarginine%3B +P0CX53 130 Glycyl +P0CX53 146 Glycyl +Q12690 144 Phosphothreonine +Q12690 152 Phosphothreonine +Q00246 264 Phosphoserine +Q00246 268 Phosphoserine +Q00246 276 Phosphoserine +Q00246 288 Cysteine +Q00246 288 S-farnesyl +P38615 199 Phosphotyrosine +Q12196 402 Phosphoserine%3B +Q12196 403 Phosphoserine%3B +Q12196 409 Phosphoserine%3B +Q12196 416 Phosphoserine%3B +Q12196 417 Phosphoserine%3B +Q12196 419 Phosphoserine%3B +P41805 143 Phosphoserine +P41805 205 Phosphoserine +P41805 40 Glycyl +P41805 101 Glycyl +P38741 525 Phosphoserine +P0C0W9 2 N-acetylserine +P0C0W9 75 N6%2CN6%2CN6-trimethyllysine +P0CX54 2 N%2CN-dimethylproline%3B +P0CX54 4 N6%2CN6%2CN6-trimethyllysine%3B +P0CX54 11 N6%2CN6%2CN6-trimethyllysine%3B +P0CX54 25 Phosphoserine +P0CX54 38 Phosphoserine +P0CX54 67 N5-methylarginine%3B +P0CX54 130 Glycyl +P0CX54 146 Glycyl +P0CX44 2 N-acetylserine +P0CX44 47 N6-methyllysine%3B +P0CX44 79 Phosphoserine +P0CX44 86 Phosphoserine +P0CX23 32 Phosphoserine +P0CX23 125 Glycyl +P0CX23 131 Glycyl +P0CX23 149 Glycyl +P24000 7 Phosphoserine +P0CX46 52 Phosphoserine +P0CX46 95 Phosphoserine +P0CX46 159 Phosphoserine +P0CX46 160 Phosphoserine +P0CX46 249 Phosphoserine +P0CX46 46 Glycyl +P0CX46 93 Glycyl +P0CX46 119 Glycyl +P0CX46 145 Glycyl +P0CX45 52 Phosphoserine +P0CX45 95 Phosphoserine +P0CX45 159 Phosphoserine +P0CX45 160 Phosphoserine +P0CX45 249 Phosphoserine +P0CX45 46 Glycyl +P0CX45 93 Glycyl +P0CX45 119 Glycyl +P0CX45 145 Glycyl +P14120 22 Glycyl +P14120 53 Glycyl +P14120 83 Glycyl +P05744 2 N-acetylalanine%3B +P05744 47 Glycyl +P0CX84 13 Phosphoserine +P0CX84 50 Phosphoserine +P05745 2 N-acetylthreonine +P49626 2 N-acetylserine +Q02753 32 Glycyl +P0CX82 30 Phosphoserine +P0CX82 37 Phosphoserine +P0CX82 91 Phosphoserine +P0CX82 21 Glycyl +P0CX82 53 Glycyl +P0CX82 60 Glycyl +P0CX82 146 Glycyl +P0CX82 186 Glycyl +P0CX83 30 Phosphoserine +P0CX83 37 Phosphoserine +P0CX83 91 Phosphoserine +P0CX83 21 Glycyl +P0CX83 53 Glycyl +P0CX83 60 Glycyl +P0CX83 146 Glycyl +P0CX83 186 Glycyl +P40212 144 Phosphothreonine +P40212 152 Phosphothreonine +P38754 2 N-acetylserine +P05740 70 Phosphothreonine +P05740 46 Glycyl +P0CX50 50 N6%2CN6%2CN6-trimethyllysine +P0CX50 116 Glycyl +P0CX43 2 N-acetylserine +P0CX43 47 N6-methyllysine%3B +P0CX43 79 Phosphoserine +P0CX43 86 Phosphoserine +P04449 7 Phosphoserine +P41056 2 N-acetylalanine%3B +P41056 47 Glycyl +P25367 143 Phosphoserine +P25367 5 Glycyl +P25367 84 Glycyl +P39956 399 Phosphothreonine +P39956 430 Phosphoserine +P39956 459 Phosphoserine +P39956 557 Phosphoserine +P39956 561 Phosphoserine +P39956 575 Phosphoserine +P39956 584 Phosphoserine +P39956 652 Phosphoserine +P39956 689 Phosphoserine +P40011 2 N-acetylserine +P35178 1 N-acetylmethionine +P35178 267 Phosphoserine +Q05022 47 Phosphothreonine +Q05022 187 Phosphoserine +Q05022 188 Phosphoserine +Q05022 1724 Phosphoserine +P25381 38 N-linked +P25381 64 N-linked +P25381 106 N-linked +P25381 121 N-linked +P25381 268 N-linked +P25381 356 N-linked +P25381 449 N-linked +P36121 61 Phosphothreonine +P32565 2 N-acetylserine +P32565 801 Phosphothreonine +P32565 932 Phosphothreonine +Q03305 181 Phosphoserine +Q03305 184 Phosphoserine +P22138 2 N-acetylserine +P22138 81 Phosphoserine +P22138 1156 Phosphoserine +P20435 24 Phosphoserine +P28000 15 Phosphothreonine +P28000 33 Phosphothreonine +P28000 134 Glycyl +P04050 1471 Phosphothreonine +P04050 695 Glycyl +P04050 1246 Glycyl +P04050 1350 Glycyl +P20433 1 N-acetylmethionine +P20433 91 Phosphothreonine +P20433 92 Phosphothreonine +P50106 121 Phosphoserine +P32349 27 Phosphothreonine +P32349 392 Phosphoserine +P32349 394 Phosphoserine +P17890 189 Phosphoserine +P35718 162 Phosphoserine +Q12377 2 N-acetylserine +Q06506 2 N-acetylserine +Q06506 50 Phosphoserine +P0CX48 2 N-acetylserine +P0CX48 15 Glycyl +P0CX48 46 Glycyl +P0CX48 56 Glycyl +P0CX48 57 Glycyl +P0CX48 79 Glycyl +P0CX48 96 Glycyl +P0CX48 105 Glycyl +P0CX48 133 Glycyl +P0CX48 141 Glycyl +P0CX48 148 Glycyl +P40693 2 N-acetylserine +P40693 14 Phosphoserine +P40693 120 Phosphothreonine +P40693 278 Phosphoserine +Q02805 138 Phosphoserine +Q02805 141 Phosphoserine +Q02805 436 Phosphoserine +Q02805 536 Phosphoserine +Q02805 720 Phosphoserine +Q02805 725 Phosphoserine +Q02805 401 Glycyl +P53046 1 N-acetylmethionine +P53046 154 Phosphoserine +P53046 155 Phosphoserine +P53046 180 Phosphothreonine +P53046 433 Phosphoserine +Q03691 103 N-linked +Q03691 107 N-linked +Q03691 139 N-linked +P47006 10 Phosphoserine +P47006 12 Phosphoserine +P47006 14 Phosphoserine +P47006 60 Phosphoserine +P46669 244 Phosphoserine +P46669 251 Phosphoserine +P46669 265 Phosphoserine +P46669 269 Phosphoserine +P46669 285 Phosphoserine +P20436 2 N-acetylserine +P20436 68 Phosphothreonine +P22139 59 Glycyl +P25441 137 Phosphoserine +P25441 138 Phosphoserine +P25441 178 Phosphoserine +P25441 182 Phosphoserine +P25441 224 Phosphoserine +P25441 228 Phosphothreonine +P25441 232 Phosphothreonine +Q12754 1059 Phosphoserine +Q12754 1067 Phosphoserine +Q06511 69 Phosphoserine +P25359 2 N-acetylalanine +P25359 26 Phosphoserine +Q01855 2 N-acetylserine +Q01855 24 Glycyl +Q01855 35 Glycyl +Q01855 64 Glycyl +P38701 2 N-acetylserine +P38701 6 Glycyl +P38701 8 Glycyl +P38701 21 Glycyl +P38701 32 Glycyl +P38701 101 Glycyl +P0C0V8 1 N-acetylmethionine +P08518 919 Phosphoserine +P32561 394 Phosphothreonine +P32561 408 Phosphoserine +P43588 1 N-acetylmethionine +P38764 16 Phosphoserine +P38764 19 Phosphoserine +P38764 24 Phosphothreonine +P38764 178 Phosphoserine +P38764 187 Phosphoserine +P38764 695 Phosphoserine +P40016 2 N-acetylalanine +P40016 454 Phosphoserine +P0CX47 2 N-acetylserine +P0CX47 15 Glycyl +P0CX47 46 Glycyl +P0CX47 56 Glycyl +P0CX47 57 Glycyl +P0CX47 79 Glycyl +P0CX47 96 Glycyl +P0CX47 105 Glycyl +P0CX47 133 Glycyl +P0CX47 141 Glycyl +P0CX47 148 Glycyl +P36160 73 Phosphoserine +O13563 2 N-acetylserine +O13563 133 Phosphoserine +O13563 135 Phosphoserine +O13563 140 Phosphoserine +Q08723 2 N-acetylserine +Q08723 314 Phosphoserine +Q08723 317 Phosphoserine +Q08723 319 Phosphoserine +Q08723 327 Phosphothreonine +Q12532 797 Phosphoserine +Q04031 113 Phosphoserine +Q04031 116 Phosphoserine +Q04031 122 Phosphoserine +P38961 62 Phosphoserine +P36080 2 N-acetylserine +P40470 197 Phosphoserine +P40470 202 Phosphoserine +P40470 203 Phosphoserine +Q3E792 2 N%2CN-dimethylproline%3B +P41058 25 Phosphoserine +P26783 2 N-acetylserine +P26783 27 Phosphothreonine +P26783 45 Glycyl +P26783 203 Glycyl +P48164 2 N-acetylserine +P48164 10 Phosphoserine +P48164 31 Phosphoserine +Q06488 612 Phosphotyrosine +Q06488 682 Phosphoserine +P43609 485 Phosphoserine +Q02950 327 Phosphoserine +Q03919 76 Glycyl +Q3E754 1 N-acetylmethionine +P0CX31 2 N-acetylserine +P0CX31 14 Phosphoserine +P0CX31 56 Phosphoserine +P0CX31 21 Glycyl +Q08932 1 N-acetylmethionine +Q08932 172 Phosphoserine +P38781 150 Phosphoserine +Q03201 193 Phosphoserine +Q05468 119 Phosphoserine +Q05468 158 Phosphothreonine +Q05468 160 Phosphoserine +Q04225 5 Phosphoserine +P38766 64 Phosphoserine +P38712 43 Phosphoserine +P38712 45 Phosphoserine +P38712 47 Phosphoserine +P48589 85 Glycyl +P48589 95 Glycyl +P48589 114 Glycyl +P23248 2 N-acetylalanine%3B +P23248 245 Phosphoserine +P23248 254 Phosphothreonine +P23248 248 Glycyl +P0CX52 2 N-acetylserine +P0CX52 34 Phosphoserine +P0CX52 61 Phosphoserine +P0CX52 70 Phosphothreonine +P0CX52 76 Phosphoserine +P0CX52 30 Glycyl +P0CX52 47 Glycyl +P0CX52 59 Glycyl +P0CX56 2 N-acetylserine +P0CX56 48 N6-methyllysine%3B +P0CX56 36 Glycyl +P0CX56 49 Glycyl +P0CX56 80 Glycyl +P0CX56 96 Glycyl +P0CX29 64 3%2C4-dihydroxyproline +P0CX29 56 Glycyl +P0CX32 2 N-acetylserine +P0CX32 14 Phosphoserine +P0CX32 56 Phosphoserine +P0CX32 21 Glycyl +P0C0T4 2 N%2CN-dimethylproline%3B +P0CX35 32 Phosphoserine +P0CX35 115 Phosphothreonine +P0CX35 247 Phosphoserine +P0CX35 62 Glycyl +P0CX35 134 Glycyl +P0CX35 161 Glycyl +P0CX35 168 Glycyl +P0CX35 174 Glycyl +P0CX35 179 Glycyl +P0CX35 211 Glycyl +P0CX35 233 Glycyl +P32832 86 Phosphoserine +Q03124 44 Phosphoserine +P38792 2 N-acetylserine +P38792 28 Phosphoserine +P38792 268 Phosphoserine +Q12149 138 Phosphoserine +Q12149 520 Phosphothreonine +Q12149 640 Phosphoserine +Q12149 645 Phosphoserine +P35997 40 S-methylcysteine +P0C0X0 1 N-acetylmethionine +P25443 2 N-acetylserine +P25443 11 Asymmetric +P25443 11 Omega-N-methylarginine%3B +P25443 33 Glycyl +P0CX34 16 Phosphoserine +P0CX34 48 Phosphothreonine +Q05942 83 Phosphoserine +Q05942 88 Phosphothreonine +Q05942 99 Phosphoserine +P53236 670 Phosphoserine +Q02206 199 Phosphoserine +Q02206 545 Phosphoserine +P33442 2 N-acetylalanine%3B +P33442 245 Phosphothreonine +P33442 254 Phosphothreonine +P33442 248 Glycyl +P0CX37 163 Phosphothreonine +P0CX37 116 Glycyl +P0CX37 131 Glycyl +P0CX37 149 Glycyl +P0CX37 214 Glycyl +P0CX40 62 Phosphothreonine +P0CX40 66 Phosphoserine +P0CX40 69 Phosphoserine +P0CX40 73 Phosphoserine +P0CX40 86 Phosphoserine +P0CX40 107 Phosphothreonine +P0CX40 154 Phosphoserine +P0CX40 155 Phosphoserine +P0CX40 158 Phosphoserine +P0CX40 161 Phosphoserine +Q08417 3 N-linked +Q08417 6 N-linked +P46974 231 Phosphoserine +P46974 322 Phosphoserine +P46974 544 Phosphoserine +P46974 632 Phosphoserine +Q03516 949 Phosphoserine +P32905 2 N-acetylserine +P40161 2 N-acetylserine +P40161 408 Phosphoserine +P40161 411 Phosphoserine +P40161 450 Phosphoserine +P53064 17 Phosphoserine +P53064 69 Phosphotyrosine +P53064 71 Phosphoserine +P53064 477 Phosphoserine +P0CX30 64 3%2C4-dihydroxyproline +P0CX30 56 Glycyl +P41057 25 Phosphoserine +P05750 44 Phosphothreonine +P05750 70 Phosphothreonine +P05750 97 Phosphoserine +P05750 129 Phosphoserine +P05750 146 Omega-N-methylarginine%3B +P05750 221 Phosphoserine +P05750 231 Phosphothreonine +P05750 106 Glycyl +P05750 132 Glycyl +P05750 141 Glycyl +P05750 151 Glycyl +P05750 200 Glycyl +P05750 212 Glycyl +O13516 184 Phosphoserine +O13516 180 Glycyl +Q12481 14 Phosphoserine +Q12481 41 Phosphoserine +Q12481 42 Phosphoserine +P05756 32 Phosphoserine +P05756 39 Glycyl +P05756 43 Glycyl +P06367 2 N-acetylserine +P05759 122 Phosphoserine +P05759 76 Glycyl +P0CX51 2 N-acetylserine +P0CX51 34 Phosphoserine +P0CX51 61 Phosphoserine +P0CX51 70 Phosphothreonine +P0CX51 76 Phosphoserine +P0CX51 30 Glycyl +P0CX51 47 Glycyl +P0CX51 59 Glycyl +P0CX55 2 N-acetylserine +P0CX55 48 N6-methyllysine%3B +P0CX55 36 Glycyl +P0CX55 49 Glycyl +P0CX55 80 Glycyl +P0CX55 96 Glycyl +Q3E7X9 1 N-acetylmethionine +P0CX33 16 Phosphoserine +P0CX33 48 Phosphothreonine +P0CX36 32 Phosphoserine +P0CX36 115 Phosphothreonine +P0CX36 247 Phosphoserine +P0CX36 62 Glycyl +P0CX36 134 Glycyl +P0CX36 161 Glycyl +P0CX36 168 Glycyl +P0CX36 174 Glycyl +P0CX36 179 Glycyl +P0CX36 211 Glycyl +P0CX36 233 Glycyl +P0CX38 163 Phosphothreonine +P0CX38 116 Glycyl +P0CX38 131 Glycyl +P0CX38 149 Glycyl +P0CX38 214 Glycyl +P0CX39 62 Phosphothreonine +P0CX39 66 Phosphoserine +P0CX39 69 Phosphoserine +P0CX39 73 Phosphoserine +P0CX39 86 Phosphoserine +P0CX39 107 Phosphothreonine +P0CX39 154 Phosphoserine +P0CX39 155 Phosphoserine +P0CX39 158 Phosphoserine +P0CX39 161 Phosphoserine +P05755 184 Phosphoserine +P05755 180 Glycyl +Q06639 95 Phosphoserine +Q06639 236 Phosphoserine +P38165 81 Phosphoserine +P38165 123 Phosphoserine +P38165 142 Phosphoserine +P38165 150 Phosphothreonine +P38165 227 Phosphoserine +P38165 236 Phosphoserine +P38165 241 Phosphoserine +P38165 269 Phosphoserine +Q12443 278 Phosphoserine +Q12443 137 N-linked +P26786 2 N-acetylserine +P26786 124 Glycyl +P38850 304 Phosphoserine +P38850 532 Phosphothreonine +P38850 591 Phosphoserine +P38850 593 Phosphoserine +P38850 720 Phosphoserine +P38850 800 Phosphoserine +P38850 806 Phosphoserine +Q08281 1036 Phosphoserine +Q08281 1080 Phosphoserine +Q08281 1087 Phosphoserine +Q08281 1089 Phosphoserine +Q08281 1123 Phosphoserine +Q08281 1133 Phosphoserine +P53330 77 Phosphoserine +P53330 122 Phosphoserine +P53850 23 Phosphoserine +Q04947 186 Phosphothreonine +Q04947 219 Phosphothreonine +Q04947 232 Phosphoserine +P20606 155 Phosphothreonine +P20606 157 Phosphoserine +P20606 133 Glycyl +P28707 2 N-acetylserine +P06105 50 Phosphothreonine +P06105 54 Phosphoserine +P06105 63 Phosphoserine +P06105 85 Phosphoserine +P06105 87 Phosphoserine +P06105 89 Phosphoserine +P06105 630 Phosphoserine +P06105 1112 Phosphoserine +P40541 28 Phosphoserine +P40541 628 Phosphoserine +P11792 570 Phosphothreonine%3B +P11792 711 Phosphoserine%3B +P11792 723 Phosphothreonine%3B +P11792 726 Phosphoserine%3B +P11792 737 Phosphothreonine%3B +P11792 758 Phosphoserine%3B +P11792 765 Phosphoserine%3B +P32607 50 Phosphoserine +P32607 52 Phosphoserine +P32607 60 Phosphothreonine +Q03940 2 N-acetylvaline +Q12158 161 Phosphoserine +Q12158 175 Phosphoserine%3B +Q12158 210 N6-acetyllysine%3B +Q12158 263 Phosphoserine%3B +Q12158 307 Phosphoserine +Q12158 354 Phosphothreonine +P34758 564 Phosphoserine +P43612 58 Phosphoserine +P43612 255 Phosphoserine +P43612 613 Phosphothreonine +P43612 618 Phosphothreonine +P17121 37 Phosphoserine +P17121 46 Phosphoserine +P17121 435 Phosphoserine +P17121 491 Phosphoserine +P17121 632 Phosphoserine +Q12136 12 Phosphoserine +Q12136 314 Phosphoserine +Q12136 316 Phosphoserine +Q12136 336 Phosphoserine +Q12136 339 Phosphoserine +Q12136 477 Phosphoserine +Q04002 43 Phosphoserine%3B +Q04002 67 Phosphothreonine +Q04002 74 Phosphoserine%3B +Q04002 127 Phosphoserine +Q04002 157 Phosphoserine +Q04002 162 Phosphoserine%3B +Q04002 163 Phosphoserine +Q04002 231 Phosphothreonine +Q04002 236 Phosphothreonine +Q04002 305 Phosphoserine +Q04002 320 Phosphoserine +Q04002 360 Phosphothreonine%3B +Q04002 753 Phosphoserine +Q04002 1179 Phosphoserine%3B +Q04002 1182 Phosphoserine +Q04002 1183 Phosphoserine%3B +Q04002 1185 Phosphoserine +P45978 2 N-acetylserine +Q04951 279 N-linked +P13856 269 Cysteine +P13856 269 S-geranylgeranyl +P46654 2 N-acetylserine +Q12100 58 Phosphothreonine +Q12100 60 Phosphoserine +Q12100 216 Phosphoserine +Q12100 334 Glycyl +P53289 172 Phosphoserine +P53289 192 Phosphoserine +P53289 214 Phosphoserine +P53289 238 Phosphoserine +Q12242 56 Phosphoserine +P39743 2 N-acetylserine +P39743 299 Phosphoserine%3B +P39743 321 Phosphoserine%3B +P39743 379 Phosphoserine%3B +P39743 242 Glycyl +P39743 481 Glycyl +P40856 20 Glycyl +P38352 16 Phosphoserine +P38352 266 Phosphoserine +P20840 627 GPI-anchor +P20840 79 N-linked +P20840 109 N-linked +P20840 135 N-linked +P20840 248 N-linked +P20840 282 O-linked +P20840 289 O-linked +P20840 299 O-linked +P20840 303 O-linked +P20840 306 N-linked +P20840 307 O-linked +P20840 308 O-linked +P20840 311 O-linked +P20840 314 O-linked +P20840 315 O-linked +P20840 316 O-linked +P20840 329 O-linked +P20840 331 O-linked +P20840 334 O-linked +P20840 335 O-linked +P20840 338 O-linked +P20840 339 O-linked +P20840 340 O-linked +P20840 341 O-linked +P20840 342 O-linked +P20840 345 O-linked +P20840 346 O-linked +P20840 349 O-linked +P20840 350 O-linked +P20840 364 N-linked +P20840 402 N-linked +P20840 460 N-linked +P20840 485 N-linked +P20840 501 N-linked +P20840 614 N-linked +P39954 2 N-acetylserine +P39954 393 Phosphothreonine +P39954 21 Glycyl +P39954 413 Glycyl +Q08985 138 Phosphothreonine +Q08873 2 N-acetylserine +Q08873 11 Phosphoserine +P40075 2 N-acetylserine +P40075 106 Phosphoserine +P40357 79 Phosphoserine +P40357 92 Phosphoserine +P40357 186 Phosphoserine +P40357 190 Phosphoserine +P40357 213 Phosphoserine +P40357 271 Phosphoserine +P40357 273 Phosphoserine +P40357 315 Phosphoserine +P40357 355 Phosphothreonine +P40357 359 Phosphoserine +Q01589 318 GPI-anchor +Q01589 22 N-linked +Q01589 56 N-linked +Q01589 78 N-linked +Q01589 92 N-linked +Q01589 114 N-linked +Q01589 136 N-linked +Q01589 152 N-linked +P34228 8 Phosphoserine +P34228 263 Phosphoserine +P34228 806 Phosphoserine +P36123 774 Phosphoserine +P36123 857 Phosphoserine +P36123 862 Phosphoserine +P36123 892 Phosphoserine +P36123 990 Phosphothreonine +P36123 991 Phosphoserine +P32368 246 Glycyl +P32368 358 Glycyl +P46674 568 Phosphoserine +P46674 748 N6-acetyllysine +P46674 866 Phosphoserine +P43589 1 N-acetylmethionine +Q08986 10 Phosphoserine +Q08986 27 Phosphoserine +Q08986 44 Phosphoserine +Q08986 184 N-linked +Q08986 243 N-linked +P53324 2 N-acetylalanine +P53324 85 N-linked +P53324 283 N-linked +P53324 401 N-linked +P38814 72 Phosphoserine +P38814 201 Phosphoserine +P38814 459 Phosphoserine +P38814 517 Phosphoserine +P38814 520 Phosphoserine +P42223 82 Phosphoserine +P42223 83 Phosphoserine +P42223 450 Phosphoserine +P42223 532 Phosphoserine +P47052 84 Tele-8alpha-FAD +P36047 56 Phosphoserine +Q06245 142 Phosphoserine +Q06245 485 Phosphoserine +Q06245 507 Phosphoserine +P48415 28 Phosphoserine +P48415 73 Phosphoserine +P48415 144 Phosphoserine +P48415 313 Phosphoserine +P48415 472 Phosphoserine +P48415 483 Phosphoserine +P48415 595 Phosphothreonine +P48415 607 Phosphoserine +P48415 660 Phosphoserine +P48415 663 Phosphoserine +P48415 665 Phosphoserine +P48415 674 Phosphoserine +P48415 678 Phosphoserine +P48415 681 Phosphoserine +P48415 701 Phosphoserine +P48415 704 Phosphoserine +P48415 706 Phosphoserine +P48415 759 Phosphoserine +P48415 762 Phosphoserine +P48415 765 Phosphoserine +P48415 768 Phosphoserine +P48415 843 Phosphoserine +P48415 1511 Phosphoserine +P48415 1515 Phosphoserine +P48415 1578 Phosphoserine +P48415 1602 Phosphoserine +P48415 1603 Phosphoserine +P48415 1611 Phosphoserine +P48415 1617 Phosphoserine +P48415 1778 Phosphoserine +P48415 1875 Phosphoserine +P48415 1973 Phosphoserine +P48415 1986 Phosphoserine +P48415 1992 Phosphoserine +P48415 2049 Phosphothreonine +P48415 2130 Phosphoserine +P18759 226 Phosphoserine +P15303 1 N-acetylmethionine +P17065 1 N-acetylmethionine +P17065 168 Phosphothreonine +P17065 171 Phosphoserine +P17065 515 Phosphoserine +P38968 349 Phosphoserine +P38968 836 Phosphoserine +P38968 974 Phosphoserine +P38968 977 Phosphoserine +P38968 980 Phosphoserine +P38968 988 Phosphoserine +P38968 992 Phosphoserine +P38968 999 Phosphoserine +P38968 1050 Phosphothreonine +P38968 1053 Phosphoserine +P21825 2 N-acetylserine +P33754 5 N-linked +P33754 12 N-linked +Q05567 380 N6-(pyridoxal +Q07657 2 N-acetylserine +Q07657 400 Phosphotyrosine +Q07657 408 Phosphoserine +Q07657 416 Phosphoserine +Q07657 447 Phosphoserine +Q07657 460 Phosphoserine +Q07657 519 Phosphoserine +Q07657 520 Phosphoserine +Q07657 522 Phosphoserine +Q07657 525 Phosphoserine +Q07657 539 Phosphothreonine +Q07657 545 Phosphoserine +Q07657 548 Phosphoserine +Q07657 426 Glycyl +Q07657 437 Glycyl +P38717 1206 N-linked +P32900 137 Phosphoserine +P32900 169 Phosphothreonine +P32900 191 Phosphoserine +P32900 193 Phosphoserine +P32900 219 Phosphoserine +P32900 221 Phosphothreonine +P32900 222 Phosphoserine +P32900 251 Phosphoserine +P32900 369 Phosphoserine +P32900 672 Phosphoserine +P32900 717 Phosphoserine +P35207 209 Phosphoserine +Q08491 88 Phosphoserine +Q08491 90 Phosphoserine +P42843 594 Phosphothreonine +Q00772 190 Phosphothreonine +Q00772 192 Phosphotyrosine +P32566 202 Phosphoserine +P32566 203 Phosphoserine +P32566 376 Phosphothreonine +P32566 381 Phosphoserine +P32566 394 Phosphoserine +P32566 400 Phosphoserine +P32566 453 Glycyl +Q04174 403 N-linked +Q04174 452 N-linked +P38990 43 Phosphothreonine +P38990 964 Phosphoserine +P38990 1126 Phosphoserine +P39955 536 Phosphoserine +Q99314 144 Phosphoserine +Q00711 90 Tele-8alpha-FAD +P24280 302 Phosphoserine +P24280 42 Glycyl +P24280 84 Glycyl +P40510 2 N-acetylserine +P40510 22 Phosphoserine +P40510 29 Phosphoserine +P40510 33 Phosphoserine +P46995 10 Phosphoserine +P46995 522 Phosphoserine +Q08446 168 Phosphoserine +Q08446 171 Phosphoserine +Q08446 32 Glycyl +P38634 5 Phosphothreonine%3B +P38634 33 Phosphothreonine +P38634 76 Phosphoserine +P38634 173 Phosphothreonine +P38634 198 Phosphoserine +P38634 201 Phosphoserine +P38634 268 Lysine +P38634 272 Lysine +P38634 274 Lysine +P38262 137 Phosphoserine +Q06315 10 Phosphoserine +Q06315 31 Phosphoserine +Q06315 578 Phosphothreonine +Q06315 580 Phosphoserine +Q06315 592 Phosphoserine +Q06315 701 Phosphoserine +Q06315 954 Phosphoserine +P38314 94 Phosphoserine +P38314 458 Phosphoserine +P38314 524 Phosphoserine +P38164 123 Phosphoserine +P38164 136 Phosphoserine +P33332 290 Phosphothreonine +P33332 606 Phosphoserine +P89102 184 Phosphoserine +P38890 517 Phosphoserine +P47166 2 N-acetylserine +P47166 151 Phosphoserine +P47166 538 Phosphoserine +P47166 549 Phosphoserine +P47166 568 Phosphoserine +P47166 571 Phosphoserine +P47166 576 Phosphoserine +P47166 589 Phosphoserine +P32578 33 Phosphoserine +P32578 181 Phosphoserine +P32578 198 Phosphoserine +P32578 200 Phosphoserine +P32578 206 Phosphoserine +P32578 209 Phosphoserine +P32578 220 Phosphoserine +P32578 331 Phosphoserine +P32578 494 Phosphoserine +P32578 497 Phosphoserine +P32578 643 Phosphoserine +P32578 2 N-myristoyl +P33336 56 Phosphoserine +P33336 65 Phosphoserine +P33336 67 Phosphoserine +P33336 92 Phosphoserine +P33336 103 Phosphoserine +P33336 142 Phosphoserine +P33336 162 Phosphoserine +P33336 165 Phosphoserine +P33336 170 Phosphoserine +P33336 176 Phosphoserine +P33336 337 N-linked +P33336 426 N-linked +P33336 513 N-linked +P33336 590 N-linked +P33336 615 N-linked +P33336 743 N-linked +Q03656 383 Phosphothreonine +Q03656 386 Phosphothreonine +Q03656 388 Phosphoserine +Q03656 393 Phosphoserine +Q03656 410 Phosphoserine +Q03656 427 Phosphoserine +Q03656 432 Phosphoserine +Q03656 445 Phosphoserine +Q03656 449 Phosphoserine +Q03656 453 Phosphoserine +P38283 268 Phosphoserine +P38283 489 Phosphoserine +P14906 512 Phosphoserine +Q04279 48 Phosphoserine +Q04279 220 Phosphoserine +Q04279 235 Phosphoserine +Q04279 238 Phosphoserine +Q04279 319 Phosphoserine +Q04279 339 Phosphoserine +Q04279 352 Phosphoserine +Q04279 434 Phosphoserine +Q04279 461 Phosphoserine +Q04279 467 Phosphothreonine +Q04279 630 Phosphoserine +Q04279 675 Phosphothreonine +Q04279 758 Phosphoserine +Q04279 816 Phosphoserine +Q04279 818 Phosphoserine +Q04279 855 Phosphoserine +P53011 257 Phosphoserine +O94742 2 N-acetylserine +O94742 12 Phosphoserine +P53953 51 Phosphoserine +P38166 2 N-acetylserine +P38166 60 Phosphoserine +P53965 94 Phosphoserine +Q04195 132 Phosphoserine +Q04195 794 Phosphoserine +Q3E784 2 N-acetylserine +Q3E784 10 Phosphoserine +Q02775 120 Phosphoserine +Q02775 212 Phosphothreonine +P40072 50 Phosphoserine +P40072 66 Phosphothreonine +P40072 67 Phosphoserine +P11655 439 N-linked +P11655 462 N-linked +P22224 286 Phosphoserine +P22214 160 Phosphoserine +P07560 201 Phosphoserine +P07560 204 Phosphoserine +P07560 214 S-geranylgeranyl +P07560 215 S-geranylgeranyl +P11075 212 Phosphoserine +P11075 215 Phosphoserine +P11075 334 Phosphothreonine +P11075 447 Phosphoserine +P11075 452 Phosphoserine +P11075 455 Phosphoserine +P11075 807 Phosphoserine +P11075 1226 Phosphoserine +P11075 1240 Phosphothreonine +P11075 1741 Phosphoserine +P11075 1752 Phosphoserine +P11075 797 Glycyl +P32855 16 Phosphoserine +P32855 19 Phosphoserine +P40316 185 Phosphoserine +P40316 186 Phosphoserine +P40316 212 Phosphoserine +P40316 213 Phosphoserine +P40316 277 Phosphoserine +P40316 292 Phosphoserine%3B +P25365 65 Phosphoserine +P25365 388 N-linked +P25365 620 N-linked +P25365 1039 N-linked +P40054 22 Phosphoserine +P40054 29 Phosphoserine +P40054 33 Phosphoserine +P36124 236 Phosphoserine +P36124 684 Phosphoserine +P36124 718 Phosphoserine +P36124 719 Phosphothreonine +P36124 741 Phosphoserine +Q12314 204 Phosphoserine +Q12314 207 Phosphoserine +P53313 278 Phosphoserine +P32602 2 N-acetylserine +P32602 261 Glycyl +P40482 178 Phosphoserine +P32844 2 N-acetylserine +P34250 137 Phosphoserine +P34250 280 Phosphoserine +P34250 504 Phosphoserine +P34250 507 Phosphoserine +P34250 556 Phosphoserine +P34250 980 Phosphoserine +P34250 1022 Phosphoserine +P34250 526 Glycyl +P34250 743 Glycyl +P38272 343 Phosphoserine +P38272 394 Phosphoserine +P53334 89 N-linked +P33330 20 Phosphothreonine +P33330 112 Phosphoserine +P33330 218 N6-(pyridoxal +P38827 625 Phosphoserine +P38827 875 Phosphothreonine +Q12369 10 Phosphoserine +Q12369 855 Phosphoserine +P35735 208 Phosphoserine +P20134 220 Phosphoserine +P20134 556 Phosphoserine +P20134 733 Phosphoserine +Q12234 55 Phosphoserine +Q12234 64 Phosphoserine +Q12234 468 Phosphoserine +Q07458 2 N-acetylserine +P34218 367 N6-acetyllysine%3B +P40963 168 N6-acetyllysine%3B +P36048 85 Phosphoserine +P36048 88 Phosphothreonine +P10870 383 N-linked +P18888 165 Phosphothreonine +P39929 72 Phosphothreonine +P39929 119 Phosphoserine +P39929 193 Phosphoserine +P39929 229 Glycyl +P00445 26 Phosphoserine +P00445 39 Phosphoserine +P00445 99 Phosphoserine +P00445 117 Phosphoserine +P00445 132 Phosphothreonine +P00445 138 Phosphothreonine +P00445 19 Glycyl +P00445 70 Glycyl +Q03954 107 Phosphoserine +Q03954 116 Phosphoserine +Q12455 5 Phosphoserine +P06843 2 N-acetylserine +P06843 126 Phosphoserine +P35177 78 Phosphothreonine%3B +P35177 88 Phosphoserine +P35177 1293 Phosphoserine +P38985 8 Phosphoserine +P32342 2 N-acetylserine +P40505 166 Phosphoserine +P40505 211 Phosphoserine +P15367 121 N-linked +P38810 15 Phosphoserine +P38810 72 Phosphothreonine +P38810 83 Phosphoserine +P38810 85 Phosphoserine +P38810 94 Phosphoserine +P38810 101 Phosphoserine +P38810 110 Phosphoserine +P38810 216 Phosphothreonine +P51534 18 Phosphoserine +P40073 166 Phosphoserine +P40073 59 N-linked +P25294 275 Phosphoserine +P52286 177 Phosphothreonine +P33338 294 Phosphothreonine +P33338 298 Phosphothreonine +P33338 308 Phosphoserine +P33338 555 Phosphoserine +Q12078 87 N-linked +P25357 187 Phosphoserine +P25357 395 Phosphoserine +P25357 796 Phosphothreonine +P25357 1037 Phosphoserine +P50278 65 Phosphoserine +P50278 68 Phosphoserine +P50278 320 Phosphothreonine +Q08199 105 N-linked +Q08199 181 N-linked +Q08199 215 N-linked +Q08199 233 N-linked +Q08199 315 N-linked +Q08199 333 N-linked +P40472 423 N-linked +P11978 692 Phosphoserine +P11978 1128 Glycyl +P36169 142 Phosphoserine +P36169 273 Phosphothreonine +P32790 447 Phosphoserine +P32790 449 Phosphoserine +P32790 454 Phosphoserine +P32790 799 Phosphoserine +P32790 831 Phosphothreonine +P32790 858 Phosphothreonine +P32790 887 Phosphothreonine +P32790 904 Phosphothreonine +P32790 984 Phosphothreonine +P32790 993 Phosphothreonine +P32790 996 Phosphoserine +P32790 1075 Phosphothreonine +P32790 471 Glycyl +P32790 548 Glycyl +P47037 112 N6-acetyllysine +P47037 113 N6-acetyllysine +P38925 24 Phosphoserine +P38925 33 Glycyl +P38925 34 Glycyl +Q04007 309 Phosphoserine +Q04007 310 Phosphoserine +Q04007 311 Phosphoserine +Q04007 332 Phosphoserine +Q04007 334 Phosphoserine +Q04007 692 Phosphoserine +Q04007 694 Phosphoserine +Q04007 706 Phosphoserine +Q04007 841 Phosphoserine +Q04007 668 Glycyl +Q04007 670 Glycyl +P38956 2 N-acetylserine +P22082 358 Phosphoserine +P22082 383 Phosphothreonine +P22082 716 Phosphoserine +P22082 1340 Phosphoserine +P22082 543 Glycyl +P46950 91 Phosphothreonine +P53438 771 Phosphoserine +P37262 42 Phosphoserine +P37262 64 Phosphoserine +P31109 95 S-palmitoyl +P31109 63 Glycyl +P33328 58 Phosphoserine +P33328 94 S-palmitoyl +P33328 62 Glycyl +Q12420 268 Phosphoserine +P40317 40 Phosphoserine +P40317 53 Phosphoserine +P40317 191 Phosphoserine +P40317 193 Phosphoserine +P40317 245 Phosphoserine +P25808 254 Phosphoserine +P46965 2 N-acetylserine +P38915 85 Phosphothreonine +P38915 108 Phosphoserine +P38915 123 Phosphoserine +P38915 131 Phosphoserine +P38915 451 Phosphoserine +Q03707 78 Phosphoserine +Q03707 80 Phosphoserine +Q03707 85 Phosphoserine +Q03707 181 Phosphoserine +Q03707 203 Phosphoserine +Q03707 204 Phosphoserine +Q03707 206 Phosphoserine +Q03707 301 Phosphoserine +Q03707 394 Phosphothreonine +Q03707 427 Phosphoserine +P39931 212 Phosphothreonine +P53172 9 Phosphoserine +P53172 42 Phosphoserine +P53172 46 Phosphoserine +P53172 430 Phosphoserine +Q12118 308 Phosphothreonine +P38200 165 Phosphoserine +P36024 47 Phosphoserine +P36024 50 Phosphoserine +P36024 54 Phosphoserine +P36024 56 Phosphoserine +P36024 155 Phosphoserine +P38889 427 4-aspartylphosphate +Q02100 94 Phosphoserine +Q02100 113 Phosphothreonine +Q02100 399 Phosphoserine +Q02100 558 Phosphoserine +P34252 84 Phosphothreonine%3B +Q04964 1 N-acetylmethionine +Q04964 56 Phosphoserine%3B +Q04964 58 Phosphoserine%3B +Q04964 60 Phosphoserine%3B +Q12306 2 N-acetylserine +Q12306 2 Phosphoserine +Q12306 4 Phosphoserine +Q12306 98 Glycyl +P32364 583 Phosphothreonine +P32909 12 Phosphoserine +P32909 96 Phosphoserine +P32909 129 Phosphothreonine +P32909 311 Phosphothreonine +P32909 545 Phosphoserine +P32909 602 Phosphoserine +P56508 71 Phosphoserine +P56508 77 Phosphoserine +P00447 147 Phosphothreonine +P00447 149 Phosphothreonine +P23201 182 Phosphoserine +P23201 183 Phosphoserine +P23201 220 Phosphothreonine +P23201 254 Phosphoserine +P23201 274 Phosphoserine +P23201 301 Phosphoserine +P23201 585 Phosphoserine +P23201 599 Phosphoserine +P23201 646 Phosphoserine +P23201 817 Phosphoserine +P23201 820 Phosphoserine +P23201 865 Phosphoserine +P23201 883 Phosphoserine +P23201 910 Phosphoserine +P23201 937 Phosphoserine +P23201 961 Phosphoserine +P23201 979 Phosphoserine +P23201 1053 Phosphoserine +P23201 1056 Phosphoserine +P23201 1080 Phosphoserine +P23201 1173 Phosphoserine +P23201 1179 Phosphothreonine +P23201 1180 Phosphoserine +P23201 1251 Phosphothreonine +P23201 1263 Phosphoserine +P36131 199 Phosphothreonine%3B +P53540 124 Phosphoserine +P53540 136 Phosphoserine +P40092 127 GPI-anchor +P40092 41 N-linked +P40092 59 N-linked +P53541 233 N-linked +P53541 293 N-linked +P53541 303 N-linked +P53541 500 N-linked +P53541 536 N-linked +P53541 560 N-linked +P53541 563 N-linked +P53541 572 N-linked +P35209 454 Phosphoserine +Q06168 78 Phosphoserine +P25554 139 Phosphoserine +P22579 137 Phosphoserine +P22579 303 Phosphothreonine +P22579 304 Phosphothreonine +P22579 316 Phosphoserine +P22579 1046 Phosphoserine +P34164 66 Phosphoserine +P34164 298 Phosphoserine +P34164 2 N-myristoyl +P40210 13 Phosphoserine +P40210 183 Phosphothreonine +P40210 433 Phosphothreonine +P40210 436 Phosphoserine +P40210 438 Phosphothreonine +P53955 626 Phosphoserine +P53955 649 Phosphoserine +P53955 653 Phosphoserine +Q12098 72 Phosphothreonine%3B +Q12098 113 Phosphothreonine%3B +Q12098 289 Phosphoserine%3B +Q12098 319 Phosphothreonine%3B +Q12098 329 Phosphoserine%3B +Q12098 355 Phosphoserine%3B +P54867 331 Phosphoserine +P54867 353 Phosphoserine +P54867 65 N-linked +P40485 145 Phosphoserine +P40485 150 Phosphoserine +P40485 153 Phosphoserine +P39928 502 Phosphoserine +P39928 576 Phosphohistidine%3B +P39928 758 Phosphoserine +P39928 833 Phosphoserine +P39928 1041 Phosphoserine +P39928 1044 Phosphoserine +P39928 1144 4-aspartylphosphate +P39928 100 N-linked +P39928 138 N-linked +P39928 142 N-linked +P39928 181 N-linked +P39928 224 N-linked +P39928 272 N-linked +Q12267 2 N-acetylserine +Q12267 43 Phosphothreonine +Q12267 113 Phosphoserine +P18480 818 Phosphoserine +P32568 2 N-acetylserine +P32568 26 Phosphoserine +P32568 29 Phosphoserine +P32568 64 Phosphoserine +P32568 80 Phosphoserine +P32568 86 Phosphoserine +P32568 1153 Phosphothreonine +P32568 273 N-linked +P32568 334 N-linked +P32568 518 N-linked +P32568 730 N-linked +P32568 874 N-linked +P32568 1401 N-linked +P53207 512 Phosphoserine +P53207 514 Phosphoserine +Q12133 102 N-linked +Q12133 173 N-linked +P36094 213 Phosphoserine +P36094 217 Phosphoserine +P36094 284 Phosphoserine +P36094 329 Phosphoserine +P17123 2 N-acetylserine +P17123 118 Phosphoserine +P17123 125 Phosphoserine +P50875 446 Phosphoserine +P50875 516 Phosphothreonine +Q06132 736 Phosphoserine +P06701 2 N-acetylalanine +P34226 148 Phosphoserine +P34226 561 Phosphoserine +P34226 563 Phosphoserine +P34226 564 Phosphothreonine +P34226 693 Cysteine +P34226 693 S-farnesyl +Q08581 7 Phosphothreonine%3B +Q08581 188 Phosphoserine +Q08581 189 Phosphoserine +Q08581 201 Phosphoserine%3B +Q08581 216 Phosphoserine +Q08581 273 Phosphothreonine +Q08581 283 Phosphoserine +Q12232 25 N-linked +Q12232 378 N-linked +Q12232 381 N-linked +Q12232 408 N-linked +Q12232 448 N-linked +Q12232 486 N-linked +P32380 18 Phosphothreonine +P32380 60 Phosphoserine%3B +P32380 64 Phosphothreonine%3B +P32380 68 Phosphothreonine%3B +P32380 80 Phosphoserine +P32380 529 Phosphoserine +P25582 455 Phosphoserine +P25582 464 Phosphoserine +P25582 529 Phosphoserine +Q04398 86 N-linked +P33419 18 Phosphothreonine +P33419 65 Phosphoserine +P33419 240 Phosphothreonine%3B +Q03029 198 GPI-anchor +P38904 1014 Phosphoserine +P38904 1067 Phosphoserine +P38904 981 Glycyl +P38904 1154 Glycyl +P32603 201 N-linked +P32573 188 Glycyl +P32558 526 Phosphoserine +P32558 765 Phosphoserine +P35210 468 Phosphoserine +P53866 105 Phosphoserine +P53866 217 Phosphoserine +P53866 255 Phosphoserine +P53866 334 Phosphoserine +P53866 343 Phosphoserine +P53866 345 Phosphoserine +P24276 2 N-acetylserine +P24276 40 Phosphoserine +P24276 164 Phosphoserine +P24276 183 Phosphoserine +P24276 227 Phosphothreonine +P24276 286 Phosphoserine +P24276 322 Phosphoserine +P24276 491 Phosphoserine +P24276 492 Phosphoserine +P24276 688 Phosphotyrosine +P32343 358 Phosphoserine +P32343 212 N-linked +P32343 356 N-linked +P32343 430 N-linked +P32343 507 N-linked +P32343 557 N-linked +P32343 575 N-linked +P32343 367 Glycyl +P15705 227 Phosphoserine +P15705 99 Glycyl +P15705 168 Glycyl +P15705 384 Glycyl +P14359 125 Glycyl +P38839 59 Phosphoserine +P38839 86 Phosphoserine +Q12516 45 Phosphoserine +Q12516 167 Phosphoserine +Q12516 297 N-linked +Q12516 385 N-linked +Q12020 11 Phosphoserine +Q12020 139 Phosphoserine +P36167 212 Phosphoserine +P25567 55 Phosphoserine +P25567 148 Phosphoserine +P25567 422 Phosphoserine +P25567 156 Glycyl +P25567 301 Glycyl +P25567 342 Glycyl +P25567 352 Glycyl +P42845 2 N-acetylserine +P42845 7 Phosphoserine +P42845 72 Phosphoserine +P42845 99 Phosphothreonine +P42845 102 Phosphoserine +P42845 419 Phosphothreonine +Q03497 2 N-acetylserine +Q03497 87 Phosphoserine +Q03497 165 Phosphoserine +Q03497 167 Phosphothreonine +Q03497 169 Phosphoserine +Q03497 203 Phosphothreonine +Q03497 418 Phosphoserine +Q03497 502 Phosphoserine +Q03497 547 Phosphoserine +Q03497 562 Phosphoserine +Q03497 573 Phosphothreonine +Q03497 585 Phosphoserine +Q03497 773 Phosphothreonine +Q03497 924 Phosphoserine +Q03497 927 Phosphothreonine +P32917 329 Phosphoserine +P12866 61 N-linked +P12866 1022 Glycyl +P06784 359 Phosphoserine +P06784 363 Phosphothreonine +P39932 197 N-linked +P39932 319 N-linked +P09959 149 Phosphoserine +P09959 160 Phosphoserine%3B +P09959 176 Phosphoserine +P09959 179 Phosphothreonine +P09959 182 Phosphothreonine +P09959 547 Phosphoserine +P46655 300 Phosphothreonine +P53277 45 Phosphoserine +P53277 124 Phosphoserine +P53277 125 Phosphoserine +P11972 252 Phosphoserine +P11972 408 Phosphoserine +P11972 539 Phosphoserine%3B +P11972 587 Phosphoserine +P41930 444 Phosphoserine +P41930 448 Phosphoserine +P41930 450 Phosphoserine +P08153 225 Phosphoserine +P08153 278 Phosphoserine +P08153 300 Phosphoserine +P08153 339 Phosphothreonine +P08153 376 Phosphoserine +P08153 488 Phosphoserine +P08153 492 Phosphoserine +P08153 505 Phosphoserine +P08153 522 Phosphoserine%3B +P08153 646 Phosphoserine%3B +P08153 664 Phosphoserine%3B +P53852 326 Phosphoserine +P23615 94 Phosphoserine +P23615 134 Phosphoserine +P23615 136 Phosphoserine +P23615 148 Phosphoserine +P23615 155 Phosphoserine +P23615 206 Phosphoserine +P23615 295 Phosphoserine +Q08673 23 N-linked +Q08673 174 N-linked +Q08673 200 N-linked +Q08673 206 N-linked +P10080 2 N-acetylserine +P10080 91 Phosphothreonine +P10080 119 Phosphothreonine +P10080 242 Phosphothreonine +P10080 244 Phosphoserine +P53599 57 Phosphoserine +P53599 62 Phosphoserine +P53599 78 Phosphoserine +P53599 118 Phosphoserine +P53599 290 Phosphoserine +P53599 1424 Phosphoserine +Q07084 110 Phosphoserine +Q07084 195 Phosphoserine +Q07084 327 Phosphoserine +Q07084 351 Phosphoserine +Q07084 368 Phosphoserine +Q07084 380 Phosphoserine +Q07084 554 4-aspartylphosphate +Q07084 673 Phosphoserine +Q07084 693 Phosphothreonine +Q07084 703 Phosphoserine +Q07084 706 Phosphoserine +Q12427 254 Phosphoserine +P36085 514 Phosphoserine +D6VTK4 310 Phosphoserine +D6VTK4 315 Phosphoserine +D6VTK4 329 Phosphothreonine +D6VTK4 331 Phosphoserine +D6VTK4 360 Phosphoserine +D6VTK4 363 Phosphothreonine +D6VTK4 366 Phosphoserine +D6VTK4 382 Phosphothreonine +D6VTK4 385 Phosphoserine +D6VTK4 386 Phosphoserine +D6VTK4 411 Phosphothreonine +D6VTK4 414 Phosphothreonine +D6VTK4 25 N-linked +D6VTK4 32 N-linked +D6VTK4 374 Glycyl +D6VTK4 400 Glycyl +D6VTK4 422 Glycyl +P25344 202 Phosphoserine +P25344 244 Phosphothreonine +P25344 248 Phosphoserine +P16965 28 Phosphoserine +P16965 69 Phosphoserine +P53312 102 Phosphoserine +P53312 263 Phosphoserine +P53312 276 Phosphoserine +P38359 51 N-linked +P38359 93 N-linked +P38359 358 N-linked +P38359 391 N-linked +P38359 630 N-linked +P38359 653 N-linked +P38359 718 N-linked +Q03088 471 Phosphoserine +Q03088 496 Phosphothreonine +Q03088 551 Phosphoserine +Q03088 662 Phosphoserine +Q03088 739 Phosphothreonine +Q03088 756 Phosphothreonine +Q03088 757 Phosphoserine +Q06677 52 Phosphoserine +Q06677 64 Phosphoserine +Q06677 264 Phosphoserine +Q06677 308 Phosphoserine +Q06677 312 Phosphoserine +P32828 14 Phosphoserine +P32828 29 Phosphoserine +Q08817 214 Phosphothreonine +P39543 35 N-linked +P39543 53 N-linked +P39543 85 N-linked +P39543 115 N-linked +P39543 170 N-linked +P53148 77 Phosphoserine +P53148 356 Phosphothreonine +P53148 380 Phosphoserine +P06844 270 Phosphoserine +P32916 239 Phosphoserine +P32916 523 Phosphoserine +P12954 833 Phosphoserine +P13130 26 N-linked +P13130 50 N-linked +P13130 58 N-linked +P13130 64 N-linked +P13130 76 N-linked +P13130 108 N-linked +P13130 181 N-linked +P13130 190 N-linked +P13130 199 N-linked +P13130 205 N-linked +P13130 248 N-linked +P13130 281 N-linked +Q07549 134 Phosphoserine +Q07549 2 S-palmitoyl +Q07549 3 S-palmitoyl +Q07549 5 S-palmitoyl +Q07549 7 S-palmitoyl +Q07549 8 S-palmitoyl +Q07549 128 Glycyl +Q04477 2 N-acetylserine +P40014 2 N-acetylalanine +Q03012 87 Phosphoserine +P25380 440 GPI-anchor +P25380 256 N-linked +P25380 314 N-linked +P25380 327 N-linked +P27692 35 Phosphothreonine +P27692 133 Phosphothreonine +P27692 136 Phosphoserine +P27692 188 Phosphoserine +P27692 219 Phosphoserine +P39015 2 N-acetylserine +P39015 55 Phosphoserine +P39015 118 Phosphoserine +P39015 229 Phosphoserine +P39015 46 Glycyl +P39015 121 Glycyl +P39015 171 Glycyl +P39015 184 Glycyl +Q05937 71 Phosphoserine +Q05937 111 Phosphoserine +Q07351 153 Phosphoserine +Q07351 155 Phosphoserine +Q12038 591 Phosphoserine +Q12038 602 Phosphoserine +P32583 133 Phosphoserine +P32583 289 Phosphothreonine +P32583 293 Phosphoserine +P32583 394 Phosphoserine +P38931 370 Phosphoserine +P38931 375 Phosphoserine +P38931 425 Phosphoserine +P38931 601 Phosphothreonine +P38931 608 Phosphoserine%3B +P38931 636 Phosphoserine +P38931 748 Phosphoserine +P37296 1 N-acetylmethionine +P37296 223 Phosphoserine +P37296 228 Phosphoserine +P31377 238 S-palmitoyl +P36126 2 N-acetylserine +P36126 8 Phosphoserine +P36126 30 Phosphoserine +P36126 145 Phosphoserine +P36126 1461 Phosphoserine +P36126 1462 Phosphothreonine +Q07798 2 N-linked +Q07798 184 N-linked +Q07798 503 N-linked +P08459 475 GPI-anchor +P08459 77 N-linked +P08459 135 N-linked +P08459 285 N-linked +P08459 303 N-linked +P08459 340 N-linked +P08459 343 N-linked +P08459 355 N-linked +P38789 301 Phosphothreonine +P39926 31 Phosphoserine +P39926 34 Phosphoserine +P38788 477 Phosphoserine +P38788 480 Phosphoserine +P25379 2 N-acetylserine +P25379 37 N6-(pyridoxal +P33894 377 N-linked +P33894 814 N-linked +P53101 213 N6-(pyridoxal +P46676 2 N-acetylserine +P46676 378 Phosphoserine +P46676 379 Phosphoserine +P46676 628 Phosphoserine +P46676 681 Phosphoserine +P46676 697 Phosphothreonine +P46676 712 Phosphoserine%3B +P46676 738 Phosphoserine +P46676 817 Phosphothreonine +P53616 395 N-linked +P33300 349 Phosphoserine +P54003 293 Phosphoserine +P54003 301 Phosphoserine +P54003 47 N-linked +P04802 2 N-acetylserine +P04802 14 Phosphoserine +P04802 301 Phosphoserine +P04802 502 Phosphoserine +P04802 546 Phosphoserine +Q02875 350 Phosphothreonine +P54000 119 Phosphoserine +P54000 268 Phosphoserine +P54000 269 Phosphoserine +P54000 289 Phosphoserine +Q07478 2 N-acetylserine +Q07478 13 Phosphoserine +Q07478 37 Phosphoserine +Q07478 169 Phosphothreonine +P53201 2 N-acetylserine +P38326 209 Phosphoserine +P38088 25 N-acetylserine +P38088 226 Phosphoserine +P38088 476 Phosphoserine +P38088 528 Phosphoserine +P38088 689 Phosphothreonine +Q6WNK7 68 Glycyl +P38869 115 N-linked +P32591 88 Phosphoserine +P32591 185 Phosphoserine +P32591 235 Phosphothreonine +P32591 657 Phosphoserine +P40825 504 Phosphoserine +P40825 975 Phosphoserine +P40528 172 Phosphoserine +P40528 179 Phosphoserine +P40528 859 Phosphoserine +P40528 860 Phosphoserine +P46679 594 Phosphoserine +P46679 625 Phosphoserine +P23561 323 Phosphoserine +P23561 465 Phosphoserine +P01098 24 Phosphoserine +P39007 60 N-linked +P39007 535 N-linked +P39007 539 N-linked +P38198 997 Phosphoserine +P38198 1018 Phosphoserine +P38198 1047 Phosphothreonine +P38198 1063 Phosphoserine +P38198 1167 Phosphoserine +P46675 2 Phosphoserine +P46675 277 Phosphoserine +P46675 813 Phosphoserine +P32911 2 N-acetylserine +Q12254 23 N-linked +Q12254 249 N-linked +Q12254 256 N-linked +P15180 2 N-acetylserine +P15180 30 Phosphoserine +P15180 62 Phosphothreonine +P15180 308 Glycyl +P15180 577 Glycyl +Q05506 2 N-acetylalanine +Q05506 15 Phosphoserine +P40150 2 N-acetylalanine +P40150 47 Phosphothreonine +P40150 431 Phosphothreonine +P13574 29 Phosphothreonine +P13574 214 Phosphoserine +P13574 226 Phosphoserine +P13574 289 Phosphothreonine +P13574 400 Phosphoserine +P32597 38 Phosphoserine +P37297 459 Phosphoserine +P32944 36 Phosphoserine%3B +P32944 45 Phosphothreonine%3B +P32944 56 Phosphoserine%3B +P32944 63 Phosphoserine%3B +P32944 70 Phosphoserine +P32944 74 Phosphothreonine%3B +P32944 102 Phosphoserine%3B +P32944 105 Phosphoserine%3B +P32944 111 Phosphoserine%3B +P32944 118 Phosphoserine%3B +P32944 121 Phosphothreonine%3B +P32944 124 Phosphothreonine%3B +P32944 127 Phosphoserine%3B +P32944 131 Phosphothreonine%3B +P32944 133 Phosphoserine%3B +P32944 136 Phosphoserine%3B +P32944 156 Phosphoserine%3B +P32944 169 Phosphoserine%3B +P32944 196 Phosphothreonine%3B +P32944 201 Phosphoserine%3B +P32944 225 Phosphoserine%3B +P32944 254 Phosphoserine%3B +P32944 262 Phosphoserine +P32944 263 Phosphoserine%3B +P32944 266 Phosphoserine%3B +P32944 280 Phosphothreonine%3B +P32944 284 Phosphoserine +P32944 294 Phosphoserine +P32944 312 Phosphoserine%3B +P32944 345 Phosphoserine +P32944 367 Phosphothreonine%3B +P32944 373 Phosphothreonine%3B +P32944 379 Phosphoserine%3B +P32944 384 Phosphothreonine%3B +P32944 395 Phosphoserine%3B +P32944 438 Phosphoserine%3B +P32944 610 Phosphoserine%3B +P32944 629 Phosphothreonine%3B +P32944 688 Phosphothreonine%3B +P32944 692 Phosphothreonine +P32944 741 Glycyl +P25302 255 Phosphoserine +P25302 806 Phosphoserine +P15625 2 N-acetylserine +P07806 73 Phosphoserine +P07806 294 Phosphoserine +P07806 332 Phosphoserine +P07806 707 Phosphoserine +P07806 1003 Phosphothreonine +P41895 198 Phosphoserine +P41895 200 Phosphothreonine +P41895 515 Phosphoserine +P41895 560 Phosphoserine +P41895 562 Phosphoserine +P41895 571 Phosphoserine +P41895 655 Phosphoserine +Q12030 58 Phosphoserine +Q12030 146 Phosphoserine +P35189 181 Glycyl +P23255 158 Phosphothreonine +P23255 161 Phosphothreonine +P23255 163 Phosphoserine +P23255 318 Phosphoserine +Q12297 237 Phosphothreonine +Q12297 310 Phosphoserine +Q12297 346 Phosphoserine +P09436 829 Phosphoserine +P09436 1059 Phosphoserine +P09436 486 Glycyl +Q06836 277 Phosphothreonine +Q06836 369 Phosphoserine +P25638 2 N-acetylserine +P15019 2 N-acetylserine +P13188 378 Phosphoserine +P32774 95 Phosphoserine +P32774 102 Phosphoserine +P36421 2 N-acetylserine +P36421 235 Phosphoserine +P36421 359 Phosphothreonine +Q04226 236 Phosphoserine +Q04226 238 Phosphoserine +P38129 299 Phosphoserine +P38129 411 Phosphoserine +P38129 415 Phosphoserine +P38129 787 Phosphoserine +Q03750 269 Phosphoserine +Q04545 527 Phosphoserine +Q04545 603 Phosphoserine +P34163 462 Phosphoserine +P34163 466 Phosphoserine +P34163 521 Phosphoserine +P34163 538 Phosphoserine +P34163 539 Phosphothreonine +P34163 246 Glycyl +Q12043 645 Phosphoserine +Q12043 270 N-linked +Q12043 289 N-linked +Q12043 297 N-linked +Q12043 304 N-linked +Q12043 321 N-linked +Q12043 474 N-linked +Q12043 589 N-linked +Q12043 680 N-linked +Q12043 714 N-linked +Q12043 742 N-linked +P04801 195 Phosphoserine +P04801 289 Phosphoserine +P04801 297 Phosphothreonine +P04801 381 Phosphothreonine +P04801 453 Phosphoserine +P04801 457 Phosphoserine +P04801 460 Phosphothreonine +P04801 605 Phosphoserine +P38854 236 Phosphothreonine +P38854 244 Phosphoserine +P38854 286 Phosphoserine +Q03533 504 Phosphothreonine +Q03533 509 Phosphoserine +Q03533 518 Phosphoserine +Q03533 538 Phosphothreonine +Q03533 578 Phosphoserine +P40045 2 N-acetylserine +P02557 278 Phosphoserine +P02557 280 Phosphoserine +Q12466 1000 Phosphoserine +Q03640 67 Phosphoserine +Q03640 112 Phosphoserine +Q03640 1340 Phosphoserine +Q03640 1342 Phosphoserine +Q03640 1346 Phosphoserine +Q03640 1350 Phosphothreonine +Q03640 1354 Phosphoserine +Q03640 1400 Phosphoserine +P40533 38 N-linked +P40533 147 N-linked +P40533 229 N-linked +P40533 266 N-linked +P40533 307 N-linked +Q03761 2 N-acetylserine +Q03761 129 Phosphoserine +Q03761 286 Phosphoserine +P50105 36 Phosphoserine +P50105 49 Phosphoserine +P50105 80 Phosphoserine +P53072 72 Phosphoserine +P39076 2 N-acetylserine +P39079 2 N-acetylserine +P39079 249 Phosphoserine +P38758 189 Phosphoserine +P38758 204 Phosphoserine +P38758 306 Phosphoserine +P53882 628 Phosphoserine +P53882 4 N-linked +P53882 257 N-linked +P53882 492 N-linked +P53882 557 N-linked +P53882 562 N-linked +P53882 626 N-linked +P53882 512 Glycyl +Q12004 1 N-acetylmethionine +P34111 546 Phosphoserine +P40085 22 Phosphoserine +P40085 318 N-linked +P38756 259 Phosphoserine +Q06466 61 N-linked +Q06466 124 N-linked +Q06466 141 N-linked +P47988 22 Phosphothreonine +P47988 755 Phosphothreonine +P18412 2 N-acetylserine +P18412 325 Phosphoserine +P53038 417 Phosphoserine +P53038 419 Phosphoserine +P32367 617 Phosphoserine +P53215 2 N-acetylalanine +Q07748 62 N6-(pyridoxal +Q08579 560 Phosphoserine +Q08579 572 Phosphoserine +P41544 192 Phosphoserine +P41544 15 Glycyl +P41896 28 Phosphoserine +P41896 34 Phosphoserine +P41896 56 Phosphoserine +Q05021 99 Phosphotyrosine +Q05021 101 Phosphoserine +Q05021 104 Phosphoserine +P40468 141 Phosphoserine +P40468 1144 Phosphoserine +P40468 2264 Phosphothreonine +P40468 2267 Phosphoserine +P40468 2355 Phosphoserine +P26637 2 N-acetylserine +P26637 142 Phosphothreonine +P00958 2 N-acetylserine +P36145 52 Phosphoserine +P36145 97 Phosphoserine +P36145 106 Phosphoserine +P11747 131 Phosphothreonine +P38085 13 Phosphoserine +P38085 80 Phosphoserine +P38085 84 Phosphoserine +P38085 39 Glycyl +P48606 94 Phosphoserine +P48231 991 Phosphoserine +P12612 2 N-acetylserine +P47079 505 Phosphoserine +P47079 15 Glycyl +P38321 105 Phosphoserine +P38177 433 Phosphoserine +P38177 439 Phosphoserine +Q07793 416 Phosphoserine +Q05497 113 Phosphoserine +P43600 25 N-linked +P43600 26 N-linked +P43600 53 N-linked +P43600 77 N-linked +P43600 163 N-linked +P53185 856 Phosphoserine +P53185 898 Phosphoserine +P0CX18 184 GPI-anchor +P0CX18 28 N-linked +P0CX18 138 N-linked +Q03856 416 Phosphoserine +O74302 416 Phosphoserine +P0CX70 416 Phosphoserine +Q12424 28 N-linked +Q12424 148 N-linked +Q12424 280 N-linked +Q12424 329 N-linked +Q12424 645 N-linked +Q07629 43 N-linked +Q07629 129 N-linked +P14680 38 Phosphoserine +P14680 115 Phosphoserine +P14680 118 Phosphoserine +P14680 127 Phosphoserine +P14680 206 Phosphoserine +P14680 240 Phosphoserine +P14680 245 Phosphoserine +P14680 247 Phosphoserine +P14680 288 Phosphothreonine +P14680 295 Phosphoserine +P14680 530 Phosphotyrosine +P46683 78 Phosphoserine +P39548 217 Glycyl +P40917 85 Phosphoserine +P40917 89 Phosphoserine +P40917 196 Phosphoserine +Q3E821 33 N-linked +Q3E6R4 42 GPI-anchor +Q3E6R4 20 N-linked +Q3E6R4 24 N-linked +Q3E6R4 27 N-linked +Q3E6R4 30 N-linked +Q3E6R4 33 N-linked +Q03612 416 Phosphoserine +P40052 18 Phosphoserine +P40052 39 Phosphoserine +P40052 41 Phosphoserine +P40052 57 Phosphoserine +P40052 60 Phosphoserine +P40052 178 Phosphoserine +P40052 189 Phosphoserine +P40052 192 Phosphoserine diff --git a/test_files/uniprot_mod_raw.txt b/test_files/uniprot_mod_raw.txt new file mode 100644 index 0000000..3ee2a2a --- /dev/null +++ b/test_files/uniprot_mod_raw.txt @@ -0,0 +1,92278 @@ +##gff-version 3 +##sequence-region P12688 1 680 +P12688 UniProtKB Chain 1 680 . . . ID=PRO_0000086835;Note=Serine/threonine-protein kinase YPK1 +P12688 UniProtKB Domain 347 602 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P12688 UniProtKB Domain 603 673 . . . Note=AGC-kinase C-terminal +P12688 UniProtKB Nucleotide binding 353 361 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P12688 UniProtKB Active site 470 470 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P12688 UniProtKB Binding site 376 376 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P12688 UniProtKB Modified residue 57 57 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P12688 UniProtKB Modified residue 61 61 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P12688 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P12688 UniProtKB Modified residue 71 71 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P12688 UniProtKB Modified residue 170 170 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P12688 UniProtKB Modified residue 502 502 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P12688 UniProtKB Modified residue 504 504 . . . Note=Phosphothreonine%3B by PKH1;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:10074427,ECO:0000269|PubMed:15840588;Dbxref=PMID:19779198,PMID:10074427,PMID:15840588 +P12688 UniProtKB Modified residue 644 644 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P12688 UniProtKB Modified residue 653 653 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P12688 UniProtKB Modified residue 662 662 . . . Note=Phosphothreonine%3B by PKH1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15840588;Dbxref=PMID:15840588 +P12688 UniProtKB Modified residue 671 671 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P12688 UniProtKB Mutagenesis 376 376 . . . Note=No kinase activity. ATP-binding defect. Internalization defects. K->A%2CR;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10825204,ECO:0000269|PubMed:11807089,ECO:0000269|PubMed:12221112,ECO:0000269|PubMed:15470109,ECO:0000269|PubMed:15820214,ECO:0000269|PubMed:15840588;Dbxref=PMID:10825204,PMID:11807089,PMID:12221112,PMID:15470109,PMID:15820214,PMID:15840588 +P12688 UniProtKB Mutagenesis 488 488 . . . Note=Catalytically inactive. Internalization defects. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11807089,ECO:0000269|PubMed:15470109;Dbxref=PMID:11807089,PMID:15470109 +P12688 UniProtKB Mutagenesis 490 490 . . . Note=Reduced sphingolipid biosynthesis inhibitor drug myriocin (ISP-1) resistance. Defective in growth and endocytosis. G->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11807089,ECO:0000269|PubMed:15820214;Dbxref=PMID:11807089,PMID:15820214 +P12688 UniProtKB Mutagenesis 504 504 . . . Note=Reduced sphingolipid biosynthesis inhibitor drug myriocin (ISP-1) resistance. Defective in growth and endocytosis. T->A%2CD%2CE;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11807089,ECO:0000269|PubMed:15470109,ECO:0000269|PubMed:15820214,ECO:0000269|PubMed:15840588;Dbxref=PMID:11807089,PMID:15470109,PMID:15820214,PMID:15840588 +P12688 UniProtKB Mutagenesis 504 504 . . . Note=No phosphorylation%3B when associated with A-662 or D-662. T->A%2CD;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11807089,ECO:0000269|PubMed:15470109,ECO:0000269|PubMed:15820214,ECO:0000269|PubMed:15840588;Dbxref=PMID:11807089,PMID:15470109,PMID:15820214,PMID:15840588 +P12688 UniProtKB Mutagenesis 662 662 . . . Note=No phosphorylation%3B when associated with A-504 or D-504. T->A%2CD;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11807089,ECO:0000269|PubMed:15470109,ECO:0000269|PubMed:15820214,ECO:0000269|PubMed:15840588;Dbxref=PMID:11807089,PMID:15470109,PMID:15820214,PMID:15840588 +P12688 UniProtKB Mutagenesis 662 662 . . . Note=No phosphorylation. Reduced sphingolipid biosynthesis inhibitor drug myriocin (ISP-1) resistance. No defect in growth or endocytosis. T->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11807089,ECO:0000269|PubMed:15470109,ECO:0000269|PubMed:15820214,ECO:0000269|PubMed:15840588;Dbxref=PMID:11807089,PMID:15470109,PMID:15820214,PMID:15840588 +P12688 UniProtKB Sequence conflict 201 201 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12688 UniProtKB Sequence conflict 553 553 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25491 1 409 +P25491 UniProtKB Chain 1 406 . . . ID=PRO_0000071093;Note=Mitochondrial protein import protein MAS5 +P25491 UniProtKB Propeptide 407 409 . . . ID=PRO_0000396684;Note=Removed in mature form;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25491 UniProtKB Domain 4 72 . . . Note=J +P25491 UniProtKB Repeat 143 150 . . . Note=CXXCXGXG motif +P25491 UniProtKB Repeat 159 166 . . . Note=CXXCXGXG motif +P25491 UniProtKB Repeat 185 192 . . . Note=CXXCXGXG motif +P25491 UniProtKB Repeat 201 208 . . . Note=CXXCXGXG motif +P25491 UniProtKB Zinc finger 130 213 . . . Note=CR-type +P25491 UniProtKB Region 1 172 . . . Note=Necessary for HAP1 repression in the absence of heme +P25491 UniProtKB Region 135 137 . . . Note=Substrate binding +P25491 UniProtKB Region 215 216 . . . Note=Substrate binding +P25491 UniProtKB Region 247 249 . . . Note=Substrate binding +P25491 UniProtKB Compositional bias 73 103 . . . Note=Gly-rich +P25491 UniProtKB Metal binding 143 143 . . . Note=Zinc 1 +P25491 UniProtKB Metal binding 146 146 . . . Note=Zinc 1 +P25491 UniProtKB Metal binding 159 159 . . . Note=Zinc 2 +P25491 UniProtKB Metal binding 162 162 . . . Note=Zinc 2 +P25491 UniProtKB Metal binding 185 185 . . . Note=Zinc 2 +P25491 UniProtKB Metal binding 188 188 . . . Note=Zinc 2 +P25491 UniProtKB Metal binding 201 201 . . . Note=Zinc 1 +P25491 UniProtKB Metal binding 204 204 . . . Note=Zinc 1 +P25491 UniProtKB Binding site 116 116 . . . Note=Substrate%3B via amide nitrogen +P25491 UniProtKB Site 335 335 . . . Note=Involved in dimerization +P25491 UniProtKB Modified residue 406 406 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25491 UniProtKB Lipidation 406 406 . . . Note=S-farnesyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1527016;Dbxref=PMID:1527016 +P25491 UniProtKB Cross-link 198 198 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25491 UniProtKB Mutagenesis 335 335 . . . Note=Prevents dimerization. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14656432;Dbxref=PMID:14656432 +P25491 UniProtKB Beta strand 116 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT +P25491 UniProtKB Helix 126 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT +P25491 UniProtKB Beta strand 131 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT +P25491 UniProtKB Turn 144 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT +P25491 UniProtKB Beta strand 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT +P25491 UniProtKB Turn 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT +P25491 UniProtKB Beta strand 162 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT +P25491 UniProtKB Beta strand 168 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT +P25491 UniProtKB Beta strand 189 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT +P25491 UniProtKB Beta strand 202 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT +P25491 UniProtKB Beta strand 209 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT +P25491 UniProtKB Beta strand 229 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT +P25491 UniProtKB Beta strand 247 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT +P25491 UniProtKB Beta strand 260 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XAO +P25491 UniProtKB Beta strand 265 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XAO +P25491 UniProtKB Helix 274 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XAO +P25491 UniProtKB Beta strand 281 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XAO +P25491 UniProtKB Beta strand 288 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT +P25491 UniProtKB Beta strand 292 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XAO +P25491 UniProtKB Turn 299 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT +P25491 UniProtKB Beta strand 308 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XAO +P25491 UniProtKB Beta strand 319 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NLT +P25491 UniProtKB Beta strand 327 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XAO +P25491 UniProtKB Helix 343 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XAO +P25491 UniProtKB Beta strand 367 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XAO +##sequence-region P16521 1 1044 +P16521 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:9298649;Dbxref=PMID:22814378,PMID:9298649 +P16521 UniProtKB Chain 2 1044 . . . ID=PRO_0000093458;Note=Elongation factor 3A +P16521 UniProtKB Repeat 5 42 . . . Note=HEAT 1 +P16521 UniProtKB Repeat 86 123 . . . Note=HEAT 2 +P16521 UniProtKB Repeat 125 162 . . . Note=HEAT 3 +P16521 UniProtKB Repeat 166 203 . . . Note=HEAT 4 +P16521 UniProtKB Repeat 205 241 . . . Note=HEAT 5 +P16521 UniProtKB Repeat 242 279 . . . Note=HEAT 6 +P16521 UniProtKB Repeat 285 323 . . . Note=HEAT 7 +P16521 UniProtKB Domain 426 641 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P16521 UniProtKB Domain 667 993 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P16521 UniProtKB Nucleotide binding 463 470 . . . Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P16521 UniProtKB Nucleotide binding 701 708 . . . Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P16521 UniProtKB Compositional bias 1009 1031 . . . Note=Lys-rich (basic) +P16521 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:9298649;Dbxref=PMID:22814378,PMID:9298649 +P16521 UniProtKB Modified residue 187 187 . . . Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22522802;Dbxref=PMID:22522802 +P16521 UniProtKB Modified residue 196 196 . . . Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22522802;Dbxref=PMID:22522802 +P16521 UniProtKB Modified residue 642 642 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P16521 UniProtKB Modified residue 789 789 . . . Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22522802;Dbxref=PMID:22522802 +P16521 UniProtKB Modified residue 972 972 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P16521 UniProtKB Modified residue 974 974 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P16521 UniProtKB Modified residue 1039 1039 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P16521 UniProtKB Modified residue 1040 1040 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P16521 UniProtKB Cross-link 350 350 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P16521 UniProtKB Cross-link 636 636 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P16521 UniProtKB Mutagenesis 650 650 . . . Note=Reduces ATPase activity and interaction with eEF1A. Required for growth at 37 degrees Celsius and causes a 50%25 reduction of total protein synthesis at permissive temperatures. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12493761;Dbxref=PMID:12493761 +P16521 UniProtKB Sequence conflict 153 153 . . . Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16521 UniProtKB Sequence conflict 153 153 . . . Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16521 UniProtKB Sequence conflict 153 153 . . . Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16521 UniProtKB Sequence conflict 332 332 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16521 UniProtKB Sequence conflict 332 332 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16521 UniProtKB Sequence conflict 332 332 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16521 UniProtKB Helix 3 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Turn 23 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 26 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 42 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 48 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 61 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Turn 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Turn 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 85 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 92 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 104 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 123 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 126 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 143 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 161 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 184 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 198 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Turn 204 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 210 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 222 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 241 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 257 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 260 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 280 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 284 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 291 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Turn 298 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 304 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Turn 325 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 338 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Turn 349 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 356 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 359 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 380 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 388 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Turn 392 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 397 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 426 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 430 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 443 454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 458 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 469 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Turn 487 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 492 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 508 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Turn 514 516 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IX3 +P16521 UniProtKB Helix 520 529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 534 538 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 541 543 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 546 559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 563 569 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Turn 570 573 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 576 588 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 591 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 600 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 608 614 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 617 623 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 625 631 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 633 637 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 638 640 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Turn 641 643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 664 674 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 679 681 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IX3 +P16521 UniProtKB Beta strand 683 692 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 696 699 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 705 714 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 721 727 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 733 736 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 738 743 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 744 746 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 752 759 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Turn 760 762 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Turn 766 772 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 783 785 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 788 790 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 793 806 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 809 821 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 828 831 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 834 836 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 838 841 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 842 844 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 846 863 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 872 881 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 886 891 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 894 896 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 899 911 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 916 921 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 923 925 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 929 940 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 943 949 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Helix 953 956 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Turn 957 959 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +P16521 UniProtKB Beta strand 962 964 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IW3 +##sequence-region P11484 1 613 +P11484 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P11484 UniProtKB Chain 2 613 . . . ID=PRO_0000078389;Note=Ribosome-associated molecular chaperone SSB1 +P11484 UniProtKB Nucleotide binding 16 18 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5 +P11484 UniProtKB Nucleotide binding 205 207 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5 +P11484 UniProtKB Nucleotide binding 271 278 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5 +P11484 UniProtKB Region 2 391 . . . Note=Nucleotide binding domain (NBD);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5 +P11484 UniProtKB Region 392 402 . . . Note=Inter-domain linker;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5 +P11484 UniProtKB Region 403 613 . . . Note=Substrate binding domain (SBD);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5 +P11484 UniProtKB Region 516 612 . . . Note=Lid domain (SBDalpha);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5 +P11484 UniProtKB Region 601 613 . . . Note=Required for interaction with ribosomes;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27917864;Dbxref=PMID:27917864 +P11484 UniProtKB Motif 428 430 . . . Note=Contributes to ribosome binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27917864;Dbxref=PMID:27917864 +P11484 UniProtKB Motif 574 582 . . . Note=Nuclear export signal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10347213;Dbxref=PMID:10347213 +P11484 UniProtKB Binding site 73 73 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5 +P11484 UniProtKB Binding site 342 342 . . . Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5 +P11484 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P11484 UniProtKB Modified residue 47 47 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P11484 UniProtKB Modified residue 431 431 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P11484 UniProtKB Mutagenesis 73 73 . . . Note=Unable to hydrolyze ATP and moderately reduces ribosome binding. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27882919;Dbxref=PMID:27882919 +P11484 UniProtKB Mutagenesis 567 568 . . . Note=In SSB1-L(BC): Reduces ribosome-binding to less than 50%25. KR->EE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27882919;Dbxref=PMID:27882919 +P11484 UniProtKB Mutagenesis 596 597 . . . Note=In SSB1-D1: Reduces ribosome-binding to less than 50%25. RK->DD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27882919;Dbxref=PMID:27882919 +P11484 UniProtKB Mutagenesis 603 604 . . . Note=In SSB1-D2: Reduces ribosome-binding to less than 50%25. KR->DD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27882919;Dbxref=PMID:27882919 +P11484 UniProtKB Sequence conflict 180 184 . . . Note=AAAIA->VVVIV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11484 UniProtKB Sequence conflict 189 189 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11484 UniProtKB Sequence conflict 192 192 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11484 UniProtKB Beta strand 10 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Beta strand 16 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Beta strand 38 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Beta strand 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Beta strand 51 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Helix 55 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Helix 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Helix 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Helix 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Turn 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Helix 83 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Beta strand 93 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Beta strand 102 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Beta strand 112 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Helix 118 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Beta strand 143 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Helix 154 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Beta strand 170 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Helix 177 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Turn 185 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Beta strand 196 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Beta strand 208 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Beta strand 219 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Helix 233 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Helix 260 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Turn 277 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Beta strand 280 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Beta strand 294 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Helix 302 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Helix 310 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Helix 317 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Helix 331 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Beta strand 336 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Helix 342 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Helix 347 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Turn 357 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Turn 368 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +P11484 UniProtKB Helix 371 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GL1 +##sequence-region P39940 1 809 +P39940 UniProtKB Chain 1 809 . . . ID=PRO_0000120335;Note=E3 ubiquitin-protein ligase RSP5 +P39940 UniProtKB Domain 1 88 . . . Note=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 +P39940 UniProtKB Domain 229 262 . . . Note=WW 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00224 +P39940 UniProtKB Domain 331 364 . . . Note=WW 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00224 +P39940 UniProtKB Domain 387 420 . . . Note=WW 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00224 +P39940 UniProtKB Domain 705 809 . . . Note=HECT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00104 +P39940 UniProtKB Compositional bias 315 322 . . . Note=Poly-Ala +P39940 UniProtKB Active site 777 777 . . . Note=Glycyl thioester intermediate +P39940 UniProtKB Cross-link 258 258 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P39940 UniProtKB Mutagenesis 516 516 . . . Note=Has subtle defects on both initial ubiquitination and chain elongation of substrate proteins. Y->A +P39940 UniProtKB Mutagenesis 521 521 . . . Note=Has defects on both initial ubiquitination and chain elongation of substrate proteins. Y->A +P39940 UniProtKB Mutagenesis 537 537 . . . Note=Has defects on both initial ubiquitination and chain elongation of substrate proteins. I->D +P39940 UniProtKB Mutagenesis 618 618 . . . Note=Has defects on both initial ubiquitination and chain elongation of substrate proteins. F->D +P39940 UniProtKB Mutagenesis 733 733 . . . Note=In RSP5-1%3B impairs ubiquitin-thioester formation and catalysis of substrate ubiquitination. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9858558;Dbxref=PMID:9858558 +P39940 UniProtKB Mutagenesis 777 777 . . . Note=Loss of ubiquitination. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9858558;Dbxref=PMID:9858558 +P39940 UniProtKB Beta strand 393 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LCD +P39940 UniProtKB Beta strand 405 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OLM +P39940 UniProtKB Turn 408 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OLM +P39940 UniProtKB Beta strand 412 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OLM +P39940 UniProtKB Helix 435 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 446 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Beta strand 451 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 461 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 464 473 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 479 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Beta strand 482 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 496 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 514 516 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Beta strand 517 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Beta strand 526 531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 535 537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 541 557 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 568 574 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 581 586 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 589 600 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Turn 604 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Beta strand 610 617 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Beta strand 620 627 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 630 632 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Beta strand 633 635 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LCD +P39940 UniProtKB Turn 637 639 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 640 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Turn 653 656 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 657 668 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 673 676 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 681 689 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 696 701 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Beta strand 703 708 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 713 724 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 727 738 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 748 750 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Beta strand 754 757 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LCD +P39940 UniProtKB Beta strand 760 763 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Beta strand 773 775 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Turn 776 779 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Beta strand 780 782 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +P39940 UniProtKB Helix 789 801 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HPL +##sequence-region Q04437 1 629 +Q04437 UniProtKB Chain 1 629 . . . ID=PRO_0000084339;Note=ATP-dependent DNA helicase II subunit 2 +Q04437 UniProtKB Domain 254 476 . . . Note=Ku +Q04437 UniProtKB Natural variant 149 149 . . . Note=In strain: DBVPG6044%2C SK1 and YPS128. L->V +Q04437 UniProtKB Natural variant 301 301 . . . Note=In strain: DBVPG1853. S->L +Q04437 UniProtKB Natural variant 349 349 . . . Note=In strain: DBVPG6044%2C SK1 and YPS128. N->D +Q04437 UniProtKB Natural variant 499 499 . . . Note=In strain: DBVPG1853. G->D +Q04437 UniProtKB Natural variant 518 518 . . . Note=In strain: DBVPG6044%2C SK1 and YPS128. E->A +Q04437 UniProtKB Natural variant 528 528 . . . Note=In strain: DBVPG1853. T->A +Q04437 UniProtKB Natural variant 585 585 . . . Note=In strain: DBVPG6763. I->S +##sequence-region Q06224 1 779 +Q06224 UniProtKB Chain 1 779 . . . ID=PRO_0000076368;Note=Endoribonuclease YSH1 +Q06224 UniProtKB Active site 408 408 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06224 UniProtKB Metal binding 68 68 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06224 UniProtKB Metal binding 70 70 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06224 UniProtKB Metal binding 72 72 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06224 UniProtKB Metal binding 73 73 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06224 UniProtKB Metal binding 163 163 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06224 UniProtKB Metal binding 184 184 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06224 UniProtKB Metal binding 184 184 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06224 UniProtKB Metal binding 430 430 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06224 UniProtKB Modified residue 517 517 . . . Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06224 UniProtKB Mutagenesis 37 37 . . . Note=Loss of endonuclease activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037765;Dbxref=PMID:15037765 +Q06224 UniProtKB Mutagenesis 163 163 . . . Note=Loss of endonuclease activity. H->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037765;Dbxref=PMID:15037765 +Q06224 UniProtKB Mutagenesis 184 184 . . . Note=Loss of endonuclease activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037765;Dbxref=PMID:15037765 +Q06224 UniProtKB Mutagenesis 209 209 . . . Note=Loss of endonuclease activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037765;Dbxref=PMID:15037765 +Q06224 UniProtKB Mutagenesis 408 408 . . . Note=Loss of endonuclease activity. H->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037765;Dbxref=PMID:15037765 +##sequence-region P32795 1 747 +P32795 UniProtKB Chain 1 747 . . . ID=PRO_0000084664;Note=Mitochondrial inner membrane i-AAA protease supercomplex subunit YME1 +P32795 UniProtKB Nucleotide binding 321 328 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32795 UniProtKB Active site 541 541 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32795 UniProtKB Metal binding 540 540 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32795 UniProtKB Metal binding 544 544 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32795 UniProtKB Metal binding 618 618 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32795 UniProtKB Mutagenesis 327 327 . . . Note=Does not complement a YME1 deletion mutant%2C for K327R no longer binds or degrades COX2. Probably has no ATPase activity. K->I%2CR%2CT;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16527490,ECO:0000269|PubMed:8688560;Dbxref=PMID:16527490,PMID:8688560 +P32795 UniProtKB Mutagenesis 354 354 . . . Note=Partially complements a YME1 deletion mutant. Y->A%2CC%2CI%2CL%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16527490;Dbxref=PMID:16527490 +P32795 UniProtKB Mutagenesis 354 354 . . . Note=Complements a YME1 deletion mutant. Y->F%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16527490;Dbxref=PMID:16527490 +P32795 UniProtKB Mutagenesis 354 354 . . . Note=Does not complement a YME1 deletion mutant. Y->K%2CN%2CR%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16527490;Dbxref=PMID:16527490 +P32795 UniProtKB Mutagenesis 354 354 . . . Note=Does not complement a YME1 deletion mutant%2C retains 20%25 protease activity in vitro%2C binds an unfolded hybrid substrate protein. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16527490;Dbxref=PMID:16527490 +P32795 UniProtKB Mutagenesis 381 381 . . . Note=Does not complement a YME1 deletion mutant%2C no longer binds or degrades COX2. Probably has no ATPase activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16527490;Dbxref=PMID:16527490 +P32795 UniProtKB Mutagenesis 541 541 . . . Note=Does not complement a YME1 deletion mutant%2C for E541A stabilizes otherwise unstable COX2. E->A%2CG%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8688560;Dbxref=PMID:8688560 +P32795 UniProtKB Sequence conflict 52 52 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32795 UniProtKB Sequence conflict 88 88 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32795 UniProtKB Sequence conflict 584 584 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32795 UniProtKB Helix 102 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MV3 +P32795 UniProtKB Helix 118 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MV3 +P32795 UniProtKB Helix 134 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MV3 +P32795 UniProtKB Helix 150 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MV3 +P32795 UniProtKB Helix 166 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MV3 +##sequence-region Q06102 1 208 +Q06102 UniProtKB Chain 1 208 . . . ID=PRO_0000213910;Note=mRNA 3'-end-processing protein YTH1 +Q06102 UniProtKB Zinc finger 28 59 . . . Note=C3H1-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 +Q06102 UniProtKB Zinc finger 61 88 . . . Note=C3H1-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 +Q06102 UniProtKB Zinc finger 89 117 . . . Note=C3H1-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 +Q06102 UniProtKB Zinc finger 118 145 . . . Note=C3H1-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 +Q06102 UniProtKB Zinc finger 147 170 . . . Note=C3H1-type 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 +Q06102 UniProtKB Mutagenesis 67 67 . . . Note=Lethal. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10899131;Dbxref=PMID:10899131 +Q06102 UniProtKB Mutagenesis 70 70 . . . Note=Temperature- and formamide-sensitive%3B abolishes cleavage and polyadenylation activity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10899131;Dbxref=PMID:10899131 +Q06102 UniProtKB Mutagenesis 75 75 . . . Note=Lethal. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10899131;Dbxref=PMID:10899131 +Q06102 UniProtKB Mutagenesis 79 79 . . . Note=Temperature- and formamide-sensitive%3B impaired polyadenylation activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10899131;Dbxref=PMID:10899131 +Q06102 UniProtKB Mutagenesis 81 81 . . . Note=Lethal. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10899131;Dbxref=PMID:10899131 +Q06102 UniProtKB Mutagenesis 142 142 . . . Note=Temperature- and formamide-sensitive%3B impaired polyadenylation activity. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10899131;Dbxref=PMID:10899131 +##sequence-region P02829 1 709 +P02829 UniProtKB Chain 1 709 . . . ID=PRO_0000062957;Note=ATP-dependent molecular chaperone HSP82 +P02829 UniProtKB Repeat 221 225 . . . Note=1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10786835;Dbxref=PMID:10786835 +P02829 UniProtKB Repeat 226 230 . . . Note=2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10786835;Dbxref=PMID:10786835 +P02829 UniProtKB Repeat 231 235 . . . Note=3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10786835;Dbxref=PMID:10786835 +P02829 UniProtKB Repeat 237 241 . . . Note=4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10786835;Dbxref=PMID:10786835 +P02829 UniProtKB Repeat 250 254 . . . Note=5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10786835;Dbxref=PMID:10786835 +P02829 UniProtKB Nucleotide binding 99 100 . . . Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188 +P02829 UniProtKB Nucleotide binding 119 124 . . . Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188 +P02829 UniProtKB Region 221 263 . . . Note=5 X 5 AA repeats of [DE]-[DE]-[DE]-K-K%3B highly charged region +P02829 UniProtKB Motif 705 709 . . . Note=TPR repeat-binding +P02829 UniProtKB Binding site 33 33 . . . Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188 +P02829 UniProtKB Binding site 37 37 . . . Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188 +P02829 UniProtKB Binding site 79 79 . . . Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188 +P02829 UniProtKB Binding site 84 84 . . . Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188 +P02829 UniProtKB Binding site 92 92 . . . Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188 +P02829 UniProtKB Binding site 98 98 . . . Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188 +P02829 UniProtKB Binding site 171 171 . . . Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188 +P02829 UniProtKB Binding site 380 380 . . . Note=ATP;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2CG9,ECO:0000269|PubMed:16625188;Dbxref=PMID:16625188 +P02829 UniProtKB Modified residue 657 657 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15108 +P02829 UniProtKB Mutagenesis 22 22 . . . Note=Induces a 6-fold increase in ATPase activity and a reduced client protein activation activity%2C leading to growth defect at high temperatures. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7791797;Dbxref=PMID:7791797 +P02829 UniProtKB Mutagenesis 41 41 . . . Note=Causes a 98%25 reduction in ATPase activity and a reduced client protein activation activity%2C leading to growth defect at high temperatures. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7791797;Dbxref=PMID:7791797 +P02829 UniProtKB Mutagenesis 81 81 . . . Note=Reduces client protein activation activity%2C leading to growth defect at high temperatures. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7791797;Dbxref=PMID:7791797 +P02829 UniProtKB Mutagenesis 83 83 . . . Note=Abolishes ATPase activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18256191;Dbxref=PMID:18256191 +P02829 UniProtKB Mutagenesis 97 97 . . . Note=Abolishes interaction with SBA1. A->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9632755;Dbxref=PMID:9632755 +P02829 UniProtKB Mutagenesis 101 101 . . . Note=Causes a 90%25 reduction in ATPase activity and a reduced client protein activation activity%2C leading to growth defect at high temperatures. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7791797;Dbxref=PMID:7791797 +P02829 UniProtKB Mutagenesis 107 107 . . . Note=Induces a 6-fold increase in ATPase activity. A->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10944121;Dbxref=PMID:10944121 +P02829 UniProtKB Mutagenesis 170 170 . . . Note=Induces a total loss of function at 34 degrees Celsius. Abolishes interaction with SBA1. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7791797;Dbxref=PMID:7791797 +P02829 UniProtKB Mutagenesis 313 313 . . . Note=Reduces client protein activation activity%2C leading to growth defect at high temperatures. G->N%2CS;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7791797,ECO:0000269|PubMed:8248264;Dbxref=PMID:7791797,PMID:8248264 +P02829 UniProtKB Mutagenesis 349 349 . . . Note=Induces a loss of ATPase activity. Can be reactivated by AHA1. F->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12667448;Dbxref=PMID:12667448 +P02829 UniProtKB Mutagenesis 380 380 . . . Note=Induces a loss of ATPase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12667448;Dbxref=PMID:12667448 +P02829 UniProtKB Mutagenesis 381 381 . . . Note=Reduces client protein activation activity. Resistant to ATPase activation by AHA1. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7791797;Dbxref=PMID:7791797 +P02829 UniProtKB Mutagenesis 384 384 . . . Note=Induces a loss of ATPase activity. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12667448;Dbxref=PMID:12667448 +P02829 UniProtKB Mutagenesis 387 387 . . . Note=Decreases AHA1 binding affinity%2C but has no effect on client protein activation activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14739935;Dbxref=PMID:14739935 +P02829 UniProtKB Mutagenesis 387 387 . . . Note=Decreases AHA1 binding affinity and substantially reduces client protein activation activity. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14739935;Dbxref=PMID:14739935 +P02829 UniProtKB Mutagenesis 431 431 . . . Note=Specifically reduces the activation of the exogenous ligand glucocorticoid receptor. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8248264;Dbxref=PMID:8248264 +P02829 UniProtKB Mutagenesis 485 485 . . . Note=Abolishes interaction with SBA1. S->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9632755;Dbxref=PMID:9632755 +P02829 UniProtKB Mutagenesis 525 525 . . . Note=Abolishes interaction with SBA1. Reduces client protein activation activity%2C leading to growth defect at high temperatures. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8248264;Dbxref=PMID:8248264 +P02829 UniProtKB Mutagenesis 576 576 . . . Note=Reduces client protein activation activity%3B when associated with K-579. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8248264;Dbxref=PMID:8248264 +P02829 UniProtKB Mutagenesis 577 577 . . . Note=Enhances ATPase activity and client protein activation. A->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19696785;Dbxref=PMID:19696785 +P02829 UniProtKB Mutagenesis 577 577 . . . Note=Reduces ATPase activity and client protein activation. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19696785;Dbxref=PMID:19696785 +P02829 UniProtKB Mutagenesis 577 577 . . . Note=Enhances homodimerization%2C ATPase activity and client protein activation. A->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19696785;Dbxref=PMID:19696785 +P02829 UniProtKB Mutagenesis 577 577 . . . Note=Reduces homodimerization%2C ATPase activity and client protein activation. A->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19696785;Dbxref=PMID:19696785 +P02829 UniProtKB Mutagenesis 579 579 . . . Note=Reduces client protein activation activity%3B when associated with T-576. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8248264;Dbxref=PMID:8248264 +P02829 UniProtKB Mutagenesis 587 587 . . . Note=No effect on ATPase activity. Reduces client protein activation activity%2C leading to growth defect at high temperatures. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7791797;Dbxref=PMID:7791797 +P02829 UniProtKB Sequence conflict 481 481 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02829 UniProtKB Beta strand 4 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Helix 10 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Helix 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ASB +P02829 UniProtKB Helix 29 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Turn 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Helix 53 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Beta strand 64 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Helix 70 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Beta strand 74 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Helix 86 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Turn 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BRC +P02829 UniProtKB Helix 101 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Helix 114 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Helix 123 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Beta strand 131 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Beta strand 146 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Beta strand 152 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Beta strand 162 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Beta strand 168 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Helix 182 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Helix 187 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Beta strand 200 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AKP +P02829 UniProtKB Beta strand 205 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IWX +P02829 UniProtKB Helix 276 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Helix 281 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Helix 286 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Beta strand 304 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Beta strand 313 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Beta strand 317 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Turn 329 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Beta strand 335 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9 +P02829 UniProtKB Beta strand 341 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Beta strand 348 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Beta strand 355 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HK7 +P02829 UniProtKB Helix 360 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Beta strand 366 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Helix 380 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HK7 +P02829 UniProtKB Helix 387 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Helix 411 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Turn 433 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Helix 436 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Beta strand 444 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Beta strand 450 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Helix 457 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Beta strand 470 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Helix 479 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Helix 488 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Beta strand 498 501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Helix 504 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Beta strand 519 523 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +P02829 UniProtKB Turn 524 526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HK7 +P02829 UniProtKB Beta strand 530 533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE +P02829 UniProtKB Helix 535 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE +P02829 UniProtKB Beta strand 563 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE +P02829 UniProtKB Beta strand 573 580 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE +P02829 UniProtKB Beta strand 582 584 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE +P02829 UniProtKB Helix 587 597 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE +P02829 UniProtKB Beta strand 600 602 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE +P02829 UniProtKB Beta strand 611 615 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE +P02829 UniProtKB Helix 620 629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE +P02829 UniProtKB Turn 630 632 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE +P02829 UniProtKB Helix 633 635 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE +P02829 UniProtKB Helix 637 653 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE +P02829 UniProtKB Helix 661 676 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CGE +##sequence-region P38801 1 184 +P38801 UniProtKB Chain 1 184 . . . ID=PRO_0000202902;Note=Exosome complex protein LRP1 +P38801 UniProtKB Helix 4 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFC +P38801 UniProtKB Helix 8 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFC +P38801 UniProtKB Helix 33 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFC +P38801 UniProtKB Helix 43 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFC +P38801 UniProtKB Helix 74 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFC +##sequence-region P40009 1 630 +P40009 UniProtKB Chain 1 630 . . . ID=PRO_0000209920;Note=Golgi apyrase +P40009 UniProtKB Topological domain 1 500 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40009 UniProtKB Transmembrane 501 517 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40009 UniProtKB Topological domain 518 630 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40009 UniProtKB Active site 152 152 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40009 UniProtKB Mutagenesis 152 152 . . . Note=Expressed at lower levels. GTPase activity reduced. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16227198;Dbxref=PMID:16227198 +P40009 UniProtKB Mutagenesis 189 189 . . . Note=Expressed at the same level as wild-type. GTPase and GDPase activities decreased more than 20-fold toward GTP and 3-fold for GDP. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16227198;Dbxref=PMID:16227198 +P40009 UniProtKB Sequence conflict 498 498 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P10591 1 642 +P10591 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P10591 UniProtKB Chain 2 642 . . . ID=PRO_0000078385;Note=Heat shock protein SSA1 +P10591 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P10591 UniProtKB Modified residue 62 62 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P10591 UniProtKB Modified residue 551 551 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P10591 UniProtKB Modified residue 603 603 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P10591 UniProtKB Cross-link 556 556 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P10591 UniProtKB Sequence conflict 208 208 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10591 UniProtKB Sequence conflict 418 418 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10591 UniProtKB Sequence conflict 422 422 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38340 1 232 +P38340 UniProtKB Chain 1 232 . . . ID=PRO_0000119292;Note=Alpha N-terminal protein methyltransferase 1 +P38340 UniProtKB Region 123 124 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38340 UniProtKB Binding site 71 71 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38340 UniProtKB Binding site 76 76 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38340 UniProtKB Binding site 139 139 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P41800 1 426 +P41800 UniProtKB Chain 1 426 . . . ID=PRO_0000096506;Note=Maintenance of mitochondrial morphology protein 1 +P41800 UniProtKB Topological domain 1 100 . . . Note=Lumenal +P41800 UniProtKB Transmembrane 101 121 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03103 +P41800 UniProtKB Topological domain 122 426 . . . Note=Cytoplasmic +P41800 UniProtKB Glycosylation 6 6 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03103 +P41800 UniProtKB Glycosylation 50 50 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03103 +P41800 UniProtKB Glycosylation 55 55 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03103 +P41800 UniProtKB Glycosylation 59 59 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03103 +P41800 UniProtKB Mutagenesis 215 215 . . . Note=In MMM1-6%3B impairs both mtDNA maintenance and mitochondrial morpholgy. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12454062;Dbxref=PMID:12454062 +P41800 UniProtKB Sequence conflict 200 200 . . . Note=W->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41800 UniProtKB Sequence conflict 225 225 . . . Note=S->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41800 UniProtKB Sequence conflict 357 357 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41800 UniProtKB Sequence conflict 365 365 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41800 UniProtKB Sequence conflict 368 368 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P00546 1 298 +P00546 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P00546 UniProtKB Chain 2 298 . . . ID=PRO_0000085722;Note=Cyclin-dependent kinase 1 +P00546 UniProtKB Domain 8 295 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P00546 UniProtKB Nucleotide binding 14 22 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P00546 UniProtKB Active site 136 136 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P00546 UniProtKB Binding site 40 40 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P00546 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P00546 UniProtKB Modified residue 19 19 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00546 UniProtKB Modified residue 169 169 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P15108 1 705 +P15108 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7483834;Dbxref=PMID:7483834 +P15108 UniProtKB Chain 2 705 . . . ID=PRO_0000062958;Note=ATP-dependent molecular chaperone HSC82 +P15108 UniProtKB Repeat 221 225 . . . Note=1 +P15108 UniProtKB Repeat 226 230 . . . Note=2 +P15108 UniProtKB Repeat 232 236 . . . Note=3 +P15108 UniProtKB Repeat 246 250 . . . Note=4 +P15108 UniProtKB Region 221 259 . . . Note=4 X 5 AA repeats of [DE]-[DE]-[DE]-K-K%3B highly charged region +P15108 UniProtKB Motif 701 705 . . . Note=TPR repeat-binding +P15108 UniProtKB Binding site 37 37 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15108 UniProtKB Binding site 79 79 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15108 UniProtKB Binding site 98 98 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15108 UniProtKB Binding site 124 124 . . . Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15108 UniProtKB Binding site 376 376 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15108 UniProtKB Modified residue 653 653 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P15108 UniProtKB Mutagenesis 453 453 . . . Note=Leads to growth defect at 37 degrees Celsius%2C probably by disrupting the intramolecular interaction of the N-termini with the middle domains%3B when associated with A-493. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12121981;Dbxref=PMID:12121981 +P15108 UniProtKB Mutagenesis 493 493 . . . Note=Leads to growth defect at 37 degrees Celsius%2C probably by disrupting the intramolecular interaction of the N-termini with the middle domains%3B when associated with A-453. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12121981;Dbxref=PMID:12121981 +P15108 UniProtKB Sequence conflict 619 619 . . . Note=K->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15108 UniProtKB Sequence conflict 621 621 . . . Note=L->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P31539 1 908 +P31539 UniProtKB Chain 1 908 . . . ID=PRO_0000191212;Note=Heat shock protein 104 +P31539 UniProtKB Nucleotide binding 212 219 . . . Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31539 UniProtKB Nucleotide binding 614 621 . . . Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31539 UniProtKB Region 167 411 . . . Note=NBD1 +P31539 UniProtKB Region 541 731 . . . Note=NBD2 +P31539 UniProtKB Region 905 908 . . . Note=Interaction surface for TPR repeats +P31539 UniProtKB Coiled coil 412 536 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31539 UniProtKB Motif 773 789 . . . Note=Nuclear localization signal +P31539 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P31539 UniProtKB Modified residue 206 206 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P31539 UniProtKB Modified residue 306 306 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P31539 UniProtKB Modified residue 499 499 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P31539 UniProtKB Modified residue 535 535 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P31539 UniProtKB Cross-link 442 442 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P31539 UniProtKB Cross-link 620 620 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14557538;Dbxref=PMID:14557538 +P31539 UniProtKB Mutagenesis 184 184 . . . Note=Confers resistance to prion-curing by guanidine. D->A%2CD%2CF%2CN%2CL%2CQ%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12105276;Dbxref=PMID:12105276 +P31539 UniProtKB Mutagenesis 184 184 . . . Note=Impairs prion propagation. D->K%2CW%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12105276;Dbxref=PMID:12105276 +P31539 UniProtKB Mutagenesis 217 217 . . . Note=Largely reduces ATP hydrolysis. Alters bud morphology and causes septin mislocalization%3B when associated with I-499. G->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11158570,ECO:0000269|PubMed:14978213,ECO:0000269|PubMed:9624144;Dbxref=PMID:11158570,PMID:14978213,PMID:9624144 +P31539 UniProtKB Mutagenesis 217 217 . . . Note=Completely abolishes ATP hydrolysis. G->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11158570,ECO:0000269|PubMed:14978213,ECO:0000269|PubMed:9624144;Dbxref=PMID:11158570,PMID:14978213,PMID:9624144 +P31539 UniProtKB Mutagenesis 218 218 . . . Note=Abolishes substrate binding. Unable to confer thermotolerance. Reduces ATP hydrolysis by 98%25%3B when associated with T-315. Comletely abolishes ATPase activity%3B when associated with T-620. K->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11158570,ECO:0000269|PubMed:11442834,ECO:0000269|PubMed:11983167,ECO:0000269|PubMed:12101251,ECO:0000269|PubMed:16135516,ECO:0000269|PubMed:17259993,ECO:0000269|PubMed:17543332,ECO:0000269|PubMed:1896074,ECO:0000269|PubMed:8308017,ECO:0000269|PubMed:9624144;Dbxref=PMID:11158570,PMID:11442834,PMID:11983167,PMID:12101251,PMID:16135516,PMID:17259993,PMID:17543332,PMID:1896074,PMID:8308017,PMID:9624144 +P31539 UniProtKB Mutagenesis 257 257 . . . Note=Reduces thermotolerance 10-fold. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15128736;Dbxref=PMID:15128736 +P31539 UniProtKB Mutagenesis 285 285 . . . Note=In HSP104(TRAP)%3B completely abolishes ATP hydrolysis%2C but does not affect nucleotide binding%2C thus keeping HSP104 in an ATP-bound state%3B when associated with Q-687. E->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16135516,ECO:0000269|PubMed:17543332;Dbxref=PMID:16135516,PMID:17543332 +P31539 UniProtKB Mutagenesis 315 315 . . . Note=Reduces ATP hydrolysis by 98%25%3B when associated with T-218. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983167;Dbxref=PMID:11983167 +P31539 UniProtKB Mutagenesis 317 317 . . . Note=Reduces rate of ATP hydrolysis at NBD1 nearly 10-fold. No effect on oligomerization. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11782421,ECO:0000269|PubMed:17259993;Dbxref=PMID:11782421,PMID:17259993 +P31539 UniProtKB Mutagenesis 334 334 . . . Note=Reduces ATPase activity by 80%25. Impairs oligomerization. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18160044;Dbxref=PMID:18160044 +P31539 UniProtKB Mutagenesis 419 419 . . . Note=Reduces ATPase activity by 80%25. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18160044;Dbxref=PMID:18160044 +P31539 UniProtKB Mutagenesis 444 444 . . . Note=Reduces ATPase activity by 80%25. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18160044;Dbxref=PMID:18160044 +P31539 UniProtKB Mutagenesis 462 462 . . . Note=Impairs prion propagation%2C but does not affect thermotolerance. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17367387;Dbxref=PMID:17367387 +P31539 UniProtKB Mutagenesis 495 495 . . . Note=Increases ATPase activity 3-fold. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18160044;Dbxref=PMID:18160044 +P31539 UniProtKB Mutagenesis 499 499 . . . Note=Reduces ATP hydrolysis by 50%25. Alters bud morphology and causes septin mislocalization%3B when associated with S-217. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14978213;Dbxref=PMID:14978213 +P31539 UniProtKB Mutagenesis 503 503 . . . Note=Increases basal level of ATPase activity and abolishes stimulation of ATP hydrolysis upon substrate binding. Inhibits growth at 37 degrees Celsius. A->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11983167,ECO:0000269|PubMed:14978213;Dbxref=PMID:11983167,PMID:14978213 +P31539 UniProtKB Mutagenesis 509 509 . . . Note=Reduces thermotolerance. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14978213;Dbxref=PMID:14978213 +P31539 UniProtKB Mutagenesis 557 557 . . . Note=Impairs prion propagation%2C but does not affect thermotolerance. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17367387;Dbxref=PMID:17367387 +P31539 UniProtKB Mutagenesis 619 619 . . . Note=Impairs oligomerization at low protein concentrations. G->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11158570,ECO:0000269|PubMed:9624144;Dbxref=PMID:11158570,PMID:9624144 +P31539 UniProtKB Mutagenesis 620 620 . . . Note=Impairs oligomerization at low protein concentrations. Reduces ATP hydrolysis rate. Unable to confer thermotolerance. Comletely abolishes ATPase activity%3B when associated with T-218. K->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11158570,ECO:0000269|PubMed:11442834,ECO:0000269|PubMed:12101251,ECO:0000269|PubMed:16135516,ECO:0000269|PubMed:17259993,ECO:0000269|PubMed:17543332,ECO:0000269|PubMed:1896074,ECO:0000269|PubMed:8308017,ECO:0000269|PubMed:9624144;Dbxref=PMID:11158570,PMID:11442834,PMID:12101251,PMID:16135516,PMID:17259993,PMID:17543332,PMID:1896074,PMID:8308017,PMID:9624144 +P31539 UniProtKB Mutagenesis 621 621 . . . Note=Reduces ATP hydrolysis%2C but does not affect oligomerization. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11158570;Dbxref=PMID:11158570 +P31539 UniProtKB Mutagenesis 645 645 . . . Note=Abolishes the ability to refold aggregated protein in vitro and to provide thermotolerance in vivo. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15128736;Dbxref=PMID:15128736 +P31539 UniProtKB Mutagenesis 662 662 . . . Note=Abolishes the ability to refold aggregated protein in vitro and to provide thermotolerance in vivo. Y->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15128736;Dbxref=PMID:15128736 +P31539 UniProtKB Mutagenesis 662 662 . . . Note=No effect. Y->F%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15128736;Dbxref=PMID:15128736 +P31539 UniProtKB Mutagenesis 687 687 . . . Note=In HSP104(TRAP)%3B completely abolishes ATP hydrolysis%2C but does not affect nucleotide binding%2C thus keeping HSP104 in an ATP-bound state%3B when associated with Q-285. E->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16135516,ECO:0000269|PubMed:17543332;Dbxref=PMID:16135516,PMID:17543332 +P31539 UniProtKB Mutagenesis 704 704 . . . Note=Impairs prion propagation%2C but does not affect thermotolerance. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17367387;Dbxref=PMID:17367387 +P31539 UniProtKB Mutagenesis 728 728 . . . Note=Almost completely abolishes ATP hydrolysis at NBD2%2C but does not affect nucleotide binding%2C thus keeping NBD2 in an ATP-bound state. Reduces stimulation of ATP hydrolysis upon substrate binding. N->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11782421,ECO:0000269|PubMed:11983167,ECO:0000269|PubMed:17259993,ECO:0000269|PubMed:18160044;Dbxref=PMID:11782421,PMID:11983167,PMID:17259993,PMID:18160044 +P31539 UniProtKB Mutagenesis 765 765 . . . Note=Can oligomerize in the absence of nucleotides. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18160044;Dbxref=PMID:18160044 +P31539 UniProtKB Mutagenesis 778 778 . . . Note=In NLS17KA%3B fails to concentrate in the nucleus%3B when associated with A-782 and A-789. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17973656;Dbxref=PMID:17973656 +P31539 UniProtKB Mutagenesis 782 782 . . . Note=In NLS17KA%3B fails to concentrate in the nucleus%3B when associated with A-778 and A-789. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17973656;Dbxref=PMID:17973656 +P31539 UniProtKB Mutagenesis 789 789 . . . Note=In NLS17KA%3B fails to concentrate in the nucleus%3B when associated with A-778 and A-782. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17973656;Dbxref=PMID:17973656 +P31539 UniProtKB Mutagenesis 819 819 . . . Note=Site-specific fluorescent probe in an otherwise Trp-less HSP104. Fluorescence of this Trp changes in response to ATP and ADP binding at NBD2. Has no effect on ATP hydrolysis or protein stability. Y->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11867765;Dbxref=PMID:11867765 +P31539 UniProtKB Mutagenesis 826 826 . . . Note=Reduces ATP and ADP binding at NBD2 6-fold%2C but does not affect ATP hydrolysis at NBD2. Reduces catalytic rate at NBD1. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11867765;Dbxref=PMID:11867765 +P31539 UniProtKB Helix 9 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U +P31539 UniProtKB Beta strand 28 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U +P31539 UniProtKB Helix 32 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U +P31539 UniProtKB Helix 50 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U +P31539 UniProtKB Helix 62 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U +P31539 UniProtKB Helix 90 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U +P31539 UniProtKB Beta strand 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U +P31539 UniProtKB Helix 113 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U +P31539 UniProtKB Helix 124 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U +P31539 UniProtKB Helix 137 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U2U +##sequence-region P25623 1 870 +P25623 UniProtKB Chain 1 870 . . . ID=PRO_0000072390;Note=Suppressor of yeast profilin deletion +P25623 UniProtKB Domain 609 869 . . . Note=MHD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00404 +P25623 UniProtKB Compositional bias 308 405 . . . Note=Ser-rich +P25623 UniProtKB Compositional bias 417 528 . . . Note=Pro-rich +P25623 UniProtKB Modified residue 264 264 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P25623 UniProtKB Modified residue 331 331 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25623 UniProtKB Modified residue 416 416 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25623 UniProtKB Modified residue 496 496 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P25623 UniProtKB Modified residue 500 500 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P25623 UniProtKB Modified residue 577 577 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25623 UniProtKB Cross-link 256 256 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25623 UniProtKB Helix 7 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G +P25623 UniProtKB Turn 12 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G +P25623 UniProtKB Helix 18 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G +P25623 UniProtKB Helix 67 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G +P25623 UniProtKB Helix 83 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G +P25623 UniProtKB Helix 97 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G +P25623 UniProtKB Helix 127 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G +P25623 UniProtKB Beta strand 133 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G +P25623 UniProtKB Helix 138 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G +P25623 UniProtKB Helix 168 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G +P25623 UniProtKB Helix 233 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9G +P25623 UniProtKB Beta strand 611 625 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Beta strand 628 643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Beta strand 646 648 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Beta strand 654 661 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Helix 663 665 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Beta strand 666 671 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Turn 673 675 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Beta strand 676 680 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Beta strand 683 686 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Turn 688 691 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Beta strand 695 705 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Beta strand 709 718 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Beta strand 720 731 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Beta strand 741 753 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Beta strand 758 766 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Beta strand 771 773 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Beta strand 775 779 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Beta strand 784 787 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Beta strand 793 803 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Beta strand 812 818 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Turn 827 830 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Beta strand 836 845 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +P25623 UniProtKB Beta strand 856 869 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G9H +##sequence-region P08539 1 472 +P08539 UniProtKB Initiator methionine 1 1 . . . Note=Removed +P08539 UniProtKB Chain 2 472 . . . ID=PRO_0000203616;Note=Guanine nucleotide-binding protein alpha-1 subunit +P08539 UniProtKB Nucleotide binding 48 55 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08539 UniProtKB Nucleotide binding 294 300 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08539 UniProtKB Nucleotide binding 319 323 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08539 UniProtKB Nucleotide binding 388 391 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08539 UniProtKB Region 127 235 . . . Note=Insert%3B not present in other G-proteins +P08539 UniProtKB Metal binding 55 55 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08539 UniProtKB Metal binding 300 300 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08539 UniProtKB Binding site 444 444 . . . Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08539 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1936988,ECO:0000269|PubMed:8415763,ECO:0000269|PubMed:8702760;Dbxref=PMID:1936988,PMID:8415763,PMID:8702760 +P08539 UniProtKB Lipidation 3 3 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10712512,ECO:0000269|PubMed:8942643;Dbxref=PMID:10712512,PMID:8942643 +P08539 UniProtKB Cross-link 165 165 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11955054;Dbxref=PMID:11955054 +P08539 UniProtKB Mutagenesis 2 2 . . . Note=Abolishes both palmitoylation and N-myristoylation. G->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10712512,ECO:0000269|PubMed:8702760,ECO:0000269|PubMed:8942643;Dbxref=PMID:10712512,PMID:8702760,PMID:8942643 +P08539 UniProtKB Mutagenesis 3 3 . . . Note=Abolishes palmitoylation but not N-myristoylation. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10712512,ECO:0000269|PubMed:8942643;Dbxref=PMID:10712512,PMID:8942643 +P08539 UniProtKB Mutagenesis 15 15 . . . Note=Slightly reduces ligand-dependent pheromone signaling. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14767760;Dbxref=PMID:14767760 +P08539 UniProtKB Mutagenesis 17 17 . . . Note=Leads to a hypersensitive signaling phenotype resulting in greatly enhanced signal at low alpha-factor concentrations. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14767760;Dbxref=PMID:14767760 +P08539 UniProtKB Mutagenesis 18 18 . . . Note=Reduces ligand-dependent pheromone signaling. L->P%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14767760;Dbxref=PMID:14767760 +P08539 UniProtKB Mutagenesis 21 22 . . . Note=Impairs interaction with FUS3. KR->EE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12029138;Dbxref=PMID:12029138 +P08539 UniProtKB Mutagenesis 50 50 . . . Note=Confers insensitivity to pheromone. G->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10705368,ECO:0000269|PubMed:1900495,ECO:0000269|PubMed:2117698,ECO:0000269|PubMed:2548076;Dbxref=PMID:10705368,PMID:1900495,PMID:2117698,PMID:2548076 +P08539 UniProtKB Mutagenesis 50 50 . . . Note=Has increased GTP occupancy and moderately reduces hydrolysis of GTP%2C resulting in a constitutively active form that down-regulates the pheromone response and causes hyperadaptation to pheromone. G->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10705368,ECO:0000269|PubMed:1900495,ECO:0000269|PubMed:2117698,ECO:0000269|PubMed:2548076;Dbxref=PMID:10705368,PMID:1900495,PMID:2117698,PMID:2548076 +P08539 UniProtKB Mutagenesis 54 54 . . . Note=Prevents GDP to GTP exchange%3B suppressor of L-323. K->E%2CI;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14767760,ECO:0000269|PubMed:9786851;Dbxref=PMID:14767760,PMID:9786851 +P08539 UniProtKB Mutagenesis 165 165 . . . Note=Substantial decrease in ubiquitination. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11955054;Dbxref=PMID:11955054 +P08539 UniProtKB Mutagenesis 297 297 . . . Note=Slows hydrolysis of GTP. R->H +P08539 UniProtKB Mutagenesis 302 302 . . . Note=In GPA1(SST)%3B weakens interaction to SST2 and blocks its negative regulatory effect. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9488712;Dbxref=PMID:9488712 +P08539 UniProtKB Mutagenesis 321 321 . . . Note=Causes a specific mating defect in alpha cells. G->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9604890;Dbxref=PMID:9604890 +P08539 UniProtKB Mutagenesis 322 322 . . . Note=Confers insensitivity to pheromone. G->A%2CE%2CR;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1900495,ECO:0000269|PubMed:2117698,ECO:0000269|PubMed:8887662;Dbxref=PMID:1900495,PMID:2117698,PMID:8887662 +P08539 UniProtKB Mutagenesis 323 323 . . . Note=Prevents hydrolysis of GTP%3B eliminates the interaction with STE4 and constitutively activates the pheromone response pathway. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9604890;Dbxref=PMID:9604890 +P08539 UniProtKB Mutagenesis 327 327 . . . Note=Suppressor of L-323%3B does not prevent GTP binding to GPA1. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9786851;Dbxref=PMID:9786851 +P08539 UniProtKB Mutagenesis 345 345 . . . Note=Suppressor of a STE2-L236H mutant. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866688;Dbxref=PMID:10866688 +P08539 UniProtKB Mutagenesis 353 353 . . . Note=Suppressor of L-323. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9786851;Dbxref=PMID:9786851 +P08539 UniProtKB Mutagenesis 355 355 . . . Note=Confers insensitivity to pheromone. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2117698;Dbxref=PMID:2117698 +P08539 UniProtKB Mutagenesis 364 364 . . . Note=Enhances the rate of GDP for GTP exchange and slows hydrolysis of GTP%2C resulting in a constitutively active form that down-regulates the pheromone response independently of the pheromone receptor. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11394869,ECO:0000269|PubMed:2117698,ECO:0000269|PubMed:8887662;Dbxref=PMID:11394869,PMID:2117698,PMID:8887662 +P08539 UniProtKB Mutagenesis 388 388 . . . Note=Forms a nondissociable complex with the pheromone receptor in response to receptor activation%2C resulting in reduced pheromone responsiveness. N->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11394869,ECO:0000269|PubMed:15197187,ECO:0000269|PubMed:1900495,ECO:0000269|PubMed:8887662;Dbxref=PMID:11394869,PMID:15197187,PMID:1900495,PMID:8887662 +P08539 UniProtKB Mutagenesis 388 388 . . . Note=Causes constitutive activation of the pheromone response pathway. N->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11394869,ECO:0000269|PubMed:15197187,ECO:0000269|PubMed:1900495,ECO:0000269|PubMed:8887662;Dbxref=PMID:11394869,PMID:15197187,PMID:1900495,PMID:8887662 +P08539 UniProtKB Mutagenesis 391 391 . . . Note=Causes constitutive activation of the pheromone response pathway. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1900495;Dbxref=PMID:1900495 +P08539 UniProtKB Mutagenesis 467 467 . . . Note=Impairs pheromone signaling in a and alpha cells. K->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1848203;Dbxref=PMID:1848203 +P08539 UniProtKB Mutagenesis 468 468 . . . Note=Impairs pheromone signaling specifically in a cells. K->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1848203;Dbxref=PMID:1848203 +P08539 UniProtKB Mutagenesis 470 470 . . . Note=Confers insensitivity to pheromone. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2117698;Dbxref=PMID:2117698 +P08539 UniProtKB Sequence conflict 82 82 . . . Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08539 UniProtKB Sequence conflict 194 194 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08539 UniProtKB Sequence conflict 226 226 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08539 UniProtKB Sequence conflict 246 246 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08539 UniProtKB Sequence conflict 469 469 . . . Note=I->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32502 1 381 +P32502 UniProtKB Chain 1 381 . . . ID=PRO_0000156066;Note=Translation initiation factor eIF-2B subunit beta +##sequence-region P15442 1 1659 +P15442 UniProtKB Chain 1 1659 . . . ID=PRO_0000085963;Note=eIF-2-alpha kinase GCN2 +P15442 UniProtKB Domain 17 128 . . . Note=RWD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00179 +P15442 UniProtKB Domain 256 527 . . . Note=Protein kinase 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P15442 UniProtKB Domain 599 981 . . . Note=Protein kinase 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P15442 UniProtKB Nucleotide binding 605 613 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P15442 UniProtKB Region 999 1519 . . . Note=Histidyl-tRNA synthetase-like +P15442 UniProtKB Active site 835 835 . . . Note=Proton acceptor +P15442 UniProtKB Binding site 628 628 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P15442 UniProtKB Modified residue 761 761 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P15442 UniProtKB Modified residue 882 882 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528799;Dbxref=PMID:9528799 +P15442 UniProtKB Modified residue 887 887 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528799;Dbxref=PMID:9528799 +P15442 UniProtKB Mutagenesis 74 74 . . . Note=Inhibits interaction with GCN1%2C eIF-2-alpha phosphorylation and fails to derepress GCN4 translation in amino acid-starved cells. Y->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10801780,ECO:0000269|PubMed:11350982;Dbxref=PMID:10801780,PMID:11350982 +P15442 UniProtKB Mutagenesis 582 582 . . . Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107 +P15442 UniProtKB Mutagenesis 594 594 . . . Note=Inhibits autophosphorylation%2C eIF-2-alpha kinase activity and derepression of GCN4 translation. Restores eIF-2-alpha kinase activity and derepression of GCN4%2C but not autophosphorylation%3B when associated with R-598. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17202131;Dbxref=PMID:17202131 +P15442 UniProtKB Mutagenesis 598 598 . . . Note=Inhibits autophosphorylation%2C eIF-2-alpha kinase activity and derepression of GCN4 translation. Restores eIF-2-alpha kinase activity and derepression of GCN4%2C but not autophosphorylation%3B when associated with D-594. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17202131;Dbxref=PMID:17202131 +P15442 UniProtKB Mutagenesis 601 601 . . . Note=Increases the constitutive kinase activity in absence of amino acid starvation. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2188100;Dbxref=PMID:2188100 +P15442 UniProtKB Mutagenesis 628 628 . . . Note=Inhibits autophosphorylation%2C eIF-2-alpha kinase activity and derepression of GCN4 translation in amino acid-starved cells. K->V%2CR;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10983975,ECO:0000269|PubMed:17202131,ECO:0000269|PubMed:1739968,ECO:0000269|PubMed:2188100,ECO:0000269|PubMed:2660141,ECO:0000269|PubMed:8798780;Dbxref=PMID:10983975,PMID:17202131,PMID:1739968,PMID:2188100,PMID:2660141,PMID:8798780 +P15442 UniProtKB Mutagenesis 629 629 . . . Note=Does not abolish derepression of GCN4 translation and amino acid biosynthetic genes in amino acid-starved cells. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2660141;Dbxref=PMID:2660141 +P15442 UniProtKB Mutagenesis 716 716 . . . Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107 +P15442 UniProtKB Mutagenesis 788 788 . . . Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. M->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107 +P15442 UniProtKB Mutagenesis 794 794 . . . Note=Constitutively active allele%2C bypass the tRNA binding-requirement for kinase activity. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15964839;Dbxref=PMID:15964839 +P15442 UniProtKB Mutagenesis 803 803 . . . Note=Increases tRNA binding and the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. E->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10983975,ECO:0000269|PubMed:1448107;Dbxref=PMID:10983975,PMID:1448107 +P15442 UniProtKB Mutagenesis 821 821 . . . Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1448107,ECO:0000269|PubMed:2188100;Dbxref=PMID:1448107,PMID:2188100 +P15442 UniProtKB Mutagenesis 835 835 . . . Note=Loss of function. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15964839;Dbxref=PMID:15964839 +P15442 UniProtKB Mutagenesis 861 861 . . . Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107 +P15442 UniProtKB Mutagenesis 882 882 . . . Note=Partially impairs kinase activity. T->A%2CE%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528799;Dbxref=PMID:9528799 +P15442 UniProtKB Mutagenesis 882 882 . . . Note=No effect. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528799;Dbxref=PMID:9528799 +P15442 UniProtKB Mutagenesis 887 887 . . . Note=Completely abolishes kinase activity. T->A%2CE%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528799;Dbxref=PMID:9528799 +P15442 UniProtKB Mutagenesis 887 887 . . . Note=Partially impairs kinase activity. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528799;Dbxref=PMID:9528799 +P15442 UniProtKB Mutagenesis 1080 1080 . . . Note=Inhibits dimerization%3B when associated with A-1088 and A-1090. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11250908;Dbxref=PMID:11250908 +P15442 UniProtKB Mutagenesis 1088 1088 . . . Note=Inhibits dimerization%3B when associated with A-1080 and A-1090. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11250908;Dbxref=PMID:11250908 +P15442 UniProtKB Mutagenesis 1090 1090 . . . Note=Inhibits dimerization%3B when associated with A-1080 and A-1088. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11250908;Dbxref=PMID:11250908 +P15442 UniProtKB Mutagenesis 1119 1119 . . . Note=Inhibits binding to uncharged tRNAs%2C decreases eIF-2-alpha kinase activity and derepression of GCN4 translation and amino acid biosynthetic genes in amino acid-starved cells%3B when associated with L-1120. Y->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10983975,ECO:0000269|PubMed:7623840,ECO:0000269|PubMed:8798780;Dbxref=PMID:10983975,PMID:7623840,PMID:8798780 +P15442 UniProtKB Mutagenesis 1120 1120 . . . Note=Inhibits binding to uncharged tRNAs%2C decreases eIF-2-alpha kinase activity and derepression of GCN4 translation and amino acid biosynthetic genes in amino acid-starved cells%3B when associated with L-1119. R->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10983975,ECO:0000269|PubMed:7623840,ECO:0000269|PubMed:8798780;Dbxref=PMID:10983975,PMID:7623840,PMID:8798780 +P15442 UniProtKB Mutagenesis 1134 1134 . . . Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107 +P15442 UniProtKB Mutagenesis 1138 1138 . . . Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107 +P15442 UniProtKB Mutagenesis 1197 1197 . . . Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. A->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107 +P15442 UniProtKB Mutagenesis 1308 1308 . . . Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107 +P15442 UniProtKB Mutagenesis 1338 1338 . . . Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107 +P15442 UniProtKB Mutagenesis 1552 1556 . . . Note=Fails to derepress of GCN4 translation and amino acid biosynthetic genes in amino acid-starved cells and does not inhibit autophosphorylation. KKANK->LLANI;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9430731;Dbxref=PMID:9430731 +P15442 UniProtKB Mutagenesis 1552 1552 . . . Note=Reduces interaction with TIF11%2C Inhibits binding to uncharged tRNAs%2C reduces autophosphorylation%2C eIF-2-alpha kinase activity and ribosome association%2C but not dimerization%3B when associated with I-1553 and I-1556. K->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10983975,ECO:0000269|PubMed:21849502;Dbxref=PMID:10983975,PMID:21849502 +P15442 UniProtKB Mutagenesis 1553 1553 . . . Note=Reduces interaction with TIF11%2C Inhibits binding to uncharged tRNAs%2C reduces autophosphorylation%2C eIF-2-alpha kinase activity and ribosome association%2C but not dimerization%3B when associated with L-1552 and I-1556. K->I;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10983975,ECO:0000269|PubMed:21849502;Dbxref=PMID:10983975,PMID:21849502 +P15442 UniProtKB Mutagenesis 1556 1556 . . . Note=Reduces interaction with TIF11%2C Inhibits binding to uncharged tRNAs%2C reduces autophosphorylation%2C eIF-2-alpha kinase activity and ribosome association%2C but not dimerization%3B when associated with L-1552 and I-1553. K->I;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10983975,ECO:0000269|PubMed:21849502;Dbxref=PMID:10983975,PMID:21849502 +P15442 UniProtKB Mutagenesis 1557 1557 . . . Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107 +P15442 UniProtKB Mutagenesis 1591 1591 . . . Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448107;Dbxref=PMID:1448107 +P15442 UniProtKB Mutagenesis 1606 1606 . . . Note=Increases the constitutive kinase activity and induces derepression of GCN4 translation and amino acid biosynthetic genes in absence of amino acid starvation. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1448107,ECO:0000269|PubMed:2188100;Dbxref=PMID:1448107,PMID:2188100 +P15442 UniProtKB Sequence conflict 70 70 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 220 226 . . . Note=TIKAKLP->NYKGKIA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 271 279 . . . Note=LMSSEMMEN->YVFSNHGKS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 374 374 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 392 392 . . . Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 395 395 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 407 407 . . . Note=F->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 411 413 . . . Note=IPK->MPE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 475 475 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 589 589 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 604 605 . . . Note=VL->FS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 622 622 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 640 641 . . . Note=IL->MI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 727 727 . . . Note=F->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 839 839 . . . Note=M->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 954 954 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 1144 1144 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 1328 1331 . . . Note=TLIS->RFHT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 1348 1348 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 1356 1356 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Sequence conflict 1434 1434 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15442 UniProtKB Beta strand 4 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YZ0 +P15442 UniProtKB Helix 8 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YZ0 +P15442 UniProtKB Beta strand 26 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YZ0 +P15442 UniProtKB Beta strand 37 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YZ0 +P15442 UniProtKB Beta strand 48 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YZ0 +P15442 UniProtKB Beta strand 63 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YZ0 +P15442 UniProtKB Beta strand 80 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YZ0 +P15442 UniProtKB Helix 92 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YZ0 +P15442 UniProtKB Helix 114 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YZ0 +P15442 UniProtKB Helix 594 598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Beta strand 599 607 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Beta strand 609 618 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Turn 619 621 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Beta strand 624 633 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Helix 634 647 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Beta strand 653 655 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYC +P15442 UniProtKB Beta strand 658 664 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Beta strand 781 789 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Helix 796 802 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Helix 805 807 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Helix 809 828 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Helix 838 840 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Beta strand 841 843 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Beta strand 849 851 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Helix 888 890 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZXE +P15442 UniProtKB Helix 893 896 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Helix 905 919 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Helix 925 936 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Turn 948 950 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Helix 952 961 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Helix 966 968 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Helix 972 977 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Helix 986 995 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZY4 +P15442 UniProtKB Beta strand 1541 1543 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM +P15442 UniProtKB Beta strand 1551 1553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM +P15442 UniProtKB Helix 1560 1577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM +P15442 UniProtKB Beta strand 1582 1586 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM +P15442 UniProtKB Helix 1590 1598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM +P15442 UniProtKB Beta strand 1601 1603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM +P15442 UniProtKB Helix 1604 1612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM +P15442 UniProtKB Helix 1615 1617 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM +P15442 UniProtKB Helix 1621 1636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM +P15442 UniProtKB Beta strand 1641 1646 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM +P15442 UniProtKB Turn 1647 1649 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM +P15442 UniProtKB Beta strand 1652 1656 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OTM +##sequence-region P10592 1 639 +P10592 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:9298649;Dbxref=PMID:22814378,PMID:9298649 +P10592 UniProtKB Chain 2 639 . . . ID=PRO_0000078386;Note=Heat shock protein SSA2 +P10592 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:9298649;Dbxref=PMID:22814378,PMID:9298649 +P10592 UniProtKB Modified residue 20 20 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P10592 UniProtKB Modified residue 551 551 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10591 +P10592 UniProtKB Modified residue 603 603 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10591 +P10592 UniProtKB Cross-link 556 556 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P06782 1 633 +P06782 UniProtKB Chain 1 633 . . . ID=PRO_0000086670;Note=Carbon catabolite-derepressing protein kinase +P06782 UniProtKB Domain 55 306 . . . Note=Protein kinase;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000269|PubMed:16236260,ECO:0000269|PubMed:16531232;Dbxref=PMID:16236260,PMID:16531232 +P06782 UniProtKB Domain 348 389 . . . Note=UBA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25869125;Dbxref=PMID:25869125 +P06782 UniProtKB Nucleotide binding 61 69 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P06782 UniProtKB Region 313 392 . . . Note=Auto-inhibitory domain (AID);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17851534,ECO:0000269|PubMed:19474788;Dbxref=PMID:17851534,PMID:19474788 +P06782 UniProtKB Compositional bias 18 32 . . . Note=Poly-His +P06782 UniProtKB Active site 177 177 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P06782 UniProtKB Binding site 84 84 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P06782 UniProtKB Modified residue 210 210 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11486005,ECO:0000269|PubMed:12748292,ECO:0000269|PubMed:22019086,ECO:0000269|PubMed:26394309,ECO:0000269|PubMed:7905477;Dbxref=PMID:11486005,PMID:12748292,PMID:22019086,PMID:26394309,PMID:7905477 +P06782 UniProtKB Modified residue 413 413 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P06782 UniProtKB Modified residue 487 487 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P06782 UniProtKB Modified residue 632 632 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06782 UniProtKB Cross-link 461 461 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P06782 UniProtKB Cross-link 549 549 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24108357;Dbxref=PMID:24108357 +P06782 UniProtKB Mutagenesis 53 53 . . . Note=Exhibits greater activity than wild-type SNFl in an immune complex assay where other associated molecules are present%2C but exhibits the same activity in a protein blot assay. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1468623;Dbxref=PMID:1468623 +P06782 UniProtKB Mutagenesis 84 84 . . . Note=Inactivates the kinase activity without affecting protein levels. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11486005,ECO:0000269|PubMed:2557546;Dbxref=PMID:11486005,PMID:2557546 +P06782 UniProtKB Mutagenesis 210 210 . . . Note=Inactivates the kinase activity without affecting protein levels. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11486005,ECO:0000269|PubMed:1468623;Dbxref=PMID:11486005,PMID:1468623 +P06782 UniProtKB Mutagenesis 357 357 . . . Note=Alters kinase activation and biological activity%2C including enhanced allosteric subunit associations and increased oxidative stress resistance and life span%3B when associated with I-367. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25869125;Dbxref=PMID:25869125 +P06782 UniProtKB Mutagenesis 367 367 . . . Note=Alters kinase activation and biological activity%2C including enhanced allosteric subunit associations and increased oxidative stress resistance and life span%3B when associated with A-357. L->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25869125;Dbxref=PMID:25869125 +P06782 UniProtKB Mutagenesis 549 549 . . . Note=Decreases sumoylation of SNF1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24108357;Dbxref=PMID:24108357 +P06782 UniProtKB Beta strand 56 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Helix 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MN3 +P06782 UniProtKB Beta strand 69 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Turn 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Beta strand 80 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Helix 88 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DAE +P06782 UniProtKB Helix 97 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Beta strand 118 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Beta strand 125 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Helix 139 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Helix 151 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Turn 180 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Beta strand 183 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Beta strand 191 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Turn 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MN3 +P06782 UniProtKB Helix 215 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MN3 +P06782 UniProtKB Helix 220 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Beta strand 224 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Helix 232 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Helix 257 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Helix 277 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Helix 291 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Helix 297 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Helix 304 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Helix 312 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HYH +P06782 UniProtKB Turn 317 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MN3 +P06782 UniProtKB Helix 471 473 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P06782 UniProtKB Helix 475 485 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P06782 UniProtKB Helix 489 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P06782 UniProtKB Beta strand 506 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P06782 UniProtKB Helix 515 529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P06782 UniProtKB Beta strand 532 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P06782 UniProtKB Helix 538 540 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P06782 UniProtKB Beta strand 543 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P06782 UniProtKB Beta strand 565 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P06782 UniProtKB Beta strand 579 590 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P06782 UniProtKB Helix 607 610 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV +P06782 UniProtKB Helix 613 628 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +##sequence-region P22147 1 1528 +P22147 UniProtKB Chain 1 1528 . . . ID=PRO_0000071395;Note=5'-3' exoribonuclease 1 +P22147 UniProtKB Modified residue 1506 1506 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P22147 UniProtKB Modified residue 1510 1510 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +P22147 UniProtKB Mutagenesis 37 37 . . . Note=Reduces strongly exonuclease activity. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 +P22147 UniProtKB Mutagenesis 41 41 . . . Note=Reduces strongly exonuclease activity. H->R%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 +P22147 UniProtKB Mutagenesis 86 86 . . . Note=Reduces strongly exonuclease activity. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 +P22147 UniProtKB Mutagenesis 87 87 . . . Note=Reduces strongly exonuclease activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 +P22147 UniProtKB Mutagenesis 93 93 . . . Note=Reduces strongly exonuclease activity. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 +P22147 UniProtKB Mutagenesis 97 97 . . . Note=Reduces strongly exonuclease activity. Q->E%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 +P22147 UniProtKB Mutagenesis 101 101 . . . Note=Reduces strongly exonuclease activity. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 +P22147 UniProtKB Mutagenesis 176 176 . . . Note=Reduces strongly exonuclease activity. E->G +P22147 UniProtKB Mutagenesis 178 178 . . . Note=Reduces strongly exonuclease activity. E->D%2CG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 +P22147 UniProtKB Mutagenesis 201 201 . . . Note=Reduces strongly exonuclease activity. C->Y%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 +P22147 UniProtKB Mutagenesis 206 206 . . . Note=Abolishes exonuclease activity in vitro. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10454540;Dbxref=PMID:10454540 +P22147 UniProtKB Mutagenesis 208 208 . . . Note=Abolishes exonuclease activity in vitro. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10454540;Dbxref=PMID:10454540 +P22147 UniProtKB Mutagenesis 592 592 . . . Note=Reduces strongly exonuclease activity%3B when associated with Y-710. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 +P22147 UniProtKB Mutagenesis 710 710 . . . Note=Reduces strongly exonuclease activity%3B when associated with P-592. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 +P22147 UniProtKB Mutagenesis 798 798 . . . Note=Reduces strongly exonuclease activity%3B when associated with D-1024%3B F-1043 and P-1197. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 +P22147 UniProtKB Mutagenesis 1024 1024 . . . Note=Reduces strongly exonuclease activity%3B when associated with R-798%3B F-1043 and P-1197. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 +P22147 UniProtKB Mutagenesis 1043 1043 . . . Note=Reduces strongly exonuclease activity%3B when associated with R-798%3B D-1024 and P-1197. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 +P22147 UniProtKB Mutagenesis 1197 1197 . . . Note=Reduces strongly exonuclease activity%3B when associated with R-798%3B D-1024 and F-1043. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 +##sequence-region P32598 1 312 +P32598 UniProtKB Chain 1 312 . . . ID=PRO_0000058820;Note=Serine/threonine-protein phosphatase PP1-2 +P32598 UniProtKB Active site 124 124 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32598 UniProtKB Metal binding 63 63 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32598 UniProtKB Metal binding 65 65 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32598 UniProtKB Metal binding 91 91 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32598 UniProtKB Metal binding 91 91 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32598 UniProtKB Metal binding 123 123 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32598 UniProtKB Metal binding 172 172 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32598 UniProtKB Metal binding 247 247 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32598 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32598 UniProtKB Cross-link 22 22 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32598 UniProtKB Cross-link 47 47 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32598 UniProtKB Mutagenesis 73 73 . . . Note=In GLC7-1%3B decreased glycogen accumulation. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8150278;Dbxref=PMID:8150278 +P32598 UniProtKB Sequence conflict 137 137 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32598 UniProtKB Sequence conflict 273 273 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53230 1 385 +P53230 UniProtKB Transit peptide 1 34 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53230 UniProtKB Chain 35 385 . . . ID=PRO_0000202796;Note=Phosphatidate cytidylyltransferase%2C mitochondrial +P53230 UniProtKB Natural variant 8 8 . . . Note=In strain: SK1. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P53230 UniProtKB Natural variant 127 127 . . . Note=In strain: SK1. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P53230 UniProtKB Mutagenesis 130 132 . . . Note=Completely abolishes the enzymatic activity. YGS->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23623749;Dbxref=PMID:23623749 +P53230 UniProtKB Mutagenesis 220 220 . . . Note=Completely abolishes the enzymatic activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23623749;Dbxref=PMID:23623749 +##sequence-region Q06510 1 381 +Q06510 UniProtKB Chain 1 381 . . . ID=PRO_0000220934;Note=Lysophosphatidylcholine acyltransferase +Q06510 UniProtKB Topological domain 1 25 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06510 UniProtKB Transmembrane 26 47 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06510 UniProtKB Topological domain 48 381 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06510 UniProtKB Motif 77 82 . . . Note=HXXXXD motif +Q06510 UniProtKB Sequence conflict 11 11 . . . Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02457 1 562 +Q02457 UniProtKB Chain 1 562 . . . ID=PRO_0000197125;Note=Protein TBF1 +Q02457 UniProtKB Domain 404 460 . . . Note=HTH myb-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +Q02457 UniProtKB DNA binding 431 456 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +Q02457 UniProtKB Sequence conflict 71 71 . . . Note=E->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q02457 UniProtKB Sequence conflict 371 373 . . . Note=DAA->ERR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39078 1 528 +P39078 UniProtKB Chain 1 528 . . . ID=PRO_0000128345;Note=T-complex protein 1 subunit delta +P39078 UniProtKB Sequence conflict 254 254 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q3E7C1 1 72 +Q3E7C1 UniProtKB Chain 1 72 . . . ID=PRO_0000119287;Note=RNA polymerase II transcription factor B subunit 5 +Q3E7C1 UniProtKB Beta strand 3 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP +Q3E7C1 UniProtKB Helix 14 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP +Q3E7C1 UniProtKB Beta strand 29 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP +Q3E7C1 UniProtKB Beta strand 39 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP +Q3E7C1 UniProtKB Helix 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP +Q3E7C1 UniProtKB Helix 47 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP +##sequence-region Q06339 1 672 +Q06339 UniProtKB Chain 1 672 . . . ID=PRO_0000252483;Note=Transcription factor tau 91 kDa subunit +Q06339 UniProtKB DNA binding 6 18 . . . Note=A.T hook +Q06339 UniProtKB Region 1 158 . . . Note=Required for DNA-binding +Q06339 UniProtKB Region 159 672 . . . Note=Sufficient for interaction with TFC8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16115780;Dbxref=PMID:16115780 +Q06339 UniProtKB Disulfide bond 375 383 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17052456;Dbxref=PMID:17052456 +Q06339 UniProtKB Helix 167 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Helix 178 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Helix 200 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 218 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Helix 223 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Turn 226 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Helix 241 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 253 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 261 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 270 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Helix 273 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 283 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 298 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 308 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 339 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Turn 348 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 353 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 365 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 378 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 383 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 393 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 402 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 415 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Turn 421 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 425 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 443 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 457 461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 463 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 467 473 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 481 486 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 489 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Helix 496 498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Helix 499 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 504 508 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 517 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Turn 521 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 525 529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 531 539 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 547 551 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 556 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 569 572 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Turn 573 575 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 576 578 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Turn 586 588 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 601 604 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 609 611 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 613 616 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 645 647 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Turn 651 655 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 656 660 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q06339 UniProtKB Beta strand 664 670 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +##sequence-region Q12308 1 588 +Q12308 UniProtKB Chain 1 588 . . . ID=PRO_0000252484;Note=Transcription factor tau 60 kDa subunit +Q12308 UniProtKB Region 399 588 . . . Note=Sufficient for SPT15-binding +Q12308 UniProtKB Site 358 358 . . . Note=Involved in the interaction with TFC6 +Q12308 UniProtKB Sequence conflict 36 36 . . . Note=D->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12308 UniProtKB Beta strand 7 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 15 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 29 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 34 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Helix 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 56 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Turn 68 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 88 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 95 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 100 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 109 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 116 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Turn 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 132 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 139 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 144 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 151 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Turn 162 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 169 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 185 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 194 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 204 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 211 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 218 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 232 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 238 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 244 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Turn 252 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 256 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 270 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 280 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 289 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Helix 307 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Turn 317 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 323 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 330 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 342 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 361 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 366 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Helix 386 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Turn 395 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Helix 412 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Helix 423 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Helix 434 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Turn 443 445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 446 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Helix 452 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Helix 465 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Helix 472 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 495 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 503 509 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Helix 510 512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 516 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 526 529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 531 533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 542 544 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Turn 546 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 551 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Helix 555 557 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 559 561 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Helix 565 573 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Beta strand 575 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +Q12308 UniProtKB Turn 579 581 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J04 +##sequence-region Q06490 1 572 +Q06490 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06490 UniProtKB Chain 20 572 . . . ID=PRO_0000034064;Note=Thiamine biosynthesis protein THI22 +Q06490 UniProtKB Sequence conflict 95 95 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04083 1 370 +Q04083 UniProtKB Chain 1 370 . . . ID=PRO_0000252277;Note=Thiamine-repressible mitochondrial transport protein THI74 +Q04083 UniProtKB Topological domain 1 10 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Transmembrane 11 31 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Topological domain 32 42 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Transmembrane 43 63 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Topological domain 64 119 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Transmembrane 120 140 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Topological domain 141 146 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Transmembrane 147 167 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Topological domain 168 169 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Transmembrane 170 190 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Topological domain 191 203 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Transmembrane 204 224 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Topological domain 225 239 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Transmembrane 240 260 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Topological domain 261 273 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Transmembrane 274 294 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Topological domain 295 303 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Transmembrane 304 324 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Topological domain 325 326 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Transmembrane 327 347 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Topological domain 348 370 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04083 UniProtKB Domain 129 190 . . . Note=EamA +##sequence-region P35202 1 319 +P35202 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P35202 UniProtKB Chain 2 319 . . . ID=PRO_0000072513;Note=Thiamine pyrophosphokinase +P35202 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P35202 UniProtKB Beta strand 4 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Beta strand 10 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Beta strand 23 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Helix 28 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Beta strand 37 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Helix 52 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Beta strand 63 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Helix 71 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Helix 83 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Beta strand 92 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Helix 103 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Beta strand 115 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Beta strand 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Helix 126 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Helix 141 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Turn 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Helix 156 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Turn 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Helix 164 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Helix 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Beta strand 184 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Helix 196 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Beta strand 216 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Beta strand 223 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Beta strand 235 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Helix 241 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Beta strand 248 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Beta strand 260 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Turn 279 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Beta strand 285 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Beta strand 292 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Beta strand 304 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Helix 312 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +P35202 UniProtKB Helix 316 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG0 +##sequence-region Q08231 1 455 +Q08231 UniProtKB Chain 1 455 . . . ID=PRO_0000270618;Note=Nuclear mRNA export protein THP1 +Q08231 UniProtKB Domain 297 428 . . . Note=PCI +Q08231 UniProtKB Helix 4 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Beta strand 23 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 27 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 42 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 59 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 84 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Beta strand 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 106 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 131 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 140 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 170 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TRQ +Q08231 UniProtKB Helix 195 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 202 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 211 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 216 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 236 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 258 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 284 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 288 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 293 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 311 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 322 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 331 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Turn 355 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Beta strand 362 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 365 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Turn 390 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 397 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TRQ +Q08231 UniProtKB Helix 400 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Beta strand 415 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Turn 419 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Beta strand 423 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 432 434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +Q08231 UniProtKB Helix 439 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +##sequence-region P16120 1 514 +P16120 UniProtKB Chain 1 514 . . . ID=PRO_0000185645;Note=Threonine synthase +P16120 UniProtKB Modified residue 124 124 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P16120 UniProtKB Modified residue 467 467 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P16120 UniProtKB Sequence conflict 176 176 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16120 UniProtKB Beta strand 8 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 21 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 46 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Turn 52 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 58 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Turn 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 77 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Turn 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Beta strand 106 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Beta strand 110 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 125 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Beta strand 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Beta strand 154 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Beta strand 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 164 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Beta strand 178 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 191 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Beta strand 205 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 214 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 244 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Beta strand 263 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Beta strand 270 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Beta strand 277 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 280 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Beta strand 298 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 307 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Beta strand 315 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 329 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 339 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 356 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Beta strand 374 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 380 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Turn 387 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Beta strand 390 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 397 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 421 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Beta strand 442 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 452 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 456 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 471 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 478 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 483 485 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +P16120 UniProtKB Helix 498 506 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KL7 +##sequence-region P40328 1 754 +P40328 UniProtKB Chain 1 754 . . . ID=PRO_0000084759;Note=Probable 26S proteasome subunit YTA6 +P40328 UniProtKB Nucleotide binding 511 518 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40328 UniProtKB Modified residue 255 255 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40328 UniProtKB Sequence conflict 20 20 . . . Note=L->LQL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40328 UniProtKB Sequence conflict 85 85 . . . Note=D->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39077 1 534 +P39077 UniProtKB Chain 1 534 . . . ID=PRO_0000128331;Note=T-complex protein 1 subunit gamma +P39077 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P39077 UniProtKB Modified residue 257 257 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39077 UniProtKB Disulfide bond 371 377 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39077 UniProtKB Sequence conflict 25 26 . . . Note=IT->HA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39077 UniProtKB Sequence conflict 86 89 . . . Note=DEEV->ERRG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39077 UniProtKB Sequence conflict 111 111 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39077 UniProtKB Sequence conflict 265 265 . . . Note=K->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39077 UniProtKB Sequence conflict 274 274 . . . Note=Q->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39077 UniProtKB Sequence conflict 292 292 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39077 UniProtKB Sequence conflict 478 478 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P35691 1 167 +P35691 UniProtKB Chain 1 167 . . . ID=PRO_0000211311;Note=Translationally-controlled tumor protein homolog +P35691 UniProtKB Domain 1 167 . . . Note=TCTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01133 +P35691 UniProtKB Modified residue 9 9 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35691 UniProtKB Modified residue 15 15 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35691 UniProtKB Sequence conflict 19 20 . . . Note=DA->AD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35691 UniProtKB Sequence conflict 70 70 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38987 1 245 +P38987 UniProtKB Chain 1 245 . . . ID=PRO_0000122466;Note=Protein TEM1 +P38987 UniProtKB Nucleotide binding 27 34 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38987 UniProtKB Nucleotide binding 75 79 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38987 UniProtKB Nucleotide binding 132 135 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38987 UniProtKB Region 16 244 . . . Note=Small GTPase-like +##sequence-region P53916 1 434 +P53916 UniProtKB Chain 1 434 . . . ID=PRO_0000215906;Note=Probable phosphatidylinositol 3%2C4%2C5-trisphosphate 3-phosphatase TEP1 +P53916 UniProtKB Domain 33 255 . . . Note=Phosphatase tensin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00590 +P53916 UniProtKB Active site 193 193 . . . Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00590 +##sequence-region P29055 1 345 +P29055 UniProtKB Chain 1 345 . . . ID=PRO_0000119308;Note=Transcription initiation factor IIB +P29055 UniProtKB Repeat 136 212 . . . Note=1 +P29055 UniProtKB Repeat 242 318 . . . Note=2 +P29055 UniProtKB Zinc finger 20 53 . . . Note=TFIIB-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00469 +P29055 UniProtKB Metal binding 24 24 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P29055 UniProtKB Metal binding 27 27 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P29055 UniProtKB Metal binding 45 45 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P29055 UniProtKB Metal binding 48 48 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P29055 UniProtKB Sequence conflict 10 10 . . . Note=R->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29055 UniProtKB Beta strand 34 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P29055 UniProtKB Turn 38 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P29055 UniProtKB Beta strand 42 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P29055 UniProtKB Turn 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P29055 UniProtKB Beta strand 50 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P29055 UniProtKB Helix 59 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P29055 UniProtKB Turn 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P29055 UniProtKB Beta strand 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P29055 UniProtKB Beta strand 80 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P29055 UniProtKB Helix 85 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P29055 UniProtKB Beta strand 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P29055 UniProtKB Helix 104 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P29055 UniProtKB Beta strand 122 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P29055 UniProtKB Helix 128 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P29055 UniProtKB Helix 144 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P29055 UniProtKB Turn 161 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P29055 UniProtKB Helix 168 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P29055 UniProtKB Helix 189 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P29055 UniProtKB Helix 202 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +##sequence-region P29056 1 596 +P29056 UniProtKB Chain 1 596 . . . ID=PRO_0000119346;Note=Transcription factor IIIB 70 kDa subunit +P29056 UniProtKB Repeat 90 166 . . . Note=1 +P29056 UniProtKB Repeat 185 264 . . . Note=2 +P29056 UniProtKB Zinc finger 1 33 . . . Note=TFIIB-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00469 +P29056 UniProtKB Metal binding 4 4 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P29056 UniProtKB Metal binding 7 7 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P29056 UniProtKB Metal binding 25 25 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P29056 UniProtKB Metal binding 28 28 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P29056 UniProtKB Modified residue 381 381 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P29056 UniProtKB Modified residue 384 384 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P29056 UniProtKB Helix 442 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NGM +P29056 UniProtKB Helix 448 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NGM +P29056 UniProtKB Helix 470 472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NGM +P29056 UniProtKB Helix 477 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NGM +P29056 UniProtKB Turn 491 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NGM +P29056 UniProtKB Helix 494 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NGM +P29056 UniProtKB Turn 501 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NGM +##sequence-region P38141 1 450 +P38141 UniProtKB Chain 1 450 . . . ID=PRO_0000114984;Note=Thiamine biosynthesis regulatory protein +P38141 UniProtKB DNA binding 30 57 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +##sequence-region P32318 1 326 +P32318 UniProtKB Chain 1 326 . . . ID=PRO_0000034058;Note=Thiamine thiazole synthase +P32318 UniProtKB Region 97 98 . . . Note=Substrate binding +P32318 UniProtKB Region 301 303 . . . Note=Substrate binding +P32318 UniProtKB Binding site 76 76 . . . Note=Substrate%3B via amide nitrogen +P32318 UniProtKB Binding site 105 105 . . . Note=Substrate%3B via amide nitrogen +P32318 UniProtKB Binding site 170 170 . . . Note=Substrate%3B via amide nitrogen and carbonyl oxygen +P32318 UniProtKB Binding site 207 207 . . . Note=Substrate +P32318 UniProtKB Binding site 237 237 . . . Note=Substrate +P32318 UniProtKB Binding site 291 291 . . . Note=Substrate%3B via amide nitrogen +P32318 UniProtKB Modified residue 205 205 . . . Note=2%2C3-didehydroalanine (Cys) +P32318 UniProtKB Mutagenesis 97 97 . . . Note=No activity. E->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17309261;Dbxref=PMID:17309261 +P32318 UniProtKB Mutagenesis 200 200 . . . Note=Partially active%2C trapping the enzyme at an advanced intermediate%2C just before the sulfide transfer reaction. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17309261;Dbxref=PMID:17309261 +P32318 UniProtKB Mutagenesis 204 204 . . . Note=Partially active%2C trapping the enzyme at an advanced intermediate%2C just before the sulfide transfer reaction. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17309261;Dbxref=PMID:17309261 +P32318 UniProtKB Mutagenesis 205 205 . . . Note=Partially active%2C with very weak activity toward NAD. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17309261;Dbxref=PMID:17309261 +P32318 UniProtKB Mutagenesis 207 207 . . . Note=No activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17309261;Dbxref=PMID:17309261 +P32318 UniProtKB Mutagenesis 237 237 . . . Note=No activity. H->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17309261;Dbxref=PMID:17309261 +P32318 UniProtKB Mutagenesis 238 238 . . . Note=Partially active%2C with very weak activity toward NAD. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17309261;Dbxref=PMID:17309261 +P32318 UniProtKB Mutagenesis 301 301 . . . Note=No activity. R->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17309261;Dbxref=PMID:17309261 +P32318 UniProtKB Mutagenesis 304 304 . . . Note=No activity. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17309261;Dbxref=PMID:17309261 +P32318 UniProtKB Helix 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Turn 25 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Helix 45 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Beta strand 65 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Helix 75 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Beta strand 93 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Beta strand 98 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Turn 104 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Beta strand 116 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Turn 120 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Helix 123 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Beta strand 137 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Helix 145 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Beta strand 162 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Beta strand 168 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Beta strand 180 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Beta strand 185 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Helix 194 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Turn 198 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Y4L +P32318 UniProtKB Beta strand 209 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Beta strand 220 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Beta strand 230 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Beta strand 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Helix 244 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Helix 266 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Beta strand 286 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Helix 291 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +P32318 UniProtKB Helix 307 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FPZ +##sequence-region P32897 1 222 +P32897 UniProtKB Chain 1 222 . . . ID=PRO_0000210307;Note=Mitochondrial import inner membrane translocase subunit TIM23 +P32897 UniProtKB Transmembrane 97 118 . . . Note=Helical%3B Note%3DInner membrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32897 UniProtKB Topological domain 119 144 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32897 UniProtKB Transmembrane 145 166 . . . Note=Helical%3B Note%3DInner membrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32897 UniProtKB Topological domain 167 174 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32897 UniProtKB Transmembrane 175 189 . . . Note=Helical%3B Note%3DInner membrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32897 UniProtKB Topological domain 190 196 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32897 UniProtKB Transmembrane 197 215 . . . Note=Helical%3B Note%3DInner membrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32897 UniProtKB Topological domain 216 222 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08144 1 397 +Q08144 UniProtKB Chain 1 397 . . . ID=PRO_0000210279;Note=T-SNARE affecting a late Golgi compartment protein 2 +Q08144 UniProtKB Topological domain 1 317 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08144 UniProtKB Transmembrane 318 338 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08144 UniProtKB Topological domain 339 397 . . . Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08144 UniProtKB Domain 244 306 . . . Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202 +Q08144 UniProtKB Coiled coil 74 96 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08144 UniProtKB Modified residue 109 109 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08144 UniProtKB Sequence conflict 397 397 . . . Note=L->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P07273 1 309 +P07273 UniProtKB Chain 1 309 . . . ID=PRO_0000121443;Note=Transcription elongation factor S-II +P07273 UniProtKB Domain 5 79 . . . Note=TFIIS N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00649 +P07273 UniProtKB Domain 148 264 . . . Note=TFIIS central;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00651 +P07273 UniProtKB Zinc finger 267 307 . . . Note=TFIIS-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00472 +P07273 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07273 UniProtKB Sequence conflict 35 35 . . . Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07273 UniProtKB Sequence conflict 35 35 . . . Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07273 UniProtKB Sequence conflict 74 77 . . . Note=DAIN->AQLI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07273 UniProtKB Sequence conflict 74 77 . . . Note=DAIN->AQLI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07273 UniProtKB Sequence conflict 82 82 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07273 UniProtKB Sequence conflict 82 82 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07273 UniProtKB Sequence conflict 85 85 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07273 UniProtKB Sequence conflict 85 85 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07273 UniProtKB Helix 3 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EO0 +P07273 UniProtKB Beta strand 18 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EO0 +P07273 UniProtKB Helix 21 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EO0 +P07273 UniProtKB Turn 31 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EO0 +P07273 UniProtKB Helix 40 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EO0 +P07273 UniProtKB Beta strand 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EO0 +P07273 UniProtKB Helix 61 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EO0 +P07273 UniProtKB Turn 134 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ENW +P07273 UniProtKB Helix 147 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3 +P07273 UniProtKB Beta strand 162 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3 +P07273 UniProtKB Helix 170 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3 +P07273 UniProtKB Beta strand 189 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3 +P07273 UniProtKB Helix 194 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3 +P07273 UniProtKB Beta strand 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3 +P07273 UniProtKB Helix 213 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3 +P07273 UniProtKB Helix 226 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3 +P07273 UniProtKB Turn 232 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3 +P07273 UniProtKB Helix 240 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3 +P07273 UniProtKB Beta strand 266 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3 +P07273 UniProtKB Beta strand 272 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3 +P07273 UniProtKB Beta strand 297 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3 +P07273 UniProtKB Turn 300 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3 +##sequence-region P54857 1 326 +P54857 UniProtKB Chain 1 326 . . . ID=PRO_0000090380;Note=Lipase 2 +P54857 UniProtKB Active site 144 144 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P54857 UniProtKB Sequence conflict 104 104 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54857 UniProtKB Sequence conflict 300 300 . . . Note=R->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12052 1 315 +Q12052 UniProtKB Chain 1 315 . . . ID=PRO_0000270619;Note=Trimethylguanosine synthase +Q12052 UniProtKB Region 1 58 . . . Note=Required for correct nucleolar localization +Q12052 UniProtKB Binding site 126 126 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12052 UniProtKB Mutagenesis 75 75 . . . Note=No effect. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12907733;Dbxref=PMID:12907733 +Q12052 UniProtKB Mutagenesis 81 81 . . . Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12907733;Dbxref=PMID:12907733 +Q12052 UniProtKB Mutagenesis 83 83 . . . Note=Loss of function. I->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12907733;Dbxref=PMID:12907733 +Q12052 UniProtKB Mutagenesis 103 103 . . . Note=Loss of catalytic activity%2C but not required for pre-rRNA processing. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11983179,ECO:0000269|PubMed:15340060;Dbxref=PMID:11983179,PMID:15340060 +Q12052 UniProtKB Mutagenesis 126 126 . . . Note=Loss of function. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983179;Dbxref=PMID:11983179 +Q12052 UniProtKB Mutagenesis 175 175 . . . Note=No effect. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12907733;Dbxref=PMID:12907733 +Q12052 UniProtKB Mutagenesis 175 175 . . . Note=Loss of function. S->E%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12907733;Dbxref=PMID:12907733 +Q12052 UniProtKB Mutagenesis 178 178 . . . Note=Loss of catalytic activity%2C but not required for pre-rRNA processing. W->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12907733,ECO:0000269|PubMed:15340060,ECO:0000269|PubMed:18840651;Dbxref=PMID:12907733,PMID:15340060,PMID:18840651 +##sequence-region P00927 1 576 +P00927 UniProtKB Domain 393 473 . . . Note=ACT-like 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01008 +P00927 UniProtKB Domain 495 566 . . . Note=ACT-like 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01008 +P00927 UniProtKB Modified residue 109 109 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00927 UniProtKB Sequence conflict 259 259 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P41338 1 398 +P41338 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.4;Dbxref=PMID:22814378 +P41338 UniProtKB Chain 2 398 . . . ID=PRO_0000206416;Note=Acetyl-CoA acetyltransferase +P41338 UniProtKB Active site 91 91 . . . Note=Acyl-thioester intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41338 UniProtKB Active site 354 354 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10020 +P41338 UniProtKB Active site 384 384 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10020 +P41338 UniProtKB Metal binding 186 186 . . . Note=Potassium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41338 UniProtKB Metal binding 248 248 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41338 UniProtKB Metal binding 249 249 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41338 UniProtKB Metal binding 251 251 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41338 UniProtKB Metal binding 350 350 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41338 UniProtKB Binding site 186 186 . . . Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41338 UniProtKB Binding site 231 231 . . . Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41338 UniProtKB Binding site 252 252 . . . Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41338 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.4;Dbxref=PMID:22814378 +##sequence-region P57744 1 87 +P57744 UniProtKB Chain 1 87 . . . ID=PRO_0000193594;Note=Mitochondrial import inner membrane translocase subunit TIM8 +P57744 UniProtKB Motif 44 68 . . . Note=Twin CX3C motif +P57744 UniProtKB Disulfide bond 44 68 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P57744 UniProtKB Disulfide bond 48 64 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P57744 UniProtKB Helix 30 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CJH +P57744 UniProtKB Beta strand 53 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CJH +P57744 UniProtKB Helix 59 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CJH +##sequence-region O74700 1 87 +O74700 UniProtKB Chain 1 87 . . . ID=PRO_0000193610;Note=Mitochondrial import inner membrane translocase subunit TIM9 +O74700 UniProtKB Motif 35 59 . . . Note=Twin CX3C motif;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11867522;Dbxref=PMID:11867522 +O74700 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +O74700 UniProtKB Disulfide bond 35 59 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11867522;Dbxref=PMID:11867522 +O74700 UniProtKB Disulfide bond 39 55 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11867522;Dbxref=PMID:11867522 +O74700 UniProtKB Mutagenesis 40 40 . . . Note=In tim9-3%3B impairs the import of mitochondrial carrier proteins into mitochondria%3B when associated with P-60. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12656987;Dbxref=PMID:12656987 +O74700 UniProtKB Mutagenesis 52 52 . . . Note=In tim9-19%3B impairs the import of mitochondrial carrier proteins into mitochondria. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12656987;Dbxref=PMID:12656987 +O74700 UniProtKB Mutagenesis 60 60 . . . Note=In tim9-3%3B impairs the import of mitochondrial carrier proteins into mitochondria%3B when associated with A-40. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12656987;Dbxref=PMID:12656987 +O74700 UniProtKB Mutagenesis 67 67 . . . Note=Impairs the import of mitochondrial carrier proteins into mitochondria. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9822593;Dbxref=PMID:9822593 +O74700 UniProtKB Helix 14 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DXR +O74700 UniProtKB Beta strand 44 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DXR +O74700 UniProtKB Helix 50 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DXR +##sequence-region Q12218 1 487 +Q12218 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12218 UniProtKB Chain 23 465 . . . ID=PRO_0000267640;Note=Cell wall protein TIR4 +Q12218 UniProtKB Propeptide 466 487 . . . ID=PRO_0000267641;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12218 UniProtKB Repeat 137 148 . . . Note=1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q12218 UniProtKB Repeat 149 160 . . . Note=2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q12218 UniProtKB Repeat 161 172 . . . Note=3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q12218 UniProtKB Repeat 173 184 . . . Note=4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q12218 UniProtKB Repeat 185 196 . . . Note=5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q12218 UniProtKB Repeat 197 208 . . . Note=6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q12218 UniProtKB Repeat 209 220 . . . Note=7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q12218 UniProtKB Repeat 221 232 . . . Note=8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q12218 UniProtKB Repeat 233 244 . . . Note=9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q12218 UniProtKB Repeat 245 256 . . . Note=10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q12218 UniProtKB Repeat 257 268 . . . Note=11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q12218 UniProtKB Region 137 268 . . . Note=11 X 12 AA approximate tandem repeats%2C Ser-rich +Q12218 UniProtKB Compositional bias 113 365 . . . Note=Ser-rich +Q12218 UniProtKB Lipidation 465 465 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12218 UniProtKB Glycosylation 327 327 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12218 UniProtKB Glycosylation 348 348 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12218 UniProtKB Glycosylation 368 368 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12218 UniProtKB Glycosylation 403 403 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12218 UniProtKB Glycosylation 404 404 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04562 1 672 +Q04562 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Chain 19 672 . . . ID=PRO_0000244444;Note=Transmembrane 9 superfamily member 2 +Q04562 UniProtKB Topological domain 19 307 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Transmembrane 308 328 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Topological domain 329 383 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Transmembrane 384 404 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Topological domain 405 410 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Transmembrane 411 431 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Topological domain 432 447 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Transmembrane 448 468 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Topological domain 469 479 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Transmembrane 480 500 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Topological domain 501 532 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Transmembrane 533 553 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Topological domain 554 565 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Transmembrane 566 586 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Topological domain 587 601 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Transmembrane 602 622 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Topological domain 623 628 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Transmembrane 629 649 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04562 UniProtKB Topological domain 650 672 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53507 1 60 +P53507 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8641278;Dbxref=PMID:8641278 +P53507 UniProtKB Chain 2 60 . . . ID=PRO_0000046767;Note=Mitochondrial import receptor subunit TOM7 +P53507 UniProtKB Topological domain 2 19 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53507 UniProtKB Transmembrane 20 41 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53507 UniProtKB Topological domain 42 60 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q07904 1 523 +Q07904 UniProtKB Chain 1 523 . . . ID=PRO_0000247182;Note=Thiamine pathway transporter THI73 +Q07904 UniProtKB Topological domain 1 79 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Transmembrane 80 100 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Topological domain 101 118 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Transmembrane 119 139 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Topological domain 140 141 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Transmembrane 142 162 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Topological domain 163 176 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Transmembrane 177 197 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Topological domain 198 207 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Transmembrane 208 228 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Topological domain 229 239 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Transmembrane 240 260 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Topological domain 261 312 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Transmembrane 313 333 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Topological domain 334 345 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Transmembrane 346 366 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Topological domain 367 371 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Transmembrane 372 392 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Topological domain 393 400 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Transmembrane 401 421 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Topological domain 422 432 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Transmembrane 433 452 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Topological domain 453 466 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Transmembrane 467 487 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07904 UniProtKB Topological domain 488 523 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q05998 1 598 +Q05998 UniProtKB Chain 1 598 . . . ID=PRO_0000197926;Note=Thiamine transporter +Q05998 UniProtKB Topological domain 1 41 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Topological domain 63 73 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Transmembrane 74 94 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Topological domain 95 111 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Transmembrane 112 132 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Topological domain 133 173 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Transmembrane 174 194 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Topological domain 195 197 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Transmembrane 198 218 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Topological domain 219 240 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Transmembrane 241 261 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Topological domain 262 274 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Transmembrane 275 295 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Topological domain 296 332 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Transmembrane 333 353 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Topological domain 354 371 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Transmembrane 372 392 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Topological domain 393 394 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Transmembrane 395 415 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Topological domain 416 446 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Transmembrane 447 467 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Topological domain 468 483 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Transmembrane 484 504 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Topological domain 505 598 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05998 UniProtKB Modified residue 560 560 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P40040 1 218 +P40040 UniProtKB Chain 1 218 . . . ID=PRO_0000072519;Note=Protein THO1 +P40040 UniProtKB Domain 4 38 . . . Note=SAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00186 +P40040 UniProtKB Modified residue 22 22 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40040 UniProtKB Modified residue 58 58 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40040 UniProtKB Modified residue 68 68 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40040 UniProtKB Helix 4 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H1J +P40040 UniProtKB Helix 9 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H1J +P40040 UniProtKB Helix 27 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H1J +P40040 UniProtKB Helix 122 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UZX +P40040 UniProtKB Helix 147 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UZX +P40040 UniProtKB Helix 170 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UZX +##sequence-region P53552 1 1597 +P53552 UniProtKB Chain 1 1597 . . . ID=PRO_0000097359;Note=THO complex subunit 2 +##sequence-region O13539 1 261 +O13539 UniProtKB Chain 1 261 . . . ID=PRO_0000267642;Note=THO complex subunit THP2 +##sequence-region Q07914 1 168 +Q07914 UniProtKB Chain 1 168 . . . ID=PRO_0000071118;Note=Mitochondrial import inner membrane translocase subunit TIM14 +Q07914 UniProtKB Topological domain 1 65 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07914 UniProtKB Transmembrane 66 83 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07914 UniProtKB Topological domain 84 168 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07914 UniProtKB Domain 112 168 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +Q07914 UniProtKB Mutagenesis 141 143 . . . Note=Induces lethality. HPD->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14605210;Dbxref=PMID:14605210 +Q07914 UniProtKB Mutagenesis 141 141 . . . Note=Induces lethality. H->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14517234,ECO:0000269|PubMed:14605210;Dbxref=PMID:14517234,PMID:14605210 +Q07914 UniProtKB Mutagenesis 142 142 . . . Note=Induces a strong reduction in ability to stimulate mtHSP70 activity but does not affect import of proteins into mitochondrial matrix. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16105940;Dbxref=PMID:16105940 +Q07914 UniProtKB Mutagenesis 143 143 . . . Note=Induces lethality. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16105940;Dbxref=PMID:16105940 +Q07914 UniProtKB Mutagenesis 144 144 . . . Note=Induces a strong reduction in ability to stimulate mtHSP70 activity but does not affect import of proteins into mitochondrial matrix. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16105940;Dbxref=PMID:16105940 +Q07914 UniProtKB Mutagenesis 150 150 . . . Note=Temperature-sensitive mutant that impairs heterodimerization with PAM16 and import of proteins into mitochondrial matrix when incubated at 37 degrees Celsius. L->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16105940;Dbxref=PMID:16105940 +Q07914 UniProtKB Helix 110 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ +Q07914 UniProtKB Turn 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ +Q07914 UniProtKB Helix 126 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ +Q07914 UniProtKB Helix 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ +Q07914 UniProtKB Helix 148 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ +##sequence-region P39515 1 158 +P39515 UniProtKB Chain 1 158 . . . ID=PRO_0000210296;Note=Mitochondrial import inner membrane translocase subunit TIM17 +P39515 UniProtKB Topological domain 1 11 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39515 UniProtKB Transmembrane 12 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39515 UniProtKB Topological domain 33 58 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39515 UniProtKB Transmembrane 59 79 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39515 UniProtKB Topological domain 80 87 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39515 UniProtKB Transmembrane 88 108 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39515 UniProtKB Topological domain 109 112 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39515 UniProtKB Transmembrane 113 133 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39515 UniProtKB Topological domain 134 158 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39515 UniProtKB Mutagenesis 4 4 . . . Note=Induces abolition of mitochondrial import of transit peptide-containing proteins%3B when associated with K-8. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15618217;Dbxref=PMID:15618217 +P39515 UniProtKB Mutagenesis 8 8 . . . Note=Induces abolition of mitochondrial import of transit peptide-containing proteins%3B when associated with K-4. D->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15618217;Dbxref=PMID:15618217 +P39515 UniProtKB Sequence conflict 33 33 . . . Note=H->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q01852 1 431 +Q01852 UniProtKB Nucleotide binding 101 108 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01852 UniProtKB Region 43 209 . . . Note=Interaction with SSC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18426906;Dbxref=PMID:18426906 +Q01852 UniProtKB Mutagenesis 180 180 . . . Note=Disrupts association with the translocase complex. R->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18426906;Dbxref=PMID:18426906 +Q01852 UniProtKB Helix 237 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9 +Q01852 UniProtKB Helix 249 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9 +Q01852 UniProtKB Turn 259 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FXT +Q01852 UniProtKB Helix 271 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9 +Q01852 UniProtKB Helix 286 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9 +Q01852 UniProtKB Helix 297 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9 +Q01852 UniProtKB Helix 310 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9 +Q01852 UniProtKB Helix 319 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9 +Q01852 UniProtKB Turn 334 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9 +Q01852 UniProtKB Beta strand 337 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9 +Q01852 UniProtKB Beta strand 342 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9 +Q01852 UniProtKB Beta strand 358 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9 +Q01852 UniProtKB Beta strand 363 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9 +Q01852 UniProtKB Beta strand 377 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9 +Q01852 UniProtKB Beta strand 386 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9 +Q01852 UniProtKB Beta strand 394 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9 +Q01852 UniProtKB Beta strand 406 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FXT +Q01852 UniProtKB Beta strand 412 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FXT +Q01852 UniProtKB Beta strand 417 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QK9 +##sequence-region P27654 1 210 +P27654 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10216230,ECO:0000269|PubMed:7746155,ECO:0000269|PubMed:7768807,ECO:0000269|PubMed:9818717;Dbxref=PMID:10216230,PMID:7746155,PMID:7768807,PMID:9818717 +P27654 UniProtKB Chain 20 186 . . . ID=PRO_0000033237;Note=Temperature shock-inducible protein 1 +P27654 UniProtKB Propeptide 187 210 . . . ID=PRO_0000033238;Note=Removed in mature form +P27654 UniProtKB Compositional bias 101 120 . . . Note=Ala/Ser-rich +P27654 UniProtKB Lipidation 186 186 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10216230;Dbxref=PMID:10216230 +##sequence-region P10863 1 254 +P10863 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10863 UniProtKB Chain 19 233 . . . ID=PRO_0000033233;Note=Cold shock-induced protein TIR1 +P10863 UniProtKB Propeptide 234 254 . . . ID=PRO_0000033234;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10863 UniProtKB Repeat 114 119 . . . Note=1-1 +P10863 UniProtKB Repeat 120 125 . . . Note=1-2 +P10863 UniProtKB Repeat 126 131 . . . Note=1-3 +P10863 UniProtKB Repeat 132 137 . . . Note=1-4 +P10863 UniProtKB Repeat 138 143 . . . Note=1-5 +P10863 UniProtKB Repeat 144 155 . . . Note=2-1 +P10863 UniProtKB Repeat 156 167 . . . Note=2-2 +P10863 UniProtKB Repeat 168 179 . . . Note=2-3 +P10863 UniProtKB Repeat 180 191 . . . Note=2-4 +P10863 UniProtKB Repeat 192 203 . . . Note=2-5 +P10863 UniProtKB Repeat 210 224 . . . Note=PIR1/2/3 +P10863 UniProtKB Region 114 143 . . . Note=5 X 6 AA approximate tandem repeats%2C Ala/Ser-rich +P10863 UniProtKB Region 144 203 . . . Note=5 X 12 AA approximate tandem repeats%2C Ala/Ser-rich +P10863 UniProtKB Site 220 220 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P10863 UniProtKB Lipidation 233 233 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P54837 1 211 +P54837 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10713261,ECO:0000269|PubMed:8900179;Dbxref=PMID:10713261,PMID:8900179 +P54837 UniProtKB Chain 21 211 . . . ID=PRO_0000010414;Note=Endoplasmic reticulum vesicle protein 25 +P54837 UniProtKB Topological domain 21 180 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54837 UniProtKB Transmembrane 181 201 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54837 UniProtKB Topological domain 202 211 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54837 UniProtKB Domain 33 121 . . . Note=GOLD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00096 +P54837 UniProtKB Mutagenesis 206 208 . . . Note=Decrease in COPI-binding. KTK->ATA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11560939;Dbxref=PMID:11560939 +##sequence-region P32802 1 667 +P32802 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8314797;Dbxref=PMID:8314797 +P32802 UniProtKB Chain 23 667 . . . ID=PRO_0000034371;Note=Transmembrane 9 superfamily member 1 +P32802 UniProtKB Chain 23 250 . . . ID=PRO_0000034372;Note=Protein p24a +P32802 UniProtKB Topological domain 23 302 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Transmembrane 303 323 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Topological domain 324 370 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Transmembrane 371 391 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Topological domain 392 405 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Transmembrane 406 426 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Topological domain 427 442 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Transmembrane 443 463 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Topological domain 464 474 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Transmembrane 475 495 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Topological domain 496 527 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Transmembrane 528 548 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Topological domain 549 560 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Transmembrane 561 581 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Topological domain 582 596 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Transmembrane 597 617 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Topological domain 618 635 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Transmembrane 636 656 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Topological domain 657 667 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Site 250 251 . . . Note=Cleavage%3B by KEX2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Glycosylation 61 61 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Glycosylation 282 282 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32802 UniProtKB Sequence conflict 207 207 . . . Note=R->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32802 UniProtKB Sequence conflict 268 268 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32802 UniProtKB Sequence conflict 488 488 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06417 1 326 +Q06417 UniProtKB Chain 1 326 . . . ID=PRO_0000247778;Note=Uncharacterized oxidoreductase TDA5 +Q06417 UniProtKB Transmembrane 9 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06417 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06417 UniProtKB Nucleotide binding 74 98 . . . Note=NAD or NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06417 UniProtKB Active site 214 214 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001 +Q06417 UniProtKB Binding site 201 201 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q03290 1 321 +Q03290 UniProtKB Chain 1 321 . . . ID=PRO_0000055942;Note=RNA polymerase II transcription factor B subunit 3 +Q03290 UniProtKB Zinc finger 13 60 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +Q03290 UniProtKB Modified residue 157 157 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03290 UniProtKB Modified residue 258 258 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +##sequence-region P46678 1 594 +P46678 UniProtKB Chain 1 594 . . . ID=PRO_0000072498;Note=Transcription factor TFIIIB component B'' +P46678 UniProtKB Domain 415 466 . . . Note=SANT +P46678 UniProtKB Modified residue 49 49 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P46678 UniProtKB Modified residue 178 178 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q12415 1 435 +Q12415 UniProtKB Chain 1 435 . . . ID=PRO_0000072499;Note=Transcription factor tau 55 kDa subunit +Q12415 UniProtKB Modified residue 365 365 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12415 UniProtKB Sequence conflict 9 9 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12415 UniProtKB Beta strand 5 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0 +Q12415 UniProtKB Helix 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0 +Q12415 UniProtKB Beta strand 18 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0 +Q12415 UniProtKB Helix 38 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0 +Q12415 UniProtKB Beta strand 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0 +Q12415 UniProtKB Helix 67 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0 +Q12415 UniProtKB Beta strand 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0 +Q12415 UniProtKB Helix 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0 +Q12415 UniProtKB Helix 108 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0 +Q12415 UniProtKB Turn 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0 +Q12415 UniProtKB Helix 136 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0 +Q12415 UniProtKB Beta strand 163 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0 +Q12415 UniProtKB Helix 170 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0 +Q12415 UniProtKB Beta strand 204 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0 +Q12415 UniProtKB Helix 231 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0 +Q12415 UniProtKB Beta strand 236 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0 +Q12415 UniProtKB Helix 257 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN0 +##sequence-region P40308 1 642 +P40308 UniProtKB Chain 1 642 . . . ID=PRO_0000203356;Note=Lipase 3 +P40308 UniProtKB Transmembrane 200 220 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40308 UniProtKB Transmembrane 228 248 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40308 UniProtKB Domain 204 392 . . . Note=PNPLA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161 +P40308 UniProtKB Motif 235 239 . . . Note=GXSXG;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161 +P40308 UniProtKB Active site 237 237 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40308 UniProtKB Sequence conflict 96 96 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40308 UniProtKB Sequence conflict 100 100 . . . Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P42883 1 340 +P42883 UniProtKB Chain 1 340 . . . ID=PRO_0000211620;Note=4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI12 +P42883 UniProtKB Region 115 118 . . . Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534 +P42883 UniProtKB Motif 195 199 . . . Note=CCCFC%3B essential for catalytic activity%2C may be the site of iron coordination;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534 +P42883 UniProtKB Active site 66 66 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534 +P42883 UniProtKB Modified residue 62 62 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534 +##sequence-region Q08224 1 551 +Q08224 UniProtKB Chain 1 551 . . . ID=PRO_0000192041;Note=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20 +Q08224 UniProtKB Binding site 64 64 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08224 UniProtKB Sequence conflict 323 323 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08224 UniProtKB Beta strand 3 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 15 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Beta strand 25 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Beta strand 36 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 39 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Beta strand 53 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Beta strand 69 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 77 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Beta strand 94 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 103 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Beta strand 122 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 142 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Beta strand 155 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 161 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 178 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Beta strand 196 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Beta strand 212 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Turn 220 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Beta strand 224 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 241 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 259 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Turn 293 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 300 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 333 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Turn 341 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 344 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 354 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 366 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 397 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Turn 430 434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 440 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 458 477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Turn 478 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 490 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 501 518 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 523 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +Q08224 UniProtKB Helix 526 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RM5 +##sequence-region P40340 1 1379 +P40340 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P40340 UniProtKB Chain 2 1379 . . . ID=PRO_0000084771;Note=Tat-binding homolog 7 +P40340 UniProtKB Domain 1044 1086 . . . Note=Bromo%3B divergent;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 +P40340 UniProtKB Nucleotide binding 454 461 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40340 UniProtKB Compositional bias 135 139 . . . Note=Poly-Glu +P40340 UniProtKB Compositional bias 157 160 . . . Note=Poly-Arg +P40340 UniProtKB Compositional bias 358 361 . . . Note=Poly-Asn +P40340 UniProtKB Compositional bias 390 395 . . . Note=Poly-Lys +P40340 UniProtKB Compositional bias 737 740 . . . Note=Poly-Glu +P40340 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P40340 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +P40340 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P40340 UniProtKB Modified residue 94 94 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40340 UniProtKB Modified residue 212 212 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40340 UniProtKB Modified residue 229 229 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40340 UniProtKB Modified residue 241 241 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40340 UniProtKB Modified residue 259 259 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40340 UniProtKB Modified residue 285 285 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40340 UniProtKB Modified residue 367 367 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40340 UniProtKB Modified residue 369 369 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40340 UniProtKB Modified residue 370 370 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40340 UniProtKB Modified residue 735 735 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40340 UniProtKB Modified residue 1142 1142 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40340 UniProtKB Modified residue 1256 1256 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40340 UniProtKB Sequence conflict 70 70 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40340 UniProtKB Sequence conflict 241 241 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40340 UniProtKB Sequence conflict 1016 1016 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40340 UniProtKB Sequence conflict 1142 1142 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40340 UniProtKB Sequence conflict 1153 1153 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40340 UniProtKB Sequence conflict 1250 1250 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40340 UniProtKB Sequence conflict 1276 1276 . . . Note=I->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40340 UniProtKB Sequence conflict 1283 1283 . . . Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38228 1 572 +P38228 UniProtKB Transit peptide 1 16 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38228 UniProtKB Chain 17 572 . . . ID=PRO_0000063639;Note=Mitochondrial chaperone TCM62 +P38228 UniProtKB Topological domain 17 471 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38228 UniProtKB Transmembrane 472 488 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38228 UniProtKB Topological domain 489 572 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08921 1 799 +Q08921 UniProtKB Chain 1 799 . . . ID=PRO_0000271786;Note=Target of rapamycin complex 1 subunit TCO89 +Q08921 UniProtKB Modified residue 52 52 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q08921 UniProtKB Modified residue 82 82 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08921 UniProtKB Modified residue 84 84 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08921 UniProtKB Modified residue 104 104 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q08921 UniProtKB Modified residue 107 107 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +Q08921 UniProtKB Modified residue 115 115 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08921 UniProtKB Modified residue 144 144 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q08921 UniProtKB Modified residue 203 203 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08921 UniProtKB Modified residue 215 215 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08921 UniProtKB Modified residue 290 290 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08921 UniProtKB Modified residue 397 397 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08921 UniProtKB Modified residue 575 575 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08921 UniProtKB Modified residue 707 707 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P32776 1 642 +P32776 UniProtKB Chain 1 642 . . . ID=PRO_0000119261;Note=RNA polymerase II transcription factor B subunit 1 +P32776 UniProtKB Domain 165 221 . . . Note=BSD 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00036 +P32776 UniProtKB Domain 243 295 . . . Note=BSD 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00036 +P32776 UniProtKB Modified residue 150 150 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32776 UniProtKB Sequence conflict 209 209 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32776 UniProtKB Beta strand 3 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O +P32776 UniProtKB Beta strand 13 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O +P32776 UniProtKB Beta strand 21 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O +P32776 UniProtKB Beta strand 26 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O +P32776 UniProtKB Beta strand 37 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O +P32776 UniProtKB Beta strand 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O +P32776 UniProtKB Beta strand 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LOX +P32776 UniProtKB Beta strand 56 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O +P32776 UniProtKB Beta strand 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O +P32776 UniProtKB Beta strand 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K2U +P32776 UniProtKB Beta strand 85 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O +P32776 UniProtKB Helix 94 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y5O +##sequence-region P33339 1 1025 +P33339 UniProtKB Chain 1 1025 . . . ID=PRO_0000106364;Note=Transcription factor tau 131 kDa subunit +P33339 UniProtKB Repeat 128 161 . . . Note=TPR 1 +P33339 UniProtKB Repeat 162 195 . . . Note=TPR 2 +P33339 UniProtKB Repeat 196 229 . . . Note=TPR 3 +P33339 UniProtKB Repeat 230 263 . . . Note=TPR 4 +P33339 UniProtKB Repeat 264 297 . . . Note=TPR 5 +P33339 UniProtKB Repeat 432 465 . . . Note=TPR 6 +P33339 UniProtKB Repeat 467 501 . . . Note=TPR 7 +P33339 UniProtKB Repeat 502 535 . . . Note=TPR 8 +P33339 UniProtKB Repeat 536 569 . . . Note=TPR 9 +P33339 UniProtKB Repeat 875 908 . . . Note=TPR 10 +P33339 UniProtKB Repeat 959 992 . . . Note=TPR 11 +P33339 UniProtKB Region 128 569 . . . Note=Sufficient to bind BDP1 +P33339 UniProtKB Modified residue 311 311 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33339 UniProtKB Natural variant 280 280 . . . Note=In strain: SK1. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P33339 UniProtKB Natural variant 635 635 . . . Note=In strain: SK1. M->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P33339 UniProtKB Natural variant 1025 1025 . . . Note=In strain: SK1. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P33339 UniProtKB Mutagenesis 148 148 . . . Note=In PCF1-17%3B increases RNA polymerase III gene transcription. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372943;Dbxref=PMID:9372943 +P33339 UniProtKB Mutagenesis 162 162 . . . Note=In PCF1-12%3B increases RNA polymerase III gene transcription. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372943;Dbxref=PMID:9372943 +P33339 UniProtKB Mutagenesis 162 162 . . . Note=In PCF1-139%3B increases RNA polymerase III gene transcription. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372943;Dbxref=PMID:9372943 +P33339 UniProtKB Mutagenesis 164 164 . . . Note=In PCF1-19%3B increases RNA polymerase III gene transcription. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372943;Dbxref=PMID:9372943 +P33339 UniProtKB Mutagenesis 167 167 . . . Note=In PCF1-2%3B increases RNA polymerase III gene transcription due to an increase in the recruitment of BRF1 to TFIIIC-DNA. No affect on affinity of TFIIIC for DNA. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372943;Dbxref=PMID:9372943 +P33339 UniProtKB Mutagenesis 172 172 . . . Note=In PCF1-11%3B increases RNA polymerase III gene transcription. Y->C +P33339 UniProtKB Mutagenesis 188 188 . . . Note=In PCF1-23%3B increases RNA polymerase III gene transcription. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372943;Dbxref=PMID:9372943 +P33339 UniProtKB Mutagenesis 190 190 . . . Note=In PCF1-1%3B affects the rate of recruitment of TFIIIB to the template. Increases the amount of transcriptionally active TFIIIB. Increases RNA polymerase III gene transcription. Increases the binding affinity for BRF1%2C but does not affect the binding affinity for BDP1 in the TFIIIC-dependent assembly of TFIIIB. Overcomes autoinhibition of BRF1 binding. H->Y;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12167707,ECO:0000269|PubMed:7488859,ECO:0000269|PubMed:8264649,ECO:0000269|PubMed:9372943;Dbxref=PMID:12167707,PMID:7488859,PMID:8264649,PMID:9372943 +P33339 UniProtKB Mutagenesis 192 192 . . . Note=In PCF1-138%3B increases RNA polymerase III gene transcription. N->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372943;Dbxref=PMID:9372943 +P33339 UniProtKB Mutagenesis 199 199 . . . Note=In PCF1-15%3B increases RNA polymerase III gene transcription. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372943;Dbxref=PMID:9372943 +P33339 UniProtKB Mutagenesis 469 469 . . . Note=RNA polymerase III defective. Defect in the recruitment of BRF1 into TFIIIB-TFIIIC-DNA complexes and diminished direct interaction between TFC4 and BRF1. Decreased binding affinity for BDP1 incorporation into TFIIIB-TFIIIC-DNA complexes and inhibited binary interaction between BDP1 and TFC4. L->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12930823;Dbxref=PMID:12930823 +P33339 UniProtKB Mutagenesis 472 472 . . . Note=RNA polymerase III defective. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12930823;Dbxref=PMID:12930823 +P33339 UniProtKB Mutagenesis 504 504 . . . Note=RNA polymerase III defective. V->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12930823;Dbxref=PMID:12930823 +P33339 UniProtKB Mutagenesis 541 541 . . . Note=RNA polymerase III defective. S->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12930823;Dbxref=PMID:12930823 +P33339 UniProtKB Mutagenesis 542 542 . . . Note=RNA polymerase III defective. L->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12930823;Dbxref=PMID:12930823 +P33339 UniProtKB Mutagenesis 728 728 . . . Note=In PCF1-8%3B increases RNA polymerase III transcription. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7488859;Dbxref=PMID:7488859 +P33339 UniProtKB Mutagenesis 728 728 . . . Note=In PCF1-7%3B increases RNA polymerase III transcription. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7488859;Dbxref=PMID:7488859 +P33339 UniProtKB Mutagenesis 728 728 . . . Note=In PCF1-4%3B increases RNA polymerase III transcription ninefold over wild-type. Increases the amount of transcriptionally active TFIIIB. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7488859;Dbxref=PMID:7488859 +P33339 UniProtKB Mutagenesis 728 728 . . . Note=In PCF1-3%3B increases RNA polymerase III transcription two- to threefold over wild-type. Increases the amount of transcriptionally active TFIIIB. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7488859;Dbxref=PMID:7488859 +P33339 UniProtKB Mutagenesis 728 728 . . . Note=In PCF1-5%3B increases RNA polymerase III transcription. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7488859;Dbxref=PMID:7488859 +P33339 UniProtKB Mutagenesis 728 728 . . . Note=In PCF1-6%3B increases RNA polymerase III transcription. R->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7488859;Dbxref=PMID:7488859 +P33339 UniProtKB Helix 133 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 146 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 151 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 162 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 178 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 196 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 212 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 230 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 246 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 264 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 280 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 344 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 357 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 374 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 388 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 396 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 408 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 414 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Turn 421 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Beta strand 424 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 432 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Turn 444 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 448 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 456 458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 463 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 467 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 483 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 491 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 497 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 502 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 518 530 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 536 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +P33339 UniProtKB Helix 552 563 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIO +##sequence-region Q08686 1 304 +Q08686 UniProtKB Chain 1 304 . . . ID=PRO_0000139402;Note=Thiosulfate sulfurtransferase TUM1 +Q08686 UniProtKB Domain 20 137 . . . Note=Rhodanese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173 +Q08686 UniProtKB Domain 177 299 . . . Note=Rhodanese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173 +Q08686 UniProtKB Active site 259 259 . . . Note=Cysteine persulfide intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173 +Q08686 UniProtKB Binding site 191 191 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08686 UniProtKB Modified residue 201 201 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08686 UniProtKB Modified residue 264 264 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q08686 UniProtKB Beta strand 5 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Helix 9 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Beta strand 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Beta strand 24 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Helix 34 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Helix 40 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Turn 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Beta strand 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Helix 75 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Beta strand 92 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Beta strand 98 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Helix 104 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Beta strand 117 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Helix 125 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Helix 158 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Helix 165 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Helix 177 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Beta strand 182 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Helix 189 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Beta strand 199 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Beta strand 211 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Helix 216 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Turn 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Helix 232 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Beta strand 255 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Beta strand 260 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Helix 263 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Beta strand 279 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Helix 286 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +Q08686 UniProtKB Helix 296 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UTN +##sequence-region P42949 1 149 +P42949 UniProtKB Chain 1 149 . . . ID=PRO_0000214098;Note=Mitochondrial import inner membrane translocase subunit TIM16 +P42949 UniProtKB Region 57 113 . . . Note=J-like +P42949 UniProtKB Mutagenesis 88 90 . . . Note=Does not confer ability to stimulate the ATPase activity of mtHSP70. DKE->HPD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15218029;Dbxref=PMID:15218029 +P42949 UniProtKB Sequence conflict 114 114 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P42949 UniProtKB Helix 55 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ +P42949 UniProtKB Helix 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ +P42949 UniProtKB Helix 73 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ +P42949 UniProtKB Helix 89 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ +P42949 UniProtKB Helix 95 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GUZ +##sequence-region Q12328 1 207 +Q12328 UniProtKB Chain 1 207 . . . ID=PRO_0000210301;Note=Mitochondrial import inner membrane translocase subunit TIM22 +Q12328 UniProtKB Transmembrane 47 67 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12328 UniProtKB Transmembrane 152 172 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12328 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P33315 1 681 +P33315 UniProtKB Chain 1 681 . . . ID=PRO_0000191905;Note=Transketolase 2 +P33315 UniProtKB Nucleotide binding 116 118 . . . Note=Thiamine pyrophosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Active site 418 418 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Metal binding 157 157 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Metal binding 187 187 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Metal binding 189 189 . . . Note=Magnesium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Binding site 30 30 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Binding site 69 69 . . . Note=Thiamine pyrophosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Binding site 158 158 . . . Note=Thiamine pyrophosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Binding site 187 187 . . . Note=Thiamine pyrophosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Binding site 263 263 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Binding site 263 263 . . . Note=Thiamine pyrophosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Binding site 359 359 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Binding site 386 386 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Binding site 418 418 . . . Note=Thiamine pyrophosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Binding site 445 445 . . . Note=Thiamine pyrophosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Binding site 469 469 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Binding site 477 477 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Binding site 528 528 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Site 30 30 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Site 263 263 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33315 UniProtKB Modified residue 286 286 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23254 +P33315 UniProtKB Cross-link 648 648 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23254 +##sequence-region Q12239 1 342 +Q12239 UniProtKB Chain 1 342 . . . ID=PRO_0000235931;Note=Transmembrane protein 115 homolog +Q12239 UniProtKB Topological domain 1 21 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12239 UniProtKB Transmembrane 22 42 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12239 UniProtKB Topological domain 43 121 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12239 UniProtKB Transmembrane 122 142 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12239 UniProtKB Topological domain 143 159 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12239 UniProtKB Transmembrane 160 180 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12239 UniProtKB Topological domain 181 207 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12239 UniProtKB Transmembrane 208 228 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12239 UniProtKB Topological domain 229 342 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12239 UniProtKB Glycosylation 114 114 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03525 1 211 +Q03525 UniProtKB Chain 1 211 . . . ID=PRO_0000203349;Note=Protein TMA23 +Q03525 UniProtKB Compositional bias 130 133 . . . Note=Poly-Arg +Q03525 UniProtKB Compositional bias 158 167 . . . Note=Poly-Lys +##sequence-region Q04600 1 565 +Q04600 UniProtKB Chain 1 565 . . . ID=PRO_0000244640;Note=Translation machinery-associated protein 64 +Q04600 UniProtKB Domain 89 170 . . . Note=PUA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00161 +Q04600 UniProtKB Domain 363 446 . . . Note=SWIB +Q04600 UniProtKB Domain 475 547 . . . Note=SUI1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00200 +Q04600 UniProtKB Compositional bias 558 565 . . . Note=Poly-Lys +##sequence-region P36165 1 910 +P36165 UniProtKB Chain 1 910 . . . ID=PRO_0000203227;Note=Lipase 4 +P36165 UniProtKB Transmembrane 282 302 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36165 UniProtKB Transmembrane 310 326 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36165 UniProtKB Transmembrane 426 442 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36165 UniProtKB Domain 282 483 . . . Note=PNPLA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161 +P36165 UniProtKB Motif 286 291 . . . Note=GXGXXG;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161 +P36165 UniProtKB Motif 313 317 . . . Note=GXSXG;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161 +P36165 UniProtKB Active site 315 315 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161 +P36165 UniProtKB Active site 470 470 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161 +P36165 UniProtKB Modified residue 55 55 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36165 UniProtKB Modified residue 737 737 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36165 UniProtKB Modified residue 749 749 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36165 UniProtKB Modified residue 751 751 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198 +P36165 UniProtKB Modified residue 836 836 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P47183 1 340 +P47183 UniProtKB Chain 1 340 . . . ID=PRO_0000211619;Note=4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI11 +P47183 UniProtKB Region 115 118 . . . Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534 +P47183 UniProtKB Motif 195 199 . . . Note=CCCFC%3B essential for catalytic activity%2C may be the site of iron coordination;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534 +P47183 UniProtKB Active site 66 66 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534 +P47183 UniProtKB Modified residue 62 62 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534 +##sequence-region Q07471 1 609 +Q07471 UniProtKB Chain 1 609 . . . ID=PRO_0000090836;Note=Thiamine metabolism regulatory protein THI3 +##sequence-region P43534 1 340 +P43534 UniProtKB Chain 1 340 . . . ID=PRO_0000211618;Note=4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI5 +P43534 UniProtKB Region 115 118 . . . Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037 +P43534 UniProtKB Motif 195 199 . . . Note=CCCFC%3B essential for catalytic activity%2C may be the site of iron coordination;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23048037;Dbxref=PMID:23048037 +P43534 UniProtKB Active site 66 66 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23048037;Dbxref=PMID:23048037 +P43534 UniProtKB Modified residue 62 62 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037 +P43534 UniProtKB Mutagenesis 11 11 . . . Note=Unable to sustain growth in thiamine-free medium. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037 +P43534 UniProtKB Mutagenesis 12 12 . . . Note=Unable to sustain growth in thiamine-free medium. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037 +P43534 UniProtKB Mutagenesis 62 62 . . . Note=Unable to sustain growth in thiamine-free medium. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037 +P43534 UniProtKB Mutagenesis 66 66 . . . Note=Unable to sustain growth in thiamine-free medium. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037 +P43534 UniProtKB Mutagenesis 195 195 . . . Note=Attenuates the coordination of ion and is unable to sustain growth in thiamine-free medium. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037 +P43534 UniProtKB Mutagenesis 196 196 . . . Note=Attenuates the coordination of ion and is unable to sustain growth in thiamine-free medium. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037 +P43534 UniProtKB Mutagenesis 197 197 . . . Note=Attenuates the coordination of ion and is unable to sustain growth in thiamine-free medium. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037 +P43534 UniProtKB Mutagenesis 199 199 . . . Note=Attenuates the coordination of ion and is unable to sustain growth in thiamine-free medium. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23048037;Dbxref=PMID:23048037 +P43534 UniProtKB Beta strand 6 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Beta strand 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 16 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 19 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 29 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Beta strand 37 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 45 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 48 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Beta strand 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Beta strand 59 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 64 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Turn 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Beta strand 77 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Beta strand 89 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Turn 95 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 103 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Beta strand 110 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 117 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H67 +P43534 UniProtKB Turn 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H67 +P43534 UniProtKB Beta strand 135 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 145 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Beta strand 153 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Turn 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 164 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 179 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Beta strand 182 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Beta strand 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H6D +P43534 UniProtKB Helix 196 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H6D +P43534 UniProtKB Beta strand 201 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 207 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 214 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 235 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 247 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 252 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Turn 262 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 273 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +P43534 UniProtKB Helix 315 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H65 +##sequence-region P41835 1 540 +P41835 UniProtKB Chain 1 540 . . . ID=PRO_0000157090;Note=Thiamine biosynthetic bifunctional enzyme +P41835 UniProtKB Region 1 238 . . . Note=Thiamine-phosphate synthase +P41835 UniProtKB Region 43 47 . . . Note=HMP-PP binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41835 UniProtKB Region 143 145 . . . Note=THZ-P binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41835 UniProtKB Region 209 210 . . . Note=THZ-P binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41835 UniProtKB Region 239 540 . . . Note=Hydroxyethylthiazole kinase +P41835 UniProtKB Active site 465 465 . . . Note=Proton acceptor%3B for hydroxyethylthiazole kinase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41835 UniProtKB Metal binding 76 76 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41835 UniProtKB Metal binding 95 95 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41835 UniProtKB Binding site 75 75 . . . Note=HMP-PP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41835 UniProtKB Binding site 114 114 . . . Note=HMP-PP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41835 UniProtKB Binding site 146 146 . . . Note=HMP-PP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41835 UniProtKB Binding site 181 181 . . . Note=THZ-P%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41835 UniProtKB Binding site 290 290 . . . Note=4-methyl-5-(2-hydroxyethyl)thiazole%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41835 UniProtKB Binding site 365 365 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41835 UniProtKB Binding site 415 415 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41835 UniProtKB Binding site 462 462 . . . Note=4-methyl-5-(2-hydroxyethyl)thiazole%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41835 UniProtKB Natural variant 370 370 . . . Note=In THI6-3%3B possesses TMP-PPASE activity only. E->K +P41835 UniProtKB Natural variant 476 476 . . . Note=In THI6-2%3B both enzyme activities greatly decreased. G->D +P41835 UniProtKB Natural variant 510 510 . . . Note=In THI6-1%3B both enzyme activities greatly decreased. G->D +##sequence-region P27796 1 417 +P27796 UniProtKB Active site 125 125 . . . Note=Acyl-thioester intermediate +P27796 UniProtKB Active site 375 375 . . . Note=Proton acceptor +P27796 UniProtKB Active site 403 403 . . . Note=Proton acceptor +P27796 UniProtKB Helix 1 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P27796 UniProtKB Turn 26 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Beta strand 36 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Turn 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Turn 53 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 59 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 76 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Beta strand 88 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Beta strand 93 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 100 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Beta strand 118 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 124 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 127 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Beta strand 145 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 155 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 171 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 179 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 186 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 201 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Turn 225 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 251 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Turn 263 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Turn 270 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Beta strand 276 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 288 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Beta strand 300 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 312 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 318 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 334 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Beta strand 338 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 347 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 361 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 370 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Turn 377 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Helix 380 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Beta strand 397 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Turn 405 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +P27796 UniProtKB Beta strand 408 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AFW +##sequence-region P87108 1 93 +P87108 UniProtKB Chain 1 93 . . . ID=PRO_0000193622;Note=Mitochondrial import inner membrane translocase subunit TIM10 +P87108 UniProtKB Region 1 31 . . . Note=Interaction with transmembrane regions of transmembrane proteins in transit +P87108 UniProtKB Region 73 93 . . . Note=Required for heterohexamerization +P87108 UniProtKB Motif 40 65 . . . Note=Twin CX3C motif +P87108 UniProtKB Disulfide bond 40 65 . . . . +P87108 UniProtKB Disulfide bond 44 61 . . . . +P87108 UniProtKB Mutagenesis 40 40 . . . Note=Induces impairment in folding and loss of zinc-binding. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12882976,ECO:0000269|PubMed:14973126;Dbxref=PMID:12882976,PMID:14973126 +P87108 UniProtKB Mutagenesis 44 44 . . . Note=Loss of function due to severely affected folding and the presence of non-native disulfide bonds%3B loss of zinc-binding. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12882976,ECO:0000269|PubMed:14973126;Dbxref=PMID:12882976,PMID:14973126 +P87108 UniProtKB Mutagenesis 61 61 . . . Note=Loss of function due to severely affected folding and the presence of non-native disulfide bonds%3B loss of zinc-binding. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12882976,ECO:0000269|PubMed:14973126;Dbxref=PMID:12882976,PMID:14973126 +P87108 UniProtKB Mutagenesis 65 65 . . . Note=Induces impairment in folding and loss of zinc-binding. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12882976,ECO:0000269|PubMed:14973126;Dbxref=PMID:12882976,PMID:14973126 +P87108 UniProtKB Turn 16 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DXR +P87108 UniProtKB Helix 20 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DXR +P87108 UniProtKB Helix 56 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DXR +##sequence-region P33891 1 701 +P33891 UniProtKB Chain 1 701 . . . ID=PRO_0000072543;Note=Protein transport protein TIP20 +P33891 UniProtKB Domain 147 701 . . . Note=RINT1/TIP20;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00717 +P33891 UniProtKB Helix 10 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P33891 UniProtKB Helix 46 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 59 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 73 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 115 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 142 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 161 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Turn 179 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 192 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 239 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 262 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 290 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 296 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 309 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 324 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 352 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 358 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 383 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 389 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 406 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 413 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 417 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 427 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Beta strand 446 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 450 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 478 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 500 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 513 529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 531 535 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 538 540 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 558 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 561 575 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 581 601 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Turn 602 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 611 625 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 637 649 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 650 653 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 655 657 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Turn 658 661 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 663 668 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 673 678 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Beta strand 681 683 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +P33891 UniProtKB Helix 685 696 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FHN +##sequence-region P89886 1 181 +P89886 UniProtKB Chain 1 181 . . . ID=PRO_0000245367;Note=Translation machinery-associated protein 20 +P89886 UniProtKB Domain 90 172 . . . Note=PUA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00161 +P89886 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region Q12049 1 470 +Q12049 UniProtKB Chain 1 470 . . . ID=PRO_0000257823;Note=Protein THP3 +Q12049 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P40462 1 946 +P40462 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40462 UniProtKB Chain 2 946 . . . ID=PRO_0000095121;Note=Protein TMA108 +P40462 UniProtKB Region 293 297 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40462 UniProtKB Active site 331 331 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P40462 UniProtKB Metal binding 330 330 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P40462 UniProtKB Metal binding 334 334 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P40462 UniProtKB Metal binding 353 353 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P40462 UniProtKB Site 423 423 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40462 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P36142 1 418 +P36142 UniProtKB Chain 1 418 . . . ID=PRO_0000211558;Note=Transmembrane protein 184 homolog YKR051W +P36142 UniProtKB Topological domain 1 5 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36142 UniProtKB Transmembrane 6 26 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36142 UniProtKB Topological domain 27 43 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36142 UniProtKB Transmembrane 44 64 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36142 UniProtKB Topological domain 65 78 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36142 UniProtKB Transmembrane 79 99 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36142 UniProtKB Topological domain 100 141 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36142 UniProtKB Transmembrane 142 162 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36142 UniProtKB Topological domain 163 168 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36142 UniProtKB Transmembrane 169 189 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36142 UniProtKB Topological domain 190 205 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36142 UniProtKB Transmembrane 206 226 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36142 UniProtKB Topological domain 227 246 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36142 UniProtKB Transmembrane 247 267 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36142 UniProtKB Topological domain 268 418 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12513 1 150 +Q12513 UniProtKB Chain 1 150 . . . ID=PRO_0000240701;Note=Translation machinery-associated protein 17 +Q12513 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12513 UniProtKB Modified residue 68 68 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P53840 1 1238 +P53840 UniProtKB Chain 1 1238 . . . ID=PRO_0000072620;Note=Topoisomerase 1-associated factor 1 +P53840 UniProtKB Modified residue 626 626 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53840 UniProtKB Modified residue 654 654 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53840 UniProtKB Modified residue 1056 1056 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53840 UniProtKB Modified residue 1058 1058 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53840 UniProtKB Modified residue 1213 1213 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P40310 1 691 +P40310 UniProtKB Chain 1 691 . . . ID=PRO_0000101774;Note=Outward-rectifier potassium channel TOK1 +P40310 UniProtKB Topological domain 1 71 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40310 UniProtKB Transmembrane 72 92 . . . Note=Helical%3B Name%3DS1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40310 UniProtKB Topological domain 93 137 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40310 UniProtKB Transmembrane 138 158 . . . Note=Helical%3B Name%3DS2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40310 UniProtKB Topological domain 159 170 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40310 UniProtKB Transmembrane 171 191 . . . Note=Helical%3B Name%3DS3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40310 UniProtKB Topological domain 192 203 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40310 UniProtKB Transmembrane 204 224 . . . Note=Helical%3B Name%3DS4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40310 UniProtKB Topological domain 225 246 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40310 UniProtKB Transmembrane 247 266 . . . Note=Helical%3B Name%3DS5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40310 UniProtKB Topological domain 267 301 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40310 UniProtKB Transmembrane 302 322 . . . Note=Helical%3B Name%3DS6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40310 UniProtKB Topological domain 323 379 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40310 UniProtKB Transmembrane 380 400 . . . Note=Helical%3B Name%3DS7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40310 UniProtKB Topological domain 401 435 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40310 UniProtKB Transmembrane 436 456 . . . Note=Helical%3B Name%3DS8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40310 UniProtKB Topological domain 457 691 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40310 UniProtKB Modified residue 119 119 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40310 UniProtKB Sequence conflict 442 442 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40310 UniProtKB Sequence conflict 512 512 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03280 1 3268 +Q03280 UniProtKB Chain 1 3268 . . . ID=PRO_0000120348;Note=E3 ubiquitin-protein ligase TOM1 +Q03280 UniProtKB Domain 2932 3268 . . . Note=HECT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00104 +Q03280 UniProtKB Compositional bias 1879 2054 . . . Note=Asp-rich +Q03280 UniProtKB Active site 3235 3235 . . . Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00104 +Q03280 UniProtKB Modified residue 1890 1890 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q03280 UniProtKB Modified residue 2096 2096 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03280 UniProtKB Modified residue 2119 2119 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03280 UniProtKB Modified residue 2376 2376 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03280 UniProtKB Modified residue 2406 2406 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03280 UniProtKB Modified residue 2418 2418 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q03280 UniProtKB Mutagenesis 3235 3235 . . . Note=Loss of function. Induces a decrease in transcription activation. C->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10395901,ECO:0000269|PubMed:10873801,ECO:0000269|PubMed:9753545;Dbxref=PMID:10395901,PMID:10873801,PMID:9753545 +##sequence-region P35180 1 183 +P35180 UniProtKB Chain 1 183 . . . ID=PRO_0000051550;Note=Mitochondrial import receptor subunit TOM20 +P35180 UniProtKB Topological domain 1 8 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35180 UniProtKB Transmembrane 9 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35180 UniProtKB Topological domain 29 183 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35180 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P23644 1 387 +P23644 UniProtKB Chain 1 387 . . . ID=PRO_0000051535;Note=Mitochondrial import receptor subunit TOM40 +P23644 UniProtKB Sequence conflict 387 387 . . . Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P80967 1 50 +P80967 UniProtKB Chain 1 50 . . . ID=PRO_0000218264;Note=Mitochondrial import receptor subunit TOM5 +P80967 UniProtKB Topological domain 1 26 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P80967 UniProtKB Transmembrane 27 45 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38825 1 639 +P38825 UniProtKB Chain 1 639 . . . ID=PRO_0000106420;Note=Protein TOM71 +P38825 UniProtKB Topological domain 1 14 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38825 UniProtKB Transmembrane 15 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38825 UniProtKB Topological domain 33 639 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38825 UniProtKB Repeat 127 160 . . . Note=TPR 1 +P38825 UniProtKB Repeat 162 194 . . . Note=TPR 2 +P38825 UniProtKB Repeat 345 378 . . . Note=TPR 3 +P38825 UniProtKB Repeat 379 411 . . . Note=TPR 4 +P38825 UniProtKB Repeat 412 445 . . . Note=TPR 5 +P38825 UniProtKB Repeat 447 479 . . . Note=TPR 6 +P38825 UniProtKB Repeat 480 513 . . . Note=TPR 7 +P38825 UniProtKB Repeat 530 563 . . . Note=TPR 8 +P38825 UniProtKB Repeat 565 597 . . . Note=TPR 9 +P38825 UniProtKB Modified residue 55 55 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P38825 UniProtKB Helix 112 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 120 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 147 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 161 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 177 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 195 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 211 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 235 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 266 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 278 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 295 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 310 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 338 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 361 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 378 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 395 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 412 424 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 428 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 447 458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 462 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 481 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 496 512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 521 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 543 559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 564 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 580 593 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 598 617 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP2 +P38825 UniProtKB Helix 620 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FP3 +##sequence-region P32830 1 109 +P32830 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32830 UniProtKB Chain 2 109 . . . ID=PRO_0000096581;Note=Mitochondrial import inner membrane translocase subunit TIM12 +P32830 UniProtKB Motif 40 66 . . . Note=Twin CX3C motif +P32830 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32830 UniProtKB Disulfide bond 40 66 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32830 UniProtKB Disulfide bond 44 62 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53299 1 105 +P53299 UniProtKB Chain 1 105 . . . ID=PRO_0000193632;Note=Mitochondrial import inner membrane translocase subunit TIM13 +P53299 UniProtKB Motif 57 77 . . . Note=Twin CX3C motif +P53299 UniProtKB Disulfide bond 57 77 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53299 UniProtKB Disulfide bond 61 73 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53299 UniProtKB Mutagenesis 57 57 . . . Note=Abolishes import into mitochondrion%3B when associated with S-61. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941692;Dbxref=PMID:12941692 +P53299 UniProtKB Mutagenesis 61 61 . . . Note=Abolishes import into mitochondrion%3B when associated with S-57. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941692;Dbxref=PMID:12941692 +P53299 UniProtKB Mutagenesis 73 73 . . . Note=Abolishes import into mitochondrion%3B when associated with S-77. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941692;Dbxref=PMID:12941692 +P53299 UniProtKB Mutagenesis 77 77 . . . Note=Abolishes import into mitochondrion%3B when associated with S-73. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941692;Dbxref=PMID:12941692 +P53299 UniProtKB Helix 47 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CJH +P53299 UniProtKB Helix 71 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CJH +##sequence-region Q08749 1 192 +Q08749 UniProtKB Transit peptide 1 42 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08749 UniProtKB Chain 43 192 . . . ID=PRO_0000228080;Note=Mitochondrial import inner membrane translocase subunit TIM18 +Q08749 UniProtKB Topological domain 43 88 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08749 UniProtKB Transmembrane 89 109 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08749 UniProtKB Topological domain 110 113 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08749 UniProtKB Transmembrane 114 134 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08749 UniProtKB Topological domain 135 144 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08749 UniProtKB Transmembrane 145 165 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08749 UniProtKB Topological domain 166 192 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08749 UniProtKB Sequence conflict 137 137 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08749 UniProtKB Sequence conflict 137 137 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08749 UniProtKB Sequence conflict 137 137 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53220 1 239 +P53220 UniProtKB Transit peptide 1 70 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53220 UniProtKB Chain 71 239 . . . ID=PRO_0000043166;Note=Mitochondrial import inner membrane translocase subunit TIM21 +P53220 UniProtKB Topological domain 71 75 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53220 UniProtKB Transmembrane 76 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53220 UniProtKB Topological domain 97 239 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53220 UniProtKB Sequence conflict 39 39 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53220 UniProtKB Helix 104 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU +P53220 UniProtKB Helix 120 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU +P53220 UniProtKB Beta strand 139 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU +P53220 UniProtKB Beta strand 144 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU +P53220 UniProtKB Beta strand 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU +P53220 UniProtKB Beta strand 158 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU +P53220 UniProtKB Beta strand 168 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU +P53220 UniProtKB Beta strand 182 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU +P53220 UniProtKB Beta strand 199 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU +P53220 UniProtKB Beta strand 213 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIU +##sequence-region P33890 1 251 +P33890 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33890 UniProtKB Chain 19 231 . . . ID=PRO_0000033235;Note=Cold shock-induced protein TIR2 +P33890 UniProtKB Propeptide 232 251 . . . ID=PRO_0000372445;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33890 UniProtKB Repeat 207 225 . . . Note=PIR1/2/3 +P33890 UniProtKB Compositional bias 112 251 . . . Note=Ala/Ser-rich +P33890 UniProtKB Site 217 217 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33890 UniProtKB Lipidation 231 231 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33890 UniProtKB Sequence conflict 69 69 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33890 UniProtKB Sequence conflict 179 179 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33890 UniProtKB Sequence conflict 192 192 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08422 1 150 +Q08422 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q08422 UniProtKB Chain 2 150 . . . ID=PRO_0000237648;Note=AN1-type zinc finger protein TMC1 +Q08422 UniProtKB Zinc finger 82 134 . . . Note=AN1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00449 +Q08422 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q08422 UniProtKB Modified residue 43 43 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08422 UniProtKB Modified residue 54 54 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +##sequence-region P40071 1 706 +P40071 UniProtKB Signal peptide 1 33 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Chain 34 706 . . . ID=PRO_0000034373;Note=Transmembrane 9 superfamily member 3 +P40071 UniProtKB Topological domain 34 290 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Transmembrane 291 311 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Topological domain 312 371 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Transmembrane 372 392 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Topological domain 393 405 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Transmembrane 406 426 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Topological domain 427 456 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Transmembrane 457 477 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Topological domain 478 494 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Transmembrane 495 515 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Topological domain 516 553 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Transmembrane 554 574 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Topological domain 575 592 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Transmembrane 593 613 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Topological domain 614 637 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Transmembrane 638 658 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Topological domain 659 665 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Transmembrane 666 686 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40071 UniProtKB Topological domain 687 706 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32773 1 286 +P32773 UniProtKB Chain 1 286 . . . ID=PRO_0000072617;Note=Transcription initiation factor IIA large subunit +P32773 UniProtKB Sequence conflict 15 15 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32773 UniProtKB Helix 4 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2 +P32773 UniProtKB Helix 22 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2 +P32773 UniProtKB Helix 32 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2 +P32773 UniProtKB Helix 57 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RM1 +P32773 UniProtKB Beta strand 243 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2 +P32773 UniProtKB Beta strand 257 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2 +P32773 UniProtKB Beta strand 272 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2 +##sequence-region P04786 1 769 +P04786 UniProtKB Chain 1 769 . . . ID=PRO_0000145211;Note=DNA topoisomerase 1 +P04786 UniProtKB Region 357 358 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04786 UniProtKB Region 420 425 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04786 UniProtKB Region 512 514 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04786 UniProtKB Compositional bias 16 20 . . . Note=Poly-Asp +P04786 UniProtKB Compositional bias 55 136 . . . Note=Lys-rich +P04786 UniProtKB Compositional bias 105 139 . . . Note=Glu-rich +P04786 UniProtKB Active site 727 727 . . . Note=O-(3'-phospho-DNA)-tyrosine intermediate;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10130,ECO:0000269|PubMed:2542938,ECO:0000269|PubMed:2547758;Dbxref=PMID:2542938,PMID:2547758 +P04786 UniProtKB Site 296 296 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04786 UniProtKB Site 344 344 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04786 UniProtKB Site 375 375 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04786 UniProtKB Site 432 432 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04786 UniProtKB Site 458 458 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04786 UniProtKB Site 501 501 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04786 UniProtKB Site 558 558 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04786 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P04786 UniProtKB Modified residue 15 15 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P04786 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P04786 UniProtKB Modified residue 49 49 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04786 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P04786 UniProtKB Beta strand 168 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +P04786 UniProtKB Beta strand 173 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +P04786 UniProtKB Helix 179 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +P04786 UniProtKB Turn 191 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +P04786 UniProtKB Helix 196 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +P04786 UniProtKB Helix 200 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +P04786 UniProtKB Helix 229 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +P04786 UniProtKB Helix 235 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +P04786 UniProtKB Helix 256 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +P04786 UniProtKB Beta strand 272 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +P04786 UniProtKB Beta strand 278 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +P04786 UniProtKB Turn 300 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +P04786 UniProtKB Helix 311 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +P04786 UniProtKB Beta strand 315 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +P04786 UniProtKB Beta strand 320 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +P04786 UniProtKB Beta strand 334 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +P04786 UniProtKB Beta strand 345 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +P04786 UniProtKB Turn 351 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +P04786 UniProtKB Beta strand 356 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OIS +##sequence-region P06786 1 1428 +P06786 UniProtKB Chain 1 1428 . . . ID=PRO_0000145387;Note=DNA topoisomerase 2 +P06786 UniProtKB Domain 443 557 . . . Note=Toprim;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00995 +P06786 UniProtKB Nucleotide binding 127 129 . . . Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12963818;Dbxref=PMID:12963818 +P06786 UniProtKB Nucleotide binding 140 147 . . . Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12963818;Dbxref=PMID:12963818 +P06786 UniProtKB Nucleotide binding 365 367 . . . Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12963818;Dbxref=PMID:12963818 +P06786 UniProtKB Region 333 336 . . . Note=Interaction with DNA;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23022727;Dbxref=PMID:23022727 +P06786 UniProtKB Region 965 974 . . . Note=Interaction with DNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20485342;Dbxref=PMID:20485342 +P06786 UniProtKB Active site 782 782 . . . Note=O-(5'-phospho-DNA)-tyrosine intermediate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20485342,ECO:0000269|PubMed:9685374;Dbxref=PMID:20485342,PMID:9685374 +P06786 UniProtKB Metal binding 449 449 . . . Note=Magnesium 1%3B catalytic;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00995,ECO:0000269|PubMed:18097402;Dbxref=PMID:18097402 +P06786 UniProtKB Metal binding 526 526 . . . Note=Magnesium 1%3B catalytic;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00995,ECO:0000269|PubMed:18097402;Dbxref=PMID:18097402 +P06786 UniProtKB Metal binding 526 526 . . . Note=Magnesium 2;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00995,ECO:0000269|PubMed:18097402;Dbxref=PMID:18097402 +P06786 UniProtKB Metal binding 528 528 . . . Note=Magnesium 2;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00995,ECO:0000269|PubMed:18097402;Dbxref=PMID:18097402 +P06786 UniProtKB Binding site 70 70 . . . Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12963818;Dbxref=PMID:12963818 +P06786 UniProtKB Binding site 99 99 . . . Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12963818;Dbxref=PMID:12963818 +P06786 UniProtKB Site 477 477 . . . Note=Interaction with DNA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00995 +P06786 UniProtKB Site 480 480 . . . Note=Interaction with DNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20485342;Dbxref=PMID:20485342 +P06786 UniProtKB Site 650 650 . . . Note=Interaction with DNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20485342;Dbxref=PMID:20485342 +P06786 UniProtKB Site 651 651 . . . Note=Interaction with DNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20485342;Dbxref=PMID:20485342 +P06786 UniProtKB Site 700 700 . . . Note=Interaction with DNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20485342;Dbxref=PMID:20485342 +P06786 UniProtKB Site 734 734 . . . Note=Interaction with DNA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00995 +P06786 UniProtKB Site 740 740 . . . Note=Interaction with DNA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00995 +P06786 UniProtKB Site 781 781 . . . Note=Transition state stabilizer +P06786 UniProtKB Site 833 833 . . . Note=Important for DNA bending%3B intercalates between base pairs of target DNA +P06786 UniProtKB Site 908 908 . . . Note=Interaction with DNA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00995 +P06786 UniProtKB Modified residue 1086 1086 . . . Note=Phosphothreonine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274 +P06786 UniProtKB Modified residue 1087 1087 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274 +P06786 UniProtKB Modified residue 1252 1252 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06786 UniProtKB Modified residue 1258 1258 . . . Note=Phosphothreonine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274 +P06786 UniProtKB Modified residue 1266 1266 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274 +P06786 UniProtKB Modified residue 1269 1269 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274 +P06786 UniProtKB Modified residue 1272 1272 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274 +P06786 UniProtKB Modified residue 1353 1353 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274 +P06786 UniProtKB Modified residue 1356 1356 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274 +P06786 UniProtKB Modified residue 1408 1408 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274 +P06786 UniProtKB Modified residue 1423 1423 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1316274;Dbxref=PMID:1316274 +P06786 UniProtKB Mutagenesis 333 336 . . . Note=Reduced enzyme activity%3B abolishes stimulation of ATPase activity upon DNA binding. KKKK->AAAA +P06786 UniProtKB Mutagenesis 333 336 . . . Note=Strongly reduced enzyme activity%3B abolishes stimulation of ATPase activity upon DNA binding. KKKK->AEEA +P06786 UniProtKB Mutagenesis 690 690 . . . Note=Loss of enzyme activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685374;Dbxref=PMID:9685374 +P06786 UniProtKB Mutagenesis 697 697 . . . Note=Strongly reduced enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685374;Dbxref=PMID:9685374 +P06786 UniProtKB Mutagenesis 700 700 . . . Note=Strongly reduced enzyme activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685374;Dbxref=PMID:9685374 +P06786 UniProtKB Mutagenesis 704 704 . . . Note=Strongly reduced enzyme activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685374;Dbxref=PMID:9685374 +P06786 UniProtKB Mutagenesis 736 736 . . . Note=No effect. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685374;Dbxref=PMID:9685374 +P06786 UniProtKB Mutagenesis 781 781 . . . Note=Strongly reduced enzyme activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685374;Dbxref=PMID:9685374 +P06786 UniProtKB Mutagenesis 782 782 . . . Note=Loss of enzyme activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685374;Dbxref=PMID:9685374 +P06786 UniProtKB Mutagenesis 828 828 . . . Note=Strongly reduced enzyme activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685374;Dbxref=PMID:9685374 +P06786 UniProtKB Sequence conflict 74 74 . . . Note=N->NN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06786 UniProtKB Sequence conflict 547 547 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06786 UniProtKB Sequence conflict 837 837 . . . Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06786 UniProtKB Helix 8 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Beta strand 12 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Helix 17 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Helix 26 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Beta strand 35 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Turn 44 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Beta strand 48 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Helix 58 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Beta strand 83 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Turn 90 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Beta strand 94 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Turn 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Helix 116 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Beta strand 123 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Helix 145 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Beta strand 153 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Turn 163 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Beta strand 167 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Turn 175 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Beta strand 184 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Beta strand 194 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Helix 203 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Helix 213 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Beta strand 234 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Helix 247 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Turn 253 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Beta strand 280 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Beta strand 288 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Beta strand 296 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Beta strand 300 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Helix 315 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Helix 342 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Beta strand 349 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Beta strand 362 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Helix 374 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Beta strand 377 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Helix 385 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Helix 395 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PVG +P06786 UniProtKB Turn 433 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 438 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 444 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 451 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 466 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 479 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BGW +P06786 UniProtKB Helix 486 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RGR +P06786 UniProtKB Helix 492 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Turn 503 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BGW +P06786 UniProtKB Beta strand 506 508 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 513 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 519 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 527 530 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BGW +P06786 UniProtKB Helix 534 545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 547 550 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BGW +P06786 UniProtKB Beta strand 555 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 563 568 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 574 580 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 581 590 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Turn 591 594 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 597 599 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 609 629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 634 642 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RGR +P06786 UniProtKB Helix 647 656 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RGR +P06786 UniProtKB Beta strand 668 670 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RGR +P06786 UniProtKB Helix 678 691 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Turn 695 697 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 701 713 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 721 732 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 736 738 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 741 749 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Turn 753 755 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RGR +P06786 UniProtKB Beta strand 760 765 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Turn 770 773 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Turn 780 782 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 784 787 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 791 794 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 797 802 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 805 808 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 811 816 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 824 827 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 830 833 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 838 841 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 846 857 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 874 880 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 883 887 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 889 894 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 897 902 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 909 920 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 924 926 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BGW +P06786 UniProtKB Beta strand 932 935 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 938 940 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 943 946 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 949 958 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 960 963 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 967 971 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 975 978 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 984 989 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 990 1034 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Beta strand 1041 1043 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BGW +P06786 UniProtKB Helix 1045 1054 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Turn 1108 1110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 1114 1117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 1121 1124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 1126 1147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +P06786 UniProtKB Helix 1151 1176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BJT +##sequence-region P35169 1 2470 +P35169 UniProtKB Chain 1 2470 . . . ID=PRO_0000088813;Note=Serine/threonine-protein kinase TOR1 +P35169 UniProtKB Repeat 114 151 . . . Note=HEAT 1 +P35169 UniProtKB Repeat 249 286 . . . Note=HEAT 2 +P35169 UniProtKB Repeat 627 663 . . . Note=HEAT 3 +P35169 UniProtKB Repeat 664 701 . . . Note=HEAT 4 +P35169 UniProtKB Repeat 747 784 . . . Note=HEAT 5 +P35169 UniProtKB Repeat 788 826 . . . Note=HEAT 6 +P35169 UniProtKB Repeat 832 870 . . . Note=HEAT 7 +P35169 UniProtKB Repeat 908 946 . . . Note=HEAT 8 +P35169 UniProtKB Repeat 950 987 . . . Note=HEAT 9 +P35169 UniProtKB Repeat 1069 1107 . . . Note=HEAT 10 +P35169 UniProtKB Repeat 1109 1147 . . . Note=HEAT 11 +P35169 UniProtKB Domain 1331 1919 . . . Note=FAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534 +P35169 UniProtKB Domain 2125 2437 . . . Note=PI3K/PI4K;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00269 +P35169 UniProtKB Domain 2438 2470 . . . Note=FATC;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534,ECO:0000255|PROSITE-ProRule:PRU00535 +P35169 UniProtKB Region 1775 2157 . . . Note=Interaction with FKBP-rapamycin +P35169 UniProtKB Compositional bias 441 447 . . . Note=Arg/Lys-rich (basic) +P35169 UniProtKB Mutagenesis 1972 1972 . . . Note=No effect. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7606777,ECO:0000269|PubMed:8413204;Dbxref=PMID:7606777,PMID:8413204 +P35169 UniProtKB Mutagenesis 1972 1972 . . . Note=Confers resistance to rapamycin. Abolishes interaction with FKBP-rapamycin. S->E%2CI;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7606777,ECO:0000269|PubMed:8413204;Dbxref=PMID:7606777,PMID:8413204 +P35169 UniProtKB Mutagenesis 1972 1972 . . . Note=In DRR1-27%3B confers resistance to rapamycin. S->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7606777,ECO:0000269|PubMed:8413204;Dbxref=PMID:7606777,PMID:8413204 +P35169 UniProtKB Mutagenesis 1972 1972 . . . Note=In DRR1-1%3B confers resistance to rapamycin. Abolishes interaction with FKBP-rapamycin. S->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7606777,ECO:0000269|PubMed:8413204;Dbxref=PMID:7606777,PMID:8413204 +P35169 UniProtKB Mutagenesis 2275 2275 . . . Note=Abolishes protein kinase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10436010;Dbxref=PMID:10436010 +P35169 UniProtKB Mutagenesis 2276 2276 . . . Note=Abolishes rapamycin-resistance of mutants E-1972%3B I-1972 and R-1972. R->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7606777;Dbxref=PMID:7606777 +P35169 UniProtKB Mutagenesis 2294 2294 . . . Note=Abolishes rapamycin-resistance of mutants E-1972%3B I-1972 and R-1972. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7606777;Dbxref=PMID:7606777 +P35169 UniProtKB Sequence conflict 58 58 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 115 115 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 133 133 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 231 231 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 396 396 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 396 396 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 547 547 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 547 547 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 675 675 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 1292 1292 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 1436 1436 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 1468 1468 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 1468 1468 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 1469 1471 . . . Note=WGL->GGS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 1478 1479 . . . Note=EQ->DE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 1590 1590 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 1632 1642 . . . Note=NDPSLPNTFKA->TILVYQIRSKP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 1640 1640 . . . Note=F->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 1844 1844 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 2202 2202 . . . Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 2414 2414 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Sequence conflict 2414 2414 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35169 UniProtKB Helix 2444 2460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1N +##sequence-region P53147 1 276 +P53147 UniProtKB Chain 1 276 . . . ID=PRO_0000049400;Note=Homeobox protein TOS8 +P53147 UniProtKB DNA binding 194 256 . . . Note=Homeobox%3B TALE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00108 +##sequence-region Q12272 1 230 +Q12272 UniProtKB Chain 1 230 . . . ID=PRO_0000157497;Note=tRNA 2'-phosphotransferase +##sequence-region Q06177 1 86 +Q06177 UniProtKB Chain 1 86 . . . ID=PRO_0000072270;Note=Translation machinery-associated protein 10 +Q06177 UniProtKB Modified residue 28 28 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06177 UniProtKB Modified residue 79 79 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q12116 1 473 +Q12116 UniProtKB Chain 1 473 . . . ID=PRO_0000218972;Note=Membrane protein TMS1 +Q12116 UniProtKB Topological domain 1 6 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Transmembrane 7 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Topological domain 30 38 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Transmembrane 39 61 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Topological domain 62 81 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Transmembrane 82 104 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Topological domain 105 118 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Transmembrane 119 138 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Topological domain 139 144 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Transmembrane 145 167 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Topological domain 168 194 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Transmembrane 195 217 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Topological domain 218 228 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Transmembrane 229 246 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Topological domain 247 295 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Transmembrane 296 318 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Topological domain 319 398 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Transmembrane 399 421 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Topological domain 422 435 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Transmembrane 436 458 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12116 UniProtKB Topological domain 459 473 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P13099 1 656 +P13099 UniProtKB Chain 1 656 . . . ID=PRO_0000145198;Note=DNA topoisomerase 3 +P13099 UniProtKB Domain 2 156 . . . Note=Toprim;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00995 +P13099 UniProtKB Active site 356 356 . . . Note=O-(5'-phospho-DNA)-tyrosine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P49334 1 152 +P49334 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7760834;Dbxref=PMID:7760834 +P49334 UniProtKB Chain 2 152 . . . ID=PRO_0000076113;Note=Mitochondrial import receptor subunit TOM22 +P49334 UniProtKB Topological domain 2 97 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P49334 UniProtKB Transmembrane 98 119 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P49334 UniProtKB Topological domain 120 152 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P49334 UniProtKB Modified residue 44 44 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P49334 UniProtKB Modified residue 46 46 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P38288 1 455 +P38288 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38288 UniProtKB Chain 24 455 . . . ID=PRO_0000022563;Note=Protein TOS1 +P38288 UniProtKB Compositional bias 172 273 . . . Note=Ser-rich +P38288 UniProtKB Compositional bias 206 209 . . . Note=Poly-Ala +P38288 UniProtKB Compositional bias 210 217 . . . Note=Poly-Ser +P38288 UniProtKB Glycosylation 236 236 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38288 UniProtKB Glycosylation 417 417 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43637 1 560 +P43637 UniProtKB Chain 1 560 . . . ID=PRO_0000086126;Note=Serine/threonine-protein kinase TOS3 +P43637 UniProtKB Domain 50 344 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P43637 UniProtKB Nucleotide binding 56 64 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P43637 UniProtKB Active site 189 189 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P43637 UniProtKB Binding site 79 79 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +##sequence-region Q03796 1 238 +Q03796 UniProtKB Chain 1 238 . . . ID=PRO_0000065580;Note=Polynucleotide 3'-phosphatase +##sequence-region P53738 1 135 +P53738 UniProtKB Chain 1 135 . . . ID=PRO_0000215805;Note=Multifunctional methyltransferase subunit TRM112 +P53738 UniProtKB Domain 2 131 . . . Note=TRM112 +P53738 UniProtKB Helix 3 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A +P53738 UniProtKB Helix 14 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A +P53738 UniProtKB Beta strand 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A +P53738 UniProtKB Turn 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A +P53738 UniProtKB Beta strand 33 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A +P53738 UniProtKB Helix 44 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A +P53738 UniProtKB Helix 56 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A +P53738 UniProtKB Helix 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A +P53738 UniProtKB Helix 87 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A +P53738 UniProtKB Beta strand 103 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A +P53738 UniProtKB Turn 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A +P53738 UniProtKB Beta strand 118 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A +P53738 UniProtKB Beta strand 125 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J6A +##sequence-region P12685 1 1235 +P12685 UniProtKB Chain 1 1235 . . . ID=PRO_0000070462;Note=High-affinity potassium transport protein +P12685 UniProtKB Transmembrane 49 70 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Transmembrane 78 98 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Transmembrane 107 127 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Transmembrane 778 800 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Transmembrane 813 834 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Transmembrane 838 858 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Transmembrane 862 882 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Transmembrane 898 918 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Transmembrane 923 943 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Transmembrane 971 991 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Transmembrane 1078 1098 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Transmembrane 1111 1131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Modified residue 15 15 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P12685 UniProtKB Modified residue 414 414 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P12685 UniProtKB Modified residue 534 534 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P12685 UniProtKB Glycosylation 100 100 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Glycosylation 169 169 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Glycosylation 222 222 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Glycosylation 227 227 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Glycosylation 251 251 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Glycosylation 369 369 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Glycosylation 383 383 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Glycosylation 497 497 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Glycosylation 501 501 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Glycosylation 532 532 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Glycosylation 580 580 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Glycosylation 677 677 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Glycosylation 919 919 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Glycosylation 1030 1030 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12685 UniProtKB Glycosylation 1135 1135 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12400 1 293 +Q12400 UniProtKB Chain 1 293 . . . ID=PRO_0000060520;Note=tRNA (guanine(9)-N1)-methyltransferase +Q12400 UniProtKB Domain 83 279 . . . Note=SAM-dependent MTase TRM10-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01012 +Q12400 UniProtKB Region 186 187 . . . Note=S-adenosyl-L-methionine binding +Q12400 UniProtKB Region 210 214 . . . Note=S-adenosyl-L-methionine binding +Q12400 UniProtKB Region 244 246 . . . Note=S-adenosyl-L-methionine binding +Q12400 UniProtKB Coiled coil 32 61 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12400 UniProtKB Active site 210 210 . . . Note=Proton acceptor;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24081582;Dbxref=PMID:24081582 +Q12400 UniProtKB Binding site 206 206 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen +Q12400 UniProtKB Binding site 218 218 . . . Note=S-adenosyl-L-methionine +Q12400 UniProtKB Binding site 232 232 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen +Q12400 UniProtKB Modified residue 16 16 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12400 UniProtKB Modified residue 283 283 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12400 UniProtKB Mutagenesis 118 118 . . . Note=Completely abolishes catalytic activity. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24081582;Dbxref=PMID:24081582 +Q12400 UniProtKB Mutagenesis 209 209 . . . Note=Reduces catalytic activity. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24081582;Dbxref=PMID:24081582 +Q12400 UniProtKB Mutagenesis 210 210 . . . Note=Completely abolishes catalytic activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24081582;Dbxref=PMID:24081582 +Q12400 UniProtKB Mutagenesis 211 211 . . . Note=Reduces catalytic activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24081582;Dbxref=PMID:24081582 +Q12400 UniProtKB Mutagenesis 212 212 . . . Note=Has weaker affinity for S-adenosyl-L-methionine and reduces catalytic activity by 90%25. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24081582;Dbxref=PMID:24081582 +Q12400 UniProtKB Mutagenesis 247 247 . . . Note=Reduces catalytic activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24081582;Dbxref=PMID:24081582 +Q12400 UniProtKB Beta strand 91 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Helix 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Helix 109 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Beta strand 129 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Helix 142 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Helix 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Helix 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Beta strand 163 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Beta strand 167 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Helix 170 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Beta strand 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Helix 180 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Beta strand 183 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Beta strand 191 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Beta strand 202 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Helix 217 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Beta strand 229 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Helix 235 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Helix 248 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Turn 259 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +Q12400 UniProtKB Helix 264 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JWJ +##sequence-region Q12463 1 433 +Q12463 UniProtKB Chain 1 433 . . . ID=PRO_0000270922;Note=tRNA (guanine(10)-N2)-methyltransferase +Q12463 UniProtKB Mutagenesis 215 215 . . . Note=Abolishes activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15899842;Dbxref=PMID:15899842 +Q12463 UniProtKB Mutagenesis 291 291 . . . Note=Abolishes activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15899842;Dbxref=PMID:15899842 +##sequence-region P15565 1 570 +P15565 UniProtKB Domain 43 489 . . . Note=Trm1 methyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00958 +P15565 UniProtKB Region 133 155 . . . Note=Required and sufficient for inner nuclear membrane localization +P15565 UniProtKB Motif 95 101 . . . Note=Nuclear localization signal +P15565 UniProtKB Alternative sequence 1 16 . . . ID=VSP_018902;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15565 UniProtKB Natural variant 203 203 . . . Note=In strain: D4 and YF+. T->S +P15565 UniProtKB Natural variant 467 467 . . . Note=In strain: D4%3B loss of activity. S->L +P15565 UniProtKB Natural variant 517 517 . . . Note=In strain: D4 and YF+. G->R +P15565 UniProtKB Mutagenesis 290 290 . . . Note=Loss of activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10048958;Dbxref=PMID:10048958 +##sequence-region Q02648 1 567 +Q02648 UniProtKB Chain 1 567 . . . ID=PRO_0000249911;Note=tRNA (uracil-O(2)-)-methyltransferase +Q02648 UniProtKB Modified residue 107 107 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P41814 1 478 +P41814 UniProtKB Chain 1 478 . . . ID=PRO_0000123558;Note=tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6 +P41814 UniProtKB Turn 3 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Beta strand 12 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Beta strand 22 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Beta strand 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Helix 36 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Beta strand 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Helix 43 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Beta strand 53 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Beta strand 82 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Beta strand 189 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Helix 198 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Turn 211 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Helix 219 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Beta strand 236 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Beta strand 243 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Helix 246 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Beta strand 267 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Helix 280 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Helix 289 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Beta strand 296 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Helix 301 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Helix 310 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Helix 322 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5ERG +P41814 UniProtKB Helix 330 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Beta strand 361 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Helix 369 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Helix 373 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Helix 377 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Beta strand 385 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Helix 393 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Beta strand 409 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P41814 UniProtKB Beta strand 441 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +##sequence-region Q08687 1 178 +Q08687 UniProtKB Chain 1 178 . . . ID=PRO_0000237637;Note=Translation machinery-associated protein 16 +Q08687 UniProtKB Helix 55 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM +Q08687 UniProtKB Turn 71 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM +Q08687 UniProtKB Helix 81 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM +Q08687 UniProtKB Helix 106 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM +Q08687 UniProtKB Helix 115 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM +Q08687 UniProtKB Beta strand 134 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM +Q08687 UniProtKB Helix 142 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM +Q08687 UniProtKB Helix 157 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM +Q08687 UniProtKB Beta strand 163 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM +Q08687 UniProtKB Turn 168 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KKM +##sequence-region Q3E764 1 64 +Q3E764 UniProtKB Chain 1 64 . . . ID=PRO_0000247142;Note=Translation machinery-associated protein 7 +##sequence-region P32643 1 299 +P32643 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32643 UniProtKB Chain 2 299 . . . ID=PRO_0000202658;Note=Trans-aconitate 3-methyltransferase +P32643 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32643 UniProtKB Helix 2 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Helix 11 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Helix 23 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Beta strand 38 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Turn 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Helix 49 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Beta strand 62 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Helix 71 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Turn 85 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Beta strand 91 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Helix 102 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Turn 106 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Beta strand 114 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Helix 123 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Helix 128 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Beta strand 139 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Helix 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Helix 164 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Turn 172 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Helix 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Helix 183 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Turn 189 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Turn 198 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Beta strand 201 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Helix 211 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Helix 217 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Beta strand 231 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Helix 236 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Helix 247 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Helix 256 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Helix 264 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +P32643 UniProtKB Beta strand 285 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G5T +##sequence-region P32600 1 2474 +P32600 UniProtKB Chain 1 2474 . . . ID=PRO_0000088815;Note=Serine/threonine-protein kinase TOR2 +P32600 UniProtKB Repeat 588 626 . . . Note=HEAT 1 +P32600 UniProtKB Repeat 636 674 . . . Note=HEAT 2 +P32600 UniProtKB Repeat 676 710 . . . Note=HEAT 3 +P32600 UniProtKB Repeat 756 793 . . . Note=HEAT 4 +P32600 UniProtKB Repeat 797 835 . . . Note=HEAT 5 +P32600 UniProtKB Repeat 841 879 . . . Note=HEAT 6 +P32600 UniProtKB Repeat 917 955 . . . Note=HEAT 7 +P32600 UniProtKB Repeat 1039 1076 . . . Note=HEAT 8 +P32600 UniProtKB Repeat 1079 1116 . . . Note=HEAT 9 +P32600 UniProtKB Repeat 1118 1155 . . . Note=HEAT 10 +P32600 UniProtKB Repeat 1292 1331 . . . Note=HEAT 11 +P32600 UniProtKB Domain 1338 1922 . . . Note=FAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534 +P32600 UniProtKB Domain 2123 2441 . . . Note=PI3K/PI4K;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00269 +P32600 UniProtKB Domain 2442 2474 . . . Note=FATC;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534,ECO:0000255|PROSITE-ProRule:PRU00535 +P32600 UniProtKB Modified residue 10 10 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32600 UniProtKB Mutagenesis 1975 1975 . . . Note=In TOR2-1%3B confers resistance to rapamycin. S->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8846782;Dbxref=PMID:8846782 +P32600 UniProtKB Mutagenesis 2129 2129 . . . Note=Causes defect in receptor endocytosis. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14593073;Dbxref=PMID:14593073 +P32600 UniProtKB Mutagenesis 2279 2279 . . . Note=Loss of function. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8846782;Dbxref=PMID:8846782 +P32600 UniProtKB Mutagenesis 2298 2298 . . . Note=Loss of kinase activity. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16055732;Dbxref=PMID:16055732 +P32600 UniProtKB Sequence conflict 1473 1473 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P17536 1 199 +P17536 UniProtKB Chain 1 199 . . . ID=PRO_0000205692;Note=Tropomyosin-1 +P17536 UniProtKB Coiled coil 1 199 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P17536 UniProtKB Modified residue 195 195 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P17536 UniProtKB Cross-link 39 39 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P17536 UniProtKB Cross-link 59 59 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P17536 UniProtKB Cross-link 187 187 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P53099 1 579 +P53099 UniProtKB Chain 1 579 . . . ID=PRO_0000197929;Note=Vitamin B6 transporter TPN1 +P53099 UniProtKB Topological domain 1 98 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Transmembrane 99 119 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Topological domain 120 122 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Transmembrane 123 143 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Topological domain 144 157 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Transmembrane 158 178 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Topological domain 179 198 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Transmembrane 199 219 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Topological domain 220 221 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Transmembrane 222 242 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Topological domain 243 274 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Transmembrane 275 295 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Topological domain 296 302 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Transmembrane 303 323 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Topological domain 324 362 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Transmembrane 363 383 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Topological domain 384 394 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Transmembrane 395 415 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Topological domain 416 421 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Transmembrane 422 442 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Topological domain 443 519 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Transmembrane 520 540 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Topological domain 541 545 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Transmembrane 546 566 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53099 UniProtKB Topological domain 567 579 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53283 1 614 +P53283 UniProtKB Chain 1 614 . . . ID=PRO_0000173439;Note=Polyamine transporter 2 +P53283 UniProtKB Topological domain 1 173 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Transmembrane 174 194 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Topological domain 195 206 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Transmembrane 207 227 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Topological domain 228 236 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Transmembrane 237 257 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Topological domain 258 266 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Transmembrane 267 287 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Topological domain 288 297 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Transmembrane 298 318 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Topological domain 319 326 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Transmembrane 327 347 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Topological domain 348 407 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Transmembrane 408 428 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Topological domain 429 437 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Transmembrane 438 458 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Topological domain 459 478 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Transmembrane 479 499 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Topological domain 500 503 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Transmembrane 504 524 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Topological domain 525 541 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Transmembrane 542 562 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Topological domain 563 574 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Transmembrane 575 595 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Topological domain 596 614 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53283 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q12256 1 659 +Q12256 UniProtKB Chain 1 659 . . . ID=PRO_0000262732;Note=Polyamine transporter 4 +Q12256 UniProtKB Topological domain 1 99 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Transmembrane 100 120 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Topological domain 121 128 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Transmembrane 129 149 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Topological domain 150 157 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Transmembrane 158 178 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Topological domain 179 187 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Transmembrane 188 208 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Topological domain 209 215 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Transmembrane 216 236 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Topological domain 237 246 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Transmembrane 247 267 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Topological domain 268 316 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Transmembrane 317 337 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Topological domain 338 355 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Transmembrane 356 376 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Topological domain 377 423 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Transmembrane 424 444 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Topological domain 445 456 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Transmembrane 457 477 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Topological domain 478 486 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Transmembrane 487 509 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Topological domain 510 518 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Transmembrane 519 539 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Topological domain 540 659 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12256 UniProtKB Modified residue 589 589 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12256 UniProtKB Modified residue 606 606 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12256 UniProtKB Modified residue 608 608 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12256 UniProtKB Modified residue 633 633 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12256 UniProtKB Modified residue 646 646 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q03496 1 1420 +Q03496 UniProtKB Chain 1 1420 . . . ID=PRO_0000203343;Note=tRNA (cytidine(32)-2'-O)-methyltransferase non-catalytic subunit TRM732 +##sequence-region Q05024 1 226 +Q05024 UniProtKB Chain 1 226 . . . ID=PRO_0000203334;Note=Protein TRI1 +Q05024 UniProtKB Compositional bias 103 110 . . . Note=Poly-Lys +Q05024 UniProtKB Modified residue 113 113 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05024 UniProtKB Modified residue 225 225 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q05024 UniProtKB Cross-link 201 201 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) +Q05024 UniProtKB Cross-link 215 215 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) +Q05024 UniProtKB Mutagenesis 201 201 . . . Note=Impairs sumoylation%3B when associated with R-215. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17603101;Dbxref=PMID:17603101 +Q05024 UniProtKB Mutagenesis 215 215 . . . Note=Impairs sumoylation%3B when associated with R-201. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17603101;Dbxref=PMID:17603101 +##sequence-region P33753 1 639 +P33753 UniProtKB Chain 1 639 . . . ID=PRO_0000162059;Note=tRNA (uracil(54)-C(5))-methyltransferase +P33753 UniProtKB Domain 163 228 . . . Note=TRAM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00208 +P33753 UniProtKB Compositional bias 5 12 . . . Note=Poly-Phe +P33753 UniProtKB Active site 591 591 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01024 +P33753 UniProtKB Active site 631 631 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10015 +P33753 UniProtKB Binding site 461 461 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01024 +P33753 UniProtKB Binding site 496 496 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01024 +P33753 UniProtKB Binding site 517 517 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01024 +P33753 UniProtKB Binding site 564 564 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01024 +P33753 UniProtKB Modified residue 92 92 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P33753 UniProtKB Modified residue 93 93 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P33753 UniProtKB Mutagenesis 498 498 . . . Note=Unable to methylate tRNA. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12003492;Dbxref=PMID:12003492 +P33753 UniProtKB Mutagenesis 591 591 . . . Note=Unable to methylate tRNA. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12003492;Dbxref=PMID:12003492 +P33753 UniProtKB Sequence conflict 24 24 . . . Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38793 1 499 +P38793 UniProtKB Transit peptide 1 44 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03152 +P38793 UniProtKB Chain 45 499 . . . ID=PRO_0000202899;Note=tRNA (guanine(37)-N1)-methyltransferase +P38793 UniProtKB Region 307 308 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03152 +P38793 UniProtKB Region 335 336 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03152 +P38793 UniProtKB Binding site 268 268 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03152 +P38793 UniProtKB Binding site 399 399 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03152 +P38793 UniProtKB Mutagenesis 1 33 . . . Note=Abolishes mitochondrial localization and activity%2C but not cytoplasmic activity of the enzyme. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17652090;Dbxref=PMID:17652090 +##sequence-region P09880 1 827 +P09880 UniProtKB Chain 1 827 . . . ID=PRO_0000065635;Note=tRNA ligase +P09880 UniProtKB Active site 114 114 . . . Note=N6-AMP-lysine intermediate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2207062;Dbxref=PMID:2207062 +##sequence-region P46944 1 698 +P46944 UniProtKB Chain 1 698 . . . ID=PRO_0000065642;Note=Trafficking protein particle complex III-specific subunit 85 +P46944 UniProtKB Sequence conflict 277 277 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P22217 1 103 +P22217 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7961686;Dbxref=PMID:7961686 +P22217 UniProtKB Chain 2 103 . . . ID=PRO_0000120044;Note=Thioredoxin-1 +P22217 UniProtKB Domain 2 103 . . . Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +P22217 UniProtKB Active site 30 30 . . . Note=Nucleophile +P22217 UniProtKB Active site 33 33 . . . Note=Nucleophile +P22217 UniProtKB Site 24 24 . . . Note=Deprotonates C-terminal active site Cys +P22217 UniProtKB Site 31 31 . . . Note=Contributes to redox potential value +P22217 UniProtKB Site 32 32 . . . Note=Contributes to redox potential value +P22217 UniProtKB Disulfide bond 30 33 . . . Note=Redox-active;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00691,ECO:0000269|PubMed:19362171;Dbxref=PMID:19362171 +P22217 UniProtKB Cross-link 54 54 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P22217 UniProtKB Cross-link 66 66 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P22217 UniProtKB Cross-link 96 96 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P22217 UniProtKB Beta strand 2 4 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3R +P22217 UniProtKB Helix 8 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q +P22217 UniProtKB Beta strand 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q +P22217 UniProtKB Beta strand 21 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q +P22217 UniProtKB Helix 31 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q +P22217 UniProtKB Beta strand 50 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q +P22217 UniProtKB Turn 57 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q +P22217 UniProtKB Helix 61 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q +P22217 UniProtKB Beta strand 71 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q +P22217 UniProtKB Beta strand 82 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q +P22217 UniProtKB Helix 92 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3Q +##sequence-region P34760 1 196 +P34760 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8344960;Dbxref=PMID:8344960 +P34760 UniProtKB Chain 2 196 . . . ID=PRO_0000135095;Note=Peroxiredoxin TSA1 +P34760 UniProtKB Domain 3 161 . . . Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +P34760 UniProtKB Region 45 47 . . . Note=Substrate binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3SBC,ECO:0000269|PubMed:22985967;Dbxref=PMID:22985967 +P34760 UniProtKB Active site 48 48 . . . Note=Cysteine sulfenic acid (-SOH) intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8041739;Dbxref=PMID:8041739 +P34760 UniProtKB Binding site 124 124 . . . Note=Substrate;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3SBC,ECO:0000269|PubMed:22985967;Dbxref=PMID:22985967 +P34760 UniProtKB Site 45 45 . . . Note=Important for catalytic activity%2C helps activating the peroxidatic cysteine through H-bonding +P34760 UniProtKB Modified residue 174 174 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P34760 UniProtKB Disulfide bond 48 48 . . . Note=Interchain (with C-171)%3B in linked form;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7961686;Dbxref=PMID:7961686 +P34760 UniProtKB Disulfide bond 48 48 . . . Note=Interchain (with C-84 in SRX1)%3B transient;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14586471;Dbxref=PMID:14586471 +P34760 UniProtKB Disulfide bond 171 171 . . . Note=Interchain (with C-48)%3B in linked form;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7961686;Dbxref=PMID:7961686 +P34760 UniProtKB Cross-link 14 14 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P34760 UniProtKB Cross-link 89 89 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P34760 UniProtKB Cross-link 132 132 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P34760 UniProtKB Mutagenesis 48 48 . . . Note=Exists mainly as monomer. Has no peroxiredoxin activity. Fails to protect glutamine synthetase against damage by DTT oxidation. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7961686,ECO:0000269|PubMed:8041739;Dbxref=PMID:7961686,PMID:8041739 +P34760 UniProtKB Mutagenesis 171 171 . . . Note=Exists mainly as monomer. Has no peroxiredoxin activity. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7961686,ECO:0000269|PubMed:8041739;Dbxref=PMID:7961686,PMID:8041739 +P34760 UniProtKB Beta strand 14 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC +P34760 UniProtKB Beta strand 21 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC +P34760 UniProtKB Helix 27 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC +P34760 UniProtKB Beta strand 33 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC +P34760 UniProtKB Helix 47 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC +P34760 UniProtKB Beta strand 67 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC +P34760 UniProtKB Helix 77 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC +P34760 UniProtKB Helix 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC +P34760 UniProtKB Beta strand 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC +P34760 UniProtKB Helix 107 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC +P34760 UniProtKB Turn 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC +P34760 UniProtKB Beta strand 124 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC +P34760 UniProtKB Beta strand 133 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC +P34760 UniProtKB Helix 149 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC +P34760 UniProtKB Turn 184 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC +P34760 UniProtKB Helix 187 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBC +##sequence-region P40061 1 1430 +P40061 UniProtKB Chain 1 1430 . . . ID=PRO_0000202640;Note=Target of rapamycin complex 2 subunit TSC11 +P40061 UniProtKB Domain 995 1100 . . . Note=N-terminal Ras-GEF +P40061 UniProtKB Coiled coil 91 180 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40061 UniProtKB Modified residue 19 19 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P40061 UniProtKB Modified residue 81 81 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40061 UniProtKB Modified residue 84 84 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40061 UniProtKB Modified residue 87 87 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40061 UniProtKB Modified residue 141 141 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q02776 1 476 +Q02776 UniProtKB Transit peptide 1 43 . . . Note=Mitochondrion;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12437924,ECO:0000305|PubMed:12437925;Dbxref=PMID:12437924,PMID:12437925 +Q02776 UniProtKB Chain 44 476 . . . ID=PRO_0000043139;Note=Mitochondrial import inner membrane translocase subunit TIM50 +Q02776 UniProtKB Topological domain 44 114 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02776 UniProtKB Transmembrane 115 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02776 UniProtKB Topological domain 132 476 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02776 UniProtKB Domain 187 330 . . . Note=FCP1 homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00336 +Q02776 UniProtKB Turn 186 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Beta strand 191 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Turn 200 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Beta strand 203 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Beta strand 209 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Beta strand 213 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Helix 221 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Turn 229 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Beta strand 232 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Helix 242 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Helix 250 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Turn 253 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Helix 256 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Beta strand 261 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Helix 265 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Beta strand 268 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Beta strand 274 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Helix 279 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Helix 286 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Beta strand 289 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Helix 296 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Helix 303 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Beta strand 306 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Helix 321 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Helix 324 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Helix 339 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Helix 348 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +Q02776 UniProtKB Helix 351 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QQF +##sequence-region P40552 1 269 +P40552 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40552 UniProtKB Chain 23 245 . . . ID=PRO_0000033236;Note=Cell wall protein TIR3 +P40552 UniProtKB Propeptide 246 269 . . . ID=PRO_0000372446;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40552 UniProtKB Compositional bias 126 269 . . . Note=Ala/Ser-rich +P40552 UniProtKB Lipidation 245 245 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40552 UniProtKB Glycosylation 234 234 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12000 1 345 +Q12000 UniProtKB Chain 1 345 . . . ID=PRO_0000237638;Note=Translation machinery-associated protein 46 +Q12000 UniProtKB Zinc finger 87 114 . . . Note=C3H1-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 +Q12000 UniProtKB Zinc finger 158 196 . . . Note=C3H1-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 +Q12000 UniProtKB Modified residue 301 301 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12000 UniProtKB Helix 222 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +Q12000 UniProtKB Helix 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +Q12000 UniProtKB Helix 235 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +Q12000 UniProtKB Helix 243 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +Q12000 UniProtKB Helix 272 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +Q12000 UniProtKB Helix 306 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +Q12000 UniProtKB Helix 320 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +Q12000 UniProtKB Beta strand 323 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +Q12000 UniProtKB Beta strand 329 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +##sequence-region Q06266 1 489 +Q06266 UniProtKB Chain 1 489 . . . ID=PRO_0000262748;Note=Protein TOS4 +Q06266 UniProtKB Domain 118 170 . . . Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 +Q06266 UniProtKB Compositional bias 181 184 . . . Note=Poly-Asn +Q06266 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06266 UniProtKB Modified residue 100 100 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region Q07824 1 586 +Q07824 UniProtKB Chain 1 586 . . . ID=PRO_0000262730;Note=Polyamine transporter 1 +Q07824 UniProtKB Topological domain 1 145 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Transmembrane 146 166 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Topological domain 167 181 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Transmembrane 182 202 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Topological domain 203 212 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Transmembrane 213 233 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Topological domain 234 242 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Transmembrane 243 263 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Topological domain 264 271 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Transmembrane 272 292 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Topological domain 293 301 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Transmembrane 302 322 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Topological domain 323 376 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Transmembrane 377 397 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Topological domain 398 414 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Transmembrane 415 435 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Topological domain 436 454 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Transmembrane 455 475 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Topological domain 476 483 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Transmembrane 484 504 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Topological domain 505 505 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Transmembrane 506 526 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Topological domain 527 528 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Transmembrane 529 549 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Transmembrane 550 570 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Topological domain 571 586 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07824 UniProtKB Compositional bias 17 25 . . . Note=Poly-Ser +Q07824 UniProtKB Modified residue 19 19 . . . Note=Phosphoserine%3B by PKC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637075;Dbxref=PMID:15637075 +Q07824 UniProtKB Modified residue 52 52 . . . Note=Phosphothreonine%3B by CK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637075;Dbxref=PMID:15637075 +Q07824 UniProtKB Modified residue 72 72 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q07824 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q07824 UniProtKB Modified residue 89 89 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q07824 UniProtKB Modified residue 91 91 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q07824 UniProtKB Modified residue 342 342 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637075;Dbxref=PMID:15637075 +Q07824 UniProtKB Mutagenesis 19 19 . . . Note=Reduces transport activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637075;Dbxref=PMID:15637075 +Q07824 UniProtKB Mutagenesis 19 19 . . . Note=Enhances transport activity. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637075;Dbxref=PMID:15637075 +Q07824 UniProtKB Mutagenesis 52 52 . . . Note=Reduces transport activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637075;Dbxref=PMID:15637075 +Q07824 UniProtKB Mutagenesis 52 52 . . . Note=Enhances transport activity. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637075;Dbxref=PMID:15637075 +Q07824 UniProtKB Mutagenesis 207 207 . . . Note=Loss of function. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171066;Dbxref=PMID:11171066 +Q07824 UniProtKB Mutagenesis 323 323 . . . Note=Loss of function%3B when associated with Q-324. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171066;Dbxref=PMID:11171066 +Q07824 UniProtKB Mutagenesis 324 324 . . . Note=Loss of function%3B when associated with Q-323. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171066;Dbxref=PMID:11171066 +Q07824 UniProtKB Mutagenesis 342 342 . . . Note=Interferes with correct plasma membrane localization. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637075;Dbxref=PMID:15637075 +Q07824 UniProtKB Mutagenesis 342 342 . . . Note=Enhances transport activity. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637075;Dbxref=PMID:15637075 +Q07824 UniProtKB Mutagenesis 574 574 . . . Note=Loss of function. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171066;Dbxref=PMID:11171066 +##sequence-region P47045 1 478 +P47045 UniProtKB Chain 1 478 . . . ID=PRO_0000203062;Note=Mitochondrial import inner membrane translocase subunit TIM54 +P47045 UniProtKB Topological domain 1 32 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47045 UniProtKB Transmembrane 33 49 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47045 UniProtKB Topological domain 50 478 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12199 1 356 +Q12199 UniProtKB Chain 1 356 . . . ID=PRO_0000247903;Note=Type 2A phosphatase activator TIP41 +Q12199 UniProtKB Modified residue 55 55 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P23254 1 680 +P23254 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1812485;Dbxref=PMID:1812485 +P23254 UniProtKB Chain 2 680 . . . ID=PRO_0000191904;Note=Transketolase 1 +P23254 UniProtKB Nucleotide binding 116 118 . . . Note=Thiamine pyrophosphate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8176731,ECO:0000269|PubMed:8999873,ECO:0000269|PubMed:9398292;Dbxref=PMID:8176731,PMID:8999873,PMID:9398292 +P23254 UniProtKB Active site 418 418 . . . Note=Proton donor;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23254 UniProtKB Metal binding 157 157 . . . Note=Magnesium +P23254 UniProtKB Metal binding 187 187 . . . Note=Magnesium +P23254 UniProtKB Metal binding 189 189 . . . Note=Magnesium%3B via carbonyl oxygen +P23254 UniProtKB Binding site 30 30 . . . Note=Substrate +P23254 UniProtKB Binding site 69 69 . . . Note=Thiamine pyrophosphate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8176731,ECO:0000269|PubMed:8999873,ECO:0000269|PubMed:9398292;Dbxref=PMID:8176731,PMID:8999873,PMID:9398292 +P23254 UniProtKB Binding site 158 158 . . . Note=Thiamine pyrophosphate%3B via amide nitrogen;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8176731,ECO:0000269|PubMed:8999873,ECO:0000269|PubMed:9398292;Dbxref=PMID:8176731,PMID:8999873,PMID:9398292 +P23254 UniProtKB Binding site 187 187 . . . Note=Thiamine pyrophosphate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8176731,ECO:0000269|PubMed:8999873,ECO:0000269|PubMed:9398292;Dbxref=PMID:8176731,PMID:8999873,PMID:9398292 +P23254 UniProtKB Binding site 263 263 . . . Note=Substrate +P23254 UniProtKB Binding site 263 263 . . . Note=Thiamine pyrophosphate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8176731,ECO:0000269|PubMed:8999873,ECO:0000269|PubMed:9398292;Dbxref=PMID:8176731,PMID:8999873,PMID:9398292 +P23254 UniProtKB Binding site 359 359 . . . Note=Substrate +P23254 UniProtKB Binding site 386 386 . . . Note=Substrate +P23254 UniProtKB Binding site 418 418 . . . Note=Thiamine pyrophosphate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8176731,ECO:0000269|PubMed:8999873,ECO:0000269|PubMed:9398292;Dbxref=PMID:8176731,PMID:8999873,PMID:9398292 +P23254 UniProtKB Binding site 445 445 . . . Note=Thiamine pyrophosphate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8176731,ECO:0000269|PubMed:8999873,ECO:0000269|PubMed:9398292;Dbxref=PMID:8176731,PMID:8999873,PMID:9398292 +P23254 UniProtKB Binding site 469 469 . . . Note=Substrate +P23254 UniProtKB Binding site 477 477 . . . Note=Substrate +P23254 UniProtKB Binding site 528 528 . . . Note=Substrate +P23254 UniProtKB Site 30 30 . . . Note=Important for catalytic activity +P23254 UniProtKB Site 263 263 . . . Note=Important for catalytic activity +P23254 UniProtKB Modified residue 286 286 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P23254 UniProtKB Modified residue 335 335 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P23254 UniProtKB Modified residue 402 402 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P23254 UniProtKB Modified residue 492 492 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P23254 UniProtKB Cross-link 647 647 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P23254 UniProtKB Mutagenesis 30 30 . . . Note=Strongly reduced catalytic activity. Decreases affinity for xylulose 5-phosphate about 15 times. H->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9398292;Dbxref=PMID:9398292 +P23254 UniProtKB Mutagenesis 30 30 . . . Note=Loss of activity. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9398292;Dbxref=PMID:9398292 +P23254 UniProtKB Mutagenesis 69 69 . . . Note=Reduces catalytic activity by about 98%25. Decreased affinity for donor substrate. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9398292;Dbxref=PMID:9398292 +P23254 UniProtKB Mutagenesis 103 103 . . . Note=Reduces activity by over 96%25 and decreases affinity for thiamine pyrophosphate and xylulose 5-phosphate. H->A%2CN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8521838,ECO:0000269|PubMed:9398292;Dbxref=PMID:8521838,PMID:9398292 +P23254 UniProtKB Mutagenesis 103 103 . . . Note=Loss of activity. H->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8521838,ECO:0000269|PubMed:9398292;Dbxref=PMID:8521838,PMID:9398292 +P23254 UniProtKB Mutagenesis 162 162 . . . Note=Most catalytic properties similar to wild-type. E->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9119035;Dbxref=PMID:9119035 +P23254 UniProtKB Mutagenesis 263 263 . . . Note=Strongly reduced catalytic activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9398292;Dbxref=PMID:9398292 +P23254 UniProtKB Mutagenesis 359 359 . . . Note=Slightly reduced affinity for xylulose 5-phosphate and strongly reduced affinity for ribose 5-phosphate. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8999873;Dbxref=PMID:8999873 +P23254 UniProtKB Mutagenesis 382 382 . . . Note=Severe loss of activity. D->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9119035;Dbxref=PMID:9119035 +P23254 UniProtKB Mutagenesis 469 469 . . . Note=Strongly reduced affinity for xylulose 5-phosphate and ribose 5-phosphate. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8999873;Dbxref=PMID:8999873 +P23254 UniProtKB Mutagenesis 477 477 . . . Note=Strongly reduced catalytic activity. Strongly reduced affinity for xylulose 5-phosphate and ribose 5-phosphate. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8999873;Dbxref=PMID:8999873 +P23254 UniProtKB Mutagenesis 481 481 . . . Note=Reduces catalytic activity by about 95%25. H->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9398292;Dbxref=PMID:9398292 +P23254 UniProtKB Mutagenesis 528 528 . . . Note=Reduced affinity for xylulose 5-phosphate and strongly reduced affinity for ribose 5-phosphate. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8999873;Dbxref=PMID:8999873 +P23254 UniProtKB Sequence conflict 37 38 . . . Note=MA->RS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23254 UniProtKB Sequence conflict 45 77 . . . Note=WSQMRMNPTNPDWINRDRFVLSNGHAVALLYSM->GESNAHEPNQPKTGSTEIDLSCLTVTRSLCCIY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23254 UniProtKB Sequence conflict 136 143 . . . Note=AATYNKPG->DMPLTTSRA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23254 UniProtKB Sequence conflict 232 234 . . . Note=AQA->RQR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23254 UniProtKB Sequence conflict 243 257 . . . Note=LIKMTTTIGYGSLHA->FDQNDHNHWLRFLRS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23254 UniProtKB Sequence conflict 383 383 . . . Note=L->LVLPIL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23254 UniProtKB Sequence conflict 396 396 . . . Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23254 UniProtKB Sequence conflict 528 538 . . . Note=RQNLPQLEGSS->PDKTCHNWKVAL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23254 UniProtKB Sequence conflict 639 680 . . . Note=SGKAPEVFKFFGFTPEGVAERAQKTIAFYKGDKLISPLKKAF->PVRHQKSSSSSVSPQKVLLKELKRPLHSIRVTS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23254 UniProtKB Helix 6 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 32 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 62 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 68 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 71 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 87 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Turn 91 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 120 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 151 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 157 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 163 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 180 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 191 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKB +P23254 UniProtKB Helix 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 203 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 213 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Turn 220 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 224 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 242 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Turn 250 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Turn 255 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 260 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 263 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 269 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 291 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 302 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 324 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 342 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 358 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Turn 370 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 376 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 384 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 402 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 411 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 418 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 436 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 443 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 447 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 450 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 464 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 472 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Turn 479 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 486 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 493 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 497 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 504 516 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 522 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 528 531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TRK +P23254 UniProtKB Helix 539 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 547 550 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 556 561 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 565 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Turn 578 580 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 583 587 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 591 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 599 605 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 608 610 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 612 615 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 623 625 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Beta strand 628 631 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 642 648 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +P23254 UniProtKB Helix 653 667 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPU +##sequence-region Q03322 1 224 +Q03322 UniProtKB Chain 1 224 . . . ID=PRO_0000210277;Note=T-SNARE affecting a late Golgi compartment protein 1 +Q03322 UniProtKB Topological domain 1 203 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03322 UniProtKB Transmembrane 204 224 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03322 UniProtKB Domain 132 194 . . . Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202 +Q03322 UniProtKB Region 1 106 . . . Note=Interaction with VPS51;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12377769;Dbxref=PMID:12377769 +Q03322 UniProtKB Coiled coil 35 101 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03322 UniProtKB Modified residue 31 31 . . . Note=Phosphothreonine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12006655;Dbxref=PMID:12006655 +Q03322 UniProtKB Lipidation 205 205 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15973437;Dbxref=PMID:15973437 +Q03322 UniProtKB Lipidation 206 206 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15973437;Dbxref=PMID:15973437 +Q03322 UniProtKB Cross-link 183 183 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q03322 UniProtKB Mutagenesis 31 31 . . . Note=Results in an aktivated t-SNARE that confers endocytosis%2C but not exocytosis. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12006655;Dbxref=PMID:12006655 +Q03322 UniProtKB Mutagenesis 205 206 . . . Note=Not palmitoylated%2C rapidly degraded in a TUL1-dependent manner. CC->SS%2CLL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15973437;Dbxref=PMID:15973437 +Q03322 UniProtKB Helix 7 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5K +Q03322 UniProtKB Helix 38 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5K +Q03322 UniProtKB Helix 71 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5K +##sequence-region P53322 1 534 +P53322 UniProtKB Chain 1 534 . . . ID=PRO_0000121369;Note=High-affinity nicotinic acid transporter +P53322 UniProtKB Topological domain 1 130 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Transmembrane 131 151 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Topological domain 152 152 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Transmembrane 153 173 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Topological domain 174 187 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Transmembrane 188 208 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Topological domain 209 217 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Transmembrane 218 238 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Topological domain 239 250 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Transmembrane 251 271 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Topological domain 272 323 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Transmembrane 324 344 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Topological domain 345 355 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Transmembrane 356 376 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Topological domain 377 384 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Transmembrane 385 405 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Topological domain 406 410 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Transmembrane 411 431 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Topological domain 432 444 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Transmembrane 445 465 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Topological domain 466 474 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Transmembrane 475 495 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Topological domain 496 534 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53322 UniProtKB Modified residue 27 27 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53322 UniProtKB Cross-link 283 283 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region Q08919 1 783 +Q08919 UniProtKB Chain 1 783 . . . ID=PRO_0000238622;Note=Uncharacterized protein TRE1 +Q08919 UniProtKB Topological domain 1 109 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08919 UniProtKB Transmembrane 110 127 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08919 UniProtKB Topological domain 128 783 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08919 UniProtKB Domain 241 333 . . . Note=PA +Q08919 UniProtKB Glycosylation 139 139 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08919 UniProtKB Glycosylation 213 213 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08919 UniProtKB Glycosylation 529 529 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03774 1 444 +Q03774 UniProtKB Chain 1 444 . . . ID=PRO_0000051295;Note=tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit TRM82 +Q03774 UniProtKB Repeat 1 47 . . . Note=WD 1 +Q03774 UniProtKB Repeat 48 99 . . . Note=WD 2 +Q03774 UniProtKB Repeat 100 147 . . . Note=WD 3 +Q03774 UniProtKB Repeat 148 192 . . . Note=WD 4 +Q03774 UniProtKB Repeat 193 237 . . . Note=WD 5 +Q03774 UniProtKB Repeat 238 279 . . . Note=WD 6 +Q03774 UniProtKB Repeat 308 354 . . . Note=WD 7 +Q03774 UniProtKB Modified residue 93 93 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03774 UniProtKB Beta strand 9 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 14 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 26 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Turn 34 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 37 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 105 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 114 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Helix 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 126 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 134 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 140 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 152 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 161 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 171 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 191 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 198 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 211 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 222 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 233 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 244 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 254 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Turn 269 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 274 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Helix 281 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Helix 285 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 310 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 317 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 330 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 339 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 345 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 357 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 366 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 383 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Turn 391 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Beta strand 395 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Helix 400 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Turn 418 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q03774 UniProtKB Helix 424 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +##sequence-region P38334 1 175 +P38334 UniProtKB Chain 1 175 . . . ID=PRO_0000211568;Note=Trafficking protein particle complex subunit 20 +##sequence-region P32893 1 560 +P32893 UniProtKB Chain 1 560 . . . ID=PRO_0000084328;Note=Trafficking protein particle complex II-specific subunit 65 +P32893 UniProtKB Modified residue 393 393 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32893 UniProtKB Modified residue 398 398 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q02208 1 771 +Q02208 UniProtKB Chain 1 771 . . . ID=PRO_0000072621;Note=Topoisomerase 1-associated factor 2 +Q02208 UniProtKB Modified residue 397 397 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02208 UniProtKB Modified residue 405 405 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02208 UniProtKB Helix 503 512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HOI +##sequence-region P07213 1 617 +P07213 UniProtKB Chain 1 617 . . . ID=PRO_0000106340;Note=Mitochondrial import receptor subunit TOM70 +P07213 UniProtKB Topological domain 1 10 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07213 UniProtKB Transmembrane 11 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07213 UniProtKB Topological domain 31 617 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07213 UniProtKB Repeat 99 132 . . . Note=TPR 1 +P07213 UniProtKB Repeat 134 165 . . . Note=TPR 2 +P07213 UniProtKB Repeat 281 315 . . . Note=TPR 3 +P07213 UniProtKB Repeat 363 396 . . . Note=TPR 4 +P07213 UniProtKB Repeat 397 430 . . . Note=TPR 5 +P07213 UniProtKB Repeat 432 464 . . . Note=TPR 6 +P07213 UniProtKB Repeat 465 498 . . . Note=TPR 7 +P07213 UniProtKB Repeat 505 541 . . . Note=TPR 8 +P07213 UniProtKB Repeat 542 575 . . . Note=TPR 9 +P07213 UniProtKB Modified residue 174 174 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P07213 UniProtKB Natural variant 30 30 . . . Note=In strain: SK1%2C V1-09%2C YJM339 and YJM627. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P07213 UniProtKB Natural variant 68 68 . . . Note=In strain: V1-09 and YJM627. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P07213 UniProtKB Natural variant 277 277 . . . Note=In strain: YJM1129. N->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P07213 UniProtKB Natural variant 359 359 . . . Note=In strain: SK1. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P07213 UniProtKB Natural variant 364 364 . . . Note=In strain: YJM269 and YJM270. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P07213 UniProtKB Natural variant 385 385 . . . Note=In strain: YJM1129. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P07213 UniProtKB Natural variant 429 429 . . . Note=In ytrain: V1-09. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P07213 UniProtKB Sequence conflict 185 185 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07213 UniProtKB Helix 95 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 115 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 132 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 148 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 166 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 182 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Beta strand 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 200 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 204 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 254 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 278 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 297 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Turn 316 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 323 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 346 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 363 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 382 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 385 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 398 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 415 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 432 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Turn 441 445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 447 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 466 477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 481 496 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Beta strand 498 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 506 516 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 523 537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 542 554 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 558 571 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 575 594 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +P07213 UniProtKB Helix 598 605 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GW1 +##sequence-region P48560 1 102 +P48560 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48560 UniProtKB Chain 19 80 . . . ID=PRO_0000203371;Note=Protein TOS6 +P48560 UniProtKB Propeptide 81 102 . . . ID=PRO_0000372450;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48560 UniProtKB Compositional bias 21 77 . . . Note=Thr-rich +P48560 UniProtKB Lipidation 80 80 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48560 UniProtKB Glycosylation 69 69 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P00942 1 248 +P00942 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7005233;Dbxref=PMID:7005233 +P00942 UniProtKB Chain 2 248 . . . ID=PRO_0000090169;Note=Triosephosphate isomerase +P00942 UniProtKB Active site 95 95 . . . Note=Electrophile +P00942 UniProtKB Active site 165 165 . . . Note=Proton acceptor +P00942 UniProtKB Binding site 10 10 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12509510;Dbxref=PMID:12509510 +P00942 UniProtKB Binding site 12 12 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12509510;Dbxref=PMID:12509510 +P00942 UniProtKB Modified residue 4 4 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00942 UniProtKB Modified residue 71 71 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P00942 UniProtKB Modified residue 215 215 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P00942 UniProtKB Cross-link 223 223 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00942 UniProtKB Beta strand 5 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Helix 17 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Beta strand 36 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Helix 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Helix 47 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Beta strand 59 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Beta strand 68 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Helix 80 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Beta strand 90 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Helix 96 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Helix 106 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Beta strand 122 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Helix 131 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Helix 139 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Beta strand 160 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Helix 167 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Turn 170 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Helix 178 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Helix 198 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Beta strand 206 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Turn 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Helix 217 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Beta strand 228 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Helix 233 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Helix 239 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +P00942 UniProtKB Turn 245 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NEY +##sequence-region P40414 1 161 +P40414 UniProtKB Chain 1 161 . . . ID=PRO_0000205693;Note=Tropomyosin-2 +P40414 UniProtKB Coiled coil 1 161 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40414 UniProtKB Modified residue 55 55 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40414 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40414 UniProtKB Modified residue 157 157 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q06451 1 622 +Q06451 UniProtKB Chain 1 622 . . . ID=PRO_0000262731;Note=Polyamine transporter 3 +Q06451 UniProtKB Topological domain 1 182 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Transmembrane 183 203 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Topological domain 204 215 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Transmembrane 216 236 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Topological domain 237 245 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Transmembrane 246 266 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Topological domain 267 275 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Transmembrane 276 296 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Topological domain 297 305 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Transmembrane 306 326 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Topological domain 327 335 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Transmembrane 336 356 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Topological domain 357 416 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Transmembrane 417 437 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Topological domain 438 446 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Transmembrane 447 467 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Topological domain 468 487 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Transmembrane 488 508 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Topological domain 509 512 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Transmembrane 513 533 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Topological domain 534 550 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Transmembrane 551 571 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Topological domain 572 583 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Transmembrane 584 604 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Topological domain 605 622 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06451 UniProtKB Modified residue 55 55 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06451 UniProtKB Modified residue 98 98 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06451 UniProtKB Modified residue 101 101 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06451 UniProtKB Modified residue 132 132 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P36029 1 618 +P36029 UniProtKB Chain 1 618 . . . ID=PRO_0000054165;Note=Polyamine transporter TPO5 +P36029 UniProtKB Topological domain 1 60 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Transmembrane 61 84 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Topological domain 85 90 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Transmembrane 91 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Topological domain 111 131 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Transmembrane 132 148 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Topological domain 149 154 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Transmembrane 155 171 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Topological domain 172 179 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Transmembrane 180 200 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Topological domain 201 211 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Transmembrane 212 231 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Topological domain 232 297 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Transmembrane 298 317 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Topological domain 318 342 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Transmembrane 343 367 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Topological domain 368 402 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Transmembrane 403 419 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Topological domain 420 425 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Transmembrane 426 449 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Topological domain 450 464 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Transmembrane 465 486 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Topological domain 487 498 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Transmembrane 499 516 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Topological domain 517 618 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36029 UniProtKB Modified residue 569 569 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q04183 1 1289 +Q04183 UniProtKB Chain 1 1289 . . . ID=PRO_0000076355;Note=Trafficking protein particle complex II-specific subunit 120 +Q04183 UniProtKB Modified residue 379 379 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04183 UniProtKB Modified residue 387 387 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04183 UniProtKB Sequence conflict 435 435 . . . Note=A->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03660 1 1102 +Q03660 UniProtKB Chain 1 1102 . . . ID=PRO_0000193512;Note=Trafficking protein particle complex II-specific subunit 130 +##sequence-region P38342 1 320 +P38342 UniProtKB Chain 1 320 . . . ID=PRO_0000054800;Note=3-ketodihydrosphingosine reductase TSC10 +P38342 UniProtKB Transmembrane 280 300 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38342 UniProtKB Nucleotide binding 11 37 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38342 UniProtKB Active site 180 180 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38342 UniProtKB Active site 184 184 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38342 UniProtKB Binding site 167 167 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38342 UniProtKB Sequence conflict 255 255 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38342 UniProtKB Sequence conflict 255 255 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38427 1 1098 +P38427 UniProtKB Chain 1 1098 . . . ID=PRO_0000122511;Note=Trehalose synthase complex regulatory subunit TSL1 +P38427 UniProtKB Repeat 144 150 . . . Note=1 +P38427 UniProtKB Repeat 158 164 . . . Note=2 +P38427 UniProtKB Region 144 164 . . . Note=2 X 7 AA repeats of R-I-A-S-P-I-Q +P38427 UniProtKB Region 320 812 . . . Note=TPS complex domain +P38427 UniProtKB Compositional bias 42 45 . . . Note=Poly-Gln +P38427 UniProtKB Compositional bias 164 168 . . . Note=Poly-Gln +P38427 UniProtKB Modified residue 49 49 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38427 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38427 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38427 UniProtKB Modified residue 71 71 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38427 UniProtKB Modified residue 77 77 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38427 UniProtKB Modified residue 135 135 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38427 UniProtKB Modified residue 147 147 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38427 UniProtKB Modified residue 161 161 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38427 UniProtKB Modified residue 229 229 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38427 UniProtKB Modified residue 251 251 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38427 UniProtKB Modified residue 303 303 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38427 UniProtKB Modified residue 815 815 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P50078 1 622 +P50078 UniProtKB Chain 1 622 . . . ID=PRO_0000072633;Note=Protein TOS2 +P50078 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53257 1 314 +P53257 UniProtKB Chain 1 314 . . . ID=PRO_0000090696;Note=Mitochondrial thiamine pyrophosphate carrier 1 +P53257 UniProtKB Transmembrane 14 30 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53257 UniProtKB Transmembrane 84 100 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53257 UniProtKB Transmembrane 116 136 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53257 UniProtKB Transmembrane 170 186 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53257 UniProtKB Transmembrane 217 233 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53257 UniProtKB Transmembrane 285 302 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53257 UniProtKB Repeat 14 103 . . . Note=Solcar 1 +P53257 UniProtKB Repeat 110 195 . . . Note=Solcar 2 +P53257 UniProtKB Repeat 210 310 . . . Note=Solcar 3 +P53257 UniProtKB Sequence conflict 66 66 . . . Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q00764 1 495 +Q00764 UniProtKB Chain 1 495 . . . ID=PRO_0000122502;Note=Alpha%2Calpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunit +Q00764 UniProtKB Mutagenesis 223 223 . . . Note=In GLC6-1%3B low glycogen accumulation. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8150278;Dbxref=PMID:8150278 +Q00764 UniProtKB Sequence conflict 75 75 . . . Note=K->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00764 UniProtKB Sequence conflict 101 101 . . . Note=H->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00764 UniProtKB Sequence conflict 104 104 . . . Note=G->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00764 UniProtKB Sequence conflict 129 130 . . . Note=LA->FG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00764 UniProtKB Sequence conflict 217 217 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00764 UniProtKB Sequence conflict 288 288 . . . Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P35172 1 780 +P35172 UniProtKB Chain 1 780 . . . ID=PRO_0000173800;Note=Probable trehalase +P35172 UniProtKB Region 338 339 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35172 UniProtKB Region 384 386 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35172 UniProtKB Active site 507 507 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35172 UniProtKB Active site 703 703 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35172 UniProtKB Binding site 331 331 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35172 UniProtKB Binding site 375 375 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35172 UniProtKB Binding site 384 384 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35172 UniProtKB Binding site 505 505 . . . Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35172 UniProtKB Modified residue 52 52 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35172 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35172 UniProtKB Modified residue 88 88 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P35172 UniProtKB Modified residue 112 112 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q07527 1 1436 +Q07527 UniProtKB Chain 1 1436 . . . ID=PRO_0000270921;Note=tRNA (guanosine(18)-2'-O)-methyltransferase +Q07527 UniProtKB Region 1365 1367 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13395 +Q07527 UniProtKB Region 1409 1418 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13395 +Q07527 UniProtKB Binding site 1389 1389 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13395 +##sequence-region Q02721 1 264 +Q02721 UniProtKB Chain 1 264 . . . ID=PRO_0000097213;Note=Meiotic recombination protein REC102 +##sequence-region P34219 1 525 +P34219 UniProtKB Chain 1 525 . . . ID=PRO_0000197146;Note=Transcriptional regulatory protein TOD6 +P34219 UniProtKB Domain 67 124 . . . Note=HTH myb-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +P34219 UniProtKB DNA binding 97 120 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +P34219 UniProtKB Modified residue 280 280 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34219 UniProtKB Modified residue 333 333 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34219 UniProtKB Modified residue 341 341 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34219 UniProtKB Modified residue 366 366 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region P33448 1 61 +P33448 UniProtKB Chain 1 61 . . . ID=PRO_0000210820;Note=Mitochondrial import receptor subunit TOM6 +P33448 UniProtKB Topological domain 1 31 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33448 UniProtKB Transmembrane 32 52 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33448 UniProtKB Topological domain 53 61 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33448 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P38811 1 3744 +P38811 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38811 UniProtKB Chain 2 3744 . . . ID=PRO_0000088854;Note=Transcription-associated protein 1 +P38811 UniProtKB Domain 2622 3177 . . . Note=FAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534 +P38811 UniProtKB Domain 3414 3711 . . . Note=PI3K/PI4K +P38811 UniProtKB Domain 3712 3744 . . . Note=FATC;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534,ECO:0000255|PROSITE-ProRule:PRU00535 +P38811 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38811 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38811 UniProtKB Modified residue 542 542 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38811 UniProtKB Mutagenesis 241 241 . . . Note=In TRA1-2%3B when associated with L-604%3B R-2733%3B P-3145%3B S-3222 and G-3302. Defects in its ability to interact with acidic activators. L->S +P38811 UniProtKB Mutagenesis 604 604 . . . Note=In TRA1-2%3B when associated with S-241%3B R-2733%3B P-3145%3B S-3222 and G-3302. Defects in its ability to interact with acidic activators. F->L +P38811 UniProtKB Mutagenesis 2733 2733 . . . Note=In TRA1-2%3B when associated with S-241%3B L-604%3B P-3145%3B S-3222 and G-3302. Defects in its ability to interact with acidic activators. W->R +P38811 UniProtKB Mutagenesis 3145 3145 . . . Note=In TRA1-2%3B when associated with S-241%3B L-604%3B R-2733%3B S-3222 and G-3302. Defects in its ability to interact with acidic activators. S->P +P38811 UniProtKB Mutagenesis 3222 3222 . . . Note=In TRA1-2%3B when associated with S-241%3B L-604%3B R-2733%3B P-3145 and G-3302. Defects in its ability to interact with acidic activators. L->S +P38811 UniProtKB Mutagenesis 3302 3302 . . . Note=In TRA1-2%3B when associated with S-241%3B L-604%3B R-2733%3B P-3145 and S-3222. Defects in its ability to interact with acidic activators. D->G +##sequence-region Q08693 1 809 +Q08693 UniProtKB Chain 1 809 . . . ID=PRO_0000237639;Note=Putative zinc metalloprotease TRE2 +Q08693 UniProtKB Topological domain 1 125 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08693 UniProtKB Transmembrane 126 146 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08693 UniProtKB Topological domain 147 809 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08693 UniProtKB Domain 255 349 . . . Note=PA +Q08693 UniProtKB Glycosylation 228 228 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08693 UniProtKB Glycosylation 669 669 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08693 UniProtKB Glycosylation 736 736 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P48561 1 642 +P48561 UniProtKB Chain 1 642 . . . ID=PRO_0000120316;Note=Poly(A) RNA polymerase protein 1 +P48561 UniProtKB Domain 368 428 . . . Note=PAP-associated +P48561 UniProtKB Metal binding 233 233 . . . Note=Magnesium or manganese%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P48561 UniProtKB Metal binding 235 235 . . . Note=Magnesium or manganese%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P48561 UniProtKB Modified residue 596 596 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48561 UniProtKB Modified residue 602 602 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48561 UniProtKB Sequence conflict 354 355 . . . Note=MH->ID;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P28584 1 889 +P28584 UniProtKB Chain 1 889 . . . ID=PRO_0000070464;Note=Low-affinity potassium transport protein +P28584 UniProtKB Topological domain 1 51 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Transmembrane 52 73 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Topological domain 74 80 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Transmembrane 81 101 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Topological domain 102 109 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Transmembrane 110 130 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Topological domain 131 464 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Transmembrane 465 487 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Topological domain 488 499 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Transmembrane 500 521 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Topological domain 522 524 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Transmembrane 525 545 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Topological domain 546 548 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Transmembrane 549 569 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Topological domain 570 584 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Transmembrane 585 605 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Topological domain 606 609 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Transmembrane 610 630 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Topological domain 631 657 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Transmembrane 658 678 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Topological domain 679 743 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Transmembrane 744 764 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Topological domain 765 776 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Transmembrane 777 797 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Topological domain 798 889 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Glycosylation 216 216 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Glycosylation 233 233 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28584 UniProtKB Glycosylation 265 265 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12383 1 476 +Q12383 UniProtKB Chain 1 476 . . . ID=PRO_0000235932;Note=tRNA:m(4)X modification enzyme TRM13 +Q12383 UniProtKB Zinc finger 72 99 . . . Note=CHHC U11-48K-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01141 +##sequence-region P25040 1 408 +P25040 UniProtKB Chain 1 408 . . . ID=PRO_0000203487;Note=20S rRNA accumulation protein 4 +##sequence-region P36164 1 337 +P36164 UniProtKB Chain 1 337 . . . ID=PRO_0000203226;Note=Golgi apparatus membrane protein TVP38 +P36164 UniProtKB Topological domain 1 95 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36164 UniProtKB Transmembrane 96 116 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36164 UniProtKB Topological domain 117 137 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36164 UniProtKB Transmembrane 138 158 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36164 UniProtKB Topological domain 159 169 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36164 UniProtKB Transmembrane 170 190 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36164 UniProtKB Topological domain 191 251 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36164 UniProtKB Transmembrane 252 272 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36164 UniProtKB Topological domain 273 286 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36164 UniProtKB Transmembrane 287 307 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36164 UniProtKB Topological domain 308 337 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P33122 1 291 +P33122 UniProtKB Chain 1 291 . . . ID=PRO_0000127495;Note=Serine-rich protein TYE7 +P33122 UniProtKB Domain 180 265 . . . Note=bHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981 +P33122 UniProtKB Compositional bias 63 69 . . . Note=Poly-Ser +P33122 UniProtKB Modified residue 104 104 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P33122 UniProtKB Modified residue 237 237 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P33122 UniProtKB Mutagenesis 189 189 . . . Note=In SGC1-1%3B suppresses transcriptional defect caused by a GCR1 null mutation. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7739544;Dbxref=PMID:7739544 +P33122 UniProtKB Mutagenesis 210 210 . . . Note=In SGC1-2/3/4%3B suppresses transcriptional defect caused by a GCR1 null mutation. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7739544;Dbxref=PMID:7739544 +##sequence-region P06785 1 304 +P06785 UniProtKB Chain 1 304 . . . ID=PRO_0000140912;Note=Thymidylate synthase +P06785 UniProtKB Nucleotide binding 157 158 . . . Note=dUMP%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A884 +P06785 UniProtKB Nucleotide binding 206 209 . . . Note=dUMP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A884 +P06785 UniProtKB Nucleotide binding 247 249 . . . Note=dUMP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A884 +P06785 UniProtKB Active site 177 177 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A884 +P06785 UniProtKB Binding site 30 30 . . . Note=dUMP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A884 +P06785 UniProtKB Binding site 209 209 . . . Note=5%2C10-methylenetetrahydrofolate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A884 +P06785 UniProtKB Binding site 217 217 . . . Note=dUMP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A884 +P06785 UniProtKB Sequence conflict 34 78 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CF16 1 290 +P0CF16 UniProtKB Chain 1 290 . . . ID=PRO_0000203265;Note=UPF0507 protein YML003W +##sequence-region P21734 1 215 +P21734 UniProtKB Chain 1 215 . . . ID=PRO_0000082525;Note=Ubiquitin-conjugating enzyme E2 1 +P21734 UniProtKB Active site 88 88 . . . Note=Glycyl thioester intermediate +P21734 UniProtKB Cross-link 93 93 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P21734 UniProtKB Helix 3 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY +P21734 UniProtKB Helix 18 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY +P21734 UniProtKB Beta strand 22 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY +P21734 UniProtKB Beta strand 28 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TTE +P21734 UniProtKB Beta strand 32 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY +P21734 UniProtKB Beta strand 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FXT +P21734 UniProtKB Turn 46 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY +P21734 UniProtKB Beta strand 51 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY +P21734 UniProtKB Turn 60 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY +P21734 UniProtKB Beta strand 68 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY +P21734 UniProtKB Beta strand 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TTE +P21734 UniProtKB Turn 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY +P21734 UniProtKB Helix 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY +P21734 UniProtKB Turn 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY +P21734 UniProtKB Helix 102 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY +P21734 UniProtKB Beta strand 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FXT +P21734 UniProtKB Helix 124 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY +P21734 UniProtKB Helix 134 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FZY +P21734 UniProtKB Helix 170 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TTE +P21734 UniProtKB Helix 183 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TTE +P21734 UniProtKB Helix 204 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TTE +##sequence-region P33296 1 250 +P33296 UniProtKB Chain 1 250 . . . ID=PRO_0000082552;Note=Ubiquitin-conjugating enzyme E2 6 +P33296 UniProtKB Topological domain 1 232 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33296 UniProtKB Transmembrane 233 249 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33296 UniProtKB Active site 87 87 . . . Note=Glycyl thioester intermediate +P33296 UniProtKB Modified residue 139 139 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33296 UniProtKB Modified residue 178 178 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P33296 UniProtKB Mutagenesis 87 87 . . . Note=Loss of activity. C->S +##sequence-region P36026 1 717 +P36026 UniProtKB Chain 1 717 . . . ID=PRO_0000080596;Note=Ubiquitin carboxyl-terminal hydrolase 11 +P36026 UniProtKB Domain 298 707 . . . Note=USP +P36026 UniProtKB Compositional bias 557 564 . . . Note=Poly-His +P36026 UniProtKB Active site 307 307 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +P36026 UniProtKB Active site 649 649 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +##sequence-region P38237 1 781 +P38237 UniProtKB Chain 1 781 . . . ID=PRO_0000080599;Note=Ubiquitin carboxyl-terminal hydrolase 14 +P38237 UniProtKB Domain 323 781 . . . Note=USP +P38237 UniProtKB Domain 576 626 . . . Note=UBA 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212 +P38237 UniProtKB Domain 649 689 . . . Note=UBA 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212 +P38237 UniProtKB Zinc finger 190 262 . . . Note=UBP-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502 +P38237 UniProtKB Compositional bias 92 95 . . . Note=Poly-Asn +P38237 UniProtKB Active site 332 332 . . . Note=Nucleophile +P38237 UniProtKB Active site 737 737 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +P38237 UniProtKB Mutagenesis 332 332 . . . Note=Loss of enzyme activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9305625;Dbxref=PMID:9305625 +##sequence-region P32571 1 926 +P32571 UniProtKB Chain 1 926 . . . ID=PRO_0000080589;Note=Ubiquitin carboxyl-terminal hydrolase 4 +P32571 UniProtKB Domain 205 328 . . . Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173 +P32571 UniProtKB Domain 562 923 . . . Note=USP +P32571 UniProtKB Compositional bias 386 392 . . . Note=Poly-Gln +P32571 UniProtKB Active site 571 571 . . . Note=Nucleophile +P32571 UniProtKB Active site 880 880 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +P32571 UniProtKB Modified residue 443 443 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32571 UniProtKB Mutagenesis 571 571 . . . Note=Impairs deubiquitination activity and protein sorting into the MVB pathway. C->S%2CA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17376168,ECO:0000269|PubMed:17446860;Dbxref=PMID:17376168,PMID:17446860 +P32571 UniProtKB Mutagenesis 826 826 . . . Note=Impairs deubiquitination activity and binding to BRO1%3B when associated with A-827 and A-829. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17446860;Dbxref=PMID:17446860 +P32571 UniProtKB Mutagenesis 827 827 . . . Note=Impairs deubiquitination activity and binding to BRO1%3B when associated with A-826 and A-829. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17446860;Dbxref=PMID:17446860 +P32571 UniProtKB Mutagenesis 829 829 . . . Note=Impairs deubiquitination activity and binding to BRO1%3B when associated with A-826 and A-827. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17446860;Dbxref=PMID:17446860 +P32571 UniProtKB Sequence conflict 327 327 . . . Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32571 UniProtKB Sequence conflict 345 345 . . . Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32571 UniProtKB Sequence conflict 375 378 . . . Note=MLVA->TASW;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32571 UniProtKB Sequence conflict 383 383 . . . Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32571 UniProtKB Sequence conflict 407 407 . . . Note=K->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32571 UniProtKB Sequence conflict 543 570 . . . Note=LDHTDVTPTSSHNYDLDFAVGLENLGNS->FRSYEMLHQLLLIIMTLISRLVWENLEIP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32571 UniProtKB Sequence conflict 580 580 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32571 UniProtKB Sequence conflict 836 836 . . . Note=W->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32571 UniProtKB Sequence conflict 897 897 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40453 1 1071 +P40453 UniProtKB Chain 1 1071 . . . ID=PRO_0000080592;Note=Ubiquitin carboxyl-terminal hydrolase 7 +P40453 UniProtKB Domain 609 1069 . . . Note=USP +P40453 UniProtKB Active site 618 618 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +P40453 UniProtKB Active site 1014 1014 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +##sequence-region P19812 1 1950 +P19812 UniProtKB Chain 1 1950 . . . ID=PRO_0000056135;Note=E3 ubiquitin-protein ligase UBR1 +P19812 UniProtKB Zinc finger 121 194 . . . Note=UBR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00508 +P19812 UniProtKB Zinc finger 1220 1324 . . . Note=RING-type%3B atypical +P19812 UniProtKB Region 1117 1219 . . . Note=Interaction with UBC2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10581257;Dbxref=PMID:10581257 +P19812 UniProtKB Modified residue 296 296 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P19812 UniProtKB Modified residue 300 300 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P19812 UniProtKB Modified residue 1938 1938 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P19812 UniProtKB Mutagenesis 1168 1168 . . . Note=Impairs interaction with UBC2%2C but does not affect degradation of N-end rule substrates. K->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10581257;Dbxref=PMID:10581257 +P19812 UniProtKB Mutagenesis 1169 1169 . . . Note=Impairs interaction with UBC2%2C but does not affect degradation of N-end rule substrates. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10581257;Dbxref=PMID:10581257 +P19812 UniProtKB Mutagenesis 1173 1173 . . . Note=Impairs interaction with UBC2%2C but does not affect degradation of N-end rule substrates. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10581257;Dbxref=PMID:10581257 +P19812 UniProtKB Mutagenesis 1220 1220 . . . Note=No effect on interaction with UBC2%2C but inhibits degradation of N-end rule substrates. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10581257;Dbxref=PMID:10581257 +P19812 UniProtKB Mutagenesis 1223 1223 . . . Note=No effect on interaction with UBC2%2C but inhibits degradation of N-end rule substrates. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10581257;Dbxref=PMID:10581257 +P19812 UniProtKB Mutagenesis 1295 1295 . . . Note=No effect on interaction with UBC2%2C but inhibits degradation of N-end rule substrates. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10581257;Dbxref=PMID:10581257 +P19812 UniProtKB Mutagenesis 1297 1297 . . . Note=No effect on interaction with UBC2%2C but inhibits degradation of N-end rule substrates. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10581257;Dbxref=PMID:10581257 +P19812 UniProtKB Mutagenesis 1320 1320 . . . Note=No effect on interaction with UBC2%2C but inhibits degradation of N-end rule substrates. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10581257;Dbxref=PMID:10581257 +P19812 UniProtKB Beta strand 132 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS +P19812 UniProtKB Turn 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS +P19812 UniProtKB Beta strand 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS +P19812 UniProtKB Turn 149 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS +P19812 UniProtKB Helix 154 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS +P19812 UniProtKB Beta strand 162 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS +P19812 UniProtKB Beta strand 169 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS +P19812 UniProtKB Helix 180 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS +P19812 UniProtKB Beta strand 183 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS +P19812 UniProtKB Helix 190 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NIS +##sequence-region Q07963 1 1872 +Q07963 UniProtKB Chain 1 1872 . . . ID=PRO_0000056142;Note=E3 ubiquitin-protein ligase UBR2 +Q07963 UniProtKB Zinc finger 96 172 . . . Note=UBR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00508 +Q07963 UniProtKB Zinc finger 1241 1362 . . . Note=RING-type%3B atypical +Q07963 UniProtKB Region 1134 1240 . . . Note=Interaction with UBC2 +Q07963 UniProtKB Modified residue 1218 1218 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07963 UniProtKB Modified residue 1222 1222 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q07963 UniProtKB Cross-link 709 709 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region Q04228 1 584 +Q04228 UniProtKB Chain 1 584 . . . ID=PRO_0000210999;Note=UBX domain-containing protein 2 +Q04228 UniProtKB Topological domain 1 80 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04228 UniProtKB Transmembrane 81 101 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04228 UniProtKB Topological domain 102 151 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04228 UniProtKB Transmembrane 152 172 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04228 UniProtKB Topological domain 173 584 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04228 UniProtKB Domain 426 570 . . . Note=UBX +##sequence-region Q06682 1 500 +Q06682 UniProtKB Chain 1 500 . . . ID=PRO_0000211002;Note=UBX domain-containing protein 5 +Q06682 UniProtKB Domain 415 493 . . . Note=UBX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00215 +Q06682 UniProtKB Modified residue 139 139 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region Q03337 1 283 +Q03337 UniProtKB Chain 1 283 . . . ID=PRO_0000211585;Note=Trafficking protein particle complex subunit 31 +##sequence-region Q07381 1 788 +Q07381 UniProtKB Chain 1 788 . . . ID=PRO_0000065671;Note=Ribosome biogenesis protein TSR1 +Q07381 UniProtKB Domain 82 254 . . . Note=Bms1-type G +Q07381 UniProtKB Compositional bias 413 496 . . . Note=Glu-rich +##sequence-region P20049 1 452 +P20049 UniProtKB Chain 1 452 . . . ID=PRO_0000119208;Note=Prephenate dehydrogenase [NADP(+)] +P20049 UniProtKB Domain 14 297 . . . Note=Prephenate/arogenate dehydrogenase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00522 +P20049 UniProtKB Nucleotide binding 14 43 . . . Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20049 UniProtKB Sequence conflict 38 38 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20049 UniProtKB Sequence conflict 204 211 . . . Note=IKIYPWTL->DKDSSLDS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20049 UniProtKB Sequence conflict 312 313 . . . Note=GN->SD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20049 UniProtKB Sequence conflict 433 452 . . . Note=MIKTILSHSSDRSAAEKRNT->DDKNHSESF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P07285 1 380 +P07285 UniProtKB Chain 1 380 . . . ID=PRO_0000154528;Note=Anthranilate phosphoribosyltransferase +##sequence-region Q03784 1 219 +Q03784 UniProtKB Chain 1 219 . . . ID=PRO_0000211571;Note=Trafficking protein particle complex subunit 23 +##sequence-region P25372 1 127 +P25372 UniProtKB Transit peptide 1 21 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25372 UniProtKB Chain 22 127 . . . ID=PRO_0000034155;Note=Thioredoxin-3%2C mitochondrial +P25372 UniProtKB Domain 22 127 . . . Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +P25372 UniProtKB Active site 55 55 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25372 UniProtKB Active site 58 58 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25372 UniProtKB Site 49 49 . . . Note=Deprotonates C-terminal active site Cys;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25372 UniProtKB Site 56 56 . . . Note=Contributes to redox potential value;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25372 UniProtKB Site 57 57 . . . Note=Contributes to redox potential value;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25372 UniProtKB Disulfide bond 55 58 . . . Note=Redox-active;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +P25372 UniProtKB Helix 24 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3 +P25372 UniProtKB Helix 33 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3 +P25372 UniProtKB Beta strand 44 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3 +P25372 UniProtKB Helix 56 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3 +P25372 UniProtKB Helix 62 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3 +P25372 UniProtKB Beta strand 75 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3 +P25372 UniProtKB Turn 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3 +P25372 UniProtKB Helix 86 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3 +P25372 UniProtKB Beta strand 96 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3 +P25372 UniProtKB Beta strand 107 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3 +P25372 UniProtKB Helix 117 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OE3 +##sequence-region P29509 1 319 +P29509 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7961686;Dbxref=PMID:7961686 +P29509 UniProtKB Chain 2 319 . . . ID=PRO_0000166770;Note=Thioredoxin reductase 1 +P29509 UniProtKB Nucleotide binding 11 14 . . . Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18930846,ECO:0000269|PubMed:20235561;Dbxref=PMID:18930846,PMID:20235561 +P29509 UniProtKB Nucleotide binding 40 41 . . . Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18930846,ECO:0000269|PubMed:20235561;Dbxref=PMID:18930846,PMID:20235561 +P29509 UniProtKB Nucleotide binding 295 297 . . . Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18930846,ECO:0000269|PubMed:20235561;Dbxref=PMID:18930846,PMID:20235561 +P29509 UniProtKB Binding site 45 45 . . . Note=FAD%3B via amide nitrogen;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18930846,ECO:0000269|PubMed:20235561;Dbxref=PMID:18930846,PMID:20235561 +P29509 UniProtKB Binding site 54 54 . . . Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18930846,ECO:0000269|PubMed:20235561;Dbxref=PMID:18930846,PMID:20235561 +P29509 UniProtKB Binding site 87 87 . . . Note=FAD%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18930846,ECO:0000269|PubMed:20235561;Dbxref=PMID:18930846,PMID:20235561 +P29509 UniProtKB Binding site 145 145 . . . Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18930846,ECO:0000269|PubMed:20235561;Dbxref=PMID:18930846,PMID:20235561 +P29509 UniProtKB Binding site 288 288 . . . Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18930846,ECO:0000269|PubMed:20235561;Dbxref=PMID:18930846,PMID:20235561 +P29509 UniProtKB Modified residue 303 303 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P29509 UniProtKB Disulfide bond 142 145 . . . Note=Redox-active;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20235561;Dbxref=PMID:20235561 +P29509 UniProtKB Sequence conflict 18 18 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29509 UniProtKB Sequence conflict 101 101 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29509 UniProtKB Sequence conflict 111 111 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29509 UniProtKB Sequence conflict 180 196 . . . Note=VFMLVRKDHLRASTIMQ->CLCLSEKTICVLLPLCK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29509 UniProtKB Beta strand 3 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Helix 13 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 30 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 35 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Helix 45 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 49 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Helix 64 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 87 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 93 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 110 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Helix 131 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Turn 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 139 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Helix 143 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Helix 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 155 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Helix 164 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Turn 174 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 177 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 185 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Helix 193 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 205 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 210 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Turn 231 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 235 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 242 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 250 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Helix 255 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Turn 258 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D8X +P29509 UniProtKB Beta strand 275 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Beta strand 283 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Helix 287 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +P29509 UniProtKB Helix 297 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ITJ +##sequence-region P47168 1 421 +P47168 UniProtKB Chain 1 421 . . . ID=PRO_0000203122;Note=TEL2-interacting protein 2 +##sequence-region P38962 1 199 +P38962 UniProtKB Chain 1 199 . . . ID=PRO_0000212837;Note=Golgi apparatus membrane protein TVP23 +P38962 UniProtKB Transmembrane 18 36 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38962 UniProtKB Transmembrane 43 60 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38962 UniProtKB Transmembrane 108 128 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38962 UniProtKB Transmembrane 133 153 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38962 UniProtKB Glycosylation 63 63 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38962 UniProtKB Glycosylation 86 86 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38962 UniProtKB Glycosylation 185 185 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P22803 1 104 +P22803 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7961686;Dbxref=PMID:7961686 +P22803 UniProtKB Chain 2 104 . . . ID=PRO_0000120045;Note=Thioredoxin-2 +P22803 UniProtKB Domain 2 104 . . . Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +P22803 UniProtKB Active site 31 31 . . . Note=Nucleophile +P22803 UniProtKB Active site 34 34 . . . Note=Nucleophile +P22803 UniProtKB Site 25 25 . . . Note=Deprotonates C-terminal active site Cys +P22803 UniProtKB Site 32 32 . . . Note=Contributes to redox potential value +P22803 UniProtKB Site 33 33 . . . Note=Contributes to redox potential value +P22803 UniProtKB Modified residue 62 62 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P22803 UniProtKB Disulfide bond 31 34 . . . Note=Redox-active;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00691,ECO:0000269|PubMed:17044062;Dbxref=PMID:17044062 +P22803 UniProtKB Cross-link 67 67 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P22803 UniProtKB Cross-link 97 97 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P22803 UniProtKB Beta strand 3 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS +P22803 UniProtKB Helix 8 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS +P22803 UniProtKB Beta strand 19 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS +P22803 UniProtKB Helix 32 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS +P22803 UniProtKB Beta strand 51 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS +P22803 UniProtKB Turn 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS +P22803 UniProtKB Helix 62 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS +P22803 UniProtKB Beta strand 72 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS +P22803 UniProtKB Beta strand 83 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS +P22803 UniProtKB Helix 93 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DSS +##sequence-region P38254 1 753 +P38254 UniProtKB Chain 1 753 . . . ID=PRO_0000212448;Note=Probable tubulin--tyrosine ligase PBY1 +P38254 UniProtKB Domain 343 734 . . . Note=TTL;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00568 +P38254 UniProtKB Sequence conflict 352 355 . . . Note=HALK->TPE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38254 UniProtKB Sequence conflict 450 450 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38254 UniProtKB Sequence conflict 450 450 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38254 UniProtKB Sequence conflict 563 563 . . . Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P29340 1 183 +P29340 UniProtKB Chain 1 183 . . . ID=PRO_0000082558;Note=Ubiquitin-conjugating enzyme E2-21 kDa +P29340 UniProtKB Active site 115 115 . . . Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00388,ECO:0000255|PROSITE-ProRule:PRU10133 +P29340 UniProtKB Helix 16 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P29340 UniProtKB Turn 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P29340 UniProtKB Turn 42 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P29340 UniProtKB Beta strand 47 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P29340 UniProtKB Beta strand 60 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P29340 UniProtKB Beta strand 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BWF +P29340 UniProtKB Turn 72 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P29340 UniProtKB Beta strand 77 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P29340 UniProtKB Turn 86 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P29340 UniProtKB Beta strand 94 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P29340 UniProtKB Turn 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P29340 UniProtKB Helix 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P29340 UniProtKB Turn 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P29340 UniProtKB Helix 130 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P29340 UniProtKB Helix 152 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P29340 UniProtKB Turn 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P29340 UniProtKB Helix 163 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +##sequence-region Q12094 1 313 +Q12094 UniProtKB Chain 1 313 . . . ID=PRO_0000094426;Note=Ribosome biogenesis protein TSR3 +Q12094 UniProtKB Modified residue 286 286 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12094 UniProtKB Modified residue 289 289 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q08747 1 228 +Q08747 UniProtKB Chain 1 228 . . . ID=PRO_0000245507;Note=Upstream activation factor subunit UAF30 +Q08747 UniProtKB Domain 120 194 . . . Note=SWIB +Q08747 UniProtKB Modified residue 218 218 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q08747 UniProtKB Modified residue 220 220 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q08747 UniProtKB Modified residue 223 223 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region P14682 1 295 +P14682 UniProtKB Chain 1 295 . . . ID=PRO_0000082541;Note=Ubiquitin-conjugating enzyme E2-34 kDa +P14682 UniProtKB Compositional bias 191 289 . . . Note=Asp/Glu-rich (acidic) +P14682 UniProtKB Active site 95 95 . . . Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00388,ECO:0000255|PROSITE-ProRule:PRU10133 +P14682 UniProtKB Modified residue 186 186 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14682 UniProtKB Modified residue 282 282 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14682 UniProtKB Modified residue 292 292 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P40032 1 644 +P40032 UniProtKB Chain 1 644 . . . ID=PRO_0000206670;Note=Prolyl 3%2C4-dihydroxylase TPA1 +P40032 UniProtKB Domain 141 247 . . . Note=Fe2OG dioxygenase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00805 +P40032 UniProtKB Metal binding 159 159 . . . Note=Iron;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00805,ECO:0000269|PubMed:20040577;Dbxref=PMID:20040577 +P40032 UniProtKB Metal binding 161 161 . . . Note=Iron;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00805,ECO:0000269|PubMed:20040577;Dbxref=PMID:20040577 +P40032 UniProtKB Metal binding 227 227 . . . Note=Iron;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00805,ECO:0000269|PubMed:20040577;Dbxref=PMID:20040577 +P40032 UniProtKB Binding site 173 173 . . . Note=2-oxoglutarate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00805,ECO:0000269|PubMed:20040577;Dbxref=PMID:20040577 +P40032 UniProtKB Binding site 238 238 . . . Note=2-oxoglutarate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00805,ECO:0000269|PubMed:20040577;Dbxref=PMID:20040577 +P40032 UniProtKB Modified residue 607 607 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40032 UniProtKB Mutagenesis 159 161 . . . Note=Loss of function. HDD->ADN%2CADA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20630870,ECO:0000269|PubMed:24550462;Dbxref=PMID:20630870,PMID:24550462 +P40032 UniProtKB Mutagenesis 159 159 . . . Note=Loss of function. H->A +P40032 UniProtKB Helix 27 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Helix 32 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Helix 37 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 56 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Helix 64 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 81 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 86 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Helix 111 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Helix 123 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 139 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MGU +P40032 UniProtKB Beta strand 145 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 155 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 166 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Helix 183 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 189 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 194 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 205 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 214 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Turn 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 227 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 238 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Helix 252 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NHK +P40032 UniProtKB Helix 259 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Helix 269 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT4 +P40032 UniProtKB Helix 278 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Helix 294 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Helix 332 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Helix 344 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Helix 349 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 363 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Helix 373 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Helix 396 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Turn 409 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 415 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 419 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT1 +P40032 UniProtKB Helix 428 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Helix 443 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Turn 461 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Helix 466 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Helix 481 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 492 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 497 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Turn 507 509 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Helix 521 523 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 527 540 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Turn 546 550 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 555 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 588 592 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 596 604 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 609 612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +P40032 UniProtKB Beta strand 623 634 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT7 +##sequence-region P31688 1 896 +P31688 UniProtKB Chain 1 896 . . . ID=PRO_0000122509;Note=Trehalose-phosphatase +P31688 UniProtKB Region 1 554 . . . Note=Glycosyltransferase +P31688 UniProtKB Sequence conflict 48 48 . . . Note=F->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31688 UniProtKB Sequence conflict 289 289 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31688 UniProtKB Sequence conflict 542 542 . . . Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31688 UniProtKB Sequence conflict 546 546 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31688 UniProtKB Sequence conflict 549 549 . . . Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38426 1 1054 +P38426 UniProtKB Chain 1 1054 . . . ID=PRO_0000122510;Note=Trehalose synthase complex regulatory subunit TPS3 +P38426 UniProtKB Region 287 778 . . . Note=Glycosyltransferase +P38426 UniProtKB Compositional bias 125 249 . . . Note=Ser-rich +P38426 UniProtKB Modified residue 148 148 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38426 UniProtKB Modified residue 150 150 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38426 UniProtKB Modified residue 181 181 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950 +P38426 UniProtKB Modified residue 265 265 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38426 UniProtKB Modified residue 267 267 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38426 UniProtKB Modified residue 273 273 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38426 UniProtKB Modified residue 960 960 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38426 UniProtKB Sequence conflict 186 186 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38426 UniProtKB Sequence conflict 765 765 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38426 UniProtKB Sequence conflict 834 834 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38426 UniProtKB Sequence conflict 902 902 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P46959 1 383 +P46959 UniProtKB Chain 1 383 . . . ID=PRO_0000087437;Note=tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRM61 +P46959 UniProtKB Region 121 124 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000269,ECO:0000312;evidence=ECO:0000269|PubMed:27582183,ECO:0000312|PDB:5ERG;Dbxref=PMID:27582183 +P46959 UniProtKB Region 168 169 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000269,ECO:0000312;evidence=ECO:0000269|PubMed:27582183,ECO:0000312|PDB:5ERG;Dbxref=PMID:27582183 +P46959 UniProtKB Binding site 94 94 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000269,ECO:0000312;evidence=ECO:0000269|PubMed:27582183,ECO:0000312|PDB:5ERG;Dbxref=PMID:27582183 +P46959 UniProtKB Binding site 139 139 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000269,ECO:0000312;evidence=ECO:0000269|PubMed:27582183,ECO:0000312|PDB:5ERG;Dbxref=PMID:27582183 +P46959 UniProtKB Binding site 144 144 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96FX7 +P46959 UniProtKB Binding site 203 203 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000269,ECO:0000312;evidence=ECO:0000269|PubMed:27582183,ECO:0000312|PDB:5ERG;Dbxref=PMID:27582183 +P46959 UniProtKB Modified residue 302 302 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P46959 UniProtKB Beta strand 18 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Beta strand 27 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Beta strand 38 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Beta strand 44 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Helix 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Turn 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Beta strand 58 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Beta strand 71 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Helix 80 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Helix 96 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Beta strand 113 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Helix 123 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Beta strand 133 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Helix 142 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Turn 158 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Beta strand 162 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Helix 169 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Beta strand 180 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Beta strand 197 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Helix 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Helix 211 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Beta strand 220 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Beta strand 224 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Helix 233 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Beta strand 249 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Helix 271 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Beta strand 341 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Beta strand 357 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +P46959 UniProtKB Helix 371 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EQJ +##sequence-region P38238 1 310 +P38238 UniProtKB Chain 1 310 . . . ID=PRO_0000155587;Note=tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase +P38238 UniProtKB Active site 164 164 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03162 +P38238 UniProtKB Binding site 55 55 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03162 +P38238 UniProtKB Binding site 57 57 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03162 +P38238 UniProtKB Binding site 83 83 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03162 +P38238 UniProtKB Binding site 99 99 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03162 +P38238 UniProtKB Binding site 124 124 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03162 +##sequence-region P49957 1 279 +P49957 UniProtKB Chain 1 279 . . . ID=PRO_0000203262;Note=tRNA (carboxymethyluridine(34)-5-O)-methyltransferase +##sequence-region Q12009 1 286 +Q12009 UniProtKB Chain 1 286 . . . ID=PRO_0000171437;Note=tRNA (guanine-N(7)-)-methyltransferase +Q12009 UniProtKB Region 126 127 . . . Note=S-adenosyl-L-methionine binding +Q12009 UniProtKB Region 161 162 . . . Note=S-adenosyl-L-methionine binding +Q12009 UniProtKB Region 259 261 . . . Note=S-adenosyl-L-methionine binding +Q12009 UniProtKB Active site 184 184 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12009 UniProtKB Binding site 103 103 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03055,ECO:0000269|PubMed:18184583;Dbxref=PMID:18184583 +Q12009 UniProtKB Binding site 181 181 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03055,ECO:0000269|PubMed:18184583;Dbxref=PMID:18184583 +Q12009 UniProtKB Modified residue 7 7 . . . Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12009 UniProtKB Modified residue 59 59 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q12009 UniProtKB Helix 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +Q12009 UniProtKB Helix 73 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q12009 UniProtKB Helix 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +Q12009 UniProtKB Helix 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +Q12009 UniProtKB Turn 88 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q12009 UniProtKB Beta strand 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q12009 UniProtKB Beta strand 97 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +Q12009 UniProtKB Helix 108 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +Q12009 UniProtKB Beta strand 120 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +Q12009 UniProtKB Helix 129 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +Q12009 UniProtKB Beta strand 147 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDU +Q12009 UniProtKB Turn 151 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +Q12009 UniProtKB Beta strand 155 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +Q12009 UniProtKB Helix 166 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +Q12009 UniProtKB Beta strand 175 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +Q12009 UniProtKB Helix 199 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +Q12009 UniProtKB Beta strand 209 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +Q12009 UniProtKB Helix 222 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +Q12009 UniProtKB Beta strand 238 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +Q12009 UniProtKB Helix 243 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +Q12009 UniProtKB Helix 250 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +Q12009 UniProtKB Helix 260 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +Q12009 UniProtKB Beta strand 273 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VDV +##sequence-region P00912 1 224 +P00912 UniProtKB Chain 1 224 . . . ID=PRO_0000154337;Note=N-(5'-phosphoribosyl)anthranilate isomerase +P00912 UniProtKB Natural variant 48 48 . . . Note=In strain: CLIB 556 haplotype Ha2 and CLIB 630 haplotype Ha2. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P00912 UniProtKB Natural variant 172 172 . . . Note=In strain: CLIB 556 haplotype Ha1. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P00912 UniProtKB Natural variant 212 212 . . . Note=In strain: CLIB 95%2C CLIB 382%2C CLIB 388%2C CLIB 556 haplotype Ha2%2C CLIB 630%2C K1%2C R12%2C R13%2C YIIc12 haplotype Ha2 and YIIc17 haplotype Ha1. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +##sequence-region Q03860 1 143 +Q03860 UniProtKB Chain 1 143 . . . ID=PRO_0000240392;Note=Golgi apparatus membrane protein TVP15 +Q03860 UniProtKB Topological domain 1 10 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03860 UniProtKB Transmembrane 11 31 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03860 UniProtKB Topological domain 32 35 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03860 UniProtKB Transmembrane 36 56 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03860 UniProtKB Topological domain 57 67 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03860 UniProtKB Transmembrane 68 88 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03860 UniProtKB Topological domain 89 89 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03860 UniProtKB Transmembrane 90 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03860 UniProtKB Topological domain 111 143 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03860 UniProtKB Compositional bias 133 141 . . . Note=Poly-Asp +##sequence-region P53250 1 332 +P53250 UniProtKB Chain 1 332 . . . ID=PRO_0000214953;Note=Twinfilin-1 +P53250 UniProtKB Domain 5 132 . . . Note=ADF-H 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00599 +P53250 UniProtKB Domain 173 300 . . . Note=ADF-H 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00599 +P53250 UniProtKB Modified residue 167 167 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53250 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P00899 1 507 +P00899 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7483834;Dbxref=PMID:7483834 +P00899 UniProtKB Chain 2 507 . . . ID=PRO_0000154134;Note=Anthranilate synthase component 1 +P00899 UniProtKB Region 280 282 . . . Note=Tryptophan binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00897 +P00899 UniProtKB Region 316 317 . . . Note=Chorismate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00897 +P00899 UniProtKB Region 466 468 . . . Note=Chorismate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00897 +P00899 UniProtKB Metal binding 343 343 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00897 +P00899 UniProtKB Metal binding 481 481 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00897 +P00899 UniProtKB Binding site 65 65 . . . Note=Tryptophan;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00897 +P00899 UniProtKB Binding site 431 431 . . . Note=Chorismate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00897 +P00899 UniProtKB Binding site 452 452 . . . Note=Chorismate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00897 +P00899 UniProtKB Binding site 468 468 . . . Note=Chorismate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00897 +P00899 UniProtKB Modified residue 81 81 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P00899 UniProtKB Modified residue 223 223 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P00899 UniProtKB Sequence conflict 204 212 . . . Note=TDDSSPIPY->DRRFLANTI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00899 UniProtKB Sequence conflict 220 220 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00899 UniProtKB Sequence conflict 223 238 . . . Note=TFESNVGKEGYENHVS->LLNRMWARKVTKITSP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00899 UniProtKB Sequence conflict 262 268 . . . Note=TSLHPFN->SRYILSIFTD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00899 UniProtKB Sequence conflict 276 276 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00899 UniProtKB Sequence conflict 323 323 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00899 UniProtKB Sequence conflict 330 330 . . . Note=L->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00899 UniProtKB Sequence conflict 401 402 . . . Note=SI->TN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00899 UniProtKB Sequence conflict 461 507 . . . Note=AYLQAGGGIVYDSDEYDEYVETMNKMMANHSTIVQAEELWADIVGSA->LTCKLAVVLFTIQLSTMNMLETMNNDGQSQYYCASRRIVGRYRRISLKRAFSVFFPLDDIFIVFE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P00937 1 484 +P00937 UniProtKB Chain 1 484 . . . ID=PRO_0000056866;Note=Multifunctional tryptophan biosynthesis protein +P00937 UniProtKB Domain 13 207 . . . Note=Glutamine amidotransferase type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +P00937 UniProtKB Region 64 66 . . . Note=Glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00900 +P00937 UniProtKB Region 142 143 . . . Note=Glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00900 +P00937 UniProtKB Region 215 484 . . . Note=Indole-3-glycerol phosphate synthase +P00937 UniProtKB Active site 92 92 . . . Note=Nucleophile%3B for GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +P00937 UniProtKB Active site 181 181 . . . Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +P00937 UniProtKB Active site 183 183 . . . Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +P00937 UniProtKB Binding site 96 96 . . . Note=Glutamine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00900 +P00937 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P00937 UniProtKB Sequence conflict 32 32 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00937 UniProtKB Sequence conflict 63 65 . . . Note=PGP->LGL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00937 UniProtKB Sequence conflict 129 129 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00937 UniProtKB Sequence conflict 170 170 . . . Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00937 UniProtKB Sequence conflict 236 236 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P00931 1 707 +P00931 UniProtKB Chain 1 707 . . . ID=PRO_0000098726;Note=Tryptophan synthase +P00931 UniProtKB Region 1 297 . . . Note=Tryptophan synthase alpha chain +P00931 UniProtKB Region 298 707 . . . Note=Tryptophan synthase beta chain +P00931 UniProtKB Active site 50 50 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00931 UniProtKB Active site 61 61 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00931 UniProtKB Modified residue 384 384 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00931 UniProtKB Modified residue 540 540 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P00931 UniProtKB Modified residue 683 683 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q3E790 1 80 +Q3E790 UniProtKB Chain 1 80 . . . ID=PRO_0000076358;Note=Serine palmitoyltransferase-regulating protein TSC3 +Q3E790 UniProtKB Transmembrane 54 74 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04767 1 167 +Q04767 UniProtKB Chain 1 167 . . . ID=PRO_0000203281;Note=Golgi apparatus membrane protein TVP18 +Q04767 UniProtKB Transmembrane 23 43 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04767 UniProtKB Transmembrane 49 69 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04767 UniProtKB Transmembrane 98 114 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04767 UniProtKB Transmembrane 121 137 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04767 UniProtKB Modified residue 146 146 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04767 UniProtKB Modified residue 153 153 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q04767 UniProtKB Glycosylation 22 22 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q99394 1 268 +Q99394 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q99394 UniProtKB Chain 2 268 . . . ID=PRO_0000211589;Note=Trafficking protein particle complex subunit 33 +Q99394 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region Q04120 1 196 +Q04120 UniProtKB Chain 1 196 . . . ID=PRO_0000135096;Note=Peroxiredoxin TSA2 +Q04120 UniProtKB Domain 3 161 . . . Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +Q04120 UniProtKB Active site 48 48 . . . Note=Cysteine sulfenic acid (-SOH) intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26894543;Dbxref=PMID:26894543 +Q04120 UniProtKB Modified residue 174 174 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P34760 +Q04120 UniProtKB Disulfide bond 48 48 . . . Note=Interchain (with C-171)%3B in linked form;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:5EPT,ECO:0000269|PubMed:26894543;Dbxref=PMID:26894543 +Q04120 UniProtKB Disulfide bond 171 171 . . . Note=Interchain (with C-48)%3B in linked form;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:5EPT,ECO:0000269|PubMed:26894543;Dbxref=PMID:26894543 +Q04120 UniProtKB Cross-link 14 14 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P34760 +Q04120 UniProtKB Cross-link 89 89 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P34760 +Q04120 UniProtKB Cross-link 132 132 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P34760 +Q04120 UniProtKB Mutagenesis 48 48 . . . Note=No activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10681558;Dbxref=PMID:10681558 +Q04120 UniProtKB Beta strand 13 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB +Q04120 UniProtKB Beta strand 21 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB +Q04120 UniProtKB Helix 28 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB +Q04120 UniProtKB Beta strand 33 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB +Q04120 UniProtKB Beta strand 45 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB +Q04120 UniProtKB Helix 48 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB +Q04120 UniProtKB Helix 59 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB +Q04120 UniProtKB Beta strand 67 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB +Q04120 UniProtKB Helix 77 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB +Q04120 UniProtKB Turn 88 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB +Q04120 UniProtKB Beta strand 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB +Q04120 UniProtKB Helix 107 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB +Q04120 UniProtKB Turn 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB +Q04120 UniProtKB Beta strand 124 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB +Q04120 UniProtKB Beta strand 133 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB +Q04120 UniProtKB Helix 149 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB +Q04120 UniProtKB Turn 184 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB +Q04120 UniProtKB Helix 187 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DVB +##sequence-region Q06672 1 205 +Q06672 UniProtKB Chain 1 205 . . . ID=PRO_0000076359;Note=Pre-rRNA-processing protein TSR2 +Q06672 UniProtKB Compositional bias 153 179 . . . Note=Asp-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36097 1 1038 +P36097 UniProtKB Chain 1 1038 . . . ID=PRO_0000203185;Note=TEL2-interacting protein 1 +P36097 UniProtKB Modified residue 817 817 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P16649 1 713 +P16649 UniProtKB Chain 1 713 . . . ID=PRO_0000051312;Note=General transcriptional corepressor TUP1 +P16649 UniProtKB Repeat 342 371 . . . Note=WD 1 +P16649 UniProtKB Repeat 441 471 . . . Note=WD 2 +P16649 UniProtKB Repeat 483 513 . . . Note=WD 3 +P16649 UniProtKB Repeat 524 555 . . . Note=WD 4 +P16649 UniProtKB Repeat 574 604 . . . Note=WD 5 +P16649 UniProtKB Repeat 628 658 . . . Note=WD 6 +P16649 UniProtKB Repeat 670 706 . . . Note=WD 7 +P16649 UniProtKB Compositional bias 97 118 . . . Note=Gln-rich +P16649 UniProtKB Compositional bias 181 198 . . . Note=Poly-Gln +P16649 UniProtKB Compositional bias 399 409 . . . Note=Thr-rich +P16649 UniProtKB Modified residue 439 439 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P16649 UniProtKB Sequence conflict 75 75 . . . Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16649 UniProtKB Sequence conflict 100 100 . . . Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16649 UniProtKB Sequence conflict 685 685 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16649 UniProtKB Sequence conflict 685 685 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16649 UniProtKB Turn 19 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP9 +P16649 UniProtKB Helix 27 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP9 +P16649 UniProtKB Beta strand 290 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Helix 300 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 307 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 314 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 322 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 333 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 349 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 356 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 367 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Turn 372 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 377 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 445 451 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 455 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 467 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Turn 472 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 476 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 488 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 497 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 507 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Turn 514 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 518 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 529 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 541 546 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 551 555 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Turn 556 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 561 565 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 579 584 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 588 595 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 598 604 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 622 627 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 633 638 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Helix 640 642 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 644 649 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 652 658 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Turn 659 661 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 664 669 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 675 680 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 691 697 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +P16649 UniProtKB Beta strand 700 709 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ERJ +##sequence-region P32356 1 751 +P32356 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32356 UniProtKB Chain 2 751 . . . ID=PRO_0000173798;Note=Neutral trehalase +P32356 UniProtKB Region 309 310 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32356 UniProtKB Region 355 357 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32356 UniProtKB Active site 478 478 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32356 UniProtKB Active site 674 674 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32356 UniProtKB Binding site 302 302 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32356 UniProtKB Binding site 346 346 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32356 UniProtKB Binding site 355 355 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32356 UniProtKB Binding site 476 476 . . . Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32356 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32356 UniProtKB Modified residue 20 20 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32356 UniProtKB Modified residue 21 21 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32356 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32356 UniProtKB Modified residue 58 58 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198 +P32356 UniProtKB Modified residue 60 60 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:19779198 +P32356 UniProtKB Modified residue 66 66 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +P32356 UniProtKB Modified residue 83 83 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +P32356 UniProtKB Sequence conflict 514 515 . . . Note=CD->NN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32356 UniProtKB Sequence conflict 712 712 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32356 UniProtKB Sequence conflict 712 712 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32356 UniProtKB Sequence conflict 723 724 . . . Note=HA->YE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32356 UniProtKB Sequence conflict 723 724 . . . Note=HA->YE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32356 UniProtKB Sequence conflict 727 728 . . . Note=AL->EI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32356 UniProtKB Sequence conflict 727 728 . . . Note=AL->EI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38816 1 342 +P38816 UniProtKB Transit peptide 1 23 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38816 UniProtKB Chain 24 342 . . . ID=PRO_0000030303;Note=Thioredoxin reductase 2%2C mitochondrial +P38816 UniProtKB Nucleotide binding 34 37 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509 +P38816 UniProtKB Nucleotide binding 56 68 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509 +P38816 UniProtKB Nucleotide binding 63 64 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509 +P38816 UniProtKB Nucleotide binding 311 320 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509 +P38816 UniProtKB Nucleotide binding 318 320 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509 +P38816 UniProtKB Binding site 68 68 . . . Note=FAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509 +P38816 UniProtKB Binding site 77 77 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509 +P38816 UniProtKB Binding site 110 110 . . . Note=FAD%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509 +P38816 UniProtKB Binding site 168 168 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509 +P38816 UniProtKB Binding site 311 311 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509 +P38816 UniProtKB Disulfide bond 165 168 . . . Note=Redox-active;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29509 +##sequence-region P53044 1 361 +P53044 UniProtKB Chain 1 361 . . . ID=PRO_0000194989;Note=Ubiquitin fusion degradation protein 1 +P53044 UniProtKB Region 27 28 . . . Note=Monoubiquitin-binding +P53044 UniProtKB Region 30 32 . . . Note=Monoubiquitin-binding +P53044 UniProtKB Region 99 101 . . . Note=Monoubiquitin-binding +P53044 UniProtKB Site 37 37 . . . Note=Monoubiquitin-binding +P53044 UniProtKB Site 39 39 . . . Note=Monoubiquitin-binding +P53044 UniProtKB Site 109 109 . . . Note=Monoubiquitin-binding +P53044 UniProtKB Modified residue 354 354 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53044 UniProtKB Mutagenesis 94 94 . . . Note=In UFD1-1%3B grows more slowly. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550 +P53044 UniProtKB Beta strand 19 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +P53044 UniProtKB Helix 30 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +P53044 UniProtKB Turn 35 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +P53044 UniProtKB Helix 40 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +P53044 UniProtKB Beta strand 45 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +P53044 UniProtKB Helix 52 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +P53044 UniProtKB Beta strand 69 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +P53044 UniProtKB Turn 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +P53044 UniProtKB Beta strand 79 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +P53044 UniProtKB Beta strand 93 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +P53044 UniProtKB Helix 98 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +P53044 UniProtKB Beta strand 111 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +P53044 UniProtKB Beta strand 123 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +P53044 UniProtKB Helix 131 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +P53044 UniProtKB Helix 140 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +P53044 UniProtKB Beta strand 154 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +P53044 UniProtKB Beta strand 167 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +P53044 UniProtKB Beta strand 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +P53044 UniProtKB Beta strand 192 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZC1 +##sequence-region P33202 1 1483 +P33202 UniProtKB Chain 1 1483 . . . ID=PRO_0000194998;Note=Ubiquitin fusion degradation protein 4 +P33202 UniProtKB Domain 1376 1483 . . . Note=HECT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00104 +P33202 UniProtKB Region 1007 1081 . . . Note=K-box +P33202 UniProtKB Compositional bias 898 901 . . . Note=Poly-Glu +P33202 UniProtKB Active site 1450 1450 . . . Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00104 +P33202 UniProtKB Modified residue 87 87 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33202 UniProtKB Cross-link 349 349 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P26370 1 528 +P26370 UniProtKB Chain 1 528 . . . ID=PRO_0000114986;Note=Transcriptional activator protein UGA3 +P26370 UniProtKB DNA binding 17 44 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P26370 UniProtKB Motif 55 62 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P26370 UniProtKB Mutagenesis 224 224 . . . Note=Constitutive activity%3B when associated with R-451. G->R +P26370 UniProtKB Mutagenesis 451 451 . . . Note=Loss of activity. Constitutive activity%3B when associated with R-224. G->R +##sequence-region P36137 1 443 +P36137 UniProtKB Signal peptide 1 27 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36137 UniProtKB Chain 28 443 . . . ID=PRO_0000203212;Note=Protein UIP5 +P36137 UniProtKB Topological domain 28 398 . . . Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36137 UniProtKB Transmembrane 399 420 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36137 UniProtKB Topological domain 421 443 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q02724 1 621 +Q02724 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q02724 UniProtKB Chain 2 621 . . . ID=PRO_0000101731;Note=Ubiquitin-like-specific protease 1 +Q02724 UniProtKB Region 432 621 . . . Note=Protease;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10882122;Dbxref=PMID:10882122 +Q02724 UniProtKB Active site 514 514 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10882122;Dbxref=PMID:10882122 +Q02724 UniProtKB Active site 531 531 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10882122;Dbxref=PMID:10882122 +Q02724 UniProtKB Active site 580 580 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10882122;Dbxref=PMID:10882122 +Q02724 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q02724 UniProtKB Modified residue 21 21 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q02724 UniProtKB Modified residue 25 25 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q02724 UniProtKB Modified residue 179 179 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +Q02724 UniProtKB Modified residue 264 264 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q02724 UniProtKB Helix 409 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Beta strand 426 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Beta strand 433 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Helix 437 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Helix 441 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Helix 451 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Beta strand 468 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Helix 474 482 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Helix 484 486 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Turn 487 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Helix 492 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Helix 498 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Beta strand 502 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Turn 511 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Beta strand 514 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Turn 522 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Beta strand 526 530 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Helix 539 555 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Beta strand 558 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Beta strand 565 569 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Beta strand 575 578 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Helix 580 592 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Helix 601 616 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +Q02724 UniProtKB Turn 617 620 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EUV +##sequence-region Q05776 1 175 +Q05776 UniProtKB Chain 1 175 . . . ID=PRO_0000271269;Note=Protein UPS1%2C mitochondrial +Q05776 UniProtKB Domain 2 172 . . . Note=PRELI/MSF1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00158 +Q05776 UniProtKB Region 1 80 . . . Note=Required for mitochondrial targeting;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16754953;Dbxref=PMID:16754953 +Q05776 UniProtKB Binding site 26 26 . . . Note=Phosphatidic acid;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513 +Q05776 UniProtKB Binding site 58 58 . . . Note=Phosphatidic acid;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513 +Q05776 UniProtKB Binding site 148 148 . . . Note=Phosphatidic acid;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601 +Q05776 UniProtKB Binding site 152 152 . . . Note=Phosphatidic acid;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26071601,ECO:0000269|PubMed:26235513;Dbxref=PMID:26071601,PMID:26235513 +Q05776 UniProtKB Mutagenesis 23 23 . . . Note=Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601 +Q05776 UniProtKB Mutagenesis 25 25 . . . Note=Nearly abolishes phosphatidic acid transfer activity. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513 +Q05776 UniProtKB Mutagenesis 25 25 . . . Note=No effect on phosphatidic acid transfer activity. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513 +Q05776 UniProtKB Mutagenesis 33 33 . . . Note=Failure to complement the mitochondrial defects of UPS1-deficient cells%3B when associated with E-58%3B E-61%3B E-148 and E-155. H->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601 +Q05776 UniProtKB Mutagenesis 42 42 . . . Note=Impairs interaction with MDM35. Reduces ability to complement the mitochondrial defects of UPS1-deficient cells. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601 +Q05776 UniProtKB Mutagenesis 50 50 . . . Note=Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601 +Q05776 UniProtKB Mutagenesis 54 54 . . . Note=Decreases phosphatidic acid transfer activity and impairs cardiolipin biosynthesis. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071602;Dbxref=PMID:26071602 +Q05776 UniProtKB Mutagenesis 58 58 . . . Note=Failure to complement the mitochondrial defects of UPS1-deficient cells%3B when associated with E-33%3B E-61%3B E-148 and E-155. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601 +Q05776 UniProtKB Mutagenesis 61 61 . . . Note=Failure to complement the mitochondrial defects of UPS1-deficient cells%3B when associated with E-33%3B E-58%3B E-148 and E-155. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601 +Q05776 UniProtKB Mutagenesis 61 61 . . . Note=Nearly abolishes phosphatidic acid transfer activity%3B when associated with E-155. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513 +Q05776 UniProtKB Mutagenesis 62 62 . . . Note=Decreases phosphatidic acid binding and impairs cardiolipin biosynthesis%3B when associated with A-65. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071602;Dbxref=PMID:26071602 +Q05776 UniProtKB Mutagenesis 65 65 . . . Note=Decreases phosphatidic acid binding and impairs cardiolipin biosynthesis%3B when associated with A-62. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071602;Dbxref=PMID:26071602 +Q05776 UniProtKB Mutagenesis 77 77 . . . Note=Impairs interaction with MDM35. Reduces ability to complement the mitochondrial defects of UPS1-deficient cells. W->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601 +Q05776 UniProtKB Mutagenesis 78 78 . . . Note=Failure to complement the mitochondrial defects of UPS1-deficient cells. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601 +Q05776 UniProtKB Mutagenesis 84 84 . . . Note=Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. V->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601 +Q05776 UniProtKB Mutagenesis 96 96 . . . Note=Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601 +Q05776 UniProtKB Mutagenesis 97 97 . . . Note=Failure to complement the mitochondrial defects of UPS1-deficient cells. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601 +Q05776 UniProtKB Mutagenesis 104 104 . . . Note=Failure to complement the mitochondrial defects of UPS1-deficient cells%3B when associated with E-144. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601 +Q05776 UniProtKB Mutagenesis 106 106 . . . Note=Failure to complement the mitochondrial defects of UPS1-deficient cells. V->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601 +Q05776 UniProtKB Mutagenesis 144 144 . . . Note=Failure to complement the mitochondrial defects of UPS1-deficient cells%3B when associated with E-104. W->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601 +Q05776 UniProtKB Mutagenesis 148 148 . . . Note=Failure to complement the mitochondrial defects of UPS1-deficient cells%3B when associated with E-33%3B E-58%3B E-61 and E-155. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601 +Q05776 UniProtKB Mutagenesis 155 155 . . . Note=Failure to complement the mitochondrial defects of UPS1-deficient cells%3B when associated with E-33%3B E-58%3B E-61 and E-148. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26071601;Dbxref=PMID:26071601 +Q05776 UniProtKB Mutagenesis 155 155 . . . Note=Nearly abolishes phosphatidic acid transfer activity%3B when associated with E-61. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513 +Q05776 UniProtKB Beta strand 2 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +Q05776 UniProtKB Helix 15 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +Q05776 UniProtKB Beta strand 34 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +Q05776 UniProtKB Beta strand 50 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +Q05776 UniProtKB Turn 64 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +Q05776 UniProtKB Beta strand 75 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +Q05776 UniProtKB Turn 86 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +Q05776 UniProtKB Beta strand 90 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +Q05776 UniProtKB Turn 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +Q05776 UniProtKB Beta strand 105 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +Q05776 UniProtKB Turn 116 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +Q05776 UniProtKB Beta strand 120 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +Q05776 UniProtKB Helix 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +Q05776 UniProtKB Helix 137 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +##sequence-region P28274 1 579 +P28274 UniProtKB Chain 1 579 . . . ID=PRO_0000138283;Note=CTP synthase 1 +P28274 UniProtKB Domain 305 559 . . . Note=Glutamine amidotransferase type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +P28274 UniProtKB Active site 404 404 . . . Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +P28274 UniProtKB Active site 535 535 . . . Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +P28274 UniProtKB Active site 537 537 . . . Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +P28274 UniProtKB Cross-link 422 422 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P28274 UniProtKB Sequence conflict 307 307 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28274 UniProtKB Sequence conflict 418 418 . . . Note=V->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38627 1 578 +P38627 UniProtKB Chain 1 578 . . . ID=PRO_0000138284;Note=CTP synthase 2 +P38627 UniProtKB Domain 305 564 . . . Note=Glutamine amidotransferase type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +P38627 UniProtKB Active site 404 404 . . . Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +P38627 UniProtKB Active site 537 537 . . . Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +P38627 UniProtKB Active site 539 539 . . . Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +P38627 UniProtKB Mutagenesis 161 161 . . . Note=Increases the specific activity 2-fold and decreases sensitivity to CTP product inhibition 5-fold. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9668079;Dbxref=PMID:9668079 +P38627 UniProtKB Mutagenesis 233 233 . . . Note=No effect on activity and product inhibition by CTP. H->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9668079;Dbxref=PMID:9668079 +P38627 UniProtKB Sequence conflict 96 97 . . . Note=HV->QL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38627 UniProtKB Sequence conflict 204 204 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38627 UniProtKB Sequence conflict 440 446 . . . Note=QVVIYMP->PSSHIHA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38627 UniProtKB Sequence conflict 557 563 . . . Note=AASGTLG->QLRHTC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q05946 1 817 +Q05946 UniProtKB Chain 1 817 . . . ID=PRO_0000051320;Note=U3 small nucleolar RNA-associated protein 13 +Q05946 UniProtKB Repeat 59 100 . . . Note=WD 1 +Q05946 UniProtKB Repeat 102 139 . . . Note=WD 2 +Q05946 UniProtKB Repeat 142 187 . . . Note=WD 3 +Q05946 UniProtKB Repeat 191 233 . . . Note=WD 4 +Q05946 UniProtKB Repeat 238 280 . . . Note=WD 5 +Q05946 UniProtKB Repeat 386 425 . . . Note=WD 6 +Q05946 UniProtKB Repeat 432 476 . . . Note=WD 7 +Q05946 UniProtKB Repeat 489 528 . . . Note=WD 8 +Q05946 UniProtKB Repeat 531 572 . . . Note=WD 9 +Q05946 UniProtKB Repeat 573 614 . . . Note=WD 10 +Q05946 UniProtKB Repeat 616 654 . . . Note=WD 11 +Q05946 UniProtKB Repeat 664 705 . . . Note=WD 12 +##sequence-region Q04305 1 513 +Q04305 UniProtKB Chain 1 513 . . . ID=PRO_0000051328;Note=U3 small nucleolar RNA-associated protein 15 +Q04305 UniProtKB Repeat 37 78 . . . Note=WD 1 +Q04305 UniProtKB Repeat 79 118 . . . Note=WD 2 +Q04305 UniProtKB Repeat 124 162 . . . Note=WD 3 +Q04305 UniProtKB Repeat 166 206 . . . Note=WD 4 +Q04305 UniProtKB Repeat 210 247 . . . Note=WD 5 +Q04305 UniProtKB Repeat 250 294 . . . Note=WD 6 +##sequence-region P40362 1 594 +P40362 UniProtKB Chain 1 594 . . . ID=PRO_0000051330;Note=U3 small nucleolar RNA-associated protein 18 +P40362 UniProtKB Repeat 246 285 . . . Note=WD 1 +P40362 UniProtKB Repeat 290 334 . . . Note=WD 2 +P40362 UniProtKB Repeat 463 504 . . . Note=WD 3 +P40362 UniProtKB Repeat 513 554 . . . Note=WD 4 +P40362 UniProtKB Repeat 560 593 . . . Note=WD 5 +P40362 UniProtKB Region 101 190 . . . Note=Interaction with UTP21;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140 +P40362 UniProtKB Modified residue 182 182 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40362 UniProtKB Modified residue 184 184 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P35194 1 2493 +P35194 UniProtKB Chain 1 2493 . . . ID=PRO_0000202465;Note=U3 small nucleolar RNA-associated protein 20 +P35194 UniProtKB Repeat 227 264 . . . Note=HEAT 1 +P35194 UniProtKB Repeat 495 532 . . . Note=HEAT 2 +P35194 UniProtKB Repeat 576 613 . . . Note=HEAT 3 +P35194 UniProtKB Repeat 845 882 . . . Note=HEAT 4 +P35194 UniProtKB Repeat 1176 1214 . . . Note=HEAT 5 +P35194 UniProtKB Repeat 1216 1252 . . . Note=HEAT 6 +P35194 UniProtKB Repeat 1342 1380 . . . Note=HEAT 7 +P35194 UniProtKB Repeat 1393 1430 . . . Note=HEAT 8 +P35194 UniProtKB Repeat 1480 1520 . . . Note=HEAT 9 +P35194 UniProtKB Repeat 1522 1558 . . . Note=HEAT 10 +P35194 UniProtKB Repeat 1588 1625 . . . Note=HEAT 11 +P35194 UniProtKB Repeat 1630 1667 . . . Note=HEAT 12 +P35194 UniProtKB Repeat 1890 1927 . . . Note=HEAT 13 +P35194 UniProtKB Repeat 1953 1992 . . . Note=HEAT 14 +P35194 UniProtKB Repeat 2120 2157 . . . Note=HEAT 15 +P35194 UniProtKB Repeat 2358 2397 . . . Note=HEAT 16 +P35194 UniProtKB Sequence conflict 2440 2440 . . . Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40498 1 721 +P40498 UniProtKB Chain 1 721 . . . ID=PRO_0000202974;Note=U3 small nucleolar RNA-associated protein 25 +P40498 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40498 UniProtKB Modified residue 63 63 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40498 UniProtKB Modified residue 196 196 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q02354 1 440 +Q02354 UniProtKB Chain 1 440 . . . ID=PRO_0000205765;Note=U3 small nucleolar RNA-associated protein 6 +Q02354 UniProtKB Repeat 87 119 . . . Note=HAT 1 +Q02354 UniProtKB Repeat 124 156 . . . Note=HAT 2 +Q02354 UniProtKB Repeat 159 191 . . . Note=HAT 3 +Q02354 UniProtKB Sequence conflict 138 140 . . . Note=KLH->SA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08474 1 114 +Q08474 UniProtKB Chain 1 114 . . . ID=PRO_0000065758;Note=Vacuolar morphogenesis protein 10 +##sequence-region P16140 1 517 +P16140 UniProtKB Chain 1 517 . . . ID=PRO_0000144648;Note=V-type proton ATPase subunit B +P16140 UniProtKB Modified residue 4 4 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:18407956 +P16140 UniProtKB Modified residue 137 137 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P16140 UniProtKB Modified residue 503 503 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P16140 UniProtKB Modified residue 504 504 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P16140 UniProtKB Modified residue 511 511 . . . Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P16140 UniProtKB Modified residue 515 515 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P16140 UniProtKB Cross-link 14 14 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P16140 UniProtKB Cross-link 508 508 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P16140 UniProtKB Sequence conflict 14 14 . . . Note=K->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16140 UniProtKB Sequence conflict 79 79 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16140 UniProtKB Sequence conflict 227 227 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16140 UniProtKB Sequence conflict 500 517 . . . Note=DTRSSGKKKDASQEESLI->TQEAPVRRRTPAKKNL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38358 1 474 +P38358 UniProtKB Chain 1 474 . . . ID=PRO_0000173423;Note=Vacuolar basic amino acid transporter 2 +P38358 UniProtKB Topological domain 1 33 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Transmembrane 34 54 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Topological domain 55 62 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Transmembrane 63 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Topological domain 86 97 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Transmembrane 98 118 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Topological domain 119 121 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Transmembrane 122 142 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Topological domain 143 167 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Transmembrane 168 188 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Topological domain 189 196 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Transmembrane 197 217 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Topological domain 218 238 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Transmembrane 239 259 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Topological domain 260 273 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Transmembrane 274 294 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Topological domain 295 303 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Transmembrane 304 324 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Topological domain 325 331 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Transmembrane 332 352 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Topological domain 353 375 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Transmembrane 376 396 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Topological domain 397 447 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Transmembrane 448 468 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Topological domain 469 474 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38358 UniProtKB Glycosylation 420 420 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04602 1 768 +Q04602 UniProtKB Chain 1 768 . . . ID=PRO_0000252272;Note=Vacuolar basic amino acid transporter 4 +Q04602 UniProtKB Topological domain 1 252 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Transmembrane 253 273 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Topological domain 274 282 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Transmembrane 283 305 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Topological domain 306 311 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Transmembrane 312 331 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Topological domain 332 334 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Transmembrane 335 357 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Topological domain 358 375 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Transmembrane 376 396 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Topological domain 397 406 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Transmembrane 407 427 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Topological domain 428 447 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Transmembrane 448 468 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Topological domain 469 481 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Transmembrane 482 502 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Topological domain 503 522 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Transmembrane 523 543 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Topological domain 544 562 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Transmembrane 563 583 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Topological domain 584 587 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Transmembrane 588 608 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Topological domain 609 617 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Transmembrane 618 638 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Topological domain 639 653 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Transmembrane 654 674 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Topological domain 675 734 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Transmembrane 735 755 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Topological domain 756 768 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Coiled coil 9 40 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Modified residue 62 62 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04602 UniProtKB Modified residue 99 99 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q04602 UniProtKB Modified residue 106 106 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q04602 UniProtKB Modified residue 160 160 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04602 UniProtKB Modified residue 192 192 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04602 UniProtKB Glycosylation 480 480 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04602 UniProtKB Glycosylation 553 553 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39538 1 1254 +P39538 UniProtKB Chain 1 1254 . . . ID=PRO_0000080597;Note=Ubiquitin carboxyl-terminal hydrolase 12 +P39538 UniProtKB Domain 97 199 . . . Note=DUSP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00613 +P39538 UniProtKB Domain 364 1110 . . . Note=USP +P39538 UniProtKB Active site 373 373 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +P39538 UniProtKB Active site 1068 1068 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +P39538 UniProtKB Modified residue 84 84 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39538 UniProtKB Modified residue 1160 1160 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q01477 1 912 +Q01477 UniProtKB Chain 1 912 . . . ID=PRO_0000080588;Note=Ubiquitin carboxyl-terminal hydrolase 3 +Q01477 UniProtKB Domain 460 911 . . . Note=USP +Q01477 UniProtKB Active site 469 469 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +Q01477 UniProtKB Active site 861 861 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +Q01477 UniProtKB Beta strand 208 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY +Q01477 UniProtKB Helix 214 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY +##sequence-region P39967 1 754 +P39967 UniProtKB Chain 1 754 . . . ID=PRO_0000080594;Note=Ubiquitin carboxyl-terminal hydrolase 9 +P39967 UniProtKB Domain 134 667 . . . Note=USP +P39967 UniProtKB Active site 143 143 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +P39967 UniProtKB Active site 618 618 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +##sequence-region Q12229 1 455 +Q12229 UniProtKB Chain 1 455 . . . ID=PRO_0000211000;Note=UBX domain-containing protein 3 +Q12229 UniProtKB Domain 356 455 . . . Note=UBX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00215 +##sequence-region P47049 1 396 +P47049 UniProtKB Chain 1 396 . . . ID=PRO_0000211003;Note=UBX domain-containing protein 6 +P47049 UniProtKB Domain 186 264 . . . Note=UBX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00215 +P47049 UniProtKB Modified residue 369 369 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40554 1 99 +P40554 UniProtKB Chain 1 99 . . . ID=PRO_0000203002;Note=Ubiquitin-related modifier 1 +P40554 UniProtKB Modified residue 99 99 . . . Note=1-thioglycine;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03048,ECO:0000269|PubMed:18491921,ECO:0000269|PubMed:19145231,ECO:0000269|PubMed:19151091;Dbxref=PMID:18491921,PMID:19145231,PMID:19151091 +P40554 UniProtKB Cross-link 99 99 . . . Note=Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03048 +P40554 UniProtKB Mutagenesis 98 99 . . . Note=Abolishes thiocarboxylation and function in 2-Thiolation of tRNA. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19151091;Dbxref=PMID:19151091 +P40554 UniProtKB Mutagenesis 99 99 . . . Note=Abolishes URM1 conjugate formation. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10713047;Dbxref=PMID:10713047 +P40554 UniProtKB Beta strand 2 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL +P40554 UniProtKB Helix 12 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL +P40554 UniProtKB Turn 16 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL +P40554 UniProtKB Beta strand 21 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL +P40554 UniProtKB Helix 34 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL +P40554 UniProtKB Helix 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL +P40554 UniProtKB Helix 52 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL +P40554 UniProtKB Beta strand 56 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PKO +P40554 UniProtKB Beta strand 65 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL +P40554 UniProtKB Helix 74 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL +P40554 UniProtKB Helix 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL +P40554 UniProtKB Beta strand 89 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJL +##sequence-region Q04500 1 899 +Q04500 UniProtKB Chain 1 899 . . . ID=PRO_0000065742;Note=U3 small nucleolar RNA-associated protein 14 +Q04500 UniProtKB Nucleotide binding 260 267 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04500 UniProtKB Compositional bias 162 168 . . . Note=Poly-Ser +Q04500 UniProtKB Compositional bias 179 182 . . . Note=Poly-Glu +Q04500 UniProtKB Compositional bias 704 712 . . . Note=Poly-Lys +Q04500 UniProtKB Modified residue 34 34 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q04500 UniProtKB Modified residue 35 35 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04500 UniProtKB Modified residue 151 151 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q04500 UniProtKB Modified residue 423 423 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q04500 UniProtKB Modified residue 424 424 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04500 UniProtKB Modified residue 488 488 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q04500 UniProtKB Modified residue 500 500 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q04500 UniProtKB Modified residue 562 562 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q04500 UniProtKB Modified residue 668 668 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +Q04500 UniProtKB Modified residue 738 738 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region Q12339 1 254 +Q12339 UniProtKB Chain 1 254 . . . ID=PRO_0000245250;Note=rRNA-processing protein UTP23 +Q12339 UniProtKB Compositional bias 188 239 . . . Note=Lys-rich +Q12339 UniProtKB Modified residue 182 182 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12339 UniProtKB Helix 4 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7 +Q12339 UniProtKB Beta strand 24 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7 +Q12339 UniProtKB Helix 32 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7 +Q12339 UniProtKB Helix 45 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7 +Q12339 UniProtKB Beta strand 57 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7 +Q12339 UniProtKB Helix 63 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7 +Q12339 UniProtKB Helix 75 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7 +Q12339 UniProtKB Beta strand 84 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7 +Q12339 UniProtKB Beta strand 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7 +Q12339 UniProtKB Helix 99 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7 +Q12339 UniProtKB Beta strand 117 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7 +Q12339 UniProtKB Helix 124 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7 +Q12339 UniProtKB Beta strand 138 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7 +Q12339 UniProtKB Beta strand 145 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7 +Q12339 UniProtKB Helix 153 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MJ7 +##sequence-region P43123 1 477 +P43123 UniProtKB Chain 1 477 . . . ID=PRO_0000185773;Note=UDP-N-acetylglucosamine pyrophosphorylase +P43123 UniProtKB Region 109 112 . . . Note=UTP binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3 +P43123 UniProtKB Motif 109 112 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43123 UniProtKB Motif 302 303 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43123 UniProtKB Binding site 123 123 . . . Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3 +P43123 UniProtKB Binding site 194 194 . . . Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3 +P43123 UniProtKB Binding site 221 221 . . . Note=UTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3 +P43123 UniProtKB Binding site 222 222 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43123 UniProtKB Binding site 252 252 . . . Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3 +P43123 UniProtKB Binding site 377 377 . . . Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3 +P43123 UniProtKB Binding site 409 409 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43123 UniProtKB Modified residue 218 218 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43123 UniProtKB Modified residue 461 461 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P43123 UniProtKB Mutagenesis 111 111 . . . Note=Decrease of activity. G->A +P43123 UniProtKB Mutagenesis 112 112 . . . Note=Loss of activity. G->A +P43123 UniProtKB Mutagenesis 114 114 . . . Note=Decrease of activity. G->A +P43123 UniProtKB Mutagenesis 115 115 . . . Note=Decrease of activity. T->A +P43123 UniProtKB Mutagenesis 116 116 . . . Note=Loss of activity. R->A +P43123 UniProtKB Mutagenesis 117 117 . . . Note=Decrease of activity. L->A +P43123 UniProtKB Mutagenesis 122 122 . . . Note=Decrease of activity. P->A +P43123 UniProtKB Mutagenesis 123 123 . . . Note=Loss of activity. K->A +##sequence-region P52490 1 153 +P52490 UniProtKB Chain 1 153 . . . ID=PRO_0000082565;Note=Ubiquitin-conjugating enzyme E2 13 +P52490 UniProtKB Active site 87 87 . . . Note=Glycyl thioester intermediate +P52490 UniProtKB Cross-link 92 92 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P52490 UniProtKB Mutagenesis 55 55 . . . Note=Strongly reduces MMS2 binding and interferes with error-free DNA repair. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11440714;Dbxref=PMID:11440714 +P52490 UniProtKB Mutagenesis 81 81 . . . Note=Abolishes ubiquitin chain elongation. No effect on thioester formation at the active site. D->R +P52490 UniProtKB Mutagenesis 110 110 . . . Note=Lowers rate of ubiquitin chain elongation. No effect on thioester formation at the active site. A->R +P52490 UniProtKB Helix 6 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P52490 UniProtKB Beta strand 23 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P52490 UniProtKB Beta strand 31 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P52490 UniProtKB Turn 46 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P52490 UniProtKB Beta strand 50 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P52490 UniProtKB Turn 60 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P52490 UniProtKB Beta strand 68 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P52490 UniProtKB Helix 89 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P52490 UniProtKB Turn 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P52490 UniProtKB Helix 101 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P52490 UniProtKB Helix 126 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P52490 UniProtKB Helix 133 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P52490 UniProtKB Beta strand 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +##sequence-region Q02159 1 165 +Q02159 UniProtKB Chain 1 165 . . . ID=PRO_0000082554;Note=Ubiquitin-conjugating enzyme E2 7 +Q02159 UniProtKB Active site 89 89 . . . Note=Glycyl thioester intermediate +Q02159 UniProtKB Cross-link 89 89 . . . Note=Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17310239;Dbxref=PMID:17310239 +Q02159 UniProtKB Mutagenesis 39 39 . . . Note=No effect%3B when associated with S-141. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17310239;Dbxref=PMID:17310239 +Q02159 UniProtKB Mutagenesis 81 81 . . . Note=Impairs degradation of UBC7-substrates%2C but does not prevent protein degradation. N->A +Q02159 UniProtKB Mutagenesis 89 89 . . . Note=Prevents polyubiquitin chain attachment and protein degradation. C->A%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17310239;Dbxref=PMID:17310239 +Q02159 UniProtKB Mutagenesis 141 141 . . . Note=No effect%3B when associated with S-39. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17310239;Dbxref=PMID:17310239 +Q02159 UniProtKB Helix 2 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU +Q02159 UniProtKB Beta strand 24 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU +Q02159 UniProtKB Beta strand 33 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU +Q02159 UniProtKB Turn 48 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU +Q02159 UniProtKB Beta strand 53 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU +Q02159 UniProtKB Turn 62 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU +Q02159 UniProtKB Beta strand 70 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU +Q02159 UniProtKB Beta strand 86 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU +Q02159 UniProtKB Helix 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU +Q02159 UniProtKB Beta strand 102 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UCZ +Q02159 UniProtKB Turn 105 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UCZ +Q02159 UniProtKB Helix 116 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU +Q02159 UniProtKB Helix 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU +Q02159 UniProtKB Helix 138 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU +Q02159 UniProtKB Helix 148 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU +##sequence-region Q12059 1 462 +Q12059 UniProtKB Chain 1 462 . . . ID=PRO_0000194962;Note=NEDD8-activating enzyme E1 regulatory subunit +##sequence-region Q08562 1 1619 +Q08562 UniProtKB Chain 1 1619 . . . ID=PRO_0000268702;Note=ATP-dependent helicase ULS1 +Q08562 UniProtKB Domain 956 1157 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q08562 UniProtKB Domain 1447 1606 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q08562 UniProtKB Nucleotide binding 969 976 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q08562 UniProtKB Zinc finger 1330 1386 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +Q08562 UniProtKB Motif 7 10 . . . Note=SUMO interacting motif%3B type a 1 +Q08562 UniProtKB Motif 371 378 . . . Note=SUMO interacting motif%3B type b 1 +Q08562 UniProtKB Motif 470 473 . . . Note=SUMO interacting motif%3B type a 2 +Q08562 UniProtKB Motif 543 550 . . . Note=SUMO interacting motif%3B type b 2 +Q08562 UniProtKB Modified residue 121 121 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q03010 1 460 +Q03010 UniProtKB Chain 1 460 . . . ID=PRO_0000051315;Note=Transcriptional regulatory protein UME1 +Q03010 UniProtKB Repeat 233 271 . . . Note=WD 1 +Q03010 UniProtKB Repeat 276 316 . . . Note=WD 2 +Q03010 UniProtKB Repeat 339 379 . . . Note=WD 3 +Q03010 UniProtKB Repeat 411 451 . . . Note=WD 4 +Q03010 UniProtKB Motif 14 22 . . . Note=NEE-box +##sequence-region P25386 1 1790 +P25386 UniProtKB Chain 1 1790 . . . ID=PRO_0000065730;Note=Intracellular protein transport protein USO1 +P25386 UniProtKB Repeat 45 89 . . . Note=ARM 1 +P25386 UniProtKB Repeat 127 170 . . . Note=ARM 2 +P25386 UniProtKB Repeat 173 213 . . . Note=ARM 3 +P25386 UniProtKB Repeat 215 260 . . . Note=ARM 4 +P25386 UniProtKB Repeat 261 312 . . . Note=ARM 5 +P25386 UniProtKB Repeat 314 362 . . . Note=ARM 6 +P25386 UniProtKB Repeat 363 429 . . . Note=ARM 7 +P25386 UniProtKB Repeat 431 512 . . . Note=ARM 8 +P25386 UniProtKB Repeat 543 584 . . . Note=ARM 9 +P25386 UniProtKB Repeat 586 630 . . . Note=ARM 10 +P25386 UniProtKB Region 1 724 . . . Note=Globular head +P25386 UniProtKB Region 465 487 . . . Note=Charged (hyper-hydrophilic) +P25386 UniProtKB Region 991 1790 . . . Note=Dispensable for the protein function +P25386 UniProtKB Coiled coil 725 1790 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25386 UniProtKB Compositional bias 1172 1786 . . . Note=Asp/Glu-rich (acidic) +P25386 UniProtKB Modified residue 1770 1770 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25386 UniProtKB Sequence conflict 390 391 . . . Note=NG->TA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25386 UniProtKB Sequence conflict 725 725 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25386 UniProtKB Sequence conflict 847 847 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25386 UniProtKB Sequence conflict 924 924 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25386 UniProtKB Sequence conflict 1253 1253 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25386 UniProtKB Sequence conflict 1319 1319 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25386 UniProtKB Sequence conflict 1461 1461 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25386 UniProtKB Sequence conflict 1581 1581 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25386 UniProtKB Sequence conflict 1600 1600 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25386 UniProtKB Sequence conflict 1661 1661 . . . Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25386 UniProtKB Sequence conflict 1772 1772 . . . Note=D->DEEDDEE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P42945 1 1769 +P42945 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P42945 UniProtKB Chain 2 1769 . . . ID=PRO_0000186207;Note=U3 small nucleolar RNA-associated protein 10 +P42945 UniProtKB Repeat 1729 1767 . . . Note=HEAT +P42945 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region Q06078 1 939 +Q06078 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q06078 UniProtKB Chain 2 939 . . . ID=PRO_0000051480;Note=U3 small nucleolar RNA-associated protein 21 +Q06078 UniProtKB Repeat 40 71 . . . Note=WD 1;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140 +Q06078 UniProtKB Repeat 81 111 . . . Note=WD 2;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140 +Q06078 UniProtKB Repeat 119 158 . . . Note=WD 3;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140 +Q06078 UniProtKB Repeat 168 201 . . . Note=WD 4;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140 +Q06078 UniProtKB Repeat 208 245 . . . Note=WD 5;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140 +Q06078 UniProtKB Repeat 252 287 . . . Note=WD 6;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140 +Q06078 UniProtKB Repeat 295 347 . . . Note=WD 7;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140 +Q06078 UniProtKB Repeat 354 388 . . . Note=WD 8;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140 +Q06078 UniProtKB Repeat 415 454 . . . Note=WD 9;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140 +Q06078 UniProtKB Repeat 463 497 . . . Note=WD 10;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140 +Q06078 UniProtKB Repeat 505 541 . . . Note=WD 11;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140 +Q06078 UniProtKB Repeat 546 581 . . . Note=WD 12;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140 +Q06078 UniProtKB Repeat 583 624 . . . Note=WD 13;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140 +Q06078 UniProtKB Repeat 626 664 . . . Note=WD 14;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:24466140;Dbxref=PMID:24466140 +Q06078 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q06078 UniProtKB Modified residue 772 772 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06078 UniProtKB Beta strand 22 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 40 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 47 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 58 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Turn 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 68 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 82 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 89 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 97 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 105 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 113 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 118 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 127 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 135 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 147 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 152 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Turn 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 165 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 179 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 188 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Turn 193 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 198 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 209 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 220 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Turn 235 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 239 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 251 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 259 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 263 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 273 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Turn 278 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 282 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Helix 293 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 299 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 307 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 315 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 341 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 353 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 365 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 375 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 386 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 414 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Turn 422 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 430 434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 438 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Turn 445 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 449 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 458 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 463 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 474 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 482 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Turn 489 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 494 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 505 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 516 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 524 533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 536 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 546 551 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Turn 553 555 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 557 562 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 567 571 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Turn 572 575 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 576 581 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 588 593 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 597 604 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 607 613 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Turn 614 616 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 619 624 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 629 634 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 640 647 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +Q06078 UniProtKB Beta strand 649 656 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NSX +##sequence-region P53254 1 1237 +P53254 UniProtKB Chain 1 1237 . . . ID=PRO_0000215651;Note=U3 small nucleolar RNA-associated protein 22 +P53254 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P53254 UniProtKB Modified residue 58 58 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53254 UniProtKB Modified residue 60 60 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53254 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53254 UniProtKB Helix 82 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 118 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 146 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 169 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 182 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 187 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 201 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 211 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Turn 216 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 223 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 248 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 252 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 259 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 266 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 286 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 290 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 305 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 330 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 342 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 359 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Turn 381 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 390 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 402 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 410 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 418 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 435 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 439 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 455 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 467 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Turn 470 472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Turn 476 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 482 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 502 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 507 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 519 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 523 530 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 536 538 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 539 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 549 555 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 558 574 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 575 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 578 586 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 596 598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 603 605 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 606 609 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 611 619 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Turn 621 625 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 627 633 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 640 649 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 650 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 653 657 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 663 668 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 673 675 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 677 689 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 695 697 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 699 706 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 711 713 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 716 718 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 725 742 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 750 755 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 758 761 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 779 786 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 796 817 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 821 827 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 838 843 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 849 855 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 859 869 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Turn 872 874 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 875 889 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 892 903 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 909 922 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Turn 926 928 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 931 943 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 954 967 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Turn 970 972 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 1014 1030 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 1034 1036 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Turn 1051 1055 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 1058 1078 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 1082 1088 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 1097 1103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Turn 1109 1113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 1136 1142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 1145 1157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Turn 1158 1160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 1161 1165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 1169 1172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Turn 1174 1177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 1179 1186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 1188 1190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 1204 1214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 1216 1227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Helix 1228 1230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P53254 UniProtKB Beta strand 1231 1236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +##sequence-region Q04177 1 643 +Q04177 UniProtKB Chain 1 643 . . . ID=PRO_0000051318;Note=U3 small nucleolar RNA-associated protein 5 +Q04177 UniProtKB Repeat 14 54 . . . Note=WD 1 +Q04177 UniProtKB Repeat 55 98 . . . Note=WD 2 +Q04177 UniProtKB Repeat 186 225 . . . Note=WD 3 +Q04177 UniProtKB Repeat 227 266 . . . Note=WD 4 +Q04177 UniProtKB Repeat 340 389 . . . Note=WD 5 +Q04177 UniProtKB Repeat 471 511 . . . Note=WD 6 +Q04177 UniProtKB Compositional bias 568 643 . . . Note=Glu-rich +##sequence-region P53276 1 713 +P53276 UniProtKB Chain 1 713 . . . ID=PRO_0000065743;Note=U3 small nucleolar RNA-associated protein 8 +P53276 UniProtKB Modified residue 95 95 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53276 UniProtKB Modified residue 148 148 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53276 UniProtKB Modified residue 150 150 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P21373 1 530 +P21373 UniProtKB Chain 1 530 . . . ID=PRO_0000120716;Note=NAD(+) kinase +P21373 UniProtKB Modified residue 499 499 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P21373 UniProtKB Modified residue 503 503 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P21373 UniProtKB Sequence conflict 337 337 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P35127 1 236 +P35127 UniProtKB Chain 1 236 . . . ID=PRO_0000211073;Note=Ubiquitin carboxyl-terminal hydrolase YUH1 +P35127 UniProtKB Region 10 15 . . . Note=Interaction with ubiquitin +P35127 UniProtKB Region 149 157 . . . Note=Interaction with ubiquitin +P35127 UniProtKB Region 219 228 . . . Note=Interaction with ubiquitin +P35127 UniProtKB Active site 90 90 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10091 +P35127 UniProtKB Active site 166 166 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10091 +P35127 UniProtKB Site 84 84 . . . Note=Transition state stabilizer +P35127 UniProtKB Site 181 181 . . . Note=Important for enzyme activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35127 UniProtKB Helix 15 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX +P35127 UniProtKB Beta strand 31 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX +P35127 UniProtKB Helix 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX +P35127 UniProtKB Beta strand 54 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX +P35127 UniProtKB Helix 90 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX +P35127 UniProtKB Helix 103 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX +P35127 UniProtKB Helix 111 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX +P35127 UniProtKB Beta strand 126 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX +P35127 UniProtKB Helix 132 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX +P35127 UniProtKB Helix 146 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX +P35127 UniProtKB Beta strand 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX +P35127 UniProtKB Beta strand 164 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX +P35127 UniProtKB Beta strand 174 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX +P35127 UniProtKB Beta strand 189 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX +P35127 UniProtKB Helix 201 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX +P35127 UniProtKB Helix 205 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX +P35127 UniProtKB Beta strand 227 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMX +##sequence-region Q01476 1 1272 +Q01476 UniProtKB Chain 1 1272 . . . ID=PRO_0000080586;Note=Ubiquitin carboxyl-terminal hydrolase 2 +Q01476 UniProtKB Domain 736 1258 . . . Note=USP +Q01476 UniProtKB Active site 745 745 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +Q01476 UniProtKB Active site 1209 1209 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +Q01476 UniProtKB Modified residue 907 907 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q01476 UniProtKB Sequence conflict 658 665 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P43593 1 499 +P43593 UniProtKB Chain 1 499 . . . ID=PRO_0000080591;Note=Ubiquitin carboxyl-terminal hydrolase 6 +P43593 UniProtKB Domain 6 80 . . . Note=Ubiquitin-like +P43593 UniProtKB Domain 109 497 . . . Note=USP +P43593 UniProtKB Active site 118 118 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +P43593 UniProtKB Active site 447 447 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +P43593 UniProtKB Modified residue 389 389 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P43593 UniProtKB Modified residue 470 470 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P43593 UniProtKB Helix 118 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Helix 131 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Helix 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Helix 154 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Helix 182 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Helix 193 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Helix 210 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Helix 227 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Turn 231 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Beta strand 235 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Beta strand 246 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Beta strand 257 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Beta strand 261 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Helix 272 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Beta strand 297 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Beta strand 307 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Beta strand 317 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Turn 321 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Beta strand 325 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Beta strand 337 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Helix 342 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Helix 347 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Helix 390 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Beta strand 426 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Beta strand 445 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Beta strand 461 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Beta strand 468 472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Helix 474 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Helix 479 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +P43593 UniProtKB Beta strand 488 496 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VJV +##sequence-region P50102 1 471 +P50102 UniProtKB Chain 1 471 . . . ID=PRO_0000080593;Note=Ubiquitin carboxyl-terminal hydrolase 8 +P50102 UniProtKB Domain 137 468 . . . Note=USP +P50102 UniProtKB Zinc finger 44 105 . . . Note=UBP-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502 +P50102 UniProtKB Active site 146 146 . . . Note=Nucleophile +P50102 UniProtKB Active site 427 427 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +P50102 UniProtKB Mutagenesis 46 46 . . . Note=Lowers histone H2B deubiquitination activity%3B when associated with A-49. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15657441;Dbxref=PMID:15657441 +P50102 UniProtKB Mutagenesis 49 49 . . . Note=Lowers histone H2B deubiquitination activity%3B when associated with A-46. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15657441;Dbxref=PMID:15657441 +P50102 UniProtKB Mutagenesis 77 77 . . . Note=Lowers histone H2B deubiquitination activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15657441;Dbxref=PMID:15657441 +P50102 UniProtKB Mutagenesis 146 146 . . . Note=Lowers histone H2B deubiquitination activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15657441;Dbxref=PMID:15657441 +P50102 UniProtKB Mutagenesis 419 419 . . . Note=Lowers histone H2B deubiquitination activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15657441;Dbxref=PMID:15657441 +P50102 UniProtKB Helix 5 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Helix 14 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Helix 36 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Turn 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 54 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Turn 69 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Helix 73 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 85 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Turn 89 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 94 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Turn 97 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Helix 107 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Helix 112 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Helix 118 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Helix 130 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Helix 146 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Helix 159 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Helix 169 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Turn 179 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Helix 183 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Helix 214 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Helix 228 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 231 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Helix 238 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Helix 260 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FK5 +P50102 UniProtKB Helix 274 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 281 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Turn 290 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 297 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 306 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Helix 316 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 327 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FJC +P50102 UniProtKB Turn 337 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 341 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FJC +P50102 UniProtKB Beta strand 346 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 356 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 365 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 369 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M99 +P50102 UniProtKB Beta strand 373 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 384 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Helix 389 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 409 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 425 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Turn 435 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FIP +P50102 UniProtKB Beta strand 439 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 446 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Helix 452 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P50102 UniProtKB Beta strand 460 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +##sequence-region P54730 1 416 +P54730 UniProtKB Chain 1 416 . . . ID=PRO_0000211001;Note=UBX domain-containing protein 4 +P54730 UniProtKB Domain 273 350 . . . Note=UBX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00215 +##sequence-region P36135 1 365 +P36135 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36135 UniProtKB Chain 18 365 . . . ID=PRO_0000194002;Note=Probable secreted beta-glucosidase UTH1 +P36135 UniProtKB Compositional bias 89 103 . . . Note=Poly-Ser +##sequence-region Q12220 1 943 +Q12220 UniProtKB Chain 1 943 . . . ID=PRO_0000050955;Note=U3 small nucleolar RNA-associated protein 12 +Q12220 UniProtKB Repeat 77 107 . . . Note=WD 1 +Q12220 UniProtKB Repeat 119 149 . . . Note=WD 2 +Q12220 UniProtKB Repeat 161 190 . . . Note=WD 3 +Q12220 UniProtKB Repeat 202 230 . . . Note=WD 4 +Q12220 UniProtKB Repeat 389 418 . . . Note=WD 5 +Q12220 UniProtKB Repeat 428 458 . . . Note=WD 6 +Q12220 UniProtKB Repeat 471 501 . . . Note=WD 7 +Q12220 UniProtKB Repeat 571 601 . . . Note=WD 8 +Q12220 UniProtKB Repeat 613 643 . . . Note=WD 9 +Q12220 UniProtKB Repeat 655 685 . . . Note=WD 10 +##sequence-region Q06679 1 776 +Q06679 UniProtKB Chain 1 776 . . . ID=PRO_0000051317;Note=U3 small nucleolar RNA-associated protein 4 +Q06679 UniProtKB Repeat 35 40 . . . Note=WD 1 +Q06679 UniProtKB Repeat 132 169 . . . Note=WD 2 +Q06679 UniProtKB Repeat 178 214 . . . Note=WD 3 +Q06679 UniProtKB Repeat 230 266 . . . Note=WD 4 +Q06679 UniProtKB Repeat 271 308 . . . Note=WD 5 +Q06679 UniProtKB Repeat 417 452 . . . Note=WD 6 +##sequence-region P38882 1 575 +P38882 UniProtKB Chain 1 575 . . . ID=PRO_0000065744;Note=U3 small nucleolar RNA-associated protein 9 +P38882 UniProtKB Modified residue 547 547 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38882 UniProtKB Modified residue 564 564 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P25591 1 423 +P25591 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P25591 UniProtKB Chain 2 423 . . . ID=PRO_0000202554;Note=vacuole-related protein 17 +P25591 UniProtKB Region 110 170 . . . Note=MYO2-binding +P25591 UniProtKB Region 290 380 . . . Note=VAC8-binding +P25591 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P25591 UniProtKB Modified residue 119 119 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18804442;Dbxref=PMID:18804442 +P25591 UniProtKB Modified residue 149 149 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18804442;Dbxref=PMID:18804442 +P25591 UniProtKB Modified residue 178 178 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18804442;Dbxref=PMID:18804442 +P25591 UniProtKB Modified residue 248 248 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18804442;Dbxref=PMID:18804442 +P25591 UniProtKB Modified residue 269 269 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25591 UniProtKB Mutagenesis 119 119 . . . Note=Impairs phosphorylation%3B when associated with A-149%3B A-178 and A-248. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18804442;Dbxref=PMID:18804442 +P25591 UniProtKB Mutagenesis 149 149 . . . Note=Impairs phosphorylation%3B when associated with A-119%3B A-178 and A-248. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18804442;Dbxref=PMID:18804442 +P25591 UniProtKB Mutagenesis 178 178 . . . Note=Impairs phosphorylation%3B when associated with A-119%3B A-149 and A-248. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18804442;Dbxref=PMID:18804442 +P25591 UniProtKB Mutagenesis 225 225 . . . Note=Stabilizes VAC17 whose protein levels are about 10-fold higher than wild-type. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18804442;Dbxref=PMID:18804442 +P25591 UniProtKB Mutagenesis 248 248 . . . Note=Impairs phosphorylation%3B when associated with A-119%3B A-149 and A-178. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18804442;Dbxref=PMID:18804442 +##sequence-region Q07468 1 1049 +Q07468 UniProtKB Chain 1 1049 . . . ID=PRO_0000065903;Note=Vacuolar morphogenesis protein 6 +Q07468 UniProtKB Repeat 730 896 . . . Note=CHCR +##sequence-region P17255 1 1071 +P17255 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:11884132,ECO:0000269|Ref.6;Dbxref=PMID:22814378,PMID:11884132 +P17255 UniProtKB Chain 2 283 . . . ID=PRO_0000002458;Note=V-type proton ATPase catalytic subunit A%2C 1st part +P17255 UniProtKB Chain 284 737 . . . ID=PRO_0000002459;Note=Endonuclease PI-SceI +P17255 UniProtKB Chain 738 1071 . . . ID=PRO_0000002460;Note=V-type proton ATPase catalytic subunit A%2C 2nd part +P17255 UniProtKB Domain 494 642 . . . Note=DOD-type homing endonuclease;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00273 +P17255 UniProtKB Nucleotide binding 257 264 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P17255 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.6;Dbxref=PMID:22814378 +P17255 UniProtKB Modified residue 131 131 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P17255 UniProtKB Modified residue 858 858 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P17255 UniProtKB Modified residue 928 928 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P17255 UniProtKB Mutagenesis 284 284 . . . Note=Reduces splicing reaction speed. Inhibits splicing%3B when associated with N-362%3B S-737 and S-738 in X10SSS VDE. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10828056,ECO:0000269|PubMed:11884132,ECO:0000269|PubMed:1417861;Dbxref=PMID:10828056,PMID:11884132,PMID:1417861 +P17255 UniProtKB Mutagenesis 362 362 . . . Note=Inhibits splicing%3B when associated with S-284%3B S-737 and S-738 in X10SSS VDE. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11884132;Dbxref=PMID:11884132 +P17255 UniProtKB Mutagenesis 737 737 . . . Note=Inhibits splicing%3B when associated with S-284%3B N-362 and S-738 in X10SSS VDE. N->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10828056,ECO:0000269|PubMed:11884132;Dbxref=PMID:10828056,PMID:11884132 +P17255 UniProtKB Mutagenesis 738 738 . . . Note=Reduces splicing reaction speed. Inhibits splicing%3B when associated with S-284%3B N-362 and S-737 in X10SSS VDE. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11884132,ECO:0000269|PubMed:1417861;Dbxref=PMID:11884132,PMID:1417861 +P17255 UniProtKB Sequence conflict 875 875 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17255 UniProtKB Beta strand 290 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Beta strand 298 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Helix 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Beta strand 309 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Beta strand 315 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Beta strand 325 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Beta strand 343 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EF0 +P17255 UniProtKB Beta strand 347 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EF0 +P17255 UniProtKB Beta strand 355 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Beta strand 363 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Beta strand 372 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Beta strand 382 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Beta strand 398 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDE +P17255 UniProtKB Beta strand 402 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Helix 415 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Helix 420 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Beta strand 434 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Helix 444 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Helix 452 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Beta strand 459 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Turn 471 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA +P17255 UniProtKB Beta strand 479 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDE +P17255 UniProtKB Beta strand 485 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA +P17255 UniProtKB Helix 488 501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA +P17255 UniProtKB Beta strand 506 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EF0 +P17255 UniProtKB Helix 516 528 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA +P17255 UniProtKB Beta strand 531 533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LWT +P17255 UniProtKB Beta strand 534 537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EF0 +P17255 UniProtKB Beta strand 538 540 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UM2 +P17255 UniProtKB Turn 541 543 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EF0 +P17255 UniProtKB Beta strand 544 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EF0 +P17255 UniProtKB Turn 556 559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LWT +P17255 UniProtKB Helix 570 575 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA +P17255 UniProtKB Beta strand 579 584 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA +P17255 UniProtKB Helix 588 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA +P17255 UniProtKB Helix 595 609 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA +P17255 UniProtKB Beta strand 610 613 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EF0 +P17255 UniProtKB Beta strand 619 625 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA +P17255 UniProtKB Helix 627 639 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA +P17255 UniProtKB Beta strand 643 650 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA +P17255 UniProtKB Helix 654 656 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA +P17255 UniProtKB Beta strand 657 659 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EF0 +P17255 UniProtKB Beta strand 661 669 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA +P17255 UniProtKB Helix 672 678 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA +P17255 UniProtKB Turn 684 686 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DFA +P17255 UniProtKB Helix 693 695 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Beta strand 700 702 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Beta strand 704 719 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Beta strand 721 723 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EF0 +P17255 UniProtKB Beta strand 727 729 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +P17255 UniProtKB Beta strand 733 735 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GPP +##sequence-region P38152 1 299 +P38152 UniProtKB Chain 1 299 . . . ID=PRO_0000090653;Note=Tricarboxylate transport protein +P38152 UniProtKB Transmembrane 16 36 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38152 UniProtKB Transmembrane 66 86 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38152 UniProtKB Transmembrane 113 133 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38152 UniProtKB Transmembrane 174 193 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38152 UniProtKB Transmembrane 215 235 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38152 UniProtKB Transmembrane 272 291 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38152 UniProtKB Repeat 10 97 . . . Note=Solcar 1 +P38152 UniProtKB Repeat 109 199 . . . Note=Solcar 2 +P38152 UniProtKB Repeat 212 297 . . . Note=Solcar 3 +P38152 UniProtKB Sequence conflict 97 97 . . . Note=M->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38152 UniProtKB Sequence conflict 101 101 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04235 1 462 +Q04235 UniProtKB Chain 1 462 . . . ID=PRO_0000203264;Note=tRNA wybutosine-synthesizing protein 2 +Q04235 UniProtKB Region 305 306 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01021 +Q04235 UniProtKB Binding site 257 257 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01021 +Q04235 UniProtKB Binding site 264 264 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01021 +##sequence-region P06104 1 172 +P06104 UniProtKB Chain 1 172 . . . ID=PRO_0000082540;Note=Ubiquitin-conjugating enzyme E2 2 +P06104 UniProtKB Compositional bias 150 172 . . . Note=Asp/Glu-rich (acidic tail) +P06104 UniProtKB Active site 88 88 . . . Note=Glycyl thioester intermediate +P06104 UniProtKB Modified residue 120 120 . . . Note=Phosphoserine%3B by SGV1;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:16307922;Dbxref=PMID:18407956,PMID:16307922 +P06104 UniProtKB Mutagenesis 1 9 . . . Note=Prevents H3K4me3 formation. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12077605,ECO:0000269|PubMed:8436296;Dbxref=PMID:12077605,PMID:8436296 +P06104 UniProtKB Mutagenesis 88 88 . . . Note=Loss of activity. C->A%2CV;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12077605,ECO:0000269|PubMed:2157209;Dbxref=PMID:12077605,PMID:2157209 +P06104 UniProtKB Helix 4 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62 +P06104 UniProtKB Beta strand 24 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62 +P06104 UniProtKB Beta strand 32 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62 +P06104 UniProtKB Turn 47 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62 +P06104 UniProtKB Beta strand 52 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62 +P06104 UniProtKB Turn 61 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62 +P06104 UniProtKB Beta strand 69 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62 +P06104 UniProtKB Beta strand 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62 +P06104 UniProtKB Helix 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62 +P06104 UniProtKB Turn 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62 +P06104 UniProtKB Helix 102 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62 +P06104 UniProtKB Helix 124 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62 +P06104 UniProtKB Helix 134 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R62 +##sequence-region P39944 1 805 +P39944 UniProtKB Chain 1 805 . . . ID=PRO_0000080590;Note=Ubiquitin carboxyl-terminal hydrolase 5 +P39944 UniProtKB Domain 159 283 . . . Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173 +P39944 UniProtKB Domain 446 804 . . . Note=USP +P39944 UniProtKB Active site 455 455 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +P39944 UniProtKB Active site 761 761 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +##sequence-region P38349 1 436 +P38349 UniProtKB Chain 1 436 . . . ID=PRO_0000211004;Note=UBX domain-containing protein 7 +P38349 UniProtKB Domain 212 290 . . . Note=UBX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00215 +P38349 UniProtKB Modified residue 388 388 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38349 UniProtKB Cross-link 19 19 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P47108 1 1174 +P47108 UniProtKB Chain 1 1174 . . . ID=PRO_0000203094;Note=Nucleolar pre-ribosomal-associated protein 2 +##sequence-region P53146 1 245 +P53146 UniProtKB Chain 1 245 . . . ID=PRO_0000215584;Note=Protein transport protein USE1 +P53146 UniProtKB Topological domain 1 218 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53146 UniProtKB Transmembrane 219 239 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53146 UniProtKB Topological domain 240 245 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53146 UniProtKB Mutagenesis 183 183 . . . Note=In USE1-0%3B slows down protein transport from the endoplasmic reticulum to the Golgi at 37 degrees Celsius. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12853481;Dbxref=PMID:12853481 +##sequence-region P53177 1 273 +P53177 UniProtKB Chain 1 273 . . . ID=PRO_0000202769;Note=tRNA wybutosine-synthesizing protein 3 +P53177 UniProtKB Modified residue 26 26 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53177 UniProtKB Modified residue 238 238 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P22515 1 1024 +P22515 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P22515 UniProtKB Chain 2 1024 . . . ID=PRO_0000194977;Note=Ubiquitin-activating enzyme E1 1 +P22515 UniProtKB Repeat 27 164 . . . Note=1-1 +P22515 UniProtKB Repeat 425 579 . . . Note=1-2 +P22515 UniProtKB Nucleotide binding 544 545 . . . Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24816100;Dbxref=PMID:24816100 +P22515 UniProtKB Region 27 579 . . . Note=2 approximate repeats +P22515 UniProtKB Active site 600 600 . . . Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10132,ECO:0000269|PubMed:24816100;Dbxref=PMID:24816100 +P22515 UniProtKB Binding site 444 444 . . . Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24816100;Dbxref=PMID:24816100 +P22515 UniProtKB Binding site 470 470 . . . Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24816100;Dbxref=PMID:24816100 +P22515 UniProtKB Binding site 481 481 . . . Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24816100;Dbxref=PMID:24816100 +P22515 UniProtKB Binding site 494 494 . . . Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24816100;Dbxref=PMID:24816100 +P22515 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P22515 UniProtKB Modified residue 265 265 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P22515 UniProtKB Modified residue 914 914 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P22515 UniProtKB Cross-link 595 595 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P22515 UniProtKB Cross-link 608 608 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P22515 UniProtKB Mutagenesis 912 912 . . . Note=Strongly reduces formation of the thioester intermediate with ubiquitin%3B when associated with P-914. I->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18662542;Dbxref=PMID:18662542 +P22515 UniProtKB Mutagenesis 914 914 . . . Note=Strongly reduces formation of the thioester intermediate with ubiquitin%3B when associated with P-912. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18662542;Dbxref=PMID:18662542 +P22515 UniProtKB Mutagenesis 1004 1004 . . . Note=Strongly reduces formation of the thioester intermediate with ubiquitin. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18662542;Dbxref=PMID:18662542 +P22515 UniProtKB Mutagenesis 1014 1014 . . . Note=Strongly reduces formation of the thioester intermediate with ubiquitin%3B when associated with K-1016. D->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18662542;Dbxref=PMID:18662542 +P22515 UniProtKB Mutagenesis 1016 1016 . . . Note=Strongly reduces formation of the thioester intermediate with ubiquitin%3B when associated with K-1014. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18662542;Dbxref=PMID:18662542 +P22515 UniProtKB Sequence conflict 526 526 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22515 UniProtKB Sequence conflict 736 736 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22515 UniProtKB Helix 16 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 28 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 38 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 46 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 61 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 73 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 91 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 108 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 117 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 124 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 134 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 150 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 160 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 171 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 183 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 194 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 210 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 220 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 231 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 237 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 244 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 254 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 262 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 269 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 283 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 288 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Turn 306 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 316 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Turn 334 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 345 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Turn 354 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 360 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 387 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 394 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Turn 400 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Turn 407 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 418 424 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 426 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 436 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 444 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Turn 457 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 465 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 476 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 487 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 494 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 507 509 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Turn 510 512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 513 516 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 522 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Turn 525 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 530 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 537 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 546 559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 563 569 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 572 578 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Turn 580 582 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 586 588 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 599 603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 609 624 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 626 636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 640 647 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 651 663 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 669 684 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 686 694 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 704 708 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 725 742 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 755 763 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 797 802 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 808 811 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 830 844 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 852 859 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 867 885 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 891 893 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 896 900 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Turn 901 904 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 905 909 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 916 919 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 922 925 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Turn 926 928 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 930 936 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 939 950 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 953 959 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 962 966 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 971 977 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Helix 982 990 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 1000 1008 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P22515 UniProtKB Beta strand 1019 1023 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +##sequence-region Q99344 1 299 +Q99344 UniProtKB Chain 1 299 . . . ID=PRO_0000194950;Note=NEDD8-activating enzyme E1 catalytic subunit +Q99344 UniProtKB Nucleotide binding 12 37 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99344 UniProtKB Active site 168 168 . . . Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10132 +Q99344 UniProtKB Sequence conflict 33 33 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P52492 1 156 +P52492 UniProtKB Chain 1 156 . . . ID=PRO_0000082559;Note=Ubiquitin-conjugating enzyme E2-18 kDa +P52492 UniProtKB Active site 93 93 . . . Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00388,ECO:0000255|PROSITE-ProRule:PRU10133 +##sequence-region P52491 1 188 +P52491 UniProtKB Chain 1 188 . . . ID=PRO_0000082501;Note=NEDD8-conjugating enzyme UBC12 +P52491 UniProtKB Active site 115 115 . . . Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00388,ECO:0000255|PROSITE-ProRule:PRU10133 +P52491 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21940857;Dbxref=PMID:21940857 +P52491 UniProtKB Helix 1 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U +P52491 UniProtKB Beta strand 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U +P52491 UniProtKB Helix 27 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U +P52491 UniProtKB Beta strand 45 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U +P52491 UniProtKB Beta strand 63 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U +P52491 UniProtKB Beta strand 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U +P52491 UniProtKB Turn 74 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U +P52491 UniProtKB Beta strand 80 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U +P52491 UniProtKB Turn 88 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U +P52491 UniProtKB Beta strand 96 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U +P52491 UniProtKB Beta strand 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U +P52491 UniProtKB Helix 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U +P52491 UniProtKB Turn 120 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U +P52491 UniProtKB Helix 129 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U +P52491 UniProtKB Helix 151 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U +P52491 UniProtKB Helix 161 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2U +##sequence-region P15732 1 148 +P15732 UniProtKB Chain 1 148 . . . ID=PRO_0000082546;Note=Ubiquitin-conjugating enzyme E2-16 kDa +P15732 UniProtKB Active site 86 86 . . . Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00388,ECO:0000255|PROSITE-ProRule:PRU10133 +P15732 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15731 +P15732 UniProtKB Cross-link 91 91 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15731 +##sequence-region P38187 1 747 +P38187 UniProtKB Chain 1 747 . . . ID=PRO_0000080598;Note=Ubiquitin carboxyl-terminal hydrolase 13 +P38187 UniProtKB Domain 140 668 . . . Note=USP +P38187 UniProtKB Active site 149 149 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +P38187 UniProtKB Active site 619 619 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +P38187 UniProtKB Modified residue 198 198 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38187 UniProtKB Sequence conflict 180 180 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25037 1 809 +P25037 UniProtKB Chain 1 809 . . . ID=PRO_0000080585;Note=Ubiquitin carboxyl-terminal hydrolase 1 +P25037 UniProtKB Domain 101 738 . . . Note=USP +P25037 UniProtKB Active site 110 110 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +P25037 UniProtKB Active site 697 697 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +P25037 UniProtKB Modified residue 530 530 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P25037 UniProtKB Modified residue 531 531 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P25037 UniProtKB Modified residue 555 555 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P25037 UniProtKB Modified residue 618 618 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P25037 UniProtKB Modified residue 638 638 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P25037 UniProtKB Modified residue 652 652 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25037 UniProtKB Modified residue 653 653 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25037 UniProtKB Modified residue 654 654 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25037 UniProtKB Modified residue 670 670 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P25037 UniProtKB Modified residue 755 755 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P25037 UniProtKB Sequence conflict 418 418 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38290 1 277 +P38290 UniProtKB Chain 1 277 . . . ID=PRO_0000065713;Note=Ubiquitin-conjugating enzyme suppressor 1 +##sequence-region P32861 1 499 +P32861 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32861 UniProtKB Chain 2 499 . . . ID=PRO_0000185765;Note=UTP--glucose-1-phosphate uridylyltransferase +P32861 UniProtKB Region 109 112 . . . Note=UTP binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3 +P32861 UniProtKB Region 111 112 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16851 +P32861 UniProtKB Region 244 246 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16851 +P32861 UniProtKB Region 448 499 . . . Note=Oligomerization +P32861 UniProtKB Active site 388 388 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32861 UniProtKB Metal binding 123 123 . . . Note=Magnesium;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32861 UniProtKB Metal binding 246 246 . . . Note=Magnesium;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32861 UniProtKB Binding site 123 123 . . . Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3 +P32861 UniProtKB Binding site 186 186 . . . Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3 +P32861 UniProtKB Binding site 215 215 . . . Note=UTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3 +P32861 UniProtKB Binding site 216 216 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16851 +P32861 UniProtKB Binding site 246 246 . . . Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3 +P32861 UniProtKB Binding site 388 388 . . . Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3 +P32861 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32861 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32861 UniProtKB Modified residue 19 19 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32861 UniProtKB Modified residue 21 21 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32861 UniProtKB Modified residue 79 79 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32861 UniProtKB Modified residue 369 369 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23865587;Dbxref=PMID:23865587 +P32861 UniProtKB Helix 23 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 49 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Turn 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 88 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 104 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 115 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 134 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 154 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Turn 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 164 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 172 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 180 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Turn 194 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 202 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 210 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 216 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 219 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 228 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 239 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 247 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 254 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 266 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 276 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 279 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 283 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 290 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 296 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 304 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Turn 310 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 315 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 325 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 364 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 371 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 375 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 381 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 390 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 401 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 407 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 420 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 425 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Helix 430 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 446 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 462 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 477 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +P32861 UniProtKB Beta strand 484 498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I5K +##sequence-region P38709 1 493 +P38709 UniProtKB Chain 1 493 . . . ID=PRO_0000185766;Note=Probable UTP--glucose-1-phosphate uridylyltransferase +P38709 UniProtKB Region 105 108 . . . Note=UTP binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3 +P38709 UniProtKB Region 107 108 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16851 +P38709 UniProtKB Region 240 242 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16851 +P38709 UniProtKB Binding site 181 181 . . . Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3 +P38709 UniProtKB Binding site 211 211 . . . Note=UTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3 +P38709 UniProtKB Binding site 242 242 . . . Note=UTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9M9P3 +##sequence-region P38293 1 148 +P38293 UniProtKB Chain 1 148 . . . ID=PRO_0000065720;Note=Proteasome maturation factor UMP1 +##sequence-region Q08960 1 810 +Q08960 UniProtKB Chain 1 810 . . . ID=PRO_0000217861;Note=S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase +Q08960 UniProtKB Domain 205 360 . . . Note=Flavodoxin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00088 +Q08960 UniProtKB Nucleotide binding 211 215 . . . Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00088 +Q08960 UniProtKB Nucleotide binding 304 337 . . . Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00088 +Q08960 UniProtKB Metal binding 479 479 . . . Note=Iron-sulfur (4Fe-4S-S-AdoMet) +Q08960 UniProtKB Metal binding 483 483 . . . Note=Iron-sulfur (4Fe-4S-S-AdoMet) +Q08960 UniProtKB Metal binding 486 486 . . . Note=Iron-sulfur (4Fe-4S-S-AdoMet) +Q08960 UniProtKB Cross-link 496 496 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +Q08960 UniProtKB Mutagenesis 479 479 . . . Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16642040;Dbxref=PMID:16642040 +Q08960 UniProtKB Mutagenesis 483 483 . . . Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16642040;Dbxref=PMID:16642040 +Q08960 UniProtKB Mutagenesis 486 486 . . . Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16642040;Dbxref=PMID:16642040 +Q08960 UniProtKB Mutagenesis 532 532 . . . Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16642040;Dbxref=PMID:16642040 +Q08960 UniProtKB Mutagenesis 550 550 . . . Note=Loss of function. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16642040;Dbxref=PMID:16642040 +##sequence-region Q08282 1 695 +Q08282 UniProtKB Chain 1 695 . . . ID=PRO_0000226146;Note=tRNA wybutosine-synthesizing protein 4 +Q08282 UniProtKB Region 146 147 . . . Note=S-adenosyl-L-methionine binding +Q08282 UniProtKB Region 196 197 . . . Note=S-adenosyl-L-methionine binding +Q08282 UniProtKB Active site 88 88 . . . Note=Proton donor%3B for both methylation and methoxycarbonylation activities;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19287006;Dbxref=PMID:19287006 +Q08282 UniProtKB Active site 229 229 . . . Note=Proton acceptor%3B for methoxycarbonylation activity;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19287006;Dbxref=PMID:19287006 +Q08282 UniProtKB Binding site 38 38 . . . Note=S-adenosyl-L-methionine +Q08282 UniProtKB Binding site 88 88 . . . Note=S-adenosyl-L-methionine +Q08282 UniProtKB Binding site 115 115 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen +Q08282 UniProtKB Binding site 224 224 . . . Note=S-adenosyl-L-methionine +Q08282 UniProtKB Mutagenesis 88 88 . . . Note=Loss of function. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19287006;Dbxref=PMID:19287006 +Q08282 UniProtKB Sequence conflict 417 417 . . . Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08282 UniProtKB Helix 7 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 17 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 30 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 67 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 79 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 107 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 121 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 131 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 137 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 148 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 162 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 188 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 200 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Turn 210 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 217 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 227 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 232 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 245 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 264 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 282 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 289 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 303 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 309 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 318 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 333 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 343 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 352 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZW9 +Q08282 UniProtKB Turn 358 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 375 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 392 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 400 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 406 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 414 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 424 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 444 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Turn 449 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 453 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 460 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 471 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Turn 475 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 479 482 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 490 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZW9 +Q08282 UniProtKB Beta strand 494 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 503 506 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 509 512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZW9 +Q08282 UniProtKB Beta strand 514 519 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Turn 520 523 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 524 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 533 536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 539 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZW9 +Q08282 UniProtKB Beta strand 543 547 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Turn 548 551 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 552 556 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 569 575 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 584 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 593 595 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 601 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 609 613 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Turn 624 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 627 632 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Turn 633 636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 637 640 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 645 650 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 659 661 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 668 671 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 674 676 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Helix 677 679 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZZK +Q08282 UniProtKB Beta strand 682 684 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +Q08282 UniProtKB Beta strand 688 692 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZWA +##sequence-region P38820 1 440 +P38820 UniProtKB Chain 1 440 . . . ID=PRO_0000120587;Note=Adenylyltransferase and sulfurtransferase UBA4 +P38820 UniProtKB Domain 339 438 . . . Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049 +P38820 UniProtKB Nucleotide binding 105 109 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049 +P38820 UniProtKB Nucleotide binding 166 167 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049 +P38820 UniProtKB Compositional bias 214 219 . . . Note=Poly-Pro +P38820 UniProtKB Active site 225 225 . . . Note=Glycyl thioester intermediate%3B for adenylyltransferase activity +P38820 UniProtKB Active site 397 397 . . . Note=Cysteine persulfide intermediate%3B for sulfurtransferase activity +P38820 UniProtKB Metal binding 208 208 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049 +P38820 UniProtKB Metal binding 211 211 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049 +P38820 UniProtKB Metal binding 286 286 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049 +P38820 UniProtKB Metal binding 289 289 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049 +P38820 UniProtKB Binding site 77 77 . . . Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049 +P38820 UniProtKB Binding site 98 98 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049 +P38820 UniProtKB Binding site 122 122 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03049 +P38820 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38820 UniProtKB Modified residue 326 326 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38820 UniProtKB Mutagenesis 225 225 . . . Note=Abolishes adenylyltransferase activity but not sulfurtransferase activity. C->A%2CS;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10713047,ECO:0000269|PubMed:18491921,ECO:0000269|PubMed:19145231,ECO:0000269|PubMed:19151091;Dbxref=PMID:10713047,PMID:18491921,PMID:19145231,PMID:19151091 +P38820 UniProtKB Mutagenesis 397 397 . . . Note=Abolishes sulfurtransferase activity but not adenylyltransferase activity. C->A%2CS;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18491921,ECO:0000269|PubMed:19145231,ECO:0000269|PubMed:19151091;Dbxref=PMID:18491921,PMID:19145231,PMID:19151091 +##sequence-region P15731 1 148 +P15731 UniProtKB Chain 1 148 . . . ID=PRO_0000082545;Note=Ubiquitin-conjugating enzyme E2 4 +P15731 UniProtKB Active site 86 86 . . . Note=Glycyl thioester intermediate +P15731 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P15731 UniProtKB Cross-link 91 91 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P15731 UniProtKB Helix 2 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ +P15731 UniProtKB Beta strand 20 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ +P15731 UniProtKB Beta strand 30 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ +P15731 UniProtKB Beta strand 42 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIE +P15731 UniProtKB Turn 45 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIE +P15731 UniProtKB Beta strand 50 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ +P15731 UniProtKB Turn 59 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ +P15731 UniProtKB Beta strand 67 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ +P15731 UniProtKB Helix 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ +P15731 UniProtKB Turn 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ +P15731 UniProtKB Helix 100 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ +P15731 UniProtKB Helix 122 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ +P15731 UniProtKB Helix 132 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QCQ +##sequence-region P28263 1 218 +P28263 UniProtKB Chain 1 218 . . . ID=PRO_0000082555;Note=Ubiquitin-conjugating enzyme E2-24 kDa +P28263 UniProtKB Active site 85 85 . . . Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00388,ECO:0000255|PROSITE-ProRule:PRU10133 +##sequence-region P34223 1 423 +P34223 UniProtKB Chain 1 423 . . . ID=PRO_0000210998;Note=UBX domain-containing protein 1 +P34223 UniProtKB Domain 232 297 . . . Note=SEP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00732 +P34223 UniProtKB Domain 344 421 . . . Note=UBX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00215 +P34223 UniProtKB Modified residue 128 128 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34223 UniProtKB Modified residue 210 210 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34223 UniProtKB Modified residue 224 224 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34223 UniProtKB Modified residue 315 315 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +P34223 UniProtKB Modified residue 321 321 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34223 UniProtKB Modified residue 322 322 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P34223 UniProtKB Modified residue 331 331 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34223 UniProtKB Cross-link 241 241 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P34223 UniProtKB Sequence conflict 223 223 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04511 1 668 +Q04511 UniProtKB Chain 1 668 . . . ID=PRO_0000119970;Note=Ubiquitin ligase complex F-box protein UFO1 +Q04511 UniProtKB Domain 5 51 . . . Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080 +Q04511 UniProtKB Domain 547 566 . . . Note=UIM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213 +Q04511 UniProtKB Domain 583 602 . . . Note=UIM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213 +Q04511 UniProtKB Domain 651 668 . . . Note=UIM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213 +Q04511 UniProtKB Modified residue 511 511 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04511 UniProtKB Modified residue 514 514 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P40537 1 1034 +P40537 UniProtKB Chain 1 1034 . . . ID=PRO_0000101732;Note=Ubiquitin-like-specific protease 2 +P40537 UniProtKB Modified residue 788 788 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40537 UniProtKB Modified residue 903 903 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40537 UniProtKB Modified residue 983 983 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40537 UniProtKB Modified residue 984 984 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40537 UniProtKB Helix 832 839 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5V1A +##sequence-region Q12151 1 913 +Q12151 UniProtKB Chain 1 913 . . . ID=PRO_0000114988;Note=Sterol uptake control protein 2 +Q12151 UniProtKB DNA binding 50 80 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +Q12151 UniProtKB Coiled coil 303 346 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12151 UniProtKB Coiled coil 440 472 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12151 UniProtKB Compositional bias 222 353 . . . Note=Gln-rich +Q12151 UniProtKB Compositional bias 885 888 . . . Note=Poly-Gly +Q12151 UniProtKB Modified residue 122 122 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12151 UniProtKB Modified residue 519 519 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12151 UniProtKB Mutagenesis 888 888 . . . Note=Increased aerobic expression of DAN1. G->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11238402,ECO:0000269|PubMed:3059715,ECO:0000269|PubMed:9696767;Dbxref=PMID:11238402,PMID:3059715,PMID:9696767 +Q12151 UniProtKB Mutagenesis 888 888 . . . Note=In upc2-1%3B increases aerobic sterol synthesis and uptake. Increases also aerobic expression of DAN1 and sensibility to NaCl and LiCl. G->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11238402,ECO:0000269|PubMed:3059715,ECO:0000269|PubMed:9696767;Dbxref=PMID:11238402,PMID:3059715,PMID:9696767 +Q12151 UniProtKB Helix 607 618 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Helix 621 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Helix 632 636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Helix 638 645 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Helix 647 661 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Helix 670 686 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Helix 687 692 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Helix 695 711 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Helix 732 744 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Helix 756 759 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Turn 767 769 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Beta strand 773 776 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Beta strand 784 787 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Helix 788 790 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Beta strand 795 797 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Helix 800 811 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Helix 817 824 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Helix 825 827 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Helix 831 839 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Helix 842 861 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +Q12151 UniProtKB Turn 871 873 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N9N +##sequence-region P36096 1 758 +P36096 UniProtKB Signal peptide 1 26 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36096 UniProtKB Chain 27 758 . . . ID=PRO_0000056409;Note=Transmembrane E3 ubiquitin-protein ligase 1 +P36096 UniProtKB Topological domain 27 398 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36096 UniProtKB Transmembrane 399 419 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36096 UniProtKB Topological domain 420 431 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36096 UniProtKB Transmembrane 432 452 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36096 UniProtKB Topological domain 453 458 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36096 UniProtKB Transmembrane 459 479 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36096 UniProtKB Topological domain 480 523 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36096 UniProtKB Transmembrane 524 544 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36096 UniProtKB Topological domain 545 553 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36096 UniProtKB Transmembrane 554 574 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36096 UniProtKB Topological domain 575 602 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36096 UniProtKB Transmembrane 603 623 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36096 UniProtKB Topological domain 624 635 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36096 UniProtKB Transmembrane 636 656 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36096 UniProtKB Topological domain 657 758 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36096 UniProtKB Zinc finger 699 752 . . . Note=RING-type%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +##sequence-region Q06412 1 1307 +Q06412 UniProtKB Chain 1 1307 . . . ID=PRO_0000080979;Note=Rho1 guanine nucleotide exchange factor TUS1 +Q06412 UniProtKB Domain 467 657 . . . Note=DH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00062 +Q06412 UniProtKB Domain 715 877 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +Q06412 UniProtKB Domain 938 1279 . . . Note=CNH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00795 +Q06412 UniProtKB Compositional bias 105 110 . . . Note=Poly-Pro +Q06412 UniProtKB Compositional bias 227 230 . . . Note=Poly-Pro +##sequence-region P38319 1 544 +P38319 UniProtKB Chain 1 544 . . . ID=PRO_0000212490;Note=Tyrosyl-DNA phosphodiesterase 1 +P38319 UniProtKB Region 312 316 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NUW8 +P38319 UniProtKB Active site 182 182 . . . Note=Nucleophile;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16751265;Dbxref=PMID:16751265 +P38319 UniProtKB Active site 432 432 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17707402;Dbxref=PMID:17707402 +P38319 UniProtKB Binding site 184 184 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NUW8 +P38319 UniProtKB Binding site 434 434 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NUW8 +P38319 UniProtKB Site 467 467 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NUW8 +P38319 UniProtKB Mutagenesis 182 182 . . . Note=Loss of activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16751265;Dbxref=PMID:16751265 +P38319 UniProtKB Mutagenesis 432 432 . . . Note=Strongly reduced release of the covalent intermediate with DNA that is formed during the enzyme reaction%2C leading to the accumulation of toxic adducts. No effect on bleomycin sensitivity. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17707402;Dbxref=PMID:17707402 +P38319 UniProtKB Mutagenesis 432 432 . . . Note=Interferes with the hydrolysis of the covalent intermediate with DNA that is formed during the enzyme reaction. No effect on bleomycin sensitivity. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17707402;Dbxref=PMID:17707402 +P38319 UniProtKB Beta strand 81 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Turn 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Helix 105 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 114 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Helix 126 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 139 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Helix 154 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Helix 159 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 168 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 185 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 193 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Helix 206 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 211 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 215 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Helix 232 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Helix 247 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Helix 254 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Helix 263 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 269 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 277 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ3 +P38319 UniProtKB Helix 282 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Turn 294 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 301 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 311 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 319 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Helix 325 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Helix 330 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 336 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ8 +P38319 UniProtKB Helix 356 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 368 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Helix 378 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Helix 386 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Helix 398 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Helix 401 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 414 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Turn 419 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Turn 424 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 434 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 454 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Helix 468 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 474 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 479 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Helix 489 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 492 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 498 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Helix 503 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 516 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +P38319 UniProtKB Beta strand 523 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ3 +P38319 UniProtKB Turn 530 532 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SQ7 +##sequence-region P53874 1 792 +P53874 UniProtKB Chain 1 792 . . . ID=PRO_0000080595;Note=Ubiquitin carboxyl-terminal hydrolase 10 +P53874 UniProtKB Domain 362 733 . . . Note=USP +P53874 UniProtKB Compositional bias 127 130 . . . Note=Poly-Ser +P53874 UniProtKB Compositional bias 138 144 . . . Note=Poly-Glu +P53874 UniProtKB Compositional bias 252 255 . . . Note=Poly-Glu +P53874 UniProtKB Compositional bias 302 309 . . . Note=Poly-Glu +P53874 UniProtKB Compositional bias 556 562 . . . Note=Poly-Ser +P53874 UniProtKB Active site 371 371 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10093 +P53874 UniProtKB Active site 691 691 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10093 +P53874 UniProtKB Sequence conflict 310 310 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P08067 1 215 +P08067 UniProtKB Transit peptide 1 30 . . . Note=Mitochondrion +P08067 UniProtKB Chain 31 215 . . . ID=PRO_0000030683;Note=Cytochrome b-c1 complex subunit Rieske%2C mitochondrial +P08067 UniProtKB Transmembrane 49 82 . . . Note=Helical +P08067 UniProtKB Domain 123 214 . . . Note=Rieske;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00628 +P08067 UniProtKB Metal binding 159 159 . . . Note=Iron-sulfur (2Fe-2S) +P08067 UniProtKB Metal binding 161 161 . . . Note=Iron-sulfur (2Fe-2S)%3B via pros nitrogen +P08067 UniProtKB Metal binding 178 178 . . . Note=Iron-sulfur (2Fe-2S) +P08067 UniProtKB Metal binding 181 181 . . . Note=Iron-sulfur (2Fe-2S)%3B via pros nitrogen +P08067 UniProtKB Disulfide bond 164 180 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00628,ECO:0000269|PubMed:18390544;Dbxref=PMID:18390544 +P08067 UniProtKB Mutagenesis 157 157 . . . Note=Loss of activity. G->D +P08067 UniProtKB Mutagenesis 159 159 . . . Note=Loss of activity. C->S +P08067 UniProtKB Mutagenesis 161 161 . . . Note=Loss of activity. H->R +P08067 UniProtKB Mutagenesis 163 163 . . . Note=Partial loss of activity. G->D +P08067 UniProtKB Mutagenesis 164 164 . . . Note=Loss of activity. C->S +P08067 UniProtKB Mutagenesis 166 166 . . . Note=Partial loss of activity. P->L +P08067 UniProtKB Mutagenesis 178 178 . . . Note=Loss of activity. C->S%2CY +P08067 UniProtKB Mutagenesis 179 179 . . . Note=Partial loss of activity. P->L +P08067 UniProtKB Mutagenesis 180 180 . . . Note=Loss of activity. C->S +P08067 UniProtKB Mutagenesis 181 181 . . . Note=Loss of activity. H->R +P08067 UniProtKB Mutagenesis 183 183 . . . Note=Loss of activity. S->L +P08067 UniProtKB Mutagenesis 184 184 . . . Note=No loss of activity. H->R +P08067 UniProtKB Mutagenesis 186 186 . . . Note=Partial loss of activity. D->N +P08067 UniProtKB Mutagenesis 189 189 . . . Note=Loss of activity. G->D +P08067 UniProtKB Mutagenesis 195 195 . . . Note=No loss of activity. P->S +P08067 UniProtKB Mutagenesis 196 196 . . . Note=No loss of activity. A->T +P08067 UniProtKB Mutagenesis 203 203 . . . Note=Loss of activity. P->S +P08067 UniProtKB Turn 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Beta strand 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EZV +P08067 UniProtKB Helix 51 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Helix 86 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Beta strand 94 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Helix 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Beta strand 106 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Beta strand 114 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Helix 123 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Helix 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Turn 144 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Beta strand 152 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Turn 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Beta strand 167 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Turn 171 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Beta strand 175 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Turn 179 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Beta strand 183 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Beta strand 191 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Beta strand 205 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08067 UniProtKB Beta strand 211 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +##sequence-region P41834 1 346 +P41834 UniProtKB Chain 1 346 . . . ID=PRO_0000210283;Note=Syntaxin UFE1 +P41834 UniProtKB Topological domain 1 324 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41834 UniProtKB Transmembrane 325 342 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41834 UniProtKB Topological domain 343 346 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41834 UniProtKB Domain 255 317 . . . Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202 +##sequence-region P0CF17 1 737 +P0CF17 UniProtKB Chain 1 737 . . . ID=PRO_0000393363;Note=UPF0507 protein YML002W +P0CF17 UniProtKB Domain 1 83 . . . Note=VPS9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00550 +P0CF17 UniProtKB Sequence conflict 32 32 . . . Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P52488 1 636 +P52488 UniProtKB Chain 1 636 . . . ID=PRO_0000194979;Note=Ubiquitin-activating enzyme E1-like +P52488 UniProtKB Nucleotide binding 28 33 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52488 UniProtKB Nucleotide binding 60 63 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52488 UniProtKB Nucleotide binding 121 126 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52488 UniProtKB Motif 619 622 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52488 UniProtKB Active site 177 177 . . . Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10132 +P52488 UniProtKB Metal binding 162 162 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52488 UniProtKB Metal binding 165 165 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52488 UniProtKB Metal binding 435 435 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52488 UniProtKB Metal binding 438 438 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52488 UniProtKB Binding site 52 52 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52488 UniProtKB Binding site 76 76 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52488 UniProtKB Mutagenesis 177 177 . . . Note=Loss of function. C->A%2CS +P52488 UniProtKB Beta strand 442 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH +P52488 UniProtKB Helix 450 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH +P52488 UniProtKB Helix 458 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH +P52488 UniProtKB Beta strand 473 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH +P52488 UniProtKB Turn 480 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH +P52488 UniProtKB Beta strand 484 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH +P52488 UniProtKB Turn 493 496 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH +P52488 UniProtKB Turn 499 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH +P52488 UniProtKB Beta strand 509 515 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH +P52488 UniProtKB Beta strand 518 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH +P52488 UniProtKB Beta strand 525 531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH +P52488 UniProtKB Beta strand 535 538 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONG +P52488 UniProtKB Beta strand 549 551 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONH +##sequence-region P50623 1 157 +P50623 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P50623 UniProtKB Chain 2 157 . . . ID=PRO_0000082556;Note=SUMO-conjugating enzyme UBC9 +P50623 UniProtKB Active site 93 93 . . . Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00388,ECO:0000255|PROSITE-ProRule:PRU10133 +P50623 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P50623 UniProtKB Helix 4 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD +P50623 UniProtKB Beta strand 25 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD +P50623 UniProtKB Beta strand 36 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD +P50623 UniProtKB Turn 52 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD +P50623 UniProtKB Beta strand 56 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD +P50623 UniProtKB Turn 66 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD +P50623 UniProtKB Beta strand 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD +P50623 UniProtKB Beta strand 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD +P50623 UniProtKB Helix 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD +P50623 UniProtKB Turn 99 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD +P50623 UniProtKB Helix 109 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD +P50623 UniProtKB Helix 131 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD +P50623 UniProtKB Helix 141 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GJD +##sequence-region P0CG63 1 381 +P0CG63 UniProtKB Chain 1 76 . . . ID=PRO_0000396306;Note=Ubiquitin +P0CG63 UniProtKB Chain 77 152 . . . ID=PRO_0000396307;Note=Ubiquitin +P0CG63 UniProtKB Chain 153 228 . . . ID=PRO_0000396308;Note=Ubiquitin +P0CG63 UniProtKB Chain 229 304 . . . ID=PRO_0000396309;Note=Ubiquitin +P0CG63 UniProtKB Chain 305 380 . . . ID=PRO_0000396310;Note=Ubiquitin +P0CG63 UniProtKB Propeptide 381 381 . . . ID=PRO_0000396311 +P0CG63 UniProtKB Domain 1 76 . . . Note=Ubiquitin-like 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 +P0CG63 UniProtKB Domain 77 152 . . . Note=Ubiquitin-like 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 +P0CG63 UniProtKB Domain 153 228 . . . Note=Ubiquitin-like 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 +P0CG63 UniProtKB Domain 229 304 . . . Note=Ubiquitin-like 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 +P0CG63 UniProtKB Domain 305 380 . . . Note=Ubiquitin-like 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 +P0CG63 UniProtKB Cross-link 76 76 . . . Note=Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) +P0CG63 UniProtKB Mutagenesis 29 29 . . . Note=Deficiency in ubiquitin-protein conjugate formation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550 +P0CG63 UniProtKB Mutagenesis 48 48 . . . Note=Deficiency in ubiquitin-protein conjugate formation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550 +P0CG63 UniProtKB Mutagenesis 63 63 . . . Note=Deficiency in ubiquitin-protein conjugate formation. Loss of DNA repair function. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550 +P0CG63 UniProtKB Sequence conflict 352 352 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0CG63 UniProtKB Beta strand 2 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W +P0CG63 UniProtKB Beta strand 12 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W +P0CG63 UniProtKB Helix 23 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W +P0CG63 UniProtKB Turn 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W +P0CG63 UniProtKB Beta strand 41 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W +P0CG63 UniProtKB Beta strand 52 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L10 +P0CG63 UniProtKB Helix 56 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W +P0CG63 UniProtKB Beta strand 66 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W +P0CG63 UniProtKB Beta strand 88 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W +P0CG63 UniProtKB Beta strand 101 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W +P0CG63 UniProtKB Beta strand 143 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W +P0CG63 UniProtKB Beta strand 157 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W +P0CG63 UniProtKB Helix 163 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W +P0CG63 UniProtKB Helix 170 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W +P0CG63 UniProtKB Helix 180 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W +P0CG63 UniProtKB Beta strand 184 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W +P0CG63 UniProtKB Beta strand 207 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W +P0CG63 UniProtKB Beta strand 227 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L0W +P0CG63 UniProtKB Beta strand 236 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW7 +P0CG63 UniProtKB Beta strand 241 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW7 +P0CG63 UniProtKB Helix 251 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW7 +P0CG63 UniProtKB Helix 266 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW7 +P0CG63 UniProtKB Beta strand 270 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW7 +P0CG63 UniProtKB Beta strand 274 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW7 +P0CG63 UniProtKB Helix 285 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW7 +P0CG63 UniProtKB Beta strand 294 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW7 +P0CG63 UniProtKB Beta strand 306 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q5E +P0CG63 UniProtKB Turn 312 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q0W +P0CG63 UniProtKB Beta strand 316 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q5E +P0CG63 UniProtKB Beta strand 323 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q0W +P0CG63 UniProtKB Helix 327 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q5E +P0CG63 UniProtKB Turn 342 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q5E +P0CG63 UniProtKB Beta strand 345 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q5E +P0CG63 UniProtKB Beta strand 351 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNJ +P0CG63 UniProtKB Beta strand 358 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OLM +P0CG63 UniProtKB Helix 361 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q5E +P0CG63 UniProtKB Beta strand 370 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q5E +P0CG63 UniProtKB Helix 377 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JT4 +##sequence-region P50101 1 1230 +P50101 UniProtKB Chain 1 1230 . . . ID=PRO_0000080600;Note=Ubiquitin carboxyl-terminal hydrolase 15 +P50101 UniProtKB Domain 39 179 . . . Note=MATH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00129 +P50101 UniProtKB Domain 205 536 . . . Note=USP +P50101 UniProtKB Active site 214 214 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +P50101 UniProtKB Active site 465 465 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +##sequence-region Q02863 1 499 +Q02863 UniProtKB Chain 1 499 . . . ID=PRO_0000080601;Note=Ubiquitin carboxyl-terminal hydrolase 16 +Q02863 UniProtKB Domain 53 497 . . . Note=USP +Q02863 UniProtKB Active site 62 62 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +Q02863 UniProtKB Active site 407 407 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 +##sequence-region P32837 1 571 +P32837 UniProtKB Chain 1 571 . . . ID=PRO_0000054161;Note=GABA-specific permease +P32837 UniProtKB Topological domain 1 73 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Transmembrane 74 94 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Topological domain 95 105 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Transmembrane 106 126 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Topological domain 127 153 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Transmembrane 154 174 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Topological domain 175 198 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Transmembrane 199 219 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Topological domain 220 228 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Transmembrane 229 249 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Topological domain 250 271 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Transmembrane 272 292 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Topological domain 293 312 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Transmembrane 313 333 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Topological domain 334 364 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Transmembrane 365 385 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Topological domain 386 416 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Transmembrane 417 437 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Topological domain 438 441 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Transmembrane 442 462 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Topological domain 463 482 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Transmembrane 483 503 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Topological domain 504 514 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Transmembrane 515 535 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32837 UniProtKB Topological domain 536 571 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03327 1 502 +Q03327 UniProtKB Chain 1 502 . . . ID=PRO_0000270985;Note=Mitochondrial fusion and transport protein UGO1 +Q03327 UniProtKB Topological domain 1 293 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03327 UniProtKB Transmembrane 294 314 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03327 UniProtKB Topological domain 315 502 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03327 UniProtKB Repeat 288 383 . . . Note=Solcar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03327 UniProtKB Region 1 294 . . . Note=Binds FZO1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087460;Dbxref=PMID:15087460 +Q03327 UniProtKB Region 312 502 . . . Note=Binds MGM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087460;Dbxref=PMID:15087460 +Q03327 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q03327 UniProtKB Sequence conflict 114 114 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03327 UniProtKB Sequence conflict 114 114 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39547 1 235 +P39547 UniProtKB Chain 1 235 . . . ID=PRO_0000207528;Note=ULP1-interacting protein 3 +P39547 UniProtKB Transmembrane 51 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39547 UniProtKB Transmembrane 73 93 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39547 UniProtKB Cross-link 11 11 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P39547 UniProtKB Cross-link 218 218 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q04006 1 179 +Q04006 UniProtKB Chain 1 179 . . . ID=PRO_0000253834;Note=Protein UPS3%2C mitochondrial +Q04006 UniProtKB Domain 1 175 . . . Note=PRELI/MSF1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00158 +##sequence-region P12887 1 359 +P12887 UniProtKB Transit peptide 1 21 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12887 UniProtKB Chain 22 359 . . . ID=PRO_0000036085;Note=Uracil-DNA glycosylase +P12887 UniProtKB Active site 162 162 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03166 +P12887 UniProtKB Sequence conflict 173 173 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P18562 1 216 +P18562 UniProtKB Chain 1 216 . . . ID=PRO_0000120788;Note=Uracil phosphoribosyltransferase +P18562 UniProtKB Nucleotide binding 75 78 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998 +P18562 UniProtKB Region 137 145 . . . Note=5-phospho-alpha-D-ribose 1-diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998 +P18562 UniProtKB Region 207 209 . . . Note=Uracil binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998 +P18562 UniProtKB Binding site 32 32 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998 +P18562 UniProtKB Binding site 41 41 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998 +P18562 UniProtKB Binding site 77 77 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18562 UniProtKB Binding site 85 85 . . . Note=5-phospho-alpha-D-ribose 1-diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998 +P18562 UniProtKB Binding site 102 102 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998 +P18562 UniProtKB Binding site 110 110 . . . Note=5-phospho-alpha-D-ribose 1-diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998 +P18562 UniProtKB Binding site 131 131 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998 +P18562 UniProtKB Binding site 137 137 . . . Note=5-phospho-alpha-D-ribose 1-diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998 +P18562 UniProtKB Binding site 201 201 . . . Note=Ribose-5-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18562 UniProtKB Binding site 202 202 . . . Note=Uracil%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q26998 +P18562 UniProtKB Binding site 208 208 . . . Note=5-phospho-alpha-D-ribose 1-diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18562 UniProtKB Modified residue 82 82 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P18562 UniProtKB Mutagenesis 26 26 . . . Note=In FUR1-8%3B causes resistance to 5-fluorouracil (5FU). R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2189783;Dbxref=PMID:2189783 +P18562 UniProtKB Mutagenesis 99 99 . . . Note=In FUR1-5%3B causes resistance to 5-fluorouracil (5FU). R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1913872;Dbxref=PMID:1913872 +P18562 UniProtKB Mutagenesis 106 106 . . . Note=In FUR1-7%3B causes resistance to 5-fluorouracil (5FU). I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2189783;Dbxref=PMID:2189783 +P18562 UniProtKB Mutagenesis 173 173 . . . Note=In FUR1-9%3B causes resistance to 5-fluorouracil (5FU). E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2189783;Dbxref=PMID:2189783 +P18562 UniProtKB Sequence conflict 104 104 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04411 1 772 +Q04411 UniProtKB Chain 1 772 . . . ID=PRO_0000253827;Note=Uracil catabolism protein 2 +Q04411 UniProtKB DNA binding 72 101 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +##sequence-region P27515 1 501 +P27515 UniProtKB Chain 1 501 . . . ID=PRO_0000164462;Note=Uridine kinase +P27515 UniProtKB Nucleotide binding 63 70 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27515 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P27515 UniProtKB Modified residue 276 276 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P32366 1 345 +P32366 UniProtKB Chain 1 345 . . . ID=PRO_0000119360;Note=V-type proton ATPase subunit d +P32366 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.4;Dbxref=PMID:22814378 +P32366 UniProtKB Sequence conflict 32 32 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40003 1 282 +P40003 UniProtKB Chain 1 282 . . . ID=PRO_0000202618;Note=Biogenesis of lysosome-related organelles complex 1 subunit VAB2 +P40003 UniProtKB Coiled coil 64 140 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06708 1 880 +Q06708 UniProtKB Chain 1 880 . . . ID=PRO_0000065756;Note=Vacuole morphology and inheritance protein 14 +Q06708 UniProtKB Repeat 82 119 . . . Note=HEAT 1 +Q06708 UniProtKB Repeat 243 280 . . . Note=HEAT 2 +Q06708 UniProtKB Repeat 388 425 . . . Note=HEAT 3 +Q06708 UniProtKB Repeat 429 466 . . . Note=HEAT 4 +Q06708 UniProtKB Repeat 517 554 . . . Note=HEAT 5 +Q06708 UniProtKB Modified residue 767 767 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06708 UniProtKB Modified residue 805 805 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06708 UniProtKB Modified residue 867 867 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06708 UniProtKB Mutagenesis 56 56 . . . Note=Loss of interaction with ATG18 and VAC7. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19037259;Dbxref=PMID:19037259 +Q06708 UniProtKB Mutagenesis 61 61 . . . Note=Loss of interaction with ATG18 and VAC7. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19037259;Dbxref=PMID:19037259 +Q06708 UniProtKB Mutagenesis 101 101 . . . Note=Loss of interaction with ATG18 and VAC7. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19037259;Dbxref=PMID:19037259 +Q06708 UniProtKB Mutagenesis 149 149 . . . Note=Loss of interaction with ATG18%2C FAB1 and VAC7. No loss of interaction with FIG4. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19037259;Dbxref=PMID:19037259 +##sequence-region Q99385 1 411 +Q99385 UniProtKB Chain 1 411 . . . ID=PRO_0000209504;Note=Vacuolar calcium ion transporter +Q99385 UniProtKB Topological domain 1 30 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Transmembrane 31 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Topological domain 54 59 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Transmembrane 60 82 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Topological domain 83 91 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Transmembrane 92 114 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Topological domain 115 126 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Transmembrane 127 146 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Topological domain 147 160 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Transmembrane 161 183 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Topological domain 184 203 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Transmembrane 204 226 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Topological domain 227 252 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Transmembrane 253 275 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Topological domain 276 287 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Transmembrane 288 310 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Topological domain 311 319 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Transmembrane 320 342 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Topological domain 343 348 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Transmembrane 349 371 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Topological domain 372 380 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Transmembrane 381 398 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Topological domain 399 411 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99385 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +Q99385 UniProtKB Modified residue 13 13 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q99385 UniProtKB Natural variant 204 204 . . . Note=In manganese-resistant mutant 2. S->A +Q99385 UniProtKB Natural variant 208 208 . . . Note=In manganese-resistant mutant 1. L->P +Q99385 UniProtKB Natural variant 383 383 . . . Note=In VCX1-D1. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8628289;Dbxref=PMID:8628289 +Q99385 UniProtKB Helix 25 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 41 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 46 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 60 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 91 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 104 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Turn 115 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 119 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 136 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 158 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 193 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Turn 220 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 223 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 250 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 275 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 286 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 294 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 315 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 333 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 354 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +Q99385 UniProtKB Helix 378 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K1C +##sequence-region P53058 1 206 +P53058 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53058 UniProtKB Chain 20 206 . . . ID=PRO_0000202704;Note=Protein VEL1 +P53058 UniProtKB Glycosylation 26 26 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53058 UniProtKB Glycosylation 48 48 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53058 UniProtKB Glycosylation 91 91 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53058 UniProtKB Glycosylation 139 139 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53058 UniProtKB Glycosylation 152 152 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P54860 1 961 +P54860 UniProtKB Chain 1 961 . . . ID=PRO_0000194997;Note=E4 ubiquitin-protein ligase UFD2 +P54860 UniProtKB Domain 880 954 . . . Note=U-box +P54860 UniProtKB Sequence conflict 102 102 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54860 UniProtKB Sequence conflict 102 102 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54860 UniProtKB Sequence conflict 677 677 . . . Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54860 UniProtKB Sequence conflict 677 677 . . . Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54860 UniProtKB Helix 1 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Beta strand 10 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Beta strand 16 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 28 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M63 +P54860 UniProtKB Helix 36 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 39 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 56 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 80 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 84 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Beta strand 107 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 113 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 123 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 128 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 144 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Beta strand 162 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 171 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 188 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 194 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 211 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 218 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 228 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Turn 235 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 243 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 276 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 294 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Beta strand 298 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 303 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 309 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 324 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 334 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Turn 339 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Beta strand 347 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Beta strand 356 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 361 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 381 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 397 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 407 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 429 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 463 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Beta strand 485 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJ0 +P54860 UniProtKB Turn 490 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJ0 +P54860 UniProtKB Beta strand 507 509 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJ0 +P54860 UniProtKB Helix 512 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 523 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 529 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Turn 548 551 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 555 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 575 589 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 601 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 608 624 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 625 627 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Beta strand 633 635 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 637 654 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 656 668 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 670 706 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 720 754 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 756 759 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 762 780 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 782 785 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 792 795 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 799 812 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Turn 813 815 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 817 825 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Turn 827 829 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 832 842 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Beta strand 843 846 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJ0 +P54860 UniProtKB Helix 851 878 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 883 885 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Turn 888 890 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Beta strand 895 899 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Turn 901 903 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Beta strand 906 908 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 909 916 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Turn 923 925 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 931 933 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P54860 UniProtKB Helix 938 952 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +##sequence-region P32772 1 223 +P32772 UniProtKB Chain 1 223 . . . ID=PRO_0000065718;Note=Protein UGX2 +##sequence-region Q08926 1 304 +Q08926 UniProtKB Chain 1 304 . . . ID=PRO_0000270927;Note=ULP1-interacting protein 4 +Q08926 UniProtKB Modified residue 140 140 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17761666,PMID:18407956,PMID:19779198 +Q08926 UniProtKB Modified residue 185 185 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +Q08926 UniProtKB Modified residue 205 205 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17761666,PMID:18407956,PMID:19779198 +##sequence-region P43604 1 169 +P43604 UniProtKB Chain 1 169 . . . ID=PRO_0000202692;Note=Unfolded protein response-inducible protein 1 +##sequence-region P39001 1 836 +P39001 UniProtKB Chain 1 836 . . . ID=PRO_0000114987;Note=Transcriptional regulatory protein UME6 +P39001 UniProtKB DNA binding 771 798 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P39001 UniProtKB Region 508 594 . . . Note=SIN3-binding +P39001 UniProtKB Modified residue 114 114 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39001 UniProtKB Modified residue 141 141 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P39001 UniProtKB Modified residue 150 150 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P39001 UniProtKB Modified residue 228 228 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39001 UniProtKB Modified residue 316 316 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39001 UniProtKB Modified residue 318 318 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39001 UniProtKB Modified residue 645 645 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39001 UniProtKB Mutagenesis 99 109 . . . Note=Impairs meiotic genes expression%2C sporulation and interactions with IME1 and RIM11%2C and abolishes phosphorylation. TPVHTPSGSPS->APVHAPAGAPA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372955;Dbxref=PMID:9372955 +P39001 UniProtKB Mutagenesis 99 107 . . . Note=Impairs meiotic genes expression and sporulation%2C reduces the interaction with IME1%2C and abolishes phosphorylation. TPVHTPSGS->APVHAPSGA +P39001 UniProtKB Mutagenesis 99 99 . . . Note=Impairs meiotic genes expression and sporulation%2C reduces interactions with IME1 and RIM11%2C and reduces phosphorylation. T->N%2CA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10891485,ECO:0000269|PubMed:9372955;Dbxref=PMID:10891485,PMID:9372955 +P39001 UniProtKB Mutagenesis 103 103 . . . Note=Impairs meiotic genes expression and sporulation%2C reduces interaction with IME%2C and reduces phosphorylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10891485;Dbxref=PMID:10891485 +P39001 UniProtKB Mutagenesis 107 107 . . . Note=Impairs meiotic genes expression and sporulation%2C reduces interaction with IME%2C and reduces phosphorylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10891485;Dbxref=PMID:10891485 +P39001 UniProtKB Mutagenesis 523 523 . . . Note=Impairs SIN3-binding and gene repression activity. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238941;Dbxref=PMID:11238941 +P39001 UniProtKB Mutagenesis 524 524 . . . Note=Impairs gene repression activity. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238941;Dbxref=PMID:11238941 +P39001 UniProtKB Mutagenesis 525 525 . . . Note=Impairs gene repression activity. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238941;Dbxref=PMID:11238941 +P39001 UniProtKB Mutagenesis 526 526 . . . Note=Impairs gene repression activity. V->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238941;Dbxref=PMID:11238941 +P39001 UniProtKB Mutagenesis 527 527 . . . Note=Impairs SIN3-binding and gene repression activity. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238941;Dbxref=PMID:11238941 +P39001 UniProtKB Mutagenesis 528 528 . . . Note=Impairs SIN3-binding and gene repression activity. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238941;Dbxref=PMID:11238941 +P39001 UniProtKB Mutagenesis 530 530 . . . Note=Impairs SIN3-binding and gene repression activity. M->T%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238941;Dbxref=PMID:11238941 +P39001 UniProtKB Mutagenesis 635 635 . . . Note=Impairs gene repression activity. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238941;Dbxref=PMID:11238941 +P39001 UniProtKB Sequence conflict 101 101 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39001 UniProtKB Sequence conflict 363 363 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39001 UniProtKB Sequence conflict 443 443 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39001 UniProtKB Sequence conflict 465 465 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P48412 1 387 +P48412 UniProtKB Chain 1 387 . . . ID=PRO_0000215298;Note=Nonsense-mediated mRNA decay protein 3 +P48412 UniProtKB Motif 15 31 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48412 UniProtKB Motif 58 75 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48412 UniProtKB Motif 284 300 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48412 UniProtKB Sequence conflict 26 26 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P35200 1 230 +P35200 UniProtKB Chain 1 230 . . . ID=PRO_0000096596;Note=Protein UPS2%2C mitochondrial +P35200 UniProtKB Domain 1 175 . . . Note=PRELI/MSF1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00158 +##sequence-region Q12208 1 290 +Q12208 UniProtKB Chain 1 290 . . . ID=PRO_0000262872;Note=U6 snRNA phosphodiesterase +Q12208 UniProtKB Active site 133 133 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12208 UniProtKB Active site 231 231 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12208 UniProtKB Mutagenesis 133 133 . . . Note=Cannot restore cell growth in USB1 depleted cells. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22899009,ECO:0000269|PubMed:23190533;Dbxref=PMID:22899009,PMID:23190533 +Q12208 UniProtKB Mutagenesis 231 231 . . . Note=Cannot restore cell growth in USB1 depleted cells. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22899009,ECO:0000269|PubMed:23190533;Dbxref=PMID:22899009,PMID:23190533 +##sequence-region P34247 1 250 +P34247 UniProtKB Chain 1 250 . . . ID=PRO_0000211052;Note=U3 small nucleolar RNA-associated protein 11 +##sequence-region Q02931 1 896 +Q02931 UniProtKB Chain 1 896 . . . ID=PRO_0000051088;Note=NET1-associated nuclear protein 1 +Q02931 UniProtKB Repeat 295 334 . . . Note=WD 1 +Q02931 UniProtKB Repeat 490 542 . . . Note=WD 2 +Q02931 UniProtKB Repeat 552 595 . . . Note=WD 3 +Q02931 UniProtKB Repeat 605 645 . . . Note=WD 4 +##sequence-region P40055 1 554 +P40055 UniProtKB Chain 1 554 . . . ID=PRO_0000051319;Note=U3 small nucleolar RNA-associated protein 7 +P40055 UniProtKB Repeat 108 149 . . . Note=WD 1 +P40055 UniProtKB Repeat 230 269 . . . Note=WD 2 +P40055 UniProtKB Repeat 272 311 . . . Note=WD 3 +P40055 UniProtKB Repeat 314 351 . . . Note=WD 4 +##sequence-region P32630 1 166 +P32630 UniProtKB Chain 1 166 . . . ID=PRO_0000065747;Note=Protein UTR5 +P32630 UniProtKB Sequence conflict 1 20 . . . Note=MSRYGKNLVHYIIVEHDDQR->MRDSNVKISVFPCALYNRGNTTIN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39111 1 118 +P39111 UniProtKB Chain 1 118 . . . ID=PRO_0000144812;Note=V-type proton ATPase subunit F +P39111 UniProtKB Helix 2 4 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RND +P39111 UniProtKB Beta strand 7 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9 +P39111 UniProtKB Helix 14 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9 +P39111 UniProtKB Turn 23 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9 +P39111 UniProtKB Turn 30 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9 +P39111 UniProtKB Beta strand 37 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9 +P39111 UniProtKB Turn 42 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9 +P39111 UniProtKB Helix 47 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9 +P39111 UniProtKB Beta strand 62 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9 +P39111 UniProtKB Helix 71 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9 +P39111 UniProtKB Helix 78 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9 +P39111 UniProtKB Beta strand 86 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IX9 +P39111 UniProtKB Helix 108 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RND +##sequence-region Q12063 1 375 +Q12063 UniProtKB Chain 1 375 . . . ID=PRO_0000242134;Note=Dehydrodolichyl diphosphate synthase complex subunit NUS1 +Q12063 UniProtKB Transmembrane 97 119 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12063 UniProtKB Mutagenesis 372 372 . . . Note=Loss of function. N->H +##sequence-region P34241 1 1764 +P34241 UniProtKB Chain 1 1764 . . . ID=PRO_0000203190;Note=Nucleolar pre-ribosomal-associated protein 1 +##sequence-region P23202 1 354 +P23202 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P23202 UniProtKB Chain 2 354 . . . ID=PRO_0000186013;Note=Transcriptional regulator URE2 +P23202 UniProtKB Domain 112 196 . . . Note=GST N-terminal +P23202 UniProtKB Domain 205 354 . . . Note=GST C-terminal +P23202 UniProtKB Region 2 89 . . . Note=Prion domain (PrD) +P23202 UniProtKB Region 164 165 . . . Note=Glutathione binding +P23202 UniProtKB Region 180 181 . . . Note=Glutathione binding +P23202 UniProtKB Binding site 124 124 . . . Note=Glutathione;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11695904;Dbxref=PMID:11695904 +P23202 UniProtKB Binding site 151 151 . . . Note=Glutathione;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11695904;Dbxref=PMID:11695904 +P23202 UniProtKB Modified residue 2 2 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P23202 UniProtKB Mutagenesis 122 122 . . . Note=Reduces glutaredoxin activity. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19321443;Dbxref=PMID:19321443 +P23202 UniProtKB Mutagenesis 124 124 . . . Note=Abolishes glutaredoxin activity. N->A%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19321443;Dbxref=PMID:19321443 +P23202 UniProtKB Mutagenesis 313 313 . . . Note=Destroys protein function. F->S +P23202 UniProtKB Helix 101 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Beta strand 111 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Helix 123 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Beta strand 139 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Turn 146 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Helix 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Helix 154 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Beta strand 167 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Turn 171 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Beta strand 176 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Helix 181 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Helix 206 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Helix 224 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Beta strand 237 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6W +P23202 UniProtKB Helix 242 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Turn 276 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0B +P23202 UniProtKB Helix 279 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6W +P23202 UniProtKB Beta strand 285 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6W +P23202 UniProtKB Helix 289 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6W +P23202 UniProtKB Helix 293 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6W +P23202 UniProtKB Helix 308 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Helix 314 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Helix 320 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Helix 327 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Helix 332 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +P23202 UniProtKB Helix 345 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K0D +##sequence-region Q03714 1 838 +Q03714 UniProtKB Chain 1 838 . . . ID=PRO_0000114926;Note=U1 SNP1-associating protein 1 +Q03714 UniProtKB Topological domain 1 536 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03714 UniProtKB Transmembrane 537 559 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03714 UniProtKB Topological domain 560 563 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03714 UniProtKB Transmembrane 564 583 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03714 UniProtKB Topological domain 584 838 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03714 UniProtKB Domain 259 318 . . . Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 +Q03714 UniProtKB Region 31 240 . . . Note=Required for ERAD-L function +Q03714 UniProtKB Region 319 418 . . . Note=Important for HRD1 oligomer formation +Q03714 UniProtKB Region 345 535 . . . Note=Interaction with HRD1 +Q03714 UniProtKB Region 437 490 . . . Note=Required for ERAD-L function and HRD1 oligomer formation +Q03714 UniProtKB Region 584 838 . . . Note=Interaction with DER1 +Q03714 UniProtKB Modified residue 374 374 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03714 UniProtKB Modified residue 376 376 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q03714 UniProtKB Modified residue 379 379 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P41807 1 478 +P41807 UniProtKB Chain 1 478 . . . ID=PRO_0000124202;Note=V-type proton ATPase subunit H +P41807 UniProtKB Helix 11 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 27 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 38 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 77 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 90 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Beta strand 107 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 111 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 123 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 136 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Turn 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 158 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 168 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 180 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 197 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 207 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 239 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 257 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 268 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 284 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Beta strand 299 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 305 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 318 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 333 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 355 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 372 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 377 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 385 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 390 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 393 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 414 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 435 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 438 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 446 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +P41807 UniProtKB Helix 459 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HO8 +##sequence-region P25515 1 160 +P25515 UniProtKB Chain 1 160 . . . ID=PRO_0000071762;Note=V-type proton ATPase subunit c +P25515 UniProtKB Topological domain 1 8 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25515 UniProtKB Transmembrane 9 31 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25515 UniProtKB Topological domain 32 53 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25515 UniProtKB Transmembrane 54 74 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25515 UniProtKB Topological domain 75 90 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25515 UniProtKB Transmembrane 91 112 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25515 UniProtKB Topological domain 113 124 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25515 UniProtKB Transmembrane 125 150 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25515 UniProtKB Topological domain 151 160 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25515 UniProtKB Site 137 137 . . . Note=Essential for proton translocation +P25515 UniProtKB Mutagenesis 137 137 . . . Note=Partial inactivation. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1825730;Dbxref=PMID:1825730 +P25515 UniProtKB Mutagenesis 137 137 . . . Note=Inactivation. E->Q%2CV%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1825730;Dbxref=PMID:1825730 +##sequence-region P36172 1 582 +P36172 UniProtKB Chain 1 582 . . . ID=PRO_0000173427;Note=Vacuolar basic amino acid transporter 5 +P36172 UniProtKB Topological domain 1 44 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36172 UniProtKB Transmembrane 45 65 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36172 UniProtKB Topological domain 66 80 . . . Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36172 UniProtKB Transmembrane 81 101 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36172 UniProtKB Topological domain 102 104 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36172 UniProtKB Transmembrane 105 125 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36172 UniProtKB Topological domain 126 132 . . . Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36172 UniProtKB Transmembrane 133 153 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36172 UniProtKB Topological domain 154 160 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36172 UniProtKB Transmembrane 161 181 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36172 UniProtKB Topological domain 182 191 . . . Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36172 UniProtKB Transmembrane 192 212 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36172 UniProtKB Topological domain 213 256 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36172 UniProtKB Transmembrane 257 277 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36172 UniProtKB Topological domain 278 287 . . . Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36172 UniProtKB Transmembrane 288 308 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36172 UniProtKB Topological domain 309 329 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36172 UniProtKB Transmembrane 330 350 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36172 UniProtKB Topological domain 351 372 . . . Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36172 UniProtKB Transmembrane 373 393 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36172 UniProtKB Topological domain 394 401 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36172 UniProtKB Transmembrane 402 422 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36172 UniProtKB Topological domain 423 430 . . . Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36172 UniProtKB Transmembrane 431 451 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36172 UniProtKB Topological domain 452 469 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36172 UniProtKB Transmembrane 470 492 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36172 UniProtKB Topological domain 493 539 . . . Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36172 UniProtKB Transmembrane 540 560 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36172 UniProtKB Topological domain 561 582 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36172 UniProtKB Glycosylation 70 70 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36172 UniProtKB Glycosylation 423 423 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P04840 1 283 +P04840 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7 +P04840 UniProtKB Chain 2 283 . . . ID=PRO_0000050524;Note=Mitochondrial outer membrane protein porin 1 +P04840 UniProtKB Modified residue 109 109 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:19779198;Dbxref=PMID:17761666,PMID:19779198 +P04840 UniProtKB Modified residue 117 117 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P04840 UniProtKB Mutagenesis 19 19 . . . Note=2.5-fold reduction in steepness of voltage dependence. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.9 +P04840 UniProtKB Mutagenesis 51 51 . . . Note=2-fold increase in steepness of voltage dependence. D->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.9 +P04840 UniProtKB Mutagenesis 61 61 . . . Note=Alters the selectivity of VDAC. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2478533;Dbxref=PMID:2478533 +P04840 UniProtKB Sequence conflict 118 118 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04840 UniProtKB Sequence conflict 118 118 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04840 UniProtKB Sequence conflict 203 207 . . . Note=GAKAT->AKATM;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40157 1 782 +P40157 UniProtKB Chain 1 782 . . . ID=PRO_0000065827;Note=Vacuolar import and degradation protein 27 +P40157 UniProtKB Modified residue 170 170 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40157 UniProtKB Modified residue 195 195 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40157 UniProtKB Modified residue 196 196 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40157 UniProtKB Modified residue 222 222 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P40157 UniProtKB Modified residue 486 486 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q06685 1 1146 +Q06685 UniProtKB Chain 1 1146 . . . ID=PRO_0000270924;Note=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase +Q06685 UniProtKB Nucleotide binding 402 405 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314 +Q06685 UniProtKB Nucleotide binding 412 414 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314 +Q06685 UniProtKB Nucleotide binding 487 489 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314 +Q06685 UniProtKB Region 197 198 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314 +Q06685 UniProtKB Region 377 378 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314 +Q06685 UniProtKB Region 492 495 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314 +Q06685 UniProtKB Region 530 597 . . . Note=Polyphosphoinositide-binding domain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6PFW1 +Q06685 UniProtKB Binding site 278 278 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314 +Q06685 UniProtKB Binding site 351 351 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314 +Q06685 UniProtKB Binding site 358 358 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314 +Q06685 UniProtKB Binding site 377 377 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314 +Q06685 UniProtKB Binding site 414 414 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314 +Q06685 UniProtKB Binding site 428 428 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314 +Q06685 UniProtKB Binding site 430 430 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314 +Q06685 UniProtKB Binding site 475 475 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43314 +Q06685 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06685 UniProtKB Modified residue 54 54 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q06685 UniProtKB Modified residue 77 77 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06685 UniProtKB Modified residue 895 895 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06685 UniProtKB Modified residue 1107 1107 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06685 UniProtKB Mutagenesis 487 487 . . . Note=Abolishes enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17412958;Dbxref=PMID:17412958 +Q06685 UniProtKB Mutagenesis 548 548 . . . Note=Does not affect enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17412958;Dbxref=PMID:17412958 +##sequence-region Q04311 1 632 +Q04311 UniProtKB Chain 1 632 . . . ID=PRO_0000244435;Note=Protein VMS1 +Q04311 UniProtKB Repeat 470 500 . . . Note=ANK 1 +Q04311 UniProtKB Repeat 504 530 . . . Note=ANK 2 +Q04311 UniProtKB Zinc finger 72 96 . . . Note=C2H2-type +Q04311 UniProtKB Coiled coil 544 582 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04311 UniProtKB Coiled coil 608 632 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04311 UniProtKB Sequence conflict 170 170 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38067 1 497 +P38067 UniProtKB Chain 1 497 . . . ID=PRO_0000056568;Note=Succinate-semialdehyde dehydrogenase [NADP(+)] +P38067 UniProtKB Active site 264 264 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007 +P38067 UniProtKB Active site 298 298 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007 +P38067 UniProtKB Site 164 164 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q04179 1 340 +Q04179 UniProtKB Chain 1 340 . . . ID=PRO_0000206812;Note=Uridine nucleosidase +Q04179 UniProtKB Active site 254 254 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04179 UniProtKB Mutagenesis 254 254 . . . Note=Reduces the Vmax 30-fold%2C but does not change the KM in a uridine hydrolase assay. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12111094;Dbxref=PMID:12111094 +##sequence-region Q3E7B6 1 73 +Q3E7B6 UniProtKB Chain 1 73 . . . ID=PRO_0000071737;Note=V-type proton ATPase subunit e +Q3E7B6 UniProtKB Transmembrane 4 24 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E7B6 UniProtKB Transmembrane 36 56 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39968 1 578 +P39968 UniProtKB Initiator methionine 1 1 . . . Note=Removed +P39968 UniProtKB Chain 2 578 . . . ID=PRO_0000064302;Note=Vacuolar protein 8 +P39968 UniProtKB Repeat 37 75 . . . Note=ARM 1 +P39968 UniProtKB Repeat 76 114 . . . Note=ARM 2 +P39968 UniProtKB Repeat 116 155 . . . Note=ARM 3 +P39968 UniProtKB Repeat 157 196 . . . Note=ARM 4 +P39968 UniProtKB Repeat 198 237 . . . Note=ARM 5 +P39968 UniProtKB Repeat 239 280 . . . Note=ARM 6 +P39968 UniProtKB Repeat 282 321 . . . Note=ARM 7 +P39968 UniProtKB Repeat 323 363 . . . Note=ARM 8 +P39968 UniProtKB Repeat 407 446 . . . Note=ARM 9 +P39968 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39968 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P39968 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9490720;Dbxref=PMID:9490720 +P39968 UniProtKB Lipidation 4 4 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9490720;Dbxref=PMID:9490720 +P39968 UniProtKB Lipidation 5 5 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9490720;Dbxref=PMID:9490720 +P39968 UniProtKB Lipidation 7 7 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9490720;Dbxref=PMID:9490720 +P39968 UniProtKB Cross-link 77 77 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P39968 UniProtKB Cross-link 515 515 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P39968 UniProtKB Mutagenesis 4 7 . . . Note=In VAC8-3%3B not palmitoylated. CCSC->GTSS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9490720;Dbxref=PMID:9490720 +##sequence-region P32912 1 316 +P32912 UniProtKB Chain 1 316 . . . ID=PRO_0000065760;Note=Vacuolar morphogenesis protein 7 +P32912 UniProtKB Domain 1 124 . . . Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147 +P32912 UniProtKB Domain 250 312 . . . Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202 +P32912 UniProtKB Coiled coil 168 186 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32912 UniProtKB Beta strand 16 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KMD +P32912 UniProtKB Beta strand 27 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KMD +P32912 UniProtKB Beta strand 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KMD +P32912 UniProtKB Helix 42 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KMD +P32912 UniProtKB Helix 82 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KMD +P32912 UniProtKB Helix 92 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KMD +P32912 UniProtKB Helix 107 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KMD +P32912 UniProtKB Helix 112 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KMD +##sequence-region Q05934 1 901 +Q05934 UniProtKB Chain 1 901 . . . ID=PRO_0000270928;Note=Vacuolar import and degradation protein 22 +Q05934 UniProtKB Transmembrane 381 401 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05934 UniProtKB Zinc finger 66 122 . . . Note=BED-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00027 +Q05934 UniProtKB Compositional bias 643 722 . . . Note=Asn-rich +Q05934 UniProtKB Glycosylation 21 21 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05934 UniProtKB Glycosylation 242 242 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05934 UniProtKB Glycosylation 291 291 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05934 UniProtKB Glycosylation 540 540 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05934 UniProtKB Glycosylation 645 645 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05934 UniProtKB Glycosylation 649 649 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05934 UniProtKB Glycosylation 652 652 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05934 UniProtKB Glycosylation 662 662 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05934 UniProtKB Glycosylation 669 669 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05934 UniProtKB Glycosylation 673 673 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05934 UniProtKB Glycosylation 688 688 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05934 UniProtKB Glycosylation 722 722 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12241 1 283 +Q12241 UniProtKB Chain 1 283 . . . ID=PRO_0000210280;Note=Syntaxin VAM3 +Q12241 UniProtKB Topological domain 1 261 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12241 UniProtKB Transmembrane 262 282 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12241 UniProtKB Topological domain 283 283 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12241 UniProtKB Domain 190 252 . . . Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202 +Q12241 UniProtKB Coiled coil 28 48 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12241 UniProtKB Coiled coil 84 111 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12241 UniProtKB Coiled coil 169 189 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12241 UniProtKB Compositional bias 174 179 . . . Note=Poly-Gln +Q12241 UniProtKB Compositional bias 268 271 . . . Note=Poly-Ile +Q12241 UniProtKB Helix 25 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HS7 +Q12241 UniProtKB Beta strand 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HS7 +Q12241 UniProtKB Helix 58 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HS7 +Q12241 UniProtKB Helix 68 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HS7 +Q12241 UniProtKB Helix 84 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HS7 +Q12241 UniProtKB Helix 89 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HS7 +##sequence-region P23642 1 535 +P23642 UniProtKB Chain 1 535 . . . ID=PRO_0000193672;Note=Mannan polymerase I complex VAN1 subunit +P23642 UniProtKB Topological domain 1 64 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23642 UniProtKB Transmembrane 65 81 . . . Note=Helical%3B Signal-anchor for type II membrane protein +P23642 UniProtKB Topological domain 82 535 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23642 UniProtKB Modified residue 25 25 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P23642 UniProtKB Glycosylation 215 215 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23642 UniProtKB Glycosylation 251 251 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23642 UniProtKB Mutagenesis 361 361 . . . Note=Reduced activity of the M-Pol I complex. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12235155;Dbxref=PMID:12235155 +P23642 UniProtKB Sequence conflict 87 87 . . . Note=M->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23642 UniProtKB Sequence conflict 140 140 . . . Note=Q->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23642 UniProtKB Sequence conflict 281 281 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32610 1 256 +P32610 UniProtKB Chain 1 256 . . . ID=PRO_0000144244;Note=V-type proton ATPase subunit D +P32610 UniProtKB Helix 29 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RND +P32610 UniProtKB Helix 79 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RND +P32610 UniProtKB Beta strand 91 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RND +P32610 UniProtKB Beta strand 104 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RND +P32610 UniProtKB Beta strand 115 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RND +P32610 UniProtKB Helix 128 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RND +P32610 UniProtKB Helix 177 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RND +##sequence-region P48836 1 114 +P48836 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P48836 UniProtKB Chain 2 114 . . . ID=PRO_0000192916;Note=V-type proton ATPase subunit G +P48836 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P48836 UniProtKB Helix 4 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA +P48836 UniProtKB Helix 70 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DL0 +P48836 UniProtKB Beta strand 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA +P48836 UniProtKB Helix 77 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA +P48836 UniProtKB Helix 91 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA +##sequence-region P32319 1 1579 +P32319 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32319 UniProtKB Chain 22 1579 . . . ID=PRO_0000022037;Note=Vacuolar protein sorting/targeting protein VPS10 +P32319 UniProtKB Topological domain 22 1397 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32319 UniProtKB Transmembrane 1398 1414 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32319 UniProtKB Topological domain 1415 1579 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32319 UniProtKB Repeat 57 68 . . . Note=BNR 1 +P32319 UniProtKB Repeat 101 112 . . . Note=BNR 2 +P32319 UniProtKB Repeat 179 190 . . . Note=BNR 3 +P32319 UniProtKB Repeat 415 426 . . . Note=BNR 4 +P32319 UniProtKB Repeat 487 498 . . . Note=BNR 5 +P32319 UniProtKB Repeat 533 544 . . . Note=BNR 6 +P32319 UniProtKB Repeat 764 775 . . . Note=BNR 7 +P32319 UniProtKB Repeat 861 872 . . . Note=BNR 8 +P32319 UniProtKB Repeat 1143 1154 . . . Note=BNR 9 +P32319 UniProtKB Repeat 1184 1195 . . . Note=BNR 10 +P32319 UniProtKB Glycosylation 96 96 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32319 UniProtKB Glycosylation 170 170 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32319 UniProtKB Glycosylation 447 447 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32319 UniProtKB Glycosylation 793 793 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32319 UniProtKB Glycosylation 1010 1010 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32319 UniProtKB Glycosylation 1303 1303 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32319 UniProtKB Sequence conflict 19 19 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32319 UniProtKB Sequence conflict 38 38 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32319 UniProtKB Sequence conflict 54 54 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32319 UniProtKB Sequence conflict 74 74 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32319 UniProtKB Sequence conflict 94 99 . . . Note=AMNGSY->SMYESR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32319 UniProtKB Sequence conflict 119 126 . . . Note=GESISPRE->EKNISSRG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32319 UniProtKB Sequence conflict 152 153 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32319 UniProtKB Sequence conflict 165 167 . . . Note=QFE->APV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32319 UniProtKB Sequence conflict 202 202 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32319 UniProtKB Sequence conflict 214 214 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32319 UniProtKB Sequence conflict 283 283 . . . Note=L->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32319 UniProtKB Sequence conflict 378 378 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32319 UniProtKB Sequence conflict 410 410 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32319 UniProtKB Sequence conflict 426 426 . . . Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32319 UniProtKB Sequence conflict 774 774 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32319 UniProtKB Sequence conflict 1089 1089 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32319 UniProtKB Sequence conflict 1266 1266 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32319 UniProtKB Sequence conflict 1476 1476 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32319 UniProtKB Sequence conflict 1557 1557 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32913 1 551 +P32913 UniProtKB Chain 1 551 . . . ID=PRO_0000065892;Note=Vacuolar protein sorting-associated protein 17 +P32913 UniProtKB Domain 108 227 . . . Note=PX +P32913 UniProtKB Coiled coil 359 385 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32913 UniProtKB Modified residue 544 544 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32913 UniProtKB Sequence conflict 25 25 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32913 UniProtKB Sequence conflict 30 30 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32913 UniProtKB Sequence conflict 62 62 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32913 UniProtKB Sequence conflict 68 68 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32913 UniProtKB Sequence conflict 90 90 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32913 UniProtKB Sequence conflict 402 402 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04272 1 221 +Q04272 UniProtKB Initiator methionine 1 1 . . . Note=Removed +Q04272 UniProtKB Chain 2 221 . . . ID=PRO_0000211515;Note=Vacuolar protein sorting-associated protein 20 +Q04272 UniProtKB Coiled coil 72 178 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04272 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9748261;Dbxref=PMID:9748261 +Q04272 UniProtKB Mutagenesis 2 2 . . . Note=Loss of membrane association. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12194857;Dbxref=PMID:12194857 +Q04272 UniProtKB Helix 171 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FVL +##sequence-region Q05919 1 439 +Q05919 UniProtKB Chain 1 439 . . . ID=PRO_0000065900;Note=Vacuolar protein sorting-associated protein 38 +Q05919 UniProtKB Coiled coil 223 255 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05919 UniProtKB Sequence conflict 55 55 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39702 1 1274 +P39702 UniProtKB Chain 1 1274 . . . ID=PRO_0000055901;Note=Vacuolar protein sorting-associated protein 8 +P39702 UniProtKB Repeat 75 119 . . . Note=WD 1 +P39702 UniProtKB Repeat 131 170 . . . Note=WD 2 +P39702 UniProtKB Repeat 193 233 . . . Note=WD 3 +P39702 UniProtKB Repeat 507 665 . . . Note=CHCR 1 +P39702 UniProtKB Repeat 915 1092 . . . Note=CHCR 2 +P39702 UniProtKB Zinc finger 1198 1266 . . . Note=RING-type%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +P39702 UniProtKB Compositional bias 40 43 . . . Note=Poly-Ser +P39702 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P32842 1 164 +P32842 UniProtKB Chain 1 164 . . . ID=PRO_0000071788;Note=V-type proton ATPase subunit c' +P32842 UniProtKB Topological domain 1 14 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32842 UniProtKB Transmembrane 15 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32842 UniProtKB Topological domain 38 59 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32842 UniProtKB Transmembrane 60 80 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32842 UniProtKB Topological domain 81 98 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32842 UniProtKB Transmembrane 99 120 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32842 UniProtKB Topological domain 121 132 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32842 UniProtKB Transmembrane 133 158 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32842 UniProtKB Topological domain 159 164 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32842 UniProtKB Site 145 145 . . . Note=Essential for proton translocation +P32842 UniProtKB Mutagenesis 145 145 . . . Note=Partial inactivation. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9030535;Dbxref=PMID:9030535 +P32842 UniProtKB Mutagenesis 145 145 . . . Note=Inactivation. E->L%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9030535;Dbxref=PMID:9030535 +P32842 UniProtKB Sequence conflict 27 35 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38329 1 1120 +P38329 UniProtKB Chain 1 1120 . . . ID=PRO_0000202520;Note=Vacuolar cation-chloride cotransporter 1 +P38329 UniProtKB Topological domain 1 62 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P38329 UniProtKB Transmembrane 63 83 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38329 UniProtKB Topological domain 84 85 . . . Note=Vacuolar;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P38329 UniProtKB Transmembrane 86 106 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38329 UniProtKB Topological domain 107 145 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P38329 UniProtKB Transmembrane 146 166 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38329 UniProtKB Topological domain 167 193 . . . Note=Vacuolar;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P38329 UniProtKB Transmembrane 194 214 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38329 UniProtKB Topological domain 215 221 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P38329 UniProtKB Transmembrane 222 242 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38329 UniProtKB Topological domain 243 283 . . . Note=Vacuolar;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P38329 UniProtKB Transmembrane 284 304 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38329 UniProtKB Topological domain 305 317 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P38329 UniProtKB Transmembrane 318 338 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38329 UniProtKB Topological domain 339 360 . . . Note=Vacuolar;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P38329 UniProtKB Transmembrane 361 381 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38329 UniProtKB Topological domain 382 393 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P38329 UniProtKB Transmembrane 394 414 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38329 UniProtKB Topological domain 415 430 . . . Note=Vacuolar;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P38329 UniProtKB Transmembrane 431 451 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38329 UniProtKB Topological domain 452 462 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P38329 UniProtKB Transmembrane 463 482 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38329 UniProtKB Topological domain 483 487 . . . Note=Vacuolar;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P38329 UniProtKB Transmembrane 488 506 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38329 UniProtKB Topological domain 507 1120 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +P38329 UniProtKB Modified residue 34 34 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38329 UniProtKB Modified residue 654 654 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38329 UniProtKB Modified residue 915 915 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38329 UniProtKB Modified residue 918 918 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40522 1 640 +P40522 UniProtKB Chain 1 640 . . . ID=PRO_0000202988;Note=Transcription factor VHR1 +P40522 UniProtKB Modified residue 409 409 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region Q08438 1 674 +Q08438 UniProtKB Chain 1 674 . . . ID=PRO_0000182038;Note=Phosphopantothenoylcysteine decarboxylase subunit VHS3 +Q08438 UniProtKB Compositional bias 580 661 . . . Note=Asp/Glu-rich (highly acidic) +Q08438 UniProtKB Modified residue 90 90 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +Q08438 UniProtKB Mutagenesis 459 459 . . . Note=Does not strongly affect the phosphatase inhibitor function but abolishes PPCDC activity. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15192104,ECO:0000269|PubMed:19915539;Dbxref=PMID:15192104,PMID:19915539 +##sequence-region P53285 1 467 +P53285 UniProtKB Chain 1 467 . . . ID=PRO_0000065906;Note=Vacuolar protein sorting-associated protein 62 +P53285 UniProtKB Transmembrane 17 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53285 UniProtKB Glycosylation 74 74 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53285 UniProtKB Glycosylation 145 145 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53142 1 486 +P53142 UniProtKB Chain 1 486 . . . ID=PRO_0000050462;Note=Vacuolar protein sorting-associated protein 73 +P53142 UniProtKB Topological domain 1 26 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Transmembrane 27 47 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Topological domain 48 90 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Transmembrane 91 111 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Topological domain 112 119 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Transmembrane 120 140 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Topological domain 141 146 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Transmembrane 147 167 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Topological domain 168 178 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Transmembrane 179 199 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Topological domain 200 208 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Transmembrane 209 229 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Topological domain 230 305 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Transmembrane 306 326 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Topological domain 327 342 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Transmembrane 343 363 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Topological domain 364 366 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Transmembrane 367 387 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Topological domain 388 396 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Transmembrane 397 417 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Topological domain 418 432 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Transmembrane 433 453 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Topological domain 454 454 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Transmembrane 455 475 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53142 UniProtKB Topological domain 476 486 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06525 1 465 +Q06525 UniProtKB Chain 1 465 . . . ID=PRO_0000244477;Note=Pre-mRNA-splicing factor URN1 +Q06525 UniProtKB Domain 1 32 . . . Note=WW;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00224 +Q06525 UniProtKB Domain 212 266 . . . Note=FF +Q06525 UniProtKB Compositional bias 119 192 . . . Note=Glu-rich +Q06525 UniProtKB Modified residue 150 150 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06525 UniProtKB Helix 216 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JUC +Q06525 UniProtKB Turn 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JUC +Q06525 UniProtKB Helix 235 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JUC +Q06525 UniProtKB Beta strand 242 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JUC +Q06525 UniProtKB Helix 247 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JUC +Q06525 UniProtKB Helix 253 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JUC +##sequence-region Q12132 1 391 +Q12132 UniProtKB Chain 1 391 . . . ID=PRO_0000255973;Note=Nutrient and stress factor 1 +Q12132 UniProtKB Zinc finger 41 66 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q12132 UniProtKB Zinc finger 72 95 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q12132 UniProtKB Compositional bias 102 134 . . . Note=Ser-rich +Q12132 UniProtKB Compositional bias 185 197 . . . Note=Poly-Gln +Q12132 UniProtKB Modified residue 162 162 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12132 UniProtKB Modified residue 163 163 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P53950 1 1165 +P53950 UniProtKB Chain 1 1165 . . . ID=PRO_0000065757;Note=Vacuolar segregation protein 7 +P53950 UniProtKB Topological domain 1 919 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53950 UniProtKB Transmembrane 920 940 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53950 UniProtKB Topological domain 941 1165 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53950 UniProtKB Compositional bias 277 412 . . . Note=Asn-rich +P53950 UniProtKB Compositional bias 469 485 . . . Note=Gln-rich +P53950 UniProtKB Compositional bias 1085 1119 . . . Note=Asp-rich +P53950 UniProtKB Modified residue 164 164 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53950 UniProtKB Glycosylation 1020 1020 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53950 UniProtKB Glycosylation 1099 1099 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40041 1 505 +P40041 UniProtKB Chain 1 505 . . . ID=PRO_0000202632;Note=Transcription factor VHR2 +##sequence-region P23968 1 213 +P23968 UniProtKB Chain 1 213 . . . ID=PRO_0000071780;Note=V-type proton ATPase subunit c'' +P23968 UniProtKB Topological domain 1 14 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23968 UniProtKB Transmembrane 15 35 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23968 UniProtKB Topological domain 36 61 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23968 UniProtKB Transmembrane 62 82 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23968 UniProtKB Topological domain 83 100 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23968 UniProtKB Transmembrane 101 121 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23968 UniProtKB Topological domain 122 145 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23968 UniProtKB Transmembrane 146 167 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23968 UniProtKB Topological domain 168 179 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23968 UniProtKB Transmembrane 180 205 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23968 UniProtKB Topological domain 206 213 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23968 UniProtKB Site 108 108 . . . Note=Essential for proton translocation +P23968 UniProtKB Mutagenesis 108 108 . . . Note=Partial inactivation. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9030535;Dbxref=PMID:9030535 +P23968 UniProtKB Mutagenesis 108 108 . . . Note=Inactivation. E->L%2CQ%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9030535;Dbxref=PMID:9030535 +##sequence-region P40478 1 281 +P40478 UniProtKB Chain 1 281 . . . ID=PRO_0000050525;Note=Mitochondrial outer membrane protein porin 2 +##sequence-region O13549 1 108 +O13549 UniProtKB Chain 1 108 . . . ID=PRO_0000299780;Note=Uncharacterized protein VPS63 +##sequence-region P47161 1 811 +P47161 UniProtKB Chain 1 811 . . . ID=PRO_0000174138;Note=Vacuolar protein sorting-associated protein 70 +P47161 UniProtKB Transmembrane 90 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47161 UniProtKB Metal binding 445 445 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47161 UniProtKB Metal binding 456 456 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47161 UniProtKB Metal binding 456 456 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47161 UniProtKB Metal binding 522 522 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47161 UniProtKB Metal binding 607 607 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47161 UniProtKB Glycosylation 55 55 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47161 UniProtKB Glycosylation 237 237 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47161 UniProtKB Glycosylation 568 568 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47161 UniProtKB Glycosylation 599 599 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47161 UniProtKB Glycosylation 670 670 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P37370 1 817 +P37370 UniProtKB Chain 1 817 . . . ID=PRO_0000065929;Note=Verprolin +P37370 UniProtKB Domain 30 47 . . . Note=WH2 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00406 +P37370 UniProtKB Domain 87 106 . . . Note=WH2 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00406 +P37370 UniProtKB Compositional bias 5 14 . . . Note=Poly-Pro +P37370 UniProtKB Compositional bias 239 245 . . . Note=Poly-Pro +P37370 UniProtKB Compositional bias 349 357 . . . Note=Poly-Pro +P37370 UniProtKB Compositional bias 396 406 . . . Note=Poly-Pro +P37370 UniProtKB Compositional bias 424 431 . . . Note=Poly-Pro +P37370 UniProtKB Compositional bias 462 468 . . . Note=Poly-Ser +P37370 UniProtKB Compositional bias 704 708 . . . Note=Poly-Pro +P37370 UniProtKB Modified residue 519 519 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P37370 UniProtKB Modified residue 762 762 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P37370 UniProtKB Glycosylation 109 109 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37370 UniProtKB Glycosylation 212 212 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37370 UniProtKB Glycosylation 337 337 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37370 UniProtKB Glycosylation 383 383 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37370 UniProtKB Glycosylation 784 784 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37370 UniProtKB Glycosylation 796 796 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37370 UniProtKB Sequence conflict 308 308 . . . Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37370 UniProtKB Sequence conflict 350 350 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37370 UniProtKB Sequence conflict 689 689 . . . Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37370 UniProtKB Sequence conflict 710 817 . . . Note=PSTMDTGTSNSPSKNLKQRLFSTGGSTLQHKHNTHTNQPDVDVGRYTIGGSNSIVGAKSGNERIVIDDSRFKWTNVSQMPKPRPFQNKTKLYPSGKGSSVPLDLTLFT->HLRWIPVPLIAPVKTLNNGYFLQVDRRCNTSIIRIQINQMLM;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03631 1 944 +Q03631 UniProtKB Chain 1 944 . . . ID=PRO_0000115004;Note=Weak acid resistance protein 1 +Q03631 UniProtKB DNA binding 76 109 . . . Note=Zn(2)-C6 fungal-type +Q03631 UniProtKB Modified residue 128 128 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03631 UniProtKB Mutagenesis 368 368 . . . Note=Causes hyperactivity with constitutive induction of PDR12. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18621731;Dbxref=PMID:18621731 +Q03631 UniProtKB Mutagenesis 452 452 . . . Note=Causes hyperactivity with constitutive induction of PDR12. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18621731;Dbxref=PMID:18621731 +Q03631 UniProtKB Mutagenesis 463 463 . . . Note=Causes hyperactivity with constitutive induction of PDR12. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18621731;Dbxref=PMID:18621731 +Q03631 UniProtKB Mutagenesis 640 640 . . . Note=Causes hyperactivity with constitutive induction of PDR12. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18621731;Dbxref=PMID:18621731 +Q03631 UniProtKB Mutagenesis 703 703 . . . Note=Causes hyperactivitywith constitutive induction of PDR12. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18621731;Dbxref=PMID:18621731 +Q03631 UniProtKB Mutagenesis 762 762 . . . Note=Causes hyperactivity with constitutive induction of PDR12. K->R%2CN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17509074,ECO:0000269|PubMed:18621731;Dbxref=PMID:17509074,PMID:18621731 +Q03631 UniProtKB Mutagenesis 763 763 . . . Note=Causes hyperactivity with constitutive induction of PDR12. F->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17509074;Dbxref=PMID:17509074 +Q03631 UniProtKB Mutagenesis 764 764 . . . Note=Causes hypersensitivity to sorbate through its inability to induce PDR12. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17509074;Dbxref=PMID:17509074 +##sequence-region P31412 1 392 +P31412 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6 +P31412 UniProtKB Chain 2 392 . . . ID=PRO_0000209358;Note=V-type proton ATPase subunit C +P31412 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6 +P31412 UniProtKB Mutagenesis 255 255 . . . Note=Is rapidly degraded and disrupts stable ATPase assembly. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11777935;Dbxref=PMID:11777935 +P31412 UniProtKB Beta strand 9 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Helix 30 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Helix 38 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Beta strand 43 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Helix 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Helix 61 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Beta strand 94 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Helix 107 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Turn 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Helix 127 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Turn 170 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Turn 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Helix 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Beta strand 189 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Helix 200 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Helix 203 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Helix 210 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Beta strand 213 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DL0 +P31412 UniProtKB Beta strand 223 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Beta strand 229 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Helix 240 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Helix 243 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Beta strand 256 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Helix 264 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Beta strand 325 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Helix 337 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Helix 349 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +P31412 UniProtKB Beta strand 384 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U7L +##sequence-region P22203 1 233 +P22203 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.5;Dbxref=PMID:22814378 +P22203 UniProtKB Chain 2 233 . . . ID=PRO_0000117310;Note=V-type proton ATPase subunit E +P22203 UniProtKB Region 8 20 . . . Note=Interaction with VMA5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15751969;Dbxref=PMID:15751969 +P22203 UniProtKB Region 19 38 . . . Note=Interaction with VMA10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15751969;Dbxref=PMID:15751969 +P22203 UniProtKB Coiled coil 15 45 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22203 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.5;Dbxref=PMID:22814378 +P22203 UniProtKB Mutagenesis 2 2 . . . Note=Reduces ATPase activity by 11%25. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718227;Dbxref=PMID:15718227 +P22203 UniProtKB Mutagenesis 6 6 . . . Note=Reduces ATPase activity by 73%25. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718227;Dbxref=PMID:15718227 +P22203 UniProtKB Mutagenesis 9 9 . . . Note=Increases ATPase activity 1.4-fold. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718227;Dbxref=PMID:15718227 +P22203 UniProtKB Mutagenesis 78 78 . . . Note=Reduces ATPase activity by 88%25. Prevents assembly of V1 subunits at the membrane. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718227;Dbxref=PMID:15718227 +P22203 UniProtKB Mutagenesis 145 145 . . . Note=In VMA4-1%3B is rapidly degraded at 37 degrees Celsius. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9660816;Dbxref=PMID:9660816 +P22203 UniProtKB Mutagenesis 160 160 . . . Note=Reduces ATPase activity by 22%25. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718227;Dbxref=PMID:15718227 +P22203 UniProtKB Mutagenesis 202 202 . . . Note=Increases ATPase activity 2.1-fold by increasing Vmax for ATP hydrolysis 2-fold. Reduces ATPase activity by 90%25 and produces structurally aberrant V-ATPase complexes%3B when associated with A-233. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718227;Dbxref=PMID:15718227 +P22203 UniProtKB Mutagenesis 230 230 . . . Note=Increases ATPase activity 1.3-fold. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718227;Dbxref=PMID:15718227 +P22203 UniProtKB Mutagenesis 233 233 . . . Note=Reduces ATPase activity by 74%25. Reduces ATPase activity by 90%25 and produces structurally aberrant V-ATPase complexes%3B when associated with A-202. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718227;Dbxref=PMID:15718227 +P22203 UniProtKB Sequence conflict 97 98 . . . Note=DG->ER;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22203 UniProtKB Helix 10 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA +P22203 UniProtKB Helix 114 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA +P22203 UniProtKB Beta strand 135 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA +P22203 UniProtKB Turn 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA +P22203 UniProtKB Helix 146 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA +P22203 UniProtKB Helix 153 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA +P22203 UniProtKB Turn 164 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA +P22203 UniProtKB Beta strand 171 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA +P22203 UniProtKB Turn 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA +P22203 UniProtKB Beta strand 185 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA +P22203 UniProtKB Beta strand 198 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA +P22203 UniProtKB Helix 203 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EFA +##sequence-region Q04301 1 562 +Q04301 UniProtKB Chain 1 562 . . . ID=PRO_0000173428;Note=Vacuolar basic amino acid transporter 1 +Q04301 UniProtKB Topological domain 1 30 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Transmembrane 31 51 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Topological domain 52 100 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Transmembrane 101 121 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Topological domain 122 131 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Transmembrane 132 152 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Topological domain 153 166 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Transmembrane 167 187 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Topological domain 188 190 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Transmembrane 191 211 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Topological domain 212 232 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Transmembrane 233 253 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Topological domain 254 255 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Transmembrane 256 276 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Topological domain 277 292 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Transmembrane 293 313 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Topological domain 314 331 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Transmembrane 332 352 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Topological domain 353 365 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Transmembrane 366 386 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Topological domain 387 419 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Transmembrane 420 440 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Topological domain 441 448 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Transmembrane 449 469 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Topological domain 470 528 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Transmembrane 529 549 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Topological domain 550 562 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Glycosylation 123 123 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Glycosylation 324 324 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04301 UniProtKB Glycosylation 504 504 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P25594 1 458 +P25594 UniProtKB Chain 1 458 . . . ID=PRO_0000173424;Note=Vacuolar basic amino acid transporter 3 +P25594 UniProtKB Topological domain 1 9 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Transmembrane 10 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Topological domain 31 36 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Transmembrane 37 57 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Topological domain 58 67 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Transmembrane 68 88 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Topological domain 89 132 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Transmembrane 133 153 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Topological domain 154 163 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Transmembrane 164 184 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Topological domain 185 205 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Transmembrane 206 226 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Topological domain 227 248 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Transmembrane 249 269 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Topological domain 270 277 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Transmembrane 278 298 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Topological domain 299 306 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Transmembrane 307 327 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Topological domain 328 415 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Transmembrane 416 436 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Topological domain 437 458 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25594 UniProtKB Glycosylation 195 195 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03785 1 461 +Q03785 UniProtKB Chain 1 461 . . . ID=PRO_0000086789;Note=Serine/threonine-protein kinase VHS1 +Q03785 UniProtKB Domain 12 337 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03785 UniProtKB Nucleotide binding 18 26 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03785 UniProtKB Active site 185 185 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q03785 UniProtKB Binding site 41 41 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +##sequence-region P53262 1 265 +P53262 UniProtKB Signal peptide 1 24 . . . . +P53262 UniProtKB Chain 25 265 . . . ID=PRO_0000042985;Note=V0 assembly protein 1 +P53262 UniProtKB Topological domain 25 223 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53262 UniProtKB Transmembrane 224 244 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53262 UniProtKB Topological domain 245 265 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53262 UniProtKB Motif 262 265 . . . Note=ER retention motif +P53262 UniProtKB Glycosylation 69 69 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53262 UniProtKB Glycosylation 104 104 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53262 UniProtKB Glycosylation 172 172 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32563 1 840 +P32563 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.6;Dbxref=PMID:22814378 +P32563 UniProtKB Chain 2 840 . . . ID=PRO_0000119224;Note=V-type proton ATPase subunit a%2C vacuolar isoform +P32563 UniProtKB Topological domain 2 404 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32563 UniProtKB Transmembrane 405 423 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32563 UniProtKB Topological domain 424 425 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32563 UniProtKB Transmembrane 426 442 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32563 UniProtKB Topological domain 443 456 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32563 UniProtKB Transmembrane 457 486 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32563 UniProtKB Topological domain 487 534 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32563 UniProtKB Transmembrane 535 554 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32563 UniProtKB Topological domain 555 572 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32563 UniProtKB Transmembrane 573 593 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32563 UniProtKB Topological domain 594 636 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32563 UniProtKB Transmembrane 637 656 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32563 UniProtKB Topological domain 657 719 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32563 UniProtKB Transmembrane 720 744 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32563 UniProtKB Topological domain 745 765 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32563 UniProtKB Transmembrane 766 804 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32563 UniProtKB Topological domain 805 840 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32563 UniProtKB Coiled coil 117 145 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32563 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.6;Dbxref=PMID:22814378 +P32563 UniProtKB Mutagenesis 425 425 . . . Note=Reduces assembly of V-ATPase complexes and reduces ATPase activity of the assembled complexes. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8798414;Dbxref=PMID:8798414 +P32563 UniProtKB Mutagenesis 538 538 . . . Note=Reduces assembly of V-ATPase complexes. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8798414;Dbxref=PMID:8798414 +P32563 UniProtKB Mutagenesis 593 593 . . . Note=Reduces ATPase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8798414;Dbxref=PMID:8798414 +P32563 UniProtKB Mutagenesis 634 634 . . . Note=Reduces subunit stability. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8798414;Dbxref=PMID:8798414 +P32563 UniProtKB Mutagenesis 729 729 . . . Note=Reduces ATPase activity. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970 +P32563 UniProtKB Mutagenesis 735 735 . . . Note=Reduces subunit stability. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8798414;Dbxref=PMID:8798414 +P32563 UniProtKB Mutagenesis 739 739 . . . Note=Reduces ATPase activity. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970 +P32563 UniProtKB Mutagenesis 743 743 . . . Note=Reduces ATPase activity. H->A%2CE%2CY;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8798414,ECO:0000269|PubMed:9506970;Dbxref=PMID:8798414,PMID:9506970 +P32563 UniProtKB Mutagenesis 746 746 . . . Note=Reduces ATPase activity. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970 +P32563 UniProtKB Mutagenesis 780 780 . . . Note=Reduces assembly of V-ATPase complexes. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970 +P32563 UniProtKB Mutagenesis 789 789 . . . Note=Abolishes ATPase activity and proton transport%2C but does not affect complex assembly. E->A%2CD%2CH%2CQ;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8798414,ECO:0000269|PubMed:9506970;Dbxref=PMID:8798414,PMID:9506970 +P32563 UniProtKB Mutagenesis 800 800 . . . Note=Reduces assembly of V-ATPase complexes. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970 +P32563 UniProtKB Mutagenesis 802 802 . . . Note=Reduces assembly of V-ATPase complexes. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970 +P32563 UniProtKB Mutagenesis 803 803 . . . Note=Reduces ATPase activity. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970 +P32563 UniProtKB Mutagenesis 803 803 . . . Note=Reduces assembly of V-ATPase complexes. V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970 +P32563 UniProtKB Mutagenesis 809 809 . . . Note=Reduces assembly of V-ATPase complexes. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970 +P32563 UniProtKB Mutagenesis 814 814 . . . Note=Reduces assembly of V-ATPase complexes. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9506970;Dbxref=PMID:9506970 +P32563 UniProtKB Beta strand 723 725 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NVJ +P32563 UniProtKB Helix 729 747 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JTW +##sequence-region P47142 1 202 +P47142 UniProtKB Chain 1 202 . . . ID=PRO_0000215221;Note=Vacuolar protein-sorting-associated protein 25 +P47142 UniProtKB Helix 7 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4 +P47142 UniProtKB Helix 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4 +P47142 UniProtKB Helix 20 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4 +P47142 UniProtKB Beta strand 45 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4 +P47142 UniProtKB Beta strand 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4 +P47142 UniProtKB Turn 79 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4 +P47142 UniProtKB Helix 87 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4 +P47142 UniProtKB Beta strand 102 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4 +P47142 UniProtKB Beta strand 120 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4 +P47142 UniProtKB Helix 128 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4 +P47142 UniProtKB Helix 151 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4 +P47142 UniProtKB Turn 164 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4 +P47142 UniProtKB Helix 170 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4 +P47142 UniProtKB Helix 182 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4 +P47142 UniProtKB Beta strand 187 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4 +P47142 UniProtKB Beta strand 196 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XB4 +##sequence-region P38959 1 992 +P38959 UniProtKB Chain 1 992 . . . ID=PRO_0000212827;Note=Vacuolar protein sorting-associated protein 41 +P38959 UniProtKB Repeat 114 152 . . . Note=WD 1 +P38959 UniProtKB Repeat 153 192 . . . Note=WD 2 +P38959 UniProtKB Repeat 194 234 . . . Note=WD 3 +P38959 UniProtKB Repeat 240 280 . . . Note=WD 4 +P38959 UniProtKB Repeat 324 366 . . . Note=WD 5 +P38959 UniProtKB Repeat 753 901 . . . Note=CHCR +P38959 UniProtKB Compositional bias 79 94 . . . Note=Poly-Asp +P38959 UniProtKB Compositional bias 239 244 . . . Note=Poly-Lys +P38959 UniProtKB Modified residue 26 26 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38959 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38959 UniProtKB Sequence conflict 424 424 . . . Note=K->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38932 1 577 +P38932 UniProtKB Chain 1 577 . . . ID=PRO_0000206316;Note=Vacuolar protein sorting-associated protein 45 +P38932 UniProtKB Sequence conflict 136 136 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38932 UniProtKB Sequence conflict 239 239 . . . Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12071 1 889 +Q12071 UniProtKB Chain 1 889 . . . ID=PRO_0000148737;Note=Vacuolar protein sorting-associated protein 54 +Q12071 UniProtKB Coiled coil 286 321 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12071 UniProtKB Modified residue 69 69 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12071 UniProtKB Modified residue 72 72 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12071 UniProtKB Modified residue 74 74 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P47111 1 140 +P47111 UniProtKB Chain 1 140 . . . ID=PRO_0000215201;Note=Vacuolar protein sorting-associated protein 55 +P47111 UniProtKB Topological domain 1 11 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47111 UniProtKB Transmembrane 12 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47111 UniProtKB Topological domain 33 37 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47111 UniProtKB Transmembrane 38 58 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47111 UniProtKB Topological domain 59 76 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47111 UniProtKB Transmembrane 77 97 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47111 UniProtKB Topological domain 98 107 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47111 UniProtKB Transmembrane 108 128 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47111 UniProtKB Topological domain 129 140 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47111 UniProtKB Modified residue 137 137 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q12016 1 184 +Q12016 UniProtKB Chain 1 184 . . . ID=PRO_0000174187;Note=Vacuolar protein sorting-associated protein 68 +Q12016 UniProtKB Transmembrane 26 46 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12016 UniProtKB Transmembrane 56 76 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12016 UniProtKB Transmembrane 115 135 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12016 UniProtKB Transmembrane 150 170 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12016 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +Q12016 UniProtKB Modified residue 8 8 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:18407956 +Q12016 UniProtKB Glycosylation 52 52 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06385 1 345 +Q06385 UniProtKB Chain 1 345 . . . ID=PRO_0000123823;Note=Vacuolar protein sorting-associated protein 74 +Q06385 UniProtKB Region 197 208 . . . Note=Beta-hairpin required for oligomerization +Q06385 UniProtKB Binding site 88 88 . . . Note=PtdIns4P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06385 UniProtKB Binding site 97 97 . . . Note=PtdIns4P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06385 UniProtKB Binding site 178 178 . . . Note=PtdIns4P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06385 UniProtKB Binding site 181 181 . . . Note=PtdIns4P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06385 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06385 UniProtKB Modified residue 19 19 . . . Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:22889169;Dbxref=PMID:22889169 +Q06385 UniProtKB Mutagenesis 6 8 . . . Note=Loss of coatomer-binding. RRR->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22889169;Dbxref=PMID:22889169 +Q06385 UniProtKB Mutagenesis 19 19 . . . Note=Alters phosphorylation but has not effect on Golgi enzymes localization. S->A +Q06385 UniProtKB Mutagenesis 88 88 . . . Note=Abolishes phosphoinositide binding and Golgi localization%3B when associated with A-97. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20026658;Dbxref=PMID:20026658 +Q06385 UniProtKB Mutagenesis 97 97 . . . Note=Abolishes phosphoinositide binding and Golgi localization%3B when associated with A-88. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20026658;Dbxref=PMID:20026658 +Q06385 UniProtKB Mutagenesis 178 178 . . . Note=Abolishes phosphoinositide binding and Golgi localization%3B when associated with A-181. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20026658;Dbxref=PMID:20026658 +Q06385 UniProtKB Mutagenesis 181 181 . . . Note=Abolishes phosphoinositide binding and Golgi localization%3B when associated with A-178. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20026658;Dbxref=PMID:20026658 +Q06385 UniProtKB Helix 69 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Beta strand 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Helix 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Helix 90 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Beta strand 109 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Helix 116 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Helix 123 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Beta strand 126 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Helix 139 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Helix 156 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Turn 163 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Helix 170 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Helix 180 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Beta strand 197 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Beta strand 205 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Helix 214 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Beta strand 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Beta strand 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Helix 248 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Helix 266 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Helix 274 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Beta strand 292 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Beta strand 303 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Helix 310 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Helix 325 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +Q06385 UniProtKB Turn 340 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIH +##sequence-region Q07655 1 649 +Q07655 UniProtKB Chain 1 649 . . . ID=PRO_0000262756;Note=Protein WHI4 +Q07655 UniProtKB Domain 533 625 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q07655 UniProtKB Modified residue 22 22 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07655 UniProtKB Modified residue 206 206 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07655 UniProtKB Modified residue 258 258 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07655 UniProtKB Modified residue 283 283 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40080 1 203 +P40080 UniProtKB Chain 1 203 . . . ID=PRO_0000202649;Note=VPS4-associated protein 1 +P40080 UniProtKB Coiled coil 121 157 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40080 UniProtKB Helix 189 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FVK +##sequence-region P41806 1 77 +P41806 UniProtKB Chain 1 77 . . . ID=PRO_0000065875;Note=Vacuolar ATPase assembly integral membrane protein VMA21 +P41806 UniProtKB Topological domain 1 13 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03058 +P41806 UniProtKB Transmembrane 14 34 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03058 +P41806 UniProtKB Topological domain 35 38 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03058 +P41806 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03058 +P41806 UniProtKB Topological domain 60 77 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03058 +P41806 UniProtKB Motif 74 77 . . . Note=Prevents secretion from ER +P41806 UniProtKB Mutagenesis 74 75 . . . Note=Mislocalizes to the vacuole membrane and stay associated with the V0 sector after transport out of the ER. KK->QQ;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15356264,ECO:0000269|PubMed:7841520;Dbxref=PMID:15356264,PMID:7841520 +P41806 UniProtKB Mutagenesis 74 74 . . . Note=Secretion from ER. K->Q +P41806 UniProtKB Mutagenesis 75 75 . . . Note=Secretion from ER. K->Q +P41806 UniProtKB Sequence conflict 70 70 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P42839 1 908 +P42839 UniProtKB Chain 1 908 . . . ID=PRO_0000209505;Note=Low affinity vacuolar monovalent cation/H(+) antiporter +P42839 UniProtKB Topological domain 1 244 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Transmembrane 245 265 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Topological domain 266 408 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Transmembrane 409 429 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Topological domain 430 494 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Transmembrane 495 515 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Topological domain 516 530 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Transmembrane 531 551 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Topological domain 552 560 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Transmembrane 561 581 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Topological domain 582 587 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Transmembrane 588 608 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Topological domain 609 626 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Transmembrane 627 647 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Topological domain 648 686 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Transmembrane 687 707 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Topological domain 708 746 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Transmembrane 747 767 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Topological domain 768 783 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Transmembrane 784 804 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Topological domain 805 816 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Transmembrane 817 837 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Topological domain 838 851 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Transmembrane 852 872 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Topological domain 873 885 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Transmembrane 886 906 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Topological domain 907 908 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42839 UniProtKB Modified residue 26 26 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P42839 UniProtKB Modified residue 32 32 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P42839 UniProtKB Modified residue 33 33 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P42839 UniProtKB Modified residue 110 110 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P42839 UniProtKB Modified residue 118 118 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P42839 UniProtKB Modified residue 121 121 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P42839 UniProtKB Glycosylation 361 361 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39904 1 641 +P39904 UniProtKB Chain 1 641 . . . ID=PRO_0000213318;Note=Vacuolar protein sorting-associated protein 52 +P39904 UniProtKB Coiled coil 81 110 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39904 UniProtKB Modified residue 602 602 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39904 UniProtKB Sequence conflict 204 209 . . . Note=KRLIIS->EKTYYF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03913 1 190 +Q03913 UniProtKB Chain 1 190 . . . ID=PRO_0000299779;Note=Putative uncharacterized protein VPS61 +Q03913 UniProtKB Transmembrane 152 174 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03433 1 280 +Q03433 UniProtKB Chain 1 280 . . . ID=PRO_0000173557;Note=Vacuolar protein sorting-associated protein 71 +Q03433 UniProtKB Zinc finger 244 277 . . . Note=HIT-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00453 +##sequence-region P54787 1 451 +P54787 UniProtKB Chain 1 451 . . . ID=PRO_0000191324;Note=Vacuolar protein sorting-associated protein 9 +P54787 UniProtKB Domain 170 312 . . . Note=VPS9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00550 +P54787 UniProtKB Domain 408 451 . . . Note=CUE;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00468 +P54787 UniProtKB Motif 229 237 . . . Note=GBH motif I +P54787 UniProtKB Motif 249 257 . . . Note=GBH motif II +P54787 UniProtKB Motif 287 295 . . . Note=GBH motif III +P54787 UniProtKB Compositional bias 332 341 . . . Note=Glu/Lys-rich +P54787 UniProtKB Modified residue 375 375 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P54787 UniProtKB Sequence conflict 172 172 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54787 UniProtKB Sequence conflict 305 305 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54787 UniProtKB Sequence conflict 305 305 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54787 UniProtKB Sequence conflict 314 314 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54787 UniProtKB Sequence conflict 314 314 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54787 UniProtKB Sequence conflict 327 327 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54787 UniProtKB Sequence conflict 327 327 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54787 UniProtKB Sequence conflict 345 345 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54787 UniProtKB Sequence conflict 345 345 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54787 UniProtKB Helix 401 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P3Q +P54787 UniProtKB Helix 425 434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P3Q +P54787 UniProtKB Helix 441 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P3Q +P54787 UniProtKB Helix 445 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P3Q +##sequence-region Q06263 1 330 +Q06263 UniProtKB Chain 1 330 . . . ID=PRO_0000065933;Note=Vacuolar protein sorting-associated protein VTA1 +Q06263 UniProtKB Region 1 167 . . . Note=Interaction with DID2 +Q06263 UniProtKB Region 37 68 . . . Note=Interaction with VSP60;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16505166;Dbxref=PMID:16505166 +Q06263 UniProtKB Region 280 330 . . . Note=Dimerization +Q06263 UniProtKB Region 290 330 . . . Note=Interaction with VSP4 +Q06263 UniProtKB Modified residue 183 183 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06263 UniProtKB Modified residue 195 195 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06263 UniProtKB Modified residue 233 233 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06263 UniProtKB Mutagenesis 122 122 . . . Note=Abolishes interaction with VSP60 and DID2. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18194651;Dbxref=PMID:18194651 +Q06263 UniProtKB Mutagenesis 152 152 . . . Note=Abolishes interaction with VSP60 and DID2. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18194651;Dbxref=PMID:18194651 +Q06263 UniProtKB Mutagenesis 299 299 . . . Note=Abolishes interaction with VSP4. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16505166;Dbxref=PMID:16505166 +Q06263 UniProtKB Mutagenesis 302 302 . . . Note=Abolishes interaction with VSP4. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16505166;Dbxref=PMID:16505166 +Q06263 UniProtKB Mutagenesis 303 303 . . . Note=Abolishes interaction with VSP4%2C no effect on dimerization. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18194651;Dbxref=PMID:18194651 +Q06263 UniProtKB Mutagenesis 306 306 . . . Note=Diminishes interaction with VSP4. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16505166;Dbxref=PMID:16505166 +Q06263 UniProtKB Mutagenesis 310 310 . . . Note=Abolishes interaction with VSP4%2C no effect on dimerization. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18194651;Dbxref=PMID:18194651 +Q06263 UniProtKB Mutagenesis 311 311 . . . Note=Abolishes interaction with VSP4 and dimerization. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18194651;Dbxref=PMID:18194651 +Q06263 UniProtKB Mutagenesis 312 312 . . . Note=Abolishes interaction with VSP4 and dimerization. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18194651;Dbxref=PMID:18194651 +Q06263 UniProtKB Mutagenesis 320 320 . . . Note=Abolishes dimerization. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18194651;Dbxref=PMID:18194651 +Q06263 UniProtKB Mutagenesis 322 322 . . . Note=No effect on interaction with VSP4. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16505166;Dbxref=PMID:16505166 +Q06263 UniProtKB Mutagenesis 327 327 . . . Note=Abolishes dimerization. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18194651;Dbxref=PMID:18194651 +Q06263 UniProtKB Sequence conflict 12 12 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06263 UniProtKB Helix 1 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKK +Q06263 UniProtKB Helix 21 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKK +Q06263 UniProtKB Helix 43 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKK +Q06263 UniProtKB Turn 62 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H7P +Q06263 UniProtKB Helix 68 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LUH +Q06263 UniProtKB Turn 77 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKK +Q06263 UniProtKB Helix 81 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKK +Q06263 UniProtKB Helix 86 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKK +Q06263 UniProtKB Helix 115 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKK +Q06263 UniProtKB Helix 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKK +Q06263 UniProtKB Helix 141 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKK +Q06263 UniProtKB Helix 280 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKL +Q06263 UniProtKB Turn 309 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKL +Q06263 UniProtKB Helix 313 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKL +##sequence-region P47165 1 209 +P47165 UniProtKB Chain 1 209 . . . ID=PRO_0000066042;Note=Xanthine phosphoribosyltransferase 1 +P47165 UniProtKB Modified residue 79 79 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P53076 1 958 +P53076 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53076 UniProtKB Chain 2 958 . . . ID=PRO_0000065829;Note=Vacuolar import and degradation protein 30 +P53076 UniProtKB Domain 390 592 . . . Note=B30.2/SPRY;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00548 +P53076 UniProtKB Domain 710 742 . . . Note=LisH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00126 +P53076 UniProtKB Domain 769 826 . . . Note=CTLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00058 +P53076 UniProtKB Compositional bias 165 185 . . . Note=Poly-Asp +P53076 UniProtKB Compositional bias 450 453 . . . Note=Poly-Ser +P53076 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53076 UniProtKB Modified residue 147 147 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53076 UniProtKB Modified residue 246 246 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53076 UniProtKB Modified residue 248 248 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53076 UniProtKB Modified residue 277 277 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P22219 1 1454 +P22219 UniProtKB Initiator methionine 1 1 . . . Note=Removed +P22219 UniProtKB Chain 2 1454 . . . ID=PRO_0000086802;Note=Serine/threonine-protein kinase VPS15 +P22219 UniProtKB Domain 27 300 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P22219 UniProtKB Repeat 460 497 . . . Note=HEAT 1 +P22219 UniProtKB Repeat 576 613 . . . Note=HEAT 2 +P22219 UniProtKB Repeat 615 652 . . . Note=HEAT 3 +P22219 UniProtKB Repeat 654 691 . . . Note=HEAT 4 +P22219 UniProtKB Repeat 1078 1118 . . . Note=WD 1 +P22219 UniProtKB Repeat 1126 1165 . . . Note=WD 2 +P22219 UniProtKB Repeat 1229 1268 . . . Note=WD 3 +P22219 UniProtKB Repeat 1275 1315 . . . Note=WD 4 +P22219 UniProtKB Repeat 1344 1382 . . . Note=WD 5 +P22219 UniProtKB Repeat 1422 1453 . . . Note=WD 6 +P22219 UniProtKB Nucleotide binding 33 41 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P22219 UniProtKB Active site 147 147 . . . Note=Proton acceptor +P22219 UniProtKB Binding site 54 54 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P22219 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1756716;Dbxref=PMID:1756716 +P22219 UniProtKB Mutagenesis 2 2 . . . Note=No myristoylation%2C but still membrane-association and normal activity. G->A%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1756716;Dbxref=PMID:1756716 +P22219 UniProtKB Mutagenesis 54 54 . . . Note=Loss of activity. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1756716;Dbxref=PMID:1756716 +P22219 UniProtKB Mutagenesis 147 147 . . . Note=Loss of activity. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1756716;Dbxref=PMID:1756716 +P22219 UniProtKB Mutagenesis 149 149 . . . Note=Loss of activity. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1756716;Dbxref=PMID:1756716 +P22219 UniProtKB Mutagenesis 151 151 . . . Note=Modest effect on activity and normal CPY sorting. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1756716;Dbxref=PMID:1756716 +P22219 UniProtKB Mutagenesis 165 165 . . . Note=Loss of activity. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1988155;Dbxref=PMID:1988155 +P22219 UniProtKB Mutagenesis 200 200 . . . Note=Loss of activity. No activation of VPS34 kinase activity. E->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1988155,ECO:0000269|PubMed:8387919;Dbxref=PMID:1988155,PMID:8387919 +P22219 UniProtKB Sequence conflict 134 134 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22219 UniProtKB Sequence conflict 134 134 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22219 UniProtKB Sequence conflict 443 443 . . . Note=L->PV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22219 UniProtKB Sequence conflict 610 610 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22219 UniProtKB Sequence conflict 851 851 . . . Note=R->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22219 UniProtKB Sequence conflict 851 851 . . . Note=R->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22219 UniProtKB Sequence conflict 851 851 . . . Note=R->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22219 UniProtKB Helix 1034 1036 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Helix 1046 1048 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Helix 1050 1052 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Helix 1064 1066 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1070 1075 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Turn 1077 1080 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1083 1089 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1091 1093 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1095 1100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1103 1109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Helix 1110 1114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1122 1126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1131 1136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1140 1147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1150 1162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1165 1178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Helix 1179 1182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1188 1195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1200 1206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1209 1215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Turn 1216 1218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1221 1226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Helix 1229 1231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1234 1239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1245 1250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1255 1259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Turn 1260 1263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1264 1270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1275 1282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Turn 1284 1286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1290 1297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1300 1306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Turn 1307 1310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1311 1321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Helix 1325 1328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Helix 1335 1337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Helix 1346 1349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1352 1355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1358 1363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Helix 1364 1366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1368 1373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Helix 1377 1379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1381 1384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1392 1399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1402 1408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1427 1445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +P22219 UniProtKB Beta strand 1450 1454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GRE +##sequence-region P21576 1 704 +P21576 UniProtKB Chain 1 704 . . . ID=PRO_0000206588;Note=Vacuolar protein sorting-associated protein 1 +P21576 UniProtKB Domain 26 336 . . . Note=Dynamin-type G +P21576 UniProtKB Domain 618 704 . . . Note=GED;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00720 +P21576 UniProtKB Nucleotide binding 36 43 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21576 UniProtKB Nucleotide binding 178 182 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21576 UniProtKB Nucleotide binding 247 250 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21576 UniProtKB Modified residue 579 579 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P21576 UniProtKB Modified residue 599 599 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P21576 UniProtKB Sequence conflict 33 33 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21576 UniProtKB Sequence conflict 111 111 . . . Note=N->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21576 UniProtKB Sequence conflict 141 141 . . . Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02767 1 242 +Q02767 UniProtKB Chain 1 242 . . . ID=PRO_0000120958;Note=Vacuolar protein sorting-associated protein 28 +Q02767 UniProtKB Domain 11 125 . . . Note=VPS28 N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00645 +Q02767 UniProtKB Domain 148 242 . . . Note=VPS28 C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00642 +Q02767 UniProtKB Region 148 242 . . . Note=Interaction with VSP36 and VPS20;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16749904;Dbxref=PMID:16749904 +Q02767 UniProtKB Mutagenesis 40 40 . . . Note=Abolishes ESCRT-I complex assembly%3B class E phenotype (malformed late MVB)%3B when associated with D-44. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16615894;Dbxref=PMID:16615894 +Q02767 UniProtKB Mutagenesis 44 44 . . . Note=Abolishes ESCRT-I complex assembly%3B class E phenotype (malformed late MVB)%3B when associated with D-40. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16615894;Dbxref=PMID:16615894 +Q02767 UniProtKB Mutagenesis 228 231 . . . Note=Abolishes interaction with VPS20. FDLE->ASLA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16749904;Dbxref=PMID:16749904 +Q02767 UniProtKB Sequence conflict 193 193 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q02767 UniProtKB Beta strand 10 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +Q02767 UniProtKB Helix 14 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6M +Q02767 UniProtKB Beta strand 27 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +Q02767 UniProtKB Helix 31 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6M +Q02767 UniProtKB Helix 64 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6M +Q02767 UniProtKB Turn 85 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6M +Q02767 UniProtKB Helix 89 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6M +Q02767 UniProtKB Helix 109 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6M +Q02767 UniProtKB Helix 150 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U +Q02767 UniProtKB Helix 174 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U +Q02767 UniProtKB Helix 199 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U +Q02767 UniProtKB Helix 220 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U +##sequence-region P22543 1 875 +P22543 UniProtKB Chain 1 875 . . . ID=PRO_0000088818;Note=Phosphatidylinositol 3-kinase VPS34 +P22543 UniProtKB Domain 14 188 . . . Note=C2 PI3K-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00880 +P22543 UniProtKB Domain 293 526 . . . Note=PIK helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00878 +P22543 UniProtKB Domain 619 873 . . . Note=PI3K/PI4K;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00269 +P22543 UniProtKB Mutagenesis 731 731 . . . Note=Loss of kinase activity and no vacuolar carboxypeptidase Y (PCR1) sorting to the vacuole. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8385367;Dbxref=PMID:8385367 +P22543 UniProtKB Mutagenesis 736 736 . . . Note=Loss of kinase activity and no vacuolar carboxypeptidase Y (PCR1) sorting to the vacuole. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8385367;Dbxref=PMID:8385367 +P22543 UniProtKB Mutagenesis 749 749 . . . Note=Loss of kinase activity and no vacuolar carboxypeptidase Y (PCR1) sorting to the vacuole. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8385367;Dbxref=PMID:8385367 +##sequence-region Q06696 1 566 +Q06696 UniProtKB Chain 1 566 . . . ID=PRO_0000215227;Note=Vacuolar protein-sorting-associated protein 36 +Q06696 UniProtKB Domain 7 96 . . . Note=GLUE N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00828 +Q06696 UniProtKB Domain 255 288 . . . Note=GLUE C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00828 +Q06696 UniProtKB Zinc finger 114 151 . . . Note=RanBP2-type 1%3B degenerate +Q06696 UniProtKB Zinc finger 177 205 . . . Note=RanBP2-type 2 +Q06696 UniProtKB Mutagenesis 187 188 . . . Note=Abolishes ubiquitin-binding and vacuole sorting of ubiquitinated proteins. TF->GS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15029239;Dbxref=PMID:15029239 +Q06696 UniProtKB Beta strand 23 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY +Q06696 UniProtKB Beta strand 43 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY +Q06696 UniProtKB Helix 62 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY +Q06696 UniProtKB Beta strand 67 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY +Q06696 UniProtKB Helix 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY +Q06696 UniProtKB Beta strand 74 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY +Q06696 UniProtKB Beta strand 82 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY +Q06696 UniProtKB Beta strand 89 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY +Q06696 UniProtKB Beta strand 116 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U +Q06696 UniProtKB Turn 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U +Q06696 UniProtKB Beta strand 126 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U +Q06696 UniProtKB Turn 144 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U +Q06696 UniProtKB Helix 152 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U +Q06696 UniProtKB Helix 156 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J9U +Q06696 UniProtKB Beta strand 256 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY +Q06696 UniProtKB Helix 266 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CAY +##sequence-region Q92331 1 675 +Q92331 UniProtKB Chain 1 675 . . . ID=PRO_0000213804;Note=Vacuolar protein sorting-associated protein 5 +Q92331 UniProtKB Domain 279 394 . . . Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147 +Q92331 UniProtKB Binding site 320 320 . . . Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q92331 UniProtKB Binding site 346 346 . . . Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q92331 UniProtKB Binding site 360 360 . . . Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q92331 UniProtKB Sequence conflict 376 376 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04338 1 217 +Q04338 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4 +Q04338 UniProtKB Chain 2 217 . . . ID=PRO_0000218232;Note=t-SNARE VTI1 +Q04338 UniProtKB Topological domain 2 194 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04338 UniProtKB Transmembrane 195 215 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04338 UniProtKB Topological domain 216 217 . . . Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04338 UniProtKB Domain 124 186 . . . Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202 +Q04338 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4 +Q04338 UniProtKB Modified residue 110 110 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q04338 UniProtKB Modified residue 149 149 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04338 UniProtKB Mutagenesis 130 130 . . . Note=In VTI1-2%3B exhibits defects in TGN to PVC transport at nonpermissive temperature%3B when associated with T-151. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9446565;Dbxref=PMID:9446565 +Q04338 UniProtKB Mutagenesis 141 141 . . . Note=In VTI1-12%3B blocks constitutively the traffic from the late Golgi to the vacuole and blocks the transport to the cis-Golgi compartment at nonpermissive temperature%3B when associated with R-158. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9446565;Dbxref=PMID:9446565 +Q04338 UniProtKB Mutagenesis 145 145 . . . Note=In VTI1-11%3B displays a block in traffic to the PVC and an additional defect in retrograde traffic to the cis-Golgi%3B when associated with F-155. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9446565;Dbxref=PMID:9446565 +Q04338 UniProtKB Mutagenesis 145 145 . . . Note=In VTI1-1%3B exhibits defects in TGN to PVC transport at nonpermissive temperature%3B when associated with R-148. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9446565;Dbxref=PMID:9446565 +Q04338 UniProtKB Mutagenesis 148 148 . . . Note=In VTI1-1%3B exhibits defects in TGN to PVC transport at nonpermissive temperature%3B when associated with K-145. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9446565;Dbxref=PMID:9446565 +Q04338 UniProtKB Mutagenesis 151 151 . . . Note=In VTI1-2%3B exhibits defects in TGN to PVC transport at nonpermissive temperature%3B when associated with P-130. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9446565;Dbxref=PMID:9446565 +Q04338 UniProtKB Mutagenesis 155 155 . . . Note=In VTI1-11%3B displays a block in traffic to the PVC and an additional defect in retrograde traffic to the cis-Golgi%3B when associated with G-145. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9446565;Dbxref=PMID:9446565 +Q04338 UniProtKB Mutagenesis 158 158 . . . Note=In VTI1-12%3B blocks constitutively the traffic from the late Golgi to the vacuole and blocks the transport to the cis-Golgi compartment at nonpermissive temperature%3B when associated with S-141. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9446565;Dbxref=PMID:9446565 +Q04338 UniProtKB Helix 4 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONJ +Q04338 UniProtKB Helix 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONJ +Q04338 UniProtKB Helix 31 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONJ +Q04338 UniProtKB Helix 66 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONJ +Q04338 UniProtKB Helix 88 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONJ +##sequence-region P40151 1 587 +P40151 UniProtKB Chain 1 587 . . . ID=PRO_0000084788;Note=DNA-dependent ATPase MGS1 +P40151 UniProtKB Zinc finger 11 34 . . . Note=UBZ-type;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40151 UniProtKB Nucleotide binding 177 184 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40151 UniProtKB Nucleotide binding 179 185 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 +##sequence-region P39102 1 459 +P39102 UniProtKB Chain 1 459 . . . ID=PRO_0000071121;Note=DnaJ protein homolog XDJ1 +P39102 UniProtKB Domain 7 79 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +P39102 UniProtKB Repeat 159 166 . . . Note=CXXCXGXG motif +P39102 UniProtKB Repeat 181 188 . . . Note=CXXCXGXG motif +P39102 UniProtKB Repeat 208 215 . . . Note=CXXCXGXG motif +P39102 UniProtKB Repeat 228 235 . . . Note=CXXCXGXG motif +P39102 UniProtKB Zinc finger 146 240 . . . Note=CR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00546 +P39102 UniProtKB Sequence conflict 119 119 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39102 UniProtKB Sequence conflict 448 448 . . . Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38759 1 282 +P38759 UniProtKB Chain 1 282 . . . ID=PRO_0000058305;Note=Vacuolar protein sorting-associated protein 29 +##sequence-region O13584 1 106 +O13584 UniProtKB Chain 1 106 . . . ID=PRO_0000299782;Note=Putative uncharacterized protein VPS69 +O13584 UniProtKB Transmembrane 10 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13584 UniProtKB Transmembrane 65 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40438 1 1549 +P40438 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40438 UniProtKB Chain 22 1549 . . . ID=PRO_0000014329;Note=VPS10 homolog 1 +P40438 UniProtKB Topological domain 22 1369 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40438 UniProtKB Transmembrane 1370 1390 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40438 UniProtKB Topological domain 1391 1549 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40438 UniProtKB Repeat 57 68 . . . Note=BNR 1 +P40438 UniProtKB Repeat 101 112 . . . Note=BNR 2 +P40438 UniProtKB Repeat 159 170 . . . Note=BNR 3 +P40438 UniProtKB Repeat 228 239 . . . Note=BNR 4 +P40438 UniProtKB Repeat 393 404 . . . Note=BNR 5 +P40438 UniProtKB Repeat 465 476 . . . Note=BNR 6 +P40438 UniProtKB Repeat 511 522 . . . Note=BNR 7 +P40438 UniProtKB Repeat 740 751 . . . Note=BNR 8 +P40438 UniProtKB Repeat 837 848 . . . Note=BNR 9 +P40438 UniProtKB Repeat 1040 1051 . . . Note=BNR 10 +P40438 UniProtKB Repeat 1119 1130 . . . Note=BNR 11 +P40438 UniProtKB Repeat 1160 1171 . . . Note=BNR 12 +P40438 UniProtKB Glycosylation 479 479 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40438 UniProtKB Glycosylation 769 769 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40438 UniProtKB Glycosylation 986 986 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40890 1 1549 +P40890 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40890 UniProtKB Chain 22 1549 . . . ID=PRO_0000014331;Note=VPS10 homolog 2 +P40890 UniProtKB Topological domain 22 1369 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40890 UniProtKB Transmembrane 1370 1390 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40890 UniProtKB Topological domain 1391 1549 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40890 UniProtKB Repeat 57 68 . . . Note=BNR 1 +P40890 UniProtKB Repeat 101 112 . . . Note=BNR 2 +P40890 UniProtKB Repeat 159 170 . . . Note=BNR 3 +P40890 UniProtKB Repeat 228 239 . . . Note=BNR 4 +P40890 UniProtKB Repeat 393 404 . . . Note=BNR 5 +P40890 UniProtKB Repeat 465 476 . . . Note=BNR 6 +P40890 UniProtKB Repeat 511 522 . . . Note=BNR 7 +P40890 UniProtKB Repeat 740 751 . . . Note=BNR 8 +P40890 UniProtKB Repeat 837 848 . . . Note=BNR 9 +P40890 UniProtKB Repeat 1040 1051 . . . Note=BNR 10 +P40890 UniProtKB Repeat 1119 1130 . . . Note=BNR 11 +P40890 UniProtKB Repeat 1160 1171 . . . Note=BNR 12 +P40890 UniProtKB Glycosylation 479 479 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40890 UniProtKB Glycosylation 769 769 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40890 UniProtKB Glycosylation 986 986 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08831 1 523 +Q08831 UniProtKB Chain 1 523 . . . ID=PRO_0000081458;Note=Protein VTS1 +Q08831 UniProtKB Domain 451 512 . . . Note=SAM +Q08831 UniProtKB Compositional bias 74 178 . . . Note=Gln-rich +Q08831 UniProtKB Compositional bias 374 384 . . . Note=His-rich +Q08831 UniProtKB Mutagenesis 467 467 . . . Note=Loss of RNA-binding. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12858164;Dbxref=PMID:12858164 +Q08831 UniProtKB Mutagenesis 498 498 . . . Note=Loss of RNA-binding. A->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12858164;Dbxref=PMID:12858164 +Q08831 UniProtKB Helix 444 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D3D +Q08831 UniProtKB Helix 450 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D3D +Q08831 UniProtKB Helix 456 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D3D +Q08831 UniProtKB Helix 466 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D3D +Q08831 UniProtKB Helix 469 472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D3D +Q08831 UniProtKB Helix 477 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D3D +Q08831 UniProtKB Helix 485 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D3D +Q08831 UniProtKB Helix 496 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D3D +Q08831 UniProtKB Helix 520 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D3D +##sequence-region P12611 1 486 +P12611 UniProtKB Chain 1 486 . . . ID=PRO_0000065967;Note=Growth regulation protein +P12611 UniProtKB Sequence conflict 216 216 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P34761 1 661 +P34761 UniProtKB Chain 1 661 . . . ID=PRO_0000082005;Note=Protein WHI3 +P34761 UniProtKB Domain 538 625 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P34761 UniProtKB Compositional bias 247 277 . . . Note=Gln-rich +P34761 UniProtKB Modified residue 231 231 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40463 1 436 +P40463 UniProtKB Chain 1 436 . . . ID=PRO_0000065812;Note=Protein VHS2 +P40463 UniProtKB Compositional bias 386 424 . . . Note=Asn-rich +P40463 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40463 UniProtKB Modified residue 61 61 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40463 UniProtKB Modified residue 102 102 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40463 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40463 UniProtKB Modified residue 299 299 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40463 UniProtKB Modified residue 301 301 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40463 UniProtKB Modified residue 303 303 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P40463 UniProtKB Modified residue 325 325 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region Q12045 1 647 +Q12045 UniProtKB Chain 1 647 . . . ID=PRO_0000270929;Note=Spindle pole body-associated protein VIK1 +Q12045 UniProtKB Coiled coil 202 350 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12045 UniProtKB Helix 353 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Beta strand 376 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Helix 383 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Beta strand 390 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Turn 394 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Beta strand 398 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Turn 402 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Beta strand 407 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Beta strand 411 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Turn 416 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Helix 421 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Helix 430 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Beta strand 443 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Helix 454 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Helix 470 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Beta strand 475 485 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Beta strand 486 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ETP +Q12045 UniProtKB Beta strand 490 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Beta strand 506 509 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Beta strand 514 518 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Beta strand 521 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Helix 526 529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Turn 532 535 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Beta strand 546 557 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Beta strand 570 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Helix 580 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Helix 599 610 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Beta strand 614 619 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Helix 622 624 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +Q12045 UniProtKB Helix 625 638 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O0A +##sequence-region P32341 1 215 +P32341 UniProtKB Chain 1 215 . . . ID=PRO_0000065874;Note=Vacuolar ATPase assembly integral membrane protein VPH2 +P32341 UniProtKB Topological domain 1 134 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32341 UniProtKB Transmembrane 135 155 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32341 UniProtKB Topological domain 156 167 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32341 UniProtKB Transmembrane 168 186 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32341 UniProtKB Topological domain 187 215 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07878 1 3144 +Q07878 UniProtKB Chain 1 3144 . . . ID=PRO_0000065887;Note=Vacuolar protein sorting-associated protein 13 +Q07878 UniProtKB Modified residue 1364 1364 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07878 UniProtKB Modified residue 1382 1382 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07878 UniProtKB Modified residue 1715 1715 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +Q07878 UniProtKB Modified residue 1729 1729 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07878 UniProtKB Modified residue 1731 1731 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q03390 1 229 +Q03390 UniProtKB Chain 1 229 . . . ID=PRO_0000211507;Note=Vacuolar protein-sorting-associated protein 60 +Q03390 UniProtKB Region 128 159 . . . Note=Interaction with VTA1 +Q03390 UniProtKB Coiled coil 9 155 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03390 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03390 UniProtKB Mutagenesis 144 148 . . . Note=Abolishes interaction with VTA1 and reduces endosomal localization. IEQGD->AAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18194652;Dbxref=PMID:18194652 +Q03390 UniProtKB Helix 129 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LUH +Q03390 UniProtKB Helix 140 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LUH +Q03390 UniProtKB Helix 163 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LUH +Q03390 UniProtKB Helix 168 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LUH +##sequence-region P53853 1 264 +P53853 UniProtKB Chain 1 264 . . . ID=PRO_0000185675;Note=Vacuolar protein sorting-associated protein 75 +P53853 UniProtKB Modified residue 3 3 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53853 UniProtKB Helix 7 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Helix 57 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Beta strand 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DM7 +P53853 UniProtKB Helix 68 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Helix 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Helix 77 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Beta strand 83 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Helix 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Beta strand 103 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Turn 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Beta strand 119 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Beta strand 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Beta strand 138 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Helix 150 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Turn 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Beta strand 163 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Helix 166 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Helix 179 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Beta strand 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Beta strand 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Helix 197 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Helix 208 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZD7 +P53853 UniProtKB Helix 224 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q66 +P53853 UniProtKB Turn 227 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q68 +##sequence-region Q12215 1 556 +Q12215 UniProtKB Signal peptide 1 38 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12215 UniProtKB Chain 39 556 . . . ID=PRO_0000041485;Note=Cell wall integrity and stress response component 3 +Q12215 UniProtKB Topological domain 39 384 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12215 UniProtKB Transmembrane 385 405 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12215 UniProtKB Topological domain 406 556 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12215 UniProtKB Domain 39 132 . . . Note=WSC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00558 +Q12215 UniProtKB Compositional bias 137 348 . . . Note=Ser/Thr-rich +Q12215 UniProtKB Glycosylation 84 84 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12215 UniProtKB Glycosylation 367 367 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12215 UniProtKB Glycosylation 370 370 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03944 1 604 +Q03944 UniProtKB Chain 1 604 . . . ID=PRO_0000065907;Note=Vacuolar protein sorting-associated protein 64 +Q03944 UniProtKB Topological domain 1 578 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03944 UniProtKB Transmembrane 579 598 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03944 UniProtKB Topological domain 599 604 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03944 UniProtKB Domain 185 257 . . . Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 +Q03944 UniProtKB Coiled coil 404 563 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08924 1 1013 +Q08924 UniProtKB Chain 1 1013 . . . ID=PRO_0000234366;Note=Regulator of Ty1 transposition protein 10 +Q08924 UniProtKB Repeat 5 41 . . . Note=WD 1 +Q08924 UniProtKB Repeat 45 84 . . . Note=WD 2 +Q08924 UniProtKB Repeat 132 174 . . . Note=WD 3 +Q08924 UniProtKB Repeat 177 216 . . . Note=WD 4 +Q08924 UniProtKB Repeat 219 258 . . . Note=WD 5 +Q08924 UniProtKB Repeat 269 308 . . . Note=WD 6 +Q08924 UniProtKB Repeat 465 504 . . . Note=WD 7 +Q08924 UniProtKB Repeat 586 625 . . . Note=WD 8 +Q08924 UniProtKB Repeat 652 702 . . . Note=WD 9 +Q08924 UniProtKB Repeat 709 747 . . . Note=WD 10 +Q08924 UniProtKB Repeat 761 804 . . . Note=WD 11 +Q08924 UniProtKB Repeat 811 852 . . . Note=WD 12 +Q08924 UniProtKB Repeat 880 928 . . . Note=WD 13 +Q08924 UniProtKB Repeat 934 973 . . . Note=WD 14 +Q08924 UniProtKB Repeat 975 1013 . . . Note=WD 15 +##sequence-region P38739 1 605 +P38739 UniProtKB Signal peptide 1 26 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38739 UniProtKB Chain 27 605 . . . ID=PRO_0000041486;Note=Cell wall integrity and stress response component 4 +P38739 UniProtKB Transmembrane 415 435 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38739 UniProtKB Domain 27 110 . . . Note=WSC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00558 +P38739 UniProtKB Compositional bias 116 317 . . . Note=Ser/Thr-rich +P38739 UniProtKB Glycosylation 340 340 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38739 UniProtKB Glycosylation 386 386 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38739 UniProtKB Glycosylation 389 389 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38739 UniProtKB Glycosylation 398 398 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38739 UniProtKB Glycosylation 479 479 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38739 UniProtKB Glycosylation 553 553 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38739 UniProtKB Glycosylation 583 583 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43582 1 211 +P43582 UniProtKB Chain 1 211 . . . ID=PRO_0000076096;Note=WW domain-containing protein WWM1 +P43582 UniProtKB Domain 9 43 . . . Note=WW;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00224 +P43582 UniProtKB Compositional bias 40 121 . . . Note=Pro-rich +P43582 UniProtKB Compositional bias 64 123 . . . Note=Gln-rich +P43582 UniProtKB Compositional bias 135 208 . . . Note=Gly-rich +P43582 UniProtKB Compositional bias 164 210 . . . Note=Asp-rich +P43582 UniProtKB Modified residue 75 75 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43582 UniProtKB Modified residue 78 78 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43582 UniProtKB Cross-link 50 50 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P43582 UniProtKB Cross-link 60 60 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P40489 1 647 +P40489 UniProtKB Chain 1 647 . . . ID=PRO_0000066004;Note=Transcriptional repressor XBP1 +P40489 UniProtKB Domain 282 395 . . . Note=HTH APSES-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630 +P40489 UniProtKB DNA binding 318 339 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630 +P40489 UniProtKB Sequence conflict 106 107 . . . Note=LL->FV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07993 1 356 +Q07993 UniProtKB Chain 1 356 . . . ID=PRO_0000270925;Note=D-xylulose reductase +Q07993 UniProtKB Nucleotide binding 179 184 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07993 UniProtKB Metal binding 44 44 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07993 UniProtKB Metal binding 69 69 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07993 UniProtKB Metal binding 155 155 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53241 1 593 +P53241 UniProtKB Chain 1 593 . . . ID=PRO_0000121372;Note=Vitamin H transporter +P53241 UniProtKB Topological domain 1 121 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Transmembrane 122 142 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Topological domain 143 166 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Transmembrane 167 187 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Topological domain 188 190 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Transmembrane 191 211 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Topological domain 212 224 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Transmembrane 225 245 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Topological domain 246 291 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Transmembrane 292 312 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Topological domain 313 361 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Transmembrane 362 382 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Topological domain 383 408 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Transmembrane 409 429 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Topological domain 430 432 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Transmembrane 433 453 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Topological domain 454 460 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Transmembrane 461 481 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Topological domain 482 492 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Transmembrane 493 513 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Topological domain 514 526 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Transmembrane 527 547 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Topological domain 548 593 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53241 UniProtKB Modified residue 32 32 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53241 UniProtKB Modified residue 33 33 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53241 UniProtKB Modified residue 43 43 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40547 1 921 +P40547 UniProtKB Chain 1 921 . . . ID=PRO_0000065828;Note=Vacuolar import and degradation protein 28 +P40547 UniProtKB Modified residue 226 226 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P38784 1 181 +P38784 UniProtKB Chain 1 181 . . . ID=PRO_0000065876;Note=Vacuolar ATPase assembly protein VMA22 +P38784 UniProtKB Alternative sequence 1 5 . . . ID=VSP_058123;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38735 1 1592 +P38735 UniProtKB Chain 1 1592 . . . ID=PRO_0000093465;Note=ABC transporter ATP-binding protein/permease VMR1 +P38735 UniProtKB Topological domain 1 33 . . . Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38735 UniProtKB Transmembrane 34 54 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Topological domain 55 74 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38735 UniProtKB Transmembrane 75 95 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Topological domain 96 100 . . . Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38735 UniProtKB Transmembrane 101 121 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Topological domain 122 131 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38735 UniProtKB Transmembrane 132 152 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Topological domain 153 170 . . . Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38735 UniProtKB Transmembrane 171 191 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Topological domain 192 329 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38735 UniProtKB Transmembrane 330 350 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Topological domain 351 379 . . . Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38735 UniProtKB Transmembrane 380 400 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Topological domain 401 465 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38735 UniProtKB Transmembrane 466 486 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Topological domain 487 489 . . . Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38735 UniProtKB Transmembrane 490 510 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Topological domain 511 572 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38735 UniProtKB Transmembrane 573 593 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Topological domain 594 614 . . . Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38735 UniProtKB Transmembrane 615 635 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Topological domain 636 989 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38735 UniProtKB Transmembrane 990 1010 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Topological domain 1011 1051 . . . Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38735 UniProtKB Transmembrane 1052 1072 . . . Note=Helical%3B Name%3D13;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Topological domain 1073 1115 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38735 UniProtKB Transmembrane 1116 1136 . . . Note=Helical%3B Name%3D14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Topological domain 1137 1137 . . . Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38735 UniProtKB Transmembrane 1138 1158 . . . Note=Helical%3B Name%3D15;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Topological domain 1159 1229 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38735 UniProtKB Transmembrane 1230 1250 . . . Note=Helical%3B Name%3D16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Topological domain 1251 1252 . . . Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38735 UniProtKB Transmembrane 1253 1273 . . . Note=Helical%3B Name%3D17;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Topological domain 1274 1592 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38735 UniProtKB Domain 338 632 . . . Note=ABC transmembrane type-1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Domain 664 908 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P38735 UniProtKB Domain 981 1282 . . . Note=ABC transmembrane type-1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P38735 UniProtKB Domain 1323 1572 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P38735 UniProtKB Nucleotide binding 702 709 . . . Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P38735 UniProtKB Nucleotide binding 1357 1364 . . . Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P38735 UniProtKB Glycosylation 11 11 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38735 UniProtKB Glycosylation 370 370 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P20795 1 691 +P20795 UniProtKB Chain 1 691 . . . ID=PRO_0000206311;Note=Vacuolar protein sorting-associated protein 33 +P20795 UniProtKB Modified residue 626 626 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P34110 1 944 +P34110 UniProtKB Chain 1 944 . . . ID=PRO_0000065899;Note=Vacuolar protein sorting-associated protein 35 +P34110 UniProtKB Modified residue 846 846 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34110 UniProtKB Modified residue 848 848 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34110 UniProtKB Modified residue 868 868 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P34110 UniProtKB Sequence conflict 14 20 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P34110 UniProtKB Sequence conflict 661 661 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P23643 1 1011 +P23643 UniProtKB Chain 1 1011 . . . ID=PRO_0000065904;Note=Vacuolar protein sorting-associated protein 3 +P23643 UniProtKB Domain 143 418 . . . Note=CNH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00795 +##sequence-region P52917 1 437 +P52917 UniProtKB Chain 1 437 . . . ID=PRO_0000084760;Note=Vacuolar protein sorting-associated protein 4 +P52917 UniProtKB Domain 3 80 . . . Note=MIT +P52917 UniProtKB Nucleotide binding 173 180 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52917 UniProtKB Mutagenesis 64 64 . . . Note=Inhibits membrane protein sorting to the vacuole. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17928862;Dbxref=PMID:17928862 +P52917 UniProtKB Mutagenesis 179 179 . . . Note=No ATP hydrolysis. Missorting of vacuolar proteins. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9155008;Dbxref=PMID:9155008 +P52917 UniProtKB Mutagenesis 216 216 . . . Note=Abolishes oligomerization. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18272179;Dbxref=PMID:18272179 +P52917 UniProtKB Mutagenesis 233 233 . . . Note=Defective in ATP hydrolysis. Missorting of vacuolar proteins. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9155008;Dbxref=PMID:9155008 +P52917 UniProtKB Sequence conflict 32 32 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P52917 UniProtKB Helix 3 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FVK +P52917 UniProtKB Helix 26 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FVK +P52917 UniProtKB Helix 50 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FVK +P52917 UniProtKB Beta strand 123 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Helix 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Helix 139 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Helix 150 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Helix 156 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Beta strand 168 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Beta strand 174 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Helix 179 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Beta strand 193 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Helix 199 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Turn 204 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Helix 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Helix 210 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Beta strand 225 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Helix 234 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Turn 244 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIH +P52917 UniProtKB Helix 250 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Helix 261 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Beta strand 270 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Helix 279 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Helix 284 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Beta strand 292 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Helix 301 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Beta strand 313 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RKO +P52917 UniProtKB Helix 321 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Turn 330 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Helix 336 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Helix 349 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Beta strand 358 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Beta strand 373 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Beta strand 378 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHV +P52917 UniProtKB Beta strand 383 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Helix 388 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Helix 393 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QP9 +P52917 UniProtKB Helix 403 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Helix 421 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIE +P52917 UniProtKB Beta strand 433 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EIH +##sequence-region Q02725 1 835 +Q02725 UniProtKB Chain 1 835 . . . ID=PRO_0000065936;Note=Vacuolar transporter chaperone 3 +Q02725 UniProtKB Topological domain 1 709 . . . Note=Cytoplasmic +Q02725 UniProtKB Transmembrane 710 727 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02725 UniProtKB Topological domain 728 735 . . . Note=Vacuolar +Q02725 UniProtKB Transmembrane 736 756 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02725 UniProtKB Topological domain 757 778 . . . Note=Cytoplasmic +Q02725 UniProtKB Transmembrane 779 799 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02725 UniProtKB Topological domain 800 835 . . . Note=Vacuolar +Q02725 UniProtKB Domain 1 145 . . . Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714 +Q02725 UniProtKB Region 126 133 . . . Note=Important for inositol polyphosphate binding;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:27080106;Dbxref=PMID:27080106 +Q02725 UniProtKB Coiled coil 385 413 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02725 UniProtKB Site 22 22 . . . Note=Important for inositol polyphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43585 +Q02725 UniProtKB Site 26 26 . . . Note=Important for inositol polyphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43585 +Q02725 UniProtKB Modified residue 43 43 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q02725 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02725 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02725 UniProtKB Modified residue 183 183 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q02725 UniProtKB Modified residue 195 195 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02725 UniProtKB Modified residue 198 198 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q02725 UniProtKB Modified residue 270 270 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q02725 UniProtKB Modified residue 274 274 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q02725 UniProtKB Modified residue 589 589 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q02725 UniProtKB Modified residue 592 592 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950 +Q02725 UniProtKB Modified residue 621 621 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q02725 UniProtKB Modified residue 622 622 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P47075 1 721 +P47075 UniProtKB Chain 1 721 . . . ID=PRO_0000065937;Note=Vacuolar transporter chaperone 4 +P47075 UniProtKB Topological domain 1 630 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12584253;Dbxref=PMID:12584253 +P47075 UniProtKB Transmembrane 631 651 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47075 UniProtKB Transmembrane 652 672 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47075 UniProtKB Topological domain 673 699 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12584253;Dbxref=PMID:12584253 +P47075 UniProtKB Transmembrane 700 720 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47075 UniProtKB Topological domain 721 721 . . . Note=Vacuolar;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12584253;Dbxref=PMID:12584253 +P47075 UniProtKB Domain 1 148 . . . Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714 +P47075 UniProtKB Region 126 133 . . . Note=Important for inositol polyphosphate binding;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:27080106;Dbxref=PMID:27080106 +P47075 UniProtKB Site 22 22 . . . Note=Important for inositol polyphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43585 +P47075 UniProtKB Site 26 26 . . . Note=Important for inositol polyphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43585 +P47075 UniProtKB Cross-link 75 75 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P47075 UniProtKB Helix 2 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIG +P47075 UniProtKB Helix 15 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIT +P47075 UniProtKB Helix 22 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIT +P47075 UniProtKB Turn 36 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIT +P47075 UniProtKB Helix 42 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIT +P47075 UniProtKB Beta strand 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIQ +P47075 UniProtKB Helix 96 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIT +P47075 UniProtKB Helix 143 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIT +P47075 UniProtKB Helix 160 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIT +P47075 UniProtKB Turn 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIT +P47075 UniProtKB Beta strand 195 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Helix 205 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Helix 208 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Beta strand 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3R +P47075 UniProtKB Helix 232 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Beta strand 236 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Helix 248 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Beta strand 261 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Beta strand 275 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Helix 286 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Beta strand 293 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Helix 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Helix 304 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Beta strand 310 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIG +P47075 UniProtKB Helix 314 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Helix 329 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Beta strand 352 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Beta strand 369 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Turn 393 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3R +P47075 UniProtKB Beta strand 397 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Helix 414 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Beta strand 417 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Beta strand 423 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Helix 439 445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Beta strand 447 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3Q +P47075 UniProtKB Beta strand 450 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IIG +P47075 UniProtKB Helix 458 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +P47075 UniProtKB Turn 467 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3T +##sequence-region Q12416 1 295 +Q12416 UniProtKB Chain 1 295 . . . ID=PRO_0000262757;Note=G1-specific transcriptional repressor WHI5 +Q12416 UniProtKB Modified residue 47 47 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15210110;Dbxref=PMID:15210110 +Q12416 UniProtKB Modified residue 57 57 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12416 UniProtKB Modified residue 59 59 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:15210110;Dbxref=PMID:19779198,PMID:15210110 +Q12416 UniProtKB Modified residue 62 62 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:15210110;Dbxref=PMID:19779198,PMID:15210110 +Q12416 UniProtKB Modified residue 88 88 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12416 UniProtKB Modified residue 113 113 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12416 UniProtKB Modified residue 115 115 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12416 UniProtKB Modified residue 154 154 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12416 UniProtKB Modified residue 156 156 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12416 UniProtKB Modified residue 161 161 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15210110;Dbxref=PMID:15210110 +Q12416 UniProtKB Modified residue 262 262 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15210110;Dbxref=PMID:15210110 +Q12416 UniProtKB Modified residue 288 288 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12416 UniProtKB Modified residue 290 290 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38838 1 269 +P38838 UniProtKB Chain 1 269 . . . ID=PRO_0000202919;Note=DNA-dependent metalloprotease WSS1 +P38838 UniProtKB Domain 20 221 . . . Note=WLM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00730 +P38838 UniProtKB Region 161 208 . . . Note=Required and sufficient for binding to DNA +P38838 UniProtKB Motif 152 160 . . . Note=SHP box +P38838 UniProtKB Motif 209 219 . . . Note=VCP-interaction motif (VIM) +P38838 UniProtKB Motif 247 254 . . . Note=SUMO interaction motif 1 (SIM) +P38838 UniProtKB Motif 266 269 . . . Note=SUMO interaction motif 2 (SIM) +P38838 UniProtKB Active site 116 116 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P38838 UniProtKB Metal binding 115 115 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P38838 UniProtKB Metal binding 119 119 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P38838 UniProtKB Metal binding 125 125 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P38838 UniProtKB Mutagenesis 115 115 . . . Note=In wss1-pd%3B loss of function%3B when associated with A-119. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20516210;Dbxref=PMID:20516210 +P38838 UniProtKB Mutagenesis 116 116 . . . Note=Loss of function. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24998930;Dbxref=PMID:24998930 +P38838 UniProtKB Mutagenesis 119 119 . . . Note=In wss1-pd%3B loss of function%3B when associated with A-115. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20516210;Dbxref=PMID:20516210 +##sequence-region Q12363 1 437 +Q12363 UniProtKB Chain 1 437 . . . ID=PRO_0000051463;Note=Transcriptional modulator WTM1 +Q12363 UniProtKB Repeat 103 144 . . . Note=WD 1 +Q12363 UniProtKB Repeat 221 259 . . . Note=WD 2 +Q12363 UniProtKB Repeat 264 304 . . . Note=WD 3 +Q12363 UniProtKB Repeat 326 366 . . . Note=WD 4 +Q12363 UniProtKB Modified residue 187 187 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12363 UniProtKB Modified residue 200 200 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12363 UniProtKB Modified residue 370 370 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12363 UniProtKB Modified residue 406 406 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P36095 1 224 +P36095 UniProtKB Chain 1 224 . . . ID=PRO_0000211487;Note=Vacuolar protein-sorting-associated protein 24 +P36095 UniProtKB Cross-link 203 203 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P40343 1 622 +P40343 UniProtKB Chain 1 622 . . . ID=PRO_0000065893;Note=Vacuolar protein sorting-associated protein 27 +P40343 UniProtKB Domain 18 149 . . . Note=VHS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00218 +P40343 UniProtKB Domain 258 277 . . . Note=UIM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213 +P40343 UniProtKB Domain 301 320 . . . Note=UIM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213 +P40343 UniProtKB Zinc finger 170 230 . . . Note=FYVE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091 +P40343 UniProtKB Modified residue 157 157 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956 +P40343 UniProtKB Modified residue 495 495 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40343 UniProtKB Modified residue 613 613 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40343 UniProtKB Cross-link 294 294 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P40343 UniProtKB Mutagenesis 185 186 . . . Note=Decreases the association to PtdIns(3)P containing membranes. LL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12006563;Dbxref=PMID:12006563 +P40343 UniProtKB Mutagenesis 193 193 . . . Note=Decreases the association to PtdIns(3)P containing membranes. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12006563;Dbxref=PMID:12006563 +P40343 UniProtKB Mutagenesis 270 270 . . . Note=Reduces strongly the ubiquitin-binding activity. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11988742;Dbxref=PMID:11988742 +P40343 UniProtKB Mutagenesis 313 313 . . . Note=Reduces strongly the ubiquitin-binding activity. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11988742;Dbxref=PMID:11988742 +P40343 UniProtKB Sequence conflict 321 322 . . . Note=KL->NV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40343 UniProtKB Turn 177 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VFY +P40343 UniProtKB Turn 193 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VFY +P40343 UniProtKB Helix 201 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VFY +P40343 UniProtKB Beta strand 206 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VFY +P40343 UniProtKB Helix 211 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VFY +P40343 UniProtKB Beta strand 215 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VFY +P40343 UniProtKB Helix 223 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VFY +P40343 UniProtKB Beta strand 251 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q0V +P40343 UniProtKB Helix 259 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q0V +P40343 UniProtKB Helix 274 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q0W +P40343 UniProtKB Helix 304 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O06 +P40343 UniProtKB Helix 352 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW +P40343 UniProtKB Turn 375 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW +P40343 UniProtKB Helix 381 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW +##sequence-region P36116 1 164 +P36116 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P36116 UniProtKB Chain 2 164 . . . ID=PRO_0000065905;Note=Vacuolar protein sorting-associated protein 51 +P36116 UniProtKB Coiled coil 73 164 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36116 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P36116 UniProtKB Helix 16 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5K +##sequence-region P47061 1 822 +P47061 UniProtKB Chain 1 822 . . . ID=PRO_0000215193;Note=Vacuolar protein sorting-associated protein 53 +P47061 UniProtKB Coiled coil 34 58 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47061 UniProtKB Coiled coil 460 484 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47061 UniProtKB Helix 567 569 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4 +P47061 UniProtKB Helix 571 598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4 +P47061 UniProtKB Beta strand 605 608 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4 +P47061 UniProtKB Helix 615 638 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4 +P47061 UniProtKB Helix 639 643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4 +P47061 UniProtKB Helix 653 676 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4 +P47061 UniProtKB Helix 683 693 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4 +P47061 UniProtKB Helix 700 710 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4 +P47061 UniProtKB Helix 716 729 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4 +P47061 UniProtKB Helix 746 750 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4 +P47061 UniProtKB Helix 752 763 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4 +P47061 UniProtKB Helix 768 776 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS4 +##sequence-region O13554 1 104 +O13554 UniProtKB Chain 1 104 . . . ID=PRO_0000299781;Note=Putative uncharacterized protein VPS65 +O13554 UniProtKB Transmembrane 4 24 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13554 UniProtKB Transmembrane 80 100 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03388 1 795 +Q03388 UniProtKB Chain 1 795 . . . ID=PRO_0000065909;Note=Vacuolar protein sorting-associated protein 72 +Q03388 UniProtKB Region 1 281 . . . Note=Interaction with HTZ1 +Q03388 UniProtKB Coiled coil 28 63 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03388 UniProtKB Coiled coil 121 150 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03388 UniProtKB Coiled coil 204 281 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03388 UniProtKB Compositional bias 57 85 . . . Note=Asp-rich +Q03388 UniProtKB Compositional bias 315 343 . . . Note=Lys-rich +Q03388 UniProtKB Modified residue 425 425 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P40046 1 129 +P40046 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.3;Dbxref=PMID:22814378 +P40046 UniProtKB Chain 2 129 . . . ID=PRO_0000065934;Note=Vacuolar transporter chaperone 1 +P40046 UniProtKB Topological domain 2 32 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12584253;Dbxref=PMID:12584253 +P40046 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40046 UniProtKB Topological domain 54 59 . . . Note=Vacuolar;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12584253;Dbxref=PMID:12584253 +P40046 UniProtKB Transmembrane 60 80 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40046 UniProtKB Topological domain 81 98 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12584253;Dbxref=PMID:12584253 +P40046 UniProtKB Transmembrane 99 119 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40046 UniProtKB Topological domain 120 129 . . . Note=Vacuolar;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12584253;Dbxref=PMID:12584253 +P40046 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.3;Dbxref=PMID:22814378 +##sequence-region P43585 1 828 +P43585 UniProtKB Chain 1 828 . . . ID=PRO_0000065935;Note=Vacuolar transporter chaperone 2 +P43585 UniProtKB Topological domain 1 693 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43585 UniProtKB Transmembrane 694 716 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43585 UniProtKB Topological domain 717 727 . . . Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43585 UniProtKB Transmembrane 728 748 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43585 UniProtKB Topological domain 749 766 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43585 UniProtKB Transmembrane 767 787 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43585 UniProtKB Topological domain 788 828 . . . Note=Vacuolar;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43585 UniProtKB Domain 1 146 . . . Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714 +P43585 UniProtKB Region 127 134 . . . Note=Important for inositol polyphosphate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27080106;Dbxref=PMID:27080106 +P43585 UniProtKB Site 22 22 . . . Note=Important for inositol polyphosphate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27080106;Dbxref=PMID:27080106 +P43585 UniProtKB Site 26 26 . . . Note=Important for inositol polyphosphate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27080106;Dbxref=PMID:27080106 +P43585 UniProtKB Modified residue 182 182 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P43585 UniProtKB Modified residue 187 187 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P43585 UniProtKB Modified residue 196 196 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P43585 UniProtKB Modified residue 264 264 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P43585 UniProtKB Modified residue 583 583 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198 +P43585 UniProtKB Modified residue 615 615 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P43585 UniProtKB Modified residue 616 616 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P43585 UniProtKB Modified residue 620 620 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43585 UniProtKB Modified residue 626 626 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43585 UniProtKB Modified residue 657 657 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P43585 UniProtKB Mutagenesis 22 22 . . . Note=Decreases affinity for inositol polyphosphate. Strongly decreases affinity for inositol polyphosphate%3B when associated with A-26 and A-131. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27080106;Dbxref=PMID:27080106 +P43585 UniProtKB Mutagenesis 26 26 . . . Note=Decreases affinity for inositol polyphosphate. Strongly decreases affinity for inositol polyphosphate%3B when associated with F-22 and A-131. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27080106;Dbxref=PMID:27080106 +P43585 UniProtKB Mutagenesis 127 127 . . . Note=Abolishes inositol polyphosphate binding%3B when associated with A-130 and A-134. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27080106;Dbxref=PMID:27080106 +P43585 UniProtKB Mutagenesis 130 130 . . . Note=Abolishes inositol polyphosphate binding%3B when associated with A-127 and A-134. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27080106;Dbxref=PMID:27080106 +P43585 UniProtKB Mutagenesis 131 131 . . . Note=Decreases affinity for inositol polyphosphate. Strongly decreases affinity for inositol polyphosphate%3B when associated with F-22 and A-26. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27080106;Dbxref=PMID:27080106 +P43585 UniProtKB Mutagenesis 134 134 . . . Note=Abolishes inositol polyphosphate binding%3B when associated with A-127 and A-130. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27080106;Dbxref=PMID:27080106 +P43585 UniProtKB Beta strand 204 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Helix 212 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Beta strand 278 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Helix 289 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Beta strand 303 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Helix 312 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Beta strand 318 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Beta strand 336 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Helix 345 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Helix 348 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Helix 358 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Helix 374 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Beta strand 397 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Beta strand 416 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Beta strand 434 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Beta strand 444 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Beta strand 452 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Turn 457 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Helix 463 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Beta strand 466 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Beta strand 471 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Helix 503 509 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Helix 522 531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +P43585 UniProtKB Helix 532 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3G3O +##sequence-region P53832 1 503 +P53832 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53832 UniProtKB Chain 24 503 . . . ID=PRO_0000041484;Note=Cell wall integrity and stress response component 2 +P53832 UniProtKB Topological domain 24 325 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53832 UniProtKB Transmembrane 326 346 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53832 UniProtKB Topological domain 347 503 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53832 UniProtKB Domain 25 118 . . . Note=WSC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00558 +P53832 UniProtKB Compositional bias 121 319 . . . Note=Ser/Thr-rich +P53832 UniProtKB Modified residue 402 402 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53832 UniProtKB Modified residue 455 455 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53832 UniProtKB Modified residue 458 458 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P33418 1 1100 +P33418 UniProtKB Chain 1 1100 . . . ID=PRO_0000084460;Note=Exportin-T +##sequence-region Q12206 1 467 +Q12206 UniProtKB Chain 1 467 . . . ID=PRO_0000051464;Note=Transcriptional modulator WTM2 +Q12206 UniProtKB Repeat 244 282 . . . Note=WD 1 +Q12206 UniProtKB Repeat 287 327 . . . Note=WD 2 +Q12206 UniProtKB Repeat 349 389 . . . Note=WD 3 +Q12206 UniProtKB Compositional bias 87 98 . . . Note=Poly-Asp +##sequence-region P42826 1 600 +P42826 UniProtKB Chain 1 600 . . . ID=PRO_0000059563;Note=Xylulose kinase +P42826 UniProtKB Nucleotide binding 505 506 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42826 UniProtKB Binding site 110 110 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42826 UniProtKB Binding site 184 184 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42826 UniProtKB Binding site 299 299 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42826 UniProtKB Binding site 300 300 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42826 UniProtKB Binding site 383 383 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42826 UniProtKB Binding site 509 509 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42826 UniProtKB Modified residue 244 244 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P42826 UniProtKB Sequence conflict 497 502 . . . Note=PERTFF->QKGLFL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P33301 1 854 +P33301 UniProtKB Chain 1 854 . . . ID=PRO_0000066050;Note=DNA repair protein XRS2 +P33301 UniProtKB Compositional bias 836 843 . . . Note=Poly-Asp +P33301 UniProtKB Modified residue 349 349 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P33301 UniProtKB Modified residue 533 533 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P33301 UniProtKB Modified residue 534 534 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P33301 UniProtKB Modified residue 553 553 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33301 UniProtKB Modified residue 555 555 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q02792 1 1006 +Q02792 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7608167;Dbxref=PMID:7608167 +Q02792 UniProtKB Chain 2 1006 . . . ID=PRO_0000071399;Note=5'-3' exoribonuclease 2 +Q02792 UniProtKB Repeat 955 958 . . . Note=1-1 +Q02792 UniProtKB Repeat 961 964 . . . Note=2-1 +Q02792 UniProtKB Repeat 972 975 . . . Note=2-2 +Q02792 UniProtKB Repeat 975 978 . . . Note=3-1 +Q02792 UniProtKB Repeat 984 986 . . . Note=3-2 +Q02792 UniProtKB Repeat 996 999 . . . Note=1-2 +Q02792 UniProtKB Region 492 529 . . . Note=Required for retention in the nucleus +Q02792 UniProtKB Region 955 999 . . . Note=2 X 4 AA repeats of S-R-Y-D%2C N-N-N-Y%2C Y-S-G-N +Q02792 UniProtKB Coiled coil 256 287 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02792 UniProtKB Coiled coil 453 544 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02792 UniProtKB Compositional bias 933 1004 . . . Note=Asn-rich +Q02792 UniProtKB Modified residue 574 574 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02792 UniProtKB Mutagenesis 235 235 . . . Note=Abrogates exonuclease activity and impairs termination of transcription by RNA polymerase II. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15565157;Dbxref=PMID:15565157 +Q02792 UniProtKB Mutagenesis 518 518 . . . Note=Causes mislocalization to the cytoplasm and suppresses the requirement for XRN1 function. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315672;Dbxref=PMID:9315672 +Q02792 UniProtKB Mutagenesis 520 520 . . . Note=Suppresses the requirement for XRN1 function. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315672;Dbxref=PMID:9315672 +Q02792 UniProtKB Mutagenesis 534 534 . . . Note=Causes mislocalization to the cytoplasm%3B when associated with A-535 and A-537. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315672;Dbxref=PMID:9315672 +Q02792 UniProtKB Mutagenesis 535 535 . . . Note=Causes mislocalization to the cytoplasm%3B when associated with A-534 and A-537. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315672;Dbxref=PMID:9315672 +Q02792 UniProtKB Mutagenesis 535 535 . . . Note=Causes mislocalization to the cytoplasm and suppresses the requirement for XRN1 function. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315672;Dbxref=PMID:9315672 +Q02792 UniProtKB Mutagenesis 537 537 . . . Note=Causes mislocalization to the cytoplasm%3B when associated with A-534 and A-535. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315672;Dbxref=PMID:9315672 +Q02792 UniProtKB Mutagenesis 537 537 . . . Note=Causes mislocalization to the cytoplasm and suppresses the requirement for XRN1 function. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9315672;Dbxref=PMID:9315672 +Q02792 UniProtKB Mutagenesis 683 683 . . . Note=In allele TAP1-1%3B activates transcription of the promoter-defective yeast SUP4 tRNA(Tyr) allele SUP4A53T61. Y->H +##sequence-region P30822 1 1084 +P30822 UniProtKB Chain 1 1084 . . . ID=PRO_0000204710;Note=Exportin-1 +P30822 UniProtKB Domain 34 100 . . . Note=Importin N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00115 +P30822 UniProtKB Modified residue 1080 1080 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P30822 UniProtKB Helix 1 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Beta strand 7 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DIF +P30822 UniProtKB Helix 13 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 28 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 47 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 51 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 61 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 84 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 105 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 112 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Turn 130 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 137 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Turn 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 149 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Turn 171 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 176 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Beta strand 205 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HB2 +P30822 UniProtKB Helix 208 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Turn 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 227 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Beta strand 231 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 234 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 241 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 246 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 269 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 297 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 308 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 327 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 334 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 337 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 356 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Turn 414 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 417 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 421 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Beta strand 443 445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Beta strand 451 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 459 461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 462 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 480 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Beta strand 497 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAZ +P30822 UniProtKB Helix 502 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Turn 515 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 521 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 545 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 563 568 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 570 583 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 589 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 608 611 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Beta strand 617 619 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DHA +P30822 UniProtKB Helix 621 627 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 629 633 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Beta strand 634 636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HB3 +P30822 UniProtKB Helix 638 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 658 668 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 670 685 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 689 691 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 693 713 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 714 717 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 718 746 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 748 752 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 754 776 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 780 786 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 788 801 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 804 806 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 809 822 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 823 825 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 827 845 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Beta strand 849 852 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 853 869 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 872 875 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 879 893 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 898 918 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 922 944 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Beta strand 945 947 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 949 951 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 952 967 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Turn 978 980 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HB2 +P30822 UniProtKB Helix 987 1002 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 1008 1020 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Turn 1021 1023 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 1025 1038 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Beta strand 1041 1043 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 1046 1050 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P30822 UniProtKB Helix 1051 1054 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYG +P30822 UniProtKB Turn 1055 1057 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P30822 UniProtKB Helix 1079 1081 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VYC +##sequence-region Q03308 1 798 +Q03308 UniProtKB Chain 1 798 . . . ID=PRO_0000065891;Note=Vacuolar protein sorting-associated protein 16 +Q03308 UniProtKB Sequence conflict 100 100 . . . Note=L->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03308 UniProtKB Sequence conflict 170 170 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03308 UniProtKB Sequence conflict 326 340 . . . Note=AIEILKNFVLEKGVL->QLNIKEFCLREGCT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36017 1 210 +P36017 UniProtKB Chain 1 210 . . . ID=PRO_0000121325;Note=Vacuolar protein sorting-associated protein 21 +P36017 UniProtKB Nucleotide binding 14 21 . . . Note=GTP +P36017 UniProtKB Nucleotide binding 62 66 . . . Note=GTP +P36017 UniProtKB Nucleotide binding 120 123 . . . Note=GTP +P36017 UniProtKB Motif 36 44 . . . Note=Effector region;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36017 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36017 UniProtKB Modified residue 210 210 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36017 UniProtKB Lipidation 208 208 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36017 UniProtKB Lipidation 210 210 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36017 UniProtKB Mutagenesis 21 21 . . . Note=Locks VPS21 in its GDP-bound form by abolishing binding to GTP. S->L%2CN;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10021387,ECO:0000269|PubMed:10329739,ECO:0000269|PubMed:8137814;Dbxref=PMID:10021387,PMID:10329739,PMID:8137814 +P36017 UniProtKB Mutagenesis 66 66 . . . Note=Abolishes GTP hydrolysis. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10021387;Dbxref=PMID:10021387 +P36017 UniProtKB Beta strand 6 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0 +P36017 UniProtKB Helix 20 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0 +P36017 UniProtKB Beta strand 40 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0 +P36017 UniProtKB Beta strand 54 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0 +P36017 UniProtKB Helix 67 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0 +P36017 UniProtKB Helix 73 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0 +P36017 UniProtKB Beta strand 81 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0 +P36017 UniProtKB Helix 92 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0 +P36017 UniProtKB Beta strand 114 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0 +P36017 UniProtKB Helix 122 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0 +P36017 UniProtKB Helix 135 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0 +P36017 UniProtKB Beta strand 148 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0 +P36017 UniProtKB Turn 154 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0 +P36017 UniProtKB Helix 160 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EK0 +##sequence-region Q03897 1 1148 +Q03897 UniProtKB Chain 1 1148 . . . ID=PRO_0000253807;Note=Maintenance of telomere capping protein 5 +Q03897 UniProtKB Repeat 63 106 . . . Note=WD 1 +Q03897 UniProtKB Repeat 112 152 . . . Note=WD 2 +Q03897 UniProtKB Repeat 156 195 . . . Note=WD 3 +Q03897 UniProtKB Repeat 199 239 . . . Note=WD 4 +Q03897 UniProtKB Repeat 299 348 . . . Note=WD 5 +Q03897 UniProtKB Domain 432 543 . . . Note=RWD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00179 +Q03897 UniProtKB Modified residue 759 759 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P38189 1 126 +P38189 UniProtKB Chain 1 126 . . . ID=PRO_0000202453;Note=Putative uncharacterized membrane protein YBL062W +P38189 UniProtKB Topological domain 1 9 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38189 UniProtKB Transmembrane 10 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38189 UniProtKB Topological domain 31 73 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38189 UniProtKB Transmembrane 74 94 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38189 UniProtKB Topological domain 95 126 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38216 1 128 +P38216 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38216 UniProtKB Chain 2 128 . . . ID=PRO_0000202469;Note=Uncharacterized protein YBR016W +P38216 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38216 UniProtKB Cross-link 32 32 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P38239 1 180 +P38239 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38239 UniProtKB Chain 2 180 . . . ID=PRO_0000056335;Note=Uncharacterized RING finger protein YBR062C +P38239 UniProtKB Zinc finger 109 153 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +P38239 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P38243 1 211 +P38243 UniProtKB Chain 1 211 . . . ID=PRO_0000202478;Note=Uncharacterized protein YBR071W +P38243 UniProtKB Modified residue 182 182 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38243 UniProtKB Modified residue 184 184 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38243 UniProtKB Modified residue 186 186 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P32386 1 1661 +P32386 UniProtKB Chain 1 1661 . . . ID=PRO_0000093447;Note=ATP-dependent bile acid permease +P32386 UniProtKB Topological domain 1 33 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32386 UniProtKB Transmembrane 34 54 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Topological domain 55 74 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32386 UniProtKB Transmembrane 75 95 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Topological domain 96 133 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32386 UniProtKB Transmembrane 134 154 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Topological domain 155 166 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32386 UniProtKB Transmembrane 167 187 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Topological domain 188 205 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32386 UniProtKB Transmembrane 206 226 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Topological domain 227 345 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32386 UniProtKB Transmembrane 346 366 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Topological domain 367 393 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32386 UniProtKB Transmembrane 394 414 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Topological domain 415 495 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32386 UniProtKB Transmembrane 496 516 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Topological domain 517 519 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32386 UniProtKB Transmembrane 520 540 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Topological domain 541 602 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32386 UniProtKB Transmembrane 603 623 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Topological domain 624 644 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32386 UniProtKB Transmembrane 645 665 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Topological domain 666 1053 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32386 UniProtKB Transmembrane 1054 1074 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Topological domain 1075 1114 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32386 UniProtKB Transmembrane 1115 1135 . . . Note=Helical%3B Name%3D13;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Topological domain 1136 1178 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32386 UniProtKB Transmembrane 1179 1199 . . . Note=Helical%3B Name%3D14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Topological domain 1200 1200 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32386 UniProtKB Transmembrane 1201 1221 . . . Note=Helical%3B Name%3D15;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Topological domain 1222 1292 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32386 UniProtKB Transmembrane 1293 1313 . . . Note=Helical%3B Name%3D16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Topological domain 1314 1315 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32386 UniProtKB Transmembrane 1316 1336 . . . Note=Helical%3B Name%3D17;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Topological domain 1337 1661 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32386 UniProtKB Domain 354 662 . . . Note=ABC transmembrane type-1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Domain 694 935 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P32386 UniProtKB Domain 1026 1345 . . . Note=ABC transmembrane type-1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P32386 UniProtKB Domain 1381 1636 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P32386 UniProtKB Nucleotide binding 729 736 . . . Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P32386 UniProtKB Nucleotide binding 1415 1422 . . . Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P32386 UniProtKB Modified residue 936 936 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P32386 UniProtKB Modified residue 940 940 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32386 UniProtKB Modified residue 955 955 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32386 UniProtKB Glycosylation 6 6 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32386 UniProtKB Glycosylation 97 97 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32386 UniProtKB Sequence conflict 172 174 . . . Note=TIT->QIH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32386 UniProtKB Sequence conflict 188 189 . . . Note=LR->FS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38109 1 508 +P38109 UniProtKB Chain 1 508 . . . ID=PRO_0000120563;Note=Putative serine carboxypeptidase YBR139W +P38109 UniProtKB Active site 219 219 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38109 UniProtKB Active site 415 415 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38109 UniProtKB Active site 474 474 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q96VG8 1 41 +Q96VG8 UniProtKB Chain 1 41 . . . ID=PRO_0000299836;Note=Putative uncharacterized protein YCR038W-A +##sequence-region P25383 1 438 +P25383 UniProtKB Chain 1 438 . . . ID=PRO_0000203495;Note=Transposon Ty2-C Gag polyprotein +P25383 UniProtKB Chain 1 397 . . . ID=PRO_0000279282;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25383 UniProtKB Peptide 398 438 . . . ID=PRO_0000279283;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25383 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25383 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25383 UniProtKB Sequence conflict 174 174 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25383 UniProtKB Sequence conflict 174 174 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25349 1 247 +P25349 UniProtKB Chain 1 244 . . . ID=PRO_0000200768;Note=Flavoprotein-like protein YCP4 +P25349 UniProtKB Propeptide 245 247 . . . ID=PRO_0000366191;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25349 UniProtKB Domain 4 193 . . . Note=Flavodoxin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00088 +P25349 UniProtKB Modified residue 244 244 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25349 UniProtKB Lipidation 243 243 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107 +P25349 UniProtKB Lipidation 244 244 . . . Note=S-farnesyl cysteine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P25617 1 290 +P25617 UniProtKB Chain 1 290 . . . ID=PRO_0000202563;Note=Uncharacterized protein YCR016W +P25617 UniProtKB Compositional bias 52 98 . . . Note=Lys-rich +##sequence-region P25351 1 611 +P25351 UniProtKB Chain 1 611 . . . ID=PRO_0000173425;Note=Uncharacterized membrane protein YCR023C +P25351 UniProtKB Topological domain 1 89 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25351 UniProtKB Transmembrane 90 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25351 UniProtKB Topological domain 111 152 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25351 UniProtKB Transmembrane 153 173 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25351 UniProtKB Topological domain 174 199 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25351 UniProtKB Transmembrane 200 220 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25351 UniProtKB Topological domain 221 353 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25351 UniProtKB Transmembrane 354 372 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25351 UniProtKB Topological domain 373 413 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25351 UniProtKB Transmembrane 414 434 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25351 UniProtKB Topological domain 435 442 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25351 UniProtKB Transmembrane 443 463 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25351 UniProtKB Topological domain 464 542 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25351 UniProtKB Transmembrane 543 563 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25351 UniProtKB Topological domain 564 611 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25351 UniProtKB Modified residue 313 313 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P25351 UniProtKB Modified residue 603 603 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P25361 1 127 +P25361 UniProtKB Chain 1 127 . . . ID=PRO_0000202568;Note=Uncharacterized protein YCR043C +##sequence-region P25639 1 631 +P25639 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Chain 21 631 . . . ID=PRO_0000014313;Note=Uncharacterized membrane protein YCR061W +P25639 UniProtKB Topological domain 21 105 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Transmembrane 106 126 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Topological domain 127 131 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Transmembrane 132 152 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Topological domain 153 170 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Transmembrane 171 191 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Topological domain 192 322 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Transmembrane 323 343 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Topological domain 344 351 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Transmembrane 352 372 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Topological domain 373 407 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Transmembrane 408 428 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Topological domain 429 451 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Transmembrane 452 472 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Topological domain 473 529 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Transmembrane 530 550 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Topological domain 551 598 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Transmembrane 599 619 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Topological domain 620 631 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Modified residue 219 219 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P25639 UniProtKB Glycosylation 87 87 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Glycosylation 98 98 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25639 UniProtKB Cross-link 250 250 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q12489 1 107 +Q12489 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12489 UniProtKB Chain 2 107 . . . ID=PRO_0000248456;Note=Cysteine-rich and transmembrane domain-containing protein YDL012C +Q12489 UniProtKB Transmembrane 82 101 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12489 UniProtKB Compositional bias 37 80 . . . Note=Gln-rich +Q12489 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12489 UniProtKB Cross-link 13 13 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q03205 1 200 +Q03205 UniProtKB Chain 1 200 . . . ID=PRO_0000242648;Note=Uncharacterized protein YDR042C +##sequence-region Q07438 1 124 +Q07438 UniProtKB Chain 1 124 . . . ID=PRO_0000299854;Note=Putative uncharacterized protein YDL071C +##sequence-region Q03193 1 310 +Q03193 UniProtKB Chain 1 310 . . . ID=PRO_0000244443;Note=Uncharacterized membrane protein YDR090C +Q03193 UniProtKB Topological domain 1 6 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03193 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03193 UniProtKB Topological domain 28 36 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03193 UniProtKB Transmembrane 37 57 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03193 UniProtKB Topological domain 58 61 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03193 UniProtKB Transmembrane 62 82 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03193 UniProtKB Topological domain 83 96 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03193 UniProtKB Transmembrane 97 117 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03193 UniProtKB Topological domain 118 131 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03193 UniProtKB Transmembrane 132 152 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03193 UniProtKB Topological domain 153 164 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03193 UniProtKB Transmembrane 165 185 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03193 UniProtKB Topological domain 186 191 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03193 UniProtKB Transmembrane 192 212 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03193 UniProtKB Topological domain 213 310 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03193 UniProtKB Domain 5 69 . . . Note=PQ-loop 1 +Q03193 UniProtKB Domain 138 194 . . . Note=PQ-loop 2 +Q03193 UniProtKB Modified residue 229 229 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q03193 UniProtKB Glycosylation 251 251 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03193 UniProtKB Glycosylation 259 259 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07589 1 356 +Q07589 UniProtKB Chain 1 356 . . . ID=PRO_0000202587;Note=Uncharacterized protein YDL144C +##sequence-region P0C2I2 1 1755 +P0C2I2 UniProtKB Chain 1 1755 . . . ID=PRO_0000279025;Note=Transposon Ty1-DR5 Gag-Pol polyprotein +P0C2I2 UniProtKB Chain 1 401 . . . ID=PRO_0000279026;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I2 UniProtKB Chain 402 582 . . . ID=PRO_0000279027;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I2 UniProtKB Chain 583 1217 . . . ID=PRO_0000279028;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I2 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279029;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I2 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I2 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +P0C2I2 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +P0C2I2 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I2 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +P0C2I2 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I2 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0C2I2 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +P0C2I2 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I2 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I2 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I2 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I2 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I2 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I2 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I2 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I2 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I2 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I2 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q12307 1 118 +Q12307 UniProtKB Chain 1 118 . . . ID=PRO_0000299860;Note=Putative uncharacterized protein YDL162C +##sequence-region Q12257 1 170 +Q12257 UniProtKB Chain 1 170 . . . ID=PRO_0000207658;Note=IMPACT family member YDL177C +##sequence-region P48569 1 320 +P48569 UniProtKB Chain 1 320 . . . ID=PRO_0000202590;Note=Uncharacterized protein YDL183C +##sequence-region Q03482 1 75 +Q03482 UniProtKB Chain 1 75 . . . ID=PRO_0000253837;Note=Cysteine-rich and transmembrane domain-containing protein YDR210W +Q03482 UniProtKB Transmembrane 52 69 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03482 UniProtKB Repeat 4 13 . . . Note=1 +Q03482 UniProtKB Repeat 14 23 . . . Note=2 +Q03482 UniProtKB Repeat 24 33 . . . Note=3 +Q03482 UniProtKB Region 4 33 . . . Note=3 X 10 AA tandem repeats of Q-Q-G-Y-Y-Q-Q-G-P-P +Q03482 UniProtKB Compositional bias 3 49 . . . Note=Gln-rich +Q03482 UniProtKB Compositional bias 55 73 . . . Note=Cys-rich +##sequence-region Q12472 1 1770 +Q12472 UniProtKB Chain 1 1770 . . . ID=PRO_0000279284;Note=Transposon Ty2-DR1 Gag-Pol polyprotein +Q12472 UniProtKB Chain 1 397 . . . ID=PRO_0000279285;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12472 UniProtKB Chain 398 578 . . . ID=PRO_0000279286;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12472 UniProtKB Chain 579 1232 . . . ID=PRO_0000279287;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12472 UniProtKB Chain 1233 1770 . . . ID=PRO_0000279288;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12472 UniProtKB Domain 656 831 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12472 UniProtKB Domain 1353 1491 . . . Note=Reverse transcriptase Ty1/copia-type +Q12472 UniProtKB Domain 1625 1767 . . . Note=RNase H Ty1/copia-type +Q12472 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12472 UniProtKB Region 579 636 . . . Note=Integrase-type zinc finger-like +Q12472 UniProtKB Motif 1193 1227 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12472 UniProtKB Active site 457 457 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12472 UniProtKB Metal binding 667 667 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12472 UniProtKB Metal binding 732 732 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12472 UniProtKB Metal binding 1361 1361 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12472 UniProtKB Metal binding 1442 1442 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12472 UniProtKB Metal binding 1443 1443 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12472 UniProtKB Metal binding 1625 1625 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12472 UniProtKB Metal binding 1667 1667 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12472 UniProtKB Metal binding 1700 1700 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12472 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12472 UniProtKB Site 578 579 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12472 UniProtKB Site 1232 1233 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q03780 1 787 +Q03780 UniProtKB Chain 1 787 . . . ID=PRO_0000253839;Note=Uncharacterized protein YDR239C +Q03780 UniProtKB Compositional bias 151 155 . . . Note=Poly-Pro +Q03780 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q03780 UniProtKB Modified residue 63 63 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03780 UniProtKB Modified residue 254 254 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03780 UniProtKB Modified residue 313 313 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03780 UniProtKB Modified residue 342 342 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03780 UniProtKB Modified residue 345 345 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03780 UniProtKB Modified residue 390 390 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03780 UniProtKB Modified residue 477 477 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q03780 UniProtKB Modified residue 492 492 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03780 UniProtKB Modified residue 546 546 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03780 UniProtKB Modified residue 683 683 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03780 UniProtKB Modified residue 699 699 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P0C5L8 1 45 +P0C5L8 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C5L8 UniProtKB Chain 20 45 . . . ID=PRO_0000309016;Note=Putative uncharacterized protein YDL240C-A +##sequence-region Q03788 1 91 +Q03788 UniProtKB Chain 1 91 . . . ID=PRO_0000299878;Note=Putative uncharacterized protein YDR250C +Q03788 UniProtKB Transmembrane 12 34 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGP6 1 47 +Q8TGP6 UniProtKB Chain 1 47 . . . ID=PRO_0000299886;Note=Putative uncharacterized protein YDR354C-A +##sequence-region Q04069 1 103 +Q04069 UniProtKB Chain 1 103 . . . ID=PRO_0000299892;Note=Putative uncharacterized protein YDR431W +Q04069 UniProtKB Transmembrane 37 57 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P87273 1 111 +P87273 UniProtKB Chain 1 111 . . . ID=PRO_0000299902;Note=Putative uncharacterized protein YDR521W +P87273 UniProtKB Transmembrane 18 38 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P87273 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PZE8 1 133 +A0A023PZE8 UniProtKB Chain 1 133 . . . ID=PRO_0000430985;Note=Uncharacterized protein YDR157W +##sequence-region Q2V2P8 1 89 +Q2V2P8 UniProtKB Chain 1 89 . . . ID=PRO_0000253848;Note=Uncharacterized protein YDR374W-A +##sequence-region Q02217 1 200 +Q02217 UniProtKB Chain 1 200 . . . ID=PRO_0000299907;Note=Putative uncharacterized protein YEL034C-A +Q02217 UniProtKB Transmembrane 7 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02217 UniProtKB Sequence conflict 138 139 . . . Note=VD->TS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q02217 UniProtKB Sequence conflict 170 170 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40102 1 141 +P40102 UniProtKB Chain 1 141 . . . ID=PRO_0000202663;Note=Uncharacterized protein YER187W +##sequence-region P40001 1 126 +P40001 UniProtKB Chain 1 126 . . . ID=PRO_0000202616;Note=Uncharacterized protein YEL008W +##sequence-region P34225 1 687 +P34225 UniProtKB Chain 1 687 . . . ID=PRO_0000120222;Note=Guanine-nucleotide exchange factor YEL1 +P34225 UniProtKB Domain 61 266 . . . Note=SEC7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00189 +P34225 UniProtKB Domain 412 551 . . . Note=PH +P34225 UniProtKB Modified residue 290 290 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34225 UniProtKB Modified residue 293 293 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P34225 UniProtKB Modified residue 299 299 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40062 1 109 +P40062 UniProtKB Chain 1 109 . . . ID=PRO_0000202643;Note=Putative uncharacterized protein YER097W +##sequence-region Q04210 1 160 +Q04210 UniProtKB Chain 1 160 . . . ID=PRO_0000203275;Note=Endoplasmic reticulum transmembrane protein 2 +Q04210 UniProtKB Topological domain 1 2 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04210 UniProtKB Transmembrane 3 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04210 UniProtKB Topological domain 24 45 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04210 UniProtKB Transmembrane 46 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04210 UniProtKB Topological domain 67 103 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04210 UniProtKB Transmembrane 104 124 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04210 UniProtKB Topological domain 125 160 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04210 UniProtKB Motif 157 160 . . . Note=Di-lysine motif +##sequence-region A0A023PZD0 1 216 +A0A023PZD0 UniProtKB Chain 1 216 . . . ID=PRO_0000431012;Note=Putative uncharacterized protein YFR036W-A +A0A023PZD0 UniProtKB Transmembrane 1 21 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZD0 UniProtKB Compositional bias 11 16 . . . Note=Poly-Phe;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZD0 UniProtKB Compositional bias 38 189 . . . Note=Ser-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00016 +##sequence-region P43576 1 117 +P43576 UniProtKB Chain 1 117 . . . ID=PRO_0000202677;Note=Uncharacterized protein YFL019C +##sequence-region P43539 1 102 +P43539 UniProtKB Chain 1 102 . . . ID=PRO_0000202668;Note=Uncharacterized protein YFL065C +##sequence-region P43537 1 175 +P43537 UniProtKB Chain 1 175 . . . ID=PRO_0000202667;Note=Uncharacterized membrane protein YFL067W +P43537 UniProtKB Topological domain 1 2 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43537 UniProtKB Transmembrane 3 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43537 UniProtKB Topological domain 24 151 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43537 UniProtKB Transmembrane 152 172 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43537 UniProtKB Topological domain 173 175 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43590 1 535 +P43590 UniProtKB Chain 1 535 . . . ID=PRO_0000185099;Note=Uncharacterized peptidase YFR006W +P43590 UniProtKB Transmembrane 8 24 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43590 UniProtKB Metal binding 316 316 . . . Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43590 UniProtKB Metal binding 327 327 . . . Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43590 UniProtKB Metal binding 327 327 . . . Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43590 UniProtKB Metal binding 412 412 . . . Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43590 UniProtKB Metal binding 452 452 . . . Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43590 UniProtKB Metal binding 493 493 . . . Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43590 UniProtKB Metal binding 493 493 . . . Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43590 UniProtKB Cross-link 50 50 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P43590 UniProtKB Sequence conflict 326 326 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P43591 1 353 +P43591 UniProtKB Chain 1 353 . . . ID=PRO_0000202683;Note=ATP-dependent kinase YFH7 +P43591 UniProtKB Nucleotide binding 31 39 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43591 UniProtKB Helix 4 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Turn 18 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Beta strand 25 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Helix 37 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Beta strand 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Helix 84 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Turn 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Helix 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Beta strand 109 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Beta strand 121 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Helix 129 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Beta strand 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Beta strand 155 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Helix 161 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Helix 168 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Beta strand 174 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Helix 178 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Turn 182 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Helix 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Helix 192 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Helix 222 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Beta strand 237 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Turn 244 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Beta strand 248 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Beta strand 262 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Helix 275 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Turn 286 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Beta strand 290 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Helix 299 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Helix 319 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Turn 330 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Helix 335 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +P43591 UniProtKB Beta strand 347 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GA8 +##sequence-region Q03186 1 124 +Q03186 UniProtKB Chain 1 124 . . . ID=PRO_0000299918;Note=Putative uncharacterized protein YFL012W-A +Q03186 UniProtKB Transmembrane 83 100 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGP0 1 49 +Q8TGP0 UniProtKB Chain 1 49 . . . ID=PRO_0000299921;Note=Putative uncharacterized protein YGL063C-A +##sequence-region Q3E816 1 71 +Q3E816 UniProtKB Chain 1 71 . . . ID=PRO_0000245383;Note=Uncharacterized protein YGR121W-A +##sequence-region Q3E744 1 92 +Q3E744 UniProtKB Chain 1 92 . . . ID=PRO_0000245385;Note=Uncharacterized protein YGR161W-C +##sequence-region P0CX96 1 160 +P0CX96 UniProtKB Chain 1 160 . . . ID=PRO_0000410453;Note=UPF0479 membrane protein YGR296C-B +P0CX96 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX96 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX96 UniProtKB Compositional bias 103 106 . . . Note=Poly-Ser +##sequence-region P53265 1 400 +P53265 UniProtKB Chain 1 400 . . . ID=PRO_0000202814;Note=Uncharacterized protein YGR111W +##sequence-region P53270 1 476 +P53270 UniProtKB Chain 1 476 . . . ID=PRO_0000202817;Note=Uncharacterized protein YGR117C +P53270 UniProtKB Domain 7 39 . . . Note=LisH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00126 +##sequence-region P53273 1 1036 +P53273 UniProtKB Chain 1 1036 . . . ID=PRO_0000202819;Note=Uncharacterized vacuolar membrane protein YGR125W +P53273 UniProtKB Topological domain 1 213 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Transmembrane 214 234 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Topological domain 235 236 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Transmembrane 237 257 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Topological domain 258 269 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Transmembrane 270 290 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Topological domain 291 300 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Transmembrane 301 321 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Topological domain 322 338 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Transmembrane 339 359 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Topological domain 360 375 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Transmembrane 376 396 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Topological domain 397 405 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Transmembrane 406 426 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Topological domain 427 473 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Transmembrane 474 494 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Topological domain 495 515 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Transmembrane 516 536 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Topological domain 537 546 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Transmembrane 547 567 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Topological domain 568 568 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Transmembrane 569 589 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Topological domain 590 604 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Transmembrane 605 625 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Topological domain 626 664 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Transmembrane 665 685 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Topological domain 686 1036 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53273 UniProtKB Domain 660 781 . . . Note=STAS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00198 +P53273 UniProtKB Modified residue 42 42 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198 +P53273 UniProtKB Modified residue 127 127 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53273 UniProtKB Modified residue 130 130 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53273 UniProtKB Modified residue 140 140 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53273 UniProtKB Modified residue 144 144 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53273 UniProtKB Modified residue 149 149 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53273 UniProtKB Modified residue 152 152 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P53273 UniProtKB Modified residue 153 153 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P53273 UniProtKB Modified residue 842 842 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53273 UniProtKB Modified residue 847 847 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P48236 1 432 +P48236 UniProtKB Chain 1 432 . . . ID=PRO_0000202829;Note=Uncharacterized membrane protein YGR149W +P48236 UniProtKB Topological domain 1 110 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48236 UniProtKB Transmembrane 111 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48236 UniProtKB Topological domain 132 132 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48236 UniProtKB Transmembrane 133 153 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48236 UniProtKB Topological domain 154 162 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48236 UniProtKB Transmembrane 163 183 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48236 UniProtKB Topological domain 184 187 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48236 UniProtKB Transmembrane 188 208 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48236 UniProtKB Topological domain 209 221 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48236 UniProtKB Transmembrane 222 242 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48236 UniProtKB Topological domain 243 319 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48236 UniProtKB Transmembrane 320 342 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48236 UniProtKB Topological domain 343 346 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48236 UniProtKB Transmembrane 347 369 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48236 UniProtKB Topological domain 370 432 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48236 UniProtKB Modified residue 78 78 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P42942 1 411 +P42942 UniProtKB Chain 1 411 . . . ID=PRO_0000122467;Note=Uncharacterized GTP-binding protein YGR210C +P42942 UniProtKB Domain 5 274 . . . Note=OBG-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +P42942 UniProtKB Nucleotide binding 11 18 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +P42942 UniProtKB Nucleotide binding 83 87 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +##sequence-region P53321 1 146 +P53321 UniProtKB Chain 1 146 . . . ID=PRO_0000202861;Note=Putative uncharacterized protein YGR259C +##sequence-region P53340 1 73 +P53340 UniProtKB Chain 1 73 . . . ID=PRO_0000202873;Note=Putative uncharacterized protein YGR291C +##sequence-region Q8TGT4 1 77 +Q8TGT4 UniProtKB Chain 1 77 . . . ID=PRO_0000245398;Note=Uncharacterized protein YHR213W-A +Q8TGT4 UniProtKB Transmembrane 13 33 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CX91 1 67 +P0CX91 UniProtKB Chain 1 67 . . . ID=PRO_0000410450;Note=Uncharacterized protein YHR212W-A +##sequence-region P0C5N4 1 26 +P0C5N4 UniProtKB Chain 1 26 . . . ID=PRO_0000309032;Note=Uncharacterized protein YHR073C-B +##sequence-region P38750 1 627 +P38750 UniProtKB Chain 1 627 . . . ID=PRO_0000094729;Note=Uncharacterized transporter YHL008C +P38750 UniProtKB Topological domain 1 32 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38750 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38750 UniProtKB Topological domain 54 66 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38750 UniProtKB Transmembrane 67 87 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38750 UniProtKB Topological domain 88 113 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38750 UniProtKB Transmembrane 114 134 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38750 UniProtKB Topological domain 135 165 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38750 UniProtKB Transmembrane 166 186 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38750 UniProtKB Topological domain 187 192 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38750 UniProtKB Transmembrane 193 213 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38750 UniProtKB Topological domain 214 218 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38750 UniProtKB Transmembrane 219 239 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38750 UniProtKB Topological domain 240 245 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38750 UniProtKB Transmembrane 246 266 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38750 UniProtKB Topological domain 267 627 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38750 UniProtKB Modified residue 305 305 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38750 UniProtKB Modified residue 546 546 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38750 UniProtKB Modified residue 588 588 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38726 1 115 +P38726 UniProtKB Chain 1 115 . . . ID=PRO_0000202877;Note=Putative UPF0377 protein YHL045W +P38726 UniProtKB Transmembrane 10 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38708 1 688 +P38708 UniProtKB Chain 1 688 . . . ID=PRO_0000139355;Note=Putative proline--tRNA ligase YHR020W +P38708 UniProtKB Modified residue 149 149 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38708 UniProtKB Modified residue 170 170 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38708 UniProtKB Modified residue 655 655 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38763 1 256 +P38763 UniProtKB Chain 1 256 . . . ID=PRO_0000202890;Note=Uncharacterized protein YHR022C +P38763 UniProtKB Nucleotide binding 29 36 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38780 1 354 +P38780 UniProtKB Chain 1 354 . . . ID=PRO_0000202896;Note=Uncharacterized protein YHR054C +##sequence-region P38808 1 164 +P38808 UniProtKB Chain 1 164 . . . ID=PRO_0000202906;Note=Putative uncharacterized protein YHR095W +P38808 UniProtKB Compositional bias 111 119 . . . Note=Poly-Lys +##sequence-region P38716 1 378 +P38716 UniProtKB Chain 1 378 . . . ID=PRO_0000114766;Note=Uncharacterized trans-sulfuration enzyme YHR112C +P38716 UniProtKB Modified residue 198 198 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38835 1 850 +P38835 UniProtKB Chain 1 850 . . . ID=PRO_0000202917;Note=PH domain-containing protein YHR131C +P38835 UniProtKB Domain 194 306 . . . Note=PH +P38835 UniProtKB Compositional bias 318 339 . . . Note=Arg-rich +P38835 UniProtKB Compositional bias 796 845 . . . Note=Asp-rich +##sequence-region P38864 1 112 +P38864 UniProtKB Chain 1 112 . . . ID=PRO_0000202931;Note=Uncharacterized protein YHR173C +##sequence-region P40514 1 678 +P40514 UniProtKB Chain 1 678 . . . ID=PRO_0000202981;Note=Uncharacterized protein YIL067C +P40514 UniProtKB Transmembrane 119 139 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40514 UniProtKB Transmembrane 245 265 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40514 UniProtKB Transmembrane 317 337 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40514 UniProtKB Transmembrane 340 360 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40514 UniProtKB Transmembrane 371 391 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40514 UniProtKB Transmembrane 405 425 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40514 UniProtKB Transmembrane 443 463 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40514 UniProtKB Transmembrane 475 495 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40514 UniProtKB Transmembrane 519 539 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40514 UniProtKB Sequence conflict 644 644 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40500 1 205 +P40500 UniProtKB Chain 1 205 . . . ID=PRO_0000202976;Note=Uncharacterized membrane protein YIL089W +P40500 UniProtKB Topological domain 1 63 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40500 UniProtKB Transmembrane 64 84 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40500 UniProtKB Topological domain 85 124 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40500 UniProtKB Transmembrane 125 145 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40500 UniProtKB Topological domain 146 205 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40490 1 117 +P40490 UniProtKB Chain 1 117 . . . ID=PRO_0000202968;Note=Putative uncharacterized protein YIL100W +##sequence-region P40461 1 129 +P40461 UniProtKB Chain 1 129 . . . ID=PRO_0000202959;Note=Putative uncharacterized protein YIL141W +##sequence-region P40588 1 61 +P40588 UniProtKB Chain 1 61 . . . ID=PRO_0000207535;Note=Putative uncharacterized protein YIR044C +##sequence-region Q3E827 1 93 +Q3E827 UniProtKB Chain 1 93 . . . ID=PRO_0000245415;Note=Uncharacterized protein YJR005C-A +Q3E827 UniProtKB Coiled coil 20 83 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGN2 1 85 +Q8TGN2 UniProtKB Chain 1 85 . . . ID=PRO_0000299764;Note=Putative uncharacterized protein YJL020W-A +Q8TGN2 UniProtKB Compositional bias 5 17 . . . Note=Poly-Ser +Q8TGN2 UniProtKB Compositional bias 66 83 . . . Note=Poly-Ser +##sequence-region Q3E737 1 44 +Q3E737 UniProtKB Chain 1 44 . . . ID=PRO_0000245414;Note=Uncharacterized protein YJL047C-A +##sequence-region P47106 1 120 +P47106 UniProtKB Chain 1 120 . . . ID=PRO_0000203092;Note=Putative uncharacterized protein YJR038C +P47106 UniProtKB Transmembrane 26 46 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47106 UniProtKB Transmembrane 57 77 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E743 1 109 +Q3E743 UniProtKB Chain 1 109 . . . ID=PRO_0000245416;Note=Uncharacterized protein YJR112W-A +Q3E743 UniProtKB Transmembrane 90 107 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E7A3 1 74 +Q3E7A3 UniProtKB Chain 1 74 . . . ID=PRO_0000245409;Note=Uncharacterized protein YJL133C-A +Q3E7A3 UniProtKB Transmembrane 8 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47131 1 105 +P47131 UniProtKB Chain 1 105 . . . ID=PRO_0000203105;Note=TMEM14 protein homolog YJR085C +P47131 UniProtKB Transmembrane 26 46 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47131 UniProtKB Transmembrane 53 73 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47131 UniProtKB Transmembrane 77 97 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47059 1 104 +P47059 UniProtKB Chain 1 104 . . . ID=PRO_0000203070;Note=Putative uncharacterized protein YJL032W +##sequence-region P46991 1 170 +P46991 UniProtKB Chain 1 170 . . . ID=PRO_0000203024;Note=Putative uncharacterized membrane protein YJL175W +P46991 UniProtKB Topological domain 1 15 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46991 UniProtKB Transmembrane 16 36 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46991 UniProtKB Topological domain 37 76 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46991 UniProtKB Transmembrane 77 97 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46991 UniProtKB Topological domain 98 119 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46991 UniProtKB Transmembrane 120 140 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46991 UniProtKB Topological domain 141 170 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39541 1 233 +P39541 UniProtKB Chain 1 233 . . . ID=PRO_0000203018;Note=Putative uncharacterized protein YJL195C +P39541 UniProtKB Transmembrane 78 98 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39541 UniProtKB Transmembrane 113 133 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39541 UniProtKB Transmembrane 188 208 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39529 1 758 +P39529 UniProtKB Chain 1 758 . . . ID=PRO_0000114999;Note=Putative transcriptional regulatory protein YJL206C +P39529 UniProtKB DNA binding 47 73 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +##sequence-region P36074 1 111 +P36074 UniProtKB Chain 1 111 . . . ID=PRO_0000203157;Note=Putative uncharacterized protein YKL111C +##sequence-region P36050 1 127 +P36050 UniProtKB Chain 1 127 . . . ID=PRO_0000203141;Note=Putative uncharacterized protein YKL169C +##sequence-region P34238 1 112 +P34238 UniProtKB Chain 1 112 . . . ID=PRO_0000203138;Note=Putative uncharacterized protein YKL177W +##sequence-region P34231 1 750 +P34231 UniProtKB Chain 1 750 . . . ID=PRO_0000203136;Note=Uncharacterized protein YKL187C +P34231 UniProtKB Modified residue 675 675 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P34231 UniProtKB Modified residue 678 678 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:19779198;Dbxref=PMID:17761666,PMID:19779198 +P34231 UniProtKB Glycosylation 61 61 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 84 84 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 115 115 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 154 154 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 176 176 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 197 197 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 207 207 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 228 228 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 241 241 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 267 267 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 293 293 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 299 299 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 312 312 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 335 335 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 351 351 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 373 373 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 389 389 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 519 519 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 709 709 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 714 714 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Glycosylation 724 724 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34231 UniProtKB Cross-link 697 697 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region Q07978 1 186 +Q07978 UniProtKB Chain 1 186 . . . ID=PRO_0000247174;Note=Putative uncharacterized protein YLR031W +##sequence-region Q07986 1 203 +Q07986 UniProtKB Chain 1 203 . . . ID=PRO_0000203232;Note=Uncharacterized protein YLR036C +Q07986 UniProtKB Transmembrane 60 80 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07986 UniProtKB Transmembrane 114 134 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07986 UniProtKB Transmembrane 157 177 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07986 UniProtKB Nucleotide binding 192 199 . . . Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07988 1 224 +Q07988 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07988 UniProtKB Chain 26 203 . . . ID=PRO_0000247442;Note=Cell wall protein YLR040C +Q07988 UniProtKB Propeptide 204 224 . . . ID=PRO_0000247443;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07988 UniProtKB Lipidation 203 203 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07988 UniProtKB Glycosylation 148 148 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07988 UniProtKB Glycosylation 181 181 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07988 UniProtKB Glycosylation 191 191 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGR1 1 33 +Q8TGR1 UniProtKB Chain 1 33 . . . ID=PRO_0000299613;Note=Putative uncharacterized protein YLR120W-A +##sequence-region Q12088 1 1755 +Q12088 UniProtKB Chain 1 1755 . . . ID=PRO_0000279094;Note=Transposon Ty1-LR1 Gag-Pol polyprotein +Q12088 UniProtKB Chain 1 401 . . . ID=PRO_0000279095;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12088 UniProtKB Chain 402 582 . . . ID=PRO_0000279096;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12088 UniProtKB Chain 583 1217 . . . ID=PRO_0000279097;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12088 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279098;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12088 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12088 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +Q12088 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +Q12088 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12088 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q12088 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12088 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q12088 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q12088 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12088 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12088 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12088 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12088 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12088 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12088 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12088 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12088 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12088 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12088 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q04501 1 128 +Q04501 UniProtKB Chain 1 128 . . . ID=PRO_0000203245;Note=Putative uncharacterized protein YML090W +Q04501 UniProtKB Transmembrane 1 21 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04501 UniProtKB Transmembrane 51 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04501 UniProtKB Transmembrane 76 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03675 1 126 +Q03675 UniProtKB Chain 1 126 . . . ID=PRO_0000203269;Note=Uncharacterized protein YMR007W +##sequence-region Q03687 1 405 +Q03687 UniProtKB Chain 1 405 . . . ID=PRO_0000203270;Note=Uncharacterized membrane protein YMR010W +Q03687 UniProtKB Topological domain 1 51 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03687 UniProtKB Transmembrane 52 72 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03687 UniProtKB Topological domain 73 76 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03687 UniProtKB Transmembrane 77 97 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03687 UniProtKB Topological domain 98 103 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03687 UniProtKB Transmembrane 104 124 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03687 UniProtKB Topological domain 125 178 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03687 UniProtKB Transmembrane 179 199 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03687 UniProtKB Topological domain 200 223 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03687 UniProtKB Transmembrane 224 244 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03687 UniProtKB Topological domain 245 254 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03687 UniProtKB Transmembrane 255 275 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03687 UniProtKB Topological domain 276 299 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03687 UniProtKB Transmembrane 300 320 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03687 UniProtKB Topological domain 321 405 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q05131 1 434 +Q05131 UniProtKB Chain 1 434 . . . ID=PRO_0000203274;Note=Uncharacterized membrane protein YMR034C +Q05131 UniProtKB Topological domain 1 15 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Transmembrane 16 36 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Topological domain 37 50 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Transmembrane 51 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Topological domain 72 87 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Transmembrane 88 108 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Topological domain 109 118 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Transmembrane 119 139 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Topological domain 140 149 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Transmembrane 150 170 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Topological domain 171 199 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Transmembrane 200 220 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Topological domain 221 234 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Transmembrane 235 255 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Topological domain 256 264 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Transmembrane 265 285 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Topological domain 286 327 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Transmembrane 328 348 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Topological domain 349 362 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Transmembrane 363 383 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Topological domain 384 434 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05131 UniProtKB Modified residue 425 425 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q04276 1 118 +Q04276 UniProtKB Chain 1 118 . . . ID=PRO_0000203283;Note=Uncharacterized protein YMR082C +##sequence-region Q04299 1 284 +Q04299 UniProtKB Chain 1 284 . . . ID=PRO_0000203285;Note=Probable ADP-ribose 1''-phosphate phosphatase YML087W +Q04299 UniProtKB Domain 34 230 . . . Note=Macro;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00490 +Q04299 UniProtKB Active site 80 80 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04299 UniProtKB Active site 90 90 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04299 UniProtKB Active site 145 145 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04299 UniProtKB Binding site 23 23 . . . Note=Substrate +Q04299 UniProtKB Binding site 55 55 . . . Note=Substrate +Q04299 UniProtKB Binding site 80 80 . . . Note=Substrate +Q04299 UniProtKB Binding site 90 90 . . . Note=Substrate +Q04299 UniProtKB Binding site 148 148 . . . Note=Substrate +Q04299 UniProtKB Binding site 195 195 . . . Note=Substrate +Q04299 UniProtKB Disulfide bond 128 136 . . . . +Q04299 UniProtKB Beta strand 18 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Helix 26 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Beta strand 47 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Helix 54 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Beta strand 73 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Helix 89 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Helix 100 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Turn 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Beta strand 121 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Helix 125 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Beta strand 140 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Beta strand 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Helix 162 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Helix 167 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Beta strand 186 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Beta strand 193 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXZ +Q04299 UniProtKB Helix 202 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Helix 219 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Helix 224 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Helix 240 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Helix 245 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Helix 258 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Turn 266 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +Q04299 UniProtKB Helix 271 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NJR +##sequence-region Q03177 1 834 +Q03177 UniProtKB Chain 1 834 . . . ID=PRO_0000051481;Note=WD repeat-containing protein YMR102C +Q03177 UniProtKB Repeat 171 210 . . . Note=WD 1 +Q03177 UniProtKB Repeat 276 314 . . . Note=WD 2 +Q03177 UniProtKB Repeat 316 356 . . . Note=WD 3 +Q03177 UniProtKB Repeat 358 398 . . . Note=WD 4 +Q03177 UniProtKB Repeat 423 468 . . . Note=WD 5 +Q03177 UniProtKB Modified residue 528 528 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q03177 UniProtKB Modified residue 771 771 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P53846 1 198 +P53846 UniProtKB Chain 1 198 . . . ID=PRO_0000203382;Note=Uncharacterized ORAOV1 family protein YNL260C +##sequence-region P53842 1 139 +P53842 UniProtKB Chain 1 139 . . . ID=PRO_0000203380;Note=Putative uncharacterized protein YNL266W +P53842 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53842 UniProtKB Transmembrane 57 77 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53842 UniProtKB Compositional bias 25 33 . . . Note=Poly-Ser +##sequence-region Q3E7A8 1 72 +Q3E7A8 UniProtKB Chain 1 72 . . . ID=PRO_0000247798;Note=Uncharacterized protein YNL162W-A +##sequence-region P53825 1 131 +P53825 UniProtKB Chain 1 131 . . . ID=PRO_0000203363;Note=Putative uncharacterized protein YNL324W +P53825 UniProtKB Transmembrane 61 81 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53825 UniProtKB Transmembrane 102 122 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53964 1 284 +P53964 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53964 UniProtKB Chain 25 284 . . . ID=PRO_0000014340;Note=Uncharacterized membrane protein YNL033W +P53964 UniProtKB Topological domain 25 84 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53964 UniProtKB Transmembrane 85 104 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53964 UniProtKB Topological domain 105 284 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53964 UniProtKB Glycosylation 270 270 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08216 1 224 +Q08216 UniProtKB Chain 1 224 . . . ID=PRO_0000299690;Note=Putative uncharacterized protein YOL046C +##sequence-region Q08448 1 450 +Q08448 UniProtKB Chain 1 450 . . . ID=PRO_0000237649;Note=Putative lipase YOR059C +Q08448 UniProtKB Transmembrane 269 289 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08448 UniProtKB Active site 90 90 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10037 +##sequence-region Q08238 1 132 +Q08238 UniProtKB Chain 1 132 . . . ID=PRO_0000262742;Note=Putative uncharacterized membrane protein YOL079W +Q08238 UniProtKB Topological domain 1 18 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12524434,ECO:0000305|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258 +Q08238 UniProtKB Transmembrane 19 39 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08238 UniProtKB Topological domain 40 49 . . . Note=Extracellular;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12524434,ECO:0000305|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258 +Q08238 UniProtKB Transmembrane 50 70 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08238 UniProtKB Topological domain 71 77 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12524434,ECO:0000305|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258 +Q08238 UniProtKB Transmembrane 78 98 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08238 UniProtKB Topological domain 99 132 . . . Note=Extracellular;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12524434,ECO:0000269|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258 +##sequence-region Q99247 1 1116 +Q99247 UniProtKB Chain 1 1116 . . . ID=PRO_0000235919;Note=Uncharacterized WD repeat-containing protein YOL087C +Q99247 UniProtKB Repeat 21 62 . . . Note=WD 1 +Q99247 UniProtKB Repeat 91 132 . . . Note=WD 2 +Q99247 UniProtKB Repeat 160 200 . . . Note=WD 3 +Q99247 UniProtKB Repeat 219 262 . . . Note=WD 4 +Q99247 UniProtKB Repeat 266 305 . . . Note=WD 5 +Q99247 UniProtKB Repeat 387 426 . . . Note=WD 6 +Q99247 UniProtKB Repeat 428 466 . . . Note=WD 7 +Q99247 UniProtKB Compositional bias 364 374 . . . Note=Poly-His +Q99247 UniProtKB Modified residue 668 668 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q99247 UniProtKB Modified residue 693 693 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q12496 1 1037 +Q12496 UniProtKB Chain 1 1037 . . . ID=PRO_0000178013;Note=Uncharacterized protein YOL098C +##sequence-region Q92393 1 1755 +Q92393 UniProtKB Chain 1 1755 . . . ID=PRO_0000279161;Note=Transposon Ty1-OR Gag-Pol polyprotein +Q92393 UniProtKB Chain 1 401 . . . ID=PRO_0000279162;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q92393 UniProtKB Chain 402 582 . . . ID=PRO_0000279163;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q92393 UniProtKB Chain 583 1217 . . . ID=PRO_0000279164;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q92393 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279165;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q92393 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q92393 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +Q92393 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +Q92393 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q92393 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q92393 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q92393 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q92393 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q92393 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q92393 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q92393 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q92393 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q92393 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q92393 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q92393 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q92393 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q92393 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q92393 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q92393 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q92393 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region Q3E7A5 1 60 +Q3E7A5 UniProtKB Chain 1 60 . . . ID=PRO_0000245278;Note=Uncharacterized protein YOL164W-A +##sequence-region Q08634 1 303 +Q08634 UniProtKB Chain 1 303 . . . ID=PRO_0000237669;Note=Uncharacterized protein YOR238W +##sequence-region O14468 1 76 +O14468 UniProtKB Chain 1 76 . . . ID=PRO_0000245285;Note=Uncharacterized protein YOR304C-A +##sequence-region P0C5R1 1 69 +P0C5R1 UniProtKB Chain 1 69 . . . ID=PRO_0000309059;Note=Putative uncharacterized protein YOR329W-A +P0C5R1 UniProtKB Transmembrane 39 61 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12182 1 319 +Q12182 UniProtKB Chain 1 319 . . . ID=PRO_0000245289;Note=Uncharacterized protein YOR342C +##sequence-region Q08844 1 703 +Q08844 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Chain 25 703 . . . ID=PRO_0000252268;Note=Uncharacterized membrane protein YOR365C +Q08844 UniProtKB Topological domain 25 203 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Transmembrane 204 224 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Topological domain 225 238 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Transmembrane 239 259 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Topological domain 260 374 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Transmembrane 375 395 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Topological domain 396 415 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Transmembrane 416 438 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Topological domain 439 452 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Transmembrane 453 473 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Topological domain 474 516 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Transmembrane 517 537 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Topological domain 538 545 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Transmembrane 546 566 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Topological domain 567 571 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Transmembrane 572 592 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Topological domain 593 605 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Transmembrane 606 626 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Topological domain 627 703 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Glycosylation 28 28 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Glycosylation 43 43 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Glycosylation 87 87 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08844 UniProtKB Glycosylation 103 103 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0C5R4 1 46 +P0C5R4 UniProtKB Chain 1 46 . . . ID=PRO_0000309062;Note=Uncharacterized protein YOL083C-A +##sequence-region P53049 1 1477 +P53049 UniProtKB Chain 1 1477 . . . ID=PRO_0000093450;Note=Oligomycin resistance ATP-dependent permease YOR1 +P53049 UniProtKB Topological domain 1 206 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53049 UniProtKB Transmembrane 207 227 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P53049 UniProtKB Topological domain 228 249 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53049 UniProtKB Transmembrane 250 270 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P53049 UniProtKB Topological domain 271 328 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53049 UniProtKB Transmembrane 329 349 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P53049 UniProtKB Topological domain 350 357 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53049 UniProtKB Transmembrane 358 370 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P53049 UniProtKB Topological domain 371 433 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53049 UniProtKB Transmembrane 434 454 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P53049 UniProtKB Topological domain 455 478 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53049 UniProtKB Transmembrane 479 499 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P53049 UniProtKB Topological domain 500 615 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53049 UniProtKB Transmembrane 616 636 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P53049 UniProtKB Topological domain 637 892 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53049 UniProtKB Transmembrane 893 913 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P53049 UniProtKB Topological domain 914 940 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53049 UniProtKB Transmembrane 941 961 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P53049 UniProtKB Topological domain 962 1027 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53049 UniProtKB Transmembrane 1028 1048 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P53049 UniProtKB Topological domain 1049 1117 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53049 UniProtKB Transmembrane 1118 1138 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P53049 UniProtKB Topological domain 1139 1141 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53049 UniProtKB Transmembrane 1142 1162 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P53049 UniProtKB Topological domain 1163 1477 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53049 UniProtKB Domain 207 493 . . . Note=ABC transmembrane type-1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P53049 UniProtKB Domain 581 808 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P53049 UniProtKB Domain 897 1175 . . . Note=ABC transmembrane type-1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P53049 UniProtKB Domain 1213 1464 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P53049 UniProtKB Nucleotide binding 621 628 . . . Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P53049 UniProtKB Nucleotide binding 1247 1254 . . . Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P53049 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P53049 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P53049 UniProtKB Modified residue 53 53 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P53049 UniProtKB Glycosylation 661 661 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53049 UniProtKB Glycosylation 759 759 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53049 UniProtKB Glycosylation 799 799 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12486 1 218 +Q12486 UniProtKB Chain 1 218 . . . ID=PRO_0000237658;Note=Putative uncharacterized hydrolase YOR131C +##sequence-region Q12251 1 326 +Q12251 UniProtKB Chain 1 326 . . . ID=PRO_0000243949;Note=Uncharacterized mitochondrial carrier YPR011C +Q12251 UniProtKB Transmembrane 24 40 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12251 UniProtKB Transmembrane 84 104 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12251 UniProtKB Transmembrane 126 143 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12251 UniProtKB Transmembrane 195 213 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12251 UniProtKB Transmembrane 237 254 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12251 UniProtKB Transmembrane 297 316 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12251 UniProtKB Repeat 20 107 . . . Note=Solcar 1 +Q12251 UniProtKB Repeat 120 219 . . . Note=Solcar 2 +Q12251 UniProtKB Repeat 231 322 . . . Note=Solcar 3 +##sequence-region Q12079 1 277 +Q12079 UniProtKB Chain 1 277 . . . ID=PRO_0000252275;Note=Uncharacterized membrane protein YPR027C +Q12079 UniProtKB Transmembrane 1 21 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12079 UniProtKB Topological domain 22 84 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12079 UniProtKB Transmembrane 85 105 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12079 UniProtKB Topological domain 106 277 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12079 UniProtKB Glycosylation 155 155 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12079 UniProtKB Glycosylation 265 265 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q6Q5F3 1 151 +Q6Q5F3 UniProtKB Chain 1 151 . . . ID=PRO_0000299818;Note=Uncharacterized protein YPR053C +##sequence-region Q12194 1 479 +Q12194 UniProtKB Chain 1 479 . . . ID=PRO_0000203492;Note=Uncharacterized protein YPL066W +##sequence-region Q02864 1 156 +Q02864 UniProtKB Chain 1 156 . . . ID=PRO_0000238643;Note=Uncharacterized protein YPL071C +Q02864 UniProtKB Modified residue 21 21 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region O13585 1 888 +O13585 UniProtKB Chain 1 888 . . . ID=PRO_0000257825;Note=Dilute domain-containing protein YPR089W +O13585 UniProtKB Domain 360 745 . . . Note=Dilute;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00503 +##sequence-region Q06089 1 161 +Q06089 UniProtKB Chain 1 161 . . . ID=PRO_0000252300;Note=Uncharacterized mitochondrial outer membrane protein YPR098C +Q06089 UniProtKB Transmembrane 10 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06089 UniProtKB Transmembrane 60 80 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06089 UniProtKB Transmembrane 131 151 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E751 1 87 +Q3E751 UniProtKB Chain 1 87 . . . ID=PRO_0000238648;Note=Uncharacterized protein YPL119C-A +Q3E751 UniProtKB Transmembrane 21 41 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region O13566 1 144 +O13566 UniProtKB Chain 1 144 . . . ID=PRO_0000299825;Note=Putative uncharacterized protein YPR123C +O13566 UniProtKB Transmembrane 27 47 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13566 UniProtKB Transmembrane 49 69 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13566 UniProtKB Transmembrane 83 103 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13566 UniProtKB Transmembrane 106 126 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region O13568 1 135 +O13568 UniProtKB Chain 1 135 . . . ID=PRO_0000299827;Note=Putative uncharacterized protein YPR130C +O13568 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0C2J0 1 1756 +P0C2J0 UniProtKB Chain 1 1756 . . . ID=PRO_0000279179;Note=Transposon Ty1-PR2 Gag-Pol polyprotein +P0C2J0 UniProtKB Chain 1 401 . . . ID=PRO_0000279180;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J0 UniProtKB Chain 402 582 . . . ID=PRO_0000279181;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J0 UniProtKB Chain 583 1218 . . . ID=PRO_0000279182;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J0 UniProtKB Chain 1219 1756 . . . ID=PRO_0000279183;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J0 UniProtKB Domain 660 836 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J0 UniProtKB Domain 1339 1477 . . . Note=Reverse transcriptase Ty1/copia-type +P0C2J0 UniProtKB Domain 1611 1753 . . . Note=RNase H Ty1/copia-type +P0C2J0 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J0 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +P0C2J0 UniProtKB Motif 1179 1213 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J0 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0C2J0 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +P0C2J0 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J0 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J0 UniProtKB Metal binding 1347 1347 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J0 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J0 UniProtKB Metal binding 1429 1429 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J0 UniProtKB Metal binding 1611 1611 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J0 UniProtKB Metal binding 1653 1653 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J0 UniProtKB Metal binding 1686 1686 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J0 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J0 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J0 UniProtKB Site 1218 1219 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q06537 1 140 +Q06537 UniProtKB Chain 1 140 . . . ID=PRO_0000244638;Note=Uncharacterized protein YPR153W +Q06537 UniProtKB Transmembrane 45 65 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06537 UniProtKB Transmembrane 76 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06537 UniProtKB Transmembrane 116 136 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06537 UniProtKB Glycosylation 27 27 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region O13575 1 123 +O13575 UniProtKB Chain 1 123 . . . ID=PRO_0000299833;Note=Putative uncharacterized protein YPR177C +O13575 UniProtKB Compositional bias 11 20 . . . Note=Poly-Ser +##sequence-region P0C5R9 1 85 +P0C5R9 UniProtKB Chain 1 85 . . . ID=PRO_0000309067;Note=Uncharacterized protein YPR170W-B +P0C5R9 UniProtKB Transmembrane 11 31 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C5R9 UniProtKB Transmembrane 55 75 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P18961 1 677 +P18961 UniProtKB Chain 1 677 . . . ID=PRO_0000086836;Note=Serine/threonine-protein kinase YPK2/YKR2 +P18961 UniProtKB Domain 344 599 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P18961 UniProtKB Domain 600 670 . . . Note=AGC-kinase C-terminal +P18961 UniProtKB Nucleotide binding 350 358 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P18961 UniProtKB Compositional bias 35 57 . . . Note=His-rich +P18961 UniProtKB Active site 467 467 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P18961 UniProtKB Binding site 373 373 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P18961 UniProtKB Modified residue 63 63 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P18961 UniProtKB Modified residue 66 66 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12688 +P18961 UniProtKB Modified residue 72 72 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P18961 UniProtKB Modified residue 499 499 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P18961 UniProtKB Modified residue 501 501 . . . Note=Phosphothreonine%3B by PKH2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16055732;Dbxref=PMID:16055732 +P18961 UniProtKB Modified residue 641 641 . . . Note=Phosphoserine%3B by TOR2;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000269|PubMed:16055732;Dbxref=PMID:17330950,PMID:16055732 +P18961 UniProtKB Modified residue 650 650 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P18961 UniProtKB Modified residue 659 659 . . . Note=Phosphothreonine%3B by TOR2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16055732;Dbxref=PMID:16055732 +P18961 UniProtKB Modified residue 669 669 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P18961 UniProtKB Mutagenesis 239 239 . . . Note=Rescues growth of cells compromised in TORC2%2C but not TORC1 function. Restores SLT2 activation and suppresses actin cytoskeleton organization defect in TOR2 mutant cells. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16055732;Dbxref=PMID:16055732 +P18961 UniProtKB Mutagenesis 373 373 . . . Note=No kinase activity. K->R%2CA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12221112,ECO:0000269|PubMed:15840588;Dbxref=PMID:12221112,PMID:15840588 +P18961 UniProtKB Mutagenesis 641 641 . . . Note=Reduced kinase activity%3B when associated with A-659. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16055732;Dbxref=PMID:16055732 +P18961 UniProtKB Mutagenesis 659 659 . . . Note=Reduced kinase activity%3B when associated with A-641. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16055732;Dbxref=PMID:16055732 +##sequence-region P32939 1 208 +P32939 UniProtKB Chain 1 208 . . . ID=PRO_0000121320;Note=GTP-binding protein YPT7 +P32939 UniProtKB Nucleotide binding 15 22 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32939 UniProtKB Nucleotide binding 64 68 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32939 UniProtKB Nucleotide binding 126 129 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32939 UniProtKB Motif 37 45 . . . Note=Effector region;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32939 UniProtKB Modified residue 208 208 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32939 UniProtKB Lipidation 206 206 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32939 UniProtKB Lipidation 208 208 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32939 UniProtKB Cross-link 147 147 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32939 UniProtKB Beta strand 8 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3 +P32939 UniProtKB Helix 21 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3 +P32939 UniProtKB Beta strand 46 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3 +P32939 UniProtKB Beta strand 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3 +P32939 UniProtKB Beta strand 58 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3 +P32939 UniProtKB Helix 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY2 +P32939 UniProtKB Turn 73 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY2 +P32939 UniProtKB Helix 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY2 +P32939 UniProtKB Beta strand 84 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3 +P32939 UniProtKB Helix 94 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3 +P32939 UniProtKB Helix 100 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3 +P32939 UniProtKB Turn 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3 +P32939 UniProtKB Beta strand 121 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3 +P32939 UniProtKB Helix 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3 +P32939 UniProtKB Helix 139 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3 +P32939 UniProtKB Beta strand 154 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3 +P32939 UniProtKB Turn 159 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3 +P32939 UniProtKB Helix 165 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KY3 +##sequence-region P36036 1 203 +P36036 UniProtKB Chain 1 203 . . . ID=PRO_0000082033;Note=RNA annealing protein YRA2 +P36036 UniProtKB Domain 64 138 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P36036 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P38079 1 344 +P38079 UniProtKB Chain 1 344 . . . ID=PRO_0000196286;Note=Protein YRO2 +P38079 UniProtKB Topological domain 1 34 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38079 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38079 UniProtKB Topological domain 56 62 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38079 UniProtKB Transmembrane 63 83 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38079 UniProtKB Topological domain 84 119 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38079 UniProtKB Transmembrane 120 140 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38079 UniProtKB Topological domain 141 141 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38079 UniProtKB Transmembrane 142 162 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38079 UniProtKB Topological domain 163 172 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38079 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38079 UniProtKB Topological domain 194 202 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38079 UniProtKB Transmembrane 203 223 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38079 UniProtKB Topological domain 224 238 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38079 UniProtKB Transmembrane 239 259 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38079 UniProtKB Topological domain 260 344 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38079 UniProtKB Compositional bias 304 331 . . . Note=Lys-rich +P38079 UniProtKB Compositional bias 334 344 . . . Note=Glu-rich +P38079 UniProtKB Modified residue 293 293 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38079 UniProtKB Modified residue 341 341 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17761666,PMID:18407956,PMID:19779198 +P38079 UniProtKB Modified residue 343 343 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956;Dbxref=PMID:17761666,PMID:18407956 +P38079 UniProtKB Cross-link 286 286 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region P39703 1 215 +P39703 UniProtKB Chain 1 215 . . . ID=PRO_0000202411;Note=Putative uncharacterized protein YAL004W +P39703 UniProtKB Sequence conflict 17 17 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38215 1 129 +P38215 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38215 UniProtKB Chain 21 129 . . . ID=PRO_0000014310;Note=Putative uncharacterized protein YBR013C +##sequence-region P38223 1 100 +P38223 UniProtKB Chain 1 100 . . . ID=PRO_0000202473;Note=Uncharacterized protein YBR032W +##sequence-region P38277 1 524 +P38277 UniProtKB Chain 1 524 . . . ID=PRO_0000202493;Note=Uncharacterized protein YBR138C +P38277 UniProtKB Sequence conflict 122 122 . . . Note=L->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38277 UniProtKB Sequence conflict 122 122 . . . Note=L->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q96VH3 1 125 +Q96VH3 UniProtKB Chain 1 125 . . . ID=PRO_0000248447;Note=Putative uncharacterized protein YCL021W-A +Q96VH3 UniProtKB Transmembrane 100 120 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q2V2Q2 1 79 +Q2V2Q2 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q2V2Q2 UniProtKB Chain 19 55 . . . ID=PRO_0000248449;Note=Uncharacterized protein YCL048W-A +Q2V2Q2 UniProtKB Propeptide 56 79 . . . ID=PRO_0000253885;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q2V2Q2 UniProtKB Lipidation 55 55 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q2V2Q2 UniProtKB Glycosylation 25 25 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q2V2Q2 UniProtKB Glycosylation 30 30 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q2V2Q2 UniProtKB Glycosylation 35 35 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q2V2Q2 UniProtKB Glycosylation 40 40 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39109 1 1515 +P39109 UniProtKB Chain 1 1515 . . . ID=PRO_0000093449;Note=Metal resistance protein YCF1 +P39109 UniProtKB Topological domain 1 32 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39109 UniProtKB Transmembrane 33 53 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Topological domain 54 73 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39109 UniProtKB Transmembrane 74 94 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Topological domain 95 99 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39109 UniProtKB Transmembrane 100 120 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Topological domain 121 130 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39109 UniProtKB Transmembrane 131 151 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Topological domain 152 169 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39109 UniProtKB Transmembrane 170 190 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Topological domain 191 278 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39109 UniProtKB Transmembrane 279 299 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Topological domain 300 345 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39109 UniProtKB Transmembrane 346 366 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Topological domain 367 422 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39109 UniProtKB Transmembrane 423 443 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Topological domain 444 446 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39109 UniProtKB Transmembrane 447 467 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Topological domain 468 530 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39109 UniProtKB Transmembrane 531 551 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Topological domain 552 572 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39109 UniProtKB Transmembrane 573 593 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Topological domain 594 943 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39109 UniProtKB Transmembrane 944 964 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Topological domain 965 1001 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39109 UniProtKB Transmembrane 1002 1023 . . . Note=Helical%3B Name%3D13;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Topological domain 1024 1066 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39109 UniProtKB Transmembrane 1067 1087 . . . Note=Helical%3B Name%3D14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Topological domain 1088 1088 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39109 UniProtKB Transmembrane 1089 1109 . . . Note=Helical%3B Name%3D15;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Topological domain 1110 1180 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39109 UniProtKB Transmembrane 1181 1201 . . . Note=Helical%3B Name%3D16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Topological domain 1202 1205 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39109 UniProtKB Transmembrane 1206 1226 . . . Note=Helical%3B Name%3D17;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Topological domain 1227 1515 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39109 UniProtKB Domain 287 590 . . . Note=ABC transmembrane type-1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Domain 626 853 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P39109 UniProtKB Domain 951 1235 . . . Note=ABC transmembrane type-1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P39109 UniProtKB Domain 1272 1507 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P39109 UniProtKB Nucleotide binding 663 670 . . . Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P39109 UniProtKB Nucleotide binding 1306 1313 . . . Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P39109 UniProtKB Modified residue 251 251 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39109 UniProtKB Modified residue 873 873 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39109 UniProtKB Modified residue 903 903 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +P39109 UniProtKB Modified residue 908 908 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P39109 UniProtKB Modified residue 911 911 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P39109 UniProtKB Modified residue 914 914 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39109 UniProtKB Mutagenesis 713 713 . . . Note=Loss of function. Missing +P39109 UniProtKB Mutagenesis 908 908 . . . Note=Loss of function. S->A +P39109 UniProtKB Sequence conflict 680 680 . . . Note=L->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P37264 1 122 +P37264 UniProtKB Chain 1 122 . . . ID=PRO_0000202555;Note=Putative uncharacterized protein YCL065W +P37264 UniProtKB Transmembrane 21 40 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37264 UniProtKB Transmembrane 57 77 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37264 UniProtKB Transmembrane 94 114 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12316 1 1755 +Q12316 UniProtKB Chain 1 1755 . . . ID=PRO_0000279069;Note=Transposon Ty1-GR3 Gag-Pol polyprotein +Q12316 UniProtKB Chain 1 401 . . . ID=PRO_0000279070;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12316 UniProtKB Chain 402 582 . . . ID=PRO_0000279071;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12316 UniProtKB Chain 583 1217 . . . ID=PRO_0000279072;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12316 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279073;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12316 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12316 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +Q12316 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +Q12316 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12316 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q12316 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12316 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q12316 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q12316 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12316 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12316 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12316 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12316 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12316 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12316 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12316 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12316 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12316 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12316 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12316 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region P53227 1 271 +P53227 UniProtKB Chain 1 271 . . . ID=PRO_0000202794;Note=Uncharacterized protein YGR042W +##sequence-region Q8TGT7 1 37 +Q8TGT7 UniProtKB Chain 1 37 . . . ID=PRO_0000245388;Note=Uncharacterized protein YGR204C-A +##sequence-region P53234 1 283 +P53234 UniProtKB Chain 1 283 . . . ID=PRO_0000202799;Note=Uncharacterized protein YGR053C +##sequence-region P0CX64 1 1770 +P0CX64 UniProtKB Chain 1 1770 . . . ID=PRO_0000409809;Note=Transposon Ty2-GR2 Gag-Pol polyprotein +P0CX64 UniProtKB Chain 1 397 . . . ID=PRO_0000409810;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX64 UniProtKB Chain 398 578 . . . ID=PRO_0000409811;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX64 UniProtKB Chain 579 1232 . . . ID=PRO_0000409812;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX64 UniProtKB Chain 1233 1770 . . . ID=PRO_0000409813;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX64 UniProtKB Domain 656 831 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0CX64 UniProtKB Domain 1353 1491 . . . Note=Reverse transcriptase Ty1/copia-type +P0CX64 UniProtKB Domain 1625 1767 . . . Note=RNase H Ty1/copia-type +P0CX64 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX64 UniProtKB Region 579 636 . . . Note=Integrase-type zinc finger-like +P0CX64 UniProtKB Motif 1193 1227 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX64 UniProtKB Active site 457 457 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX64 UniProtKB Metal binding 667 667 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0CX64 UniProtKB Metal binding 732 732 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0CX64 UniProtKB Metal binding 1361 1361 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0CX64 UniProtKB Metal binding 1442 1442 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0CX64 UniProtKB Metal binding 1443 1443 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0CX64 UniProtKB Metal binding 1625 1625 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0CX64 UniProtKB Metal binding 1667 1667 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0CX64 UniProtKB Metal binding 1700 1700 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0CX64 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX64 UniProtKB Site 578 579 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX64 UniProtKB Site 1232 1233 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P48238 1 217 +P48238 UniProtKB Chain 1 217 . . . ID=PRO_0000202832;Note=Uncharacterized protein YGR153W +P48238 UniProtKB Sequence conflict 158 158 . . . Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P48238 UniProtKB Sequence conflict 158 158 . . . Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q3E750 1 60 +Q3E750 UniProtKB Chain 1 60 . . . ID=PRO_0000245379;Note=Uncharacterized protein YGL041C-B +Q3E750 UniProtKB Transmembrane 19 39 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53302 1 121 +P53302 UniProtKB Chain 1 121 . . . ID=PRO_0000202841;Note=Putative uncharacterized protein YGR190C +##sequence-region P50083 1 69 +P50083 UniProtKB Chain 1 69 . . . ID=PRO_0000202849;Note=Putative uncharacterized protein YGR226C +P50083 UniProtKB Transmembrane 13 35 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53326 1 701 +P53326 UniProtKB Chain 1 701 . . . ID=PRO_0000202864;Note=Uncharacterized protein YGR266W +##sequence-region P53162 1 154 +P53162 UniProtKB Chain 1 154 . . . ID=PRO_0000202763;Note=Putative uncharacterized protein YGL069C +##sequence-region P53161 1 119 +P53161 UniProtKB Chain 1 119 . . . ID=PRO_0000202762;Note=Putative uncharacterized protein YGL072C +P53161 UniProtKB Transmembrane 30 50 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12222 1 375 +Q12222 UniProtKB Chain 1 375 . . . ID=PRO_0000086159;Note=Glycogen synthase kinase-3 homolog YGK3 +Q12222 UniProtKB Domain 41 329 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12222 UniProtKB Nucleotide binding 47 55 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12222 UniProtKB Active site 173 173 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q12222 UniProtKB Binding site 74 74 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12222 UniProtKB Modified residue 211 211 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region P53113 1 225 +P53113 UniProtKB Chain 1 225 . . . ID=PRO_0000202733;Note=Putative uncharacterized protein YGL152C +P53113 UniProtKB Transmembrane 40 60 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53113 UniProtKB Transmembrane 63 83 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53113 UniProtKB Transmembrane 151 171 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53113 UniProtKB Transmembrane 176 196 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53106 1 192 +P53106 UniProtKB Chain 1 192 . . . ID=PRO_0000202729;Note=Putative uncharacterized protein YGL165C +P53106 UniProtKB Transmembrane 81 101 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P46945 1 554 +P46945 UniProtKB Chain 1 554 . . . ID=PRO_0000202727;Note=Uncharacterized protein YGL176C +##sequence-region P53098 1 57 +P53098 UniProtKB Chain 1 57 . . . ID=PRO_0000202724;Note=Putative uncharacterized protein YGL188C +##sequence-region P53087 1 161 +P53087 UniProtKB Chain 1 161 . . . ID=PRO_0000202718;Note=Putative uncharacterized protein YGL214W +P53087 UniProtKB Transmembrane 76 94 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53069 1 104 +P53069 UniProtKB Chain 1 104 . . . ID=PRO_0000202709;Note=Putative uncharacterized protein YGL239C +P53069 UniProtKB Transmembrane 80 98 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53056 1 76 +P53056 UniProtKB Chain 1 76 . . . ID=PRO_0000202703;Note=Putative UPF0377 protein YGL260W +##sequence-region Q8TGT6 1 29 +Q8TGT6 UniProtKB Chain 1 29 . . . ID=PRO_0000245394;Note=Uncharacterized protein YHR022C-A +##sequence-region A0A023PZH9 1 153 +A0A023PZH9 UniProtKB Chain 1 153 . . . ID=PRO_0000431019;Note=Putative uncharacterized protein YHL034W-A +A0A023PZH9 UniProtKB Compositional bias 5 56 . . . Note=Ser-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00016 +##sequence-region Q3E746 1 53 +Q3E746 UniProtKB Chain 1 53 . . . ID=PRO_0000245395;Note=Uncharacterized protein YHR086W-A +##sequence-region P38893 1 341 +P38893 UniProtKB Chain 1 341 . . . ID=PRO_0000197448;Note=Uncharacterized isomerase YHR210C +P38893 UniProtKB Active site 175 175 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10126 +P38893 UniProtKB Active site 306 306 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38893 UniProtKB Binding site 70 70 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38893 UniProtKB Binding site 239 239 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q8TGN6 1 216 +Q8TGN6 UniProtKB Chain 1 216 . . . ID=PRO_0000299928;Note=Putative uncharacterized protein YHR137C-A +##sequence-region P38898 1 153 +P38898 UniProtKB Chain 1 153 . . . ID=PRO_0000202946;Note=Putative uncharacterized protein YHR217C +##sequence-region P38900 1 624 +P38900 UniProtKB Chain 1 624 . . . ID=PRO_0000202948;Note=Putative uncharacterized protein YHR219W +##sequence-region A0A023PXF5 1 105 +A0A023PXF5 UniProtKB Chain 1 105 . . . ID=PRO_0000430969;Note=Putative uncharacterized helicase-like protein YHR218W-A +A0A023PXF5 UniProtKB Domain 2 42 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +##sequence-region P38752 1 130 +P38752 UniProtKB Chain 1 130 . . . ID=PRO_0000202884;Note=Uncharacterized protein YHL005C +P38752 UniProtKB Transmembrane 15 31 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38733 1 133 +P38733 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38733 UniProtKB Chain 23 133 . . . ID=PRO_0000202880;Note=Uncharacterized protein YHL037C +P38733 UniProtKB Glycosylation 111 111 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PYH8 1 122 +A0A023PYH8 UniProtKB Chain 1 122 . . . ID=PRO_0000431034;Note=Putative uncharacterized protein YIL047C-A +##sequence-region Q8TGN4 1 89 +Q8TGN4 UniProtKB Chain 1 89 . . . ID=PRO_0000299758;Note=Putative uncharacterized protein YIL021C-A +##sequence-region A0A023PZK4 1 127 +A0A023PZK4 UniProtKB Chain 1 127 . . . ID=PRO_0000431041;Note=Putative uncharacterized protein YIR030W-A +##sequence-region Q99219 1 290 +Q99219 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12173 +Q99219 UniProtKB Chain 2 290 . . . ID=PRO_0000279376;Note=Transposon Ty3-I Gag polyprotein +Q99219 UniProtKB Chain 2 207 . . . ID=PRO_0000279377;Note=Capsid protein +Q99219 UniProtKB Peptide 208 233 . . . ID=PRO_0000279378;Note=Spacer peptide p3 +Q99219 UniProtKB Chain 234 290 . . . ID=PRO_0000279379;Note=Nucleocapsid protein p9 +Q99219 UniProtKB Zinc finger 265 282 . . . Note=CCHC-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +Q99219 UniProtKB Site 207 208 . . . Note=Cleavage%3B by Ty3 protease +Q99219 UniProtKB Site 233 234 . . . Note=Cleavage%3B by Ty3 protease +Q99219 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12173 +##sequence-region P53845 1 314 +P53845 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53845 UniProtKB Chain 2 314 . . . ID=PRO_0000203381;Note=Protein transport protein YIF1 +P53845 UniProtKB Topological domain 2 153 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53845 UniProtKB Transmembrane 154 174 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53845 UniProtKB Topological domain 175 188 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53845 UniProtKB Transmembrane 189 209 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53845 UniProtKB Topological domain 210 217 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53845 UniProtKB Transmembrane 218 238 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53845 UniProtKB Topological domain 239 243 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53845 UniProtKB Transmembrane 244 264 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53845 UniProtKB Topological domain 265 293 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53845 UniProtKB Transmembrane 294 313 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53845 UniProtKB Topological domain 314 314 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53845 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P40440 1 109 +P40440 UniProtKB Chain 1 109 . . . ID=PRO_0000050407;Note=Putative transporter-like protein YIL171W +P40440 UniProtKB Topological domain 1 56 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40440 UniProtKB Transmembrane 57 77 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40440 UniProtKB Topological domain 78 109 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40440 UniProtKB Glycosylation 87 87 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40570 1 242 +P40570 UniProtKB Chain 1 242 . . . ID=PRO_0000203004;Note=Putative uncharacterized protein YIR014W +P40570 UniProtKB Transmembrane 128 148 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40570 UniProtKB Transmembrane 152 172 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40575 1 100 +P40575 UniProtKB Chain 1 100 . . . ID=PRO_0000203006;Note=Uncharacterized protein YIR020C +##sequence-region P40579 1 254 +P40579 UniProtKB Chain 1 254 . . . ID=PRO_0000054870;Note=Uncharacterized oxidoreductase YIR035C +P40579 UniProtKB Nucleotide binding 6 30 . . . Note=NAD or NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40579 UniProtKB Active site 150 150 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001 +P40579 UniProtKB Binding site 137 137 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40579 UniProtKB Beta strand 4 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Helix 13 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Beta strand 30 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Helix 38 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Helix 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Beta strand 52 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Helix 62 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Beta strand 81 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Turn 93 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Helix 100 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Helix 112 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Beta strand 131 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Helix 148 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Helix 157 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Beta strand 171 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Turn 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Helix 200 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Helix 219 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Helix 235 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Beta strand 241 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +P40579 UniProtKB Helix 247 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KZV +##sequence-region P40584 1 110 +P40584 UniProtKB Chain 1 110 . . . ID=PRO_0000203008;Note=Putative UPF0377 protein YIR040C +##sequence-region P47101 1 745 +P47101 UniProtKB Chain 1 745 . . . ID=PRO_0000203090;Note=UPF0508 protein YJR030C +P47101 UniProtKB Compositional bias 680 736 . . . Note=Ser-rich +P47101 UniProtKB Natural variant 742 745 . . . Note=In strain: VP102-10A. LRNM->HVKTKADVWKPSRVGYTDIFSQEYKGIVVAIKFVICSDAEGTLYPREYNSRLHDIKRLGRTGLSFTDKKEAYLLEFKNQDVVDHVHKLILPFNTSWQSN +##sequence-region Q8TGJ8 1 73 +Q8TGJ8 UniProtKB Chain 1 73 . . . ID=PRO_0000299763;Note=Putative uncharacterized protein YJL026C-A +##sequence-region Q3E837 1 39 +Q3E837 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E837 UniProtKB Chain 22 39 . . . ID=PRO_0000245413;Note=Uncharacterized protein YJL052C-A +##sequence-region P0CT86 1 78 +P0CT86 UniProtKB Chain 1 78 . . . ID=PRO_0000435366;Note=Uncharacterized protein YJR107C-A +##sequence-region P47098 1 1755 +P47098 UniProtKB Chain 1 1755 . . . ID=PRO_0000199563;Note=Transposon Ty1-JR1 Gag-Pol polyprotein +P47098 UniProtKB Chain 1 401 . . . ID=PRO_0000279082;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47098 UniProtKB Chain 402 582 . . . ID=PRO_0000279083;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47098 UniProtKB Chain 583 1217 . . . ID=PRO_0000279084;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47098 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279085;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47098 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47098 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +P47098 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +P47098 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47098 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +P47098 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47098 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P47098 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +P47098 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47098 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47098 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47098 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47098 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47098 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47098 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47098 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47098 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47098 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47098 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47098 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region P47137 1 282 +P47137 UniProtKB Chain 1 282 . . . ID=PRO_0000124679;Note=Uncharacterized oxidoreductase YJR096W +P47137 UniProtKB Active site 50 50 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47137 UniProtKB Binding site 115 115 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47137 UniProtKB Site 81 81 . . . Note=Lowers pKa of active site Tyr;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q8TGT3 1 32 +Q8TGT3 UniProtKB Chain 1 32 . . . ID=PRO_0000245411;Note=Uncharacterized protein YJL077W-B +##sequence-region P47173 1 342 +P47173 UniProtKB Chain 1 342 . . . ID=PRO_0000203126;Note=Uncharacterized protein YJR142W +P47173 UniProtKB Domain 155 309 . . . Note=Nudix hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00794 +##sequence-region P47080 1 104 +P47080 UniProtKB Chain 1 104 . . . ID=PRO_0000203079;Note=Uncharacterized protein YJL007C +P47080 UniProtKB Transmembrane 72 92 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47073 1 94 +P47073 UniProtKB Chain 1 94 . . . ID=PRO_0000203076;Note=Putative uncharacterized protein YJL015C +##sequence-region P47072 1 561 +P47072 UniProtKB Chain 1 561 . . . ID=PRO_0000203075;Note=Uncharacterized protein YJL016W +P47072 UniProtKB Modified residue 514 514 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P47048 1 450 +P47048 UniProtKB Chain 1 450 . . . ID=PRO_0000203065;Note=Uncharacterized protein YJL049W +##sequence-region P47044 1 245 +P47044 UniProtKB Chain 1 245 . . . ID=PRO_0000203061;Note=LOG family protein YJL055W +##sequence-region P47004 1 100 +P47004 UniProtKB Chain 1 100 . . . ID=PRO_0000203030;Note=Putative uncharacterized protein YJL150W +##sequence-region P36127 1 104 +P36127 UniProtKB Chain 1 104 . . . ID=PRO_0000203206;Note=Uncharacterized protein YKR032W +##sequence-region P0C5P5 1 77 +P0C5P5 UniProtKB Chain 1 77 . . . ID=PRO_0000309043;Note=Putative uncharacterized YKL165C-A +P0C5P5 UniProtKB Transmembrane 36 52 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36158 1 585 +P36158 UniProtKB Chain 1 585 . . . ID=PRO_0000203224;Note=Uncharacterized protein YKR078W +##sequence-region P36103 1 277 +P36103 UniProtKB Chain 1 277 . . . ID=PRO_0000203189;Note=Uncharacterized protein YKL023W +P36103 UniProtKB Sequence conflict 25 26 . . . Note=QQ->HE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P35733 1 124 +P35733 UniProtKB Chain 1 124 . . . ID=PRO_0000203178;Note=Putative uncharacterized protein YKL053W +##sequence-region P36089 1 147 +P36089 UniProtKB Chain 1 147 . . . ID=PRO_0000203173;Note=Putative uncharacterized protein YKL066W +##sequence-region P36081 1 392 +P36081 UniProtKB Chain 1 392 . . . ID=PRO_0000203168;Note=Uncharacterized protein YKL077W +##sequence-region P34245 1 136 +P34245 UniProtKB Chain 1 136 . . . ID=PRO_0000203162;Note=Uncharacterized protein YKL097C +##sequence-region P36067 1 173 +P36067 UniProtKB Chain 1 173 . . . ID=PRO_0000203150;Note=Putative uncharacterized protein YKL131W +##sequence-region P36015 1 200 +P36015 UniProtKB Chain 1 197 . . . ID=PRO_0000206781;Note=Synaptobrevin homolog YKT6 +P36015 UniProtKB Propeptide 198 200 . . . ID=PRO_0000396675;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36015 UniProtKB Domain 7 129 . . . Note=Longin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00231 +P36015 UniProtKB Domain 140 200 . . . Note=v-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00290 +P36015 UniProtKB Modified residue 158 158 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P36015 UniProtKB Modified residue 197 197 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36015 UniProtKB Lipidation 196 196 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36015 UniProtKB Lipidation 197 197 . . . Note=S-farnesyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36015 UniProtKB Beta strand 3 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6 +P36015 UniProtKB Beta strand 13 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6 +P36015 UniProtKB Beta strand 17 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6 +P36015 UniProtKB Beta strand 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H8M +P36015 UniProtKB Turn 30 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6 +P36015 UniProtKB Helix 35 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6 +P36015 UniProtKB Beta strand 55 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6 +P36015 UniProtKB Beta strand 64 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6 +P36015 UniProtKB Beta strand 74 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6 +P36015 UniProtKB Helix 87 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6 +P36015 UniProtKB Helix 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6 +P36015 UniProtKB Turn 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6 +P36015 UniProtKB Helix 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6 +P36015 UniProtKB Helix 124 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BW6 +P36015 UniProtKB Helix 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IOU +##sequence-region P36111 1 568 +P36111 UniProtKB Chain 1 568 . . . ID=PRO_0000203196;Note=Uncharacterized protein YKR015C +##sequence-region P0CF00 1 54 +P0CF00 UniProtKB Chain 1 54 . . . ID=PRO_0000393298;Note=Putative uncharacterized protein YLR157W-E +##sequence-region P0CY01 1 160 +P0CY01 UniProtKB Chain 1 160 . . . ID=PRO_0000410457;Note=UPF0479 membrane protein YLL067W-A +P0CY01 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CY01 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CY01 UniProtKB Compositional bias 103 106 . . . Note=Poly-Ser +##sequence-region P0C5Q2 1 26 +P0C5Q2 UniProtKB Chain 1 26 . . . ID=PRO_0000309050;Note=Putative uncharacterized protein YMR013W-A +##sequence-region Q6Q572 1 108 +Q6Q572 UniProtKB Chain 1 108 . . . ID=PRO_0000299666;Note=Putative uncharacterized protein YMR031W-A +##sequence-region A0A023PZG9 1 121 +A0A023PZG9 UniProtKB Chain 1 121 . . . ID=PRO_0000431059;Note=Putative uncharacterized membrane protein YML047W-A +A0A023PZG9 UniProtKB Transmembrane 2 22 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZG9 UniProtKB Transmembrane 42 62 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZG9 UniProtKB Transmembrane 89 109 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q6B0Y6 1 121 +Q6B0Y6 UniProtKB Chain 1 121 . . . ID=PRO_0000299667;Note=Putative uncharacterized protein YMR052C-A +Q6B0Y6 UniProtKB Transmembrane 1 21 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q6B0Y6 UniProtKB Transmembrane 55 75 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q6B0Y6 UniProtKB Transmembrane 92 112 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q6B0Y6 UniProtKB Compositional bias 38 41 . . . Note=Poly-Phe +##sequence-region Q12744 1 133 +Q12744 UniProtKB Chain 1 133 . . . ID=PRO_0000299663;Note=Putative uncharacterized protein YML094C-A +##sequence-region Q3E7B5 1 62 +Q3E7B5 UniProtKB Chain 1 62 . . . ID=PRO_0000247791;Note=Uncharacterized protein YMR230W-A +##sequence-region Q04909 1 80 +Q04909 UniProtKB Chain 1 80 . . . ID=PRO_0000203361;Note=Putative UPF0377 protein YMR324C +Q04909 UniProtKB Transmembrane 13 33 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04526 1 418 +Q04526 UniProtKB Chain 1 418 . . . ID=PRO_0000203247;Note=Putative uncharacterized protein YML083C +##sequence-region P0CL35 1 160 +P0CL35 UniProtKB Chain 1 160 . . . ID=PRO_0000406010;Note=Putative UPF0479 protein YML133W-B +P0CL35 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL35 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL35 UniProtKB Compositional bias 103 106 . . . Note=Poly-Ser +##sequence-region P03881 1 472 +P03881 UniProtKB Chain 1 472 . . . ID=PRO_0000196879;Note=Uncharacterized mitochondrial protein RF1 +P03881 UniProtKB Compositional bias 20 84 . . . Note=Asn-rich +P03881 UniProtKB Compositional bias 361 427 . . . Note=Asn-rich +##sequence-region Q04674 1 123 +Q04674 UniProtKB Chain 1 123 . . . ID=PRO_0000203278;Note=Putative uncharacterized protein YMR057C +##sequence-region Q8TGL7 1 32 +Q8TGL7 UniProtKB Chain 1 32 . . . ID=PRO_0000299677;Note=Putative uncharacterized protein YNR003W-A +Q8TGL7 UniProtKB Compositional bias 4 8 . . . Note=Poly-Ser +##sequence-region Q3E7Z2 1 85 +Q3E7Z2 UniProtKB Chain 1 85 . . . ID=PRO_0000247802;Note=Uncharacterized protein YNL042W-B +##sequence-region Q8TGQ9 1 29 +Q8TGQ9 UniProtKB Chain 1 29 . . . ID=PRO_0000299675;Note=Putative uncharacterized protein YNL103W-A +##sequence-region Q8TGL9 1 27 +Q8TGL9 UniProtKB Chain 1 27 . . . ID=PRO_0000299674;Note=Putative uncharacterized protein YNL144W-A +##sequence-region P53737 1 142 +P53737 UniProtKB Chain 1 142 . . . ID=PRO_0000203479;Note=Putative uncharacterized protein YNR042W +P53737 UniProtKB Compositional bias 96 105 . . . Note=Poly-Glu +##sequence-region P53748 1 327 +P53748 UniProtKB Chain 1 327 . . . ID=PRO_0000203482;Note=Uncharacterized membrane protein YNR062C +P53748 UniProtKB Topological domain 1 19 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53748 UniProtKB Transmembrane 20 40 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53748 UniProtKB Topological domain 41 51 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53748 UniProtKB Transmembrane 52 72 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53748 UniProtKB Topological domain 73 104 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53748 UniProtKB Transmembrane 105 125 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53748 UniProtKB Topological domain 126 141 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53748 UniProtKB Transmembrane 142 162 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53748 UniProtKB Topological domain 163 199 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53748 UniProtKB Transmembrane 200 220 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53748 UniProtKB Topological domain 221 235 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53748 UniProtKB Transmembrane 236 256 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53748 UniProtKB Topological domain 257 275 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53748 UniProtKB Transmembrane 276 296 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53748 UniProtKB Topological domain 297 300 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53748 UniProtKB Transmembrane 301 321 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53748 UniProtKB Topological domain 322 327 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53976 1 612 +P53976 UniProtKB Chain 1 612 . . . ID=PRO_0000203462;Note=Uncharacterized protein YNL018C +##sequence-region P53963 1 612 +P53963 UniProtKB Chain 1 612 . . . ID=PRO_0000203458;Note=Uncharacterized protein YNL034W +##sequence-region P53952 1 270 +P53952 UniProtKB Chain 1 270 . . . ID=PRO_0000203452;Note=Uncharacterized protein YNL050C +##sequence-region P0CL36 1 160 +P0CL36 UniProtKB Chain 1 160 . . . ID=PRO_0000406011;Note=Putative UPF0479 protein YNL339W-B +P0CL36 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL36 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL36 UniProtKB Compositional bias 103 106 . . . Note=Poly-Ser +##sequence-region P53925 1 644 +P53925 UniProtKB Chain 1 644 . . . ID=PRO_0000203433;Note=Uncharacterized vacuolar membrane protein YNL115C +P53925 UniProtKB Topological domain 1 90 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53925 UniProtKB Transmembrane 91 111 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53925 UniProtKB Topological domain 112 122 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53925 UniProtKB Transmembrane 123 143 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53925 UniProtKB Topological domain 144 147 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53925 UniProtKB Transmembrane 148 168 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53925 UniProtKB Topological domain 169 174 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53925 UniProtKB Transmembrane 175 195 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53925 UniProtKB Topological domain 196 271 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53925 UniProtKB Transmembrane 272 292 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53925 UniProtKB Topological domain 293 644 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53925 UniProtKB Domain 348 619 . . . Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53925 UniProtKB Modified residue 22 22 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53925 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53925 UniProtKB Modified residue 63 63 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53925 UniProtKB Modified residue 244 244 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53925 UniProtKB Sequence conflict 644 644 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53908 1 130 +P53908 UniProtKB Chain 1 130 . . . ID=PRO_0000203424;Note=Uncharacterized membrane protein YNL143C +P53908 UniProtKB Topological domain 1 58 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53908 UniProtKB Transmembrane 59 79 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53908 UniProtKB Topological domain 80 94 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53908 UniProtKB Transmembrane 95 115 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53908 UniProtKB Topological domain 116 130 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53880 1 145 +P53880 UniProtKB Chain 1 145 . . . ID=PRO_0000203406;Note=Putative uncharacterized protein YNL179C +P53880 UniProtKB Transmembrane 46 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53856 1 143 +P53856 UniProtKB Chain 1 143 . . . ID=PRO_0000203385;Note=Putative uncharacterized protein YNL235C +P53856 UniProtKB Transmembrane 65 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E807 1 68 +Q3E807 UniProtKB Chain 1 68 . . . ID=PRO_0000235936;Note=Uncharacterized protein YOR011W-A +##sequence-region Q08205 1 117 +Q08205 UniProtKB Chain 1 117 . . . ID=PRO_0000299689;Note=Putative uncharacterized protein YOL037C +Q08205 UniProtKB Transmembrane 32 52 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08205 UniProtKB Transmembrane 56 76 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08205 UniProtKB Transmembrane 87 107 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36025 1 268 +P36025 UniProtKB Chain 1 268 . . . ID=PRO_0000203490;Note=Uncharacterized protein YOR062C +P36025 UniProtKB Sequence conflict 154 154 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36025 UniProtKB Sequence conflict 236 236 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08234 1 1294 +Q08234 UniProtKB Chain 1 1294 . . . ID=PRO_0000093467;Note=Uncharacterized ABC transporter ATP-binding protein/permease YOL075C +Q08234 UniProtKB Topological domain 1 375 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Transmembrane 376 396 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Topological domain 397 495 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Transmembrane 496 516 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Topological domain 517 530 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Transmembrane 531 551 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Topological domain 552 604 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Transmembrane 605 625 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Topological domain 626 1038 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Transmembrane 1039 1059 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Topological domain 1060 1120 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Transmembrane 1121 1141 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Topological domain 1142 1266 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Transmembrane 1267 1287 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Topological domain 1288 1294 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Domain 28 287 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q08234 UniProtKB Domain 679 941 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q08234 UniProtKB Nucleotide binding 62 69 . . . Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q08234 UniProtKB Nucleotide binding 727 734 . . . Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q08234 UniProtKB Glycosylation 41 41 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Glycosylation 86 86 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Glycosylation 101 101 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Glycosylation 151 151 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Glycosylation 341 341 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Glycosylation 349 349 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Glycosylation 371 371 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Glycosylation 528 528 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Glycosylation 983 983 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08234 UniProtKB Sequence conflict 1164 1164 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08234 UniProtKB Sequence conflict 1164 1164 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q3E7B9 1 74 +Q3E7B9 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E7B9 UniProtKB Chain 19 74 . . . ID=PRO_0000235935;Note=Uncharacterized protein YOR008C-A +Q3E7B9 UniProtKB Topological domain 19 21 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E7B9 UniProtKB Transmembrane 22 44 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E7B9 UniProtKB Topological domain 45 74 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12275 1 1648 +Q12275 UniProtKB Chain 1 1648 . . . ID=PRO_0000237653;Note=Uncharacterized protein YOR093C +Q12275 UniProtKB Transmembrane 228 248 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Transmembrane 1061 1081 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Transmembrane 1224 1244 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Domain 6 120 . . . Note=DMAP-interaction +Q12275 UniProtKB Modified residue 99 99 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12275 UniProtKB Modified residue 751 751 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12275 UniProtKB Glycosylation 28 28 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 71 71 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 98 98 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 128 128 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 151 151 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 209 209 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 288 288 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 328 328 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 575 575 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 644 644 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 730 730 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 881 881 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 917 917 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 995 995 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 1009 1009 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 1198 1198 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 1301 1301 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 1302 1302 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 1447 1447 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 1472 1472 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 1488 1488 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 1565 1565 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 1597 1597 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12275 UniProtKB Glycosylation 1634 1634 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0C272 1 63 +P0C272 UniProtKB Chain 1 63 . . . ID=PRO_0000268631;Note=Uncharacterized protein YOL013W-A +##sequence-region Q3E7Y8 1 44 +Q3E7Y8 UniProtKB Chain 1 44 . . . ID=PRO_0000235934;Note=Uncharacterized protein YOL155W-A +##sequence-region P0CF19 1 215 +P0CF19 UniProtKB Chain 1 215 . . . ID=PRO_0000269759;Note=Putative uncharacterized transporter YOL162W +P0CF19 UniProtKB Transmembrane 3 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CF19 UniProtKB Transmembrane 30 50 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CF19 UniProtKB Transmembrane 59 79 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CF19 UniProtKB Transmembrane 87 107 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CF19 UniProtKB Transmembrane 122 142 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CF19 UniProtKB Transmembrane 156 176 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGS2 1 50 +Q8TGS2 UniProtKB Chain 1 50 . . . ID=PRO_0000245273;Note=Uncharacterized protein YOL019W-A +##sequence-region Q12282 1 236 +Q12282 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12282 UniProtKB Chain 21 212 . . . ID=PRO_0000237664;Note=Cell wall protein YOR214C +Q12282 UniProtKB Propeptide 213 236 . . . ID=PRO_0000237665;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12282 UniProtKB Lipidation 212 212 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12282 UniProtKB Glycosylation 155 155 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12282 UniProtKB Glycosylation 160 160 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12282 UniProtKB Glycosylation 203 203 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12282 UniProtKB Glycosylation 212 212 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12225 1 109 +Q12225 UniProtKB Chain 1 109 . . . ID=PRO_0000299726;Note=Putative uncharacterized protein YOR225W +Q12225 UniProtKB Transmembrane 26 48 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08681 1 100 +Q08681 UniProtKB Chain 1 100 . . . ID=PRO_0000299729;Note=Putative uncharacterized protein YOR248W +##sequence-region Q08736 1 102 +Q08736 UniProtKB Chain 1 102 . . . ID=PRO_0000299731;Note=Putative uncharacterized protein YOR277C +Q08736 UniProtKB Transmembrane 27 47 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08736 UniProtKB Compositional bias 5 12 . . . Note=Poly-Ser +Q08736 UniProtKB Compositional bias 65 72 . . . Note=Poly-Ser +##sequence-region Q12040 1 230 +Q12040 UniProtKB Chain 1 230 . . . ID=PRO_0000245254;Note=Broad-specificity phosphatase YOR283W +Q12040 UniProtKB Region 36 37 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12040 UniProtKB Region 102 105 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12040 UniProtKB Active site 24 24 . . . Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62707 +Q12040 UniProtKB Active site 102 102 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62707 +Q12040 UniProtKB Site 166 166 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62707 +##sequence-region Q12261 1 157 +Q12261 UniProtKB Chain 1 157 . . . ID=PRO_0000299737;Note=Putative uncharacterized protein YOR325W +##sequence-region Q99326 1 363 +Q99326 UniProtKB Chain 1 363 . . . ID=PRO_0000245288;Note=SWIRM domain-containing protein YOR338W +Q99326 UniProtKB Domain 266 363 . . . Note=SWIRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00247 +##sequence-region Q08872 1 117 +Q08872 UniProtKB Chain 1 117 . . . ID=PRO_0000299743;Note=Putative uncharacterized protein YOR366W +##sequence-region Q08903 1 112 +Q08903 UniProtKB Chain 1 112 . . . ID=PRO_0000299744;Note=Putative uncharacterized protein YOR379C +##sequence-region Q06328 1 317 +Q06328 UniProtKB Chain 1 317 . . . ID=PRO_0000253843;Note=Probable vacuolar amino acid transporter YPQ2 +Q06328 UniProtKB Topological domain 1 13 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06328 UniProtKB Transmembrane 14 34 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06328 UniProtKB Topological domain 35 39 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06328 UniProtKB Transmembrane 40 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06328 UniProtKB Topological domain 63 71 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06328 UniProtKB Transmembrane 72 94 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06328 UniProtKB Topological domain 95 143 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06328 UniProtKB Transmembrane 144 164 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06328 UniProtKB Topological domain 165 184 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06328 UniProtKB Transmembrane 185 205 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06328 UniProtKB Topological domain 206 215 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06328 UniProtKB Transmembrane 216 236 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06328 UniProtKB Topological domain 237 249 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06328 UniProtKB Transmembrane 250 270 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06328 UniProtKB Topological domain 271 317 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06328 UniProtKB Domain 8 71 . . . Note=PQ-loop 1 +Q06328 UniProtKB Domain 185 247 . . . Note=PQ-loop 2 +Q06328 UniProtKB Modified residue 136 136 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40583 1 537 +P40583 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40583 UniProtKB Propeptide 25 52 . . . ID=PRO_0000025844;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40583 UniProtKB Chain 53 515 . . . ID=PRO_0000025845;Note=Aspartic proteinase yapsin-6 +P40583 UniProtKB Propeptide 516 537 . . . ID=PRO_0000025846;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40583 UniProtKB Domain 67 426 . . . Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103 +P40583 UniProtKB Active site 85 85 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103 +P40583 UniProtKB Active site 324 324 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103 +P40583 UniProtKB Lipidation 515 515 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40583 UniProtKB Glycosylation 57 57 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40583 UniProtKB Glycosylation 149 149 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40583 UniProtKB Glycosylation 156 156 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40583 UniProtKB Glycosylation 161 161 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40583 UniProtKB Glycosylation 183 183 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40583 UniProtKB Glycosylation 195 195 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40583 UniProtKB Glycosylation 311 311 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40583 UniProtKB Glycosylation 363 363 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40583 UniProtKB Glycosylation 375 375 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40583 UniProtKB Glycosylation 379 379 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40583 UniProtKB Glycosylation 472 472 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P48559 1 417 +P48559 UniProtKB Chain 1 417 . . . ID=PRO_0000121322;Note=GTP-binding protein YPT11 +P48559 UniProtKB Nucleotide binding 97 104 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48559 UniProtKB Nucleotide binding 228 232 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48559 UniProtKB Nucleotide binding 292 295 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48559 UniProtKB Lipidation 415 415 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P48559 UniProtKB Lipidation 416 416 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P48559 UniProtKB Mutagenesis 102 102 . . . Note=Impairs interaction with MYO2. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144 +P48559 UniProtKB Mutagenesis 206 206 . . . Note=Abolishes interaction with MYO2. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144 +##sequence-region P51996 1 222 +P51996 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38555 +P51996 UniProtKB Chain 2 222 . . . ID=PRO_0000121324;Note=GTP-binding protein YPT32/YPT11 +P51996 UniProtKB Nucleotide binding 20 27 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P51996 UniProtKB Nucleotide binding 68 72 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P51996 UniProtKB Nucleotide binding 126 129 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P51996 UniProtKB Motif 42 50 . . . Note=Effector region;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P51996 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38555 +P51996 UniProtKB Lipidation 221 221 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P51996 UniProtKB Lipidation 222 222 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P51996 UniProtKB Mutagenesis 27 27 . . . Note=Binds preferentially GDP. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12045183;Dbxref=PMID:12045183 +P51996 UniProtKB Mutagenesis 49 49 . . . Note=Cold sensitive. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12045183;Dbxref=PMID:12045183 +P51996 UniProtKB Mutagenesis 72 72 . . . Note=Reduces GTPase activity. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12045183;Dbxref=PMID:12045183 +P51996 UniProtKB Mutagenesis 126 126 . . . Note=Blocks nucleotide binding. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12045183;Dbxref=PMID:12045183 +P51996 UniProtKB Mutagenesis 141 141 . . . Note=Loss of function at 37 degrees Celsius. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9151665;Dbxref=PMID:9151665 +P51996 UniProtKB Beta strand 11 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO +P51996 UniProtKB Helix 26 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO +P51996 UniProtKB Beta strand 47 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO +P51996 UniProtKB Beta strand 60 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO +P51996 UniProtKB Helix 76 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO +P51996 UniProtKB Beta strand 88 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO +P51996 UniProtKB Helix 98 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO +P51996 UniProtKB Helix 104 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO +P51996 UniProtKB Beta strand 120 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO +P51996 UniProtKB Helix 128 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO +P51996 UniProtKB Helix 138 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO +P51996 UniProtKB Beta strand 151 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO +P51996 UniProtKB Turn 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO +P51996 UniProtKB Helix 163 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RWO +##sequence-region P40517 1 327 +P40517 UniProtKB Chain 1 327 . . . ID=PRO_0000213671;Note=Ran-specific GTPase-activating protein 2 +P40517 UniProtKB Domain 191 327 . . . Note=RanBD1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00164 +P40517 UniProtKB Modified residue 31 31 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40517 UniProtKB Modified residue 179 179 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40517 UniProtKB Beta strand 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF +P40517 UniProtKB Turn 142 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF +P40517 UniProtKB Helix 147 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF +P40517 UniProtKB Helix 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF +P40517 UniProtKB Beta strand 212 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF +P40517 UniProtKB Beta strand 232 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF +P40517 UniProtKB Beta strand 252 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF +P40517 UniProtKB Turn 259 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF +P40517 UniProtKB Beta strand 264 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF +P40517 UniProtKB Beta strand 276 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF +P40517 UniProtKB Beta strand 281 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF +P40517 UniProtKB Helix 286 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF +P40517 UniProtKB Beta strand 289 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF +P40517 UniProtKB Beta strand 303 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF +P40517 UniProtKB Helix 311 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WYF +##sequence-region P38374 1 65 +P38374 UniProtKB Chain 1 65 . . . ID=PRO_0000066513;Note=Protein YSY6 +P38374 UniProtKB Topological domain 1 44 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38374 UniProtKB Transmembrane 45 65 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P50111 1 915 +P50111 UniProtKB Chain 1 915 . . . ID=PRO_0000066569;Note=Protein ZDS1 +P50111 UniProtKB Compositional bias 716 719 . . . Note=Poly-Glu +P50111 UniProtKB Compositional bias 907 914 . . . Note=Poly-Gln +P50111 UniProtKB Modified residue 229 229 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P50111 UniProtKB Sequence conflict 84 84 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P50111 UniProtKB Sequence conflict 393 393 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P50111 UniProtKB Sequence conflict 413 413 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25620 1 114 +P25620 UniProtKB Chain 1 114 . . . ID=PRO_0000202564;Note=Uncharacterized protein YCR022C +##sequence-region P25352 1 136 +P25352 UniProtKB Chain 1 136 . . . ID=PRO_0000202565;Note=Uncharacterized protein YCR025C +##sequence-region P25640 1 136 +P25640 UniProtKB Chain 1 136 . . . ID=PRO_0000202573;Note=Putative uncharacterized protein YCR064C +##sequence-region Q12264 1 106 +Q12264 UniProtKB Chain 1 106 . . . ID=PRO_0000299845;Note=Putative uncharacterized protein YDL023C +##sequence-region Q07355 1 123 +Q07355 UniProtKB Chain 1 123 . . . ID=PRO_0000299851;Note=Putative uncharacterized protein YDL050C +Q07355 UniProtKB Transmembrane 34 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12298 1 539 +Q12298 UniProtKB Chain 1 539 . . . ID=PRO_0000244440;Note=Uncharacterized ABC transporter ATP-binding protein YDR061W +Q12298 UniProtKB Domain 8 265 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q12298 UniProtKB Domain 307 537 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q12298 UniProtKB Nucleotide binding 339 346 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +##sequence-region Q8TGP8 1 144 +Q8TGP8 UniProtKB Chain 1 144 . . . ID=PRO_0000299855;Note=Putative uncharacterized protein YDL086C-A +##sequence-region Q03864 1 110 +Q03864 UniProtKB Chain 1 110 . . . ID=PRO_0000299873;Note=Uncharacterized protein YDR102C +##sequence-region Q07535 1 126 +Q07535 UniProtKB Chain 1 126 . . . ID=PRO_0000277621;Note=Putative uncharacterized protein YDL118W +##sequence-region Q07555 1 291 +Q07555 UniProtKB Chain 1 291 . . . ID=PRO_0000240872;Note=Uncharacterized protein YDL129W +Q07555 UniProtKB Modified residue 267 267 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q03900 1 495 +Q03900 UniProtKB Chain 1 495 . . . ID=PRO_0000253831;Note=Uncharacterized protein YDR132C +##sequence-region P0CX65 1 440 +P0CX65 UniProtKB Chain 1 440 . . . ID=PRO_0000203500;Note=Transposon Ty1-DR5 Gag polyprotein +P0CX65 UniProtKB Chain 1 401 . . . ID=PRO_0000279030;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX65 UniProtKB Peptide 402 440 . . . ID=PRO_0000279031;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX65 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX65 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0CX65 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX65 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region Q3E774 1 43 +Q3E774 UniProtKB Chain 1 43 . . . ID=PRO_0000240876;Note=Uncharacterized protein YDL159W-A +##sequence-region Q12135 1 159 +Q12135 UniProtKB Chain 1 159 . . . ID=PRO_0000299862;Note=Putative uncharacterized protein YDL172C +Q12135 UniProtKB Transmembrane 17 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12135 UniProtKB Transmembrane 44 64 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12135 UniProtKB Transmembrane 67 87 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12301 1 547 +Q12301 UniProtKB Chain 1 547 . . . ID=PRO_0000241453;Note=Uncharacterized membrane protein YDL180W +Q12301 UniProtKB Topological domain 1 19 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12301 UniProtKB Transmembrane 20 40 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12301 UniProtKB Topological domain 41 64 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12301 UniProtKB Transmembrane 65 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12301 UniProtKB Topological domain 86 89 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12301 UniProtKB Transmembrane 90 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12301 UniProtKB Topological domain 111 139 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12301 UniProtKB Transmembrane 140 160 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12301 UniProtKB Topological domain 161 340 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12301 UniProtKB Transmembrane 341 361 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12301 UniProtKB Topological domain 362 394 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12301 UniProtKB Transmembrane 395 415 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12301 UniProtKB Topological domain 416 523 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12301 UniProtKB Transmembrane 524 544 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12301 UniProtKB Topological domain 545 547 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12301 UniProtKB Modified residue 225 225 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q8TGR6 1 39 +Q8TGR6 UniProtKB Chain 1 39 . . . ID=PRO_0000299751;Note=Putative uncharacterized protein YDR524C-A +##sequence-region Q6Q5X2 1 51 +Q6Q5X2 UniProtKB Chain 1 51 . . . ID=PRO_0000242623;Note=Cysteine-rich and transmembrane domain-containing protein YDR034W-B +Q6Q5X2 UniProtKB Transmembrane 28 44 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q6Q5X2 UniProtKB Compositional bias 30 48 . . . Note=Cys-rich +##sequence-region Q04170 1 232 +Q04170 UniProtKB Chain 1 232 . . . ID=PRO_0000253851;Note=Uncharacterized protein YDR391C +##sequence-region P87269 1 146 +P87269 UniProtKB Chain 1 146 . . . ID=PRO_0000299893;Note=Putative uncharacterized protein YDR433W +P87269 UniProtKB Compositional bias 39 117 . . . Note=Val-rich +##sequence-region Q04100 1 135 +Q04100 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04100 UniProtKB Chain 26 135 . . . ID=PRO_0000299895;Note=Putative uncharacterized protein YDR445C +Q04100 UniProtKB Transmembrane 51 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04434 1 166 +Q04434 UniProtKB Chain 1 166 . . . ID=PRO_0000299904;Note=Putative uncharacterized protein YDR535C +##sequence-region Q03051 1 99 +Q03051 UniProtKB Chain 1 99 . . . ID=PRO_0000211369;Note=Putative UPF0320 protein YDR543C +##sequence-region Q04585 1 715 +Q04585 UniProtKB Chain 1 715 . . . ID=PRO_0000244445;Note=Uncharacterized sugar kinase YDR109C +##sequence-region Q3E7X8 1 1277 +Q3E7X8 UniProtKB Chain 1 1277 . . . ID=PRO_0000268166;Note=Y' element ATP-dependent helicase YEL077C +Q3E7X8 UniProtKB Domain 222 399 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q3E7X8 UniProtKB Domain 454 605 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q3E7X8 UniProtKB Nucleotide binding 235 242 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q3E7X8 UniProtKB Motif 345 348 . . . Note=DEAH box +Q3E7X8 UniProtKB Compositional bias 683 875 . . . Note=Thr-rich +##sequence-region P0C5M8 1 29 +P0C5M8 UniProtKB Chain 1 29 . . . ID=PRO_0000309026;Note=Uncharacterized protein YER090C-A +##sequence-region A0A023PZG5 1 101 +A0A023PZG5 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZG5 UniProtKB Chain 26 101 . . . ID=PRO_0000431000;Note=Putative uncharacterized protein YER137W-A +##sequence-region A0A023PXK2 1 192 +A0A023PXK2 UniProtKB Chain 1 192 . . . ID=PRO_0000431003;Note=Putative uncharacterized membrane protein YER148W-A +A0A023PXK2 UniProtKB Transmembrane 7 29 . . . Note=Helical%3B Signal-anchor;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXK2 UniProtKB Transmembrane 51 67 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXK2 UniProtKB Compositional bias 10 192 . . . Note=Ser-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00016 +##sequence-region P39992 1 682 +P39992 UniProtKB Chain 1 682 . . . ID=PRO_0000202610;Note=Uncharacterized protein YEL023C +P39992 UniProtKB Sequence conflict 281 281 . . . Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32616 1 141 +P32616 UniProtKB Chain 1 141 . . . ID=PRO_0000202606;Note=Uncharacterized protein YEL045C +P32616 UniProtKB Transmembrane 38 58 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32616 UniProtKB Transmembrane 67 87 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32616 UniProtKB Nucleotide binding 15 22 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07804 1 573 +Q07804 UniProtKB Chain 1 573 . . . ID=PRO_0000248404;Note=Sterol esterase 1 +Q07804 UniProtKB Topological domain 1 12 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07804 UniProtKB Intramembrane 13 33 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07804 UniProtKB Topological domain 34 573 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07804 UniProtKB Active site 315 315 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07804 UniProtKB Active site 489 489 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07804 UniProtKB Active site 520 520 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P0CX61 1 438 +P0CX61 UniProtKB Chain 1 438 . . . ID=PRO_0000279313;Note=Transposon Ty2-F Gag polyprotein +P0CX61 UniProtKB Chain 1 397 . . . ID=PRO_0000279314;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX61 UniProtKB Peptide 398 438 . . . ID=PRO_0000279315;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX61 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX61 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q45U48 1 73 +Q45U48 UniProtKB Chain 1 73 . . . ID=PRO_0000245382;Note=Uncharacterized protein YGR035W-A +##sequence-region Q2V2P6 1 80 +Q2V2P6 UniProtKB Chain 1 80 . . . ID=PRO_0000245377;Note=Uncharacterized protein YGL194C-A +Q2V2P6 UniProtKB Transmembrane 12 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53225 1 103 +P53225 UniProtKB Chain 1 103 . . . ID=PRO_0000202793;Note=Uncharacterized protein YGR039W +P53225 UniProtKB Natural variant 26 26 . . . Note=In strain: SK1. E->G +P53225 UniProtKB Natural variant 39 39 . . . Note=In strain: SK1. S->R +P53225 UniProtKB Natural variant 79 79 . . . Note=In strain: SK1. N->D +##sequence-region P0C2J2 1 438 +P0C2J2 UniProtKB Chain 1 438 . . . ID=PRO_0000279321;Note=Transposon Ty2-GR1 Gag polyprotein +P0C2J2 UniProtKB Chain 1 397 . . . ID=PRO_0000279322;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J2 UniProtKB Peptide 398 438 . . . ID=PRO_0000279323;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J2 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J2 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q3E786 1 66 +Q3E786 UniProtKB Chain 1 66 . . . ID=PRO_0000245389;Note=Uncharacterized protein YGR240C-A +##sequence-region P53242 1 292 +P53242 UniProtKB Chain 1 292 . . . ID=PRO_0000202803;Note=Uncharacterized protein YGR066C +P53242 UniProtKB Natural variant 231 231 . . . Note=In strain: SK1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P53242 UniProtKB Sequence conflict 229 229 . . . Note=L->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53268 1 129 +P53268 UniProtKB Chain 1 129 . . . ID=PRO_0000202815;Note=Putative uncharacterized protein YGR114C +P53268 UniProtKB Transmembrane 15 35 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53268 UniProtKB Transmembrane 48 68 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53268 UniProtKB Transmembrane 107 127 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q99315 1 1547 +Q99315 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15956549;Dbxref=PMID:15956549 +Q99315 UniProtKB Chain 2 1547 . . . ID=PRO_0000279356;Note=Transposon Ty3-G Gag-Pol polyprotein +Q99315 UniProtKB Chain 2 207 . . . ID=PRO_0000279357;Note=Capsid protein +Q99315 UniProtKB Peptide 208 233 . . . ID=PRO_0000279358;Note=Spacer peptide p3 +Q99315 UniProtKB Chain 234 309 . . . ID=PRO_0000279359;Note=Nucleocapsid protein p11 +Q99315 UniProtKB Chain 310 442 . . . ID=PRO_0000279360;Note=Ty3 protease +Q99315 UniProtKB Peptide 443 535 . . . ID=PRO_0000279361;Note=Spacer peptide J;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99315 UniProtKB Chain 536 1011 . . . ID=PRO_0000279362;Note=Reverse transcriptase/ribonuclease H +Q99315 UniProtKB Chain 1012 1547 . . . ID=PRO_0000279363;Note=Integrase p61 +Q99315 UniProtKB Chain 1038 1547 . . . ID=PRO_0000279364;Note=Integrase p58 +Q99315 UniProtKB Domain 620 797 . . . Note=Reverse transcriptase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405 +Q99315 UniProtKB Domain 893 1011 . . . Note=RNase H Ty3/gyspy-type +Q99315 UniProtKB Domain 1159 1324 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99315 UniProtKB Zinc finger 265 282 . . . Note=CCHC-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +Q99315 UniProtKB Region 1106 1145 . . . Note=Integrase-type zinc finger-like +Q99315 UniProtKB Active site 336 336 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99315 UniProtKB Metal binding 686 686 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99315 UniProtKB Metal binding 748 748 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99315 UniProtKB Metal binding 749 749 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99315 UniProtKB Metal binding 893 893 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99315 UniProtKB Metal binding 936 936 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99315 UniProtKB Metal binding 961 961 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99315 UniProtKB Metal binding 1175 1175 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99315 UniProtKB Metal binding 1236 1236 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99315 UniProtKB Site 207 208 . . . Note=Cleavage%3B by Ty3 protease +Q99315 UniProtKB Site 233 234 . . . Note=Cleavage%3B by Ty3 protease +Q99315 UniProtKB Site 309 310 . . . Note=Cleavage%3B by Ty3 protease +Q99315 UniProtKB Site 442 443 . . . Note=Cleavage%3B by Ty3 protease;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99315 UniProtKB Site 535 536 . . . Note=Cleavage%3B by Ty3 protease +Q99315 UniProtKB Site 1011 1012 . . . Note=Cleavage%3B by Ty3 protease +Q99315 UniProtKB Site 1037 1038 . . . Note=Cleavage%3B by Ty3 protease%3B partial +Q99315 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15956549;Dbxref=PMID:15956549 +Q99315 UniProtKB Mutagenesis 267 267 . . . Note=Reduces level of VLP formation and maturation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7515969;Dbxref=PMID:7515969 +Q99315 UniProtKB Mutagenesis 275 275 . . . Note=Reduces level of VLP formation and maturation. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7515969;Dbxref=PMID:7515969 +Q99315 UniProtKB Turn 552 555 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 558 563 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Turn 565 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 608 621 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Beta strand 636 640 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Beta strand 646 650 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 653 656 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 669 673 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Beta strand 681 687 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 690 693 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Beta strand 694 696 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 698 704 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Beta strand 712 717 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 725 737 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Beta strand 743 746 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Beta strand 749 756 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 757 773 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 780 782 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Beta strand 795 797 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Beta strand 802 804 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 806 809 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Turn 810 814 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 821 832 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Turn 833 837 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 841 844 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 849 853 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 863 871 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Turn 876 878 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Beta strand 884 891 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Beta strand 899 906 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Beta strand 908 911 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Beta strand 913 921 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 932 944 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 948 951 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Beta strand 957 959 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 965 969 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Beta strand 970 972 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 976 986 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Beta strand 997 1000 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +Q99315 UniProtKB Helix 1001 1008 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OL8 +##sequence-region P53278 1 816 +P53278 UniProtKB Chain 1 816 . . . ID=PRO_0000202822;Note=Uncharacterized protein YGR130C +P53278 UniProtKB Compositional bias 164 185 . . . Note=Poly-Ser +P53278 UniProtKB Compositional bias 205 218 . . . Note=Poly-Thr +P53278 UniProtKB Modified residue 286 286 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53278 UniProtKB Modified residue 343 343 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P53278 UniProtKB Modified residue 347 347 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P53278 UniProtKB Modified residue 809 809 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P0C5N3 1 154 +P0C5N3 UniProtKB Transit peptide 1 42 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C5N3 UniProtKB Chain 43 154 . . . ID=PRO_0000309031;Note=Uncharacterized protein YGL041W-A%2C mitochondrial +##sequence-region P42936 1 225 +P42936 UniProtKB Chain 1 225 . . . ID=PRO_0000186046;Note=Putative elongation factor 1 gamma homolog +P42936 UniProtKB Domain 94 225 . . . Note=GST C-terminal +##sequence-region P53310 1 102 +P53310 UniProtKB Chain 1 102 . . . ID=PRO_0000202857;Note=Putative uncharacterized protein YGR242W +P53310 UniProtKB Transmembrane 29 52 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40326 1 108 +P40326 UniProtKB Chain 1 108 . . . ID=PRO_0000202866;Note=Uncharacterized protein YGR269W +P40326 UniProtKB Sequence conflict 53 53 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53156 1 320 +P53156 UniProtKB Chain 1 320 . . . ID=PRO_0000202758;Note=Uncharacterized protein YGL081W +P53156 UniProtKB Domain 22 86 . . . Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 +P53156 UniProtKB Compositional bias 235 269 . . . Note=Asp/Glu-rich (highly acidic) +P53156 UniProtKB Compositional bias 248 258 . . . Note=Poly-Glu +##sequence-region P53143 1 142 +P53143 UniProtKB Chain 1 142 . . . ID=PRO_0000202753;Note=Putative uncharacterized protein YGL102C +##sequence-region P53071 1 178 +P53071 UniProtKB Chain 1 178 . . . ID=PRO_0000202710;Note=Uncharacterized protein YGL235W +##sequence-region A0A023PXE5 1 117 +A0A023PXE5 UniProtKB Chain 1 117 . . . ID=PRO_0000431015;Note=Putative uncharacterized protein YHL006W-A +##sequence-region O13535 1 1793 +O13535 UniProtKB Chain 1 1793 . . . ID=PRO_0000279074;Note=Transposon Ty1-H Gag-Pol polyprotein +O13535 UniProtKB Chain 1 439 . . . ID=PRO_0000279075;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +O13535 UniProtKB Chain 440 620 . . . ID=PRO_0000279076;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +O13535 UniProtKB Chain 621 1255 . . . ID=PRO_0000279077;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +O13535 UniProtKB Chain 1256 1793 . . . ID=PRO_0000279078;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +O13535 UniProtKB Domain 698 873 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +O13535 UniProtKB Domain 1376 1514 . . . Note=Reverse transcriptase Ty1/copia-type +O13535 UniProtKB Domain 1648 1790 . . . Note=RNase H Ty1/copia-type +O13535 UniProtKB Region 337 439 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +O13535 UniProtKB Region 621 678 . . . Note=Integrase-type zinc finger-like +O13535 UniProtKB Motif 1216 1250 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +O13535 UniProtKB Compositional bias 72 146 . . . Note=Pro-rich +O13535 UniProtKB Active site 499 499 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +O13535 UniProtKB Metal binding 709 709 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +O13535 UniProtKB Metal binding 774 774 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +O13535 UniProtKB Metal binding 1384 1384 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +O13535 UniProtKB Metal binding 1465 1465 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +O13535 UniProtKB Metal binding 1466 1466 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +O13535 UniProtKB Metal binding 1648 1648 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +O13535 UniProtKB Metal binding 1690 1690 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +O13535 UniProtKB Metal binding 1723 1723 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +O13535 UniProtKB Site 439 440 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +O13535 UniProtKB Site 620 621 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +O13535 UniProtKB Site 1255 1256 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q05451 1 56 +Q05451 UniProtKB Chain 1 56 . . . ID=PRO_0000202894;Note=Putative uncharacterized protein YHR050W-A +##sequence-region P38809 1 366 +P38809 UniProtKB Chain 1 366 . . . ID=PRO_0000202907;Note=Uncharacterized protein YHR097C +P38809 UniProtKB Modified residue 69 69 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38809 UniProtKB Modified residue 76 76 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38809 UniProtKB Modified residue 189 189 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38809 UniProtKB Modified residue 288 288 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38809 UniProtKB Modified residue 294 294 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38809 UniProtKB Modified residue 359 359 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38809 UniProtKB Cross-link 78 78 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P38809 UniProtKB Cross-link 187 187 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P38809 UniProtKB Cross-link 242 242 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region P38834 1 111 +P38834 UniProtKB Chain 1 111 . . . ID=PRO_0000202916;Note=Uncharacterized protein YHR130C +P38834 UniProtKB Transmembrane 18 41 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38841 1 114 +P38841 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38841 UniProtKB Chain 20 114 . . . ID=PRO_0000026706;Note=Uncharacterized protein YHR138C +P38841 UniProtKB Modified residue 41 41 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P0CI67 1 198 +P0CI67 UniProtKB Chain 1 198 . . . ID=PRO_0000402771;Note=Uncharacterized protein YHR213W +P0CI67 UniProtKB Domain 1 110 . . . Note=PA14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01164 +P0CI67 UniProtKB Compositional bias 133 198 . . . Note=Ser/Thr-rich +##sequence-region Q3E7Z3 1 45 +Q3E7Z3 UniProtKB Chain 1 45 . . . ID=PRO_0000245406;Note=Uncharacterized protein YIR018C-A +##sequence-region Q3E739 1 70 +Q3E739 UniProtKB Chain 1 70 . . . ID=PRO_0000245407;Note=Uncharacterized protein YIR021W-A +Q3E739 UniProtKB Transmembrane 15 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03884 1 112 +Q03884 UniProtKB Chain 1 112 . . . ID=PRO_0000299757;Note=Putative uncharacterized protein YIL100C-A +Q03884 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03884 UniProtKB Transmembrane 58 78 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03884 UniProtKB Transmembrane 91 111 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CL42 1 160 +P0CL42 UniProtKB Chain 1 160 . . . ID=PRO_0000406015;Note=Putative UPF0479 protein YJL225W-A +P0CL42 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL42 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL42 UniProtKB Compositional bias 103 106 . . . Note=Poly-Ser +##sequence-region P0CL25 1 75 +P0CL25 UniProtKB Chain 1 75 . . . ID=PRO_0000202950;Note=Putative UPF0377 protein YIL174W +##sequence-region P40566 1 764 +P40566 UniProtKB Chain 1 764 . . . ID=PRO_0000184056;Note=Uncharacterized glycosyl hydrolase YIR007W +P40566 UniProtKB Active site 265 265 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40566 UniProtKB Modified residue 594 594 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40572 1 265 +P40572 UniProtKB Chain 1 265 . . . ID=PRO_0000203005;Note=Uncharacterized protein YIR016W +P40572 UniProtKB Nucleotide binding 137 144 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40586 1 236 +P40586 UniProtKB Chain 1 236 . . . ID=PRO_0000203009;Note=Uncharacterized protein YIR042C +P40586 UniProtKB Domain 47 191 . . . Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532 +##sequence-region P47100 1 1755 +P47100 UniProtKB Chain 1 1755 . . . ID=PRO_0000199564;Note=Transposon Ty1-JR2 Gag-Pol polyprotein +P47100 UniProtKB Chain 1 401 . . . ID=PRO_0000279088;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47100 UniProtKB Chain 402 582 . . . ID=PRO_0000279089;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47100 UniProtKB Chain 583 1217 . . . ID=PRO_0000279090;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47100 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279091;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47100 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47100 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +P47100 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +P47100 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47100 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +P47100 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47100 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +P47100 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47100 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47100 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47100 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47100 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47100 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47100 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47100 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47100 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47100 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47100 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47100 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region P0CL41 1 160 +P0CL41 UniProtKB Chain 1 160 . . . ID=PRO_0000299787;Note=Putative UPF0479 protein YIL177W-A +P0CL41 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL41 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL41 UniProtKB Compositional bias 103 106 . . . Note=Poly-Ser +##sequence-region P47139 1 656 +P47139 UniProtKB Chain 1 656 . . . ID=PRO_0000203108;Note=Uncharacterized protein YJR098C +P47139 UniProtKB Modified residue 39 39 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47139 UniProtKB Sequence conflict 410 415 . . . Note=TIFTKE->LFSLR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47145 1 328 +P47145 UniProtKB Chain 1 328 . . . ID=PRO_0000090374;Note=Putative lipase YJR107W +P47145 UniProtKB Active site 181 181 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59952 +P47145 UniProtKB Active site 253 253 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59952 +P47145 UniProtKB Active site 315 315 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59952 +P47145 UniProtKB Sequence conflict 14 14 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47145 UniProtKB Sequence conflict 66 66 . . . Note=G->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47148 1 283 +P47148 UniProtKB Chain 1 283 . . . ID=PRO_0000203112;Note=Uncharacterized protein YJR111C +##sequence-region P47172 1 347 +P47172 UniProtKB Chain 1 347 . . . ID=PRO_0000203125;Note=Uncharacterized protein YJR141W +##sequence-region P47184 1 120 +P47184 UniProtKB Chain 1 120 . . . ID=PRO_0000203129;Note=Putative uncharacterized protein YJR157W +##sequence-region P47022 1 219 +P47022 UniProtKB Chain 1 219 . . . ID=PRO_0000203044;Note=Uncharacterized protein YJL118W +P47022 UniProtKB Transmembrane 81 101 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47022 UniProtKB Transmembrane 168 188 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47022 UniProtKB Compositional bias 149 155 . . . Note=Poly-Arg +P47022 UniProtKB Compositional bias 191 196 . . . Note=Poly-Gln +##sequence-region P47020 1 107 +P47020 UniProtKB Chain 1 107 . . . ID=PRO_0000203042;Note=Putative uncharacterized protein YJL120W +P47020 UniProtKB Transmembrane 15 35 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47020 UniProtKB Transmembrane 43 63 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47020 UniProtKB Transmembrane 87 107 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47014 1 750 +P47014 UniProtKB Chain 1 750 . . . ID=PRO_0000203038;Note=Uncharacterized protein YJL132W +P47014 UniProtKB Transmembrane 1 21 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47014 UniProtKB Transmembrane 465 485 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47014 UniProtKB Transmembrane 586 606 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47085 1 338 +P47085 UniProtKB Chain 1 338 . . . ID=PRO_0000134398;Note=MEMO1 family protein YJR008W +##sequence-region P47090 1 510 +P47090 UniProtKB Chain 1 510 . . . ID=PRO_0000203085;Note=Uncharacterized endoplasmic reticulum membrane protein YJR015W +P47090 UniProtKB Topological domain 1 89 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47090 UniProtKB Transmembrane 90 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47090 UniProtKB Topological domain 111 123 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47090 UniProtKB Transmembrane 124 144 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47090 UniProtKB Topological domain 145 312 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47090 UniProtKB Transmembrane 313 333 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47090 UniProtKB Topological domain 334 349 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47090 UniProtKB Transmembrane 350 370 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47090 UniProtKB Topological domain 371 381 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47090 UniProtKB Transmembrane 382 402 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47090 UniProtKB Topological domain 403 416 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47090 UniProtKB Transmembrane 417 437 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47090 UniProtKB Topological domain 438 474 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47090 UniProtKB Transmembrane 475 495 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47090 UniProtKB Topological domain 496 510 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47090 UniProtKB Sequence conflict 324 324 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q3E826 1 78 +Q3E826 UniProtKB Chain 1 78 . . . ID=PRO_0000245421;Note=Uncharacterized protein YKL068W-A +##sequence-region P36140 1 101 +P36140 UniProtKB Chain 1 101 . . . ID=PRO_0000203214;Note=Putative uncharacterized protein YKR047W +##sequence-region P36153 1 106 +P36153 UniProtKB Chain 1 106 . . . ID=PRO_0000203220;Note=Uncharacterized protein YKR073C +##sequence-region P36099 1 201 +P36099 UniProtKB Chain 1 201 . . . ID=PRO_0000203188;Note=Putative uncharacterized protein YKL030W +##sequence-region P36087 1 169 +P36087 UniProtKB Chain 1 169 . . . ID=PRO_0000203172;Note=Uncharacterized protein YKL070W +##sequence-region P36079 1 204 +P36079 UniProtKB Chain 1 204 . . . ID=PRO_0000203166;Note=Putative uncharacterized protein YKL083W +##sequence-region P36030 1 115 +P36030 UniProtKB Chain 1 115 . . . ID=PRO_0000211374;Note=Putative UPF0320 protein YKL225W +##sequence-region P36109 1 125 +P36109 UniProtKB Chain 1 125 . . . ID=PRO_0000203195;Note=Putative uncharacterized protein YKR012C +##sequence-region Q07895 1 862 +Q07895 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07895 UniProtKB Chain 24 862 . . . ID=PRO_0000247181;Note=FAS1 domain-containing protein YLR001C +Q07895 UniProtKB Topological domain 24 762 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07895 UniProtKB Transmembrane 763 783 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07895 UniProtKB Topological domain 784 862 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07895 UniProtKB Domain 34 162 . . . Note=FAS1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00082 +Q07895 UniProtKB Domain 463 604 . . . Note=FAS1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00082 +Q07895 UniProtKB Domain 606 744 . . . Note=FAS1 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00082 +Q07895 UniProtKB Glycosylation 68 68 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07895 UniProtKB Glycosylation 112 112 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07895 UniProtKB Glycosylation 152 152 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07895 UniProtKB Glycosylation 200 200 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07895 UniProtKB Glycosylation 291 291 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07895 UniProtKB Glycosylation 333 333 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07895 UniProtKB Glycosylation 450 450 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07895 UniProtKB Glycosylation 521 521 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07895 UniProtKB Glycosylation 542 542 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07895 UniProtKB Glycosylation 569 569 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07895 UniProtKB Glycosylation 663 663 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07895 UniProtKB Glycosylation 679 679 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07895 UniProtKB Glycosylation 688 688 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07927 1 99 +Q07927 UniProtKB Chain 1 99 . . . ID=PRO_0000247155;Note=Uncharacterized protein YLR012C +##sequence-region P0CF33 1 103 +P0CF33 UniProtKB Chain 1 103 . . . ID=PRO_0000393435;Note=Putative truncated guanine nucleotide exchange factor YLL017W +P0CF33 UniProtKB Domain 26 97 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +##sequence-region Q07967 1 263 +Q07967 UniProtKB Chain 1 263 . . . ID=PRO_0000247203;Note=Putative uncharacterized protein YLR030W +##sequence-region Q07834 1 825 +Q07834 UniProtKB Chain 1 825 . . . ID=PRO_0000247115;Note=KH domain-containing protein YLL032C +Q07834 UniProtKB Domain 482 556 . . . Note=KH +Q07834 UniProtKB Compositional bias 783 806 . . . Note=Tyr-rich +Q07834 UniProtKB Modified residue 762 762 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +##sequence-region Q12110 1 428 +Q12110 UniProtKB Chain 1 428 . . . ID=PRO_0000247204;Note=Uncharacterized protein YLR049C +Q12110 UniProtKB Compositional bias 89 97 . . . Note=Poly-Ser +Q12110 UniProtKB Modified residue 127 127 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198 +##sequence-region Q12244 1 843 +Q12244 UniProtKB Chain 1 843 . . . ID=PRO_0000247135;Note=Uncharacterized transcriptional regulatory protein YLL054C +Q12244 UniProtKB DNA binding 15 42 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +##sequence-region Q99208 1 1374 +Q99208 UniProtKB Chain 1 1374 . . . ID=PRO_0000268167;Note=Y' element ATP-dependent helicase YLL066C +Q99208 UniProtKB Domain 375 552 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q99208 UniProtKB Domain 609 758 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q99208 UniProtKB Nucleotide binding 388 395 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q99208 UniProtKB Motif 498 501 . . . Note=DEAH box +Q99208 UniProtKB Compositional bias 836 972 . . . Note=Thr-rich +##sequence-region P0CX68 1 440 +P0CX68 UniProtKB Chain 1 440 . . . ID=PRO_0000409785;Note=Transposon Ty1-LR1 Gag polyprotein +P0CX68 UniProtKB Chain 1 401 . . . ID=PRO_0000409786;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX68 UniProtKB Peptide 402 440 . . . ID=PRO_0000409787;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX68 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX68 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0CX68 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX68 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region Q12138 1 136 +Q12138 UniProtKB Chain 1 136 . . . ID=PRO_0000247351;Note=Putative uncharacterized protein YLR125W +##sequence-region P0CE96 1 114 +P0CE96 UniProtKB Chain 1 114 . . . ID=PRO_0000203233;Note=Putative uncharacterized protein YLR156W +##sequence-region O13531 1 108 +O13531 UniProtKB Chain 1 108 . . . ID=PRO_0000299622;Note=Putative uncharacterized protein YLR202C +##sequence-region Q05948 1 407 +Q05948 UniProtKB Chain 1 407 . . . ID=PRO_0000247175;Note=Uncharacterized SVF1-like protein YLR225C +Q05948 UniProtKB Cross-link 22 22 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region A0A023PXG7 1 101 +A0A023PXG7 UniProtKB Chain 1 101 . . . ID=PRO_0000431044;Note=Putative uncharacterized membrane protein YLR230W +A0A023PXG7 UniProtKB Transmembrane 68 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PXP4 1 132 +A0A023PXP4 UniProtKB Chain 1 132 . . . ID=PRO_0000431045;Note=Putative uncharacterized protein YLR235C +##sequence-region O13574 1 117 +O13574 UniProtKB Chain 1 117 . . . ID=PRO_0000299626;Note=Uncharacterized protein YLR255C +##sequence-region Q06146 1 321 +Q06146 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q06146 UniProtKB Chain 2 321 . . . ID=PRO_0000247208;Note=Uncharacterized protein YLR257W +Q06146 UniProtKB Modified residue 2 2 . . . Note=N-acetylvaline;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q06146 UniProtKB Modified residue 44 44 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q06146 UniProtKB Modified residue 49 49 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06146 UniProtKB Modified residue 69 69 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06146 UniProtKB Modified residue 121 121 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +Q06146 UniProtKB Modified residue 126 126 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06146 UniProtKB Modified residue 129 129 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q06146 UniProtKB Modified residue 137 137 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06146 UniProtKB Modified residue 139 139 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06146 UniProtKB Modified residue 159 159 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06146 UniProtKB Modified residue 238 238 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q06146 UniProtKB Modified residue 240 240 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q06146 UniProtKB Modified residue 242 242 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q06146 UniProtKB Modified residue 270 270 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q06152 1 274 +Q06152 UniProtKB Chain 1 274 . . . ID=PRO_0000247779;Note=Uncharacterized protein YLR271W +Q06152 UniProtKB Domain 41 87 . . . Note=G-patch;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00092 +##sequence-region O13540 1 129 +O13540 UniProtKB Chain 1 129 . . . ID=PRO_0000299628;Note=Putative uncharacterized protein YLR279W +O13540 UniProtKB Transmembrane 46 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E810 1 57 +Q3E810 UniProtKB Chain 1 57 . . . ID=PRO_0000247211;Note=Uncharacterized protein YLR342W-A +Q3E810 UniProtKB Transmembrane 4 26 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06137 1 509 +Q06137 UniProtKB Chain 1 509 . . . ID=PRO_0000268185;Note=Putative 6-phosphofructo-2-kinase/fructose-2%2C6-bisphosphatase YLR345W +Q06137 UniProtKB Nucleotide binding 90 98 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +Q06137 UniProtKB Nucleotide binding 212 217 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +Q06137 UniProtKB Nucleotide binding 415 418 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07953 +Q06137 UniProtKB Nucleotide binding 460 464 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07953 +Q06137 UniProtKB Region 6 291 . . . Note=6-phosphofructo-2-kinase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06137 UniProtKB Region 292 466 . . . Note=Fructose-2%2C6-bisphosphatase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06137 UniProtKB Active site 173 173 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +Q06137 UniProtKB Binding site 237 237 . . . Note=Fructose 6-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +Q06137 UniProtKB Binding site 298 298 . . . Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +Q06137 UniProtKB Binding site 433 433 . . . Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +Q06137 UniProtKB Binding site 464 464 . . . Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07953 +Q06137 UniProtKB Site 298 298 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +Q06137 UniProtKB Site 459 459 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +Q06137 UniProtKB Modified residue 6 6 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q7LIF2 1 110 +Q7LIF2 UniProtKB Chain 1 110 . . . ID=PRO_0000299642;Note=Uncharacterized protein YLR365W +##sequence-region O13545 1 129 +O13545 UniProtKB Chain 1 129 . . . ID=PRO_0000299644;Note=Putative uncharacterized protein YLR374C +O13545 UniProtKB Transmembrane 33 50 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGT1 1 49 +Q8TGT1 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q8TGT1 UniProtKB Chain 23 49 . . . ID=PRO_0000247217;Note=Uncharacterized protein YLR406C-A +##sequence-region Q06204 1 433 +Q06204 UniProtKB Chain 1 433 . . . ID=PRO_0000268190;Note=Putative hexokinase YLR446W +Q06204 UniProtKB Domain 1 424 . . . Note=Hexokinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084 +Q06204 UniProtKB Region 51 194 . . . Note=Hexokinase small subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084 +Q06204 UniProtKB Region 132 154 . . . Note=Glucose-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06204 UniProtKB Region 195 413 . . . Note=Hexokinase large subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084 +Q06204 UniProtKB Sequence conflict 52 52 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region O13557 1 183 +O13557 UniProtKB Chain 1 183 . . . ID=PRO_0000299653;Note=Putative uncharacterized protein YLR463C +##sequence-region P0CY00 1 160 +P0CY00 UniProtKB Chain 1 160 . . . ID=PRO_0000410456;Note=UPF0479 membrane protein YLL066W-A +P0CY00 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CY00 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CY00 UniProtKB Compositional bias 103 106 . . . Note=Poly-Ser +##sequence-region P0CL39 1 160 +P0CL39 UniProtKB Chain 1 160 . . . ID=PRO_0000406013;Note=Putative UPF0479 protein YLR467C-A +P0CL39 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL39 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL39 UniProtKB Compositional bias 103 106 . . . Note=Poly-Ser +##sequence-region Q8TGS9 1 76 +Q8TGS9 UniProtKB Chain 1 76 . . . ID=PRO_0000247784;Note=Uncharacterized protein YMR001C-A +##sequence-region Q6B0Y1 1 158 +Q6B0Y1 UniProtKB Chain 1 158 . . . ID=PRO_0000299665;Note=Putative uncharacterized protein YML009W-B +Q6B0Y1 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PXP7 1 132 +A0A023PXP7 UniProtKB Chain 1 132 . . . ID=PRO_0000431060;Note=Putative uncharacterized protein YML034C-A +##sequence-region Q6B0Y7 1 121 +Q6B0Y7 UniProtKB Chain 1 121 . . . ID=PRO_0000299668;Note=Putative uncharacterized protein YMR075C-A +Q6B0Y7 UniProtKB Compositional bias 70 75 . . . Note=Poly-Leu +Q6B0Y7 UniProtKB Compositional bias 79 88 . . . Note=Poly-Leu +##sequence-region Q8TGT0 1 57 +Q8TGT0 UniProtKB Chain 1 57 . . . ID=PRO_0000247781;Note=Uncharacterized protein YML100W-A +##sequence-region Q04214 1 1755 +Q04214 UniProtKB Chain 1 1755 . . . ID=PRO_0000199567;Note=Transposon Ty1-MR1 Gag-Pol polyprotein +Q04214 UniProtKB Chain 1 401 . . . ID=PRO_0000279127;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04214 UniProtKB Chain 402 582 . . . ID=PRO_0000279128;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04214 UniProtKB Chain 583 1217 . . . ID=PRO_0000279129;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04214 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279130;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04214 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04214 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +Q04214 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +Q04214 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04214 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q04214 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04214 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q04214 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04214 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04214 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04214 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04214 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04214 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04214 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04214 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04214 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04214 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04214 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q6B0R2 1 128 +Q6B0R2 UniProtKB Chain 1 128 . . . ID=PRO_0000299672;Note=Putative uncharacterized protein YMR193C-A +Q6B0R2 UniProtKB Transmembrane 45 65 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q6B0R2 UniProtKB Transmembrane 95 115 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04304 1 227 +Q04304 UniProtKB Chain 1 227 . . . ID=PRO_0000203286;Note=UPF0659 protein YMR090W +##sequence-region Q3E841 1 98 +Q3E841 UniProtKB Chain 1 98 . . . ID=PRO_0000247803;Note=Uncharacterized protein YNR034W-A +Q3E841 UniProtKB Helix 7 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GRG +Q3E841 UniProtKB Beta strand 15 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GRG +Q3E841 UniProtKB Beta strand 26 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GRG +Q3E841 UniProtKB Helix 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GRG +Q3E841 UniProtKB Helix 41 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GRG +Q3E841 UniProtKB Beta strand 53 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GRG +Q3E841 UniProtKB Beta strand 66 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GRG +Q3E841 UniProtKB Beta strand 75 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GRG +##sequence-region P53837 1 131 +P53837 UniProtKB Chain 1 131 . . . ID=PRO_0000203379;Note=Putative uncharacterized protein YNL276C +##sequence-region P53729 1 429 +P53729 UniProtKB Chain 1 429 . . . ID=PRO_0000203476;Note=Uncharacterized protein YNR029C +P53729 UniProtKB Domain 362 428 . . . Note=CobW C-terminal +P53729 UniProtKB Nucleotide binding 78 85 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53729 UniProtKB Nucleotide binding 139 143 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53729 UniProtKB Nucleotide binding 244 247 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53751 1 1116 +P53751 UniProtKB Chain 1 1116 . . . ID=PRO_0000203483;Note=Uncharacterized membrane glycoprotein YNR065C +P53751 UniProtKB Transmembrane 934 957 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53751 UniProtKB Repeat 21 32 . . . Note=BNR 1 +P53751 UniProtKB Repeat 67 78 . . . Note=BNR 2 +P53751 UniProtKB Repeat 307 318 . . . Note=BNR 3 +P53751 UniProtKB Repeat 404 415 . . . Note=BNR 4 +P53751 UniProtKB Repeat 607 618 . . . Note=BNR 5 +P53751 UniProtKB Repeat 686 697 . . . Note=BNR 6 +P53751 UniProtKB Repeat 727 738 . . . Note=BNR 7 +P53751 UniProtKB Glycosylation 35 35 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53751 UniProtKB Glycosylation 336 336 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53751 UniProtKB Glycosylation 553 553 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53751 UniProtKB Glycosylation 846 846 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53751 UniProtKB Glycosylation 985 985 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53754 1 272 +P53754 UniProtKB Chain 1 272 . . . ID=PRO_0000203485;Note=Uncharacterized protein YNR068C +##sequence-region P53757 1 342 +P53757 UniProtKB Chain 1 342 . . . ID=PRO_0000197449;Note=Uncharacterized isomerase YNR071C +P53757 UniProtKB Active site 176 176 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10126 +P53757 UniProtKB Binding site 69 69 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53757 UniProtKB Binding site 240 240 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53757 UniProtKB Beta strand 13 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Turn 18 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 21 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 31 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Helix 49 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 68 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Helix 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 74 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 80 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Helix 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 111 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 117 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 128 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 136 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Turn 150 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 154 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Turn 181 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 193 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 201 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Turn 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 212 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 240 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Turn 246 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 253 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Turn 257 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 263 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Turn 271 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 276 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 304 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Helix 314 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Helix 318 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Helix 322 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 325 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +P53757 UniProtKB Beta strand 332 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGA +##sequence-region P53977 1 112 +P53977 UniProtKB Chain 1 112 . . . ID=PRO_0000203463;Note=Putative uncharacterized protein YNL017C +##sequence-region P53962 1 389 +P53962 UniProtKB Chain 1 389 . . . ID=PRO_0000051485;Note=Uncharacterized WD repeat-containing protein YNL035C +P53962 UniProtKB Repeat 11 53 . . . Note=WD 1 +P53962 UniProtKB Repeat 146 186 . . . Note=WD 2 +P53962 UniProtKB Repeat 289 330 . . . Note=WD 3 +P53962 UniProtKB Modified residue 351 351 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P0CL30 1 191 +P0CL30 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL30 UniProtKB Chain 18 191 . . . ID=PRO_0000406007;Note=Putative uncharacterized protein YNL339W-A +P0CL30 UniProtKB Transmembrane 168 188 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL30 UniProtKB Compositional bias 13 159 . . . Note=Gly/Ser-rich +##sequence-region P53921 1 115 +P53921 UniProtKB Natural variant 11 11 . . . Note=In strain: V1-09 and YJM339. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53921 UniProtKB Natural variant 31 31 . . . Note=In strain: YJM269%2C YJM270%2C YJM326 and YJM1129. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +##sequence-region Q08207 1 100 +Q08207 UniProtKB Chain 1 100 . . . ID=PRO_0000299688;Note=Putative uncharacterized protein YOL035C +Q08207 UniProtKB Transmembrane 9 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08207 UniProtKB Transmembrane 41 61 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08207 UniProtKB Transmembrane 72 92 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08439 1 144 +Q08439 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08439 UniProtKB Chain 23 144 . . . ID=PRO_0000299708;Note=Putative uncharacterized protein YOR055W +##sequence-region Q08240 1 163 +Q08240 UniProtKB Chain 1 163 . . . ID=PRO_0000262743;Note=Putative uncharacterized membrane protein YOL099C +Q08240 UniProtKB Topological domain 1 33 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q08240 UniProtKB Transmembrane 34 54 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08240 UniProtKB Topological domain 55 117 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q08240 UniProtKB Transmembrane 118 138 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08240 UniProtKB Topological domain 139 163 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +##sequence-region Q12322 1 202 +Q12322 UniProtKB Chain 1 202 . . . ID=PRO_0000203489;Note=Putative uncharacterized protein YOL114C +##sequence-region P0CX59 1 440 +P0CX59 UniProtKB Chain 1 440 . . . ID=PRO_0000279166;Note=Transposon Ty1-OR Gag polyprotein +P0CX59 UniProtKB Chain 1 401 . . . ID=PRO_0000279167;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX59 UniProtKB Peptide 402 440 . . . ID=PRO_0000279168;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX59 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX59 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0CX59 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX59 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region Q08272 1 129 +Q08272 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08272 UniProtKB Chain 25 129 . . . ID=PRO_0000299696;Note=Putative uncharacterized protein YOL134C +Q08272 UniProtKB Transmembrane 38 58 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08272 UniProtKB Transmembrane 95 115 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08272 UniProtKB Compositional bias 61 66 . . . Note=Poly-Ser +##sequence-region Q03080 1 316 +Q03080 UniProtKB Chain 1 316 . . . ID=PRO_0000238637;Note=Uncharacterized protein YPL039W +##sequence-region P0C5E1 1 128 +P0C5E1 UniProtKB Chain 1 128 . . . ID=PRO_0000302032;Note=Putative uncharacterized protein YPR059C +##sequence-region Q02749 1 293 +Q02749 UniProtKB Chain 1 293 . . . ID=PRO_0000238642;Note=Uncharacterized protein YPL068C +##sequence-region Q06813 1 372 +Q06813 UniProtKB Chain 1 372 . . . ID=PRO_0000255980;Note=Uncharacterized protein YPR078C +##sequence-region Q06839 1 1073 +Q06839 UniProtKB Chain 1 1073 . . . ID=PRO_0000257826;Note=PX domain-containing protein YPR097W +Q06839 UniProtKB Domain 273 506 . . . Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147 +Q06839 UniProtKB Modified residue 310 310 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06839 UniProtKB Modified residue 451 451 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06839 UniProtKB Sequence conflict 848 848 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0C2I9 1 1755 +P0C2I9 UniProtKB Chain 1 1755 . . . ID=PRO_0000279174;Note=Transposon Ty1-PR1 Gag-Pol polyprotein +P0C2I9 UniProtKB Chain 1 401 . . . ID=PRO_0000279175;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I9 UniProtKB Chain 402 582 . . . ID=PRO_0000279176;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I9 UniProtKB Chain 583 1217 . . . ID=PRO_0000279177;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I9 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279178;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I9 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I9 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +P0C2I9 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +P0C2I9 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I9 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +P0C2I9 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I9 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +P0C2I9 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I9 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I9 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I9 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I9 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I9 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I9 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I9 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I9 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I9 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I9 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I9 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region P0C2J1 1 1755 +P0C2J1 UniProtKB Chain 1 1755 . . . ID=PRO_0000279184;Note=Transposon Ty1-PR3 Gag-Pol polyprotein +P0C2J1 UniProtKB Chain 1 401 . . . ID=PRO_0000279185;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J1 UniProtKB Chain 402 582 . . . ID=PRO_0000279186;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J1 UniProtKB Chain 583 1217 . . . ID=PRO_0000279187;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J1 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279188;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J1 UniProtKB Domain 660 829 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J1 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +P0C2J1 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +P0C2J1 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J1 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +P0C2J1 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J1 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0C2J1 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +P0C2J1 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J1 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J1 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J1 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J1 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J1 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J1 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J1 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J1 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J1 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J1 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J1 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region Q08922 1 127 +Q08922 UniProtKB Chain 1 127 . . . ID=PRO_0000299806;Note=Putative uncharacterized protein YPL182C +Q08922 UniProtKB Transmembrane 47 67 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08922 UniProtKB Transmembrane 84 104 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08922 UniProtKB Compositional bias 6 42 . . . Note=Ser-rich +##sequence-region Q08954 1 240 +Q08954 UniProtKB Chain 1 240 . . . ID=PRO_0000238659;Note=Smr domain-containing protein YPL199C +Q08954 UniProtKB Domain 97 173 . . . Note=Smr;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00321 +##sequence-region Q99401 1 129 +Q99401 UniProtKB Chain 1 129 . . . ID=PRO_0000299811;Note=Putative uncharacterized protein YPL238C +Q99401 UniProtKB Transmembrane 22 42 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99401 UniProtKB Transmembrane 55 75 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99401 UniProtKB Transmembrane 88 108 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99401 UniProtKB Compositional bias 35 42 . . . Note=Poly-Phe +Q99401 UniProtKB Compositional bias 70 75 . . . Note=Poly-Phe +Q99401 UniProtKB Compositional bias 104 108 . . . Note=Poly-Phe +##sequence-region Q12523 1 523 +Q12523 UniProtKB Chain 1 523 . . . ID=PRO_0000242490;Note=WD repeat-containing protein YPL247C +Q12523 UniProtKB Repeat 173 213 . . . Note=WD 1 +Q12523 UniProtKB Repeat 241 281 . . . Note=WD 2 +Q12523 UniProtKB Repeat 285 325 . . . Note=WD 3 +Q12523 UniProtKB Repeat 392 432 . . . Note=WD 4 +Q12523 UniProtKB Modified residue 47 47 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12523 UniProtKB Modified residue 65 65 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region Q08980 1 353 +Q08980 UniProtKB Chain 1 353 . . . ID=PRO_0000252279;Note=Probable transport protein YPL264C +Q08980 UniProtKB Topological domain 1 16 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Transmembrane 17 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Topological domain 38 51 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Transmembrane 52 69 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Topological domain 70 94 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Transmembrane 95 115 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Topological domain 116 116 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Transmembrane 117 137 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Topological domain 138 144 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Transmembrane 145 165 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Topological domain 166 188 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Transmembrane 189 209 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Topological domain 210 218 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Transmembrane 219 239 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Topological domain 240 254 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Transmembrane 255 275 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Topological domain 276 282 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Transmembrane 283 303 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Topological domain 304 304 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Transmembrane 305 325 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Topological domain 326 353 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08980 UniProtKB Domain 24 160 . . . Note=EamA 1 +Q08980 UniProtKB Domain 200 326 . . . Note=EamA 2 +##sequence-region Q08990 1 100 +Q08990 UniProtKB Chain 1 100 . . . ID=PRO_0000269761;Note=Putative uncharacterized protein YPL278C +##sequence-region A0A023PXI5 1 187 +A0A023PXI5 UniProtKB Chain 1 187 . . . ID=PRO_0000431064;Note=Putative uncharacterized protein YPR197C +##sequence-region P43587 1 155 +P43587 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P43587 UniProtKB Chain 2 155 . . . ID=PRO_0000202681;Note=Type 1 phosphatases regulator YPI1 +P43587 UniProtKB Motif 51 53 . . . Note=GLC7-binding +P43587 UniProtKB Compositional bias 93 103 . . . Note=Poly-Ser +P43587 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P43587 UniProtKB Modified residue 22 22 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P43587 UniProtKB Modified residue 133 133 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P43587 UniProtKB Mutagenesis 51 51 . . . Note=Prevents interaction with GLC7. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18172024;Dbxref=PMID:18172024 +P43587 UniProtKB Mutagenesis 53 53 . . . Note=Prevents interaction with GLC7 and reduces nuclear levels of GLC7 and SDS22. W->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14506263,ECO:0000269|PubMed:18172024;Dbxref=PMID:14506263,PMID:18172024 +##sequence-region P46951 1 817 +P46951 UniProtKB Chain 1 817 . . . ID=PRO_0000202843;Note=Cargo-transport protein YPP1 +P46951 UniProtKB Helix 17 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 39 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 63 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Turn 85 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 90 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 114 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 137 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 161 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 185 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 203 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 217 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 239 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 264 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 291 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 306 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 326 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 361 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 377 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Turn 382 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 387 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 414 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 418 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 429 445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 446 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 450 454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 457 467 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 485 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 507 516 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Turn 517 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 526 536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Beta strand 538 540 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 543 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 569 588 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 590 595 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 598 607 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 614 616 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Beta strand 619 622 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 626 643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Beta strand 644 646 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 649 659 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Beta strand 663 665 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 668 679 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 686 697 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 702 712 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 747 767 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 769 772 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 775 784 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 791 804 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +P46951 UniProtKB Helix 812 815 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5C +##sequence-region P36019 1 220 +P36019 UniProtKB Chain 1 220 . . . ID=PRO_0000121327;Note=GTP-binding protein YPT53 +P36019 UniProtKB Nucleotide binding 19 26 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36019 UniProtKB Nucleotide binding 67 71 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36019 UniProtKB Nucleotide binding 125 128 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36019 UniProtKB Modified residue 220 220 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36019 UniProtKB Lipidation 218 218 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36019 UniProtKB Lipidation 220 220 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P0CX57 1 440 +P0CX57 UniProtKB Chain 1 440 . . . ID=PRO_0000278982;Note=Transposon Ty1-A Gag polyprotein +P0CX57 UniProtKB Chain 1 401 . . . ID=PRO_0000278983;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX57 UniProtKB Peptide 402 440 . . . ID=PRO_0000278984;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX57 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX57 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX57 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region P39557 1 106 +P39557 UniProtKB Chain 1 106 . . . ID=PRO_0000202428;Note=Putative uncharacterized membrane protein YAR047C +P39557 UniProtKB Topological domain 1 6 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39557 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39557 UniProtKB Topological domain 28 32 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39557 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39557 UniProtKB Topological domain 54 73 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39557 UniProtKB Transmembrane 74 94 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39557 UniProtKB Topological domain 95 106 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38749 1 330 +P38749 UniProtKB Chain 1 330 . . . ID=PRO_0000076523;Note=AP-1-like transcription factor YAP3 +P38749 UniProtKB Domain 144 207 . . . Note=bZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P38749 UniProtKB Region 147 168 . . . Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P38749 UniProtKB Region 172 207 . . . Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P38749 UniProtKB Compositional bias 107 112 . . . Note=Poly-Asn +P38749 UniProtKB Modified residue 135 135 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q03935 1 383 +Q03935 UniProtKB Chain 1 383 . . . ID=PRO_0000076526;Note=AP-1-like transcription factor YAP6 +Q03935 UniProtKB Domain 221 284 . . . Note=bZIP +Q03935 UniProtKB Region 223 247 . . . Note=Basic motif;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03935 UniProtKB Region 249 277 . . . Note=Leucine-zipper;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03935 UniProtKB Compositional bias 263 333 . . . Note=Asn-rich +##sequence-region Q8TGQ6 1 49 +Q8TGQ6 UniProtKB Chain 1 49 . . . ID=PRO_0000299792;Note=Putative uncharacterized protein YBL006W-A +##sequence-region O43137 1 85 +O43137 UniProtKB Chain 1 85 . . . ID=PRO_0000248436;Note=Uncharacterized protein YBR085C-A +O43137 UniProtKB Modified residue 22 22 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P89495 1 111 +P89495 UniProtKB Chain 1 111 . . . ID=PRO_0000299790;Note=Putative uncharacterized protein YBL109W +P89495 UniProtKB Compositional bias 63 99 . . . Note=His-rich +##sequence-region Q12217 1 440 +Q12217 UniProtKB Chain 1 440 . . . ID=PRO_0000278998;Note=Transposon Ty1-BR Gag polyprotein +Q12217 UniProtKB Chain 1 401 . . . ID=PRO_0000278999;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12217 UniProtKB Peptide 402 440 . . . ID=PRO_0000279000;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12217 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12217 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q12217 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12217 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region Q12193 1 1756 +Q12193 UniProtKB Chain 1 1756 . . . ID=PRO_0000278993;Note=Transposon Ty1-BR Gag-Pol polyprotein +Q12193 UniProtKB Chain 1 401 . . . ID=PRO_0000278994;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12193 UniProtKB Chain 402 582 . . . ID=PRO_0000278995;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12193 UniProtKB Chain 583 1218 . . . ID=PRO_0000278996;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12193 UniProtKB Chain 1219 1756 . . . ID=PRO_0000278997;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12193 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12193 UniProtKB Domain 1339 1477 . . . Note=Reverse transcriptase Ty1/copia-type +Q12193 UniProtKB Domain 1611 1753 . . . Note=RNase H Ty1/copia-type +Q12193 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12193 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q12193 UniProtKB Motif 1179 1213 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12193 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q12193 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q12193 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12193 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12193 UniProtKB Metal binding 1347 1347 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12193 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12193 UniProtKB Metal binding 1429 1429 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12193 UniProtKB Metal binding 1611 1611 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12193 UniProtKB Metal binding 1653 1653 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12193 UniProtKB Metal binding 1686 1686 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12193 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12193 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12193 UniProtKB Site 1218 1219 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12193 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region Q3E762 1 66 +Q3E762 UniProtKB Chain 1 66 . . . ID=PRO_0000248443;Note=Putative uncharacterized protein YBR230W-A +##sequence-region P0C5K9 1 27 +P0C5K9 UniProtKB Chain 1 27 . . . ID=PRO_0000309007;Note=Uncharacterized protein YBL039C-A +##sequence-region P38309 1 107 +P38309 UniProtKB Chain 1 107 . . . ID=PRO_0000202510;Note=Putative uncharacterized protein YBR206W +##sequence-region P38318 1 560 +P38318 UniProtKB Chain 1 560 . . . ID=PRO_0000202514;Note=Uncharacterized membrane protein YBR220C +P38318 UniProtKB Topological domain 1 17 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Transmembrane 18 38 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Topological domain 39 54 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Transmembrane 55 75 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Topological domain 76 88 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Transmembrane 89 109 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Topological domain 110 139 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Transmembrane 140 160 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Topological domain 161 172 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Topological domain 194 214 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Transmembrane 215 235 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Topological domain 236 329 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Transmembrane 330 350 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Topological domain 351 374 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Transmembrane 375 395 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Topological domain 396 421 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Transmembrane 422 442 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Topological domain 443 521 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Transmembrane 522 542 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38318 UniProtKB Topological domain 543 560 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38355 1 427 +P38355 UniProtKB Chain 1 427 . . . ID=PRO_0000123805;Note=Uncharacterized transporter YBR287W +P38355 UniProtKB Transmembrane 10 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38355 UniProtKB Transmembrane 43 63 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38355 UniProtKB Transmembrane 71 91 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38355 UniProtKB Transmembrane 253 273 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38355 UniProtKB Transmembrane 288 308 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38355 UniProtKB Transmembrane 327 347 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38355 UniProtKB Transmembrane 358 378 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38355 UniProtKB Transmembrane 397 417 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38355 UniProtKB Modified residue 199 199 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38355 UniProtKB Modified residue 234 234 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38355 UniProtKB Sequence conflict 425 425 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38142 1 488 +P38142 UniProtKB Chain 1 488 . . . ID=PRO_0000050463;Note=Probable metabolite transport protein YBR241C +P38142 UniProtKB Topological domain 1 18 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Transmembrane 19 39 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Topological domain 40 87 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Transmembrane 88 108 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Topological domain 109 121 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Transmembrane 122 142 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Topological domain 143 146 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Transmembrane 147 167 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Topological domain 168 178 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Transmembrane 179 198 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Topological domain 199 204 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Transmembrane 205 225 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Topological domain 226 299 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Transmembrane 300 320 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Topological domain 321 322 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Transmembrane 323 337 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Topological domain 338 344 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Transmembrane 345 364 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Topological domain 365 390 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Transmembrane 391 411 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Topological domain 412 419 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Transmembrane 420 442 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Topological domain 443 446 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Transmembrane 447 463 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Topological domain 464 488 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Glycosylation 63 63 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38142 UniProtKB Sequence conflict 438 438 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38338 1 688 +P38338 UniProtKB Chain 1 688 . . . ID=PRO_0000202526;Note=Uncharacterized protein YBR259W +##sequence-region P38083 1 404 +P38083 UniProtKB Chain 1 404 . . . ID=PRO_0000202476;Note=Uncharacterized protein YBR063C +P38083 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38083 UniProtKB Transmembrane 92 112 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38253 1 122 +P38253 UniProtKB Chain 1 122 . . . ID=PRO_0000202481;Note=Uncharacterized protein YBR090C +P38253 UniProtKB Transmembrane 9 25 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38253 UniProtKB Sequence conflict 101 101 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38253 UniProtKB Sequence conflict 101 101 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P87012 1 153 +P87012 UniProtKB Chain 1 153 . . . ID=PRO_0000248411;Note=Putative pelota-like protein YCL001W-A +##sequence-region Q8TGQ0 1 78 +Q8TGQ0 UniProtKB Chain 1 78 . . . ID=PRO_0000299839;Note=Putative uncharacterized protein YCR081C-A +Q8TGQ0 UniProtKB Transmembrane 25 45 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q8TGQ0 UniProtKB Transmembrane 50 70 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q96VG5 1 65 +Q96VG5 UniProtKB Chain 1 65 . . . ID=PRO_0000299841;Note=Putative uncharacterized protein YCR102W-A +##sequence-region Q8J0M4 1 134 +Q8J0M4 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q8J0M4 UniProtKB Chain 24 134 . . . ID=PRO_0000045281;Note=UPF0357 protein YCL012C +Q8J0M4 UniProtKB Modified residue 71 71 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q8J0M4 UniProtKB Modified residue 74 74 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q8J0M4 UniProtKB Cross-link 86 86 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P25562 1 171 +P25562 UniProtKB Chain 1 171 . . . ID=PRO_0000202541;Note=Putative uncharacterized protein YCL022C +##sequence-region P25593 1 260 +P25593 UniProtKB Chain 1 260 . . . ID=PRO_0000202556;Note=Putative uncharacterized protein YCL068C +P25593 UniProtKB Sequence conflict 76 76 . . . Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25614 1 215 +P25614 UniProtKB Chain 1 215 . . . ID=PRO_0000202561;Note=Putative uncharacterized protein YCR013C +##sequence-region Q12235 1 531 +Q12235 UniProtKB Chain 1 531 . . . ID=PRO_0000247151;Note=High affinity cysteine transporter +Q12235 UniProtKB Topological domain 1 54 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Transmembrane 55 75 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Topological domain 76 97 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Transmembrane 98 118 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Topological domain 119 120 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Transmembrane 121 141 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Topological domain 142 154 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Transmembrane 155 175 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Topological domain 176 186 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Transmembrane 187 207 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Topological domain 208 218 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Transmembrane 219 239 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Topological domain 240 285 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Transmembrane 286 306 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Topological domain 307 324 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Transmembrane 325 345 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Topological domain 346 352 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Transmembrane 353 373 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Topological domain 374 378 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Transmembrane 379 399 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Topological domain 400 413 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Transmembrane 414 436 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Topological domain 437 447 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Transmembrane 448 468 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Topological domain 469 531 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Coiled coil 469 498 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12235 UniProtKB Modified residue 500 500 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12235 UniProtKB Modified residue 501 501 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12235 UniProtKB Glycosylation 146 146 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P25631 1 222 +P25631 UniProtKB Chain 1 222 . . . ID=PRO_0000067244;Note=Ankyrin repeat-containing protein YCR051W +P25631 UniProtKB Repeat 1 29 . . . Note=ANK 1 +P25631 UniProtKB Repeat 36 66 . . . Note=ANK 2 +P25631 UniProtKB Repeat 70 99 . . . Note=ANK 3 +##sequence-region P25607 1 182 +P25607 UniProtKB Chain 1 182 . . . ID=PRO_0000202584;Note=Uncharacterized protein YCR101C +P25607 UniProtKB Repeat 58 69 . . . Note=BNR 1 +P25607 UniProtKB Repeat 102 113 . . . Note=BNR 2 +##sequence-region Q12023 1 107 +Q12023 UniProtKB Chain 1 107 . . . ID=PRO_0000299843;Note=Putative uncharacterized protein YDL011C +Q12023 UniProtKB Transmembrane 20 40 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12023 UniProtKB Transmembrane 49 69 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12023 UniProtKB Transmembrane 86 106 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGP7 1 34 +Q8TGP7 UniProtKB Chain 1 34 . . . ID=PRO_0000299846;Note=Putative uncharacterized protein YDL025W-A +##sequence-region Q07790 1 131 +Q07790 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07790 UniProtKB Chain 20 131 . . . ID=PRO_0000299871;Note=Putative uncharacterized protein YDR053W +Q07790 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07790 UniProtKB Transmembrane 111 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07410 1 141 +Q07410 UniProtKB Chain 1 141 . . . ID=PRO_0000299852;Note=Putative uncharacterized protein YDL062W +##sequence-region Q07454 1 984 +Q07454 UniProtKB Chain 1 984 . . . ID=PRO_0000248460;Note=UPF0592 protein YDL073W +##sequence-region Q12103 1 647 +Q12103 UniProtKB Chain 1 647 . . . ID=PRO_0000240859;Note=Putative lipase YDL109C +Q12103 UniProtKB Active site 274 274 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10037 +##sequence-region Q03855 1 1755 +Q03855 UniProtKB Chain 1 1755 . . . ID=PRO_0000279001;Note=Transposon Ty1-DR1 Gag-Pol polyprotein +Q03855 UniProtKB Chain 1 401 . . . ID=PRO_0000279002;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03855 UniProtKB Chain 402 582 . . . ID=PRO_0000279003;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03855 UniProtKB Chain 583 1217 . . . ID=PRO_0000279004;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03855 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279005;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03855 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03855 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +Q03855 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +Q03855 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03855 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q03855 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03855 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q03855 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q03855 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03855 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03855 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03855 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03855 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03855 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03855 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03855 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03855 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03855 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03855 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03855 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region P0C5L7 1 38 +P0C5L7 UniProtKB Chain 1 38 . . . ID=PRO_0000309015;Note=Uncharacterized protein YDR118W-A +##sequence-region Q12407 1 687 +Q12407 UniProtKB Chain 1 687 . . . ID=PRO_0000242140;Note=Putative metabolite transport protein YDL199C +Q12407 UniProtKB Topological domain 1 122 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Transmembrane 123 143 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Topological domain 144 164 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Transmembrane 165 185 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Topological domain 186 192 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Transmembrane 193 213 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Topological domain 214 216 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Transmembrane 217 237 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Topological domain 238 251 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Transmembrane 252 272 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Topological domain 273 283 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Transmembrane 284 304 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Topological domain 305 410 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Transmembrane 411 431 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Topological domain 432 439 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Transmembrane 440 460 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Topological domain 461 469 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Transmembrane 470 490 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Topological domain 491 500 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Transmembrane 501 521 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Topological domain 522 533 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Transmembrane 534 554 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Topological domain 555 687 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12407 UniProtKB Modified residue 90 90 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q12240 1 137 +Q12240 UniProtKB Chain 1 137 . . . ID=PRO_0000299876;Note=Uncharacterized protein YDR215C +Q12240 UniProtKB Transmembrane 75 91 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07649 1 183 +Q07649 UniProtKB Chain 1 183 . . . ID=PRO_0000299865;Note=Putative uncharacterized protein YDL221W +##sequence-region Q03494 1 1770 +Q03494 UniProtKB Chain 1 1770 . . . ID=PRO_0000279292;Note=Transposon Ty2-DR2 Gag-Pol polyprotein +Q03494 UniProtKB Chain 1 397 . . . ID=PRO_0000279293;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03494 UniProtKB Chain 398 578 . . . ID=PRO_0000279294;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03494 UniProtKB Chain 579 1232 . . . ID=PRO_0000279295;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03494 UniProtKB Chain 1233 1770 . . . ID=PRO_0000279296;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03494 UniProtKB Domain 656 831 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03494 UniProtKB Domain 1353 1491 . . . Note=Reverse transcriptase Ty1/copia-type +Q03494 UniProtKB Domain 1625 1767 . . . Note=RNase H Ty1/copia-type +Q03494 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03494 UniProtKB Region 579 636 . . . Note=Integrase-type zinc finger-like +Q03494 UniProtKB Motif 1193 1227 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03494 UniProtKB Active site 457 457 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03494 UniProtKB Metal binding 667 667 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03494 UniProtKB Metal binding 732 732 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03494 UniProtKB Metal binding 1361 1361 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03494 UniProtKB Metal binding 1442 1442 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03494 UniProtKB Metal binding 1443 1443 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03494 UniProtKB Metal binding 1625 1625 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03494 UniProtKB Metal binding 1667 1667 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03494 UniProtKB Metal binding 1700 1700 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03494 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03494 UniProtKB Site 578 579 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03494 UniProtKB Site 1232 1233 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q07746 1 117 +Q07746 UniProtKB Chain 1 117 . . . ID=PRO_0000299867;Note=Uncharacterized protein YDL242W +##sequence-region P87281 1 107 +P87281 UniProtKB Chain 1 107 . . . ID=PRO_0000299879;Note=Putative uncharacterized protein YDR269C +P87281 UniProtKB Transmembrane 16 36 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P87281 UniProtKB Transmembrane 47 67 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P87281 UniProtKB Transmembrane 85 105 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P87280 1 109 +P87280 UniProtKB Chain 1 109 . . . ID=PRO_0000299882;Note=Putative uncharacterized protein YDR290W +P87280 UniProtKB Transmembrane 63 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q05503 1 100 +Q05503 UniProtKB Chain 1 100 . . . ID=PRO_0000299884;Note=Putative uncharacterized protein YDR340W +Q05503 UniProtKB Transmembrane 28 45 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03418 1 163 +Q03418 UniProtKB Chain 1 163 . . . ID=PRO_0000299899;Note=Putative uncharacterized protein YDR491C +Q03418 UniProtKB Transmembrane 11 31 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PXB9 1 121 +A0A023PXB9 UniProtKB Chain 1 121 . . . ID=PRO_0000430988;Note=Putative uncharacterized membrane protein YDR199W +A0A023PXB9 UniProtKB Transmembrane 26 46 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXB9 UniProtKB Transmembrane 57 77 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXB9 UniProtKB Transmembrane 90 110 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0C5M6 1 65 +P0C5M6 UniProtKB Signal peptide 1 16 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C5M6 UniProtKB Chain 17 65 . . . ID=PRO_0000309024;Note=Putative uncharacterized protein YEL020C-B +##sequence-region Q8TGP4 1 53 +Q8TGP4 UniProtKB Chain 1 53 . . . ID=PRO_0000299908;Note=Putative uncharacterized protein YEL032C-A +##sequence-region A0A023PYE4 1 107 +A0A023PYE4 UniProtKB Chain 1 107 . . . ID=PRO_0000430993;Note=Putative uncharacterized membrane protein YER067C-A +A0A023PYE4 UniProtKB Transmembrane 37 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P89888 1 203 +P89888 UniProtKB Chain 1 203 . . . ID=PRO_0000299657;Note=Putative uncharacterized protein YEL075W-A +##sequence-region Q3E7A2 1 54 +Q3E7A2 UniProtKB Chain 1 54 . . . ID=PRO_0000245371;Note=Uncharacterized protein YER078W-A +##sequence-region A0A023PZG0 1 170 +A0A023PZG0 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZG0 UniProtKB Chain 22 170 . . . ID=PRO_0000430996;Note=Putative uncharacterized membrane protein YER084W-A;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZG0 UniProtKB Transmembrane 36 56 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CX66 1 440 +P0CX66 UniProtKB Chain 1 440 . . . ID=PRO_0000409779;Note=Transposon Ty1-ER2 Gag polyprotein +P0CX66 UniProtKB Chain 1 401 . . . ID=PRO_0000409780;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX66 UniProtKB Peptide 402 440 . . . ID=PRO_0000409781;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX66 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX66 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0CX66 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX66 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region A0A023PYF7 1 126 +A0A023PYF7 UniProtKB Chain 1 126 . . . ID=PRO_0000431006;Note=Putative uncharacterized protein YER172C-A +##sequence-region P0CX94 1 160 +P0CX94 UniProtKB Chain 1 160 . . . ID=PRO_0000277622;Note=UPF0479 membrane protein YER190C-B +P0CX94 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX94 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX94 UniProtKB Compositional bias 103 106 . . . Note=Poly-Ser +##sequence-region A0A023PXD3 1 107 +A0A023PXD3 UniProtKB Chain 1 107 . . . ID=PRO_0000431009;Note=Putative uncharacterized protein YER088C-A +##sequence-region P40004 1 342 +P40004 UniProtKB Chain 1 342 . . . ID=PRO_0000213361;Note=UDP-N-acetylglucosamine transporter YEA4 +P40004 UniProtKB Topological domain 1 6 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40004 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40004 UniProtKB Topological domain 28 35 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40004 UniProtKB Transmembrane 36 56 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40004 UniProtKB Topological domain 57 61 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40004 UniProtKB Transmembrane 62 82 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40004 UniProtKB Topological domain 83 96 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40004 UniProtKB Transmembrane 97 117 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40004 UniProtKB Topological domain 118 123 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40004 UniProtKB Transmembrane 124 144 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40004 UniProtKB Topological domain 145 168 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40004 UniProtKB Transmembrane 169 189 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40004 UniProtKB Topological domain 190 253 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40004 UniProtKB Transmembrane 254 274 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40004 UniProtKB Topological domain 275 307 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40004 UniProtKB Transmembrane 308 328 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40004 UniProtKB Topological domain 329 342 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39999 1 101 +P39999 UniProtKB Chain 1 101 . . . ID=PRO_0000202614;Note=Uncharacterized protein YEL014C +##sequence-region P39991 1 1188 +P39991 UniProtKB Chain 1 1188 . . . ID=PRO_0000202609;Note=Uncharacterized protein YEL025C +P39991 UniProtKB Transmembrane 73 93 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39991 UniProtKB Transmembrane 878 898 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39991 UniProtKB Transmembrane 1089 1109 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39989 1 153 +P39989 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39989 UniProtKB Chain 22 153 . . . ID=PRO_0000014314;Note=Uncharacterized protein YEL028W +##sequence-region P39977 1 110 +P39977 UniProtKB Chain 1 110 . . . ID=PRO_0000202601;Note=Uncharacterized protein YEL068C +##sequence-region P39971 1 216 +P39971 UniProtKB Chain 1 216 . . . ID=PRO_0000202597;Note=Uncharacterized protein YEL076C +##sequence-region P40028 1 759 +P40028 UniProtKB Chain 1 759 . . . ID=PRO_0000202629;Note=Holliday junction resolvase YEN1 +P40028 UniProtKB Modified residue 730 730 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40028 UniProtKB Modified residue 731 731 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40028 UniProtKB Sequence conflict 59 59 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40028 UniProtKB Sequence conflict 164 165 . . . Note=LL->FV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40028 UniProtKB Sequence conflict 346 346 . . . Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40076 1 114 +P40076 UniProtKB Chain 1 114 . . . ID=PRO_0000202646;Note=Uncharacterized protein YER121W +##sequence-region P0C5M9 1 85 +P0C5M9 UniProtKB Chain 1 85 . . . ID=PRO_0000309027;Note=Uncharacterized protein YFR009W-A +##sequence-region Q3E817 1 63 +Q3E817 UniProtKB Chain 1 63 . . . ID=PRO_0000245373;Note=Uncharacterized protein YFL041W-A +##sequence-region Q06676 1 274 +Q06676 UniProtKB Chain 1 274 . . . ID=PRO_0000252273;Note=FIT family protein YFT2 +Q06676 UniProtKB Topological domain 1 11 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06676 UniProtKB Transmembrane 12 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06676 UniProtKB Topological domain 33 60 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06676 UniProtKB Transmembrane 61 81 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06676 UniProtKB Topological domain 82 124 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06676 UniProtKB Transmembrane 125 145 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06676 UniProtKB Topological domain 146 170 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06676 UniProtKB Transmembrane 171 191 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06676 UniProtKB Topological domain 192 215 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06676 UniProtKB Transmembrane 216 236 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06676 UniProtKB Topological domain 237 247 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06676 UniProtKB Transmembrane 248 268 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06676 UniProtKB Topological domain 269 274 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12141 1 1755 +Q12141 UniProtKB Chain 1 1755 . . . ID=PRO_0000279053;Note=Transposon Ty1-GR1 Gag-Pol polyprotein +Q12141 UniProtKB Chain 1 401 . . . ID=PRO_0000279054;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12141 UniProtKB Chain 402 582 . . . ID=PRO_0000279055;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12141 UniProtKB Chain 583 1217 . . . ID=PRO_0000279056;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12141 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279057;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12141 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12141 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +Q12141 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +Q12141 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12141 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q12141 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12141 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q12141 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12141 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12141 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12141 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12141 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12141 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12141 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12141 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12141 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12141 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12141 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12141 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region Q3E772 1 92 +Q3E772 UniProtKB Chain 1 92 . . . ID=PRO_0000245386;Note=Uncharacterized protein YGR169C-A +Q3E772 UniProtKB Coiled coil 17 80 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53216 1 100 +P53216 UniProtKB Chain 1 100 . . . ID=PRO_0000202789;Note=Uncharacterized protein YGR025W +##sequence-region P53229 1 120 +P53229 UniProtKB Chain 1 120 . . . ID=PRO_0000202795;Note=Uncharacterized protein YGR045C +P53229 UniProtKB Transmembrane 63 83 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E740 1 77 +Q3E740 UniProtKB Chain 1 77 . . . ID=PRO_0000245376;Note=Uncharacterized protein YGL258W-A +Q3E740 UniProtKB Domain 1 77 . . . Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103 +##sequence-region P53263 1 149 +P53263 UniProtKB Chain 1 149 . . . ID=PRO_0000202812;Note=Putative uncharacterized protein YGR107W +##sequence-region P53272 1 402 +P53272 UniProtKB Chain 1 402 . . . ID=PRO_0000202818;Note=Uncharacterized protein YGR122W +##sequence-region P53274 1 230 +P53274 UniProtKB Chain 1 230 . . . ID=PRO_0000202820;Note=Uncharacterized protein YGR126W +P53274 UniProtKB Modified residue 106 106 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P53287 1 111 +P53287 UniProtKB Chain 1 111 . . . ID=PRO_0000202831;Note=Uncharacterized protein YGR151C +##sequence-region P32475 1 115 +P32475 UniProtKB Chain 1 115 . . . ID=PRO_0000202839;Note=Putative uncharacterized protein YGR176W +P32475 UniProtKB Sequence conflict 56 59 . . . Note=IRHD->NSPR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53308 1 114 +P53308 UniProtKB Chain 1 114 . . . ID=PRO_0000202850;Note=Putative uncharacterized protein YGR228W +P53308 UniProtKB Transmembrane 21 41 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53308 UniProtKB Transmembrane 65 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53308 UniProtKB Transmembrane 93 113 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53316 1 781 +P53316 UniProtKB Chain 1 781 . . . ID=PRO_0000082030;Note=Uncharacterized RNA-binding protein YGR250C +P53316 UniProtKB Domain 195 273 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P53316 UniProtKB Domain 295 418 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P53316 UniProtKB Domain 540 638 . . . Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P53316 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53316 UniProtKB Modified residue 433 433 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53316 UniProtKB Modified residue 435 435 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53316 UniProtKB Modified residue 482 482 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53316 UniProtKB Modified residue 485 485 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53316 UniProtKB Modified residue 486 486 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53316 UniProtKB Modified residue 501 501 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P53336 1 341 +P53336 UniProtKB Chain 1 341 . . . ID=PRO_0000202872;Note=Putative methyltransferase YGR283C +##sequence-region P53190 1 111 +P53190 UniProtKB Chain 1 111 . . . ID=PRO_0000202774;Note=Putative uncharacterized protein YGL024W +P53190 UniProtKB Transmembrane 22 42 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53190 UniProtKB Transmembrane 48 68 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53190 UniProtKB Transmembrane 75 95 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53175 1 101 +P53175 UniProtKB Chain 1 101 . . . ID=PRO_0000202768;Note=Putative uncharacterized protein YGL052W +##sequence-region P53160 1 108 +P53160 UniProtKB Chain 1 108 . . . ID=PRO_0000202761;Note=Putative uncharacterized protein YGL074C +P53160 UniProtKB Transmembrane 51 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53160 UniProtKB Transmembrane 86 106 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53122 1 345 +P53122 UniProtKB Chain 1 345 . . . ID=PRO_0000202739;Note=Uncharacterized protein YGL138C +##sequence-region P53110 1 370 +P53110 UniProtKB Chain 1 370 . . . ID=PRO_0000202732;Note=Uncharacterized protein YGL159W +P53110 UniProtKB Compositional bias 81 86 . . . Note=Poly-Asn +P53110 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P53097 1 103 +P53097 UniProtKB Chain 1 103 . . . ID=PRO_0000202723;Note=Uncharacterized protein YGL193C +##sequence-region P53074 1 147 +P53074 UniProtKB Chain 1 147 . . . ID=PRO_0000202712;Note=Uncharacterized protein YGL230C +P53074 UniProtKB Transmembrane 85 105 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07074 1 71 +Q07074 UniProtKB Chain 1 71 . . . ID=PRO_0000245393;Note=Uncharacterized protein YHR007C-A +Q07074 UniProtKB Transmembrane 21 43 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07074 UniProtKB Sequence conflict 24 26 . . . Note=LFL->FFF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region A0A023PXL1 1 197 +A0A023PXL1 UniProtKB Chain 1 197 . . . ID=PRO_0000431016;Note=Putative uncharacterized membrane protein YHL019W-A +A0A023PXL1 UniProtKB Transmembrane 150 172 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PYG5 1 108 +A0A023PYG5 UniProtKB Chain 1 108 . . . ID=PRO_0000431020;Note=Putative uncharacterized protein YHL046W-A +##sequence-region P0C5B8 1 160 +P0C5B8 UniProtKB Chain 1 160 . . . ID=PRO_0000299785;Note=Putative UPF0479 protein YHL050W-A +P0C5B8 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C5B8 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C5B8 UniProtKB Compositional bias 103 106 . . . Note=Poly-Ser +##sequence-region A0A023PXF2 1 106 +A0A023PXF2 UniProtKB Chain 1 106 . . . ID=PRO_0000431025;Note=Putative uncharacterized protein YHR071C-A +##sequence-region P0C2I4 1 478 +P0C2I4 UniProtKB Chain 1 478 . . . ID=PRO_0000279079;Note=Transposon Ty1-H Gag polyprotein +P0C2I4 UniProtKB Chain 1 439 . . . ID=PRO_0000279080;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I4 UniProtKB Peptide 440 478 . . . ID=PRO_0000279081;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I4 UniProtKB Region 337 439 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I4 UniProtKB Compositional bias 72 146 . . . Note=Pro-rich +P0C2I4 UniProtKB Site 439 440 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region A0A023PXM2 1 81 +A0A023PXM2 UniProtKB Chain 1 81 . . . ID=PRO_0000431026;Note=Putative uncharacterized protein YHR131W-A +##sequence-region P32792 1 385 +P32792 UniProtKB Chain 1 385 . . . ID=PRO_0000202888;Note=UPF0744 protein YSC83 +##sequence-region P38799 1 552 +P38799 UniProtKB Chain 1 552 . . . ID=PRO_0000202900;Note=Uncharacterized protein YHR078W +P38799 UniProtKB Transmembrane 127 147 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38799 UniProtKB Transmembrane 160 180 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38799 UniProtKB Transmembrane 393 413 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38799 UniProtKB Transmembrane 517 537 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38831 1 101 +P38831 UniProtKB Chain 1 101 . . . ID=PRO_0000202914;Note=Uncharacterized protein YHR125W +##sequence-region P38833 1 243 +P38833 UniProtKB Chain 1 243 . . . ID=PRO_0000202915;Note=Uncharacterized protein YHR127W +P38833 UniProtKB Modified residue 96 96 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region P38867 1 453 +P38867 UniProtKB Chain 1 453 . . . ID=PRO_0000202932;Note=Uncharacterized protein YHR177W +P38867 UniProtKB Compositional bias 256 259 . . . Note=Poly-Gln +P38867 UniProtKB Beta strand 7 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B +P38867 UniProtKB Helix 15 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B +P38867 UniProtKB Helix 39 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B +P38867 UniProtKB Beta strand 50 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B +P38867 UniProtKB Helix 56 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B +P38867 UniProtKB Beta strand 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B +P38867 UniProtKB Beta strand 79 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B +P38867 UniProtKB Beta strand 108 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B +P38867 UniProtKB Beta strand 112 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B +P38867 UniProtKB Beta strand 136 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B +P38867 UniProtKB Helix 147 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B +P38867 UniProtKB Helix 158 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B +P38867 UniProtKB Helix 162 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B +P38867 UniProtKB Helix 171 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8B +##sequence-region P38870 1 785 +P38870 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38870 UniProtKB Chain 2 785 . . . ID=PRO_0000202935;Note=Uncharacterized protein YHR182W +P38870 UniProtKB Domain 520 702 . . . Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172 +P38870 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region A0A023PZF9 1 107 +A0A023PZF9 UniProtKB Chain 1 107 . . . ID=PRO_0000431030;Note=Putative uncharacterized membrane protein YIR023C-A +A0A023PZF9 UniProtKB Transmembrane 13 33 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PZE9 1 123 +A0A023PZE9 UniProtKB Chain 1 123 . . . ID=PRO_0000431031;Note=Putative uncharacterized protein YIL029W-A +##sequence-region A0A023PYI5 1 133 +A0A023PYI5 UniProtKB Chain 1 133 . . . ID=PRO_0000431033;Note=Putative uncharacterized membrane protein YIR036W-A +A0A023PYI5 UniProtKB Transmembrane 91 113 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PXN3 1 127 +A0A023PXN3 UniProtKB Chain 1 127 . . . ID=PRO_0000431036;Note=Putative uncharacterized protein YIL068W-A +##sequence-region Q45U18 1 67 +Q45U18 UniProtKB Chain 1 67 . . . ID=PRO_0000245401;Note=Uncharacterized protein YIL134C-A +Q45U18 UniProtKB Transmembrane 13 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q45U18 UniProtKB Transmembrane 45 64 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40538 1 142 +P40538 UniProtKB Chain 1 142 . . . ID=PRO_0000202996;Note=Uncharacterized protein YIL029C +P40538 UniProtKB Transmembrane 3 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40538 UniProtKB Transmembrane 30 50 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40538 UniProtKB Transmembrane 91 111 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40434 1 1758 +P40434 UniProtKB Chain 1 1758 . . . ID=PRO_0000102207;Note=Y' element ATP-dependent helicase YIL177C +P40434 UniProtKB Domain 668 845 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P40434 UniProtKB Domain 900 1051 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P40434 UniProtKB Nucleotide binding 681 688 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +##sequence-region P0C5P1 1 38 +P0C5P1 UniProtKB Chain 1 38 . . . ID=PRO_0000309039;Note=Putative uncharacterized protein YJL127W-A +##sequence-region P47126 1 109 +P47126 UniProtKB Chain 1 109 . . . ID=PRO_0000203102;Note=Uncharacterized protein YJR079W +P47126 UniProtKB Compositional bias 16 20 . . . Note=Poly-Phe +##sequence-region P47028 1 122 +P47028 UniProtKB Chain 1 122 . . . ID=PRO_0000203048;Note=Putative uncharacterized protein YJL086C +P47028 UniProtKB Transmembrane 93 113 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P42947 1 387 +P42947 UniProtKB Chain 1 387 . . . ID=PRO_0000203046;Note=Uncharacterized UPF0442 protein YJL107C +##sequence-region P47003 1 119 +P47003 UniProtKB Chain 1 119 . . . ID=PRO_0000203029;Note=Putative uncharacterized protein YJL152W +P47003 UniProtKB Transmembrane 74 94 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P46994 1 122 +P46994 UniProtKB Chain 1 122 . . . ID=PRO_0000203026;Note=Putative uncharacterized protein YJL169W +##sequence-region P39542 1 402 +P39542 UniProtKB Chain 1 402 . . . ID=PRO_0000206786;Note=Uncharacterized transporter YJL193W +P39542 UniProtKB Topological domain 1 12 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39542 UniProtKB Transmembrane 13 33 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39542 UniProtKB Topological domain 34 50 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39542 UniProtKB Transmembrane 51 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39542 UniProtKB Topological domain 72 103 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39542 UniProtKB Transmembrane 104 124 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39542 UniProtKB Topological domain 125 134 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39542 UniProtKB Transmembrane 135 155 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39542 UniProtKB Topological domain 156 165 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39542 UniProtKB Transmembrane 166 186 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39542 UniProtKB Topological domain 187 206 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39542 UniProtKB Transmembrane 207 227 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39542 UniProtKB Topological domain 228 271 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39542 UniProtKB Transmembrane 272 292 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39542 UniProtKB Topological domain 293 353 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39542 UniProtKB Transmembrane 354 374 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39542 UniProtKB Topological domain 375 402 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40898 1 147 +P40898 UniProtKB Chain 1 147 . . . ID=PRO_0000203014;Note=Putative uncharacterized protein YJL211C +##sequence-region P47092 1 110 +P47092 UniProtKB Chain 1 110 . . . ID=PRO_0000203087;Note=Putative uncharacterized protein YJR020W +##sequence-region Q3E7A7 1 99 +Q3E7A7 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E7A7 UniProtKB Chain 20 99 . . . ID=PRO_0000245424;Note=Uncharacterized protein YKL018C-A +##sequence-region P36133 1 167 +P36133 UniProtKB Chain 1 167 . . . ID=PRO_0000203209;Note=Putative uncharacterized protein YKR040C +P36133 UniProtKB Compositional bias 144 167 . . . Note=Lys-rich (highly basic) +##sequence-region P36134 1 250 +P36134 UniProtKB Chain 1 250 . . . ID=PRO_0000203210;Note=Uncharacterized protein YKR041W +P36134 UniProtKB Cross-link 17 17 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region Q86ZR7 1 236 +Q86ZR7 UniProtKB Chain 1 236 . . . ID=PRO_0000203186;Note=Putative uncharacterized hydrolase YKL033W-A +##sequence-region P35736 1 922 +P35736 UniProtKB Chain 1 922 . . . ID=PRO_0000203180;Note=Uncharacterized protein YKL050C +##sequence-region P36083 1 450 +P36083 UniProtKB Chain 1 450 . . . ID=PRO_0000203170;Note=Uncharacterized protein YKL075C +##sequence-region P0CX72 1 440 +P0CX72 UniProtKB Chain 1 440 . . . ID=PRO_0000409794;Note=Transposon Ty1-LR2 Gag polyprotein +P0CX72 UniProtKB Chain 1 401 . . . ID=PRO_0000409795;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX72 UniProtKB Peptide 402 440 . . . ID=PRO_0000409796;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX72 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX72 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0CX72 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX72 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region P0CY04 1 43 +P0CY04 UniProtKB Chain 1 43 . . . ID=PRO_0000410460;Note=Uncharacterized protein YLR157C-C +##sequence-region P0C5P6 1 37 +P0C5P6 UniProtKB Chain 1 37 . . . ID=PRO_0000309044;Note=Uncharacterized protein YLR163W-A +##sequence-region O13546 1 115 +O13546 UniProtKB Chain 1 115 . . . ID=PRO_0000299624;Note=Putative uncharacterized protein YLR232W +##sequence-region O13542 1 113 +O13542 UniProtKB Chain 1 113 . . . ID=PRO_0000299630;Note=Putative uncharacterized protein YLR282C +##sequence-region Q3E771 1 56 +Q3E771 UniProtKB Chain 1 56 . . . ID=PRO_0000247137;Note=Uncharacterized protein YLR285C-A +##sequence-region Q8TGM3 1 30 +Q8TGM3 UniProtKB Chain 1 30 . . . ID=PRO_0000299634;Note=Putative uncharacterized protein YLR299C-A +##sequence-region Q3E825 1 87 +Q3E825 UniProtKB Chain 1 87 . . . ID=PRO_0000247162;Note=Uncharacterized protein YLR307C-A +##sequence-region Q06409 1 1932 +Q06409 UniProtKB Chain 1 1932 . . . ID=PRO_0000247776;Note=DOCK-like protein YLR422W +Q06409 UniProtKB Domain 1410 1824 . . . Note=DHR-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00984 +##sequence-region O13560 1 100 +O13560 UniProtKB Chain 1 100 . . . ID=PRO_0000299652;Note=Putative uncharacterized protein YLR444C +O13560 UniProtKB Transmembrane 50 70 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13560 UniProtKB Transmembrane 75 95 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06199 1 204 +Q06199 UniProtKB Chain 1 204 . . . ID=PRO_0000268191;Note=Pyridoxamine 5'-phosphate oxidase YLR456W homolog +Q06199 UniProtKB Nucleotide binding 65 66 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06199 UniProtKB Binding site 127 127 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q3E760 1 96 +Q3E760 UniProtKB Chain 1 96 . . . ID=PRO_0000247785;Note=Uncharacterized protein YMR030W-A +Q3E760 UniProtKB Transmembrane 59 81 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E760 UniProtKB Glycosylation 4 4 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E809 1 52 +Q3E809 UniProtKB Chain 1 52 . . . ID=PRO_0000247782;Note=Uncharacterized protein YML054C-A +##sequence-region P0CF18 1 432 +P0CF18 UniProtKB Chain 1 432 . . . ID=PRO_0000393382;Note=Uncharacterized protein YMR085W +P0CF18 UniProtKB Domain 105 244 . . . Note=SIS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00797 +P0CF18 UniProtKB Domain 277 422 . . . Note=SIS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00797 +##sequence-region Q6B0Z2 1 105 +Q6B0Z2 UniProtKB Chain 1 105 . . . ID=PRO_0000299661;Note=Putative uncharacterized protein YML101C-A +Q6B0Z2 UniProtKB Transmembrane 20 40 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q6B0Z2 UniProtKB Transmembrane 45 65 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q6B0Z2 UniProtKB Sequence conflict 11 11 . . . Note=K->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0C5Q4 1 74 +P0C5Q4 UniProtKB Chain 1 74 . . . ID=PRO_0000309052;Note=Putative uncharacterized protein YMR141W-A +P0C5Q4 UniProtKB Transmembrane 54 72 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PXH6 1 127 +A0A023PXH6 UniProtKB Chain 1 127 . . . ID=PRO_0000431055;Note=Putative uncharacterized membrane protein YMR172C-A +A0A023PXH6 UniProtKB Transmembrane 48 68 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXH6 UniProtKB Transmembrane 83 103 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E766 1 64 +Q3E766 UniProtKB Chain 1 64 . . . ID=PRO_0000247788;Note=Uncharacterized protein YMR175W-A +##sequence-region Q03703 1 340 +Q03703 UniProtKB Chain 1 340 . . . ID=PRO_0000203258;Note=Uncharacterized protein YML037C +##sequence-region Q04502 1 122 +Q04502 UniProtKB Chain 1 122 . . . ID=PRO_0000203246;Note=Putative uncharacterized protein YML089C +##sequence-region P0CL29 1 191 +P0CL29 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL29 UniProtKB Chain 18 191 . . . ID=PRO_0000406006;Note=Putative uncharacterized protein YML133W-A +P0CL29 UniProtKB Transmembrane 168 188 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL29 UniProtKB Compositional bias 13 159 . . . Note=Gly/Ser-rich +##sequence-region Q03207 1 126 +Q03207 UniProtKB Chain 1 126 . . . ID=PRO_0000203239;Note=Uncharacterized protein YML122C +##sequence-region Q03099 1 1374 +Q03099 UniProtKB Chain 1 1374 . . . ID=PRO_0000102209;Note=Y' element ATP-dependent helicase YML133C +Q03099 UniProtKB Domain 375 552 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q03099 UniProtKB Domain 609 758 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q03099 UniProtKB Nucleotide binding 388 395 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +##sequence-region Q04364 1 514 +Q04364 UniProtKB Chain 1 514 . . . ID=PRO_0000106320;Note=TPR repeat-containing protein YMR018W +Q04364 UniProtKB Repeat 174 207 . . . Note=TPR 1 +Q04364 UniProtKB Repeat 218 252 . . . Note=TPR 2 +Q04364 UniProtKB Repeat 254 286 . . . Note=TPR 3 +Q04364 UniProtKB Repeat 288 320 . . . Note=TPR 4 +Q04364 UniProtKB Repeat 326 359 . . . Note=TPR 5 +Q04364 UniProtKB Repeat 360 393 . . . Note=TPR 6 +Q04364 UniProtKB Repeat 394 427 . . . Note=TPR 7 +Q04364 UniProtKB Repeat 429 461 . . . Note=TPR 8 +Q04364 UniProtKB Sequence conflict 9 9 . . . Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q99337 1 1749 +Q99337 UniProtKB Chain 1 1749 . . . ID=PRO_0000279145;Note=Transposon Ty1-NL2 Gag-Pol polyprotein +Q99337 UniProtKB Chain 1 401 . . . ID=PRO_0000279146;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99337 UniProtKB Chain 402 582 . . . ID=PRO_0000279147;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99337 UniProtKB Chain 583 1211 . . . ID=PRO_0000279148;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99337 UniProtKB Chain 1212 1749 . . . ID=PRO_0000279149;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99337 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99337 UniProtKB Domain 1332 1470 . . . Note=Reverse transcriptase Ty1/copia-type +Q99337 UniProtKB Domain 1604 1746 . . . Note=RNase H Ty1/copia-type +Q99337 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99337 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q99337 UniProtKB Motif 1172 1206 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99337 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q99337 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99337 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99337 UniProtKB Metal binding 1340 1340 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99337 UniProtKB Metal binding 1421 1421 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99337 UniProtKB Metal binding 1422 1422 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99337 UniProtKB Metal binding 1604 1604 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99337 UniProtKB Metal binding 1646 1646 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99337 UniProtKB Metal binding 1679 1679 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99337 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99337 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99337 UniProtKB Site 1211 1212 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53740 1 393 +P53740 UniProtKB Chain 1 393 . . . ID=PRO_0000207672;Note=Probable phospholipid translocase non-catalytic subunit CRF1 +P53740 UniProtKB Topological domain 1 46 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P53740 UniProtKB Transmembrane 47 67 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53740 UniProtKB Topological domain 68 334 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P53740 UniProtKB Transmembrane 335 355 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53740 UniProtKB Topological domain 356 393 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +P53740 UniProtKB Glycosylation 78 78 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53740 UniProtKB Glycosylation 123 123 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53740 UniProtKB Glycosylation 187 187 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53740 UniProtKB Glycosylation 202 202 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53740 UniProtKB Glycosylation 213 213 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53740 UniProtKB Glycosylation 240 240 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53740 UniProtKB Glycosylation 291 291 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53967 1 105 +P53967 UniProtKB Chain 1 105 . . . ID=PRO_0000203459;Note=Putative uncharacterized protein YNL028W +##sequence-region P53932 1 642 +P53932 UniProtKB Chain 1 642 . . . ID=PRO_0000123807;Note=Uncharacterized transporter YNL095C +P53932 UniProtKB Topological domain 1 15 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Transmembrane 16 36 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Topological domain 37 42 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Transmembrane 43 63 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Topological domain 64 73 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Transmembrane 74 94 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Topological domain 95 104 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Transmembrane 105 125 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Topological domain 126 142 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Transmembrane 143 163 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Topological domain 164 460 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Transmembrane 461 481 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Topological domain 482 499 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Transmembrane 500 520 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Topological domain 521 538 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Transmembrane 539 559 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Topological domain 560 574 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Transmembrane 575 595 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Topological domain 596 614 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Transmembrane 615 635 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53932 UniProtKB Topological domain 636 642 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53929 1 270 +P53929 UniProtKB Chain 1 270 . . . ID=PRO_0000203436;Note=Uncharacterized protein YNL108C +P53929 UniProtKB Beta strand 5 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Helix 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Beta strand 18 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Helix 38 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Beta strand 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Helix 67 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Beta strand 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Helix 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Helix 107 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Turn 115 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Helix 135 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Beta strand 162 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Helix 169 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Beta strand 185 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Beta strand 189 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Beta strand 203 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Helix 218 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Beta strand 224 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Beta strand 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +P53929 UniProtKB Helix 253 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YN2 +##sequence-region P53907 1 740 +P53907 UniProtKB Chain 1 740 . . . ID=PRO_0000203423;Note=Uncharacterized protein YNL144C +##sequence-region P53878 1 407 +P53878 UniProtKB Chain 1 407 . . . ID=PRO_0000203405;Note=Uncharacterized oxidoreductase YNL181W +P53878 UniProtKB Topological domain 1 290 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53878 UniProtKB Transmembrane 291 311 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53878 UniProtKB Topological domain 312 407 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53878 UniProtKB Nucleotide binding 57 79 . . . Note=NAD or NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53878 UniProtKB Coiled coil 361 390 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53878 UniProtKB Sequence conflict 262 262 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40163 1 203 +P40163 UniProtKB Chain 1 203 . . . ID=PRO_0000203394;Note=Putative uncharacterized protein YNL203C +P40163 UniProtKB Transmembrane 89 109 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40163 UniProtKB Sequence conflict 160 160 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40163 UniProtKB Sequence conflict 178 178 . . . Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40163 UniProtKB Sequence conflict 183 183 . . . Note=K->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40163 UniProtKB Sequence conflict 186 186 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53857 1 426 +P53857 UniProtKB Chain 1 426 . . . ID=PRO_0000053402;Note=Uncharacterized globin-like protein YNL234W +##sequence-region Q12169 1 119 +Q12169 UniProtKB Chain 1 119 . . . ID=PRO_0000299701;Note=Uncharacterized protein YOR015W +Q12169 UniProtKB Transmembrane 57 77 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12169 UniProtKB Transmembrane 80 100 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q870I1 1 96 +Q870I1 UniProtKB Chain 1 96 . . . ID=PRO_0000299687;Note=Putative uncharacterized protein YOL013W-B +Q870I1 UniProtKB Transmembrane 1 21 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q870I1 UniProtKB Natural variant 48 48 . . . Note=In strain: CEN.PK 113-7D. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14654430;Dbxref=PMID:14654430 +Q870I1 UniProtKB Natural variant 59 59 . . . Note=In strain: CEN.PK 113-7D. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14654430;Dbxref=PMID:14654430 +Q870I1 UniProtKB Natural variant 69 69 . . . Note=In strain: CEN.PK 113-7D. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14654430;Dbxref=PMID:14654430 +##sequence-region Q08540 1 154 +Q08540 UniProtKB Chain 1 154 . . . ID=PRO_0000299719;Note=Putative uncharacterized protein YOR169C +##sequence-region Q08560 1 144 +Q08560 UniProtKB Chain 1 144 . . . ID=PRO_0000237662;Note=Putative uncharacterized protein YOR186W +Q08560 UniProtKB Transmembrane 90 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08560 UniProtKB Glycosylation 14 14 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08560 UniProtKB Glycosylation 15 15 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12501 1 1770 +Q12501 UniProtKB Chain 1 1770 . . . ID=PRO_0000279348;Note=Transposon Ty2-OR2 Gag-Pol polyprotein +Q12501 UniProtKB Chain 1 397 . . . ID=PRO_0000279349;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12501 UniProtKB Chain 398 578 . . . ID=PRO_0000279350;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12501 UniProtKB Chain 579 1232 . . . ID=PRO_0000279351;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12501 UniProtKB Chain 1233 1770 . . . ID=PRO_0000279352;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12501 UniProtKB Domain 656 831 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12501 UniProtKB Domain 1353 1491 . . . Note=Reverse transcriptase Ty1/copia-type +Q12501 UniProtKB Domain 1625 1767 . . . Note=RNase H Ty1/copia-type +Q12501 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12501 UniProtKB Region 579 636 . . . Note=Integrase-type zinc finger-like +Q12501 UniProtKB Motif 1193 1227 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12501 UniProtKB Active site 457 457 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12501 UniProtKB Metal binding 667 667 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12501 UniProtKB Metal binding 732 732 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12501 UniProtKB Metal binding 1361 1361 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12501 UniProtKB Metal binding 1442 1442 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12501 UniProtKB Metal binding 1443 1443 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12501 UniProtKB Metal binding 1625 1625 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12501 UniProtKB Metal binding 1667 1667 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12501 UniProtKB Metal binding 1700 1700 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12501 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12501 UniProtKB Site 578 579 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12501 UniProtKB Site 1232 1233 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q3E7Y7 1 49 +Q3E7Y7 UniProtKB Chain 1 49 . . . ID=PRO_0000245283;Note=Uncharacterized protein YOR293C-A +##sequence-region Q12506 1 109 +Q12506 UniProtKB Chain 1 109 . . . ID=PRO_0000299735;Note=Uncharacterized protein YOR314W +##sequence-region Q08842 1 122 +Q08842 UniProtKB Chain 1 122 . . . ID=PRO_0000299742;Note=Putative uncharacterized protein YOR364W +Q08842 UniProtKB Sequence conflict 96 96 . . . Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08902 1 515 +Q08902 UniProtKB Chain 1 515 . . . ID=PRO_0000244476;Note=Drug resistance protein YOR378W +Q08902 UniProtKB Topological domain 1 78 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Transmembrane 79 99 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Topological domain 100 111 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Transmembrane 112 132 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Topological domain 133 140 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Transmembrane 141 161 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Topological domain 162 171 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Transmembrane 172 192 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Topological domain 193 202 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Transmembrane 203 223 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Topological domain 224 241 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Transmembrane 242 262 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Topological domain 263 270 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Transmembrane 271 291 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Topological domain 292 310 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Transmembrane 311 331 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Topological domain 332 346 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Transmembrane 347 367 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Topological domain 368 374 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Transmembrane 375 395 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Topological domain 396 403 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Transmembrane 404 424 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Topological domain 425 435 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Transmembrane 436 456 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Topological domain 457 479 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Transmembrane 480 500 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08902 UniProtKB Topological domain 501 515 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08915 1 147 +Q08915 UniProtKB Chain 1 147 . . . ID=PRO_0000299745;Note=Putative uncharacterized protein YOR392W +Q08915 UniProtKB Transmembrane 69 89 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E769 1 90 +Q3E769 UniProtKB Chain 1 90 . . . ID=PRO_0000245277;Note=Uncharacterized protein YOL159C-A +##sequence-region P0C5R3 1 77 +P0C5R3 UniProtKB Chain 1 77 . . . ID=PRO_0000309061;Note=Putative uncharacterized protein YOR073W-A +##sequence-region A0A023PZ99 1 116 +A0A023PZ99 UniProtKB Chain 1 116 . . . ID=PRO_0000430979;Note=Putative uncharacterized protein YDR008C +A0A023PZ99 UniProtKB Transmembrane 20 42 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PZE6 1 104 +A0A023PZE6 UniProtKB Signal peptide 1 16 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZE6 UniProtKB Chain 17 104 . . . ID=PRO_0000430980;Note=Putative uncharacterized membrane protein YDR048C +A0A023PZE6 UniProtKB Transmembrane 74 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07379 1 328 +Q07379 UniProtKB Chain 1 328 . . . ID=PRO_0000248458;Note=Putative uncharacterized protein YDL057W +##sequence-region Q07509 1 169 +Q07509 UniProtKB Chain 1 169 . . . ID=PRO_0000299856;Note=Putative uncharacterized protein YDL094C +Q07509 UniProtKB Transmembrane 55 77 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12441 1 440 +Q12441 UniProtKB Chain 1 440 . . . ID=PRO_0000279014;Note=Transposon Ty1-DR3 Gag polyprotein +Q12441 UniProtKB Chain 1 401 . . . ID=PRO_0000279015;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12441 UniProtKB Peptide 402 440 . . . ID=PRO_0000279016;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12441 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12441 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q12441 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12441 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q99231 1 1755 +Q99231 UniProtKB Chain 1 1755 . . . ID=PRO_0000279009;Note=Transposon Ty1-DR3 Gag-Pol polyprotein +Q99231 UniProtKB Chain 1 401 . . . ID=PRO_0000279010;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99231 UniProtKB Chain 402 582 . . . ID=PRO_0000279011;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99231 UniProtKB Chain 583 1217 . . . ID=PRO_0000279012;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99231 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279013;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99231 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99231 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +Q99231 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +Q99231 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99231 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q99231 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99231 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q99231 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q99231 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99231 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99231 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99231 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99231 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99231 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99231 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99231 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q99231 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99231 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99231 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99231 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q12047 1 102 +Q12047 UniProtKB Chain 1 102 . . . ID=PRO_0000299858;Note=Putative uncharacterized protein YDL158C +##sequence-region Q3E789 1 49 +Q3E789 UniProtKB Chain 1 49 . . . ID=PRO_0000253832;Note=Uncharacterized protein YDR169C-A +##sequence-region Q3E796 1 67 +Q3E796 UniProtKB Chain 1 67 . . . ID=PRO_0000253833;Note=Uncharacterized protein YDR182W-A +Q3E796 UniProtKB Transmembrane 12 34 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0C5E0 1 132 +P0C5E0 UniProtKB Chain 1 132 . . . ID=PRO_0000302031;Note=Putative uncharacterized protein YDR193W +P0C5E0 UniProtKB Transmembrane 66 86 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0C5L9 1 24 +P0C5L9 UniProtKB Chain 1 24 . . . ID=PRO_0000309017;Note=Putative uncharacterized protein YDL247W-A +##sequence-region P87282 1 123 +P87282 UniProtKB Chain 1 123 . . . ID=PRO_0000299880;Note=Putative uncharacterized protein YDR271C +##sequence-region P0C5M0 1 45 +P0C5M0 UniProtKB Chain 1 45 . . . ID=PRO_0000309018;Note=Uncharacterized protein YDR320W-B +P0C5M0 UniProtKB Compositional bias 40 44 . . . Note=Poly-Lys +##sequence-region P87285 1 100 +P87285 UniProtKB Chain 1 100 . . . ID=PRO_0000299887;Note=Putative uncharacterized protein YDR355C +P87285 UniProtKB Transmembrane 20 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P87285 UniProtKB Transmembrane 44 61 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region O13522 1 166 +O13522 UniProtKB Chain 1 166 . . . ID=PRO_0000299888;Note=Putative uncharacterized protein YDR396W +O13522 UniProtKB Transmembrane 4 24 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13522 UniProtKB Transmembrane 101 121 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13522 UniProtKB Transmembrane 146 166 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04033 1 374 +Q04033 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04033 UniProtKB Chain 19 374 . . . ID=PRO_0000253823;Note=Probable aminopeptidase YDR415C +Q04033 UniProtKB Metal binding 177 177 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04033 UniProtKB Metal binding 196 196 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04033 UniProtKB Metal binding 196 196 . . . Note=Zinc 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04033 UniProtKB Metal binding 235 235 . . . Note=Zinc 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04033 UniProtKB Metal binding 262 262 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04033 UniProtKB Metal binding 340 340 . . . Note=Zinc 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P87270 1 130 +P87270 UniProtKB Chain 1 130 . . . ID=PRO_0000299894;Note=Putative uncharacterized protein YDR442W +P87270 UniProtKB Transmembrane 21 43 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P87271 1 102 +P87271 UniProtKB Chain 1 102 . . . ID=PRO_0000299896;Note=Putative uncharacterized protein YDR455C +##sequence-region Q03362 1 224 +Q03362 UniProtKB Chain 1 224 . . . ID=PRO_0000253853;Note=Uncharacterized protein YDR476C +Q03362 UniProtKB Glycosylation 10 10 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03362 UniProtKB Glycosylation 70 70 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03362 UniProtKB Glycosylation 74 74 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03057 1 142 +Q03057 UniProtKB Chain 1 142 . . . ID=PRO_0000299906;Note=Putative uncharacterized protein YDR544C +Q03057 UniProtKB Compositional bias 20 47 . . . Note=His-rich +##sequence-region Q8TGP9 1 58 +Q8TGP9 UniProtKB Chain 1 58 . . . ID=PRO_0000299859;Note=Putative uncharacterized protein YDL159C-B +Q8TGP9 UniProtKB Transmembrane 18 38 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0C5M3 1 85 +P0C5M3 UniProtKB Chain 1 85 . . . ID=PRO_0000309021;Note=Putative uncharacterized protein YDR183C-A +P0C5M3 UniProtKB Transmembrane 20 42 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C5M3 UniProtKB Transmembrane 52 69 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PYD3 1 111 +A0A023PYD3 UniProtKB Chain 1 111 . . . ID=PRO_0000430987;Note=Putative uncharacterized protein YDR094W +##sequence-region P0C5M5 1 37 +P0C5M5 UniProtKB Chain 1 37 . . . ID=PRO_0000309023;Note=Putative uncharacterized protein YDL114W-A +##sequence-region Q04925 1 415 +Q04925 UniProtKB Chain 1 415 . . . ID=PRO_0000253838;Note=SVF1-like protein YDR222W +##sequence-region Q8TGR5 1 104 +Q8TGR5 UniProtKB Chain 1 104 . . . ID=PRO_0000299909;Note=Putative uncharacterized protein YEL030C-A +##sequence-region P0CX95 1 160 +P0CX95 UniProtKB Chain 1 160 . . . ID=PRO_0000410452;Note=UPF0479 membrane protein YEL077W-A +P0CX95 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX95 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX95 UniProtKB Compositional bias 103 106 . . . Note=Poly-Ser +##sequence-region Q02590 1 73 +Q02590 UniProtKB Chain 1 73 . . . ID=PRO_0000299913;Note=Putative uncharacterized protein YER091C-A +##sequence-region P0CX71 1 440 +P0CX71 UniProtKB Chain 1 440 . . . ID=PRO_0000409791;Note=Transposon Ty1-ER1 Gag polyprotein +P0CX71 UniProtKB Chain 1 401 . . . ID=PRO_0000409792;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX71 UniProtKB Peptide 402 440 . . . ID=PRO_0000409793;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX71 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX71 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0CX71 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX71 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region P40097 1 107 +P40097 UniProtKB Chain 1 107 . . . ID=PRO_0000202659;Note=Uncharacterized protein YER181C%2C mitochondrial +P40097 UniProtKB Transmembrane 11 31 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40097 UniProtKB Transmembrane 58 78 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PZC3 1 113 +A0A023PZC3 UniProtKB Chain 1 113 . . . ID=PRO_0000430999;Note=Putative uncharacterized protein YER133W-A +##sequence-region Q03619 1 1755 +Q03619 UniProtKB Chain 1 1755 . . . ID=PRO_0000279048;Note=Transposon Ty1-ER2 Gag-Pol polyprotein +Q03619 UniProtKB Chain 1 401 . . . ID=PRO_0000279049;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03619 UniProtKB Chain 402 582 . . . ID=PRO_0000279050;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03619 UniProtKB Chain 583 1217 . . . ID=PRO_0000279051;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03619 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279052;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03619 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03619 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +Q03619 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +Q03619 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03619 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q03619 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03619 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q03619 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q03619 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03619 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03619 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03619 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03619 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03619 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03619 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03619 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03619 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03619 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03619 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P40000 1 116 +P40000 UniProtKB Chain 1 116 . . . ID=PRO_0000202615;Note=Putative uncharacterized protein YEL010W +##sequence-region P40083 1 148 +P40083 UniProtKB Chain 1 148 . . . ID=PRO_0000202652;Note=Uncharacterized protein YEL137C +##sequence-region A0A023PXK7 1 284 +A0A023PXK7 UniProtKB Chain 1 284 . . . ID=PRO_0000431011;Note=Putative uncharacterized membrane protein YFL021C-A +A0A023PXK7 UniProtKB Transmembrane 174 194 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXK7 UniProtKB Transmembrane 217 237 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXK7 UniProtKB Transmembrane 241 261 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXK7 UniProtKB Compositional bias 44 96 . . . Note=Ser-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00016 +##sequence-region A0A023PZH4 1 101 +A0A023PZH4 UniProtKB Chain 1 101 . . . ID=PRO_0000431013;Note=Putative uncharacterized protein YFR052C-A +A0A023PZH4 UniProtKB Transmembrane 58 80 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43562 1 540 +P43562 UniProtKB Chain 1 540 . . . ID=PRO_0000050464;Note=Probable metabolite transport protein YFL040W +P43562 UniProtKB Topological domain 1 29 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Transmembrane 30 50 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Topological domain 51 67 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Transmembrane 68 88 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Topological domain 89 101 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Transmembrane 102 122 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Topological domain 123 126 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Transmembrane 127 147 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Topological domain 148 158 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Transmembrane 159 179 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Topological domain 180 187 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Transmembrane 188 208 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Topological domain 209 275 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Transmembrane 276 296 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Topological domain 297 313 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Transmembrane 314 334 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Topological domain 335 341 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Transmembrane 342 362 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Topological domain 363 385 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Transmembrane 386 406 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Topological domain 407 428 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Transmembrane 429 449 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Topological domain 450 455 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Transmembrane 456 476 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Topological domain 477 540 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Glycosylation 52 52 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43562 UniProtKB Glycosylation 374 374 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43552 1 160 +P43552 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43552 UniProtKB Chain 24 160 . . . ID=PRO_0000014318;Note=Uncharacterized membrane protein YFL051C +P43552 UniProtKB Topological domain 24 132 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43552 UniProtKB Transmembrane 133 155 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43552 UniProtKB Topological domain 156 160 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43549 1 646 +P43549 UniProtKB Chain 1 646 . . . ID=PRO_0000064099;Note=Uncharacterized membrane protein YFL054C +P43549 UniProtKB Topological domain 1 350 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43549 UniProtKB Transmembrane 351 371 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43549 UniProtKB Topological domain 372 383 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43549 UniProtKB Transmembrane 384 404 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43549 UniProtKB Topological domain 405 427 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43549 UniProtKB Transmembrane 428 448 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43549 UniProtKB Topological domain 449 481 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43549 UniProtKB Transmembrane 482 502 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43549 UniProtKB Topological domain 503 509 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43549 UniProtKB Transmembrane 510 530 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43549 UniProtKB Topological domain 531 569 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43549 UniProtKB Transmembrane 570 590 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43549 UniProtKB Topological domain 591 646 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43549 UniProtKB Motif 408 410 . . . Note=NPA 1 +P43549 UniProtKB Motif 538 540 . . . Note=NPA 2 +##sequence-region P0CX99 1 160 +P0CX99 UniProtKB Chain 1 160 . . . ID=PRO_0000202666;Note=UPF0479 membrane protein YFL068W +P0CX99 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX99 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX99 UniProtKB Compositional bias 103 106 . . . Note=Poly-Ser +P0CX99 UniProtKB Sequence conflict 47 47 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P43625 1 151 +P43625 UniProtKB Chain 1 151 . . . ID=PRO_0000202701;Note=Uncharacterized protein YFR057W +##sequence-region Q8TGT8 1 28 +Q8TGT8 UniProtKB Chain 1 28 . . . ID=PRO_0000245387;Note=Uncharacterized protein YGR174W-A +##sequence-region P53217 1 278 +P53217 UniProtKB Chain 1 278 . . . ID=PRO_0000202790;Note=Uncharacterized membrane protein YGR026W +P53217 UniProtKB Topological domain 1 34 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53217 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53217 UniProtKB Topological domain 56 129 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53217 UniProtKB Transmembrane 130 150 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53217 UniProtKB Topological domain 151 180 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53217 UniProtKB Transmembrane 181 201 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53217 UniProtKB Topological domain 202 205 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53217 UniProtKB Transmembrane 206 222 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53217 UniProtKB Topological domain 223 278 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53232 1 107 +P53232 UniProtKB Chain 1 107 . . . ID=PRO_0000202798;Note=Putative uncharacterized protein YGR051C +##sequence-region Q12337 1 1770 +Q12337 UniProtKB Chain 1 1770 . . . ID=PRO_0000279316;Note=Transposon Ty2-GR1 Gag-Pol polyprotein +Q12337 UniProtKB Chain 1 397 . . . ID=PRO_0000279317;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12337 UniProtKB Chain 398 578 . . . ID=PRO_0000279318;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12337 UniProtKB Chain 579 1232 . . . ID=PRO_0000279319;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12337 UniProtKB Chain 1233 1770 . . . ID=PRO_0000279320;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12337 UniProtKB Domain 656 831 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12337 UniProtKB Domain 1353 1491 . . . Note=Reverse transcriptase Ty1/copia-type +Q12337 UniProtKB Domain 1625 1767 . . . Note=RNase H Ty1/copia-type +Q12337 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12337 UniProtKB Region 579 636 . . . Note=Integrase-type zinc finger-like +Q12337 UniProtKB Motif 1193 1227 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12337 UniProtKB Active site 457 457 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12337 UniProtKB Metal binding 667 667 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12337 UniProtKB Metal binding 732 732 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12337 UniProtKB Metal binding 1361 1361 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12337 UniProtKB Metal binding 1442 1442 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12337 UniProtKB Metal binding 1443 1443 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12337 UniProtKB Metal binding 1625 1625 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12337 UniProtKB Metal binding 1667 1667 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12337 UniProtKB Metal binding 1700 1700 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12337 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12337 UniProtKB Site 578 579 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12337 UniProtKB Site 1232 1233 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53249 1 370 +P53249 UniProtKB Signal peptide 1 27 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53249 UniProtKB Chain 28 370 . . . ID=PRO_0000014322;Note=Putative uncharacterized protein YGR079W +P53249 UniProtKB Compositional bias 140 146 . . . Note=Poly-Asp +P53249 UniProtKB Glycosylation 59 59 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53249 UniProtKB Glycosylation 98 98 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53249 UniProtKB Glycosylation 126 126 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53249 UniProtKB Glycosylation 171 171 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53249 UniProtKB Glycosylation 221 221 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53249 UniProtKB Glycosylation 230 230 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53249 UniProtKB Glycosylation 262 262 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53275 1 312 +P53275 UniProtKB Chain 1 312 . . . ID=PRO_0000202821;Note=Uncharacterized protein YGR127W +##sequence-region P53291 1 111 +P53291 UniProtKB Chain 1 111 . . . ID=PRO_0000202836;Note=Uncharacterized protein YGR164W +##sequence-region P53339 1 147 +P53339 UniProtKB Chain 1 147 . . . ID=PRO_0000014323;Note=Putative uncharacterized membrane protein YGR290W +P53339 UniProtKB Topological domain 1 16 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53339 UniProtKB Transmembrane 17 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53339 UniProtKB Topological domain 38 105 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53339 UniProtKB Transmembrane 106 126 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53339 UniProtKB Topological domain 127 147 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53144 1 215 +P53144 UniProtKB Chain 1 215 . . . ID=PRO_0000202754;Note=HD domain-containing protein YGL101W +P53144 UniProtKB Domain 58 164 . . . Note=HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01175 +##sequence-region P53134 1 725 +P53134 UniProtKB Chain 1 725 . . . ID=PRO_0000213789;Note=Putative oligopeptide transporter YGL114W +P53134 UniProtKB Transmembrane 28 48 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53134 UniProtKB Transmembrane 134 154 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53134 UniProtKB Transmembrane 254 274 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53134 UniProtKB Transmembrane 353 373 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53134 UniProtKB Transmembrane 449 469 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53134 UniProtKB Transmembrane 472 492 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53134 UniProtKB Transmembrane 564 584 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53134 UniProtKB Transmembrane 644 664 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53134 UniProtKB Transmembrane 697 717 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38887 1 602 +P38887 UniProtKB Chain 1 602 . . . ID=PRO_0000202941;Note=Uncharacterized protein YHR202W +P38887 UniProtKB Glycosylation 305 305 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38887 UniProtKB Glycosylation 497 497 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38887 UniProtKB Glycosylation 577 577 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PXL7 1 144 +A0A023PXL7 UniProtKB Chain 1 144 . . . ID=PRO_0000431021;Note=Putative uncharacterized membrane protein YHR056W-A +A0A023PXL7 UniProtKB Transmembrane 10 30 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXL7 UniProtKB Transmembrane 60 80 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PZI4 1 120 +A0A023PZI4 UniProtKB Chain 1 120 . . . ID=PRO_0000431023;Note=Putative uncharacterized membrane protein YHR069C-A +A0A023PZI4 UniProtKB Transmembrane 8 28 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZI4 UniProtKB Transmembrane 55 75 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region O13537 1 118 +O13537 UniProtKB Chain 1 118 . . . ID=PRO_0000299930;Note=Putative uncharacterized protein YHR145C +O13537 UniProtKB Transmembrane 71 91 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PZI9 1 157 +A0A023PZI9 UniProtKB Chain 1 157 . . . ID=PRO_0000431028;Note=Putative uncharacterized protein YHR182C-A +##sequence-region Q8TGK0 1 99 +Q8TGK0 UniProtKB Chain 1 99 . . . ID=PRO_0000202437;Note=Putative uncharacterized protein YHR214C-E +##sequence-region Q8TGK1 1 99 +Q8TGK1 UniProtKB Chain 1 99 . . . ID=PRO_0000245399;Note=Uncharacterized protein YHR213W-B +##sequence-region P0C5N6 1 59 +P0C5N6 UniProtKB Chain 1 59 . . . ID=PRO_0000309034;Note=Uncharacterized protein YHR032W-A +##sequence-region P0C2J7 1 1802 +P0C2J7 UniProtKB Chain 1 1802 . . . ID=PRO_0000279380;Note=Transposon Ty4-H Gag-Pol polyprotein +P0C2J7 UniProtKB Domain 619 786 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J7 UniProtKB Domain 1375 1510 . . . Note=Reverse transcriptase Ty1/copia-type +P0C2J7 UniProtKB Domain 1644 1790 . . . Note=RNase H Ty1/copia-type +P0C2J7 UniProtKB Region 381 501 . . . Note=Ty4 protease +P0C2J7 UniProtKB Region 539 599 . . . Note=Integrase-type zinc finger-like +P0C2J7 UniProtKB Coiled coil 39 115 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C2J7 UniProtKB Active site 414 414 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J7 UniProtKB Metal binding 630 630 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J7 UniProtKB Metal binding 695 695 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J7 UniProtKB Metal binding 1383 1383 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J7 UniProtKB Metal binding 1462 1462 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J7 UniProtKB Metal binding 1463 1463 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J7 UniProtKB Metal binding 1644 1644 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J7 UniProtKB Metal binding 1686 1686 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J7 UniProtKB Metal binding 1720 1720 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +##sequence-region P0C5N7 1 58 +P0C5N7 UniProtKB Chain 1 58 . . . ID=PRO_0000309035;Note=Uncharacterized protein YHR073W-A +##sequence-region Q03888 1 244 +Q03888 UniProtKB Chain 1 244 . . . ID=PRO_0000299761;Note=Putative uncharacterized protein YIR020C-B +Q03888 UniProtKB Sequence conflict 38 38 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region A0A023PZF3 1 158 +A0A023PZF3 UniProtKB Chain 1 158 . . . ID=PRO_0000431037;Note=Putative uncharacterized protein YIL071W-A +A0A023PZF3 UniProtKB Transmembrane 66 86 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZF3 UniProtKB Transmembrane 94 114 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PZJ9 1 123 +A0A023PZJ9 UniProtKB Chain 1 123 . . . ID=PRO_0000431038;Note=Putative uncharacterized protein YIL115W-A +##sequence-region P0CF21 1 127 +P0CF21 UniProtKB Chain 1 127 . . . ID=PRO_0000393393;Note=Putative truncated L-serine dehydratase YIL168W +P0CF21 UniProtKB Modified residue 39 39 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q7LHG5 1 1498 +Q7LHG5 UniProtKB Chain 1 1498 . . . ID=PRO_0000279367;Note=Transposon Ty3-I Gag-Pol polyprotein +Q7LHG5 UniProtKB Chain 1 207 . . . ID=PRO_0000279368;Note=Capsid protein +Q7LHG5 UniProtKB Peptide 208 233 . . . ID=PRO_0000279369;Note=Spacer peptide p3 +Q7LHG5 UniProtKB Chain 234 309 . . . ID=PRO_0000279370;Note=Nucleocapsid protein p11 +Q7LHG5 UniProtKB Chain 310 442 . . . ID=PRO_0000279371;Note=Ty3 protease +Q7LHG5 UniProtKB Peptide 443 561 . . . ID=PRO_0000279372;Note=Spacer peptide J;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q7LHG5 UniProtKB Chain 562 1037 . . . ID=PRO_0000279373;Note=Reverse transcriptase/ribonuclease H +Q7LHG5 UniProtKB Chain 1038 1498 . . . ID=PRO_0000279374;Note=Integrase p52 +Q7LHG5 UniProtKB Chain 1064 1498 . . . ID=PRO_0000279375;Note=Integrase p49 +Q7LHG5 UniProtKB Domain 646 823 . . . Note=Reverse transcriptase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405 +Q7LHG5 UniProtKB Domain 919 1037 . . . Note=RNase H Ty3/gyspy-type +Q7LHG5 UniProtKB Domain 1185 1350 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q7LHG5 UniProtKB Zinc finger 265 282 . . . Note=CCHC-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +Q7LHG5 UniProtKB Region 1132 1171 . . . Note=Integrase-type zinc finger-like +Q7LHG5 UniProtKB Active site 336 336 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q7LHG5 UniProtKB Metal binding 712 712 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q7LHG5 UniProtKB Metal binding 774 774 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q7LHG5 UniProtKB Metal binding 775 775 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q7LHG5 UniProtKB Metal binding 1201 1201 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q7LHG5 UniProtKB Metal binding 1262 1262 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q7LHG5 UniProtKB Site 207 208 . . . Note=Cleavage%3B by Ty3 protease +Q7LHG5 UniProtKB Site 233 234 . . . Note=Cleavage%3B by Ty3 protease +Q7LHG5 UniProtKB Site 309 310 . . . Note=Cleavage%3B by Ty3 protease +Q7LHG5 UniProtKB Site 442 443 . . . Note=Cleavage%3B by Ty3 protease;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q7LHG5 UniProtKB Site 561 562 . . . Note=Cleavage%3B by Ty3 protease +Q7LHG5 UniProtKB Site 1037 1038 . . . Note=Cleavage%3B by Ty3 protease +Q7LHG5 UniProtKB Site 1063 1064 . . . Note=Cleavage%3B by Ty3 protease%3B partial +Q7LHG5 UniProtKB Sequence conflict 502 502 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40520 1 121 +P40520 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40520 UniProtKB Chain 24 121 . . . ID=PRO_0000202985;Note=Uncharacterized protein YIL059C +P40520 UniProtKB Glycosylation 68 68 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40520 UniProtKB Glycosylation 84 84 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53039 1 248 +P53039 UniProtKB Chain 1 248 . . . ID=PRO_0000066269;Note=Protein transport protein YIP1 +P53039 UniProtKB Topological domain 1 110 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53039 UniProtKB Transmembrane 111 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53039 UniProtKB Topological domain 132 132 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53039 UniProtKB Transmembrane 133 153 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53039 UniProtKB Topological domain 154 172 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53039 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53039 UniProtKB Topological domain 194 196 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53039 UniProtKB Transmembrane 197 217 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53039 UniProtKB Topological domain 218 227 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53039 UniProtKB Transmembrane 228 248 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53039 UniProtKB Mutagenesis 70 70 . . . Note=In YIP1-41%3B lethal%3B abolishes binding to YIF1%2C YPT1 and YPT31. In YIP1-40%3B temperature sensitive%3B reduces binding to YPT31%2C and inhibits ER vesicle budding%3B when associated with A-130. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160 +P53039 UniProtKB Mutagenesis 70 70 . . . Note=In YIP1-4%3B temperature sensitive%3B reduces binding to YIF1%2C YPT1 and YPT31. In YIP1-44%3B lethal%3B when associated with E-130. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160 +P53039 UniProtKB Mutagenesis 70 70 . . . Note=In YIP1-42%3B temperature sensitive%3B abolishes binding to YPT1 and YPT31%2C and inhibits ER vesicle budding. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160 +P53039 UniProtKB Mutagenesis 76 76 . . . Note=In YIP1-6%3B lethal%3B reduces binding to YIF1. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160 +P53039 UniProtKB Mutagenesis 81 81 . . . Note=In YIP1-9%3B lethal. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160 +P53039 UniProtKB Mutagenesis 114 114 . . . Note=In YIP1-1%3B blocks ER-Golgi protein transport%2C and causes a severe growth defect at 36 degrees Celsius%3B when associated with E-129. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9724632;Dbxref=PMID:9724632 +P53039 UniProtKB Mutagenesis 129 129 . . . Note=In YIP1-1%3B blocks ER-Golgi protein transport%2C and causes a severe growth defect at 36 degrees Celsius%3B when associated with L-114. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9724632;Dbxref=PMID:9724632 +P53039 UniProtKB Mutagenesis 130 130 . . . Note=In YIP1-40%3B temperature sensitive%3B reduces binding to YPT31%2C and inhibits ER vesicle budding%3B when associated with G-70. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160 +P53039 UniProtKB Mutagenesis 130 130 . . . Note=In YIP1-44%3B lethal%3B when associated with K-70. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160 +P53039 UniProtKB Mutagenesis 153 155 . . . Note=In YIP1-12%3B abolishes binding to YPT1 and YPT31. LMS->GGG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160 +P53039 UniProtKB Mutagenesis 175 175 . . . Note=In YIP1-2%3B abolishes binding to YPT1 and YPT31%2C reduces binding to YIF1%2C blocks ER-Golgi protein transport%2C and causes a severe growth defect at 36 degrees Celsius. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9724632;Dbxref=PMID:9724632 +P53039 UniProtKB Mutagenesis 177 177 . . . Note=In YIP1-18%3B abolishes binding to YIF1%2C YPT1 and YPT31. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160 +P53039 UniProtKB Mutagenesis 180 180 . . . Note=In YIP1-19%3B lethal%3B abolishes binding to YPT1 and YPT31%2C and reduces binding to YIF1. P->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611160;Dbxref=PMID:15611160 +##sequence-region P40446 1 119 +P40446 UniProtKB Chain 1 119 . . . ID=PRO_0000204050;Note=Putative nitrilase-like protein YIL165C +P40446 UniProtKB Domain 1 82 . . . Note=CN hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054 +P40446 UniProtKB Active site 21 21 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q8TGN3 1 28 +Q8TGN3 UniProtKB Chain 1 28 . . . ID=PRO_0000299762;Note=Uncharacterized protein YJL077W-A +##sequence-region P47151 1 130 +P47151 UniProtKB Chain 1 130 . . . ID=PRO_0000203113;Note=Putative uncharacterized protein YJR114W +##sequence-region P47174 1 117 +P47174 UniProtKB Chain 1 117 . . . ID=PRO_0000203127;Note=Uncharacterized protein YJR146W +##sequence-region P47063 1 138 +P47063 UniProtKB Chain 1 138 . . . ID=PRO_0000203072;Note=Uncharacterized protein YJL027C +##sequence-region P40365 1 116 +P40365 UniProtKB Chain 1 116 . . . ID=PRO_0000203055;Note=Putative uncharacterized protein YJL067W +P40365 UniProtKB Transmembrane 40 60 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40365 UniProtKB Transmembrane 72 92 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0C5P2 1 29 +P0C5P2 UniProtKB Chain 1 29 . . . ID=PRO_0000309040;Note=Uncharacterized protein YKL100W-A +##sequence-region P36155 1 307 +P36155 UniProtKB Chain 1 307 . . . ID=PRO_0000203222;Note=Uncharacterized protein YKR075C +P36155 UniProtKB Compositional bias 254 270 . . . Note=His-rich +##sequence-region P36092 1 106 +P36092 UniProtKB Chain 1 106 . . . ID=PRO_0000203182;Note=Uncharacterized protein YKL044W +P36092 UniProtKB Transmembrane 85 101 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P35725 1 167 +P35725 UniProtKB Chain 1 167 . . . ID=PRO_0000203175;Note=Uncharacterized protein YKL063C +##sequence-region P36031 1 110 +P36031 UniProtKB Chain 1 110 . . . ID=PRO_0000203130;Note=Putative UPF0377 protein YKL223W +##sequence-region Q2V2P1 1 62 +Q2V2P1 UniProtKB Chain 1 62 . . . ID=PRO_0000262874;Note=Coiled-coil domain-containing protein YLR146W-A +Q2V2P1 UniProtKB Coiled coil 14 49 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0C2I7 1 1755 +P0C2I7 UniProtKB Chain 1 1755 . . . ID=PRO_0000279109;Note=Transposon Ty1-LR4 Gag-Pol polyprotein +P0C2I7 UniProtKB Chain 1 401 . . . ID=PRO_0000279110;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I7 UniProtKB Chain 402 582 . . . ID=PRO_0000279111;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I7 UniProtKB Chain 583 1217 . . . ID=PRO_0000279112;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I7 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279113;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I7 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I7 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +P0C2I7 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +P0C2I7 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I7 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +P0C2I7 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I7 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0C2I7 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +P0C2I7 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I7 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I7 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I7 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I7 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I7 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I7 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I7 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I7 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I7 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I7 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I7 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region Q06479 1 807 +Q06479 UniProtKB Chain 1 807 . . . ID=PRO_0000268189;Note=F-box protein YLR352W +Q06479 UniProtKB Domain 220 266 . . . Note=F-box +##sequence-region O13579 1 124 +O13579 UniProtKB Chain 1 124 . . . ID=PRO_0000299645;Note=Putative uncharacterized protein YLR379W +O13579 UniProtKB Transmembrane 94 114 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06051 1 157 +Q06051 UniProtKB Chain 1 157 . . . ID=PRO_0000299646;Note=Putative uncharacterized protein YLR400W +Q06051 UniProtKB Transmembrane 42 64 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGJ4 1 38 +Q8TGJ4 UniProtKB Chain 1 38 . . . ID=PRO_0000247780;Note=Putative uncharacterized protein YLR466C-B +##sequence-region P0C5Q0 1 46 +P0C5Q0 UniProtKB Chain 1 46 . . . ID=PRO_0000309048;Note=Putative uncharacterized protein YLR154W-F +##sequence-region P0CE97 1 114 +P0CE97 UniProtKB Chain 1 114 . . . ID=PRO_0000393295;Note=Putative uncharacterized protein YLR159W +##sequence-region P0C5Q1 1 40 +P0C5Q1 UniProtKB Chain 1 40 . . . ID=PRO_0000309049;Note=Uncharacterized protein YLR364C-A +##sequence-region Q8TGJ7 1 56 +Q8TGJ7 UniProtKB Chain 1 56 . . . ID=PRO_0000247154;Note=Uncharacterized protein YLL066W-B +Q8TGJ7 UniProtKB Compositional bias 20 51 . . . Note=His/Thr-rich +##sequence-region P53956 1 172 +P53956 UniProtKB Chain 1 172 . . . ID=PRO_0000203454;Note=Uncharacterized endoplasmic reticulum membrane protein YNL046W +P53956 UniProtKB Topological domain 1 101 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53956 UniProtKB Transmembrane 102 122 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53956 UniProtKB Topological domain 123 145 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53956 UniProtKB Transmembrane 146 164 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53956 UniProtKB Topological domain 165 172 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53948 1 110 +P53948 UniProtKB Chain 1 110 . . . ID=PRO_0000203450;Note=Putative uncharacterized protein YNL057W +##sequence-region Q08465 1 219 +Q08465 UniProtKB Chain 1 219 . . . ID=PRO_0000240248;Note=Protein YNG1 +Q08465 UniProtKB Zinc finger 155 204 . . . Note=PHD-type%3B degenerate +Q08465 UniProtKB Metal binding 158 158 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +Q08465 UniProtKB Metal binding 160 160 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +Q08465 UniProtKB Metal binding 171 171 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +Q08465 UniProtKB Metal binding 176 176 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +Q08465 UniProtKB Metal binding 182 182 . . . Note=Zinc 1%3B via pros nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +Q08465 UniProtKB Metal binding 185 185 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +Q08465 UniProtKB Metal binding 198 198 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +Q08465 UniProtKB Metal binding 202 202 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +Q08465 UniProtKB Binding site 157 157 . . . Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +Q08465 UniProtKB Binding site 168 168 . . . Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +Q08465 UniProtKB Binding site 172 172 . . . Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +Q08465 UniProtKB Binding site 180 180 . . . Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +Q08465 UniProtKB Turn 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JMI +Q08465 UniProtKB Beta strand 165 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JMI +Q08465 UniProtKB Beta strand 173 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JMI +Q08465 UniProtKB Turn 183 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JMI +Q08465 UniProtKB Helix 200 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JMI +##sequence-region P53926 1 123 +P53926 UniProtKB Chain 1 123 . . . ID=PRO_0000203434;Note=Putative uncharacterized protein YNL114C +P53926 UniProtKB Transmembrane 53 73 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53926 UniProtKB Transmembrane 75 95 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53922 1 161 +P53922 UniProtKB Chain 1 161 . . . ID=PRO_0000203431;Note=Putative uncharacterized protein YNL120C +##sequence-region P40162 1 140 +P40162 UniProtKB Chain 1 140 . . . ID=PRO_0000203393;Note=Putative uncharacterized protein YNL205C +##sequence-region Q99248 1 730 +Q99248 UniProtKB Chain 1 730 . . . ID=PRO_0000235938;Note=Uncharacterized protein YOR019W +##sequence-region Q3E735 1 80 +Q3E735 UniProtKB Chain 1 80 . . . ID=PRO_0000237646;Note=Uncharacterized membrane protein YOR034C-A +Q3E735 UniProtKB Transmembrane 10 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08504 1 108 +Q08504 UniProtKB Chain 1 108 . . . ID=PRO_0000299712;Note=Uncharacterized protein YOR105W +Q08504 UniProtKB Compositional bias 46 97 . . . Note=Ile-rich +##sequence-region Q08532 1 130 +Q08532 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08532 UniProtKB Chain 21 130 . . . ID=PRO_0000299716;Note=Putative uncharacterized protein YOR139C +##sequence-region P0C5R0 1 36 +P0C5R0 UniProtKB Chain 1 36 . . . ID=PRO_0000309058;Note=Putative uncharacterized protein YOR314W-A +##sequence-region Q08321 1 113 +Q08321 UniProtKB Chain 1 113 . . . ID=PRO_0000299698;Note=Uncharacterized protein YOL160W +##sequence-region Q8TGJ1 1 51 +Q8TGJ1 UniProtKB Chain 1 51 . . . ID=PRO_0000211379;Note=UPF0320 protein YOL166W-A +##sequence-region Q08620 1 132 +Q08620 UniProtKB Chain 1 132 . . . ID=PRO_0000299723;Note=Putative uncharacterized protein YOR200W +##sequence-region Q12439 1 438 +Q12439 UniProtKB Chain 1 438 . . . ID=PRO_0000279345;Note=Transposon Ty2-OR1 Gag polyprotein +Q12439 UniProtKB Chain 1 397 . . . ID=PRO_0000279346;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12439 UniProtKB Peptide 398 438 . . . ID=PRO_0000279347;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12439 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12439 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q12293 1 438 +Q12293 UniProtKB Chain 1 438 . . . ID=PRO_0000279353;Note=Transposon Ty2-OR2 Gag polyprotein +Q12293 UniProtKB Chain 1 397 . . . ID=PRO_0000279354;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12293 UniProtKB Peptide 398 438 . . . ID=PRO_0000279355;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12293 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12293 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q8TGL2 1 66 +Q8TGL2 UniProtKB Chain 1 66 . . . ID=PRO_0000299727;Note=Putative uncharacterized protein YOR231C-A +##sequence-region Q08728 1 135 +Q08728 UniProtKB Chain 1 135 . . . ID=PRO_0000299730;Note=Putative uncharacterized protein YOR263C +Q08728 UniProtKB Compositional bias 57 63 . . . Note=Poly-Ser +##sequence-region Q08373 1 112 +Q08373 UniProtKB Chain 1 112 . . . ID=PRO_0000299699;Note=Putative uncharacterized protein YOL166C +Q08373 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08373 UniProtKB Transmembrane 69 89 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12402 1 180 +Q12402 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.4;Dbxref=PMID:22814378 +Q12402 UniProtKB Chain 2 180 . . . ID=PRO_0000101859;Note=Protein YOP1 +Q12402 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12402 UniProtKB Transmembrane 61 81 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12402 UniProtKB Transmembrane 89 109 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12402 UniProtKB Transmembrane 110 130 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12402 UniProtKB Region 2 17 . . . Note=Interaction with YIP1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278413;Dbxref=PMID:11278413 +Q12402 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.4;Dbxref=PMID:22814378 +##sequence-region Q02659 1 185 +Q02659 UniProtKB Chain 1 185 . . . ID=PRO_0000299797;Note=Putative uncharacterized protein YPL025C +Q02659 UniProtKB Compositional bias 110 117 . . . Note=Poly-Phe +##sequence-region Q3E7B4 1 63 +Q3E7B4 UniProtKB Chain 1 63 . . . ID=PRO_0000238636;Note=Uncharacterized protein YPL038W-A +##sequence-region Q02781 1 134 +Q02781 UniProtKB Chain 1 134 . . . ID=PRO_0000299800;Note=Uncharacterized protein YPL062W +##sequence-region Q02754 1 198 +Q02754 UniProtKB Chain 1 198 . . . ID=PRO_0000238641;Note=Uncharacterized protein YPL067C +Q02754 UniProtKB Sequence conflict 78 78 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q02754 UniProtKB Helix 18 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI +Q02754 UniProtKB Helix 30 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI +Q02754 UniProtKB Helix 37 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI +Q02754 UniProtKB Helix 55 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI +Q02754 UniProtKB Helix 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI +Q02754 UniProtKB Beta strand 86 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI +Q02754 UniProtKB Beta strand 101 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI +Q02754 UniProtKB Helix 119 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI +Q02754 UniProtKB Helix 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI +Q02754 UniProtKB Helix 140 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI +Q02754 UniProtKB Beta strand 148 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI +Q02754 UniProtKB Turn 155 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI +Q02754 UniProtKB Beta strand 163 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI +Q02754 UniProtKB Turn 174 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI +Q02754 UniProtKB Helix 179 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KCI +##sequence-region Q02831 1 240 +Q02831 UniProtKB Chain 1 240 . . . ID=PRO_0000238644;Note=Uncharacterized protein YPL077C +Q02831 UniProtKB Modified residue 59 59 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02831 UniProtKB Modified residue 95 95 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region O13586 1 101 +O13586 UniProtKB Chain 1 101 . . . ID=PRO_0000299822;Note=Putative uncharacterized protein YPR092W +##sequence-region O13548 1 118 +O13548 UniProtKB Chain 1 118 . . . ID=PRO_0000299824;Note=Putative uncharacterized protein YPR099C +##sequence-region O13519 1 122 +O13519 UniProtKB Signal peptide 1 33 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13519 UniProtKB Chain 34 122 . . . ID=PRO_0000299805;Note=Putative uncharacterized protein YPL136W +##sequence-region Q2V2P0 1 78 +Q2V2P0 UniProtKB Chain 1 78 . . . ID=PRO_0000242692;Note=Uncharacterized protein YPR145C-A +##sequence-region Q6Q5H1 1 440 +Q6Q5H1 UniProtKB Chain 1 440 . . . ID=PRO_0000279189;Note=Transposon Ty1-PR3 Gag polyprotein +Q6Q5H1 UniProtKB Chain 1 401 . . . ID=PRO_0000279190;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q6Q5H1 UniProtKB Peptide 402 440 . . . ID=PRO_0000279191;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q6Q5H1 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q6Q5H1 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q6Q5H1 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q6Q5H1 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +Q6Q5H1 UniProtKB Sequence conflict 199 199 . . . Note=G->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12042 1 273 +Q12042 UniProtKB Chain 1 273 . . . ID=PRO_0000238655;Note=Vacuolar membrane protein YPL162C +Q12042 UniProtKB Topological domain 1 13 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12042 UniProtKB Transmembrane 14 34 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12042 UniProtKB Topological domain 35 51 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12042 UniProtKB Transmembrane 52 72 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12042 UniProtKB Topological domain 73 97 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12042 UniProtKB Transmembrane 98 118 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12042 UniProtKB Topological domain 119 156 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12042 UniProtKB Transmembrane 157 177 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12042 UniProtKB Topological domain 178 198 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12042 UniProtKB Transmembrane 199 219 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12042 UniProtKB Topological domain 220 273 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08930 1 360 +Q08930 UniProtKB Chain 1 360 . . . ID=PRO_0000238658;Note=Ubiquitin carboxyl-terminal hydrolase MIY1 +Q08930 UniProtKB Active site 28 28 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N5J2 +Q08930 UniProtKB Active site 216 216 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N5J2 +Q08930 UniProtKB Site 296 296 . . . Note=Ubiquitin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N5J2 +Q08930 UniProtKB Site 299 300 . . . Note=Ubiquitin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N5J2 +Q08930 UniProtKB Site 303 303 . . . Note=Ubiquitin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8N5J2 +##sequence-region Q08958 1 114 +Q08958 UniProtKB Chain 1 114 . . . ID=PRO_0000299809;Note=Putative uncharacterized protein YPL205C +Q08958 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q99395 1 206 +Q99395 UniProtKB Chain 1 206 . . . ID=PRO_0000242135;Note=Uncharacterized protein YPL229W +Q99395 UniProtKB Compositional bias 40 65 . . . Note=Gln-rich +Q99395 UniProtKB Modified residue 68 68 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q12179 1 454 +Q12179 UniProtKB Chain 1 454 . . . ID=PRO_0000242145;Note=Uncharacterized protein YPL245W +##sequence-region Q08977 1 551 +Q08977 UniProtKB Chain 1 551 . . . ID=PRO_0000255978;Note=UPF0662 protein YPL260W +Q08977 UniProtKB Coiled coil 174 213 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08977 UniProtKB Coiled coil 249 300 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08977 UniProtKB Sequence conflict 90 90 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08977 UniProtKB Sequence conflict 128 128 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38298 1 316 +P38298 UniProtKB Chain 1 316 . . . ID=PRO_0000212466;Note=Alkaline ceramidase YPC1 +P38298 UniProtKB Topological domain 1 68 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38298 UniProtKB Transmembrane 69 89 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38298 UniProtKB Topological domain 90 93 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38298 UniProtKB Transmembrane 94 114 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38298 UniProtKB Topological domain 115 135 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38298 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38298 UniProtKB Topological domain 157 160 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38298 UniProtKB Transmembrane 161 181 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38298 UniProtKB Topological domain 182 195 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38298 UniProtKB Transmembrane 196 216 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38298 UniProtKB Topological domain 217 228 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38298 UniProtKB Transmembrane 229 249 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38298 UniProtKB Topological domain 250 316 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07688 1 167 +Q07688 UniProtKB Chain 1 167 . . . ID=PRO_0000262758;Note=Phosphorelay intermediate protein YPD1 +Q07688 UniProtKB Domain 24 129 . . . Note=HPt;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00110 +Q07688 UniProtKB Modified residue 64 64 . . . Note=Phosphohistidine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00110,ECO:0000269|PubMed:8808622;Dbxref=PMID:8808622 +Q07688 UniProtKB Mutagenesis 64 64 . . . Note=Loss of function. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8808622;Dbxref=PMID:8808622 +Q07688 UniProtKB Mutagenesis 67 67 . . . Note=Reduces binding of the 4-aspartylphosphate of SLN1. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15628880;Dbxref=PMID:15628880 +Q07688 UniProtKB Mutagenesis 68 68 . . . Note=Reduces phosphoryl transfer rate. G->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15628880;Dbxref=PMID:15628880 +Q07688 UniProtKB Mutagenesis 74 74 . . . Note=In NH1%3B causes resistance to the antifungal antibiotic pradimicin. G->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15015733;Dbxref=PMID:15015733 +Q07688 UniProtKB Mutagenesis 86 86 . . . Note=Reduces phosphoryl transfer rate. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15628880;Dbxref=PMID:15628880 +Q07688 UniProtKB Mutagenesis 90 90 . . . Note=Reduces phosphoryl transfer rate. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15628880;Dbxref=PMID:15628880 +Q07688 UniProtKB Helix 11 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +Q07688 UniProtKB Turn 20 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +Q07688 UniProtKB Helix 26 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +Q07688 UniProtKB Helix 56 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +Q07688 UniProtKB Helix 76 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +Q07688 UniProtKB Helix 99 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +Q07688 UniProtKB Helix 109 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +Q07688 UniProtKB Beta strand 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +Q07688 UniProtKB Turn 117 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +Q07688 UniProtKB Beta strand 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +Q07688 UniProtKB Helix 135 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +##sequence-region P53819 1 1859 +P53819 UniProtKB Chain 1 1859 . . . ID=PRO_0000102205;Note=Y' element ATP-dependent helicase protein 1 copy 6 +P53819 UniProtKB Domain 861 1038 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P53819 UniProtKB Domain 1095 1244 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P53819 UniProtKB Nucleotide binding 874 881 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +##sequence-region P53584 1 459 +P53584 UniProtKB Chain 1 459 . . . ID=PRO_0000066529;Note=Protein YTP1 +P53584 UniProtKB Topological domain 1 6 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Topological domain 28 59 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Transmembrane 60 80 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Topological domain 81 82 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Transmembrane 83 103 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Topological domain 104 122 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Transmembrane 123 143 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Topological domain 144 170 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Transmembrane 171 191 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Topological domain 192 205 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Transmembrane 206 226 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Topological domain 227 266 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Transmembrane 267 287 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Topological domain 288 295 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Transmembrane 296 316 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Topological domain 317 322 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Transmembrane 323 343 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Topological domain 344 351 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Transmembrane 352 372 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Topological domain 373 389 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Transmembrane 390 410 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53584 UniProtKB Topological domain 411 459 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E741 1 30 +Q3E741 UniProtKB Chain 1 30 . . . ID=PRO_0000248427;Note=Putative uncharacterized protein YAL037C-A +##sequence-region Q3E791 1 96 +Q3E791 UniProtKB Chain 1 96 . . . ID=PRO_0000248428;Note=Uncharacterized protein YAL063C-A +##sequence-region O13588 1 104 +O13588 UniProtKB Chain 1 104 . . . ID=PRO_0000299789;Note=Putative uncharacterized protein YAL069W +##sequence-region A0A023PXA5 1 189 +A0A023PXA5 UniProtKB Chain 1 189 . . . ID=PRO_0000430976;Note=Putative uncharacterized protein YAL019W-A +##sequence-region P39559 1 98 +P39559 UniProtKB Chain 1 98 . . . ID=PRO_0000202429;Note=Putative uncharacterized protein YA5053W +P39559 UniProtKB Transmembrane 13 33 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39559 UniProtKB Transmembrane 65 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39563 1 99 +P39563 UniProtKB Chain 1 99 . . . ID=PRO_0000202433;Note=Uncharacterized protein YAR064W +P39563 UniProtKB Transmembrane 74 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39566 1 99 +P39566 UniProtKB Chain 1 99 . . . ID=PRO_0000202436;Note=Putative uncharacterized protein YAR070C +##sequence-region Q08182 1 245 +Q08182 UniProtKB Chain 1 245 . . . ID=PRO_0000076527;Note=AP-1-like transcription factor YAP7 +Q08182 UniProtKB Domain 125 188 . . . Note=bZIP +Q08182 UniProtKB Region 130 149 . . . Note=Basic motif;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08182 UniProtKB Region 153 181 . . . Note=Leucine-zipper;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38294 1 104 +P38294 UniProtKB Chain 1 104 . . . ID=PRO_0000202503;Note=Putative uncharacterized protein YBR174C +##sequence-region Q8TGK4 1 73 +Q8TGK4 UniProtKB Chain 1 73 . . . ID=PRO_0000248446;Note=Uncharacterized protein YBR298C-A +Q8TGK4 UniProtKB Sequence conflict 48 48 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q8TGK4 UniProtKB Sequence conflict 48 48 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q8TGK4 UniProtKB Sequence conflict 48 48 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q8TGK4 UniProtKB Sequence conflict 48 48 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38299 1 523 +P38299 UniProtKB Chain 1 523 . . . ID=PRO_0000202505;Note=Uncharacterized protein YBR184W +##sequence-region P38306 1 217 +P38306 UniProtKB Chain 1 217 . . . ID=PRO_0000202508;Note=Uncharacterized protein YBR197C +##sequence-region I2HB52 1 66 +I2HB52 UniProtKB Chain 1 66 . . . ID=PRO_0000419187;Note=Uncharacterized protein YBR056W-A +I2HB52 UniProtKB Compositional bias 26 29 . . . Note=Poly-Pro +I2HB52 UniProtKB Compositional bias 33 62 . . . Note=Cys-rich +##sequence-region P38161 1 101 +P38161 UniProtKB Chain 1 101 . . . ID=PRO_0000202438;Note=Putative UPF0377 protein YBL108W +##sequence-region P38233 1 116 +P38233 UniProtKB Chain 1 116 . . . ID=PRO_0000202475;Note=Putative uncharacterized protein YBR051W +P38233 UniProtKB Transmembrane 24 44 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38233 UniProtKB Transmembrane 70 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38235 1 358 +P38235 UniProtKB Chain 1 358 . . . ID=PRO_0000173052;Note=Uncharacterized protein YBR053C +P38235 UniProtKB Sequence conflict 178 178 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38268 1 175 +P38268 UniProtKB Chain 1 175 . . . ID=PRO_0000202488;Note=Putative uncharacterized protein YBR116C +P38268 UniProtKB Transmembrane 143 166 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38269 1 119 +P38269 UniProtKB Chain 1 119 . . . ID=PRO_0000202489;Note=Putative uncharacterized protein YBR124W +P38269 UniProtKB Transmembrane 80 104 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGQ2 1 116 +Q8TGQ2 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q8TGQ2 UniProtKB Chain 22 116 . . . ID=PRO_0000299837;Note=Putative uncharacterized protein YCR045W-A +##sequence-region Q3E830 1 75 +Q3E830 UniProtKB Chain 1 75 . . . ID=PRO_0000248451;Note=Uncharacterized protein YCR075W-A +Q3E830 UniProtKB Beta strand 11 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM +Q3E830 UniProtKB Beta strand 21 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM +Q3E830 UniProtKB Helix 27 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM +Q3E830 UniProtKB Helix 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM +Q3E830 UniProtKB Helix 35 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM +Q3E830 UniProtKB Beta strand 47 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM +Q3E830 UniProtKB Beta strand 66 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM +##sequence-region Q3E7Z8 1 88 +Q3E7Z8 UniProtKB Chain 1 88 . . . ID=PRO_0000248452;Note=Uncharacterized protein YCR024C-B +Q3E7Z8 UniProtKB Transmembrane 5 25 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E7Z8 UniProtKB Transmembrane 36 56 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P25384 1 1770 +P25384 UniProtKB Chain 1 1770 . . . ID=PRO_0000199562;Note=Transposon Ty2-C Gag-Pol polyprotein +P25384 UniProtKB Chain 1 397 . . . ID=PRO_0000279278;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25384 UniProtKB Chain 398 578 . . . ID=PRO_0000279279;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25384 UniProtKB Chain 579 1232 . . . ID=PRO_0000279280;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25384 UniProtKB Chain 1233 1770 . . . ID=PRO_0000279281;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25384 UniProtKB Domain 656 831 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P25384 UniProtKB Domain 1353 1491 . . . Note=Reverse transcriptase Ty1/copia-type +P25384 UniProtKB Domain 1625 1767 . . . Note=RNase H Ty1/copia-type +P25384 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25384 UniProtKB Region 579 636 . . . Note=Integrase-type zinc finger-like +P25384 UniProtKB Motif 1193 1227 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25384 UniProtKB Active site 457 457 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25384 UniProtKB Metal binding 667 667 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P25384 UniProtKB Metal binding 732 732 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P25384 UniProtKB Metal binding 1361 1361 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P25384 UniProtKB Metal binding 1442 1442 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P25384 UniProtKB Metal binding 1443 1443 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P25384 UniProtKB Metal binding 1625 1625 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P25384 UniProtKB Metal binding 1667 1667 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P25384 UniProtKB Metal binding 1700 1700 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P25384 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25384 UniProtKB Site 578 579 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25384 UniProtKB Site 1232 1233 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25384 UniProtKB Sequence conflict 460 460 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25384 UniProtKB Sequence conflict 460 460 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25384 UniProtKB Sequence conflict 629 629 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25384 UniProtKB Sequence conflict 629 629 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25384 UniProtKB Sequence conflict 814 814 . . . Note=S->SA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25384 UniProtKB Sequence conflict 814 814 . . . Note=S->SA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25384 UniProtKB Sequence conflict 1577 1578 . . . Note=AQ->LN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25384 UniProtKB Sequence conflict 1577 1578 . . . Note=AQ->LN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25563 1 115 +P25563 UniProtKB Chain 1 115 . . . ID=PRO_0000202542;Note=Putative uncharacterized protein YCL023C +##sequence-region P25600 1 308 +P25600 UniProtKB Chain 1 308 . . . ID=PRO_0000203503;Note=Putative transposon Ty5-1 protein YCL074W +##sequence-region P39978 1 195 +P39978 UniProtKB Chain 1 195 . . . ID=PRO_0000202602;Note=Uncharacterized protein YEL067C +##sequence-region P39972 1 122 +P39972 UniProtKB Chain 1 122 . . . ID=PRO_0000202598;Note=Uncharacterized protein YEL075C +##sequence-region P40049 1 302 +P40049 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40049 UniProtKB Chain 24 302 . . . ID=PRO_0000014316;Note=Putative uncharacterized protein YER076C +P40049 UniProtKB Glycosylation 65 65 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40049 UniProtKB Glycosylation 86 86 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40049 UniProtKB Glycosylation 93 93 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40049 UniProtKB Glycosylation 220 220 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40049 UniProtKB Glycosylation 231 231 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CL27 1 191 +P0CL27 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL27 UniProtKB Chain 18 191 . . . ID=PRO_0000299916;Note=Putative uncharacterized protein YER190C-A +P0CL27 UniProtKB Transmembrane 168 188 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL27 UniProtKB Compositional bias 13 159 . . . Note=Gly/Ser-rich +##sequence-region Q07451 1 203 +Q07451 UniProtKB Chain 1 203 . . . ID=PRO_0000248402;Note=Endoplasmic reticulum transmembrane protein 3 +Q07451 UniProtKB Topological domain 1 6 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07451 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07451 UniProtKB Topological domain 28 45 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07451 UniProtKB Transmembrane 46 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07451 UniProtKB Topological domain 67 110 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07451 UniProtKB Transmembrane 111 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07451 UniProtKB Topological domain 132 203 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGU2 1 87 +Q8TGU2 UniProtKB Chain 1 87 . . . ID=PRO_0000245375;Note=Uncharacterized protein YFR032C-B +Q8TGU2 UniProtKB Transmembrane 20 42 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43580 1 148 +P43580 UniProtKB Chain 1 148 . . . ID=PRO_0000202679;Note=Uncharacterized protein YFL012W +##sequence-region P43564 1 1073 +P43564 UniProtKB Chain 1 1073 . . . ID=PRO_0000202674;Note=Uncharacterized membrane protein YFL034W +P43564 UniProtKB Topological domain 1 552 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43564 UniProtKB Transmembrane 553 573 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43564 UniProtKB Topological domain 574 576 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43564 UniProtKB Transmembrane 577 597 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43564 UniProtKB Topological domain 598 694 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43564 UniProtKB Transmembrane 695 715 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43564 UniProtKB Topological domain 716 752 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43564 UniProtKB Transmembrane 753 773 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43564 UniProtKB Topological domain 774 1073 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43564 UniProtKB Modified residue 435 435 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43564 UniProtKB Modified residue 1037 1037 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P43564 UniProtKB Sequence conflict 323 323 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P43546 1 152 +P43546 UniProtKB Chain 1 152 . . . ID=PRO_0000070371;Note=Putative aryl-alcohol dehydrogenase YFL057C +##sequence-region P43622 1 192 +P43622 UniProtKB Chain 1 192 . . . ID=PRO_0000202699;Note=Uncharacterized protein YFR054C +##sequence-region P53151 1 121 +P53151 UniProtKB Chain 1 121 . . . ID=PRO_0000202756;Note=Uncharacterized protein YGL088W +P53151 UniProtKB Transmembrane 26 46 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53151 UniProtKB Transmembrane 72 92 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53084 1 216 +P53084 UniProtKB Chain 1 216 . . . ID=PRO_0000202716;Note=Putative uncharacterized protein YGL218W +##sequence-region P53066 1 181 +P53066 UniProtKB Chain 1 181 . . . ID=PRO_0000067245;Note=Ankyrin repeat-containing protein YGL242C +P53066 UniProtKB Repeat 49 78 . . . Note=ANK 1 +P53066 UniProtKB Repeat 85 120 . . . Note=ANK 2 +P53066 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53066 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region O13533 1 98 +O13533 UniProtKB Chain 1 98 . . . ID=PRO_0000299926;Note=Putative uncharacterized protein YHR049C-A +O13533 UniProtKB Transmembrane 8 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13533 UniProtKB Transmembrane 73 93 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CL33 1 64 +P0CL33 UniProtKB Chain 1 64 . . . ID=PRO_0000406009;Note=Putative uncharacterized protein YHR054W-A +P0CL33 UniProtKB Transmembrane 33 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PZE1 1 111 +A0A023PZE1 UniProtKB Chain 1 111 . . . ID=PRO_0000431022;Note=Putative uncharacterized membrane protein YHR063W-A +A0A023PZE1 UniProtKB Transmembrane 7 29 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZE1 UniProtKB Transmembrane 49 71 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZE1 UniProtKB Compositional bias 77 110 . . . Note=Ser-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00016 +##sequence-region A0A023PZE4 1 103 +A0A023PZE4 UniProtKB Chain 1 103 . . . ID=PRO_0000431027;Note=Putative uncharacterized protein YHR165W-A +A0A023PZE4 UniProtKB Compositional bias 24 97 . . . Note=Gly-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00008 +##sequence-region P0C5N5 1 34 +P0C5N5 UniProtKB Chain 1 34 . . . ID=PRO_0000309033;Note=Putative uncharacterized protein YHR180C-B +##sequence-region O13534 1 161 +O13534 UniProtKB Chain 1 161 . . . ID=PRO_0000202944;Note=Putative uncharacterized protein YHR214W-A +##sequence-region P0CX19 1 203 +P0CX19 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX19 UniProtKB Chain 24 184 . . . ID=PRO_0000409754;Note=Putative GPI-anchored protein YHR214W +P0CX19 UniProtKB Propeptide 185 203 . . . ID=PRO_0000409755;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX19 UniProtKB Compositional bias 25 57 . . . Note=Ser-rich +P0CX19 UniProtKB Lipidation 184 184 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX19 UniProtKB Glycosylation 28 28 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX19 UniProtKB Glycosylation 138 138 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CX93 1 97 +P0CX93 UniProtKB Chain 1 97 . . . ID=PRO_0000410451;Note=Uncharacterized protein YHR214C-D +P0CX93 UniProtKB Transmembrane 5 25 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX93 UniProtKB Transmembrane 27 47 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX93 UniProtKB Transmembrane 77 97 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q6Q5P6 1 413 +Q6Q5P6 UniProtKB Chain 1 413 . . . ID=PRO_0000279381;Note=Transposon Ty4-H Gag polyprotein +Q6Q5P6 UniProtKB Coiled coil 39 115 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38745 1 532 +P38745 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38745 UniProtKB Chain 21 532 . . . ID=PRO_0000014326;Note=Uncharacterized membrane protein YHL071W +P38745 UniProtKB Topological domain 21 193 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38745 UniProtKB Transmembrane 194 214 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38745 UniProtKB Topological domain 215 226 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38745 UniProtKB Transmembrane 227 247 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38745 UniProtKB Topological domain 248 262 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38745 UniProtKB Transmembrane 263 283 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38745 UniProtKB Topological domain 284 301 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38745 UniProtKB Transmembrane 302 322 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38745 UniProtKB Topological domain 323 330 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38745 UniProtKB Transmembrane 331 351 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38745 UniProtKB Topological domain 352 375 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38745 UniProtKB Transmembrane 376 396 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38745 UniProtKB Topological domain 397 414 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38745 UniProtKB Transmembrane 415 435 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38745 UniProtKB Topological domain 436 532 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38745 UniProtKB Modified residue 497 497 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38745 UniProtKB Glycosylation 152 152 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38745 UniProtKB Glycosylation 253 253 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38740 1 315 +P38740 UniProtKB Chain 1 315 . . . ID=PRO_0000014325;Note=Uncharacterized protein YHL026C +P38740 UniProtKB Transmembrane 18 38 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38740 UniProtKB Transmembrane 202 222 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38740 UniProtKB Transmembrane 244 264 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38775 1 560 +P38775 UniProtKB Chain 1 560 . . . ID=PRO_0000202893;Note=Putative uncharacterized protein YHR045W +P38775 UniProtKB Transmembrane 9 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38775 UniProtKB Transmembrane 61 81 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38775 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38775 UniProtKB Transmembrane 305 325 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38775 UniProtKB Transmembrane 442 462 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04013 1 314 +Q04013 UniProtKB Chain 1 314 . . . ID=PRO_0000090688;Note=Citrate/oxoglutarate carrier protein +Q04013 UniProtKB Transmembrane 23 44 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04013 UniProtKB Transmembrane 77 97 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04013 UniProtKB Transmembrane 111 127 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04013 UniProtKB Transmembrane 178 198 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04013 UniProtKB Transmembrane 218 238 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04013 UniProtKB Transmembrane 273 294 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04013 UniProtKB Repeat 18 100 . . . Note=Solcar 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00282 +Q04013 UniProtKB Repeat 107 199 . . . Note=Solcar 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00282 +Q04013 UniProtKB Repeat 217 301 . . . Note=Solcar 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00282 +Q04013 UniProtKB DNA binding 246 259 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9742088;Dbxref=PMID:9742088 +Q04013 UniProtKB Mutagenesis 249 253 . . . Note=Fails to bind DNA in vitro. PNRPK->GGGGG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9742088;Dbxref=PMID:9742088 +##sequence-region Q04116 1 353 +Q04116 UniProtKB Chain 1 353 . . . ID=PRO_0000049386;Note=Homeobox protein YHP1 +Q04116 UniProtKB DNA binding 173 232 . . . Note=Homeobox;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00108 +Q04116 UniProtKB Modified residue 315 315 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region Q03885 1 199 +Q03885 UniProtKB Chain 1 199 . . . ID=PRO_0000299759;Note=Putative uncharacterized protein YIR017W-A +Q03885 UniProtKB Transmembrane 40 60 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03885 UniProtKB Transmembrane 86 106 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03885 UniProtKB Transmembrane 117 137 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03885 UniProtKB Transmembrane 166 186 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03885 UniProtKB Sequence conflict 185 185 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03885 UniProtKB Sequence conflict 198 199 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region A0A023PZJ3 1 112 +A0A023PZJ3 UniProtKB Chain 1 112 . . . ID=PRO_0000431032;Note=Putative uncharacterized membrane protein YIL030W-A +A0A023PZJ3 UniProtKB Transmembrane 62 82 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PXF8 1 147 +A0A023PXF8 UniProtKB Chain 1 147 . . . ID=PRO_0000431035;Note=Putative uncharacterized membrane protein YIL066W-A +A0A023PXF8 UniProtKB Transmembrane 13 35 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q2V2P5 1 75 +Q2V2P5 UniProtKB Chain 1 75 . . . ID=PRO_0000245402;Note=Uncharacterized protein YIL102C-A +Q2V2P5 UniProtKB Transmembrane 5 25 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q2V2P5 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q2V2P4 1 73 +Q2V2P4 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q2V2P4 UniProtKB Chain 23 73 . . . ID=PRO_0000245400;Note=Uncharacterized protein YIL156W-B +##sequence-region Q03886 1 80 +Q03886 UniProtKB Chain 1 80 . . . ID=PRO_0000299760;Note=Putative uncharacterized protein YIR020W-A +##sequence-region P40543 1 189 +P40543 UniProtKB Chain 1 189 . . . ID=PRO_0000203000;Note=Uncharacterized protein YIL024C +P40543 UniProtKB Modified residue 107 107 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40543 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40508 1 320 +P40508 UniProtKB Chain 1 320 . . . ID=PRO_0000202980;Note=Uncharacterized protein YIL077C +P40508 UniProtKB Modified residue 230 230 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q06596 1 294 +Q06596 UniProtKB Chain 1 294 . . . ID=PRO_0000076528;Note=AP-1-like transcription factor YAP8 +Q06596 UniProtKB Domain 22 72 . . . Note=bZIP +Q06596 UniProtKB Region 22 45 . . . Note=Basic motif;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06596 UniProtKB Region 44 72 . . . Note=Leucine-zipper;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P40017 1 923 +P40017 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40017 UniProtKB Chain 2 923 . . . ID=PRO_0000210176;Note=Carnitine O-acetyltransferase YAT2 +P40017 UniProtKB Region 530 541 . . . Note=Coenzyme A binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40017 UniProtKB Binding site 576 576 . . . Note=Carnitine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40017 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40017 UniProtKB Modified residue 783 783 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P0C269 1 39 +P0C269 UniProtKB Chain 1 39 . . . ID=PRO_0000268623;Note=Uncharacterized protein YBL100W-C +##sequence-region P0C5L2 1 88 +P0C5L2 UniProtKB Chain 1 88 . . . ID=PRO_0000309010;Note=Putative uncharacterized protein YBR076C-A +P0C5L2 UniProtKB Transmembrane 8 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C5L2 UniProtKB Transmembrane 45 65 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E7Y4 1 105 +Q3E7Y4 UniProtKB Chain 1 105 . . . ID=PRO_0000248407;Note=Putative uncharacterized helicase-like protein YBL112C +Q3E7Y4 UniProtKB Domain 2 44 . . . Note=Helicase C-terminal +##sequence-region Q12266 1 440 +Q12266 UniProtKB Chain 1 440 . . . ID=PRO_0000278990;Note=Transposon Ty1-BL Gag polyprotein +Q12266 UniProtKB Chain 1 401 . . . ID=PRO_0000278991;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12266 UniProtKB Peptide 402 440 . . . ID=PRO_0000278992;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12266 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12266 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q12490 1 1755 +Q12490 UniProtKB Chain 1 1755 . . . ID=PRO_0000278985;Note=Transposon Ty1-BL Gag-Pol polyprotein +Q12490 UniProtKB Chain 1 401 . . . ID=PRO_0000278986;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12490 UniProtKB Chain 402 582 . . . ID=PRO_0000278987;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12490 UniProtKB Chain 583 1217 . . . ID=PRO_0000278988;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12490 UniProtKB Chain 1218 1755 . . . ID=PRO_0000278989;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12490 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12490 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +Q12490 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +Q12490 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12490 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q12490 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12490 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q12490 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12490 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12490 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12490 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12490 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12490 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12490 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12490 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12490 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12490 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12490 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q3E776 1 120 +Q3E776 UniProtKB Chain 1 120 . . . ID=PRO_0000248444;Note=Uncharacterized protein YBR255C-A +Q3E776 UniProtKB Transmembrane 22 44 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E776 UniProtKB Glycosylation 114 114 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38201 1 376 +P38201 UniProtKB Chain 1 376 . . . ID=PRO_0000202461;Note=Uncharacterized protein YBL029W +##sequence-region P38194 1 122 +P38194 UniProtKB Chain 1 122 . . . ID=PRO_0000202459;Note=Uncharacterized protein YBL044W +##sequence-region P34224 1 193 +P34224 UniProtKB Chain 1 193 . . . ID=PRO_0000202454;Note=Uncharacterized protein YBL059W +P34224 UniProtKB Transmembrane 119 143 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38180 1 368 +P38180 UniProtKB Chain 1 368 . . . ID=PRO_0000202447;Note=Uncharacterized protein YBL081W +##sequence-region P38220 1 110 +P38220 UniProtKB Chain 1 110 . . . ID=PRO_0000202471;Note=Uncharacterized protein YBR027C +P38220 UniProtKB Transmembrane 6 26 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38220 UniProtKB Transmembrane 38 58 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q96VH1 1 84 +Q96VH1 UniProtKB Chain 1 84 . . . ID=PRO_0000299835;Note=Putative uncharacterized protein YCR018C-A +Q96VH1 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q96VH1 UniProtKB Transmembrane 52 72 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E787 1 52 +Q3E787 UniProtKB Chain 1 52 . . . ID=PRO_0000248453;Note=Putative uncharacterized protein YCR095W-A +##sequence-region Q3E819 1 63 +Q3E819 UniProtKB Chain 1 63 . . . ID=PRO_0000248454;Note=Uncharacterized protein YCR108C +##sequence-region P37263 1 153 +P37263 UniProtKB Chain 1 153 . . . ID=PRO_0000202578;Note=UPF0743 protein YCR087C-A +P37263 UniProtKB Zinc finger 1 26 . . . Note=C2HC LYAR-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01145 +P37263 UniProtKB Zinc finger 27 52 . . . Note=C2HC LYAR-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01145 +##sequence-region P42937 1 148 +P42937 UniProtKB Chain 1 148 . . . ID=PRO_0000202844;Note=CDC25-like phosphatase YCH1 +P42937 UniProtKB Domain 29 137 . . . Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173 +P42937 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P42937 UniProtKB Beta strand 3 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FS5 +P42937 UniProtKB Beta strand 8 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A +P42937 UniProtKB Helix 14 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A +P42937 UniProtKB Turn 27 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A +P42937 UniProtKB Beta strand 33 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A +P42937 UniProtKB Helix 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FS5 +P42937 UniProtKB Helix 56 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A +P42937 UniProtKB Helix 63 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A +P42937 UniProtKB Beta strand 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A +P42937 UniProtKB Beta strand 84 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A +P42937 UniProtKB Beta strand 91 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A +P42937 UniProtKB Helix 96 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A +P42937 UniProtKB Helix 110 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A +P42937 UniProtKB Beta strand 116 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A +P42937 UniProtKB Helix 124 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A +P42937 UniProtKB Turn 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A +P42937 UniProtKB Beta strand 139 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A +P42937 UniProtKB Helix 144 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4A +##sequence-region P25347 1 104 +P25347 UniProtKB Chain 1 104 . . . ID=PRO_0000202559;Note=Uncharacterized protein YCR001W +##sequence-region P25354 1 239 +P25354 UniProtKB Chain 1 239 . . . ID=PRO_0000207531;Note=DUP240 protein YCR007C +P25354 UniProtKB Topological domain 1 54 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25354 UniProtKB Transmembrane 55 75 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25354 UniProtKB Topological domain 76 79 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25354 UniProtKB Transmembrane 80 104 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25354 UniProtKB Topological domain 105 239 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25354 UniProtKB Natural variant 2 2 . . . Note=In strain: CLIB 219. Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P25354 UniProtKB Natural variant 42 42 . . . Note=In strain: CLIB 219%2C CLIB 410%2C CLIB 413%2C CLIB 630 haplotype Ha1%2C K1%2C YIIc12 haplotype Ha2 and CLIB 382. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P25354 UniProtKB Natural variant 215 215 . . . Note=In strain: CLIB 630. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +##sequence-region P25654 1 182 +P25654 UniProtKB Chain 1 182 . . . ID=PRO_0000202580;Note=UPF0587 protein YCR090C +##sequence-region Q12195 1 79 +Q12195 UniProtKB Chain 1 79 . . . ID=PRO_0000299869;Note=Putative uncharacterized protein YDR015C +##sequence-region P0C1Z1 1 29 +P0C1Z1 UniProtKB Chain 1 29 . . . ID=PRO_0000253882;Note=Uncharacterized protein YDR524W-C +##sequence-region Q04408 1 483 +Q04408 UniProtKB Chain 1 483 . . . ID=PRO_0000253854;Note=Uncharacterized protein YDR514C +##sequence-region Q03049 1 344 +Q03049 UniProtKB Chain 1 344 . . . ID=PRO_0000253887;Note=Putative uncharacterized oxidoreductase YDR541C +Q03049 UniProtKB Sequence conflict 341 341 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03049 UniProtKB Sequence conflict 341 341 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q3E7B7 1 68 +Q3E7B7 UniProtKB Chain 1 68 . . . ID=PRO_0000268193;Note=SERF-like protein YDL085C-A +Q3E7B7 UniProtKB Modified residue 37 37 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q12331 1 272 +Q12331 UniProtKB Signal peptide 1 26 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12331 UniProtKB Chain 27 272 . . . ID=PRO_0000008801;Note=FAS1 domain-containing protein YDR262W +Q12331 UniProtKB Domain 100 269 . . . Note=FAS1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00082 +##sequence-region P43551 1 465 +P43551 UniProtKB Chain 1 465 . . . ID=PRO_0000114996;Note=Uncharacterized transcriptional regulatory protein YFL052W +P43551 UniProtKB DNA binding 8 34 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +##sequence-region P43624 1 122 +P43624 UniProtKB Chain 1 122 . . . ID=PRO_0000202700;Note=Putative uncharacterized protein YFR056C +P43624 UniProtKB Transmembrane 36 56 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43624 UniProtKB Transmembrane 72 92 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGU0 1 28 +Q8TGU0 UniProtKB Chain 1 28 . . . ID=PRO_0000245380;Note=Uncharacterized protein YGL007C-A +##sequence-region Q8TGP1 1 76 +Q8TGP1 UniProtKB Chain 1 76 . . . ID=PRO_0000299920;Note=Putative uncharacterized protein YGL123C-A +##sequence-region P0CX67 1 440 +P0CX67 UniProtKB Chain 1 440 . . . ID=PRO_0000409782;Note=Transposon Ty1-GR3 Gag polyprotein +P0CX67 UniProtKB Chain 1 401 . . . ID=PRO_0000409783;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX67 UniProtKB Peptide 402 440 . . . ID=PRO_0000409784;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX67 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX67 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0CX67 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX67 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region Q8TGU1 1 46 +Q8TGU1 UniProtKB Chain 1 46 . . . ID=PRO_0000245378;Note=Uncharacterized protein YGL188C-A +##sequence-region P53212 1 290 +P53212 UniProtKB Chain 1 290 . . . ID=PRO_0000175945;Note=Probable transcriptional regulatory protein HAH1 +##sequence-region Q8TGN7 1 72 +Q8TGN7 UniProtKB Chain 1 72 . . . ID=PRO_0000299924;Note=Putative uncharacterized protein YGR270C-A +Q8TGN7 UniProtKB Transmembrane 46 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53243 1 804 +P53243 UniProtKB Chain 1 804 . . . ID=PRO_0000046863;Note=Zinc finger protein YGR067C +P53243 UniProtKB Zinc finger 8 30 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P53243 UniProtKB Zinc finger 36 59 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +##sequence-region P53182 1 67 +P53182 UniProtKB Chain 1 67 . . . ID=PRO_0000202771;Note=Putative uncharacterized protein YGL041C +P53182 UniProtKB Transmembrane 13 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53182 UniProtKB Transmembrane 42 64 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53139 1 140 +P53139 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53139 UniProtKB Chain 2 140 . . . ID=PRO_0000202751;Note=Uncharacterized protein YGL108C +P53139 UniProtKB Compositional bias 41 49 . . . Note=Poly-Lys +P53139 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53139 UniProtKB Lipidation 4 4 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53116 1 101 +P53116 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53116 UniProtKB Chain 19 101 . . . ID=PRO_0000014321;Note=Uncharacterized protein YGL149W +P53116 UniProtKB Transmembrane 62 82 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53116 UniProtKB Compositional bias 24 28 . . . Note=Poly-Leu +##sequence-region P53105 1 115 +P53105 UniProtKB Chain 1 115 . . . ID=PRO_0000202726;Note=Putative uncharacterized protein YGL177W +##sequence-region P53100 1 379 +P53100 UniProtKB Chain 1 379 . . . ID=PRO_0000076037;Note=Putative 2-hydroxyacid dehydrogenase YGL185C +P53100 UniProtKB Nucleotide binding 207 208 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53100 UniProtKB Nucleotide binding 291 293 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53100 UniProtKB Nucleotide binding 341 344 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53100 UniProtKB Active site 293 293 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53100 UniProtKB Active site 322 322 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53100 UniProtKB Active site 341 341 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53100 UniProtKB Binding site 317 317 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53089 1 101 +P53089 UniProtKB Chain 1 101 . . . ID=PRO_0000202719;Note=Uncharacterized protein YGL204C +P53089 UniProtKB Transmembrane 20 40 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53089 UniProtKB Transmembrane 59 79 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PYG1 1 162 +A0A023PYG1 UniProtKB Chain 1 162 . . . ID=PRO_0000431014;Note=Putative uncharacterized membrane protein YHL002C-A +A0A023PYG1 UniProtKB Transmembrane 132 151 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PXE8 1 106 +A0A023PXE8 UniProtKB Chain 1 106 . . . ID=PRO_0000431017;Note=Putative uncharacterized protein YHR028W-A +##sequence-region Q8TGT5 1 39 +Q8TGT5 UniProtKB Chain 1 39 . . . ID=PRO_0000299925;Note=Putative uncharacterized protein YHR032C-A +##sequence-region P38899 1 603 +P38899 UniProtKB Chain 1 603 . . . ID=PRO_0000202947;Note=Putative uncharacterized protein YHR218W +##sequence-region P38730 1 149 +P38730 UniProtKB Chain 1 149 . . . ID=PRO_0000202878;Note=Uncharacterized protein YHL041W +P38730 UniProtKB Sequence conflict 124 124 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38727 1 235 +P38727 UniProtKB Chain 1 235 . . . ID=PRO_0000207533;Note=DUP240 protein YHL044W +P38727 UniProtKB Topological domain 1 44 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38727 UniProtKB Transmembrane 45 65 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38727 UniProtKB Topological domain 66 72 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38727 UniProtKB Transmembrane 73 93 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38727 UniProtKB Topological domain 94 235 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38727 UniProtKB Natural variant 9 9 . . . Note=In strain: CLIB 95%2C CLIB 219%2C CLIB 382%2C CLIB 388%2C CLIB 410%2C CLIB 413%2C CLIB 556%2C CLIB 630%2C K1%2C R12%2C R13%2C YIIc12 and YIIc17. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38727 UniProtKB Natural variant 47 47 . . . Note=In strain: CLIB 219%2C CLIB 388%2C CLIB 410%2C CLIB 413%2C CLIB 556%2C CLIB 630%2C YIIc12 haplotype Ha2 and YIIc17 haplotype Ha2. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38727 UniProtKB Natural variant 75 75 . . . Note=In strain: CLIB 95%2C CLIB 382%2C CLIB 556 haplotype Ha1%2C K1%2C R12%2C R13%2C YIIc12 haplotype Ha1 and YIIc17 haplotype Ha1. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38727 UniProtKB Natural variant 77 77 . . . Note=In strain: CLIB 388. L->F +P38727 UniProtKB Natural variant 86 86 . . . Note=In strain: CLIB 388. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38727 UniProtKB Natural variant 96 96 . . . Note=In strain: CLIB 95%2C CLIB 219%2C CLIB 382%2C CLIB 388%2C CLIB 410%2C CLIB 413%2C CLIB 556%2C CLIB 630%2C K1%2C R12%2C R13%2C YIIc12 and YIIc17. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38727 UniProtKB Natural variant 103 103 . . . Note=In strain: CLIB 388%2C CLIB 410%2C CLIB 556 haplotype Ha2%2C CLIB 630%2C YIIc12 haplotype Ha2 and YIIc17 haplotype Ha2. R->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38727 UniProtKB Natural variant 124 124 . . . Note=In strain: CLIB 95%2C CLIB 219%2C CLIB 382%2C CLIB 388%2C CLIB 410%2C CLIB 413%2C CLIB 556%2C CLIB 630%2C K1%2C R12%2C R13%2C YIIc12 and YIIc17. M->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38727 UniProtKB Natural variant 145 145 . . . Note=In strain: R12 haplotype Ha2. I->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38727 UniProtKB Natural variant 157 157 . . . Note=In strain: CLIB 95%2C CLIB 219%2C CLIB 382%2C CLIB 388%2C CLIB 410%2C CLIB 413%2C CLIB 556%2C CLIB 630%2C K1%2C R12%2C R13%2C YIIc12 and YIIc17. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38727 UniProtKB Natural variant 160 160 . . . Note=In strain: CLIB 556 haplotype Ha1. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38727 UniProtKB Natural variant 180 180 . . . Note=In strain: CLIB 95%2C CLIB 382%2C K1%2C R12%2C R13%2C YIIc12 haplotype Ha1 and YIIc17 haplotype Ha1. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38727 UniProtKB Natural variant 189 189 . . . Note=In strain: CLIB 95%2C CLIB 219%2C CLIB 382%2C CLIB 388%2C CLIB 410%2C CLIB 413%2C CLIB 556%2C CLIB 630%2C K1%2C R12%2C R13%2C YIIc12 and YIIc17. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38727 UniProtKB Natural variant 225 235 . . . Note=In strain: CLIB 630. EDKYPEMGVTV->RISIQRWGTQF +P38727 UniProtKB Natural variant 233 233 . . . Note=In strain: CLIB 219%2C CLIB 388%2C CLIB 410%2C CLIB 413%2C CLIB 556%2C CLIB 630%2C YIIc12 haplotype Ha2 and YIIc17 haplotype Ha2. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38727 UniProtKB Natural variant 234 234 . . . Note=In strain: CLIB 413 haplotype Ha1. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +##sequence-region P38765 1 294 +P38765 UniProtKB Chain 1 294 . . . ID=PRO_0000162387;Note=Uncharacterized isomerase YHI9 +P38765 UniProtKB Active site 52 52 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38765 UniProtKB Beta strand 3 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Beta strand 19 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Helix 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Helix 38 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Beta strand 53 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Beta strand 65 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Beta strand 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Helix 81 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Beta strand 101 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Beta strand 110 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Beta strand 120 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Beta strand 129 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Helix 135 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Beta strand 154 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Helix 170 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Helix 180 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Beta strand 194 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Beta strand 209 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Helix 217 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Beta strand 221 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Helix 228 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Beta strand 248 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Helix 256 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Beta strand 262 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Beta strand 276 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +P38765 UniProtKB Beta strand 284 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YM5 +##sequence-region P38690 1 423 +P38690 UniProtKB Chain 1 423 . . . ID=PRO_0000109779;Note=Uncharacterized protein YHR033W +P38690 UniProtKB Domain 315 406 . . . Note=PUA +P38690 UniProtKB Nucleotide binding 170 171 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38690 UniProtKB Nucleotide binding 214 220 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38690 UniProtKB Binding site 51 51 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38690 UniProtKB Binding site 138 138 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38690 UniProtKB Binding site 150 150 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38690 UniProtKB Sequence conflict 117 117 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38769 1 630 +P38769 UniProtKB Chain 1 630 . . . ID=PRO_0000202891;Note=Uncharacterized protein YHR035W +##sequence-region P38842 1 239 +P38842 UniProtKB Chain 1 239 . . . ID=PRO_0000202921;Note=UPF0641 membrane protein YHR140W +P38842 UniProtKB Topological domain 1 11 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38842 UniProtKB Transmembrane 12 31 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38842 UniProtKB Topological domain 32 45 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38842 UniProtKB Transmembrane 46 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38842 UniProtKB Topological domain 67 99 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38842 UniProtKB Transmembrane 100 120 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38842 UniProtKB Topological domain 121 125 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38842 UniProtKB Transmembrane 126 146 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38842 UniProtKB Topological domain 147 162 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38842 UniProtKB Transmembrane 163 183 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38842 UniProtKB Topological domain 184 204 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38842 UniProtKB Transmembrane 205 225 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38842 UniProtKB Topological domain 226 239 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q02598 1 104 +Q02598 UniProtKB Chain 1 104 . . . ID=PRO_0000245404;Note=Uncharacterized protein YIL014C-A +##sequence-region A0A023PXN9 1 150 +A0A023PXN9 UniProtKB Chain 1 150 . . . ID=PRO_0000431040;Note=Putative uncharacterized membrane protein YIL171W-A +A0A023PXN9 UniProtKB Transmembrane 15 35 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXN9 UniProtKB Transmembrane 51 71 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXN9 UniProtKB Transmembrane 73 93 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXN9 UniProtKB Transmembrane 110 130 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40521 1 94 +P40521 UniProtKB Chain 1 94 . . . ID=PRO_0000202986;Note=Putative uncharacterized protein YIL058W +P40521 UniProtKB Natural variant 7 7 . . . Note=In strain: CEN.PK 113-7D. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14654430;Dbxref=PMID:14654430 +P40521 UniProtKB Natural variant 40 40 . . . Note=In strain: CEN.PK 113-7D. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14654430;Dbxref=PMID:14654430 +P40521 UniProtKB Natural variant 49 49 . . . Note=In strain: CEN.PK 113-7D. V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14654430;Dbxref=PMID:14654430 +P40521 UniProtKB Natural variant 70 71 . . . Note=In strain: CEN.PK 113-7D. IL->VF +##sequence-region P40519 1 144 +P40519 UniProtKB Chain 1 144 . . . ID=PRO_0000202984;Note=Uncharacterized protein YIL060W +P40519 UniProtKB Transmembrane 72 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40455 1 235 +P40455 UniProtKB Chain 1 235 . . . ID=PRO_0000202956;Note=Uncharacterized protein YIL152W +##sequence-region P53093 1 235 +P53093 UniProtKB Chain 1 235 . . . ID=PRO_0000202721;Note=Protein YIP4 +P53093 UniProtKB Transmembrane 89 109 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53093 UniProtKB Transmembrane 114 134 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53093 UniProtKB Transmembrane 145 165 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53093 UniProtKB Transmembrane 186 206 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53093 UniProtKB Transmembrane 215 235 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CX74 1 440 +P0CX74 UniProtKB Chain 1 440 . . . ID=PRO_0000203496;Note=Transposon Ty1-JR1 Gag polyprotein +P0CX74 UniProtKB Chain 1 401 . . . ID=PRO_0000279086;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX74 UniProtKB Peptide 402 440 . . . ID=PRO_0000279087;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX74 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX74 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0CX74 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX74 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region Q3E828 1 52 +Q3E828 UniProtKB Chain 1 52 . . . ID=PRO_0000245410;Note=UPF0618 protein YJL127C-B +Q3E828 UniProtKB Transmembrane 28 46 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E801 1 27 +Q3E801 UniProtKB Chain 1 27 . . . ID=PRO_0000245408;Note=Uncharacterized protein YJL136W-A +##sequence-region P0C5N9 1 73 +P0C5N9 UniProtKB Chain 1 73 . . . ID=PRO_0000309037;Note=Putative uncharacterized protein YJL156W-A +P0C5N9 UniProtKB Transmembrane 54 72 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47023 1 414 +P47023 UniProtKB Chain 1 414 . . . ID=PRO_0000203501;Note=Transposon Ty4-J Gag polyprotein +P47023 UniProtKB Coiled coil 39 115 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47121 1 122 +P47121 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47121 UniProtKB Chain 19 122 . . . ID=PRO_0000014334;Note=Putative uncharacterized protein YJR071W +P47121 UniProtKB Glycosylation 15 15 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47024 1 1803 +P47024 UniProtKB Chain 1 1803 . . . ID=PRO_0000203502;Note=Transposon Ty4-J Gag-Pol polyprotein +P47024 UniProtKB Domain 620 787 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47024 UniProtKB Domain 1376 1511 . . . Note=Reverse transcriptase Ty1/copia-type +P47024 UniProtKB Domain 1645 1791 . . . Note=RNase H Ty1/copia-type +P47024 UniProtKB Region 382 502 . . . Note=Ty4 protease +P47024 UniProtKB Region 540 600 . . . Note=Integrase-type zinc finger-like +P47024 UniProtKB Coiled coil 39 115 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47024 UniProtKB Active site 415 415 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47024 UniProtKB Metal binding 631 631 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47024 UniProtKB Metal binding 696 696 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47024 UniProtKB Metal binding 1384 1384 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47024 UniProtKB Metal binding 1463 1463 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47024 UniProtKB Metal binding 1464 1464 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47024 UniProtKB Metal binding 1645 1645 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47024 UniProtKB Metal binding 1687 1687 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47024 UniProtKB Metal binding 1721 1721 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P47024 UniProtKB Sequence conflict 452 452 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47024 UniProtKB Sequence conflict 684 684 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47024 UniProtKB Sequence conflict 920 920 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47024 UniProtKB Sequence conflict 1020 1020 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47024 UniProtKB Sequence conflict 1803 1803 . . . Note=Y->YLINEVLNTQISVEVQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47152 1 169 +P47152 UniProtKB Chain 1 169 . . . ID=PRO_0000203114;Note=Uncharacterized protein YJR115W +##sequence-region P47157 1 116 +P47157 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47157 UniProtKB Chain 20 116 . . . ID=PRO_0000014335;Note=Putative uncharacterized protein YJR120W +P47157 UniProtKB Sequence conflict 111 111 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47162 1 119 +P47162 UniProtKB Chain 1 119 . . . ID=PRO_0000203119;Note=Uncharacterized protein YJR128W +##sequence-region P40361 1 888 +P40361 UniProtKB Chain 1 888 . . . ID=PRO_0000194416;Note=Inactive deaminase YJL070C +P40361 UniProtKB Modified residue 9 9 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40361 UniProtKB Modified residue 41 41 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40361 UniProtKB Modified residue 178 178 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40361 UniProtKB Modified residue 180 180 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P47009 1 104 +P47009 UniProtKB Chain 1 104 . . . ID=PRO_0000203034;Note=Uncharacterized protein YJL144W +P47009 UniProtKB Compositional bias 72 78 . . . Note=Poly-Asn +##sequence-region P46996 1 555 +P46996 UniProtKB Chain 1 555 . . . ID=PRO_0000203027;Note=Uncharacterized membrane protein YJL163C +P46996 UniProtKB Topological domain 1 83 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Transmembrane 84 104 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Topological domain 105 125 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Transmembrane 126 146 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Topological domain 147 188 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Transmembrane 189 209 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Topological domain 210 229 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Transmembrane 230 250 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Topological domain 251 257 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Transmembrane 258 278 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Topological domain 279 356 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Transmembrane 357 377 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Topological domain 378 386 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Transmembrane 387 407 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Topological domain 408 428 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Transmembrane 429 449 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Topological domain 450 459 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Transmembrane 460 480 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Topological domain 481 491 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Transmembrane 492 512 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Topological domain 513 523 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Transmembrane 524 544 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46996 UniProtKB Topological domain 545 555 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P46986 1 105 +P46986 UniProtKB Chain 1 105 . . . ID=PRO_0000203022;Note=Putative uncharacterized protein YJL182C +P46986 UniProtKB Transmembrane 41 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39532 1 115 +P39532 UniProtKB Chain 1 115 . . . ID=PRO_0000203016;Note=Putative uncharacterized protein YJL202C +P39532 UniProtKB Transmembrane 69 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40889 1 1758 +P40889 UniProtKB Chain 1 1758 . . . ID=PRO_0000102208;Note=Y' element ATP-dependent helicase YJL225C +P40889 UniProtKB Domain 668 845 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P40889 UniProtKB Domain 900 1051 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P40889 UniProtKB Nucleotide binding 681 688 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +##sequence-region P47094 1 133 +P47094 UniProtKB Chain 1 133 . . . ID=PRO_0000203089;Note=Putative uncharacterized protein YJR023C +P47094 UniProtKB Transmembrane 8 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47094 UniProtKB Transmembrane 46 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47094 UniProtKB Compositional bias 10 30 . . . Note=Poly-Leu +P47094 UniProtKB Sequence conflict 28 28 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q8TGM9 1 89 +Q8TGM9 UniProtKB Chain 1 89 . . . ID=PRO_0000299767;Note=Putative uncharacterized protein YKR075W-A +Q8TGM9 UniProtKB Transmembrane 39 61 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGN0 1 38 +Q8TGN0 UniProtKB Chain 1 38 . . . ID=PRO_0000299766;Note=Putative uncharacterized protein YKL156C-A +##sequence-region P36138 1 183 +P36138 UniProtKB Chain 1 183 . . . ID=PRO_0000203213;Note=Uncharacterized protein YKR045C +P36138 UniProtKB Compositional bias 25 29 . . . Note=Poly-Thr +P36138 UniProtKB Compositional bias 99 108 . . . Note=Gln-rich +P36138 UniProtKB Cross-link 21 21 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P36151 1 352 +P36151 UniProtKB Chain 1 352 . . . ID=PRO_0000203218;Note=Uncharacterized protein YKR070W +P36151 UniProtKB Beta strand 14 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Turn 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Beta strand 24 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Helix 34 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Beta strand 48 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Helix 59 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Helix 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Helix 84 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Turn 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Beta strand 94 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Helix 104 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Beta strand 114 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Helix 119 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Helix 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Helix 137 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Turn 148 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Beta strand 157 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Helix 167 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Beta strand 200 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Beta strand 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Beta strand 212 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Helix 220 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Helix 249 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Beta strand 268 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RF6 +P36151 UniProtKB Turn 285 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Beta strand 290 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Turn 300 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Helix 303 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Beta strand 313 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Beta strand 318 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Beta strand 334 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +P36151 UniProtKB Helix 340 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KC2 +##sequence-region P40544 1 346 +P40544 UniProtKB Chain 1 346 . . . ID=PRO_0000213698;Note=Zinc transporter YKE4 +P40544 UniProtKB Topological domain 1 2 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Transmembrane 3 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Topological domain 24 69 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Transmembrane 70 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Topological domain 91 99 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Transmembrane 100 120 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Topological domain 121 126 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Transmembrane 127 147 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Topological domain 148 202 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Transmembrane 203 223 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Topological domain 224 252 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Transmembrane 253 273 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Topological domain 274 290 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Transmembrane 291 311 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Topological domain 312 322 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Transmembrane 323 343 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Topological domain 344 346 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Glycosylation 184 184 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Glycosylation 274 274 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40544 UniProtKB Glycosylation 285 285 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P34251 1 309 +P34251 UniProtKB Chain 1 309 . . . ID=PRO_0000203158;Note=Uncharacterized oxidoreductase YKL107W +P34251 UniProtKB Transmembrane 23 39 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36073 1 130 +P36073 UniProtKB Chain 1 130 . . . ID=PRO_0000203156;Note=Putative uncharacterized protein YKL115C +##sequence-region P36065 1 132 +P36065 UniProtKB Chain 1 132 . . . ID=PRO_0000203148;Note=Putative uncharacterized protein YKL136W +##sequence-region P36042 1 193 +P36042 UniProtKB Chain 1 193 . . . ID=PRO_0000203134;Note=Putative uncharacterized protein YKL202W +P36042 UniProtKB Compositional bias 100 181 . . . Note=Leu/Phe/Pro/Ser-rich +##sequence-region Q02203 1 525 +Q02203 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02203 UniProtKB Chain 22 525 . . . ID=PRO_0000203192;Note=Uncharacterized protein YKR005C +Q02203 UniProtKB Topological domain 22 448 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02203 UniProtKB Transmembrane 449 469 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02203 UniProtKB Topological domain 470 525 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02203 UniProtKB Compositional bias 304 361 . . . Note=Thr-rich +##sequence-region Q8TGM8 1 30 +Q8TGM8 UniProtKB Chain 1 30 . . . ID=PRO_0000299601;Note=Putative uncharacterized protein YLL019W-A +##sequence-region Q07865 1 126 +Q07865 UniProtKB Chain 1 126 . . . ID=PRO_0000299604;Note=Putative uncharacterized protein YLL037W +Q07865 UniProtKB Transmembrane 5 25 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07989 1 106 +Q07989 UniProtKB Chain 1 106 . . . ID=PRO_0000299608;Note=Putative uncharacterized protein YLR041W +##sequence-region Q12253 1 270 +Q12253 UniProtKB Chain 1 270 . . . ID=PRO_0000247195;Note=Uncharacterized membrane protein YLR046C +Q12253 UniProtKB Topological domain 1 37 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12253 UniProtKB Transmembrane 38 58 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12253 UniProtKB Topological domain 59 65 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12253 UniProtKB Transmembrane 66 86 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12253 UniProtKB Topological domain 87 93 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12253 UniProtKB Transmembrane 94 114 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12253 UniProtKB Topological domain 115 140 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12253 UniProtKB Transmembrane 141 161 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12253 UniProtKB Topological domain 162 181 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12253 UniProtKB Transmembrane 182 202 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12253 UniProtKB Topological domain 203 220 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12253 UniProtKB Transmembrane 221 241 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12253 UniProtKB Topological domain 242 270 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12026 1 108 +Q12026 UniProtKB Chain 1 108 . . . ID=PRO_0000247206;Note=Putative uncharacterized protein YLR053C +##sequence-region Q12177 1 298 +Q12177 UniProtKB Chain 1 298 . . . ID=PRO_0000247152;Note=Uncharacterized protein YLL056C +##sequence-region P25575 1 107 +P25575 UniProtKB Chain 1 107 . . . ID=PRO_0000202548;Note=Putative uncharacterized protein YCL046W +##sequence-region P25602 1 247 +P25602 UniProtKB Chain 1 247 . . . ID=PRO_0000202558;Note=Putative uncharacterized protein YCL076W +##sequence-region P37265 1 110 +P37265 UniProtKB Chain 1 110 . . . ID=PRO_0000202567;Note=Uncharacterized protein YCR041W +P37265 UniProtKB Transmembrane 32 52 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37265 UniProtKB Transmembrane 57 77 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37265 UniProtKB Transmembrane 90 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P25652 1 171 +P25652 UniProtKB Chain 1 171 . . . ID=PRO_0000202579;Note=Putative uncharacterized protein YCR087W +##sequence-region Q12115 1 100 +Q12115 UniProtKB Chain 1 100 . . . ID=PRO_0000299844;Note=Putative uncharacterized protein YDL016C +Q12115 UniProtKB Compositional bias 41 95 . . . Note=Ser-rich +##sequence-region P0C5L6 1 82 +P0C5L6 UniProtKB Chain 1 82 . . . ID=PRO_0000309014;Note=Uncharacterized protein YDL022C-A +##sequence-region A0A023PXH9 1 235 +A0A023PXH9 UniProtKB Chain 1 235 . . . ID=PRO_0000430981;Note=Putative uncharacterized membrane protein YDR149C +A0A023PXH9 UniProtKB Transmembrane 167 187 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXH9 UniProtKB Transmembrane 190 210 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12394 1 121 +Q12394 UniProtKB Chain 1 121 . . . ID=PRO_0000299857;Note=Putative uncharacterized protein YDL152W +Q12394 UniProtKB Transmembrane 65 84 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12394 UniProtKB Compositional bias 5 54 . . . Note=Ser-rich +##sequence-region P0C2I3 1 1755 +P0C2I3 UniProtKB Chain 1 1755 . . . ID=PRO_0000279032;Note=Transposon Ty1-DR6 Gag-Pol polyprotein +P0C2I3 UniProtKB Chain 1 401 . . . ID=PRO_0000279033;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I3 UniProtKB Chain 402 582 . . . ID=PRO_0000279034;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I3 UniProtKB Chain 583 1217 . . . ID=PRO_0000279035;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I3 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279036;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I3 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I3 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +P0C2I3 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +P0C2I3 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I3 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +P0C2I3 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I3 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0C2I3 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +P0C2I3 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I3 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I3 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I3 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I3 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I3 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I3 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I3 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I3 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I3 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I3 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I3 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region A0A023PXI4 1 105 +A0A023PXI4 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXI4 UniProtKB Chain 25 105 . . . ID=PRO_0000430983;Note=Putative uncharacterized protein YDR203W +##sequence-region Q03480 1 137 +Q03480 UniProtKB Chain 1 137 . . . ID=PRO_0000299875;Note=Uncharacterized protein YDR209C +Q03480 UniProtKB Transmembrane 111 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q00590 1 100 +Q00590 UniProtKB Chain 1 100 . . . ID=PRO_0000299748;Note=Putative uncharacterized protein YDL213W-A +Q00590 UniProtKB Transmembrane 68 88 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12392 1 438 +Q12392 UniProtKB Chain 1 438 . . . ID=PRO_0000279289;Note=Transposon Ty2-DR1 Gag polyprotein +Q12392 UniProtKB Chain 1 397 . . . ID=PRO_0000279290;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12392 UniProtKB Peptide 398 438 . . . ID=PRO_0000279291;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12392 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12392 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q03483 1 438 +Q03483 UniProtKB Chain 1 438 . . . ID=PRO_0000279297;Note=Transposon Ty2-DR2 Gag polyprotein +Q03483 UniProtKB Chain 1 397 . . . ID=PRO_0000279298;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03483 UniProtKB Peptide 398 438 . . . ID=PRO_0000279299;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03483 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03483 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q07738 1 123 +Q07738 UniProtKB Chain 1 123 . . . ID=PRO_0000242485;Note=Uncharacterized protein YDL241W +##sequence-region Q06640 1 478 +Q06640 UniProtKB Chain 1 478 . . . ID=PRO_0000253805;Note=F-box protein YDR306C +Q06640 UniProtKB Domain 112 173 . . . Note=F-box +Q06640 UniProtKB Compositional bias 81 90 . . . Note=Poly-Ser +##sequence-region P87287 1 132 +P87287 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P87287 UniProtKB Chain 25 132 . . . ID=PRO_0000253845;Note=Uncharacterized protein YDR366C +P87287 UniProtKB Transmembrane 75 95 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P87287 UniProtKB Transmembrane 112 132 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0C5M2 1 81 +P0C5M2 UniProtKB Chain 1 81 . . . ID=PRO_0000309020;Note=Putative uncharacterized protein YDR406W-A +P0C5M2 UniProtKB Transmembrane 1 21 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C5M2 UniProtKB Transmembrane 27 47 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q2V2P7 1 80 +Q2V2P7 UniProtKB Chain 1 80 . . . ID=PRO_0000253852;Note=Uncharacterized protein YDR461C-A +##sequence-region P87272 1 115 +P87272 UniProtKB Chain 1 115 . . . ID=PRO_0000299900;Note=Putative uncharacterized protein YDR509W +P87272 UniProtKB Transmembrane 5 25 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P87272 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0C5M4 1 75 +P0C5M4 UniProtKB Chain 1 75 . . . ID=PRO_0000309022;Note=Putative uncharacterized protein YDL185C-A +##sequence-region Q12147 1 103 +Q12147 UniProtKB Chain 1 103 . . . ID=PRO_0000299847;Note=Putative uncharacterized protein YDL026W +Q12147 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12147 UniProtKB Transmembrane 65 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12426 1 110 +Q12426 UniProtKB Chain 1 110 . . . ID=PRO_0000299868;Note=Uncharacterized protein YDR010C +##sequence-region A0A023PXI8 1 105 +A0A023PXI8 UniProtKB Chain 1 105 . . . ID=PRO_0000430989;Note=Putative uncharacterized protein YER006C-A +##sequence-region Q8TGP2 1 70 +Q8TGP2 UniProtKB Chain 1 70 . . . ID=PRO_0000299911;Note=Putative uncharacterized protein YER023C-A +##sequence-region A0A023PZF5 1 109 +A0A023PZF5 UniProtKB Chain 1 109 . . . ID=PRO_0000430992;Note=Putative uncharacterized protein YER046W-A +##sequence-region A0A023PXC7 1 143 +A0A023PXC7 UniProtKB Chain 1 143 . . . ID=PRO_0000430994;Note=Putative uncharacterized membrane protein YER068C-A +A0A023PXC7 UniProtKB Transmembrane 20 39 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXC7 UniProtKB Transmembrane 113 135 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CX16 1 216 +P0CX16 UniProtKB Chain 1 216 . . . ID=PRO_0000268170;Note=Putative uncharacterized protein YEL076C-A +##sequence-region A0A023PZB8 1 112 +A0A023PZB8 UniProtKB Chain 1 112 . . . ID=PRO_0000430995;Note=Putative uncharacterized membrane protein YER079C-A +A0A023PZB8 UniProtKB Transmembrane 55 75 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZB8 UniProtKB Transmembrane 91 111 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P87191 1 123 +P87191 UniProtKB Chain 1 123 . . . ID=PRO_0000299914;Note=Putative uncharacterized protein YER119C-A +##sequence-region A0A023PYF4 1 145 +A0A023PYF4 UniProtKB Signal peptide 1 26 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PYF4 UniProtKB Chain 27 145 . . . ID=PRO_0000431001;Note=Uncharacterized protein YER145C-A +##sequence-region Q8TGR3 1 71 +Q8TGR3 UniProtKB Chain 1 71 . . . ID=PRO_0000299915;Note=Putative uncharacterized protein YER158W-A +Q8TGR3 UniProtKB Transmembrane 44 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39961 1 794 +P39961 UniProtKB Chain 1 794 . . . ID=PRO_0000114995;Note=Uncharacterized transcriptional regulatory protein YER184C +P39961 UniProtKB DNA binding 18 44 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P39961 UniProtKB Metal binding 18 18 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39961 UniProtKB Metal binding 18 18 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39961 UniProtKB Metal binding 21 21 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39961 UniProtKB Metal binding 28 28 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39961 UniProtKB Metal binding 34 34 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39961 UniProtKB Metal binding 34 34 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39961 UniProtKB Metal binding 37 37 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39961 UniProtKB Metal binding 44 44 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P39953 1 335 +P39953 UniProtKB Chain 1 335 . . . ID=PRO_0000090694;Note=Mitochondrial nicotinamide adenine dinucleotide transporter 2 +P39953 UniProtKB Transmembrane 42 62 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39953 UniProtKB Transmembrane 104 124 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39953 UniProtKB Transmembrane 142 162 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39953 UniProtKB Transmembrane 198 218 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39953 UniProtKB Transmembrane 247 267 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39953 UniProtKB Transmembrane 298 318 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39953 UniProtKB Repeat 36 128 . . . Note=Solcar 1 +P39953 UniProtKB Repeat 136 225 . . . Note=Solcar 2 +P39953 UniProtKB Repeat 241 329 . . . Note=Solcar 3 +##sequence-region P40095 1 573 +P40095 UniProtKB Chain 1 573 . . . ID=PRO_0000202656;Note=Uncharacterized protein YER158C +P40095 UniProtKB Repeat 102 103 . . . Note=1 +P40095 UniProtKB Repeat 104 105 . . . Note=2 +P40095 UniProtKB Repeat 106 107 . . . Note=3 +P40095 UniProtKB Repeat 108 109 . . . Note=4 +P40095 UniProtKB Repeat 110 111 . . . Note=5 +P40095 UniProtKB Repeat 112 113 . . . Note=6 +P40095 UniProtKB Repeat 114 115 . . . Note=7 +P40095 UniProtKB Repeat 116 117 . . . Note=8 +P40095 UniProtKB Repeat 118 119 . . . Note=9 +P40095 UniProtKB Repeat 120 121 . . . Note=10 +P40095 UniProtKB Region 102 121 . . . Note=10 X 2 AA tandem repeats of N-M +P40095 UniProtKB Glycosylation 63 63 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40095 UniProtKB Glycosylation 123 123 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40095 UniProtKB Glycosylation 236 236 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40095 UniProtKB Glycosylation 437 437 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40095 UniProtKB Glycosylation 442 442 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40095 UniProtKB Glycosylation 498 498 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40095 UniProtKB Glycosylation 535 535 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40095 UniProtKB Glycosylation 541 541 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0C5N0 1 62 +P0C5N0 UniProtKB Chain 1 62 . . . ID=PRO_0000309028;Note=Uncharacterized protein YFR010W-A +P0C5N0 UniProtKB Transmembrane 9 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C5N0 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PXD9 1 105 +A0A023PXD9 UniProtKB Chain 1 105 . . . ID=PRO_0000431010;Note=Putative uncharacterized membrane protein YFL015W-A +A0A023PXD9 UniProtKB Transmembrane 25 47 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGU3 1 33 +Q8TGU3 UniProtKB Chain 1 33 . . . ID=PRO_0000299659;Note=Putative uncharacterized protein YFL031C-A +##sequence-region Q12085 1 440 +Q12085 UniProtKB Chain 1 440 . . . ID=PRO_0000279058;Note=Transposon Ty1-GR1 Gag polyprotein +Q12085 UniProtKB Chain 1 401 . . . ID=PRO_0000279059;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12085 UniProtKB Peptide 402 440 . . . ID=PRO_0000279060;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12085 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12085 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12085 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region Q12485 1 440 +Q12485 UniProtKB Chain 1 440 . . . ID=PRO_0000279066;Note=Transposon Ty1-GR2 Gag polyprotein +Q12485 UniProtKB Chain 1 401 . . . ID=PRO_0000279067;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12485 UniProtKB Peptide 402 440 . . . ID=PRO_0000279068;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12485 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12485 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q12485 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12485 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region Q12269 1 1755 +Q12269 UniProtKB Chain 1 1755 . . . ID=PRO_0000279061;Note=Transposon Ty1-GR2 Gag-Pol polyprotein +Q12269 UniProtKB Chain 1 401 . . . ID=PRO_0000279062;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12269 UniProtKB Chain 402 582 . . . ID=PRO_0000279063;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12269 UniProtKB Chain 583 1217 . . . ID=PRO_0000279064;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12269 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279065;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12269 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12269 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +Q12269 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +Q12269 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12269 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q12269 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12269 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q12269 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q12269 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12269 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12269 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12269 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12269 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12269 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12269 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12269 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12269 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12269 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12269 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12269 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region P53209 1 190 +P53209 UniProtKB Chain 1 190 . . . ID=PRO_0000202783;Note=Uncharacterized membrane protein YGR016W +P53209 UniProtKB Topological domain 1 55 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53209 UniProtKB Transmembrane 56 76 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53209 UniProtKB Topological domain 77 80 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53209 UniProtKB Transmembrane 81 101 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53209 UniProtKB Topological domain 102 123 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53209 UniProtKB Transmembrane 124 144 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53209 UniProtKB Topological domain 145 149 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53209 UniProtKB Transmembrane 150 170 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53209 UniProtKB Topological domain 171 190 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53211 1 109 +P53211 UniProtKB Chain 1 109 . . . ID=PRO_0000202785;Note=Uncharacterized protein YGR018C +##sequence-region P53231 1 118 +P53231 UniProtKB Chain 1 118 . . . ID=PRO_0000202797;Note=Uncharacterized protein YGR050C +##sequence-region P0CX62 1 438 +P0CX62 UniProtKB Chain 1 438 . . . ID=PRO_0000409814;Note=Transposon Ty2-GR2 Gag polyprotein +P0CX62 UniProtKB Chain 1 397 . . . ID=PRO_0000409815;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX62 UniProtKB Peptide 398 438 . . . ID=PRO_0000409816;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX62 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX62 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38722 1 271 +P38722 UniProtKB Chain 1 271 . . . ID=PRO_0000202876;Note=Uncharacterized protein YHL049C +##sequence-region A0A023PXG3 1 133 +A0A023PXG3 UniProtKB Chain 1 133 . . . ID=PRO_0000431042;Note=Putative uncharacterized membrane protein YIL156W-A +A0A023PXG3 UniProtKB Transmembrane 13 33 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXG3 UniProtKB Transmembrane 73 93 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40539 1 132 +P40539 UniProtKB Chain 1 132 . . . ID=PRO_0000202997;Note=Putative uncharacterized protein YIL028W +##sequence-region P40448 1 117 +P40448 UniProtKB Chain 1 117 . . . ID=PRO_0000202951;Note=Uncharacterized protein YIL163C +##sequence-region P40442 1 995 +P40442 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40442 UniProtKB Chain 24 995 . . . ID=PRO_0000014330;Note=Putative uncharacterized protein YIL169C +P40442 UniProtKB Domain 26 253 . . . Note=Methyl-accepting transducer;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00284 +P40442 UniProtKB Glycosylation 28 28 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40442 UniProtKB Glycosylation 35 35 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40442 UniProtKB Glycosylation 468 468 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40442 UniProtKB Glycosylation 664 664 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGT2 1 49 +Q8TGT2 UniProtKB Chain 1 49 . . . ID=PRO_0000245420;Note=Uncharacterized protein YKL096C-B +Q8TGT2 UniProtKB Transmembrane 31 48 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36128 1 141 +P36128 UniProtKB Chain 1 141 . . . ID=PRO_0000203207;Note=Putative uncharacterized protein YKR033C +##sequence-region P36086 1 256 +P36086 UniProtKB Chain 1 256 . . . ID=PRO_0000203171;Note=Uncharacterized oxidoreductase YKL071W +P36086 UniProtKB Nucleotide binding 13 19 . . . Note=NAD or NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36086 UniProtKB Active site 164 164 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36086 UniProtKB Binding site 148 148 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P34248 1 587 +P34248 UniProtKB Chain 1 587 . . . ID=PRO_0000073915;Note=Probable intramembrane protease YKL100C +P34248 UniProtKB Topological domain 1 85 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Transmembrane 86 106 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Topological domain 107 156 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Transmembrane 157 177 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Topological domain 178 192 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Transmembrane 193 213 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Topological domain 214 303 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Transmembrane 304 324 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Topological domain 325 328 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Transmembrane 329 349 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Topological domain 350 351 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Transmembrane 352 372 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Topological domain 373 401 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Transmembrane 402 422 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Topological domain 423 450 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Transmembrane 451 471 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Topological domain 472 475 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Transmembrane 476 496 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Topological domain 497 587 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34248 UniProtKB Motif 477 479 . . . Note=PAL +P34248 UniProtKB Compositional bias 550 587 . . . Note=Asp/Glu-rich (highly acidic) +P34248 UniProtKB Active site 366 366 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P34248 UniProtKB Active site 411 411 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P36072 1 103 +P36072 UniProtKB Chain 1 103 . . . ID=PRO_0000203155;Note=Putative uncharacterized protein YKL118W +##sequence-region P36058 1 169 +P36058 UniProtKB Chain 1 169 . . . ID=PRO_0000203145;Note=Putative uncharacterized protein YKL153W +##sequence-region P36114 1 725 +P36114 UniProtKB Chain 1 725 . . . ID=PRO_0000203198;Note=Mitochondrial outer membrane protein YKR018C +P36114 UniProtKB Transmembrane 296 316 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36114 UniProtKB Transmembrane 341 361 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36114 UniProtKB Modified residue 196 196 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36114 UniProtKB Modified residue 246 246 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36114 UniProtKB Modified residue 377 377 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36114 UniProtKB Modified residue 380 380 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P36114 UniProtKB Beta strand 55 57 . . . . +##sequence-region P35995 1 705 +P35995 UniProtKB Chain 1 705 . . . ID=PRO_0000115000;Note=Uncharacterized transcriptional regulatory protein YKL222C +P35995 UniProtKB DNA binding 24 52 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +##sequence-region Q02209 1 353 +Q02209 UniProtKB Chain 1 353 . . . ID=PRO_0000203194;Note=Uncharacterized protein YKR011C +##sequence-region Q3E814 1 58 +Q3E814 UniProtKB Chain 1 58 . . . ID=PRO_0000247097;Note=Uncharacterized protein YLL006W-A +Q3E814 UniProtKB Transmembrane 12 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0C2I6 1 1755 +P0C2I6 UniProtKB Chain 1 1755 . . . ID=PRO_0000279104;Note=Transposon Ty1-LR3 Gag-Pol polyprotein +P0C2I6 UniProtKB Chain 1 401 . . . ID=PRO_0000279105;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I6 UniProtKB Chain 402 582 . . . ID=PRO_0000279106;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I6 UniProtKB Chain 583 1217 . . . ID=PRO_0000279107;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I6 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279108;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I6 UniProtKB Domain 660 829 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I6 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +P0C2I6 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +P0C2I6 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I6 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +P0C2I6 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I6 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0C2I6 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +P0C2I6 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I6 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I6 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I6 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I6 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I6 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I6 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I6 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I6 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I6 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I6 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I6 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region P0CY02 1 43 +P0CY02 UniProtKB Chain 1 43 . . . ID=PRO_0000410458;Note=Uncharacterized protein YLR154C-H +##sequence-region Q06235 1 118 +Q06235 UniProtKB Chain 1 118 . . . ID=PRO_0000262878;Note=Protein YLR162W +Q06235 UniProtKB Transmembrane 38 58 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06251 1 628 +Q06251 UniProtKB Chain 1 628 . . . ID=PRO_0000247127;Note=Uncharacterized protein YLR177W +Q06251 UniProtKB Domain 472 565 . . . Note=PSP1 C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00744 +Q06251 UniProtKB Compositional bias 154 169 . . . Note=Poly-Gln +Q06251 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q06251 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06251 UniProtKB Modified residue 34 34 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06251 UniProtKB Modified residue 84 84 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06251 UniProtKB Modified residue 235 235 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region Q06267 1 115 +Q06267 UniProtKB Chain 1 115 . . . ID=PRO_0000299620;Note=Putative uncharacterized protein YLR184W +##sequence-region Q05777 1 254 +Q05777 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05777 UniProtKB Chain 18 232 . . . ID=PRO_0000247130;Note=Cell wall protein YLR194C +Q05777 UniProtKB Propeptide 233 254 . . . ID=PRO_0000247131;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05777 UniProtKB Compositional bias 104 206 . . . Note=Ser-rich +Q05777 UniProtKB Lipidation 232 232 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05777 UniProtKB Glycosylation 229 229 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0C2J4 1 438 +P0C2J4 UniProtKB Chain 1 438 . . . ID=PRO_0000279329;Note=Transposon Ty2-LR1 Gag polyprotein +P0C2J4 UniProtKB Chain 1 397 . . . ID=PRO_0000279330;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J4 UniProtKB Peptide 398 438 . . . ID=PRO_0000279331;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J4 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J4 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P0C2J3 1 1770 +P0C2J3 UniProtKB Chain 1 1770 . . . ID=PRO_0000279324;Note=Transposon Ty2-LR1 Gag-Pol polyprotein +P0C2J3 UniProtKB Chain 1 397 . . . ID=PRO_0000279325;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J3 UniProtKB Chain 398 578 . . . ID=PRO_0000279326;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J3 UniProtKB Chain 579 1232 . . . ID=PRO_0000279327;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J3 UniProtKB Chain 1233 1770 . . . ID=PRO_0000279328;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J3 UniProtKB Domain 656 831 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J3 UniProtKB Domain 1353 1491 . . . Note=Reverse transcriptase Ty1/copia-type +P0C2J3 UniProtKB Domain 1625 1767 . . . Note=RNase H Ty1/copia-type +P0C2J3 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J3 UniProtKB Region 579 636 . . . Note=Integrase-type zinc finger-like +P0C2J3 UniProtKB Motif 1193 1227 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J3 UniProtKB Active site 457 457 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J3 UniProtKB Metal binding 667 667 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J3 UniProtKB Metal binding 732 732 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J3 UniProtKB Metal binding 1361 1361 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J3 UniProtKB Metal binding 1442 1442 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J3 UniProtKB Metal binding 1443 1443 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J3 UniProtKB Metal binding 1625 1625 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J3 UniProtKB Metal binding 1667 1667 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J3 UniProtKB Metal binding 1700 1700 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J3 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J3 UniProtKB Site 578 579 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J3 UniProtKB Site 1232 1233 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q8TGR0 1 75 +Q8TGR0 UniProtKB Chain 1 75 . . . ID=PRO_0000299651;Note=Putative uncharacterized protein YLR437C-A +##sequence-region Q8TGM1 1 34 +Q8TGM1 UniProtKB Chain 1 34 . . . ID=PRO_0000299752;Note=Putative uncharacterized protein YLR399W-A +##sequence-region Q06057 1 63 +Q06057 UniProtKB Chain 1 63 . . . ID=PRO_0000299647;Note=Putative uncharacterized protein YLR402W +Q06057 UniProtKB Transmembrane 15 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E742 1 68 +Q3E742 UniProtKB Chain 1 68 . . . ID=PRO_0000247219;Note=Uncharacterized protein YLR412C-A +Q3E742 UniProtKB Compositional bias 19 59 . . . Note=Lys-rich +##sequence-region Q06695 1 132 +Q06695 UniProtKB Chain 1 132 . . . ID=PRO_0000299648;Note=Putative uncharacterized protein YLR416C +##sequence-region P0CX17 1 216 +P0CX17 UniProtKB Chain 1 216 . . . ID=PRO_0000409752;Note=Putative uncharacterized protein YLR464W +##sequence-region P0C5P8 1 28 +P0C5P8 UniProtKB Chain 1 28 . . . ID=PRO_0000309046;Note=Putative uncharacterized protein YLR149C-A +##sequence-region P0C5P9 1 54 +P0C5P9 UniProtKB Chain 1 54 . . . ID=PRO_0000309047;Note=Putative uncharacterized protein YLR154W-B +##sequence-region P38746 1 405 +P38746 UniProtKB Chain 1 405 . . . ID=PRO_0000122455;Note=Obg-like ATPase homolog +P38746 UniProtKB Domain 17 283 . . . Note=OBG-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +P38746 UniProtKB Nucleotide binding 26 31 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +P38746 UniProtKB Binding site 231 231 . . . Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38746 UniProtKB Sequence conflict 63 63 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38746 UniProtKB Sequence conflict 149 149 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38746 UniProtKB Sequence conflict 323 323 . . . Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q6B0Y8 1 125 +Q6B0Y8 UniProtKB Chain 1 125 . . . ID=PRO_0000299664;Note=Putative uncharacterized protein YML012C-A +Q6B0Y8 UniProtKB Compositional bias 7 21 . . . Note=Poly-Ser +##sequence-region P0C261 1 129 +P0C261 UniProtKB Chain 1 129 . . . ID=PRO_0000262741;Note=Putative uncharacterized membrane protein YML057C-A +P0C261 UniProtKB Topological domain 1 28 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C261 UniProtKB Transmembrane 29 49 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C261 UniProtKB Topological domain 50 54 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C261 UniProtKB Transmembrane 55 75 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C261 UniProtKB Topological domain 76 129 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q6B2I9 1 109 +Q6B2I9 UniProtKB Chain 1 109 . . . ID=PRO_0000299662;Note=Putative uncharacterized protein YML099W-A +Q6B2I9 UniProtKB Transmembrane 12 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGS8 1 64 +Q8TGS8 UniProtKB Chain 1 64 . . . ID=PRO_0000247786;Note=Uncharacterized protein YMR105W-A +##sequence-region P0CX76 1 440 +P0CX76 UniProtKB Chain 1 440 . . . ID=PRO_0000409803;Note=Transposon Ty1-ML2 Gag polyprotein +P0CX76 UniProtKB Chain 1 401 . . . ID=PRO_0000409804;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX76 UniProtKB Peptide 402 440 . . . ID=PRO_0000409805;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX76 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX76 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0CX76 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX76 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region Q6B0X1 1 177 +Q6B0X1 UniProtKB Chain 1 177 . . . ID=PRO_0000299670;Note=Putative uncharacterized protein YMR135W-A +##sequence-region P0C5Q3 1 49 +P0C5Q3 UniProtKB Chain 1 49 . . . ID=PRO_0000309051;Note=Uncharacterized protein YMR013C-A +P0C5Q3 UniProtKB Transmembrane 5 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04223 1 302 +Q04223 UniProtKB Chain 1 302 . . . ID=PRO_0000203300;Note=Uncharacterized protein YMR130W +##sequence-region P40207 1 237 +P40207 UniProtKB Chain 1 237 . . . ID=PRO_0000203302;Note=Uncharacterized protein YMR134W +P40207 UniProtKB Transmembrane 36 56 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E782 1 47 +Q3E782 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E782 UniProtKB Chain 26 47 . . . ID=PRO_0000247794;Note=Uncharacterized protein YMR247W-A +##sequence-region A0A023PXH2 1 111 +A0A023PXH2 UniProtKB Chain 1 111 . . . ID=PRO_0000431048;Note=Putative uncharacterized membrane protein YML031C-A +##sequence-region Q03236 1 431 +Q03236 UniProtKB Chain 1 431 . . . ID=PRO_0000203323;Note=Uncharacterized protein YMR187C +Q03236 UniProtKB Transmembrane 228 248 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03236 UniProtKB Transmembrane 279 299 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03236 UniProtKB Transmembrane 349 369 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03236 UniProtKB Transmembrane 388 408 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03695 1 313 +Q03695 UniProtKB Chain 1 313 . . . ID=PRO_0000203329;Note=Uncharacterized protein YMR206W +Q03695 UniProtKB Compositional bias 3 6 . . . Note=Poly-Ser +Q03695 UniProtKB Compositional bias 146 149 . . . Note=Poly-Gln +Q03695 UniProtKB Compositional bias 246 252 . . . Note=Poly-Ser +##sequence-region Q04018 1 355 +Q04018 UniProtKB Chain 1 355 . . . ID=PRO_0000203336;Note=Uncharacterized protein YMR244W +Q04018 UniProtKB Transmembrane 6 26 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04835 1 414 +Q04835 UniProtKB Chain 1 414 . . . ID=PRO_0000203340;Note=Uncharacterized membrane protein YMR253C +Q04835 UniProtKB Topological domain 1 66 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Transmembrane 67 87 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Topological domain 88 106 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Transmembrane 107 127 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Topological domain 128 144 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Transmembrane 145 167 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Topological domain 168 171 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Transmembrane 172 191 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Topological domain 192 199 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Transmembrane 200 220 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Topological domain 221 241 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Transmembrane 242 262 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Topological domain 263 269 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Transmembrane 270 290 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Topological domain 291 307 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Transmembrane 308 328 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Topological domain 329 357 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Transmembrane 358 378 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Topological domain 379 414 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04835 UniProtKB Domain 78 215 . . . Note=EamA 1 +Q04835 UniProtKB Domain 253 379 . . . Note=EamA 2 +Q04835 UniProtKB Cross-link 40 40 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q04835 UniProtKB Sequence conflict 278 278 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03263 1 540 +Q03263 UniProtKB Chain 1 540 . . . ID=PRO_0000173429;Note=Uncharacterized transporter YMR279C +Q03263 UniProtKB Topological domain 1 61 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Transmembrane 62 82 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Topological domain 83 108 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Transmembrane 109 129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Topological domain 130 131 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Transmembrane 132 152 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Topological domain 153 169 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Transmembrane 170 190 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Topological domain 191 203 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Transmembrane 204 224 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Topological domain 225 232 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Transmembrane 233 253 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Topological domain 254 272 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Transmembrane 273 293 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Topological domain 294 295 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Transmembrane 296 316 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Topological domain 317 334 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Transmembrane 335 355 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Topological domain 356 372 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Transmembrane 373 393 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Topological domain 394 398 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Transmembrane 399 419 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Topological domain 420 429 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Transmembrane 430 450 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Topological domain 451 461 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Transmembrane 462 482 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Topological domain 483 502 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Transmembrane 503 523 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03263 UniProtKB Topological domain 524 540 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0C5Q6 1 74 +P0C5Q6 UniProtKB Chain 1 74 . . . ID=PRO_0000309054;Note=Putative uncharacterized protein YMR194C-A +##sequence-region Q04898 1 105 +Q04898 UniProtKB Chain 1 105 . . . ID=PRO_0000114626;Note=Putative uncharacterized protein YMR321C +Q04898 UniProtKB Domain 1 101 . . . Note=Hcy-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00333 +##sequence-region Q03730 1 393 +Q03730 UniProtKB Chain 1 393 . . . ID=PRO_0000203261;Note=Uncharacterized vacuolar membrane protein YML018C +Q03730 UniProtKB Topological domain 1 17 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Transmembrane 18 38 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Topological domain 39 46 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Transmembrane 47 67 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Topological domain 68 132 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Transmembrane 133 153 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Topological domain 154 156 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Transmembrane 157 176 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Topological domain 177 182 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Transmembrane 183 200 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Topological domain 201 219 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Transmembrane 220 240 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Topological domain 241 257 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Transmembrane 258 278 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Topological domain 279 292 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Transmembrane 293 313 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Topological domain 314 321 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Transmembrane 322 342 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Topological domain 343 345 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Transmembrane 346 366 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Topological domain 367 393 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03730 UniProtKB Modified residue 93 93 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q03730 UniProtKB Sequence conflict 257 257 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03161 1 297 +Q03161 UniProtKB Chain 1 297 . . . ID=PRO_0000213035;Note=Glucose-6-phosphate 1-epimerase +Q03161 UniProtKB Active site 159 159 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16857670;Dbxref=PMID:16857670 +Q03161 UniProtKB Active site 264 264 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16857670;Dbxref=PMID:16857670 +Q03161 UniProtKB Binding site 57 57 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16857670;Dbxref=PMID:16857670 +Q03161 UniProtKB Binding site 81 81 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16857670;Dbxref=PMID:16857670 +Q03161 UniProtKB Binding site 86 86 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16857670;Dbxref=PMID:16857670 +Q03161 UniProtKB Binding site 203 203 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16857670;Dbxref=PMID:16857670 +Q03161 UniProtKB Modified residue 88 88 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03161 UniProtKB Beta strand 3 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 7 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 17 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 30 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 51 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 57 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 62 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Helix 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Helix 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 91 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Turn 98 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 102 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Helix 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Helix 114 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 125 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 134 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 152 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Helix 167 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 170 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 179 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Turn 183 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 187 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 193 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 202 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 215 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 222 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 234 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Helix 241 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Helix 256 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 260 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +Q03161 UniProtKB Beta strand 279 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CIR +##sequence-region Q8TGL8 1 51 +Q8TGL8 UniProtKB Chain 1 51 . . . ID=PRO_0000299676;Note=Putative uncharacterized protein YNL097W-A +Q8TGL8 UniProtKB Compositional bias 43 47 . . . Note=Poly-Cys +##sequence-region Q3E7Z1 1 64 +Q3E7Z1 UniProtKB Chain 1 64 . . . ID=PRO_0000247799;Note=Uncharacterized protein YNL146C-A +##sequence-region P53828 1 104 +P53828 UniProtKB Chain 1 104 . . . ID=PRO_0000203373;Note=Putative uncharacterized protein YNL296W +##sequence-region P53826 1 146 +P53826 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53826 UniProtKB Chain 25 146 . . . ID=PRO_0000014338;Note=Putative uncharacterized protein YNL319W +P53826 UniProtKB Glycosylation 99 99 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53826 UniProtKB Glycosylation 106 106 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53736 1 256 +P53736 UniProtKB Chain 1 256 . . . ID=PRO_0000203478;Note=Uncharacterized protein YNR040W +##sequence-region P53749 1 607 +P53749 UniProtKB Chain 1 607 . . . ID=PRO_0000115005;Note=Uncharacterized transcriptional regulatory protein YNR063W +P53749 UniProtKB DNA binding 16 44 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +##sequence-region P0C271 1 40 +P0C271 UniProtKB Chain 1 40 . . . ID=PRO_0000268630;Note=Uncharacterized protein YNL097C-B +##sequence-region P53758 1 84 +P53758 UniProtKB Chain 1 84 . . . ID=PRO_0000211378;Note=UPF0320 protein YNR077C +##sequence-region P53979 1 125 +P53979 UniProtKB Chain 1 125 . . . ID=PRO_0000203464;Note=Putative uncharacterized protein YNL013C +P53979 UniProtKB Transmembrane 28 48 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53979 UniProtKB Transmembrane 54 74 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53960 1 456 +P53960 UniProtKB Chain 1 456 . . . ID=PRO_0000203457;Note=Putative alanyl-tRNA editing protein alaX +P53960 UniProtKB Metal binding 125 125 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53960 UniProtKB Metal binding 129 129 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53960 UniProtKB Metal binding 240 240 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53960 UniProtKB Metal binding 244 244 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53947 1 316 +P53947 UniProtKB Chain 1 316 . . . ID=PRO_0000203449;Note=Vacuolar membrane protein YNL058C +P53947 UniProtKB Transmembrane 93 113 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53947 UniProtKB Compositional bias 26 65 . . . Note=Ser-rich +P53947 UniProtKB Compositional bias 235 243 . . . Note=Poly-Glu +P53947 UniProtKB Modified residue 148 148 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53947 UniProtKB Modified residue 256 256 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P53947 UniProtKB Modified residue 276 276 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38806 1 282 +P38806 UniProtKB Chain 1 282 . . . ID=PRO_0000212679;Note=Chromatin modification-related protein YNG2 +P38806 UniProtKB Zinc finger 222 271 . . . Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 +P38806 UniProtKB Coiled coil 35 86 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38806 UniProtKB Metal binding 225 225 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P38806 UniProtKB Metal binding 227 227 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P38806 UniProtKB Metal binding 238 238 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P38806 UniProtKB Metal binding 243 243 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P38806 UniProtKB Metal binding 249 249 . . . Note=Zinc 1%3B via pros nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P38806 UniProtKB Metal binding 252 252 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P38806 UniProtKB Metal binding 265 265 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P38806 UniProtKB Metal binding 268 268 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P38806 UniProtKB Binding site 224 224 . . . Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P38806 UniProtKB Binding site 235 235 . . . Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P38806 UniProtKB Binding site 239 239 . . . Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P38806 UniProtKB Binding site 247 247 . . . Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P38806 UniProtKB Modified residue 183 183 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38806 UniProtKB Modified residue 185 185 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38806 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38806 UniProtKB Helix 3 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P38806 UniProtKB Turn 14 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P38806 UniProtKB Helix 17 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P38806 UniProtKB Beta strand 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P38806 UniProtKB Helix 65 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P38806 UniProtKB Beta strand 225 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MUM +P38806 UniProtKB Turn 250 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MUM +P38806 UniProtKB Helix 266 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MUM +##sequence-region P53936 1 158 +P53936 UniProtKB Chain 1 158 . . . ID=PRO_0000203443;Note=Putative uncharacterized protein YNL089C +##sequence-region P53906 1 100 +P53906 UniProtKB Chain 1 100 . . . ID=PRO_0000203422;Note=Uncharacterized protein YNL146W +P53906 UniProtKB Transmembrane 17 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53906 UniProtKB Transmembrane 78 98 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53906 UniProtKB Sequence conflict 15 15 . . . Note=K->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53906 UniProtKB Sequence conflict 21 21 . . . Note=T->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53888 1 131 +P53888 UniProtKB Chain 1 131 . . . ID=PRO_0000203410;Note=Putative uncharacterized protein YNL170W +##sequence-region P53862 1 258 +P53862 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53862 UniProtKB Chain 24 258 . . . ID=PRO_0000014339;Note=putative uncharacterized membrane protein YNL228W +P53862 UniProtKB Topological domain 24 64 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53862 UniProtKB Transmembrane 65 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53862 UniProtKB Topological domain 86 123 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53862 UniProtKB Transmembrane 124 144 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53862 UniProtKB Topological domain 145 230 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53862 UniProtKB Transmembrane 231 251 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53862 UniProtKB Topological domain 252 258 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53862 UniProtKB Compositional bias 79 82 . . . Note=Poly-Phe +P53862 UniProtKB Compositional bias 88 92 . . . Note=Poly-Ser +P53862 UniProtKB Compositional bias 129 141 . . . Note=Poly-Phe +P53862 UniProtKB Glycosylation 118 118 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08187 1 201 +Q08187 UniProtKB Chain 1 201 . . . ID=PRO_0000245275;Note=Uncharacterized protein YOL029C +Q08187 UniProtKB Compositional bias 85 93 . . . Note=Poly-Ser +##sequence-region Q08206 1 761 +Q08206 UniProtKB Chain 1 761 . . . ID=PRO_0000235921;Note=Uncharacterized protein YOL036W +Q08206 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region Q08498 1 113 +Q08498 UniProtKB Signal peptide 1 29 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08498 UniProtKB Chain 30 113 . . . ID=PRO_0000299710;Note=Putative uncharacterized protein YOR082C +Q08498 UniProtKB Transmembrane 34 54 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08498 UniProtKB Transmembrane 56 76 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E7Y9 1 61 +Q3E7Y9 UniProtKB Chain 1 61 . . . ID=PRO_0000235930;Note=Uncharacterized protein YOL097W-A +##sequence-region Q08241 1 117 +Q08241 UniProtKB Chain 1 117 . . . ID=PRO_0000299694;Note=Putative uncharacterized protein YOL106W +##sequence-region Q08270 1 108 +Q08270 UniProtKB Chain 1 108 . . . ID=PRO_0000235933;Note=Uncharacterized protein YOL131W +##sequence-region Q12243 1 111 +Q12243 UniProtKB Chain 1 111 . . . ID=PRO_0000299704;Note=Uncharacterized protein YOR029W +##sequence-region O13521 1 115 +O13521 UniProtKB Chain 1 115 . . . ID=PRO_0000299798;Note=Putative uncharacterized protein YPL035C +##sequence-region A0A023PZM3 1 137 +A0A023PZM3 UniProtKB Chain 1 137 . . . ID=PRO_0000431062;Note=Putative uncharacterized membrane protein YPR050C +A0A023PZM3 UniProtKB Transmembrane 26 42 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZM3 UniProtKB Transmembrane 52 69 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region O13582 1 124 +O13582 UniProtKB Chain 1 124 . . . ID=PRO_0000299820;Note=Putative uncharacterized protein YPR076W +O13582 UniProtKB Compositional bias 33 40 . . . Note=Poly-Glu +##sequence-region O13517 1 100 +O13517 UniProtKB Chain 1 100 . . . ID=PRO_0000299802;Note=Putative uncharacterized protein YPL102C +##sequence-region Q02961 1 396 +Q02961 UniProtKB Chain 1 396 . . . ID=PRO_0000234369;Note=Putative 2-hydroxyacid dehydrogenase YPL113C +Q02961 UniProtKB Nucleotide binding 227 228 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02961 UniProtKB Nucleotide binding 311 313 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02961 UniProtKB Nucleotide binding 361 364 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02961 UniProtKB Active site 313 313 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02961 UniProtKB Active site 342 342 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02961 UniProtKB Active site 361 361 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02961 UniProtKB Binding site 337 337 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P0CX73 1 440 +P0CX73 UniProtKB Chain 1 440 . . . ID=PRO_0000409797;Note=Transposon Ty1-PL Gag polyprotein +P0CX73 UniProtKB Chain 1 401 . . . ID=PRO_0000409798;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX73 UniProtKB Peptide 402 440 . . . ID=PRO_0000409799;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX73 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX73 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0CX73 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX73 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region P0CX58 1 440 +P0CX58 UniProtKB Chain 1 440 . . . ID=PRO_0000409776;Note=Transposon Ty1-PR1 Gag polyprotein +P0CX58 UniProtKB Chain 1 401 . . . ID=PRO_0000409777;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX58 UniProtKB Peptide 402 440 . . . ID=PRO_0000409778;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX58 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX58 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX58 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region Q06522 1 304 +Q06522 UniProtKB Chain 1 304 . . . ID=PRO_0000257828;Note=Uncharacterized protein YPR147C +Q06522 UniProtKB Transmembrane 156 176 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06522 UniProtKB Glycosylation 95 95 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12152 1 901 +Q12152 UniProtKB Chain 1 901 . . . ID=PRO_0000234368;Note=Putative serine/threonine-protein kinase YPL150W +Q12152 UniProtKB Domain 41 287 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12152 UniProtKB Nucleotide binding 47 55 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12152 UniProtKB Compositional bias 398 517 . . . Note=Ser-rich +Q12152 UniProtKB Compositional bias 588 712 . . . Note=Ser-rich +Q12152 UniProtKB Active site 157 157 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q12152 UniProtKB Binding site 70 70 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12152 UniProtKB Modified residue 456 456 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +Q12152 UniProtKB Modified residue 533 533 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region A0A023PYK2 1 111 +A0A023PYK2 UniProtKB Chain 1 111 . . . ID=PRO_0000431063;Note=Putative uncharacterized membrane protein YPR170C +A0A023PYK2 UniProtKB Transmembrane 20 39 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06594 1 109 +Q06594 UniProtKB Chain 1 109 . . . ID=PRO_0000299834;Note=Uncharacterized protein YPR195C +##sequence-region Q08993 1 238 +Q08993 UniProtKB Chain 1 238 . . . ID=PRO_0000268172;Note=Putative uncharacterized protein YPR202W +##sequence-region P0CX98 1 160 +P0CX98 UniProtKB Chain 1 160 . . . ID=PRO_0000410455;Note=UPF0479 membrane protein YPR204C-A +P0CX98 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX98 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX98 UniProtKB Compositional bias 103 106 . . . Note=Poly-Ser +##sequence-region Q8TGL0 1 81 +Q8TGL0 UniProtKB Chain 1 81 . . . ID=PRO_0000299810;Note=Putative uncharacterized protein YPL222C-A +##sequence-region P0C5S0 1 95 +P0C5S0 UniProtKB Chain 1 95 . . . ID=PRO_0000309068;Note=Putative uncharacterized protein YPL250W-A +##sequence-region Q08976 1 102 +Q08976 UniProtKB Signal peptide 1 41 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08976 UniProtKB Chain 42 102 . . . ID=PRO_0000299813;Note=Uncharacterized protein YPL261C +Q08976 UniProtKB Sequence conflict 99 99 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CF36 1 145 +P0CF36 UniProtKB Chain 1 145 . . . ID=PRO_0000393443;Note=Putative uncharacterized protein YPL276W +P0CF36 UniProtKB Binding site 97 97 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160 +P0CF36 UniProtKB Binding site 121 121 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160 +##sequence-region A0A0B7P3V8 1 1104 +A0A0B7P3V8 UniProtKB Chain 1 1104 . . . ID=PRO_0000434006;Note=Transposon Ty4-P Gag-Pol polyprotein +A0A0B7P3V8 UniProtKB Domain 619 786 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +A0A0B7P3V8 UniProtKB Region 381 501 . . . Note=Ty4 protease +A0A0B7P3V8 UniProtKB Region 539 599 . . . Note=Integrase-type zinc finger-like +A0A0B7P3V8 UniProtKB Coiled coil 48 112 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A0B7P3V8 UniProtKB Active site 414 414 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +A0A0B7P3V8 UniProtKB Metal binding 630 630 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +A0A0B7P3V8 UniProtKB Metal binding 695 695 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +##sequence-region P0C5S1 1 26 +P0C5S1 UniProtKB Chain 1 26 . . . ID=PRO_0000309069;Note=Uncharacterized protein YPR160W-A +##sequence-region P0C1V3 1 61 +P0C1V3 UniProtKB Chain 1 61 . . . ID=PRO_0000248425;Note=Putative uncharacterized protein YAL016C-B +##sequence-region A0A023PXH4 1 145 +A0A023PXH4 UniProtKB Chain 1 145 . . . ID=PRO_0000430971;Note=Putative uncharacterized membrane protein YAL026C-A +A0A023PXH4 UniProtKB Transmembrane 104 124 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGK6 1 75 +Q8TGK6 UniProtKB Chain 1 75 . . . ID=PRO_0000248403;Note=Putative UPF0377 protein YAL067W-A +##sequence-region Q8TGK7 1 84 +Q8TGK7 UniProtKB Chain 1 84 . . . ID=PRO_0000211368;Note=Putative UPF0320 protein YAL068W-A +##sequence-region D6VPM8 1 179 +D6VPM8 UniProtKB Chain 1 179 . . . ID=PRO_0000402276;Note=Putative DUP240 protein YAR023C +D6VPM8 UniProtKB Transmembrane 4 24 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +D6VPM8 UniProtKB Transmembrane 26 46 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +D6VPM8 UniProtKB Sequence conflict 20 20 . . . Note=F->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +D6VPM8 UniProtKB Sequence conflict 20 20 . . . Note=F->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +D6VPM8 UniProtKB Sequence conflict 20 20 . . . Note=F->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +D6VPM8 UniProtKB Sequence conflict 46 46 . . . Note=F->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +D6VPM8 UniProtKB Sequence conflict 46 46 . . . Note=F->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +D6VPM8 UniProtKB Sequence conflict 46 46 . . . Note=F->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39549 1 74 +P39549 UniProtKB Chain 1 74 . . . ID=PRO_0000207530;Note=DUP240 protein YAR029W +##sequence-region P39550 1 113 +P39550 UniProtKB Chain 1 113 . . . ID=PRO_0000202427;Note=Putative uncharacterized protein YAR030C +##sequence-region Q8TGU8 1 32 +Q8TGU8 UniProtKB Chain 1 32 . . . ID=PRO_0000248432;Note=Uncharacterized protein YBL071C-B +##sequence-region P0C5L3 1 47 +P0C5L3 UniProtKB Chain 1 47 . . . ID=PRO_0000309011;Note=Putative uncharacterized protein YBR103C-A +##sequence-region Q8TGQ4 1 31 +Q8TGQ4 UniProtKB Chain 1 31 . . . ID=PRO_0000299795;Note=Putative uncharacterized protein YBR141W-A +##sequence-region Q2V2Q3 1 67 +Q2V2Q3 UniProtKB Chain 1 67 . . . ID=PRO_0000248441;Note=Putative uncharacterized protein YBR201C-A +##sequence-region Q3E781 1 34 +Q3E781 UniProtKB Chain 1 34 . . . ID=PRO_0000248442;Note=Uncharacterized protein YBR221W-A +##sequence-region A0A023PXH5 1 47 +A0A023PXH5 UniProtKB Chain 1 47 . . . ID=PRO_0000430977;Note=Putative uncharacterized protein YBR126W-B +##sequence-region P38303 1 103 +P38303 UniProtKB Chain 1 103 . . . ID=PRO_0000202506;Note=Putative uncharacterized protein YBR190W +##sequence-region P38320 1 171 +P38320 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38320 UniProtKB Chain 25 171 . . . ID=PRO_0000014311;Note=Putative uncharacterized membrane protein YBR224W +P38320 UniProtKB Topological domain 25 70 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38320 UniProtKB Transmembrane 71 91 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38320 UniProtKB Topological domain 92 140 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38320 UniProtKB Transmembrane 141 161 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38320 UniProtKB Topological domain 162 171 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38150 1 797 +P38150 UniProtKB Chain 1 797 . . . ID=PRO_0000194415;Note=Inactive deaminase YBR284W +P38150 UniProtKB Transmembrane 627 647 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38209 1 133 +P38209 UniProtKB Chain 1 133 . . . ID=PRO_0000202463;Note=Putative uncharacterized protein YBL012C +##sequence-region P38202 1 106 +P38202 UniProtKB Chain 1 106 . . . ID=PRO_0000202462;Note=UPF0642 protein YBL028C +##sequence-region Q03904 1 111 +Q03904 UniProtKB Chain 1 111 . . . ID=PRO_0000299874;Note=Putative uncharacterized protein YDR133C +Q03904 UniProtKB Transmembrane 64 86 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGP3 1 30 +Q8TGP3 UniProtKB Chain 1 30 . . . ID=PRO_0000299910;Note=Putative uncharacterized protein YEL008C-A +##sequence-region A0A023PYD9 1 177 +A0A023PYD9 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PYD9 UniProtKB Chain 23 177 . . . ID=PRO_0000430991;Note=Putative uncharacterized membrane protein YEL018C-A +A0A023PYD9 UniProtKB Transmembrane 31 51 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PYD9 UniProtKB Transmembrane 94 114 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PYD9 UniProtKB Transmembrane 136 156 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0C5M7 1 63 +P0C5M7 UniProtKB Chain 1 63 . . . ID=PRO_0000309025;Note=Putative uncharacterized protein YEL050W-A +P0C5M7 UniProtKB Transmembrane 38 58 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGU4 1 54 +Q8TGU4 UniProtKB Chain 1 54 . . . ID=PRO_0000245372;Note=Uncharacterized protein YER175W-A +##sequence-region P32618 1 956 +P32618 UniProtKB Chain 1 956 . . . ID=PRO_0000202607;Note=Uncharacterized protein YEL043W +P32618 UniProtKB Domain 40 141 . . . Note=Fibronectin type-III;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 +P32618 UniProtKB Modified residue 154 154 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198 +P32618 UniProtKB Modified residue 501 501 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32618 UniProtKB Modified residue 520 520 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32618 UniProtKB Modified residue 802 802 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32618 UniProtKB Modified residue 842 842 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32618 UniProtKB Modified residue 895 895 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32618 UniProtKB Sequence conflict 467 467 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07950 1 538 +Q07950 UniProtKB Chain 1 538 . . . ID=PRO_0000248405;Note=Sterol esterase 2 +Q07950 UniProtKB Topological domain 1 11 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07950 UniProtKB Transmembrane 12 32 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07950 UniProtKB Topological domain 33 538 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07950 UniProtKB Active site 287 287 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07950 UniProtKB Active site 480 480 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07950 UniProtKB Active site 511 511 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07950 UniProtKB Modified residue 73 73 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q07950 UniProtKB Modified residue 107 107 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P39974 1 107 +P39974 UniProtKB Chain 1 107 . . . ID=PRO_0000202599;Note=Uncharacterized protein YEL073C +##sequence-region P40058 1 173 +P40058 UniProtKB Chain 1 173 . . . ID=PRO_0000202639;Note=Uncharacterized protein YER085C +##sequence-region P40082 1 130 +P40082 UniProtKB Chain 1 130 . . . ID=PRO_0000202651;Note=Uncharacterized protein YER135C +##sequence-region P43540 1 174 +P43540 UniProtKB Chain 1 174 . . . ID=PRO_0000202669;Note=Uncharacterized protein YFL064C +P43540 UniProtKB Sequence conflict 104 104 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P43538 1 392 +P43538 UniProtKB Chain 1 392 . . . ID=PRO_0000102206;Note=Y' element ATP-dependent helicase YFL066C +P43538 UniProtKB Domain 1 175 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P43538 UniProtKB Domain 232 381 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P43538 UniProtKB Nucleotide binding 11 18 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +##sequence-region P43597 1 1233 +P43597 UniProtKB Chain 1 1233 . . . ID=PRO_0000202686;Note=Uncharacterized protein YFR016C +P43597 UniProtKB Domain 1132 1233 . . . Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686 +P43597 UniProtKB Modified residue 180 180 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198 +P43597 UniProtKB Modified residue 462 462 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43597 UniProtKB Modified residue 523 523 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43597 UniProtKB Modified residue 861 861 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P43597 UniProtKB Modified residue 975 975 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P43597 UniProtKB Modified residue 1037 1037 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43597 UniProtKB Modified residue 1046 1046 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P43608 1 114 +P43608 UniProtKB Chain 1 114 . . . ID=PRO_0000202693;Note=Uncharacterized protein YFR035C +P43608 UniProtKB Transmembrane 58 78 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43608 UniProtKB Transmembrane 94 114 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43617 1 309 +P43617 UniProtKB Chain 1 309 . . . ID=PRO_0000090695;Note=Uncharacterized mitochondrial carrier YFR045W +P43617 UniProtKB Transmembrane 12 32 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43617 UniProtKB Transmembrane 47 67 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43617 UniProtKB Transmembrane 100 120 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43617 UniProtKB Transmembrane 184 204 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43617 UniProtKB Transmembrane 222 242 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43617 UniProtKB Transmembrane 285 305 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43617 UniProtKB Repeat 6 83 . . . Note=Solcar 1 +P43617 UniProtKB Repeat 97 211 . . . Note=Solcar 2 +P43617 UniProtKB Repeat 216 302 . . . Note=Solcar 3 +##sequence-region Q8TGN8 1 31 +Q8TGN8 UniProtKB Chain 1 31 . . . ID=PRO_0000299923;Note=Putative uncharacterized protein YGR068W-A +##sequence-region P53205 1 108 +P53205 UniProtKB Chain 1 108 . . . ID=PRO_0000202780;Note=Putative uncharacterized protein YGR011W +##sequence-region P53213 1 109 +P53213 UniProtKB Chain 1 109 . . . ID=PRO_0000202786;Note=Putative uncharacterized protein YGR022C +##sequence-region P53240 1 122 +P53240 UniProtKB Chain 1 122 . . . ID=PRO_0000202802;Note=Putative uncharacterized protein YGR064W +##sequence-region P53245 1 111 +P53245 UniProtKB Chain 1 111 . . . ID=PRO_0000202805;Note=Putative uncharacterized protein YGR069W +P53245 UniProtKB Transmembrane 27 47 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53245 UniProtKB Compositional bias 36 47 . . . Note=Poly-Phe +##sequence-region P53282 1 124 +P53282 UniProtKB Chain 1 124 . . . ID=PRO_0000202826;Note=Putative uncharacterized protein YGR137W +P53282 UniProtKB Transmembrane 70 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53288 1 203 +P53288 UniProtKB Chain 1 203 . . . ID=PRO_0000202834;Note=Putative uncharacterized protein YGR160W +P53288 UniProtKB Transmembrane 182 202 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53288 UniProtKB Compositional bias 43 52 . . . Note=Poly-Ser +P53288 UniProtKB Compositional bias 89 98 . . . Note=Poly-Ser +P53288 UniProtKB Compositional bias 99 108 . . . Note=Poly-Glu +P53288 UniProtKB Compositional bias 163 167 . . . Note=Poly-Glu +##sequence-region P53307 1 113 +P53307 UniProtKB Chain 1 113 . . . ID=PRO_0000202848;Note=Uncharacterized protein YGR219W +##sequence-region P53329 1 174 +P53329 UniProtKB Chain 1 174 . . . ID=PRO_0000202868;Note=Uncharacterized protein YGR273C +##sequence-region P25338 1 174 +P25338 UniProtKB Chain 1 174 . . . ID=PRO_0000202776;Note=Uncharacterized endoplasmic reticulum membrane protein YGL010W +P25338 UniProtKB Topological domain 1 23 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25338 UniProtKB Transmembrane 24 44 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25338 UniProtKB Topological domain 45 63 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25338 UniProtKB Transmembrane 64 84 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25338 UniProtKB Topological domain 85 98 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25338 UniProtKB Transmembrane 99 119 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25338 UniProtKB Topological domain 120 131 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25338 UniProtKB Transmembrane 132 152 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25338 UniProtKB Topological domain 153 174 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25338 UniProtKB Sequence conflict 105 105 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25338 UniProtKB Sequence conflict 105 105 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25338 UniProtKB Sequence conflict 122 174 . . . Note=RPALIDNLVQSLVLAPYFIMFEFLFKLGFMPRLKATLEHDLEIKQRNLRMQRQ->TSQR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25338 UniProtKB Sequence conflict 122 174 . . . Note=RPALIDNLVQSLVLAPYFIMFEFLFKLGFMPRLKATLEHDLEIKQRNLRMQRQ->TSQR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53186 1 121 +P53186 UniProtKB Chain 1 121 . . . ID=PRO_0000202772;Note=Uncharacterized protein YGL034C +P53186 UniProtKB Nucleotide binding 77 84 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53181 1 101 +P53181 UniProtKB Chain 1 101 . . . ID=PRO_0000202770;Note=Putative uncharacterized protein YGL042C +P53181 UniProtKB Transmembrane 3 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53181 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53138 1 107 +P53138 UniProtKB Chain 1 107 . . . ID=PRO_0000202750;Note=Putative uncharacterized protein YGL109W +##sequence-region P53132 1 145 +P53132 UniProtKB Chain 1 145 . . . ID=PRO_0000202746;Note=Uncharacterized protein YGL118C +##sequence-region P53126 1 111 +P53126 UniProtKB Chain 1 111 . . . ID=PRO_0000202741;Note=Putative uncharacterized protein YGL132W +##sequence-region P53120 1 1219 +P53120 UniProtKB Chain 1 1219 . . . ID=PRO_0000202737;Note=Uncharacterized membrane protein YGL140C +P53120 UniProtKB Topological domain 1 36 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Transmembrane 37 57 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Topological domain 58 74 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Transmembrane 75 95 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Topological domain 96 123 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Transmembrane 124 144 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Topological domain 145 146 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Transmembrane 147 167 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Topological domain 168 183 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Transmembrane 184 204 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Topological domain 205 629 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Transmembrane 630 650 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Topological domain 651 663 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Transmembrane 664 684 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Topological domain 685 687 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Transmembrane 688 705 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Topological domain 706 709 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Transmembrane 710 730 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Topological domain 731 732 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Transmembrane 733 753 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Topological domain 754 766 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Transmembrane 767 787 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Topological domain 788 796 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Transmembrane 797 817 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Topological domain 818 1219 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53120 UniProtKB Modified residue 1167 1167 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198 +P53120 UniProtKB Modified residue 1191 1191 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53120 UniProtKB Modified residue 1198 1198 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53120 UniProtKB Modified residue 1199 1199 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P0CL28 1 191 +P0CL28 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL28 UniProtKB Chain 18 191 . . . ID=PRO_0000406005;Note=Putative uncharacterized protein YGR296C-A +P0CL28 UniProtKB Transmembrane 168 188 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL28 UniProtKB Compositional bias 13 159 . . . Note=Gly/Ser-rich +##sequence-region P53085 1 113 +P53085 UniProtKB Chain 1 113 . . . ID=PRO_0000202717;Note=Putative uncharacterized protein YGL217C +##sequence-region Q3E7Z6 1 27 +Q3E7Z6 UniProtKB Chain 1 27 . . . ID=PRO_0000245392;Note=Uncharacterized protein YHL015W-A +##sequence-region A0A023PZD5 1 153 +A0A023PZD5 UniProtKB Chain 1 153 . . . ID=PRO_0000431018;Note=Putative uncharacterized protein YHL030W-A +##sequence-region Q3E758 1 44 +Q3E758 UniProtKB Chain 1 44 . . . ID=PRO_0000245391;Note=Uncharacterized protein YHL048C-A +##sequence-region P0CL32 1 64 +P0CL32 UniProtKB Chain 1 64 . . . ID=PRO_0000299927;Note=Putative uncharacterized protein YHR052W-A +P0CL32 UniProtKB Transmembrane 33 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PYH0 1 136 +A0A023PYH0 UniProtKB Signal peptide 1 35 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PYH0 UniProtKB Chain 36 136 . . . ID=PRO_0000431024;Note=Putative uncharacterized protein YHR070C-A +##sequence-region O13536 1 103 +O13536 UniProtKB Chain 1 103 . . . ID=PRO_0000299929;Note=Uncharacterized protein YHR139C-A +##sequence-region Q3E815 1 49 +Q3E815 UniProtKB Chain 1 49 . . . ID=PRO_0000245396;Note=Uncharacterized membrane protein YHR175W-A +Q3E815 UniProtKB Transmembrane 17 39 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38868 1 163 +P38868 UniProtKB Chain 1 163 . . . ID=PRO_0000202933;Note=Uncharacterized protein YHR180W +P38868 UniProtKB Transmembrane 7 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E7Z5 1 69 +Q3E7Z5 UniProtKB Chain 1 69 . . . ID=PRO_0000245405;Note=Uncharacterized protein YIL002W-A +Q3E7Z5 UniProtKB Coiled coil 21 64 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E7Z4 1 54 +Q3E7Z4 UniProtKB Chain 1 54 . . . ID=PRO_0000245403;Note=Uncharacterized protein YIL046W-A +Q3E7Z4 UniProtKB Transmembrane 21 43 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGN5 1 46 +Q8TGN5 UniProtKB Chain 1 46 . . . ID=PRO_0000299756;Note=Uncharacterized protein YIL105W-A +##sequence-region A0A023PYI2 1 110 +A0A023PYI2 UniProtKB Chain 1 110 . . . ID=PRO_0000431039;Note=Putative uncharacterized protein YIL142C-A +##sequence-region P0CF22 1 210 +P0CF22 UniProtKB Chain 1 210 . . . ID=PRO_0000393394;Note=Putative truncated L-serine dehydratase SDL1 +##sequence-region P40551 1 113 +P40551 UniProtKB Chain 1 113 . . . ID=PRO_0000203001;Note=Uncharacterized protein YIL012W +##sequence-region P40542 1 124 +P40542 UniProtKB Chain 1 124 . . . ID=PRO_0000202999;Note=Putative uncharacterized protein YIL025C +##sequence-region Q08956 1 461 +Q08956 UniProtKB Chain 1 461 . . . ID=PRO_0000238632;Note=Protein YIG1 +##sequence-region P25637 1 258 +P25637 UniProtKB Chain 1 258 . . . ID=PRO_0000207657;Note=Protein IMPACT homolog +P25637 UniProtKB Domain 10 114 . . . Note=RWD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00179 +P25637 UniProtKB Cross-link 187 187 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25637 UniProtKB Mutagenesis 87 87 . . . Note=Slightly increases interaction with GCN1 and ACT1 and does not prevent inhibition of GCN2 activity in amino acid-starved cells%3B when associated with A-90. E->A +P25637 UniProtKB Mutagenesis 90 90 . . . Note=Slightly increases interaction with GCN1 and ACT1 and does not prevent inhibition of GCN2 activity in amino acid-starved cells%3B when associated with A-87. D->A +P25637 UniProtKB Mutagenesis 102 102 . . . Note=Decreases interaction with GCN1%2C but not with ACT1%2C and prevents inhibition of GCN2 activity in amino acid-starved cells%3B when associated with A-106. D->A +P25637 UniProtKB Mutagenesis 106 106 . . . Note=Decreases interaction with GCN1%2C but not with ACT1%2C and prevents inhibition of GCN2 activity in amino acid-starved cells%3B when associated with A-102. E->A +##sequence-region P40497 1 633 +P40497 UniProtKB Chain 1 633 . . . ID=PRO_0000202973;Note=Uncharacterized protein YIL092W +P40497 UniProtKB Transmembrane 99 118 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40497 UniProtKB Transmembrane 217 233 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40488 1 101 +P40488 UniProtKB Chain 1 101 . . . ID=PRO_0000202967;Note=Uncharacterized protein YIL102C +##sequence-region P40483 1 696 +P40483 UniProtKB Chain 1 696 . . . ID=PRO_0000078181;Note=Putative zinc metalloproteinase YIL108W +P40483 UniProtKB Domain 522 695 . . . Note=Jacalin-type lectin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01088 +P40483 UniProtKB Active site 319 319 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P40483 UniProtKB Metal binding 318 318 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P40483 UniProtKB Metal binding 322 322 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P40483 UniProtKB Metal binding 328 328 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P40483 UniProtKB Modified residue 361 361 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40483 UniProtKB Cross-link 245 245 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P40483 UniProtKB Cross-link 478 478 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P40483 UniProtKB Cross-link 518 518 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P40483 UniProtKB Cross-link 579 579 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P40483 UniProtKB Cross-link 590 590 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P40483 UniProtKB Cross-link 596 596 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P40483 UniProtKB Sequence conflict 696 696 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region A0A023PXM7 1 112 +A0A023PXM7 UniProtKB Chain 1 112 . . . ID=PRO_0000431043;Note=Putative uncharacterized protein YIL020C-A +A0A023PXM7 UniProtKB Transmembrane 7 26 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXM7 UniProtKB Transmembrane 36 58 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P28626 1 145 +P28626 UniProtKB Chain 1 145 . . . ID=PRO_0000203309;Note=Putative uncharacterized protein YIM2 +P28626 UniProtKB Transmembrane 20 40 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28626 UniProtKB Transmembrane 116 136 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28626 UniProtKB Sequence conflict 39 39 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28626 UniProtKB Sequence conflict 83 83 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28626 UniProtKB Sequence conflict 115 115 . . . Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28626 UniProtKB Sequence conflict 132 132 . . . Note=C->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28626 UniProtKB Sequence conflict 143 143 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53108 1 310 +P53108 UniProtKB Chain 1 310 . . . ID=PRO_0000202730;Note=Protein YIP5 +P53108 UniProtKB Transmembrane 131 151 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53108 UniProtKB Transmembrane 181 201 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53108 UniProtKB Transmembrane 220 240 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53108 UniProtKB Transmembrane 249 269 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53108 UniProtKB Transmembrane 290 310 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53108 UniProtKB Modified residue 60 60 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P0CL23 1 45 +P0CL23 UniProtKB Chain 1 45 . . . ID=PRO_0000202949;Note=Putative UPF0377 protein YIL175W +##sequence-region Q8TGN1 1 49 +Q8TGN1 UniProtKB Chain 1 49 . . . ID=PRO_0000299765;Note=Putative uncharacterized protein YJR140W-A +##sequence-region P47159 1 448 +P47159 UniProtKB Chain 1 448 . . . ID=PRO_0000203118;Note=Uncharacterized membrane protein YJR124C +P47159 UniProtKB Topological domain 1 50 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Transmembrane 51 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Topological domain 72 93 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Transmembrane 94 114 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Topological domain 115 146 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Transmembrane 147 167 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Topological domain 168 184 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Transmembrane 185 205 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Topological domain 206 260 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Transmembrane 261 281 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Topological domain 282 287 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Transmembrane 288 308 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Topological domain 309 333 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Transmembrane 334 354 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Topological domain 355 386 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Transmembrane 387 407 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Topological domain 408 416 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Transmembrane 417 437 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Topological domain 438 448 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Nucleotide binding 386 393 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47159 UniProtKB Sequence conflict 448 448 . . . Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47188 1 116 +P47188 UniProtKB Chain 1 116 . . . ID=PRO_0000211373;Note=Putative UPF0320 protein YJR162C +##sequence-region P47078 1 108 +P47078 UniProtKB Chain 1 108 . . . ID=PRO_0000203078;Note=Uncharacterized protein YJL009W +P47078 UniProtKB Glycosylation 33 33 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47021 1 107 +P47021 UniProtKB Chain 1 107 . . . ID=PRO_0000203043;Note=Putative uncharacterized protein YJL119C +##sequence-region P47012 1 105 +P47012 UniProtKB Chain 1 105 . . . ID=PRO_0000203036;Note=Putative uncharacterized protein YJL135W +##sequence-region P40895 1 119 +P40895 UniProtKB Chain 1 119 . . . ID=PRO_0000203012;Note=Putative uncharacterized protein YJL215C +##sequence-region P40892 1 196 +P40892 UniProtKB Chain 1 196 . . . ID=PRO_0000068743;Note=Putative acetyltransferase YJL218W +##sequence-region P47086 1 261 +P47086 UniProtKB Chain 1 261 . . . ID=PRO_0000203082;Note=Uncharacterized protein YJR011C +P47086 UniProtKB Sequence conflict 142 142 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36119 1 530 +P36119 UniProtKB Chain 1 530 . . . ID=PRO_0000203202;Note=Uncharacterized protein YKR023W +P36119 UniProtKB Modified residue 426 426 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36119 UniProtKB Modified residue 431 431 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36119 UniProtKB Modified residue 434 434 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P36119 UniProtKB Modified residue 457 457 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36119 UniProtKB Cross-link 509 509 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P0CE69 1 306 +P0CE69 UniProtKB Chain 1 306 . . . ID=PRO_0000392613;Note=Putative uncharacterized protein YKR104W +P0CE69 UniProtKB Domain 33 286 . . . Note=ABC transporter;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P0CE69 UniProtKB Nucleotide binding 67 74 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +##sequence-region P0C5P3 1 30 +P0C5P3 UniProtKB Chain 1 30 . . . ID=PRO_0000309041;Note=Uncharacterized protein YKL145W-A +P0C5P3 UniProtKB Transmembrane 7 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E765 1 70 +Q3E765 UniProtKB Chain 1 70 . . . ID=PRO_0000245418;Note=Uncharacterized protein YKL183C-A +Q3E765 UniProtKB Transmembrane 12 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36098 1 137 +P36098 UniProtKB Chain 1 137 . . . ID=PRO_0000203187;Note=Putative uncharacterized protein YKL031W +P36098 UniProtKB Transmembrane 36 52 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36098 UniProtKB Transmembrane 113 129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P34249 1 101 +P34249 UniProtKB Chain 1 101 . . . ID=PRO_0000203160;Note=Uncharacterized protein YKL102C +##sequence-region P36071 1 126 +P36071 UniProtKB Chain 1 126 . . . ID=PRO_0000203154;Note=Putative uncharacterized protein YKL123W +##sequence-region Q08018 1 140 +Q08018 UniProtKB Chain 1 140 . . . ID=PRO_0000299609;Note=Putative uncharacterized protein YLR076C +##sequence-region Q12528 1 110 +Q12528 UniProtKB Chain 1 110 . . . ID=PRO_0000299611;Note=Uncharacterized protein YLR111W +Q12528 UniProtKB Transmembrane 29 49 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12174 1 109 +Q12174 UniProtKB Chain 1 109 . . . ID=PRO_0000299615;Note=Putative uncharacterized protein YLR123C +Q12174 UniProtKB Transmembrane 75 95 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12288 1 251 +Q12288 UniProtKB Chain 1 251 . . . ID=PRO_0000247340;Note=Putative glutamine amidotransferase YLR126C +Q12288 UniProtKB Domain 48 232 . . . Note=Glutamine amidotransferase type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +Q12288 UniProtKB Active site 112 112 . . . Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +Q12288 UniProtKB Active site 198 198 . . . Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +Q12288 UniProtKB Active site 200 200 . . . Note=For GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +##sequence-region P0CY05 1 43 +P0CY05 UniProtKB Chain 1 43 . . . ID=PRO_0000410461;Note=Uncharacterized protein YLR159C-A +##sequence-region Q06070 1 228 +Q06070 UniProtKB Chain 1 228 . . . ID=PRO_0000268628;Note=Uncharacterized protein YLR407W +Q06070 UniProtKB Sequence conflict 226 228 . . . Note=GMP->ACHD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region O13578 1 112 +O13578 UniProtKB Transit peptide 1 21 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13578 UniProtKB Chain 22 112 . . . ID=PRO_0000247258;Note=Putative uncharacterized protein YLR415C%2C mitochondrial +##sequence-region Q06698 1 1435 +Q06698 UniProtKB Chain 1 1435 . . . ID=PRO_0000247257;Note=Putative ATP-dependent RNA helicase YLR419W +Q06698 UniProtKB Domain 365 406 . . . Note=UBA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212 +Q06698 UniProtKB Domain 430 531 . . . Note=RWD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00179 +Q06698 UniProtKB Domain 614 782 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q06698 UniProtKB Domain 845 1020 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q06698 UniProtKB Nucleotide binding 627 634 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q06698 UniProtKB Motif 729 732 . . . Note=DEAH box +Q06698 UniProtKB Modified residue 9 9 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06698 UniProtKB Modified residue 816 816 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q06188 1 304 +Q06188 UniProtKB Chain 1 304 . . . ID=PRO_0000247356;Note=PWWP domain-containing protein YLR455W +Q06188 UniProtKB Domain 7 68 . . . Note=PWWP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00162 +##sequence-region Q6B0Y5 1 42 +Q6B0Y5 UniProtKB Chain 1 42 . . . ID=PRO_0000270976;Note=Putative uncharacterized membrane protein YMR046W-A +Q6B0Y5 UniProtKB Transmembrane 5 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PZL2 1 124 +A0A023PZL2 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZL2 UniProtKB Chain 20 124 . . . ID=PRO_0000431057;Note=Putative uncharacterized membrane protein YMR119W-A +A0A023PZL2 UniProtKB Transmembrane 37 57 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZL2 UniProtKB Transmembrane 86 108 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04711 1 1755 +Q04711 UniProtKB Chain 1 1755 . . . ID=PRO_0000199566;Note=Transposon Ty1-ML1 Gag-Pol polyprotein +Q04711 UniProtKB Chain 1 401 . . . ID=PRO_0000279117;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04711 UniProtKB Chain 402 582 . . . ID=PRO_0000279118;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04711 UniProtKB Chain 583 1217 . . . ID=PRO_0000279119;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04711 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279120;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04711 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04711 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +Q04711 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +Q04711 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04711 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q04711 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04711 UniProtKB Compositional bias 72 146 . . . Note=Pro-rich +Q04711 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q04711 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04711 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04711 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04711 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04711 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04711 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04711 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04711 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04711 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04711 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04711 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q03434 1 1755 +Q03434 UniProtKB Chain 1 1755 . . . ID=PRO_0000199565;Note=Transposon Ty1-ML2 Gag-Pol polyprotein +Q03434 UniProtKB Chain 1 401 . . . ID=PRO_0000279123;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03434 UniProtKB Chain 402 582 . . . ID=PRO_0000279124;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03434 UniProtKB Chain 583 1217 . . . ID=PRO_0000279125;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03434 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279126;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03434 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03434 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +Q03434 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +Q03434 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03434 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q03434 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03434 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q03434 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q03434 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03434 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03434 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03434 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03434 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03434 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03434 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03434 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03434 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03434 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03434 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03434 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region A0A023PYJ4 1 111 +A0A023PYJ4 UniProtKB Chain 1 111 . . . ID=PRO_0000431056;Note=Putative uncharacterized protein YMR153C-A +##sequence-region P40218 1 223 +P40218 UniProtKB Chain 1 223 . . . ID=PRO_0000203307;Note=Uncharacterized protein YMR147W +##sequence-region Q04336 1 1088 +Q04336 UniProtKB Chain 1 1088 . . . ID=PRO_0000203326;Note=Uncharacterized protein YMR196W +Q04336 UniProtKB Modified residue 299 299 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04336 UniProtKB Modified residue 984 984 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04336 UniProtKB Modified residue 1013 1013 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04336 UniProtKB Modified residue 1081 1081 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q04019 1 206 +Q04019 UniProtKB Chain 1 206 . . . ID=PRO_0000203337;Note=Putative uncharacterized protein YMR245W +##sequence-region Q04838 1 102 +Q04838 UniProtKB Chain 1 102 . . . ID=PRO_0000203341;Note=Uncharacterized protein YMR254C +Q04838 UniProtKB Transmembrane 1 21 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04838 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04838 UniProtKB Transmembrane 68 88 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03508 1 461 +Q03508 UniProtKB Chain 1 461 . . . ID=PRO_0000203347;Note=Uncharacterized protein YMR265C +##sequence-region Q03559 1 197 +Q03559 UniProtKB Chain 1 197 . . . ID=PRO_0000203351;Note=Uncharacterized protein YMR295C +Q03559 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q03559 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q03559 UniProtKB Cross-link 26 26 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q03559 UniProtKB Cross-link 32 32 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q04869 1 349 +Q04869 UniProtKB Chain 1 349 . . . ID=PRO_0000203357;Note=Uncharacterized protein YMR315W +Q04869 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q6Q571 1 112 +Q6Q571 UniProtKB Chain 1 112 . . . ID=PRO_0000299669;Note=Putative uncharacterized protein YMR086C-A +##sequence-region A0A023PYJ0 1 108 +A0A023PYJ0 UniProtKB Chain 1 108 . . . ID=PRO_0000431058;Note=Putative uncharacterized membrane protein YML009C-A +A0A023PYJ0 UniProtKB Transmembrane 25 45 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39523 1 943 +P39523 UniProtKB Chain 1 943 . . . ID=PRO_0000203298;Note=Uncharacterized protein YMR124W +P39523 UniProtKB Compositional bias 59 66 . . . Note=Poly-Gln +P39523 UniProtKB Compositional bias 93 100 . . . Note=Poly-Gln +P39523 UniProtKB Compositional bias 164 169 . . . Note=Poly-Gly +P39523 UniProtKB Compositional bias 170 175 . . . Note=Poly-Asp +P39523 UniProtKB Compositional bias 371 381 . . . Note=Poly-Gln +P39523 UniProtKB Compositional bias 536 539 . . . Note=Poly-Glu +P39523 UniProtKB Compositional bias 715 718 . . . Note=Poly-Ser +P39523 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P39523 UniProtKB Modified residue 553 553 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39523 UniProtKB Modified residue 586 586 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39523 UniProtKB Modified residue 619 619 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39523 UniProtKB Modified residue 649 649 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P39523 UniProtKB Modified residue 681 681 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39523 UniProtKB Modified residue 766 766 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P39523 UniProtKB Modified residue 771 771 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q04215 1 440 +Q04215 UniProtKB Chain 1 440 . . . ID=PRO_0000203499;Note=Transposon Ty1-MR1 Gag polyprotein +Q04215 UniProtKB Chain 1 401 . . . ID=PRO_0000279131;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04215 UniProtKB Peptide 402 440 . . . ID=PRO_0000279132;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04215 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04215 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region I2HB70 1 103 +I2HB70 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +I2HB70 UniProtKB Chain 22 103 . . . ID=PRO_0000419188;Note=Uncharacterized protein YMR316C-A +##sequence-region A0A023PXQ4 1 394 +A0A023PXQ4 UniProtKB Chain 1 394 . . . ID=PRO_0000431054;Note=Putative uncharacterized membrane protein YMR173W-A +A0A023PXQ4 UniProtKB Transmembrane 13 33 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXQ4 UniProtKB Transmembrane 35 55 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXQ4 UniProtKB Transmembrane 73 95 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXQ4 UniProtKB Transmembrane 110 130 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXQ4 UniProtKB Transmembrane 152 172 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXQ4 UniProtKB Transmembrane 179 198 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXQ4 UniProtKB Transmembrane 216 236 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXQ4 UniProtKB Transmembrane 241 261 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXQ4 UniProtKB Transmembrane 267 287 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXQ4 UniProtKB Transmembrane 293 313 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXQ4 UniProtKB Transmembrane 340 360 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXQ4 UniProtKB Transmembrane 372 392 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXQ4 UniProtKB Compositional bias 2 361 . . . Note=Thr-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00017 +A0A023PXQ4 UniProtKB Compositional bias 19 167 . . . Note=Met-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00013 +A0A023PXQ4 UniProtKB Compositional bias 243 344 . . . Note=Met-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00013 +##sequence-region Q8TGS7 1 28 +Q8TGS7 UniProtKB Chain 1 28 . . . ID=PRO_0000247789;Note=Uncharacterized protein YMR182W-A +Q8TGS7 UniProtKB Transmembrane 5 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40214 1 342 +P40214 UniProtKB Chain 1 342 . . . ID=PRO_0000203305;Note=Uncharacterized protein YMR144W +##sequence-region Q8TGS5 1 35 +Q8TGS5 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q8TGS5 UniProtKB Chain 19 35 . . . ID=PRO_0000247795;Note=Uncharacterized protein YMR272W-B +##sequence-region A0A023PXI0 1 129 +A0A023PXI0 UniProtKB Chain 1 129 . . . ID=PRO_0000431050;Note=Putative uncharacterized membrane protein YMR306C-A +A0A023PXI0 UniProtKB Transmembrane 35 55 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXI0 UniProtKB Transmembrane 98 118 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03795 1 547 +Q03795 UniProtKB Chain 1 547 . . . ID=PRO_0000203311;Note=Uncharacterized membrane protein YMR155W +Q03795 UniProtKB Topological domain 1 21 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Transmembrane 22 42 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Topological domain 43 58 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Transmembrane 59 79 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Topological domain 80 83 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Transmembrane 84 104 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Topological domain 105 110 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Transmembrane 111 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Topological domain 132 144 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Transmembrane 145 165 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Topological domain 166 175 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Transmembrane 176 196 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Topological domain 197 323 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Transmembrane 324 344 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Topological domain 345 398 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Transmembrane 399 419 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Topological domain 420 437 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Transmembrane 438 458 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Topological domain 459 469 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Transmembrane 470 490 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Topological domain 491 514 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Transmembrane 515 535 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Topological domain 536 547 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03795 UniProtKB Modified residue 237 237 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q03648 1 457 +Q03648 UniProtKB Chain 1 457 . . . ID=PRO_0000203330;Note=Uncharacterized protein YMR209C +Q03648 UniProtKB Transmembrane 1 21 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03648 UniProtKB Transmembrane 250 270 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q05016 1 267 +Q05016 UniProtKB Chain 1 267 . . . ID=PRO_0000054873;Note=NADP-dependent 3-hydroxy acid dehydrogenase +Q05016 UniProtKB Nucleotide binding 20 25 . . . Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7 +Q05016 UniProtKB Nucleotide binding 48 49 . . . Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7 +Q05016 UniProtKB Nucleotide binding 75 76 . . . Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7 +Q05016 UniProtKB Nucleotide binding 198 205 . . . Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7 +Q05016 UniProtKB Active site 168 168 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001 +Q05016 UniProtKB Binding site 102 102 . . . Note=NADP%3B via carbonyl oxygen;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7 +Q05016 UniProtKB Binding site 155 155 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05016 UniProtKB Binding site 168 168 . . . Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7 +Q05016 UniProtKB Binding site 172 172 . . . Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7 +Q05016 UniProtKB Modified residue 260 260 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05016 UniProtKB Helix 5 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Beta strand 15 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Helix 24 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Turn 37 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Beta strand 41 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Helix 50 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Beta strand 68 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Helix 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Helix 82 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Helix 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Beta strand 98 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Helix 117 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Helix 129 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Beta strand 149 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Helix 156 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Helix 166 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Turn 186 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Beta strand 192 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Beta strand 201 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Helix 205 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Turn 210 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Helix 214 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Helix 229 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Beta strand 246 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +Q05016 UniProtKB Beta strand 258 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKU +##sequence-region P38430 1 313 +P38430 UniProtKB Chain 1 313 . . . ID=PRO_0000203344;Note=Uncharacterized deoxyribonuclease YMR262W +P38430 UniProtKB Metal binding 8 8 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38430 UniProtKB Metal binding 10 10 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38430 UniProtKB Metal binding 126 126 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38430 UniProtKB Metal binding 126 126 . . . Note=Divalent metal cation 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38430 UniProtKB Metal binding 180 180 . . . Note=Divalent metal cation 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38430 UniProtKB Metal binding 207 207 . . . Note=Divalent metal cation 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38430 UniProtKB Metal binding 262 262 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38430 UniProtKB Sequence conflict 24 24 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38430 UniProtKB Sequence conflict 167 167 . . . Note=C->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04893 1 1140 +Q04893 UniProtKB Chain 1 1140 . . . ID=PRO_0000203359;Note=Uncharacterized protein YMR317W +Q04893 UniProtKB Sequence conflict 271 272 . . . Note=VI->SV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q04893 UniProtKB Sequence conflict 278 279 . . . Note=WA->SS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q6B0R7 1 102 +Q6B0R7 UniProtKB Chain 1 102 . . . ID=PRO_0000211375;Note=Putative UPF0320 protein YMR326C +Q6B0R7 UniProtKB Sequence conflict 99 99 . . . Note=F->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32331 1 307 +P32331 UniProtKB Transmembrane 29 49 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32331 UniProtKB Transmembrane 83 103 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32331 UniProtKB Transmembrane 118 138 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32331 UniProtKB Transmembrane 183 203 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32331 UniProtKB Transmembrane 223 243 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32331 UniProtKB Transmembrane 277 298 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32331 UniProtKB Repeat 26 106 . . . Note=Solcar 1 +P32331 UniProtKB Repeat 121 204 . . . Note=Solcar 2 +P32331 UniProtKB Repeat 218 305 . . . Note=Solcar 3 +P32331 UniProtKB Sequence conflict 101 101 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04521 1 102 +Q04521 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04521 UniProtKB Chain 20 102 . . . ID=PRO_0000014337;Note=Putative uncharacterized protein YML084W +##sequence-region Q03759 1 105 +Q03759 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q03759 UniProtKB Chain 2 105 . . . ID=PRO_0000203242;Note=Uncharacterized protein YML108W +Q03759 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q03759 UniProtKB Beta strand 7 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z +Q03759 UniProtKB Turn 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z +Q03759 UniProtKB Beta strand 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z +Q03759 UniProtKB Beta strand 37 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z +Q03759 UniProtKB Helix 50 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z +Q03759 UniProtKB Beta strand 72 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z +Q03759 UniProtKB Turn 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z +Q03759 UniProtKB Beta strand 81 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z +Q03759 UniProtKB Helix 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z +Q03759 UniProtKB Helix 91 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N6Z +##sequence-region P47147 1 688 +P47147 UniProtKB Chain 1 688 . . . ID=PRO_0000094948;Note=Phosphoinositide 3-phosphatase +P47147 UniProtKB Domain 155 637 . . . Note=Myotubularin phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00669 +P47147 UniProtKB Active site 397 397 . . . Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10044 +P47147 UniProtKB Sequence conflict 85 85 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47147 UniProtKB Sequence conflict 85 85 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CX09 1 502 +P0CX09 UniProtKB Chain 1 502 . . . ID=PRO_0000409748;Note=Mannitol dehydrogenase YNR073C +##sequence-region Q12112 1 1755 +Q12112 UniProtKB Chain 1 1755 . . . ID=PRO_0000279137;Note=Transposon Ty1-NL1 Gag-Pol polyprotein +Q12112 UniProtKB Chain 1 401 . . . ID=PRO_0000279138;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12112 UniProtKB Chain 402 582 . . . ID=PRO_0000279139;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12112 UniProtKB Chain 583 1217 . . . ID=PRO_0000279140;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12112 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279141;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12112 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12112 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +Q12112 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +Q12112 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12112 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q12112 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12112 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q12112 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12112 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12112 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12112 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12112 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12112 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12112 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12112 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12112 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12112 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12112 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q3E7Z0 1 62 +Q3E7Z0 UniProtKB Chain 1 62 . . . ID=PRO_0000247797;Note=Uncharacterized protein YNL277W-A +##sequence-region P53827 1 115 +P53827 UniProtKB Chain 1 115 . . . ID=PRO_0000203370;Note=Putative uncharacterized protein YNL303W +##sequence-region Q3E767 1 46 +Q3E767 UniProtKB Chain 1 46 . . . ID=PRO_0000247801;Note=Uncharacterized protein YNL067W-B +##sequence-region P53820 1 52 +P53820 UniProtKB Chain 1 52 . . . ID=PRO_0000203362;Note=Putative uncharacterized protein YNL338W +##sequence-region P53723 1 404 +P53723 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.3;Dbxref=PMID:22814378 +P53723 UniProtKB Chain 2 404 . . . ID=PRO_0000203473;Note=UPF0674 endoplasmic reticulum membrane protein YNR021W +P53723 UniProtKB Transmembrane 49 68 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53723 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.3;Dbxref=PMID:22814378 +P53723 UniProtKB Glycosylation 44 44 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53723 UniProtKB Glycosylation 98 98 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08300 1 171 +Q08300 UniProtKB Chain 1 171 . . . ID=PRO_0000245276;Note=Uncharacterized protein YOL159C +##sequence-region P0CF20 1 169 +P0CF20 UniProtKB Chain 1 169 . . . ID=PRO_0000393392;Note=Putative uncharacterized transporter YOL163W +P0CF20 UniProtKB Transmembrane 25 45 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CF20 UniProtKB Transmembrane 57 77 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CF20 UniProtKB Transmembrane 91 111 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E736 1 78 +Q3E736 UniProtKB Chain 1 78 . . . ID=PRO_0000237663;Note=Uncharacterized protein YOR192C-C +##sequence-region Q08756 1 102 +Q08756 UniProtKB Chain 1 102 . . . ID=PRO_0000299733;Note=Putative uncharacterized protein YOR300W +##sequence-region Q3E806 1 69 +Q3E806 UniProtKB Chain 1 69 . . . ID=PRO_0000245287;Note=Uncharacterized protein YOR316C-A +##sequence-region Q08786 1 185 +Q08786 UniProtKB Chain 1 185 . . . ID=PRO_0000262744;Note=Putative uncharacterized membrane protein YOR331C +Q08786 UniProtKB Topological domain 1 69 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08786 UniProtKB Transmembrane 70 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08786 UniProtKB Topological domain 91 91 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08786 UniProtKB Transmembrane 92 112 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08786 UniProtKB Topological domain 113 118 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08786 UniProtKB Transmembrane 119 139 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08786 UniProtKB Topological domain 140 185 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12484 1 108 +Q12484 UniProtKB Chain 1 108 . . . ID=PRO_0000299740;Note=Uncharacterized protein YOR343C +##sequence-region Q08910 1 206 +Q08910 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08910 UniProtKB Chain 20 206 . . . ID=PRO_0000243950;Note=VEL1-related protein YOR387C +Q08910 UniProtKB Glycosylation 26 26 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08910 UniProtKB Glycosylation 48 48 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08910 UniProtKB Glycosylation 91 91 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08910 UniProtKB Glycosylation 139 139 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08910 UniProtKB Glycosylation 152 152 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08910 UniProtKB Glycosylation 183 183 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E832 1 53 +Q3E832 UniProtKB Chain 1 53 . . . ID=PRO_0000237652;Note=Uncharacterized protein YOR072W-B +##sequence-region Q08157 1 551 +Q08157 UniProtKB Chain 1 551 . . . ID=PRO_0000245272;Note=Uncharacterized membrane protein YOL019W +Q08157 UniProtKB Topological domain 1 7 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08157 UniProtKB Transmembrane 8 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08157 UniProtKB Topological domain 29 88 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08157 UniProtKB Transmembrane 89 109 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08157 UniProtKB Topological domain 110 135 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08157 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08157 UniProtKB Topological domain 157 160 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08157 UniProtKB Transmembrane 161 181 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08157 UniProtKB Topological domain 182 551 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08157 UniProtKB Compositional bias 449 470 . . . Note=Gln-rich +Q08157 UniProtKB Modified residue 224 224 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08157 UniProtKB Modified residue 232 232 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08157 UniProtKB Modified residue 363 363 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38070 1 525 +P38070 UniProtKB Chain 1 525 . . . ID=PRO_0000086073;Note=Serine/threonine-protein kinase YPK3 +P38070 UniProtKB Domain 128 424 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38070 UniProtKB Domain 445 524 . . . Note=AGC-kinase C-terminal +P38070 UniProtKB Nucleotide binding 134 142 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38070 UniProtKB Active site 277 277 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P38070 UniProtKB Binding site 157 157 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38070 UniProtKB Modified residue 90 90 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950;Dbxref=PMID:15665377,PMID:17330950 +P38070 UniProtKB Modified residue 105 105 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38070 UniProtKB Modified residue 107 107 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38070 UniProtKB Modified residue 321 321 . . . Note=Phosphoserine%3B by PKH1 or PKH2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12706 +P38070 UniProtKB Modified residue 490 490 . . . Note=Phosphothreonine%3B by TORC1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12706 +P38070 UniProtKB Modified residue 513 513 . . . Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12706 +##sequence-region Q3E7B3 1 70 +Q3E7B3 UniProtKB Chain 1 70 . . . ID=PRO_0000242624;Note=Uncharacterized protein YPR108W-A +##sequence-region Q6B0W0 1 111 +Q6B0W0 UniProtKB Chain 1 111 . . . ID=PRO_0000299817;Note=Putative uncharacterized protein YPR039W +Q6B0W0 UniProtKB Transmembrane 48 70 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region O13572 1 173 +O13572 UniProtKB Chain 1 173 . . . ID=PRO_0000299831;Note=Putative uncharacterized protein YPR150W +O13572 UniProtKB Transmembrane 9 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13572 UniProtKB Transmembrane 32 52 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13572 UniProtKB Transmembrane 100 120 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13572 UniProtKB Transmembrane 127 147 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13572 UniProtKB Sequence conflict 129 129 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53057 1 165 +P53057 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53057 UniProtKB Chain 25 165 . . . ID=PRO_0000014320;Note=Yapsin-5 +P53057 UniProtKB Domain 67 165 . . . Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103 +P53057 UniProtKB Glycosylation 57 57 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38815 1 214 +P38815 UniProtKB Chain 1 214 . . . ID=PRO_0000202910;Note=PX domain-containing protein YPT35 +P38815 UniProtKB Domain 73 213 . . . Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147 +P38815 UniProtKB Modified residue 65 65 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38815 UniProtKB Modified residue 66 66 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38815 UniProtKB Mutagenesis 123 123 . . . Note=Abolishes partially PtdIns(3)P-binding. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15263065;Dbxref=PMID:15263065 +##sequence-region Q99260 1 215 +Q99260 UniProtKB Chain 1 215 . . . ID=PRO_0000121319;Note=GTP-binding protein YPT6 +Q99260 UniProtKB Nucleotide binding 17 24 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99260 UniProtKB Nucleotide binding 65 69 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99260 UniProtKB Nucleotide binding 124 127 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99260 UniProtKB Motif 39 47 . . . Note=Effector region;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q99260 UniProtKB Modified residue 215 215 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99260 UniProtKB Lipidation 213 213 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99260 UniProtKB Lipidation 215 215 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P31111 1 875 +P31111 UniProtKB Chain 1 875 . . . ID=PRO_0000066584;Note=Synaptonemal complex protein ZIP1 +P31111 UniProtKB Coiled coil 177 333 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31111 UniProtKB Coiled coil 397 438 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31111 UniProtKB Coiled coil 456 752 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31111 UniProtKB Modified residue 481 481 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P31111 UniProtKB Sequence conflict 55 55 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40021 1 1076 +P40021 UniProtKB Chain 1 1076 . . . ID=PRO_0000202624;Note=Zinc-regulated protein 8 +P40021 UniProtKB Compositional bias 119 126 . . . Note=Poly-Pro +P40021 UniProtKB Compositional bias 428 448 . . . Note=Poly-Asp +P40021 UniProtKB Modified residue 275 275 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40021 UniProtKB Modified residue 354 354 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198 +P40021 UniProtKB Modified residue 403 403 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40021 UniProtKB Modified residue 407 407 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40021 UniProtKB Modified residue 632 632 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40021 UniProtKB Modified residue 676 676 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region Q12512 1 249 +Q12512 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12512 UniProtKB Chain 21 249 . . . ID=PRO_0000041751;Note=Protein ZPS1 +Q12512 UniProtKB Glycosylation 28 28 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12512 UniProtKB Glycosylation 57 57 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12512 UniProtKB Glycosylation 98 98 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12512 UniProtKB Glycosylation 217 217 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region O13518 1 139 +O13518 UniProtKB Chain 1 139 . . . ID=PRO_0000299803;Note=Putative uncharacterized protein YPL114W +O13518 UniProtKB Transmembrane 22 38 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13518 UniProtKB Sequence conflict 9 9 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region O13571 1 109 +O13571 UniProtKB Chain 1 109 . . . ID=PRO_0000299830;Note=Putative uncharacterized protein YPR146C +##sequence-region O13583 1 123 +O13583 UniProtKB Chain 1 123 . . . ID=PRO_0000299821;Note=Putative uncharacterized protein YPR077C +O13583 UniProtKB Transmembrane 14 34 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06325 1 596 +Q06325 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06325 UniProtKB Chain 26 596 . . . ID=PRO_0000270564;Note=Aspartic proteinase yapsin-7 +Q06325 UniProtKB Topological domain 26 575 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06325 UniProtKB Transmembrane 576 596 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06325 UniProtKB Domain 56 440 . . . Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103 +Q06325 UniProtKB Active site 74 74 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06325 UniProtKB Active site 321 321 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06325 UniProtKB Glycosylation 26 26 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06325 UniProtKB Glycosylation 59 59 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06325 UniProtKB Glycosylation 106 106 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06325 UniProtKB Glycosylation 131 131 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06325 UniProtKB Glycosylation 140 140 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06325 UniProtKB Glycosylation 143 143 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06325 UniProtKB Glycosylation 148 148 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06325 UniProtKB Glycosylation 175 175 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06325 UniProtKB Glycosylation 308 308 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06325 UniProtKB Glycosylation 391 391 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06325 UniProtKB Glycosylation 455 455 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06325 UniProtKB Glycosylation 478 478 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06325 UniProtKB Glycosylation 484 484 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06325 UniProtKB Glycosylation 549 549 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06325 UniProtKB Glycosylation 552 552 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06325 UniProtKB Sequence conflict 299 299 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38146 1 199 +P38146 UniProtKB Chain 1 199 . . . ID=PRO_0000121321;Note=GTP-binding protein YPT10 +P38146 UniProtKB Nucleotide binding 11 18 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38146 UniProtKB Nucleotide binding 65 69 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38146 UniProtKB Nucleotide binding 122 125 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38146 UniProtKB Modified residue 199 199 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36586 +P38146 UniProtKB Lipidation 197 197 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36586 +P38146 UniProtKB Lipidation 199 199 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36586 +##sequence-region P38555 1 223 +P38555 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.5 +P38555 UniProtKB Chain 2 223 . . . ID=PRO_0000121323;Note=GTP-binding protein YPT31/YPT8 +P38555 UniProtKB Nucleotide binding 20 27 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38555 UniProtKB Nucleotide binding 68 72 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38555 UniProtKB Nucleotide binding 126 129 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38555 UniProtKB Motif 42 50 . . . Note=Effector region;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38555 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.5 +P38555 UniProtKB Lipidation 222 222 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38555 UniProtKB Lipidation 223 223 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38555 UniProtKB Beta strand 12 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ +P38555 UniProtKB Helix 26 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ +P38555 UniProtKB Beta strand 49 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ +P38555 UniProtKB Beta strand 60 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ +P38555 UniProtKB Turn 70 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ +P38555 UniProtKB Helix 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ +P38555 UniProtKB Turn 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ +P38555 UniProtKB Beta strand 88 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ +P38555 UniProtKB Helix 98 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ +P38555 UniProtKB Beta strand 120 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ +P38555 UniProtKB Helix 128 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ +P38555 UniProtKB Helix 138 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ +P38555 UniProtKB Beta strand 151 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ +P38555 UniProtKB Helix 163 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ +##sequence-region P36018 1 234 +P36018 UniProtKB Chain 1 234 . . . ID=PRO_0000121326;Note=GTP-binding protein YPT52 +P36018 UniProtKB Nucleotide binding 10 17 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36018 UniProtKB Nucleotide binding 66 70 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36018 UniProtKB Nucleotide binding 111 114 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36018 UniProtKB Modified residue 139 139 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36018 UniProtKB Modified residue 142 142 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36018 UniProtKB Lipidation 232 232 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36018 UniProtKB Lipidation 233 233 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36018 UniProtKB Cross-link 151 151 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P0CX22 1 1796 +P0CX22 UniProtKB Chain 1 1796 . . . ID=PRO_0000409757;Note=Y' element ATP-dependent helicase protein 1 copy 8 +P0CX22 UniProtKB Domain 797 974 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P0CX22 UniProtKB Domain 1031 1180 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P0CX22 UniProtKB Nucleotide binding 810 817 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P0CX22 UniProtKB Sequence conflict 1293 1293 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38280 1 609 +P38280 UniProtKB Chain 1 609 . . . ID=PRO_0000066511;Note=Spore-specific protein YSW1 +P38280 UniProtKB Modified residue 159 159 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38280 UniProtKB Modified residue 160 160 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38280 UniProtKB Sequence conflict 58 58 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38280 UniProtKB Sequence conflict 117 118 . . . Note=KE->NQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38280 UniProtKB Sequence conflict 223 224 . . . Note=TP->IHR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38280 UniProtKB Sequence conflict 271 271 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38280 UniProtKB Sequence conflict 365 365 . . . Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38280 UniProtKB Sequence conflict 415 416 . . . Note=QQ->HE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38280 UniProtKB Sequence conflict 460 460 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38280 UniProtKB Sequence conflict 481 482 . . . Note=LS->SR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38280 UniProtKB Sequence conflict 488 494 . . . Note=HNVYGND->PMFMAMI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38280 UniProtKB Sequence conflict 495 609 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12324 1 675 +Q12324 UniProtKB Chain 1 675 . . . ID=PRO_0000215376;Note=Calcium channel YVC1 +Q12324 UniProtKB Topological domain 1 236 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12324 UniProtKB Transmembrane 237 257 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12324 UniProtKB Topological domain 258 295 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12324 UniProtKB Transmembrane 296 316 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12324 UniProtKB Topological domain 317 335 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12324 UniProtKB Transmembrane 336 355 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12324 UniProtKB Topological domain 356 376 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12324 UniProtKB Transmembrane 377 397 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12324 UniProtKB Topological domain 398 405 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12324 UniProtKB Transmembrane 406 426 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12324 UniProtKB Topological domain 427 436 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12324 UniProtKB Transmembrane 437 457 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12324 UniProtKB Topological domain 458 675 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12324 UniProtKB Compositional bias 573 576 . . . Note=Poly-Asp;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12324 UniProtKB Modified residue 636 636 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P53303 1 486 +P53303 UniProtKB Chain 1 486 . . . ID=PRO_0000119040;Note=Zinc finger protein ZPR1 +P53303 UniProtKB Zinc finger 54 86 . . . Note=C4-type 1 +P53303 UniProtKB Zinc finger 295 327 . . . Note=C4-type 2 +P53303 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53303 UniProtKB Modified residue 407 407 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P0CF34 1 1048 +P0CF34 UniProtKB Chain 1 1048 . . . ID=PRO_0000393436;Note=Putative truncated guanine nucleotide exchange factor SDC25 +P0CF34 UniProtKB Domain 578 710 . . . Note=N-terminal Ras-GEF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00135 +P0CF34 UniProtKB Domain 748 995 . . . Note=Ras-GEF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00168 +##sequence-region Q07880 1 148 +Q07880 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07880 UniProtKB Chain 23 148 . . . ID=PRO_0000299605;Note=Putative uncharacterized protein YLL044W +##sequence-region Q07881 1 127 +Q07881 UniProtKB Chain 1 127 . . . ID=PRO_0000299606;Note=Putative uncharacterized protein YLL047W +Q07881 UniProtKB Transmembrane 12 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E798 1 87 +Q3E798 UniProtKB Chain 1 87 . . . ID=PRO_0000247352;Note=Uncharacterized protein YLR099W-A +##sequence-region P0C2I5 1 1755 +P0C2I5 UniProtKB Chain 1 1755 . . . ID=PRO_0000279099;Note=Transposon Ty1-LR2 Gag-Pol polyprotein +P0C2I5 UniProtKB Chain 1 401 . . . ID=PRO_0000279100;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I5 UniProtKB Chain 402 582 . . . ID=PRO_0000279101;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I5 UniProtKB Chain 583 1217 . . . ID=PRO_0000279102;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I5 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279103;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I5 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I5 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +P0C2I5 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +P0C2I5 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I5 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +P0C2I5 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I5 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0C2I5 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +P0C2I5 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I5 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I5 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I5 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I5 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I5 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I5 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I5 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2I5 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I5 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I5 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I5 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region Q12077 1 108 +Q12077 UniProtKB Chain 1 108 . . . ID=PRO_0000299617;Note=Putative uncharacterized protein YLR140W +Q12077 UniProtKB Transmembrane 10 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12077 UniProtKB Compositional bias 28 34 . . . Note=Poly-Phe +##sequence-region Q3E813 1 49 +Q3E813 UniProtKB Chain 1 49 . . . ID=PRO_0000262876;Note=Uncharacterized protein YLR154C-G +##sequence-region P0CE98 1 114 +P0CE98 UniProtKB Chain 1 114 . . . ID=PRO_0000393296;Note=Putative uncharacterized protein YLR161W +##sequence-region A0A023PZG4 1 107 +A0A023PZG4 UniProtKB Chain 1 107 . . . ID=PRO_0000431046;Note=Uncharacterized protein YLR236C +##sequence-region O13573 1 101 +O13573 UniProtKB Chain 1 101 . . . ID=PRO_0000299625;Note=Putative uncharacterized protein YLR252W +##sequence-region O13541 1 116 +O13541 UniProtKB Chain 1 116 . . . ID=PRO_0000299629;Note=Putative uncharacterized protein YLR280C +##sequence-region Q05867 1 314 +Q05867 UniProtKB Transit peptide 1 29 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05867 UniProtKB Chain 30 314 . . . ID=PRO_0000247160;Note=Uncharacterized protein YLR283W%2C mitochondrial +Q05867 UniProtKB Transmembrane 262 279 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05867 UniProtKB Coiled coil 177 207 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q05898 1 108 +Q05898 UniProtKB Chain 1 108 . . . ID=PRO_0000299633;Note=Uncharacterized protein YLR296W +Q05898 UniProtKB Transmembrane 72 94 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05898 UniProtKB Compositional bias 61 68 . . . Note=Poly-Lys +##sequence-region O94085 1 183 +O94085 UniProtKB Chain 1 183 . . . ID=PRO_0000299638;Note=Putative uncharacterized protein YLR339C +O94085 UniProtKB Transmembrane 153 175 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06139 1 101 +Q06139 UniProtKB Chain 1 101 . . . ID=PRO_0000247212;Note=Uncharacterized protein YLR346C%2C mitochondrial +##sequence-region Q3E795 1 98 +Q3E795 UniProtKB Chain 1 98 . . . ID=PRO_0000247214;Note=Uncharacterized protein YLR361C-A +Q3E795 UniProtKB Compositional bias 5 11 . . . Note=Poly-Asn +##sequence-region Q06689 1 675 +Q06689 UniProtKB Signal peptide 1 28 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Chain 29 675 . . . ID=PRO_0000247220;Note=Cell membrane protein YLR413W +Q06689 UniProtKB Topological domain 29 532 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Transmembrane 533 553 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Topological domain 554 568 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Transmembrane 569 589 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Topological domain 590 610 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Transmembrane 611 631 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Topological domain 632 675 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Compositional bias 122 235 . . . Note=Thr-rich +Q06689 UniProtKB Modified residue 654 654 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06689 UniProtKB Modified residue 665 665 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06689 UniProtKB Glycosylation 49 49 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Glycosylation 72 72 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Glycosylation 103 103 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Glycosylation 142 142 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Glycosylation 160 160 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Glycosylation 194 194 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Glycosylation 215 215 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Glycosylation 228 228 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Glycosylation 252 252 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Glycosylation 286 286 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Glycosylation 299 299 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Glycosylation 318 318 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Glycosylation 322 322 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Glycosylation 358 358 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Glycosylation 375 375 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Glycosylation 405 405 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Glycosylation 429 429 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Glycosylation 468 468 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06689 UniProtKB Cross-link 671 671 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region O13564 1 114 +O13564 UniProtKB Chain 1 114 . . . ID=PRO_0000299649;Note=Putative uncharacterized protein YLR428C +##sequence-region A0A023PZK9 1 126 +A0A023PZK9 UniProtKB Chain 1 126 . . . ID=PRO_0000431047;Note=Putative uncharacterized membrane protein YLR458W +A0A023PZK9 UniProtKB Transmembrane 21 43 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZK9 UniProtKB Transmembrane 48 70 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CE99 1 70 +P0CE99 UniProtKB Chain 1 70 . . . ID=PRO_0000393297;Note=Putative uncharacterized protein YLR157W-D +##sequence-region Q04461 1 462 +Q04461 UniProtKB Chain 1 462 . . . ID=PRO_0000203291;Note=Uncharacterized protein YMR111C +Q04461 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04461 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04461 UniProtKB Modified residue 237 237 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04461 UniProtKB Modified residue 249 249 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q04461 UniProtKB Modified residue 254 254 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q04471 1 368 +Q04471 UniProtKB Chain 1 368 . . . ID=PRO_0000203292;Note=Putative peptidase YMR114C +Q04471 UniProtKB Modified residue 338 338 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region A2P2R3 1 262 +A2P2R3 UniProtKB Chain 1 262 . . . ID=PRO_0000269757;Note=Putative glutamine--fructose-6-phosphate aminotransferase [isomerizing] +A2P2R3 UniProtKB Domain 2 262 . . . Note=Glutamine amidotransferase type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609 +A2P2R3 UniProtKB Active site 2 2 . . . Note=Nucleophile%3B for GATase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609 +##sequence-region Q04670 1 1755 +Q04670 UniProtKB Chain 1 1755 . . . ID=PRO_0000199568;Note=Transposon Ty1-MR2 Gag-Pol polyprotein +Q04670 UniProtKB Chain 1 401 . . . ID=PRO_0000279133;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04670 UniProtKB Chain 402 582 . . . ID=PRO_0000279134;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04670 UniProtKB Chain 583 1217 . . . ID=PRO_0000279135;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04670 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279136;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04670 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04670 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +Q04670 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +Q04670 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04670 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q04670 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04670 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q04670 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q04670 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04670 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04670 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04670 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04670 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04670 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04670 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04670 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q04670 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04670 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04670 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04670 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region Q8TGS6 1 29 +Q8TGS6 UniProtKB Chain 1 29 . . . ID=PRO_0000247792;Note=Uncharacterized protein YMR242W-A +##sequence-region A0A023PZL7 1 119 +A0A023PZL7 UniProtKB Chain 1 119 . . . ID=PRO_0000431052;Note=Putative uncharacterized protein YMR294W-A +##sequence-region P0C5Q5 1 64 +P0C5Q5 UniProtKB Chain 1 64 . . . ID=PRO_0000309053;Note=Putative uncharacterized protein YMR307C-A +##sequence-region Q8TGS4 1 35 +Q8TGS4 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q8TGS4 UniProtKB Chain 26 35 . . . ID=PRO_0000247796;Note=Uncharacterized protein YMR315W-A +##sequence-region Q03823 1 816 +Q03823 UniProtKB Chain 1 816 . . . ID=PRO_0000203313;Note=Uncharacterized protein YMR160W +Q03823 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03823 UniProtKB Modified residue 79 79 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q03231 1 154 +Q03231 UniProtKB Chain 1 154 . . . ID=PRO_0000203320;Note=Uncharacterized protein YMR181C +Q03231 UniProtKB Modified residue 47 47 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q04814 1 134 +Q04814 UniProtKB Chain 1 134 . . . ID=PRO_0000203339;Note=Uncharacterized protein YMR252C +##sequence-region Q04867 1 317 +Q04867 UniProtKB Chain 1 317 . . . ID=PRO_0000203354;Note=Putative methyltransferase YMR310C +Q04867 UniProtKB Modified residue 190 190 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P32843 1 850 +P32843 UniProtKB Transit peptide 1 44 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32843 UniProtKB Chain 45 850 . . . ID=PRO_0000081806;Note=Mitochondrial escape protein 2 +P32843 UniProtKB Topological domain 45 287 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32843 UniProtKB Transmembrane 288 308 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32843 UniProtKB Topological domain 309 850 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32843 UniProtKB Domain 198 272 . . . Note=RRM +P32843 UniProtKB Mutagenesis 502 502 . . . Note=In YME2-4%3B prevents mtDNA escape%2C growth on nonfermentable carbon sources and growth at 37 degrees Celsius on glucose. N->Y;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1557037,ECO:0000269|PubMed:16850347,ECO:0000269|PubMed:8649384;Dbxref=PMID:1557037,PMID:16850347,PMID:8649384 +##sequence-region Q03629 1 201 +Q03629 UniProtKB Chain 1 201 . . . ID=PRO_0000203248;Note=Uncharacterized protein YML079W +Q03629 UniProtKB Helix 17 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Helix 28 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Beta strand 45 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Beta strand 57 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Beta strand 74 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Beta strand 80 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Beta strand 92 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Beta strand 102 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Beta strand 111 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Beta strand 122 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Helix 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Beta strand 136 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Beta strand 146 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Turn 155 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Beta strand 161 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Helix 173 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Beta strand 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Helix 181 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Helix 191 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +Q03629 UniProtKB Helix 198 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XE7 +##sequence-region Q03208 1 357 +Q03208 UniProtKB Chain 1 357 . . . ID=PRO_0000203240;Note=Uncharacterized protein YML119W +Q03208 UniProtKB Modified residue 72 72 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +##sequence-region Q03102 1 365 +Q03102 UniProtKB Chain 1 365 . . . ID=PRO_0000203238;Note=Uncharacterized membrane protein YML131W +Q03102 UniProtKB Topological domain 1 133 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03102 UniProtKB Transmembrane 134 154 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03102 UniProtKB Topological domain 155 169 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03102 UniProtKB Transmembrane 170 190 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03102 UniProtKB Topological domain 191 365 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03102 UniProtKB Sequence conflict 239 239 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04773 1 145 +Q04773 UniProtKB Chain 1 145 . . . ID=PRO_0000121548;Note=Uncharacterized protein YMR074C +Q04773 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q04773 UniProtKB Modified residue 121 121 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q04773 UniProtKB Modified residue 126 126 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04773 UniProtKB Helix 3 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JXN +Q04773 UniProtKB Helix 44 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FH0 +Q04773 UniProtKB Helix 52 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FH0 +Q04773 UniProtKB Helix 66 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FH0 +Q04773 UniProtKB Helix 91 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FH0 +##sequence-region Q04436 1 120 +Q04436 UniProtKB Chain 1 120 . . . ID=PRO_0000203289;Note=Uncharacterized protein YMR103C +##sequence-region P0C5Q7 1 72 +P0C5Q7 UniProtKB Chain 1 72 . . . ID=PRO_0000309055;Note=Putative uncharacterized protein YNR001W-A +##sequence-region Q8TGJ2 1 30 +Q8TGJ2 UniProtKB Chain 1 30 . . . ID=PRO_0000247804;Note=Putative UPF0377 protein YNR075C-A +##sequence-region Q12391 1 440 +Q12391 UniProtKB Chain 1 440 . . . ID=PRO_0000279142;Note=Transposon Ty1-NL1 Gag polyprotein +Q12391 UniProtKB Chain 1 401 . . . ID=PRO_0000279143;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12391 UniProtKB Peptide 402 440 . . . ID=PRO_0000279144;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12391 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12391 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q12470 1 440 +Q12470 UniProtKB Chain 1 440 . . . ID=PRO_0000279150;Note=Transposon Ty1-NL2 Gag polyprotein +Q12470 UniProtKB Chain 1 401 . . . ID=PRO_0000279151;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12470 UniProtKB Peptide 402 440 . . . ID=PRO_0000279152;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12470 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12470 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12470 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region P42840 1 284 +P42840 UniProtKB Chain 1 284 . . . ID=PRO_0000203364;Note=Uncharacterized membrane protein YNL320W +P42840 UniProtKB Topological domain 1 8 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42840 UniProtKB Transmembrane 9 25 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42840 UniProtKB Topological domain 26 80 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42840 UniProtKB Transmembrane 81 101 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42840 UniProtKB Topological domain 102 284 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53821 1 84 +P53821 UniProtKB Chain 1 84 . . . ID=PRO_0000211377;Note=Putative UPF0320 protein YNL337W +##sequence-region P53719 1 212 +P53719 UniProtKB Chain 1 212 . . . ID=PRO_0000203471;Note=Uncharacterized protein YNR014W +P53719 UniProtKB Compositional bias 30 42 . . . Note=Poly-Ser +P53719 UniProtKB Modified residue 136 136 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:18407956,PMID:19779198 +##sequence-region P53726 1 119 +P53726 UniProtKB Chain 1 119 . . . ID=PRO_0000203475;Note=Putative uncharacterized protein YNR025C +P53726 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53726 UniProtKB Transmembrane 32 52 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53747 1 219 +P53747 UniProtKB Chain 1 219 . . . ID=PRO_0000203481;Note=Uncharacterized vacuolar membrane protein YNR061C +P53747 UniProtKB Topological domain 1 15 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53747 UniProtKB Transmembrane 16 36 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53747 UniProtKB Topological domain 37 41 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53747 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53747 UniProtKB Topological domain 63 63 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53747 UniProtKB Transmembrane 64 84 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53747 UniProtKB Topological domain 85 116 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53747 UniProtKB Transmembrane 117 137 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53747 UniProtKB Topological domain 138 219 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53980 1 444 +P53980 UniProtKB Chain 1 444 . . . ID=PRO_0000203465;Note=Uncharacterized protein YNL011C +##sequence-region P53902 1 135 +P53902 UniProtKB Chain 1 135 . . . ID=PRO_0000203420;Note=Putative uncharacterized protein YNL150W +P53902 UniProtKB Compositional bias 41 50 . . . Note=Poly-Ser +##sequence-region P53887 1 122 +P53887 UniProtKB Chain 1 122 . . . ID=PRO_0000203409;Note=Putative uncharacterized protein YNL171C +##sequence-region P40169 1 301 +P40169 UniProtKB Chain 1 301 . . . ID=PRO_0000203399;Note=Uncharacterized plasma membrane protein YNL194C +P40169 UniProtKB Topological domain 1 5 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40169 UniProtKB Transmembrane 6 26 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40169 UniProtKB Topological domain 27 112 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40169 UniProtKB Transmembrane 113 133 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40169 UniProtKB Topological domain 134 143 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40169 UniProtKB Transmembrane 144 164 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40169 UniProtKB Topological domain 165 191 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40169 UniProtKB Transmembrane 192 212 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40169 UniProtKB Topological domain 213 301 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40159 1 199 +P40159 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40159 UniProtKB Chain 2 199 . . . ID=PRO_0000203391;Note=Uncharacterized protein YNL208W +P40159 UniProtKB Compositional bias 25 196 . . . Note=Gly-rich +P40159 UniProtKB Compositional bias 119 123 . . . Note=Poly-Asn +P40159 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40159 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40159 UniProtKB Modified residue 70 70 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q08110 1 124 +Q08110 UniProtKB Chain 1 124 . . . ID=PRO_0000245271;Note=Putative uncharacterized protein YOL014W +##sequence-region Q8TGS1 1 66 +Q8TGS1 UniProtKB Chain 1 66 . . . ID=PRO_0000237645;Note=Uncharacterized protein YOR032W-A +Q8TGS1 UniProtKB Transmembrane 4 24 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q8TGS1 UniProtKB Transmembrane 38 58 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E7Z9 1 31 +Q3E7Z9 UniProtKB Chain 1 31 . . . ID=PRO_0000235922;Note=Uncharacterized protein YOL038C-A +##sequence-region Q8TGL6 1 69 +Q8TGL6 UniProtKB Chain 1 69 . . . ID=PRO_0000299713;Note=Putative uncharacterized protein YOR108C-A +##sequence-region Q92392 1 440 +Q92392 UniProtKB Chain 1 440 . . . ID=PRO_0000279158;Note=Transposon Ty1-OL Gag polyprotein +Q92392 UniProtKB Chain 1 401 . . . ID=PRO_0000279159;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q92392 UniProtKB Peptide 402 440 . . . ID=PRO_0000279160;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q92392 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q92392 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q92392 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q92392 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region Q08521 1 101 +Q08521 UniProtKB Chain 1 101 . . . ID=PRO_0000299714;Note=Putative uncharacterized protein YOR121C +##sequence-region Q08293 1 103 +Q08293 UniProtKB Chain 1 103 . . . ID=PRO_0000299697;Note=Putative uncharacterized protein YOL150C +##sequence-region Q08621 1 117 +Q08621 UniProtKB Chain 1 117 . . . ID=PRO_0000299724;Note=Putative uncharacterized protein YOR203W +##sequence-region Q12015 1 292 +Q12015 UniProtKB Chain 1 292 . . . ID=PRO_0000237667;Note=Transmembrane protein YOR223W +Q12015 UniProtKB Topological domain 1 243 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12015 UniProtKB Transmembrane 244 264 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12015 UniProtKB Topological domain 265 273 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12015 UniProtKB Transmembrane 274 291 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12015 UniProtKB Topological domain 292 292 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12015 UniProtKB Glycosylation 11 11 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12015 UniProtKB Glycosylation 41 41 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12015 UniProtKB Glycosylation 77 77 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12015 UniProtKB Glycosylation 99 99 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12015 UniProtKB Glycosylation 145 145 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08741 1 106 +Q08741 UniProtKB Chain 1 106 . . . ID=PRO_0000299732;Note=Putative uncharacterized protein YOR282W +Q08741 UniProtKB Transmembrane 39 56 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08741 UniProtKB Transmembrane 74 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08743 1 309 +Q08743 UniProtKB Chain 1 309 . . . ID=PRO_0000245252;Note=Vacuolar membrane protein YOR292C +Q08743 UniProtKB Topological domain 1 52 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08743 UniProtKB Transmembrane 53 73 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08743 UniProtKB Topological domain 74 81 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08743 UniProtKB Transmembrane 82 102 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08743 UniProtKB Topological domain 103 183 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08743 UniProtKB Transmembrane 184 204 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08743 UniProtKB Topological domain 205 225 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08743 UniProtKB Transmembrane 226 246 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08743 UniProtKB Topological domain 247 260 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08743 UniProtKB Transmembrane 261 281 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08743 UniProtKB Topological domain 282 309 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08743 UniProtKB Glycosylation 19 19 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08743 UniProtKB Glycosylation 121 121 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08789 1 138 +Q08789 UniProtKB Chain 1 138 . . . ID=PRO_0000299738;Note=Putative uncharacterized protein YOR333C +Q08789 UniProtKB Compositional bias 114 119 . . . Note=Poly-Arg +##sequence-region Q08811 1 116 +Q08811 UniProtKB Chain 1 116 . . . ID=PRO_0000299741;Note=Putative uncharacterized protein YOR345C +Q08811 UniProtKB Transmembrane 22 42 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E805 1 51 +Q3E805 UniProtKB Chain 1 51 . . . ID=PRO_0000244634;Note=Uncharacterized protein YOR376W-A +##sequence-region Q3E804 1 55 +Q3E804 UniProtKB Chain 1 55 . . . ID=PRO_0000244635;Note=Uncharacterized protein YOR381W-A +##sequence-region Q08912 1 624 +Q08912 UniProtKB Signal peptide 1 29 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08912 UniProtKB Chain 30 624 . . . ID=PRO_0000244637;Note=Uncharacterized protein YOR389W +Q08912 UniProtKB Glycosylation 68 68 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08912 UniProtKB Glycosylation 150 150 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08912 UniProtKB Glycosylation 219 219 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08912 UniProtKB Glycosylation 366 366 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08912 UniProtKB Glycosylation 441 441 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08912 UniProtKB Glycosylation 447 447 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08912 UniProtKB Glycosylation 464 464 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08912 UniProtKB Glycosylation 528 528 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGL5 1 26 +Q8TGL5 UniProtKB Chain 1 26 . . . ID=PRO_0000299717;Note=Putative uncharacterized protein YOR161W-A +##sequence-region Q8TGQ8 1 70 +Q8TGQ8 UniProtKB Chain 1 70 . . . ID=PRO_0000299693;Note=Putative uncharacterized protein YOL085W-A +##sequence-region P0CL40 1 160 +P0CL40 UniProtKB Chain 1 160 . . . ID=PRO_0000406014;Note=Putative UPF0479 protein YOR396C-A +P0CL40 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL40 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL40 UniProtKB Compositional bias 103 106 . . . Note=Poly-Ser +##sequence-region Q12219 1 294 +Q12219 UniProtKB Chain 1 294 . . . ID=PRO_0000237656;Note=Uncharacterized protein YOR114W +##sequence-region P34161 1 385 +P34161 UniProtKB Chain 1 385 . . . ID=PRO_0000049387;Note=Homeobox protein YOX1 +P34161 UniProtKB DNA binding 176 235 . . . Note=Homeobox;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00108 +P34161 UniProtKB Sequence conflict 291 296 . . . Note=PRPHHS->QGLIIP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03083 1 165 +Q03083 UniProtKB Chain 1 165 . . . ID=PRO_0000240704;Note=Uncharacterized protein YPL034W +##sequence-region O13520 1 182 +O13520 UniProtKB Chain 1 182 . . . ID=PRO_0000299799;Note=Putative uncharacterized protein YPL044C +O13520 UniProtKB Transmembrane 76 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13520 UniProtKB Transmembrane 114 130 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13520 UniProtKB Compositional bias 40 49 . . . Note=Poly-Ser +##sequence-region Q12160 1 140 +Q12160 UniProtKB Chain 1 140 . . . ID=PRO_0000257824;Note=Uncharacterized protein YPR063C +Q12160 UniProtKB Transmembrane 91 107 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12160 UniProtKB Glycosylation 36 36 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40323 1 161 +P40323 UniProtKB Chain 1 161 . . . ID=PRO_0000203493;Note=Uncharacterized protein YPL073C +##sequence-region Q06821 1 456 +Q06821 UniProtKB Chain 1 456 . . . ID=PRO_0000242638;Note=Uncharacterized protein YPR084W +##sequence-region O13587 1 100 +O13587 UniProtKB Chain 1 100 . . . ID=PRO_0000299823;Note=Uncharacterized protein YPR096C +##sequence-region Q02873 1 248 +Q02873 UniProtKB Transit peptide 1 26 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02873 UniProtKB Chain 27 248 . . . ID=PRO_0000238646;Note=UPF0651 protein YPL107W%2C mitochondrial +Q02873 UniProtKB Domain 69 116 . . . Note=Oxidoreductase-like +##sequence-region Q06116 1 2489 +Q06116 UniProtKB Chain 1 2489 . . . ID=PRO_0000257827;Note=Uncharacterized protein YPR117W +Q06116 UniProtKB Transmembrane 19 39 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Transmembrane 128 148 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Coiled coil 1610 1676 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Modified residue 2254 2254 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06116 UniProtKB Modified residue 2278 2278 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06116 UniProtKB Glycosylation 191 191 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Glycosylation 210 210 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Glycosylation 311 311 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Glycosylation 452 452 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Glycosylation 468 468 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Glycosylation 605 605 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Glycosylation 638 638 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Glycosylation 663 663 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Glycosylation 698 698 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Glycosylation 789 789 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Glycosylation 835 835 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Glycosylation 981 981 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Glycosylation 1255 1255 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Glycosylation 1404 1404 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Glycosylation 1476 1476 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Glycosylation 1978 1978 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Glycosylation 2189 2189 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06116 UniProtKB Glycosylation 2279 2279 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region O13567 1 102 +O13567 UniProtKB Chain 1 102 . . . ID=PRO_0000299826;Note=Putative uncharacterized protein YPR126C +O13567 UniProtKB Transmembrane 38 58 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13567 UniProtKB Transmembrane 64 84 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CX60 1 440 +P0CX60 UniProtKB Chain 1 440 . . . ID=PRO_0000409806;Note=Transposon Ty1-PR2 Gag polyprotein +P0CX60 UniProtKB Chain 1 401 . . . ID=PRO_0000409807;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX60 UniProtKB Peptide 402 440 . . . ID=PRO_0000409808;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX60 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX60 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0CX60 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX60 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region Q06523 1 435 +Q06523 UniProtKB Chain 1 435 . . . ID=PRO_0000257829;Note=Uncharacterized protein YPR148C +Q06523 UniProtKB Modified residue 47 47 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q8TGR9 1 32 +Q8TGR9 UniProtKB Chain 1 32 . . . ID=PRO_0000238654;Note=Uncharacterized protein YPL152W-A +##sequence-region Q8TGK8 1 94 +Q8TGK8 UniProtKB Chain 1 94 . . . ID=PRO_0000299832;Note=Putative uncharacterized protein YPR160C-A +Q8TGK8 UniProtKB Sequence conflict 12 12 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q8TGK8 UniProtKB Sequence conflict 79 80 . . . Note=PT->RR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0C5R8 1 61 +P0C5R8 UniProtKB Chain 1 61 . . . ID=PRO_0000309066;Note=Putative uncharacterized protein YPR170W-A +P0C5R8 UniProtKB Transmembrane 5 25 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C5R8 UniProtKB Transmembrane 29 49 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08927 1 131 +Q08927 UniProtKB Chain 1 131 . . . ID=PRO_0000299807;Note=Putative uncharacterized protein YPL185W +Q08927 UniProtKB Transmembrane 13 35 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08927 UniProtKB Transmembrane 60 79 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08927 UniProtKB Transmembrane 100 119 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08953 1 137 +Q08953 UniProtKB Chain 1 137 . . . ID=PRO_0000299808;Note=Putative uncharacterized protein YPL197C +##sequence-region Q08995 1 1032 +Q08995 UniProtKB Chain 1 1032 . . . ID=PRO_0000268169;Note=Y' element ATP-dependent helicase YPR204W +Q08995 UniProtKB Domain 1 175 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q08995 UniProtKB Domain 232 381 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q08995 UniProtKB Nucleotide binding 11 18 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q08995 UniProtKB Motif 121 124 . . . Note=DEAH box +Q08995 UniProtKB Compositional bias 459 631 . . . Note=Thr-rich +##sequence-region Q08971 1 146 +Q08971 UniProtKB Chain 1 146 . . . ID=PRO_0000242144;Note=Protein PBDC1 homolog +Q08971 UniProtKB Beta strand 4 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN +Q08971 UniProtKB Helix 12 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN +Q08971 UniProtKB Helix 48 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN +Q08971 UniProtKB Turn 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN +Q08971 UniProtKB Helix 65 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN +Q08971 UniProtKB Turn 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN +Q08971 UniProtKB Helix 79 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN +Q08971 UniProtKB Turn 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN +Q08971 UniProtKB Beta strand 103 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN +Q08971 UniProtKB Beta strand 118 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN +Q08971 UniProtKB Helix 123 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN +Q08971 UniProtKB Turn 136 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN +Q08971 UniProtKB Helix 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JYN +##sequence-region Q12058 1 100 +Q12058 UniProtKB Chain 1 100 . . . ID=PRO_0000299812;Note=Putative uncharacterized protein YPL251W +Q12058 UniProtKB Compositional bias 51 57 . . . Note=Poly-Val +##sequence-region Q08984 1 517 +Q08984 UniProtKB Chain 1 517 . . . ID=PRO_0000242637;Note=Uncharacterized protein YPL272C +##sequence-region P0CX97 1 160 +P0CX97 UniProtKB Chain 1 160 . . . ID=PRO_0000410454;Note=UPF0479 membrane protein YPL283W-B +P0CX97 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX97 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX97 UniProtKB Compositional bias 103 106 . . . Note=Poly-Ser +##sequence-region Q12159 1 226 +Q12159 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +Q12159 UniProtKB Chain 2 226 . . . ID=PRO_0000082007;Note=RNA annealing protein YRA1 +Q12159 UniProtKB Domain 78 158 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q12159 UniProtKB Compositional bias 201 210 . . . Note=Arg/Lys-rich (basic) +Q12159 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +Q12159 UniProtKB Modified residue 8 8 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q12159 UniProtKB Modified residue 100 100 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12159 UniProtKB Helix 212 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +##sequence-region P53107 1 440 +P53107 UniProtKB Chain 1 440 . . . ID=PRO_0000213672;Note=Ran-specific GTPase-activating protein 30 +P53107 UniProtKB Domain 1 314 . . . Note=RanBD1 +P53107 UniProtKB Modified residue 272 272 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q12436 1 422 +Q12436 UniProtKB Chain 1 422 . . . ID=PRO_0000068769;Note=Zinc-regulated transporter 2 +Q12436 UniProtKB Topological domain 1 27 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12436 UniProtKB Transmembrane 28 48 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12436 UniProtKB Topological domain 49 60 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12436 UniProtKB Transmembrane 61 81 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12436 UniProtKB Topological domain 82 99 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12436 UniProtKB Transmembrane 100 120 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12436 UniProtKB Topological domain 121 262 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12436 UniProtKB Transmembrane 263 283 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12436 UniProtKB Topological domain 284 290 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12436 UniProtKB Transmembrane 291 311 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12436 UniProtKB Topological domain 312 326 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12436 UniProtKB Transmembrane 327 347 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12436 UniProtKB Topological domain 348 358 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12436 UniProtKB Transmembrane 359 379 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12436 UniProtKB Topological domain 380 400 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12436 UniProtKB Transmembrane 401 421 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12436 UniProtKB Topological domain 422 422 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12436 UniProtKB Region 276 277 . . . Note=Heavy metals binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12436 UniProtKB Modified residue 148 148 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12436 UniProtKB Modified residue 149 149 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12436 UniProtKB Modified residue 162 162 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12436 UniProtKB Modified residue 170 170 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12436 UniProtKB Modified residue 188 188 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P32527 1 433 +P32527 UniProtKB Chain 1 433 . . . ID=PRO_0000071122;Note=Zuotin +P32527 UniProtKB Domain 98 170 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +P32527 UniProtKB Compositional bias 306 357 . . . Note=Ala/Lys-rich +P32527 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198 +P32527 UniProtKB Mutagenesis 128 128 . . . Note=Loss of function%2C but still forms a heterodimer with SSZ1 and associates with ribosomes. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11929994;Dbxref=PMID:11929994 +P32527 UniProtKB Helix 184 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DJE +P32527 UniProtKB Beta strand 199 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DJE +P32527 UniProtKB Helix 214 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DJE +P32527 UniProtKB Helix 234 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DJE +P32527 UniProtKB Helix 249 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DJE +P32527 UniProtKB Helix 284 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DJE +P32527 UniProtKB Helix 348 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LWX +P32527 UniProtKB Helix 371 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LWX +P32527 UniProtKB Helix 374 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LWX +P32527 UniProtKB Helix 390 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LWX +P32527 UniProtKB Helix 404 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LWX +P32527 UniProtKB Helix 408 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LWX +P32527 UniProtKB Helix 426 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LWX +P32527 UniProtKB Turn 430 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LWX +##sequence-region P40523 1 627 +P40523 UniProtKB Chain 1 627 . . . ID=PRO_0000202989;Note=Uncharacterized protein YIL055C +P40523 UniProtKB Modified residue 559 559 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P40445 1 542 +P40445 UniProtKB Chain 1 542 . . . ID=PRO_0000121373;Note=Uncharacterized transporter YIL166C +P40445 UniProtKB Topological domain 1 78 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Transmembrane 79 99 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Topological domain 100 119 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Transmembrane 120 140 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Topological domain 141 147 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Transmembrane 148 168 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Topological domain 169 176 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Transmembrane 177 197 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Topological domain 198 208 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Transmembrane 209 229 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Topological domain 230 241 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Transmembrane 242 262 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Topological domain 263 326 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Transmembrane 327 347 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Topological domain 348 359 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Transmembrane 360 380 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Topological domain 381 387 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Transmembrane 388 408 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Topological domain 409 416 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Transmembrane 417 437 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Topological domain 438 482 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Transmembrane 483 503 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40445 UniProtKB Topological domain 504 542 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E775 1 16 +Q3E775 UniProtKB Chain 1 16 . . . ID=PRO_0000245417;Note=Uncharacterized protein YJR151W-A +##sequence-region P0C5P0 1 93 +P0C5P0 UniProtKB Chain 1 93 . . . ID=PRO_0000309038;Note=Uncharacterized protein YJL197C-A +##sequence-region P47114 1 497 +P47114 UniProtKB Chain 1 497 . . . ID=PRO_0000203096;Note=Uncharacterized vacuolar membrane protein YJR054W +P47114 UniProtKB Topological domain 1 29 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47114 UniProtKB Transmembrane 30 50 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47114 UniProtKB Topological domain 51 80 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47114 UniProtKB Transmembrane 81 101 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47114 UniProtKB Topological domain 102 216 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47114 UniProtKB Transmembrane 217 237 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47114 UniProtKB Topological domain 238 497 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47114 UniProtKB Modified residue 291 291 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47114 UniProtKB Modified residue 319 319 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P47062 1 111 +P47062 UniProtKB Chain 1 111 . . . ID=PRO_0000203071;Note=Uncharacterized protein YJL028W +P47062 UniProtKB Transmembrane 29 49 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47062 UniProtKB Transmembrane 52 72 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CL24 1 45 +P0CL24 UniProtKB Chain 1 45 . . . ID=PRO_0000406004;Note=Putative UPF0377 protein YJL222W-B +##sequence-region P46992 1 396 +P46992 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46992 UniProtKB Chain 20 368 . . . ID=PRO_0000042986;Note=Cell wall protein YJL171C +P46992 UniProtKB Propeptide 369 396 . . . ID=PRO_0000406124;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46992 UniProtKB Lipidation 368 368 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46992 UniProtKB Glycosylation 51 51 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46992 UniProtKB Glycosylation 99 99 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46992 UniProtKB Glycosylation 122 122 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46992 UniProtKB Glycosylation 146 146 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46992 UniProtKB Glycosylation 174 174 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46992 UniProtKB Glycosylation 219 219 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46992 UniProtKB Glycosylation 249 249 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46992 UniProtKB Glycosylation 267 267 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46992 UniProtKB Glycosylation 300 300 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46992 UniProtKB Glycosylation 328 328 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46992 UniProtKB Glycosylation 346 346 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46992 UniProtKB Sequence conflict 366 366 . . . Note=K->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46992 UniProtKB Sequence conflict 371 371 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46992 UniProtKB Sequence conflict 374 374 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40891 1 150 +P40891 UniProtKB Chain 1 150 . . . ID=PRO_0000203010;Note=Putative uncharacterized protein YJL220W +##sequence-region P47087 1 207 +P47087 UniProtKB Chain 1 207 . . . ID=PRO_0000203083;Note=Uncharacterized protein YJR012C +P47087 UniProtKB Transmembrane 17 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47087 UniProtKB Modified residue 176 176 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q2V2P2 1 73 +Q2V2P2 UniProtKB Chain 1 73 . . . ID=PRO_0000245422;Note=Uncharacterized protein YKL065W-A +Q2V2P2 UniProtKB Transmembrane 37 54 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E7A0 1 39 +Q3E7A0 UniProtKB Chain 1 39 . . . ID=PRO_0000245419;Note=Uncharacterized protein YKL106C-A +##sequence-region P0C5P4 1 50 +P0C5P4 UniProtKB Chain 1 50 . . . ID=PRO_0000309042;Note=Putative uncharacterized protein YKL162C-A +##sequence-region P32859 1 130 +P32859 UniProtKB Chain 1 130 . . . ID=PRO_0000203184;Note=Putative uncharacterized protein YKL036C +##sequence-region P33324 1 310 +P33324 UniProtKB Chain 1 310 . . . ID=PRO_0000210747;Note=CRAL-TRIO domain-containing protein YKL091C +P33324 UniProtKB Domain 101 274 . . . Note=CRAL-TRIO;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00056 +P33324 UniProtKB Helix 5 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 27 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 51 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Turn 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 65 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 87 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 95 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Beta strand 111 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Beta strand 122 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 133 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 142 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 160 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Beta strand 175 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 186 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 193 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Beta strand 211 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 223 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Turn 228 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 231 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 236 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Beta strand 242 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 249 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 259 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 264 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 279 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Beta strand 282 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B74 +P33324 UniProtKB Helix 286 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Turn 290 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +P33324 UniProtKB Helix 304 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q8G +##sequence-region P36061 1 205 +P36061 UniProtKB Chain 1 205 . . . ID=PRO_0000203146;Note=Putative uncharacterized protein YKL147C +##sequence-region Q07799 1 665 +Q07799 UniProtKB Chain 1 665 . . . ID=PRO_0000247098;Note=Uncharacterized protein YLL007C +##sequence-region Q07811 1 101 +Q07811 UniProtKB Chain 1 101 . . . ID=PRO_0000299602;Note=Putative uncharacterized protein YLL020C +Q07811 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07811 UniProtKB Transmembrane 66 86 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07990 1 161 +Q07990 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07990 UniProtKB Chain 25 139 . . . ID=PRO_0000247444;Note=Cell wall protein YLR042C +Q07990 UniProtKB Propeptide 140 161 . . . ID=PRO_0000247445;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07990 UniProtKB Compositional bias 62 136 . . . Note=Ser-rich +Q07990 UniProtKB Lipidation 139 139 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07990 UniProtKB Glycosylation 77 77 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07990 UniProtKB Glycosylation 104 104 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07990 UniProtKB Glycosylation 120 120 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12155 1 161 +Q12155 UniProtKB Chain 1 161 . . . ID=PRO_0000247205;Note=Uncharacterized membrane protein YLR050C +Q12155 UniProtKB Topological domain 1 10 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12155 UniProtKB Transmembrane 11 31 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12155 UniProtKB Topological domain 32 61 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12155 UniProtKB Transmembrane 62 82 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12155 UniProtKB Topological domain 83 101 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12155 UniProtKB Transmembrane 102 122 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12155 UniProtKB Topological domain 123 161 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12155 UniProtKB Domain 7 159 . . . Note=EXPERA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01087 +##sequence-region Q07888 1 1374 +Q07888 UniProtKB Chain 1 1374 . . . ID=PRO_0000268168;Note=Y' element ATP-dependent helicase YLL067C +Q07888 UniProtKB Domain 375 552 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q07888 UniProtKB Domain 609 758 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q07888 UniProtKB Nucleotide binding 388 395 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q07888 UniProtKB Motif 498 501 . . . Note=DEAH box +Q07888 UniProtKB Compositional bias 836 1008 . . . Note=Thr-rich +##sequence-region Q08027 1 131 +Q08027 UniProtKB Chain 1 131 . . . ID=PRO_0000299610;Note=Putative uncharacterized protein YLR101C +Q08027 UniProtKB Transmembrane 3 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08027 UniProtKB Transmembrane 41 61 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08027 UniProtKB Transmembrane 98 118 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12130 1 139 +Q12130 UniProtKB Chain 1 139 . . . ID=PRO_0000299612;Note=Uncharacterized protein YLR112W +##sequence-region Q12312 1 125 +Q12312 UniProtKB Chain 1 125 . . . ID=PRO_0000299614;Note=Uncharacterized protein YLR122C +Q12312 UniProtKB Transmembrane 7 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CX75 1 440 +P0CX75 UniProtKB Chain 1 440 . . . ID=PRO_0000409800;Note=Transposon Ty1-LR3 Gag polyprotein +P0CX75 UniProtKB Chain 1 401 . . . ID=PRO_0000409801;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX75 UniProtKB Peptide 402 440 . . . ID=PRO_0000409802;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX75 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX75 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0CX75 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX75 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +P0CX75 UniProtKB Sequence conflict 255 255 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q99296 1 730 +Q99296 UniProtKB Chain 1 730 . . . ID=PRO_0000262875;Note=Uncharacterized protein YLR149C +Q99296 UniProtKB Compositional bias 455 460 . . . Note=Poly-Asn +Q99296 UniProtKB Modified residue 82 82 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +Q99296 UniProtKB Modified residue 89 89 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q99296 UniProtKB Modified residue 483 483 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q99296 UniProtKB Modified residue 651 651 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P54072 1 576 +P54072 UniProtKB Chain 1 576 . . . ID=PRO_0000123806;Note=Uncharacterized transporter YLR152C +P54072 UniProtKB Topological domain 1 8 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Transmembrane 9 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Topological domain 30 45 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Transmembrane 46 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Topological domain 67 71 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Transmembrane 72 92 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Topological domain 93 103 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Transmembrane 104 124 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Topological domain 125 141 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Transmembrane 142 162 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Topological domain 163 400 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Transmembrane 401 421 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Topological domain 422 437 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Transmembrane 438 458 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Topological domain 459 476 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Transmembrane 477 497 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Topological domain 498 512 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Transmembrane 513 533 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Topological domain 534 545 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Transmembrane 546 566 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54072 UniProtKB Topological domain 567 576 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CY03 1 43 +P0CY03 UniProtKB Chain 1 43 . . . ID=PRO_0000410459;Note=Uncharacterized protein YLR156C-A +##sequence-region P0C2J5 1 1598 +P0C2J5 UniProtKB Chain 1 1598 . . . ID=PRO_0000279332;Note=Transposon Ty2-LR2 Gag-Pol polyprotein +P0C2J5 UniProtKB Chain 1 397 . . . ID=PRO_0000279333;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J5 UniProtKB Chain 398 578 . . . ID=PRO_0000279334;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J5 UniProtKB Chain 579 1232 . . . ID=PRO_0000279335;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J5 UniProtKB Chain 1233 1598 . . . ID=PRO_0000279336;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J5 UniProtKB Domain 656 831 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J5 UniProtKB Domain 1353 1491 . . . Note=Reverse transcriptase Ty1/copia-type +P0C2J5 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J5 UniProtKB Region 579 636 . . . Note=Integrase-type zinc finger-like +P0C2J5 UniProtKB Motif 1193 1227 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J5 UniProtKB Active site 457 457 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J5 UniProtKB Metal binding 667 667 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J5 UniProtKB Metal binding 732 732 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J5 UniProtKB Metal binding 1361 1361 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J5 UniProtKB Metal binding 1442 1442 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J5 UniProtKB Metal binding 1443 1443 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0C2J5 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J5 UniProtKB Site 578 579 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J5 UniProtKB Site 1232 1233 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q3E732 1 38 +Q3E732 UniProtKB Chain 1 38 . . . ID=PRO_0000247136;Note=Putative uncharacterized protein YLR264C-A +##sequence-region O13550 1 116 +O13550 UniProtKB Chain 1 116 . . . ID=PRO_0000299627;Note=Putative uncharacterized protein YLR269C +O13550 UniProtKB Transmembrane 5 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q05854 1 1341 +Q05854 UniProtKB Chain 1 1341 . . . ID=PRO_0000115003;Note=Uncharacterized transcriptional regulatory protein YLR278C +Q05854 UniProtKB DNA binding 41 68 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +Q05854 UniProtKB Compositional bias 255 261 . . . Note=Poly-Asn +Q05854 UniProtKB Compositional bias 873 885 . . . Note=Poly-Ser +Q05854 UniProtKB Compositional bias 918 943 . . . Note=Poly-Asn +Q05854 UniProtKB Compositional bias 1231 1238 . . . Note=Poly-Gln +Q05854 UniProtKB Modified residue 1143 1143 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region Q05863 1 155 +Q05863 UniProtKB Transit peptide 1 17 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05863 UniProtKB Chain 18 155 . . . ID=PRO_0000247341;Note=Uncharacterized peptide chain release factor-like protein YLR281C%2C mitochondrial +##sequence-region Q8TGM4 1 44 +Q8TGM4 UniProtKB Chain 1 44 . . . ID=PRO_0000299631;Note=Putative uncharacterized protein YLR286W-A +##sequence-region O13544 1 120 +O13544 UniProtKB Chain 1 120 . . . ID=PRO_0000299635;Note=Uncharacterized protein YLR302C +O13544 UniProtKB Transmembrane 40 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region O13553 1 144 +O13553 UniProtKB Chain 1 144 . . . ID=PRO_0000299636;Note=Putative uncharacterized protein YLR317W +##sequence-region Q8TGM2 1 46 +Q8TGM2 UniProtKB Chain 1 46 . . . ID=PRO_0000299639;Note=Putative uncharacterized protein YLR347W-A +##sequence-region Q3E747 1 85 +Q3E747 UniProtKB Chain 1 85 . . . ID=PRO_0000247215;Note=Uncharacterized protein YLR363W-A +Q3E747 UniProtKB Compositional bias 4 48 . . . Note=Lys-rich +##sequence-region O13576 1 127 +O13576 UniProtKB Chain 1 127 . . . ID=PRO_0000299650;Note=Putative uncharacterized protein YLR434C +##sequence-region P54007 1 376 +P54007 UniProtKB Chain 1 376 . . . ID=PRO_0000203236;Note=Uncharacterized protein YLR460C +##sequence-region Q06493 1 454 +Q06493 UniProtKB Transit peptide 1 45 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06493 UniProtKB Chain 46 454 . . . ID=PRO_0000244478;Note=LETM1 domain-containing protein YLH47%2C mitochondrial +Q06493 UniProtKB Topological domain 46 136 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06493 UniProtKB Transmembrane 137 157 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06493 UniProtKB Topological domain 158 454 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06493 UniProtKB Domain 177 371 . . . Note=Letm1 RBD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01094 +Q06493 UniProtKB Coiled coil 376 423 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06493 UniProtKB Sequence conflict 265 265 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06493 UniProtKB Sequence conflict 265 265 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06493 UniProtKB Sequence conflict 439 439 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06493 UniProtKB Sequence conflict 439 439 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06493 UniProtKB Sequence conflict 442 442 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06493 UniProtKB Sequence conflict 442 442 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CD98 1 152 +P0CD98 UniProtKB Chain 1 152 . . . ID=PRO_0000391656;Note=Putative uncharacterized protein YLL053C +P0CD98 UniProtKB Topological domain 1 5 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD98 UniProtKB Transmembrane 6 26 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD98 UniProtKB Topological domain 27 38 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD98 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD98 UniProtKB Topological domain 60 65 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD98 UniProtKB Transmembrane 66 86 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD98 UniProtKB Topological domain 87 110 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD98 UniProtKB Transmembrane 111 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD98 UniProtKB Topological domain 132 152 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD98 UniProtKB Motif 92 94 . . . Note=NPA +##sequence-region Q3E7A6 1 36 +Q3E7A6 UniProtKB Chain 1 36 . . . ID=PRO_0000247783;Note=Uncharacterized protein YML007C-A%2C mitochondrial +##sequence-region Q03879 1 124 +Q03879 UniProtKB Chain 1 124 . . . ID=PRO_0000203296;Note=Uncharacterized protein YMR122C +##sequence-region Q6B108 1 100 +Q6B108 UniProtKB Chain 1 100 . . . ID=PRO_0000299660;Note=Putative uncharacterized protein YML116W-A +##sequence-region Q04706 1 440 +Q04706 UniProtKB Chain 1 440 . . . ID=PRO_0000203498;Note=Transposon Ty1-ML1 Gag polyprotein +Q04706 UniProtKB Chain 1 401 . . . ID=PRO_0000279121;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04706 UniProtKB Peptide 402 440 . . . ID=PRO_0000279122;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04706 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04706 UniProtKB Compositional bias 72 146 . . . Note=Pro-rich +Q04706 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04706 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region Q3E842 1 84 +Q3E842 UniProtKB Chain 1 84 . . . ID=PRO_0000247787;Note=Uncharacterized endoplasmic reticulum membrane protein YMR122W-A +Q3E842 UniProtKB Transmembrane 66 83 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E842 UniProtKB Compositional bias 3 50 . . . Note=Ser-rich +Q3E842 UniProtKB Glycosylation 45 45 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CX69 1 440 +P0CX69 UniProtKB Chain 1 440 . . . ID=PRO_0000409788;Note=Transposon Ty1-MR2 Gag polyprotein +P0CX69 UniProtKB Chain 1 401 . . . ID=PRO_0000409789;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX69 UniProtKB Peptide 402 440 . . . ID=PRO_0000409790;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX69 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX69 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0CX69 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX69 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region Q6B0X2 1 106 +Q6B0X2 UniProtKB Signal peptide 1 27 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q6B0X2 UniProtKB Chain 28 106 . . . ID=PRO_0000299671;Note=Putative uncharacterized protein YMR158W-B +Q6B0X2 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q6B0X2 UniProtKB Sequence conflict 79 79 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40211 1 102 +P40211 UniProtKB Chain 1 102 . . . ID=PRO_0000203304;Note=Uncharacterized protein YMR141C +##sequence-region A0A023PZH5 1 115 +A0A023PZH5 UniProtKB Chain 1 115 . . . ID=PRO_0000431053;Note=Putative uncharacterized membrane protein YMR290W-A +A0A023PZH5 UniProtKB Transmembrane 15 35 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZH5 UniProtKB Transmembrane 52 72 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZH5 UniProtKB Compositional bias 58 66 . . . Note=Poly-Leu;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZH5 UniProtKB Compositional bias 99 107 . . . Note=Poly-Lys;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PYJ7 1 116 +A0A023PYJ7 UniProtKB Chain 1 116 . . . ID=PRO_0000431051;Note=Putative uncharacterized membrane protein YMR304C-A +A0A023PYJ7 UniProtKB Transmembrane 55 77 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PYJ7 UniProtKB Transmembrane 87 109 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PXQ9 1 102 +A0A023PXQ9 UniProtKB Chain 1 102 . . . ID=PRO_0000431049;Note=Putative uncharacterized membrane protein YMR316C-B +A0A023PXQ9 UniProtKB Transmembrane 33 55 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXQ9 UniProtKB Transmembrane 57 79 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXQ9 UniProtKB Compositional bias 44 81 . . . Note=Val-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00020 +##sequence-region Q03829 1 368 +Q03829 UniProtKB Chain 1 368 . . . ID=PRO_0000090699;Note=Uncharacterized mitochondrial carrier YMR166C +Q03829 UniProtKB Transmembrane 56 77 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03829 UniProtKB Transmembrane 115 135 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03829 UniProtKB Transmembrane 149 165 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03829 UniProtKB Transmembrane 219 239 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03829 UniProtKB Transmembrane 260 280 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03829 UniProtKB Transmembrane 332 353 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03829 UniProtKB Repeat 51 138 . . . Note=Solcar 1 +Q03829 UniProtKB Repeat 146 240 . . . Note=Solcar 2 +Q03829 UniProtKB Repeat 254 360 . . . Note=Solcar 3 +##sequence-region Q03219 1 274 +Q03219 UniProtKB Chain 1 274 . . . ID=PRO_0000203319;Note=Uncharacterized protein YMR178W +Q03219 UniProtKB Modified residue 263 263 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q3E843 1 45 +Q3E843 UniProtKB Chain 1 45 . . . ID=PRO_0000268629;Note=Uncharacterized protein YMR158C-A +##sequence-region Q03649 1 449 +Q03649 UniProtKB Chain 1 449 . . . ID=PRO_0000212455;Note=Putative esterase YMR210W +Q03649 UniProtKB Domain 151 392 . . . Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03649 UniProtKB Active site 232 232 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03649 UniProtKB Active site 364 364 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03649 UniProtKB Active site 392 392 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03649 UniProtKB Cross-link 82 82 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q8TGM0 1 37 +Q8TGM0 UniProtKB Chain 1 37 . . . ID=PRO_0000299673;Note=Uncharacterized protein YMR272W-A +##sequence-region Q04897 1 101 +Q04897 UniProtKB Chain 1 101 . . . ID=PRO_0000203360;Note=Uncharacterized protein YMR320W +##sequence-region Q03722 1 664 +Q03722 UniProtKB Chain 1 664 . . . ID=PRO_0000203260;Note=Uncharacterized protein YML020W +Q03722 UniProtKB Sequence conflict 34 34 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38087 1 329 +P38087 UniProtKB Transit peptide 1 33 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38087 UniProtKB Chain 34 329 . . . ID=PRO_0000019266;Note=Carrier protein YMC2%2C mitochondrial +P38087 UniProtKB Transmembrane 38 58 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38087 UniProtKB Transmembrane 84 104 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38087 UniProtKB Transmembrane 140 160 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38087 UniProtKB Transmembrane 205 225 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38087 UniProtKB Transmembrane 243 263 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38087 UniProtKB Transmembrane 297 318 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38087 UniProtKB Repeat 34 115 . . . Note=Solcar 1 +P38087 UniProtKB Repeat 143 226 . . . Note=Solcar 2 +P38087 UniProtKB Repeat 238 325 . . . Note=Solcar 3 +##sequence-region Q03697 1 442 +Q03697 UniProtKB Chain 1 442 . . . ID=PRO_0000213402;Note=Putative nucleotide-sugar transporter YMD8 +Q03697 UniProtKB Topological domain 1 3 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Transmembrane 4 24 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Topological domain 25 32 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Topological domain 54 76 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Transmembrane 77 97 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Topological domain 98 107 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Transmembrane 108 128 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Topological domain 129 132 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Transmembrane 133 153 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Topological domain 154 166 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Transmembrane 167 187 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Topological domain 188 254 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Transmembrane 255 275 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Topological domain 276 301 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Transmembrane 302 322 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Topological domain 323 329 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Transmembrane 330 350 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Topological domain 351 355 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Transmembrane 356 376 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Topological domain 377 442 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03697 UniProtKB Modified residue 209 209 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03697 UniProtKB Glycosylation 99 99 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53957 1 106 +P53957 UniProtKB Chain 1 106 . . . ID=PRO_0000203455;Note=Putative uncharacterized protein YNL043C +##sequence-region P53912 1 376 +P53912 UniProtKB Chain 1 376 . . . ID=PRO_0000203426;Note=Uncharacterized protein YNL134C +##sequence-region P40168 1 261 +P40168 UniProtKB Chain 1 261 . . . ID=PRO_0000203398;Note=Uncharacterized protein YNL195C +##sequence-region Q08411 1 143 +Q08411 UniProtKB Chain 1 143 . . . ID=PRO_0000299705;Note=Putative uncharacterized protein YOR041C +Q08411 UniProtKB Compositional bias 9 121 . . . Note=Ser-rich +##sequence-region Q99345 1 113 +Q99345 UniProtKB Chain 1 113 . . . ID=PRO_0000299692;Note=Uncharacterized protein YOL085C +Q99345 UniProtKB Compositional bias 91 96 . . . Note=Poly-Asp +##sequence-region P0C5Q9 1 33 +P0C5Q9 UniProtKB Chain 1 33 . . . ID=PRO_0000309057;Note=Putative uncharacterized protein YOR008W-B +##sequence-region Q08503 1 116 +Q08503 UniProtKB Chain 1 116 . . . ID=PRO_0000299711;Note=Putative uncharacterized protein YOR102W +##sequence-region Q99210 1 232 +Q99210 UniProtKB Chain 1 232 . . . ID=PRO_0000123091;Note=Maf-like protein YOR111W +Q99210 UniProtKB Active site 52 52 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12273 1 1755 +Q12273 UniProtKB Chain 1 1755 . . . ID=PRO_0000279153;Note=Transposon Ty1-OL Gag-Pol polyprotein +Q12273 UniProtKB Chain 1 401 . . . ID=PRO_0000279154;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12273 UniProtKB Chain 402 582 . . . ID=PRO_0000279155;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12273 UniProtKB Chain 583 1217 . . . ID=PRO_0000279156;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12273 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279157;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12273 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12273 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +Q12273 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +Q12273 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12273 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q12273 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12273 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q12273 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q12273 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12273 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12273 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12273 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12273 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12273 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12273 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12273 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12273 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12273 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12273 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12273 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region Q08533 1 101 +Q08533 UniProtKB Chain 1 101 . . . ID=PRO_0000299753;Note=Putative uncharacterized protein YOR146W +Q08533 UniProtKB Transmembrane 70 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08533 UniProtKB Compositional bias 41 69 . . . Note=Ser-rich +##sequence-region Q12249 1 139 +Q12249 UniProtKB Chain 1 139 . . . ID=PRO_0000299725;Note=Putative uncharacterized protein YOR218C +Q12249 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12113 1 1770 +Q12113 UniProtKB Chain 1 1770 . . . ID=PRO_0000279340;Note=Transposon Ty2-OR1 Gag-Pol polyprotein +Q12113 UniProtKB Chain 1 397 . . . ID=PRO_0000279341;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12113 UniProtKB Chain 398 578 . . . ID=PRO_0000279342;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12113 UniProtKB Chain 579 1232 . . . ID=PRO_0000279343;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12113 UniProtKB Chain 1233 1770 . . . ID=PRO_0000279344;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12113 UniProtKB Domain 656 831 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12113 UniProtKB Domain 1353 1491 . . . Note=Reverse transcriptase Ty1/copia-type +Q12113 UniProtKB Domain 1625 1767 . . . Note=RNase H Ty1/copia-type +Q12113 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12113 UniProtKB Region 579 636 . . . Note=Integrase-type zinc finger-like +Q12113 UniProtKB Motif 1193 1227 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12113 UniProtKB Active site 457 457 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12113 UniProtKB Metal binding 667 667 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12113 UniProtKB Metal binding 732 732 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12113 UniProtKB Metal binding 1361 1361 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12113 UniProtKB Metal binding 1442 1442 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12113 UniProtKB Metal binding 1443 1443 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12113 UniProtKB Metal binding 1625 1625 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12113 UniProtKB Metal binding 1667 1667 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12113 UniProtKB Metal binding 1700 1700 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12113 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12113 UniProtKB Site 578 579 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12113 UniProtKB Site 1232 1233 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q08734 1 132 +Q08734 UniProtKB Chain 1 132 . . . ID=PRO_0000245282;Note=Uncharacterized protein YOR268C +Q08734 UniProtKB Transmembrane 92 112 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12012 1 251 +Q12012 UniProtKB Chain 1 251 . . . ID=PRO_0000142373;Note=Uncharacterized protein YOR289W +Q12012 UniProtKB Domain 21 246 . . . Note=AMMECR1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00467 +##sequence-region Q99318 1 101 +Q99318 UniProtKB Chain 1 101 . . . ID=PRO_0000299736;Note=Putative uncharacterized protein YOR318C +##sequence-region Q8TGL1 1 26 +Q8TGL1 UniProtKB Chain 1 26 . . . ID=PRO_0000299739;Note=Putative uncharacterized protein YOR335W-A +##sequence-region P0C5R2 1 82 +P0C5R2 UniProtKB Chain 1 82 . . . ID=PRO_0000309060;Note=Putative uncharacterized protein YOR072W-A +##sequence-region Q08428 1 113 +Q08428 UniProtKB Chain 1 113 . . . ID=PRO_0000299707;Note=Putative uncharacterized protein YOR053W +Q08428 UniProtKB Transmembrane 4 26 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08428 UniProtKB Compositional bias 21 76 . . . Note=Arg/His-rich +##sequence-region Q3E834 1 85 +Q3E834 UniProtKB Chain 1 85 . . . ID=PRO_0000232636;Note=Protein transport protein YOS1 +Q3E834 UniProtKB Transmembrane 2 22 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E834 UniProtKB Transmembrane 65 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E834 UniProtKB Mutagenesis 18 18 . . . Note=In YOS1-1%3B impairs interaction with YIP1%2C blocks ER-Golgi protein transport%2C and causes a severe growth defect at 37 degrees Celsius. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15659647;Dbxref=PMID:15659647 +Q3E834 UniProtKB Mutagenesis 69 69 . . . Note=Lethal. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15659647;Dbxref=PMID:15659647 +##sequence-region Q12145 1 317 +Q12145 UniProtKB Chain 1 317 . . . ID=PRO_0000255974;Note=Zinc finger protein YPR013C +Q12145 UniProtKB Zinc finger 254 276 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q12145 UniProtKB Zinc finger 282 306 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +##sequence-region P0C5R5 1 86 +P0C5R5 UniProtKB Chain 1 86 . . . ID=PRO_0000309063;Note=Putative uncharacterized protein YPR016W-A +##sequence-region Q12139 1 1133 +Q12139 UniProtKB Chain 1 1133 . . . ID=PRO_0000255976;Note=Zinc finger protein YPR022C +Q12139 UniProtKB Zinc finger 31 55 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q12139 UniProtKB Zinc finger 61 91 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q12139 UniProtKB Compositional bias 159 320 . . . Note=Gln-rich +##sequence-region Q3E752 1 67 +Q3E752 UniProtKB Chain 1 67 . . . ID=PRO_0000242699;Note=Uncharacterized protein YPR036W-A +Q3E752 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q3E752 UniProtKB Modified residue 32 32 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q02826 1 108 +Q02826 UniProtKB Chain 1 108 . . . ID=PRO_0000299801;Note=Uncharacterized protein YPL080C +##sequence-region Q06833 1 770 +Q06833 UniProtKB Chain 1 770 . . . ID=PRO_0000257815;Note=Uncharacterized PH domain-containing protein YPR091C +Q06833 UniProtKB Topological domain 1 5 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06833 UniProtKB Transmembrane 6 26 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06833 UniProtKB Topological domain 27 770 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06833 UniProtKB Domain 114 266 . . . Note=PH +Q06833 UniProtKB Modified residue 640 640 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +Q06833 UniProtKB Modified residue 669 669 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +Q06833 UniProtKB Modified residue 717 717 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06833 UniProtKB Modified residue 720 720 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q06833 UniProtKB Modified residue 723 723 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06833 UniProtKB Glycosylation 228 228 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06833 UniProtKB Glycosylation 263 263 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06833 UniProtKB Glycosylation 279 279 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06833 UniProtKB Glycosylation 300 300 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06833 UniProtKB Glycosylation 391 391 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06833 UniProtKB Glycosylation 528 528 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06833 UniProtKB Glycosylation 529 529 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06833 UniProtKB Glycosylation 595 595 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06833 UniProtKB Glycosylation 620 620 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06833 UniProtKB Glycosylation 700 700 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06833 UniProtKB Glycosylation 718 718 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q02981 1 657 +Q02981 UniProtKB Transit peptide 1 15 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02981 UniProtKB Chain 16 657 . . . ID=PRO_0000200738;Note=ABC1 family protein YPL109C%2C mitochondrial +##sequence-region Q8TGK9 1 57 +Q8TGK9 UniProtKB Chain 1 57 . . . ID=PRO_0000299804;Note=Putative uncharacterized protein YPL135C-A +##sequence-region Q8TGQ7 1 33 +Q8TGQ7 UniProtKB Chain 1 33 . . . ID=PRO_0000244639;Note=Uncharacterized protein YPR159C-A +Q8TGQ7 UniProtKB Transmembrane 11 31 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06616 1 221 +Q06616 UniProtKB Chain 1 221 . . . ID=PRO_0000257831;Note=Nuclear envelope protein YPR174C +Q06616 UniProtKB Modified residue 158 158 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06616 UniProtKB Modified residue 170 170 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06616 UniProtKB Modified residue 175 175 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q12697 1 1472 +Q12697 UniProtKB Chain 1 1472 . . . ID=PRO_0000046351;Note=Vacuolar cation-transporting ATPase YPK9 +Q12697 UniProtKB Topological domain 1 293 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Transmembrane 294 315 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Topological domain 316 321 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Transmembrane 322 344 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Topological domain 345 488 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Transmembrane 489 511 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Topological domain 512 514 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Transmembrane 515 533 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Topological domain 534 693 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Transmembrane 694 713 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Topological domain 714 726 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Transmembrane 727 748 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Topological domain 749 1244 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Transmembrane 1245 1264 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Topological domain 1265 1271 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Transmembrane 1272 1289 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Topological domain 1290 1307 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Transmembrane 1308 1331 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Topological domain 1332 1351 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Transmembrane 1352 1374 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Topological domain 1375 1387 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Transmembrane 1388 1407 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Topological domain 1408 1423 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Transmembrane 1424 1446 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Topological domain 1447 1472 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12697 UniProtKB Active site 781 781 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12697 UniProtKB Metal binding 1187 1187 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12697 UniProtKB Metal binding 1191 1191 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12697 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12697 UniProtKB Modified residue 95 95 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q12697 UniProtKB Modified residue 108 108 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12697 UniProtKB Modified residue 1117 1117 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12697 UniProtKB Modified residue 1120 1120 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38279 1 296 +P38279 UniProtKB Chain 1 296 . . . ID=PRO_0000202496;Note=Probable vacuolar amino acid transporter YPQ3 +P38279 UniProtKB Topological domain 1 12 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38279 UniProtKB Transmembrane 13 33 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38279 UniProtKB Topological domain 34 44 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38279 UniProtKB Transmembrane 45 65 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38279 UniProtKB Topological domain 66 68 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38279 UniProtKB Transmembrane 69 89 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38279 UniProtKB Topological domain 90 163 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38279 UniProtKB Transmembrane 164 184 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38279 UniProtKB Topological domain 185 199 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38279 UniProtKB Transmembrane 200 220 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38279 UniProtKB Topological domain 221 238 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38279 UniProtKB Transmembrane 239 259 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38279 UniProtKB Topological domain 260 262 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38279 UniProtKB Transmembrane 263 283 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38279 UniProtKB Topological domain 284 296 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38279 UniProtKB Domain 10 76 . . . Note=PQ-loop 1 +P38279 UniProtKB Domain 208 270 . . . Note=PQ-loop 2 +##sequence-region Q6B0W2 1 109 +Q6B0W2 UniProtKB Chain 1 109 . . . ID=PRO_0000299815;Note=Uncharacterized protein YPR014C +##sequence-region O13569 1 170 +O13569 UniProtKB Chain 1 170 . . . ID=PRO_0000299828;Note=Putative uncharacterized protein YPR136C +O13569 UniProtKB Compositional bias 34 136 . . . Note=Ser-rich +##sequence-region O13570 1 187 +O13570 UniProtKB Chain 1 187 . . . ID=PRO_0000299829;Note=Putative uncharacterized protein YPR142C +O13570 UniProtKB Transmembrane 80 100 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13570 UniProtKB Transmembrane 105 125 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13570 UniProtKB Transmembrane 129 149 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13570 UniProtKB Compositional bias 42 55 . . . Note=Poly-Ser +O13570 UniProtKB Compositional bias 73 81 . . . Note=Poly-Ser +##sequence-region Q12346 1 211 +Q12346 UniProtKB Chain 1 211 . . . ID=PRO_0000252276;Note=Uncharacterized membrane protein YPR071W +Q12346 UniProtKB Topological domain 1 33 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12346 UniProtKB Transmembrane 34 54 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12346 UniProtKB Topological domain 55 58 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12346 UniProtKB Transmembrane 59 79 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12346 UniProtKB Topological domain 80 116 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12346 UniProtKB Transmembrane 117 137 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12346 UniProtKB Topological domain 138 162 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12346 UniProtKB Transmembrane 163 183 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12346 UniProtKB Topological domain 184 211 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12303 1 508 +Q12303 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12303 UniProtKB Propeptide 21 47 . . . ID=PRO_0000025841;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10191273;Dbxref=PMID:10191273 +Q12303 UniProtKB Chain 48 483 . . . ID=PRO_0000025842;Note=Aspartic proteinase yapsin-3 +Q12303 UniProtKB Propeptide 484 508 . . . ID=PRO_0000025843;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12303 UniProtKB Domain 63 394 . . . Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103 +Q12303 UniProtKB Active site 81 81 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q12303 UniProtKB Active site 288 288 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q12303 UniProtKB Lipidation 483 483 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12303 UniProtKB Glycosylation 75 75 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12303 UniProtKB Glycosylation 120 120 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12303 UniProtKB Glycosylation 160 160 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12303 UniProtKB Glycosylation 163 163 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12303 UniProtKB Glycosylation 275 275 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12303 UniProtKB Glycosylation 309 309 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12303 UniProtKB Glycosylation 328 328 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12303 UniProtKB Glycosylation 367 367 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12303 UniProtKB Glycosylation 422 422 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12303 UniProtKB Glycosylation 445 445 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12303 UniProtKB Glycosylation 462 462 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CD97 1 72 +P0CD97 UniProtKB Chain 1 72 . . . ID=PRO_0000391664;Note=Uncharacterized protein YER039C-A +P0CD97 UniProtKB Topological domain 1 12 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD97 UniProtKB Transmembrane 13 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD97 UniProtKB Topological domain 33 46 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD97 UniProtKB Transmembrane 47 69 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD97 UniProtKB Topological domain 70 72 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P41920 1 201 +P41920 UniProtKB Chain 1 201 . . . ID=PRO_0000213670;Note=Ran-specific GTPase-activating protein 1 +P41920 UniProtKB Domain 64 200 . . . Note=RanBD1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00164 +P41920 UniProtKB Modified residue 60 60 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P41920 UniProtKB Beta strand 83 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P41920 UniProtKB Turn 98 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P41920 UniProtKB Beta strand 102 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P41920 UniProtKB Turn 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P41920 UniProtKB Beta strand 122 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P41920 UniProtKB Turn 129 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P41920 UniProtKB Beta strand 134 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P41920 UniProtKB Beta strand 153 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P41920 UniProtKB Beta strand 165 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WVF +P41920 UniProtKB Beta strand 170 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +P41920 UniProtKB Helix 181 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HAT +##sequence-region Q12172 1 810 +Q12172 UniProtKB Chain 1 810 . . . ID=PRO_0000269651;Note=Zinc finger transcription factor YRR1 +Q12172 UniProtKB DNA binding 54 82 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +##sequence-region P25036 1 478 +P25036 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25036 UniProtKB Chain 18 478 . . . ID=PRO_0000027206;Note=Subtilisin-like protease 3 +P25036 UniProtKB Domain 210 446 . . . Note=Peptidase S8 +P25036 UniProtKB Active site 213 213 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25036 UniProtKB Active site 245 245 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25036 UniProtKB Active site 407 407 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25036 UniProtKB Sequence conflict 22 22 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25036 UniProtKB Sequence conflict 105 105 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25036 UniProtKB Sequence conflict 189 205 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25036 UniProtKB Sequence conflict 289 289 . . . Note=Y->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12024 1 460 +Q12024 UniProtKB Chain 1 460 . . . ID=PRO_0000051466;Note=Ribosome biogenesis protein YTM1 +Q12024 UniProtKB Repeat 101 140 . . . Note=WD 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03029 +Q12024 UniProtKB Repeat 142 180 . . . Note=WD 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03029 +Q12024 UniProtKB Repeat 206 244 . . . Note=WD 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03029 +Q12024 UniProtKB Repeat 285 325 . . . Note=WD 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03029 +Q12024 UniProtKB Repeat 327 366 . . . Note=WD 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03029 +Q12024 UniProtKB Repeat 373 413 . . . Note=WD 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03029 +Q12024 UniProtKB Repeat 424 460 . . . Note=WD 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03029 +Q12024 UniProtKB Region 99 460 . . . Note=Sufficient for interaction with ERB1 and association with 66S pre-ribosomes;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18448671,ECO:0000269|PubMed:26657628;Dbxref=PMID:18448671,PMID:26657628 +Q12024 UniProtKB Mutagenesis 104 104 . . . Note=Weakens the interaction with ERB1%2C leading to mostly ribosome-unbound YTM1 and defects in 60S maturation. Disrupts the interaction with YTM1 and cannot sustain growth%3B when associated with E-310. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26657628;Dbxref=PMID:26657628 +Q12024 UniProtKB Mutagenesis 123 123 . . . Note=Disrupts the interaction with YTM1 and cannot sustain growth%3B when associated with E-310. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26657628;Dbxref=PMID:26657628 +Q12024 UniProtKB Mutagenesis 310 310 . . . Note=Disrupts the interaction with YTM1 and cannot sustain growth%3B when associated with R-104 or A-123. H->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26657628;Dbxref=PMID:26657628 +Q12024 UniProtKB Mutagenesis 398 398 . . . Note=In ytm1-1%3B abrogates binding to ERB1 and impairs 27S pre-rRNA processing and 66S pre-ribosome maturation%3B when associated with N-442. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16287855;Dbxref=PMID:16287855 +Q12024 UniProtKB Mutagenesis 442 442 . . . Note=In ytm1-1%3B abrogates binding to ERB1 and impairs 27S pre-rRNA processing and 66S pre-ribosome maturation%3B when associated with D-398. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16287855;Dbxref=PMID:16287855 +##sequence-region Q08245 1 113 +Q08245 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000269|Ref.4;Dbxref=PMID:15665377 +Q08245 UniProtKB Chain 2 113 . . . ID=PRO_0000066571;Note=Protein ZEO1 +Q08245 UniProtKB Coiled coil 2 97 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08245 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000269|Ref.4;Dbxref=PMID:15665377 +Q08245 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q08245 UniProtKB Modified residue 25 25 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:17761666,PMID:18407956,PMID:19779198 +Q08245 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:17761666,PMID:18407956,PMID:19779198 +Q08245 UniProtKB Modified residue 49 49 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:17761666,PMID:18407956,PMID:19779198 +Q08245 UniProtKB Cross-link 18 18 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q08245 UniProtKB Cross-link 23 23 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q08245 UniProtKB Cross-link 29 29 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q08245 UniProtKB Cross-link 34 34 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q08245 UniProtKB Cross-link 45 45 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q08245 UniProtKB Cross-link 57 57 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q08245 UniProtKB Cross-link 82 82 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P53061 1 704 +P53061 UniProtKB Chain 1 704 . . . ID=PRO_0000202706;Note=Protein ZIP2 +##sequence-region P53831 1 123 +P53831 UniProtKB Chain 1 123 . . . ID=PRO_0000203376;Note=Putative uncharacterized protein YNL285W +##sequence-region P0C5Q8 1 48 +P0C5Q8 UniProtKB Chain 1 48 . . . ID=PRO_0000309056;Note=Putative uncharacterized protein YNL067W-A +##sequence-region P53717 1 134 +P53717 UniProtKB Chain 1 134 . . . ID=PRO_0000203469;Note=Putative uncharacterized protein YNR005C +P53717 UniProtKB Transmembrane 110 130 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53750 1 290 +P53750 UniProtKB Chain 1 290 . . . ID=PRO_0000207080;Note=Uncharacterized hydrolase YNR064C +P53750 UniProtKB Domain 30 274 . . . Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53750 UniProtKB Active site 269 269 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53752 1 436 +P53752 UniProtKB Chain 1 436 . . . ID=PRO_0000203484;Note=Uncharacterized membrane glycoprotein YNR066C +P53752 UniProtKB Transmembrane 1 21 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53752 UniProtKB Repeat 57 68 . . . Note=BNR 1 +P53752 UniProtKB Repeat 101 112 . . . Note=BNR 2 +P53752 UniProtKB Repeat 229 240 . . . Note=BNR 3 +P53752 UniProtKB Repeat 394 405 . . . Note=BNR 4 +P53752 UniProtKB Glycosylation 157 157 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53981 1 241 +P53981 UniProtKB Chain 1 241 . . . ID=PRO_0000203466;Note=Uncharacterized phosphatase YNL010W +##sequence-region P53975 1 284 +P53975 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53975 UniProtKB Chain 25 284 . . . ID=PRO_0000014341;Note=Uncharacterized membrane protein YNL019C +P53975 UniProtKB Topological domain 25 84 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53975 UniProtKB Transmembrane 85 104 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53975 UniProtKB Topological domain 105 284 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53975 UniProtKB Glycosylation 270 270 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53928 1 181 +P53928 UniProtKB Chain 1 181 . . . ID=PRO_0000203435;Note=Putative uncharacterized membrane protein YNL109W +P53928 UniProtKB Topological domain 1 14 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53928 UniProtKB Transmembrane 15 35 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53928 UniProtKB Topological domain 36 58 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53928 UniProtKB Transmembrane 59 79 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53928 UniProtKB Topological domain 80 84 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53928 UniProtKB Transmembrane 85 105 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53928 UniProtKB Topological domain 106 116 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53928 UniProtKB Transmembrane 117 137 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53928 UniProtKB Topological domain 138 153 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53928 UniProtKB Transmembrane 154 174 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53928 UniProtKB Topological domain 175 181 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53910 1 189 +P53910 UniProtKB Chain 1 189 . . . ID=PRO_0000203425;Note=Uncharacterized protein YNL140C +P53910 UniProtKB Sequence conflict 18 18 . . . Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53891 1 406 +P53891 UniProtKB Chain 1 406 . . . ID=PRO_0000203412;Note=Uncharacterized protein YNL165W +##sequence-region P53884 1 190 +P53884 UniProtKB Chain 1 190 . . . ID=PRO_0000203408;Note=Putative uncharacterized protein YNL174W +P53884 UniProtKB Transmembrane 15 35 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53884 UniProtKB Transmembrane 58 78 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53884 UniProtKB Transmembrane 94 114 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53884 UniProtKB Transmembrane 148 168 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53884 UniProtKB Compositional bias 61 65 . . . Note=Poly-Phe +##sequence-region P53876 1 108 +P53876 UniProtKB Chain 1 108 . . . ID=PRO_0000203404;Note=Uncharacterized protein YNL184C +##sequence-region P53870 1 558 +P53870 UniProtKB Chain 1 558 . . . ID=PRO_0000203400;Note=Uncharacterized protein YNL193W +P53870 UniProtKB Sequence conflict 122 122 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40166 1 100 +P40166 UniProtKB Transit peptide 1 45 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40166 UniProtKB Chain 46 100 . . . ID=PRO_0000203396;Note=Uncharacterized protein YNL198C%2C mitochondrial +##sequence-region P40152 1 326 +P40152 UniProtKB Signal peptide 1 26 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40152 UniProtKB Chain 27 326 . . . ID=PRO_0000042987;Note=Putative metallophosphoesterase YNL217W +##sequence-region P53864 1 136 +P53864 UniProtKB Chain 1 136 . . . ID=PRO_0000203387;Note=Putative uncharacterized protein YNL226W +##sequence-region Q12351 1 137 +Q12351 UniProtKB Chain 1 137 . . . ID=PRO_0000235937;Note=Uncharacterized protein YOR012W +##sequence-region Q08172 1 172 +Q08172 UniProtKB Chain 1 172 . . . ID=PRO_0000245274;Note=Putative uncharacterized protein YOL024W +##sequence-region Q3E824 1 90 +Q3E824 UniProtKB Chain 1 90 . . . ID=PRO_0000235939;Note=Uncharacterized protein YOR020W-A +Q3E824 UniProtKB Transmembrane 15 34 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E824 UniProtKB Glycosylation 44 44 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08222 1 106 +Q08222 UniProtKB Chain 1 106 . . . ID=PRO_0000299691;Note=Putative uncharacterized protein YOL050C +##sequence-region Q08232 1 322 +Q08232 UniProtKB Chain 1 322 . . . ID=PRO_0000235926;Note=Uncharacterized membrane protein YOL073C +Q08232 UniProtKB Topological domain 1 19 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08232 UniProtKB Transmembrane 20 40 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08232 UniProtKB Topological domain 41 54 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08232 UniProtKB Transmembrane 55 75 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08232 UniProtKB Topological domain 76 90 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08232 UniProtKB Transmembrane 91 111 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08232 UniProtKB Topological domain 112 120 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08232 UniProtKB Transmembrane 121 141 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08232 UniProtKB Topological domain 142 189 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08232 UniProtKB Transmembrane 190 210 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08232 UniProtKB Topological domain 211 322 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08232 UniProtKB Compositional bias 244 269 . . . Note=Ala-rich +##sequence-region Q6B0V7 1 65 +Q6B0V7 UniProtKB Chain 1 65 . . . ID=PRO_0000299755;Note=Putative uncharacterized protein YPR002C-A +Q6B0V7 UniProtKB Sequence conflict 35 35 . . . Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06104 1 294 +Q06104 UniProtKB Chain 1 294 . . . ID=PRO_0000242625;Note=Uncharacterized membrane protein YPR109W +Q06104 UniProtKB Topological domain 1 139 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06104 UniProtKB Transmembrane 140 160 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06104 UniProtKB Topological domain 161 215 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06104 UniProtKB Transmembrane 216 236 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06104 UniProtKB Topological domain 237 294 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06104 UniProtKB Sequence conflict 11 11 . . . Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12458 1 312 +Q12458 UniProtKB Chain 1 312 . . . ID=PRO_0000124612;Note=Putative reductase 1 +Q12458 UniProtKB Nucleotide binding 220 274 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12458 UniProtKB Active site 56 56 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12458 UniProtKB Binding site 112 112 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12458 UniProtKB Site 81 81 . . . Note=Lowers pKa of active site Tyr;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P32329 1 569 +P32329 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32329 UniProtKB Propeptide 22 67 . . . ID=PRO_0000025838;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9417119;Dbxref=PMID:9417119 +P32329 UniProtKB Chain 68 548 . . . ID=PRO_0000025839;Note=Aspartic proteinase 3 +P32329 UniProtKB Chain 68 128 . . . ID=PRO_0000372455;Note=Aspartic proteinase 3 subunit alpha +P32329 UniProtKB Chain 145 548 . . . ID=PRO_0000372456;Note=Aspartic proteinase 3 subunit beta +P32329 UniProtKB Propeptide 549 569 . . . ID=PRO_0000025840;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32329 UniProtKB Domain 83 475 . . . Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103 +P32329 UniProtKB Active site 101 101 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +P32329 UniProtKB Active site 371 371 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +P32329 UniProtKB Site 128 129 . . . Note=Cleavage%3B by autolysis;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32329 UniProtKB Site 144 145 . . . Note=Cleavage%3B by autolysis +P32329 UniProtKB Lipidation 548 548 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32329 UniProtKB Glycosylation 95 95 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32329 UniProtKB Glycosylation 203 203 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32329 UniProtKB Glycosylation 232 232 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32329 UniProtKB Glycosylation 242 242 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32329 UniProtKB Glycosylation 245 245 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32329 UniProtKB Glycosylation 299 299 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32329 UniProtKB Glycosylation 358 358 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32329 UniProtKB Glycosylation 480 480 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32329 UniProtKB Glycosylation 522 522 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32329 UniProtKB Glycosylation 532 532 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32329 UniProtKB Mutagenesis 101 101 . . . Note=Loss of function. D->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9417119;Dbxref=PMID:9417119 +P32329 UniProtKB Sequence conflict 370 370 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P01123 1 206 +P01123 UniProtKB Chain 1 206 . . . ID=PRO_0000121318;Note=GTP-binding protein YPT1 +P01123 UniProtKB Nucleotide binding 15 23 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62820 +P01123 UniProtKB Nucleotide binding 33 40 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62820 +P01123 UniProtKB Nucleotide binding 63 67 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62820 +P01123 UniProtKB Nucleotide binding 121 124 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62820 +P01123 UniProtKB Nucleotide binding 151 153 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62820 +P01123 UniProtKB Region 63 80 . . . Note=Interaction with GDI1 +P01123 UniProtKB Region 189 195 . . . Note=Interaction with GDI1 +P01123 UniProtKB Motif 37 45 . . . Note=Effector region;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P01123 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.5 +P01123 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P01123 UniProtKB Modified residue 174 174 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P01123 UniProtKB Lipidation 23 23 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P01123 UniProtKB Lipidation 123 123 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P01123 UniProtKB Lipidation 205 205 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10071213;Dbxref=PMID:10071213 +P01123 UniProtKB Lipidation 206 206 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10071213;Dbxref=PMID:10071213 +P01123 UniProtKB Cross-link 144 144 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P01123 UniProtKB Mutagenesis 17 17 . . . Note=Decreases GTP binding and increases GTP hydrolysis. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3311726;Dbxref=PMID:3311726 +P01123 UniProtKB Mutagenesis 21 21 . . . Note=Abolishes GTP binding. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3311726;Dbxref=PMID:3311726 +P01123 UniProtKB Mutagenesis 37 37 . . . Note=No change. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2009858;Dbxref=PMID:2009858 +P01123 UniProtKB Mutagenesis 39 39 . . . Note=No change. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2009858;Dbxref=PMID:2009858 +P01123 UniProtKB Mutagenesis 40 40 . . . Note=No change. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2009858;Dbxref=PMID:2009858 +P01123 UniProtKB Mutagenesis 41 41 . . . Note=Lethal. I->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2009858;Dbxref=PMID:2009858 +P01123 UniProtKB Mutagenesis 43 43 . . . Note=No change. V->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2009858;Dbxref=PMID:2009858 +P01123 UniProtKB Mutagenesis 44 44 . . . Note=Temperature-sensitive phenotype. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2009858;Dbxref=PMID:2009858 +P01123 UniProtKB Mutagenesis 65 65 . . . Note=Decreases GTP binding and GTP hydrolysis. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3311726;Dbxref=PMID:3311726 +P01123 UniProtKB Mutagenesis 67 67 . . . Note=Locks YPT1 in the GTP-bound form by reducing GTP hydrolysis rate 40-fold. Q->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15082776,ECO:0000269|PubMed:9447979;Dbxref=PMID:15082776,PMID:9447979 +P01123 UniProtKB Mutagenesis 121 121 . . . Note=Abolishes GTP binding. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3311726;Dbxref=PMID:3311726 +P01123 UniProtKB Mutagenesis 136 136 . . . Note=Loss of function at 37 degrees Celsius. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7593181;Dbxref=PMID:7593181 +P01123 UniProtKB Mutagenesis 205 205 . . . Note=Abolishes membrane association. Lethal%3B when associated with S-206. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10071213,ECO:0000269|PubMed:3042385;Dbxref=PMID:10071213,PMID:3042385 +P01123 UniProtKB Mutagenesis 206 206 . . . Note=Abolishes membrane association. Lethal%3B when associated with S-205. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10071213,ECO:0000269|PubMed:3042385;Dbxref=PMID:10071213,PMID:3042385 +P01123 UniProtKB Sequence conflict 171 171 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P01123 UniProtKB Beta strand 6 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P01123 UniProtKB Helix 21 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P01123 UniProtKB Beta strand 45 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P01123 UniProtKB Beta strand 55 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P01123 UniProtKB Turn 65 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P01123 UniProtKB Helix 75 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P01123 UniProtKB Beta strand 82 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P01123 UniProtKB Helix 93 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P01123 UniProtKB Beta strand 115 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P01123 UniProtKB Turn 126 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P01123 UniProtKB Helix 133 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P01123 UniProtKB Beta strand 147 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P01123 UniProtKB Turn 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P01123 UniProtKB Helix 158 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P01123 UniProtKB Helix 175 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P01123 UniProtKB Helix 183 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +##sequence-region P40105 1 1681 +P40105 UniProtKB Chain 1 1681 . . . ID=PRO_0000102202;Note=Y' element ATP-dependent helicase protein 1 copy 2 +P40105 UniProtKB Domain 683 860 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P40105 UniProtKB Domain 917 1066 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P40105 UniProtKB Nucleotide binding 696 703 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +##sequence-region P0CX15 1 1859 +P0CX15 UniProtKB Chain 1 1859 . . . ID=PRO_0000409751;Note=Y' element ATP-dependent helicase protein 1 copy 7 +P0CX15 UniProtKB Domain 861 1038 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P0CX15 UniProtKB Domain 1095 1244 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P0CX15 UniProtKB Nucleotide binding 874 881 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +##sequence-region Q12340 1 786 +Q12340 UniProtKB Chain 1 786 . . . ID=PRO_0000269650;Note=Zinc finger transcription factor YRM1 +Q12340 UniProtKB DNA binding 31 59 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +Q12340 UniProtKB Sequence conflict 158 158 . . . Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12340 UniProtKB Sequence conflict 604 604 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47043 1 880 +P47043 UniProtKB Chain 1 880 . . . ID=PRO_0000046859;Note=Zinc-responsive transcriptional regulator ZAP1 +P47043 UniProtKB Zinc finger 579 604 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P47043 UniProtKB Zinc finger 616 641 . . . Note=C2H2-type 2%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P47043 UniProtKB Zinc finger 705 730 . . . Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P47043 UniProtKB Zinc finger 738 762 . . . Note=C2H2-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P47043 UniProtKB Zinc finger 768 790 . . . Note=C2H2-type 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P47043 UniProtKB Zinc finger 796 818 . . . Note=C2H2-type 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P47043 UniProtKB Zinc finger 824 846 . . . Note=C2H2-type 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P47043 UniProtKB Modified residue 156 156 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47043 UniProtKB Modified residue 166 166 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47043 UniProtKB Modified residue 515 515 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47043 UniProtKB Helix 593 603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW8 +P47043 UniProtKB Beta strand 626 629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW8 +P47043 UniProtKB Helix 630 640 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZW8 +##sequence-region P54786 1 942 +P54786 UniProtKB Chain 1 942 . . . ID=PRO_0000066570;Note=Protein ZDS2 +P54786 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P54786 UniProtKB Sequence conflict 7 7 . . . Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54786 UniProtKB Sequence conflict 23 23 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54786 UniProtKB Sequence conflict 530 530 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54786 UniProtKB Sequence conflict 546 546 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54786 UniProtKB Sequence conflict 633 633 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54786 UniProtKB Sequence conflict 668 668 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54786 UniProtKB Sequence conflict 711 711 . . . Note=V->VNC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54786 UniProtKB Sequence conflict 723 723 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54786 UniProtKB Sequence conflict 729 729 . . . Note=A->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54786 UniProtKB Sequence conflict 833 833 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54786 UniProtKB Sequence conflict 914 942 . . . Note=TGDIAFNGDSALGMMDKNDSDGTILIPDI->HWRYSLQW;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25650 1 117 +P25650 UniProtKB Chain 1 117 . . . ID=PRO_0000202576;Note=Uncharacterized protein YCR085W +##sequence-region P25657 1 155 +P25657 UniProtKB Chain 1 155 . . . ID=PRO_0000202582;Note=Uncharacterized protein YCR099C +##sequence-region P25606 1 316 +P25606 UniProtKB Chain 1 316 . . . ID=PRO_0000202583;Note=Uncharacterized protein YCR100C +P25606 UniProtKB Repeat 62 73 . . . Note=BNR 1 +P25606 UniProtKB Repeat 124 135 . . . Note=BNR 2 +P25606 UniProtKB Repeat 196 207 . . . Note=BNR 3 +P25606 UniProtKB Repeat 242 253 . . . Note=BNR 4 +##sequence-region Q12210 1 107 +Q12210 UniProtKB Chain 1 107 . . . ID=PRO_0000299842;Note=Uncharacterized protein YDL009C +Q12210 UniProtKB Transmembrane 52 72 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12111 1 104 +Q12111 UniProtKB Chain 1 104 . . . ID=PRO_0000299870;Note=Uncharacterized protein YDR029W +Q12111 UniProtKB Transmembrane 45 65 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12111 UniProtKB Transmembrane 70 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12025 1 205 +Q12025 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12025 UniProtKB Chain 18 205 . . . ID=PRO_0000244437;Note=Uncharacterized protein YDR056C +Q12025 UniProtKB Glycosylation 47 47 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07435 1 109 +Q07435 UniProtKB Chain 1 109 . . . ID=PRO_0000299853;Note=Putative uncharacterized protein YDL068W +Q07435 UniProtKB Transmembrane 32 52 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07435 UniProtKB Transmembrane 66 86 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38966 1 869 +P38966 UniProtKB Chain 1 869 . . . ID=PRO_0000202595;Note=Uncharacterized protein YDR089W +P38966 UniProtKB Domain 1 154 . . . Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714 +P38966 UniProtKB Modified residue 238 238 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38966 UniProtKB Modified residue 241 241 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38966 UniProtKB Modified residue 316 316 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38966 UniProtKB Modified residue 324 324 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38966 UniProtKB Modified residue 327 327 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38966 UniProtKB Modified residue 609 609 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38966 UniProtKB Modified residue 612 612 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38966 UniProtKB Modified residue 668 668 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38966 UniProtKB Modified residue 760 760 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q07530 1 308 +Q07530 UniProtKB Chain 1 308 . . . ID=PRO_0000240705;Note=Uncharacterized oxidoreductase YDL114W +Q07530 UniProtKB Nucleotide binding 42 66 . . . Note=NAD or NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07530 UniProtKB Active site 182 182 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001 +Q07530 UniProtKB Binding site 169 169 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q04608 1 324 +Q04608 UniProtKB Chain 1 324 . . . ID=PRO_0000253830;Note=Uncharacterized protein YDR124W +##sequence-region Q03899 1 556 +Q03899 UniProtKB Chain 1 556 . . . ID=PRO_0000253804;Note=F-box protein YDR131C +Q03899 UniProtKB Domain 1 44 . . . Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080 +##sequence-region A0A023PZA4 1 116 +A0A023PZA4 UniProtKB Chain 1 116 . . . ID=PRO_0000430982;Note=Putative uncharacterized protein YDR154C +##sequence-region Q07613 1 109 +Q07613 UniProtKB Chain 1 109 . . . ID=PRO_0000299863;Note=Putative uncharacterized protein YDL187C +##sequence-region Q12121 1 372 +Q12121 UniProtKB Chain 1 372 . . . ID=PRO_0000242481;Note=Uncharacterized protein YDL211C +Q12121 UniProtKB Transmembrane 224 244 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12121 UniProtKB Compositional bias 104 193 . . . Note=Thr-rich +Q12121 UniProtKB Modified residue 329 329 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q07658 1 213 +Q07658 UniProtKB Chain 1 213 . . . ID=PRO_0000299866;Note=Putative uncharacterized protein YDL228C +##sequence-region Q3E763 1 66 +Q3E763 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E763 UniProtKB Chain 20 66 . . . ID=PRO_0000253840;Note=Uncharacterized protein YDR246W-A +##sequence-region P87283 1 123 +P87283 UniProtKB Chain 1 123 . . . ID=PRO_0000299749;Note=Uncharacterized protein YDR274C +##sequence-region Q05530 1 114 +Q05530 UniProtKB Chain 1 114 . . . ID=PRO_0000253812;Note=Glutaredoxin-like protein YDR286C +Q05530 UniProtKB Disulfide bond 31 34 . . . Note=Redox-active;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P87288 1 108 +P87288 UniProtKB Chain 1 108 . . . ID=PRO_0000299883;Note=Putative uncharacterized protein YDR327W +##sequence-region P0C289 1 58 +P0C289 UniProtKB Chain 1 58 . . . ID=PRO_0000269763;Note=Putative uncharacterized protein YDR034C-A +P0C289 UniProtKB Transmembrane 5 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region O13523 1 187 +O13523 UniProtKB Chain 1 187 . . . ID=PRO_0000299889;Note=Putative uncharacterized protein YDR401W +O13523 UniProtKB Transmembrane 66 86 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13523 UniProtKB Transmembrane 120 140 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P87267 1 123 +P87267 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P87267 UniProtKB Chain 25 123 . . . ID=PRO_0000299750;Note=Putative uncharacterized protein YDR417C +P87267 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P87267 UniProtKB Transmembrane 101 121 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04093 1 687 +Q04093 UniProtKB Chain 1 687 . . . ID=PRO_0000253824;Note=Putative lipase YDR444W +Q04093 UniProtKB Active site 284 284 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10037 +##sequence-region P87264 1 108 +P87264 UniProtKB Chain 1 108 . . . ID=PRO_0000299898;Note=Putative uncharacterized protein YDR467C +P87264 UniProtKB Transmembrane 32 52 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P87264 UniProtKB Transmembrane 68 88 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGR7 1 38 +Q8TGR7 UniProtKB Chain 1 38 . . . ID=PRO_0000299901;Note=Putative uncharacterized protein YDR510C-A +Q8TGR7 UniProtKB Transmembrane 10 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P87263 1 166 +P87263 UniProtKB Chain 1 166 . . . ID=PRO_0000299912;Note=Putative uncharacterized protein YER066C-A +##sequence-region A0A023PYE9 1 183 +A0A023PYE9 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PYE9 UniProtKB Chain 18 183 . . . ID=PRO_0000430997;Note=Putative uncharacterized protein YER087C-A +##sequence-region A0A023PXJ7 1 106 +A0A023PXJ7 UniProtKB Chain 1 106 . . . ID=PRO_0000430998;Note=Putative uncharacterized membrane protein YER107W-A +A0A023PXJ7 UniProtKB Transmembrane 17 37 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXJ7 UniProtKB Transmembrane 55 75 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PXD5 1 136 +A0A023PXD5 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXD5 UniProtKB Chain 20 136 . . . ID=PRO_0000431002;Note=Putative uncharacterized membrane protein YER147C-A +A0A023PXD5 UniProtKB Transmembrane 75 97 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PZC7 1 188 +A0A023PZC7 UniProtKB Chain 1 188 . . . ID=PRO_0000431004;Note=Putative uncharacterized protein YER152W-A +##sequence-region A0A023PZH1 1 118 +A0A023PZH1 UniProtKB Chain 1 118 . . . ID=PRO_0000431005;Note=Putative uncharacterized membrane protein YER165C-A +A0A023PZH1 UniProtKB Transmembrane 7 27 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZH1 UniProtKB Transmembrane 34 58 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40101 1 306 +P40101 UniProtKB Chain 1 306 . . . ID=PRO_0000202662;Note=Uncharacterized protein YER186C +##sequence-region P0C0V2 1 99 +P0C0V2 UniProtKB Chain 1 99 . . . ID=PRO_0000211371;Note=UPF0320 protein YER188C-A +##sequence-region P0C270 1 34 +P0C270 UniProtKB Chain 1 34 . . . ID=PRO_0000268625;Note=Putative uncharacterized protein YER138W-A +##sequence-region A0A023PXC2 1 115 +A0A023PXC2 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXC2 UniProtKB Chain 25 115 . . . ID=PRO_0000431007;Note=Putative uncharacterized membrane protein YEL053W-A +A0A023PXC2 UniProtKB Transmembrane 39 59 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXC2 UniProtKB Transmembrane 93 113 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PXJ3 1 115 +A0A023PXJ3 UniProtKB Chain 1 115 . . . ID=PRO_0000431008;Note=Putative uncharacterized membrane protein YER076W-A +A0A023PXJ3 UniProtKB Transmembrane 36 56 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39994 1 560 +P39994 UniProtKB Chain 1 560 . . . ID=PRO_0000090826;Note=Putative 2-hydroxyacyl-CoA lyase +##sequence-region P39983 1 233 +P39983 UniProtKB Chain 1 233 . . . ID=PRO_0000202604;Note=Uncharacterized protein YEL057C +##sequence-region P39973 1 112 +P39973 UniProtKB Chain 1 112 . . . ID=PRO_0000211370;Note=Putative UPF0320 protein YEL074W +##sequence-region P40022 1 185 +P40022 UniProtKB Chain 1 185 . . . ID=PRO_0000202625;Note=Uncharacterized protein YER034W +P40022 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P35723 1 206 +P35723 UniProtKB Chain 1 206 . . . ID=PRO_0000203174;Note=Endoplasmic reticulum transmembrane protein 1 +P35723 UniProtKB Topological domain 1 7 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35723 UniProtKB Transmembrane 8 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35723 UniProtKB Topological domain 29 45 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35723 UniProtKB Transmembrane 46 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35723 UniProtKB Topological domain 67 104 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35723 UniProtKB Transmembrane 105 125 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35723 UniProtKB Topological domain 126 206 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35723 UniProtKB Motif 203 206 . . . Note=Di-lysine motif +P35723 UniProtKB Cross-link 190 190 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14557538;Dbxref=PMID:14557538 +P35723 UniProtKB Sequence conflict 16 16 . . . Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35723 UniProtKB Sequence conflict 16 16 . . . Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35723 UniProtKB Sequence conflict 16 16 . . . Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39959 1 443 +P39959 UniProtKB Chain 1 443 . . . ID=PRO_0000046862;Note=Zinc finger protein YER130C +P39959 UniProtKB Zinc finger 389 412 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P39959 UniProtKB Zinc finger 418 440 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +##sequence-region P10356 1 443 +P10356 UniProtKB Chain 1 443 . . . ID=PRO_0000202655;Note=Uncharacterized protein YER152C +##sequence-region Q03187 1 267 +Q03187 UniProtKB Signal peptide 1 27 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03187 UniProtKB Chain 28 267 . . . ID=PRO_0000299917;Note=Putative uncharacterized protein YFL013W-A +Q03187 UniProtKB Transmembrane 125 145 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03187 UniProtKB Transmembrane 165 185 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03187 UniProtKB Compositional bias 190 267 . . . Note=Ser-rich +##sequence-region Q8TGR2 1 95 +Q8TGR2 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q8TGR2 UniProtKB Chain 18 95 . . . ID=PRO_0000299919;Note=Putative uncharacterized protein YFR034W-A +##sequence-region P0CX63 1 1770 +P0CX63 UniProtKB Chain 1 1770 . . . ID=PRO_0000279308;Note=Transposon Ty2-F Gag-Pol polyprotein +P0CX63 UniProtKB Chain 1 397 . . . ID=PRO_0000279309;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX63 UniProtKB Chain 398 578 . . . ID=PRO_0000279310;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX63 UniProtKB Chain 579 1232 . . . ID=PRO_0000279311;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX63 UniProtKB Chain 1233 1770 . . . ID=PRO_0000279312;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX63 UniProtKB Domain 656 831 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0CX63 UniProtKB Domain 1353 1491 . . . Note=Reverse transcriptase Ty1/copia-type +P0CX63 UniProtKB Domain 1625 1767 . . . Note=RNase H Ty1/copia-type +P0CX63 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX63 UniProtKB Region 579 636 . . . Note=Integrase-type zinc finger-like +P0CX63 UniProtKB Motif 1193 1227 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX63 UniProtKB Active site 457 457 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX63 UniProtKB Metal binding 667 667 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0CX63 UniProtKB Metal binding 732 732 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0CX63 UniProtKB Metal binding 1361 1361 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0CX63 UniProtKB Metal binding 1442 1442 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0CX63 UniProtKB Metal binding 1443 1443 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0CX63 UniProtKB Metal binding 1625 1625 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0CX63 UniProtKB Metal binding 1667 1667 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0CX63 UniProtKB Metal binding 1700 1700 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +P0CX63 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX63 UniProtKB Site 578 579 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX63 UniProtKB Site 1232 1233 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P43578 1 164 +P43578 UniProtKB Chain 1 164 . . . ID=PRO_0000202678;Note=Uncharacterized protein YFL015C +P43578 UniProtKB Transmembrane 11 31 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43578 UniProtKB Transmembrane 51 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43566 1 106 +P43566 UniProtKB Chain 1 106 . . . ID=PRO_0000202675;Note=Putative uncharacterized protein YFL032W +P43566 UniProtKB Transmembrane 25 45 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43566 UniProtKB Transmembrane 62 82 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43599 1 363 +P43599 UniProtKB Chain 1 363 . . . ID=PRO_0000202688;Note=Uncharacterized protein YFR018C +##sequence-region Q3E802 1 36 +Q3E802 UniProtKB Chain 1 36 . . . ID=PRO_0000245381;Note=Uncharacterized protein YGL006W-A +##sequence-region P0C5N2 1 42 +P0C5N2 UniProtKB Chain 1 42 . . . ID=PRO_0000309030;Note=Putative uncharacterized protein YGR122C-A +##sequence-region Q8TGT9 1 53 +Q8TGT9 UniProtKB Chain 1 53 . . . ID=PRO_0000245384;Note=Uncharacterized protein YGR146C-A +Q8TGT9 UniProtKB Transmembrane 13 35 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53208 1 328 +P53208 UniProtKB Chain 1 328 . . . ID=PRO_0000202782;Note=Uncharacterized abhydrolase domain-containing protein YGR015C +P53208 UniProtKB Domain 39 309 . . . Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53208 UniProtKB Active site 115 115 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53208 UniProtKB Active site 302 302 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53210 1 297 +P53210 UniProtKB Chain 1 297 . . . ID=PRO_0000202784;Note=Uncharacterized protein YGR017W +##sequence-region P53222 1 116 +P53222 UniProtKB Chain 1 116 . . . ID=PRO_0000202792;Note=Uncharacterized protein YGR035C +##sequence-region P53247 1 123 +P53247 UniProtKB Chain 1 123 . . . ID=PRO_0000202807;Note=Putative uncharacterized protein YGR073C +P53247 UniProtKB Transmembrane 1 21 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53247 UniProtKB Transmembrane 103 123 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12173 1 290 +Q12173 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15956549;Dbxref=PMID:15956549 +Q12173 UniProtKB Chain 2 290 . . . ID=PRO_5000143279;Note=Transposon Ty3-G Gag polyprotein +Q12173 UniProtKB Chain 2 207 . . . ID=PRO_0000279365;Note=Capsid protein +Q12173 UniProtKB Peptide 208 233 . . . ID=PRO_0000279366;Note=Spacer peptide p3 +Q12173 UniProtKB Chain 234 290 . . . ID=PRO_5000143280;Note=Nucleocapsid protein p9 +Q12173 UniProtKB Zinc finger 265 282 . . . Note=CCHC-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +Q12173 UniProtKB Site 207 208 . . . Note=Cleavage%3B by Ty3 protease +Q12173 UniProtKB Site 233 234 . . . Note=Cleavage%3B by Ty3 protease +Q12173 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15956549;Dbxref=PMID:15956549 +Q12173 UniProtKB Mutagenesis 267 267 . . . Note=Reduces level of VLP formation and maturation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7515969;Dbxref=PMID:7515969 +Q12173 UniProtKB Mutagenesis 275 275 . . . Note=Reduces level of VLP formation and maturation. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7515969;Dbxref=PMID:7515969 +##sequence-region P53269 1 259 +P53269 UniProtKB Chain 1 259 . . . ID=PRO_0000202816;Note=Putative uncharacterized protein YGR115C +P53269 UniProtKB Transmembrane 14 34 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53269 UniProtKB Transmembrane 161 181 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53269 UniProtKB Transmembrane 221 241 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53269 UniProtKB Compositional bias 38 42 . . . Note=Poly-Ser +P53269 UniProtKB Compositional bias 45 48 . . . Note=Poly-Ser +P53269 UniProtKB Compositional bias 68 73 . . . Note=Poly-Ser +P53269 UniProtKB Compositional bias 87 93 . . . Note=Poly-Ser +P53269 UniProtKB Compositional bias 152 163 . . . Note=Poly-Ser +P53269 UniProtKB Compositional bias 179 185 . . . Note=Poly-Ser +P53269 UniProtKB Compositional bias 197 208 . . . Note=Poly-Ser +P53269 UniProtKB Compositional bias 214 220 . . . Note=Poly-Ser +P53269 UniProtKB Compositional bias 233 236 . . . Note=Poly-Ser +##sequence-region P53284 1 112 +P53284 UniProtKB Chain 1 112 . . . ID=PRO_0000202827;Note=Putative uncharacterized protein YGR139W +##sequence-region P53293 1 376 +P53293 UniProtKB Chain 1 376 . . . ID=PRO_0000202838;Note=Uncharacterized protein YGR168C +P53293 UniProtKB Transmembrane 153 173 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53293 UniProtKB Transmembrane 188 208 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53300 1 117 +P53300 UniProtKB Chain 1 117 . . . ID=PRO_0000202840;Note=Putative uncharacterized protein YGR182C +##sequence-region P50089 1 785 +P50089 UniProtKB Chain 1 785 . . . ID=PRO_0000202854;Note=Uncharacterized protein YGR237C +P50089 UniProtKB Modified residue 215 215 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P50089 UniProtKB Modified residue 667 667 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P53325 1 136 +P53325 UniProtKB Chain 1 136 . . . ID=PRO_0000202863;Note=Putative uncharacterized protein YGR265W +P53325 UniProtKB Transmembrane 102 118 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53325 UniProtKB Compositional bias 106 111 . . . Note=Poly-Phe +##sequence-region P53342 1 153 +P53342 UniProtKB Chain 1 153 . . . ID=PRO_0000202874;Note=Putative uncharacterized protein YGR293C +P53342 UniProtKB Transmembrane 1 21 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53342 UniProtKB Transmembrane 106 126 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P33199 1 130 +P33199 UniProtKB Chain 1 130 . . . ID=PRO_0000202775;Note=Uncharacterized protein YGL015C +##sequence-region P53183 1 348 +P53183 UniProtKB Chain 1 348 . . . ID=PRO_0000215577;Note=Putative uncharacterized oxidoreductase YGL039W +P53183 UniProtKB Modified residue 339 339 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12068 +##sequence-region P53155 1 381 +P53155 UniProtKB Chain 1 381 . . . ID=PRO_0000202757;Note=Uncharacterized protein YGL082W +P53155 UniProtKB Sequence conflict 263 263 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53133 1 265 +P53133 UniProtKB Chain 1 265 . . . ID=PRO_0000202747;Note=Uncharacterized protein YGL117W +P53133 UniProtKB Modified residue 223 223 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P38616 1 354 +P38616 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38616 UniProtKB Propeptide 20 37 . . . ID=PRO_0000022705;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8139573;Dbxref=PMID:8139573 +P38616 UniProtKB Chain 38 354 . . . ID=PRO_0000022706;Note=Protein YGP1 +P38616 UniProtKB Domain 50 354 . . . Note=Asparaginase/glutaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01068 +P38616 UniProtKB Glycosylation 40 40 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38616 UniProtKB Glycosylation 50 50 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38616 UniProtKB Glycosylation 53 53 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38616 UniProtKB Glycosylation 58 58 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38616 UniProtKB Glycosylation 61 61 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38616 UniProtKB Glycosylation 65 65 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38616 UniProtKB Glycosylation 87 87 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38616 UniProtKB Glycosylation 94 94 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38616 UniProtKB Glycosylation 100 100 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38616 UniProtKB Glycosylation 106 106 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38616 UniProtKB Glycosylation 118 118 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38616 UniProtKB Glycosylation 172 172 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38616 UniProtKB Glycosylation 239 239 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38616 UniProtKB Glycosylation 286 286 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38616 UniProtKB Sequence conflict 47 47 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38616 UniProtKB Sequence conflict 79 79 . . . Note=T->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53103 1 107 +P53103 UniProtKB Chain 1 107 . . . ID=PRO_0000202725;Note=Putative uncharacterized protein YGL182C +##sequence-region P53092 1 156 +P53092 UniProtKB Chain 1 156 . . . ID=PRO_0000202720;Note=Putative uncharacterized protein YGL199C +##sequence-region P53054 1 175 +P53054 UniProtKB Chain 1 175 . . . ID=PRO_0000202702;Note=Putative uncharacterized protein YGL262W +##sequence-region A0A023PYH5 1 124 +A0A023PYH5 UniProtKB Chain 1 124 . . . ID=PRO_0000431029;Note=Putative uncharacterized protein YHR193C-A +##sequence-region P0CX89 1 111 +P0CX89 UniProtKB Chain 1 111 . . . ID=PRO_0000410449;Note=Putative uncharacterized protein YHR212C +##sequence-region P0CL34 1 160 +P0CL34 UniProtKB Chain 1 160 . . . ID=PRO_0000299786;Note=Putative UPF0479 protein YHR219C-A +P0CL34 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL34 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL34 UniProtKB Compositional bias 103 106 . . . Note=Poly-Ser +##sequence-region P0C5N8 1 60 +P0C5N8 UniProtKB Chain 1 60 . . . ID=PRO_0000309036;Note=Putative uncharacterized protein YHR180W-A +P0C5N8 UniProtKB Transmembrane 38 58 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38729 1 150 +P38729 UniProtKB Signal peptide 1 39 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38729 UniProtKB Chain 40 150 . . . ID=PRO_0000014324;Note=Putative uncharacterized protein YHL042W +##sequence-region P38721 1 697 +P38721 UniProtKB Chain 1 697 . . . ID=PRO_0000202875;Note=Uncharacterized protein YHL050C +P38721 UniProtKB Transmembrane 65 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38721 UniProtKB Transmembrane 106 126 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38721 UniProtKB Transmembrane 131 151 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38721 UniProtKB Transmembrane 163 183 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38721 UniProtKB Transmembrane 194 214 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38721 UniProtKB Transmembrane 227 247 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38721 UniProtKB Transmembrane 286 306 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38721 UniProtKB Transmembrane 316 336 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38721 UniProtKB Transmembrane 361 381 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38721 UniProtKB Transmembrane 394 414 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38721 UniProtKB Transmembrane 419 439 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38721 UniProtKB Transmembrane 450 470 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38721 UniProtKB Transmembrane 487 507 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38721 UniProtKB Transmembrane 558 578 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38776 1 514 +P38776 UniProtKB Chain 1 514 . . . ID=PRO_0000173440;Note=Probable drug/proton antiporter YHK8 +P38776 UniProtKB Topological domain 1 74 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Transmembrane 75 95 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Topological domain 96 111 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Transmembrane 112 132 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Topological domain 133 141 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Transmembrane 142 162 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Topological domain 163 170 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Transmembrane 171 191 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Topological domain 192 200 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Transmembrane 201 221 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Topological domain 222 227 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Transmembrane 228 248 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Topological domain 249 307 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Transmembrane 308 328 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Topological domain 329 342 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Transmembrane 343 363 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Topological domain 364 386 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Transmembrane 387 407 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Topological domain 408 412 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Transmembrane 413 433 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Topological domain 434 447 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Transmembrane 448 468 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Topological domain 469 477 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Transmembrane 478 498 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38776 UniProtKB Topological domain 499 514 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38829 1 231 +P38829 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38829 UniProtKB Chain 2 231 . . . ID=PRO_0000212699;Note=MIP18 family protein YHR122W +P38829 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P40556 1 373 +P40556 UniProtKB Chain 1 373 . . . ID=PRO_0000090698;Note=Mitochondrial nicotinamide adenine dinucleotide transporter 1 +P40556 UniProtKB Topological domain 1 80 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40556 UniProtKB Transmembrane 81 101 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40556 UniProtKB Topological domain 102 141 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40556 UniProtKB Transmembrane 142 162 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40556 UniProtKB Topological domain 163 176 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40556 UniProtKB Transmembrane 177 199 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40556 UniProtKB Topological domain 200 235 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40556 UniProtKB Transmembrane 236 256 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40556 UniProtKB Topological domain 257 280 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40556 UniProtKB Transmembrane 281 297 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40556 UniProtKB Topological domain 298 335 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40556 UniProtKB Transmembrane 336 358 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40556 UniProtKB Topological domain 359 373 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40556 UniProtKB Repeat 75 166 . . . Note=Solcar 1 +P40556 UniProtKB Repeat 174 263 . . . Note=Solcar 2 +P40556 UniProtKB Repeat 276 364 . . . Note=Solcar 3 +##sequence-region P40524 1 105 +P40524 UniProtKB Chain 1 105 . . . ID=PRO_0000202990;Note=Uncharacterized membrane protein YIL054W +P40524 UniProtKB Topological domain 1 48 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40524 UniProtKB Transmembrane 49 69 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40524 UniProtKB Topological domain 70 70 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40524 UniProtKB Transmembrane 71 91 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40524 UniProtKB Topological domain 92 105 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40503 1 102 +P40503 UniProtKB Chain 1 102 . . . ID=PRO_0000202978;Note=Uncharacterized protein YIL086C +##sequence-region P28625 1 365 +P28625 UniProtKB Chain 1 365 . . . ID=PRO_0000203310;Note=Protein YIM1 +P28625 UniProtKB Sequence conflict 121 121 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28625 UniProtKB Sequence conflict 234 234 . . . Note=S->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28625 UniProtKB Sequence conflict 280 280 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28625 UniProtKB Sequence conflict 296 296 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40449 1 235 +P40449 UniProtKB Chain 1 235 . . . ID=PRO_0000202952;Note=Uncharacterized protein YIL161W +P40449 UniProtKB Cross-link 16 16 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P40449 UniProtKB Cross-link 35 35 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P40587 1 230 +P40587 UniProtKB Chain 1 230 . . . ID=PRO_0000207534;Note=Putative uncharacterized protein YIR043C +P40587 UniProtKB Transmembrane 93 115 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47105 1 127 +P47105 UniProtKB Chain 1 127 . . . ID=PRO_0000203091;Note=Putative uncharacterized protein YJR037W +##sequence-region P47107 1 1121 +P47107 UniProtKB Chain 1 1121 . . . ID=PRO_0000203093;Note=Uncharacterized protein YJR039W +##sequence-region P47099 1 440 +P47099 UniProtKB Chain 1 440 . . . ID=PRO_0000203497;Note=Transposon Ty1-JR2 Gag polyprotein +P47099 UniProtKB Chain 1 401 . . . ID=PRO_0000279092;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47099 UniProtKB Peptide 402 440 . . . ID=PRO_0000279093;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47099 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47099 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47099 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region P47115 1 236 +P47115 UniProtKB Chain 1 236 . . . ID=PRO_0000203097;Note=Uncharacterized protein YJR056C +P47115 UniProtKB Modified residue 221 221 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40355 1 935 +P40355 UniProtKB Chain 1 935 . . . ID=PRO_0000203098;Note=Uncharacterized protein YJR061W +P40355 UniProtKB Sequence conflict 197 197 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40355 UniProtKB Sequence conflict 312 312 . . . Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47132 1 116 +P47132 UniProtKB Chain 1 116 . . . ID=PRO_0000203106;Note=Putative uncharacterized protein YJR087W +##sequence-region P47181 1 346 +P47181 UniProtKB Chain 1 346 . . . ID=PRO_0000215232;Note=Uncharacterized protein YJR154W +P47181 UniProtKB Sequence conflict 300 300 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47066 1 102 +P47066 UniProtKB Chain 1 102 . . . ID=PRO_0000203073;Note=Putative uncharacterized protein YJL009W +##sequence-region P47053 1 257 +P47053 UniProtKB Chain 1 257 . . . ID=PRO_0000203067;Note=Uncharacterized protein YJL043W +P47053 UniProtKB Sequence conflict 251 251 . . . Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47038 1 131 +P47038 UniProtKB Chain 1 131 . . . ID=PRO_0000203058;Note=Putative uncharacterized protein YJL064W +##sequence-region P0CL26 1 75 +P0CL26 UniProtKB Chain 1 75 . . . ID=PRO_0000406045;Note=Putative UPF0377 protein YJL222W-A +##sequence-region P46987 1 611 +P46987 UniProtKB Chain 1 611 . . . ID=PRO_0000203023;Note=UPF0508 protein YJL181W +P46987 UniProtKB Compositional bias 6 10 . . . Note=Poly-Glu +##sequence-region P40896 1 331 +P40896 UniProtKB Chain 1 331 . . . ID=PRO_0000203013;Note=Uncharacterized protein YJL213W +##sequence-region P47091 1 120 +P47091 UniProtKB Chain 1 120 . . . ID=PRO_0000203086;Note=Putative uncharacterized protein YJR018W +P47091 UniProtKB Transmembrane 93 109 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q2V2P3 1 75 +Q2V2P3 UniProtKB Chain 1 75 . . . ID=PRO_0000245423;Note=Uncharacterized protein YKL023C-A +Q2V2P3 UniProtKB Transmembrane 47 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12336 1 168 +Q12336 UniProtKB Chain 1 168 . . . ID=PRO_0000299607;Note=Putative uncharacterized protein YLL059C +Q12336 UniProtKB Transmembrane 27 47 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12336 UniProtKB Transmembrane 147 167 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12259 1 485 +Q12259 UniProtKB Chain 1 485 . . . ID=PRO_0000247339;Note=BTB/POZ domain-containing protein YLR108C +Q12259 UniProtKB Domain 26 121 . . . Note=BTB +##sequence-region Q12327 1 114 +Q12327 UniProtKB Chain 1 114 . . . ID=PRO_0000299616;Note=Putative uncharacterized protein YLR124W +Q12327 UniProtKB Compositional bias 77 82 . . . Note=Poly-Lys +##sequence-region P0C2I8 1 440 +P0C2I8 UniProtKB Chain 1 440 . . . ID=PRO_0000279114;Note=Transposon Ty1-LR4 Gag polyprotein +P0C2I8 UniProtKB Chain 1 401 . . . ID=PRO_0000279115;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I8 UniProtKB Peptide 402 440 . . . ID=PRO_0000279116;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I8 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I8 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0C2I8 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2I8 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region O13561 1 117 +O13561 UniProtKB Chain 1 117 . . . ID=PRO_0000299618;Note=Putative uncharacterized protein YLR169W +O13561 UniProtKB Transmembrane 9 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13561 UniProtKB Transmembrane 56 76 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region O13562 1 129 +O13562 UniProtKB Chain 1 129 . . . ID=PRO_0000299619;Note=Putative uncharacterized protein YLR171W +O13562 UniProtKB Transmembrane 49 69 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13562 UniProtKB Transmembrane 72 92 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13562 UniProtKB Transmembrane 101 118 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06247 1 608 +Q06247 UniProtKB Chain 1 608 . . . ID=PRO_0000247113;Note=Putative uncharacterized protein YLR173W +Q06247 UniProtKB Transmembrane 55 75 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06247 UniProtKB Modified residue 24 24 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06247 UniProtKB Modified residue 27 27 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06247 UniProtKB Glycosylation 115 115 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06247 UniProtKB Glycosylation 141 141 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06247 UniProtKB Glycosylation 169 169 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06247 UniProtKB Glycosylation 407 407 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06247 UniProtKB Glycosylation 425 425 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06247 UniProtKB Glycosylation 449 449 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06247 UniProtKB Glycosylation 453 453 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06247 UniProtKB Glycosylation 527 527 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06247 UniProtKB Glycosylation 580 580 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06252 1 201 +Q06252 UniProtKB Chain 1 201 . . . ID=PRO_0000204754;Note=Uncharacterized protein YLR179C +##sequence-region O13530 1 119 +O13530 UniProtKB Chain 1 119 . . . ID=PRO_0000299621;Note=Putative uncharacterized protein YLR198C +O13530 UniProtKB Transmembrane 19 39 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13530 UniProtKB Transmembrane 68 88 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region O13532 1 107 +O13532 UniProtKB Chain 1 107 . . . ID=PRO_0000299623;Note=Putative uncharacterized protein YLR217W +##sequence-region P0C5P7 1 76 +P0C5P7 UniProtKB Chain 1 76 . . . ID=PRO_0000309045;Note=Putative uncharacterized protein YLR222C-A +##sequence-region Q05947 1 369 +Q05947 UniProtKB Chain 1 369 . . . ID=PRO_0000269758;Note=F-box protein YLR224W +Q05947 UniProtKB Domain 8 45 . . . Note=F-box +##sequence-region P0C2J6 1 438 +P0C2J6 UniProtKB Chain 1 438 . . . ID=PRO_0000279337;Note=Transposon Ty2-LR2 Gag polyprotein +P0C2J6 UniProtKB Chain 1 397 . . . ID=PRO_0000279338;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J6 UniProtKB Peptide 398 438 . . . ID=PRO_0000279339;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J6 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C2J6 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q05881 1 355 +Q05881 UniProtKB Chain 1 355 . . . ID=PRO_0000247209;Note=Uncharacterized protein YLR287C +##sequence-region O13543 1 109 +O13543 UniProtKB Chain 1 109 . . . ID=PRO_0000299632;Note=Putative uncharacterized protein YLR294C +O13543 UniProtKB Transmembrane 82 102 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13543 UniProtKB Compositional bias 86 89 . . . Note=Poly-Leu +##sequence-region Q05899 1 129 +Q05899 UniProtKB Chain 1 129 . . . ID=PRO_0000247161;Note=Uncharacterized vacuolar protein YLR297W +Q05899 UniProtKB Transmembrane 77 97 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06158 1 115 +Q06158 UniProtKB Chain 1 115 . . . ID=PRO_0000262740;Note=Putative uncharacterized membrane protein YLR311C +Q06158 UniProtKB Topological domain 1 11 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06158 UniProtKB Transmembrane 12 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06158 UniProtKB Topological domain 33 52 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06158 UniProtKB Transmembrane 53 73 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06158 UniProtKB Topological domain 74 78 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06158 UniProtKB Transmembrane 79 98 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06158 UniProtKB Topological domain 99 115 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06170 1 240 +Q06170 UniProtKB Chain 1 240 . . . ID=PRO_0000247210;Note=Uncharacterized membrane protein YLR326W +Q06170 UniProtKB Topological domain 1 85 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06170 UniProtKB Transmembrane 86 106 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06170 UniProtKB Topological domain 107 131 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06170 UniProtKB Transmembrane 132 152 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06170 UniProtKB Topological domain 153 240 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06127 1 126 +Q06127 UniProtKB Chain 1 126 . . . ID=PRO_0000299637;Note=Putative uncharacterized protein YLR334C +Q06127 UniProtKB Transmembrane 4 24 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06127 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06127 UniProtKB Transmembrane 64 84 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region O94086 1 168 +O94086 UniProtKB Chain 1 168 . . . ID=PRO_0000299640;Note=Putative uncharacterized protein YLR349W +##sequence-region O13565 1 187 +O13565 UniProtKB Chain 1 187 . . . ID=PRO_0000299641;Note=Uncharacterized protein YLR358C +O13565 UniProtKB Compositional bias 50 81 . . . Note=Ser-rich +##sequence-region Q7LIF1 1 101 +Q7LIF1 UniProtKB Chain 1 101 . . . ID=PRO_0000299643;Note=Putative uncharacterized protein YLR366W +##sequence-region O13556 1 202 +O13556 UniProtKB Chain 1 202 . . . ID=PRO_0000268171;Note=Putative uncharacterized protein YLR462W +##sequence-region P0CL38 1 160 +P0CL38 UniProtKB Chain 1 160 . . . ID=PRO_0000406012;Note=Putative UPF0479 protein YLR466C-A +P0CL38 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL38 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL38 UniProtKB Compositional bias 103 106 . . . Note=Poly-Ser +##sequence-region Q04978 1 212 +Q04978 UniProtKB Chain 1 212 . . . ID=PRO_0000203254;Note=Uncharacterized protein YML053C +##sequence-region Q12204 1 715 +Q12204 UniProtKB Transit peptide 1 22 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12204 UniProtKB Chain 23 715 . . . ID=PRO_0000237644;Note=Probable phospholipase YOR022C%2C mitochondrial +Q12204 UniProtKB Domain 519 700 . . . Note=DDHD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00378 +Q12204 UniProtKB Active site 501 501 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q08419 1 115 +Q08419 UniProtKB Chain 1 115 . . . ID=PRO_0000299706;Note=Putative uncharacterized protein YOR050C +##sequence-region Q08486 1 104 +Q08486 UniProtKB Chain 1 104 . . . ID=PRO_0000299709;Note=Uncharacterized protein YOR072W +##sequence-region Q08994 1 102 +Q08994 UniProtKB Chain 1 102 . . . ID=PRO_0000268173;Note=Putative uncharacterized protein YPR203W +##sequence-region Q08974 1 193 +Q08974 UniProtKB Chain 1 193 . . . ID=PRO_0000242486;Note=Uncharacterized membrane protein YPL257W +Q08974 UniProtKB Topological domain 1 58 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08974 UniProtKB Transmembrane 59 79 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08974 UniProtKB Topological domain 80 119 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08974 UniProtKB Transmembrane 120 140 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08974 UniProtKB Topological domain 141 147 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08974 UniProtKB Transmembrane 148 168 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08974 UniProtKB Topological domain 169 193 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08989 1 487 +Q08989 UniProtKB Signal peptide 1 31 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08989 UniProtKB Chain 32 487 . . . ID=PRO_0000269760;Note=Uncharacterized protein YPL277C +Q08989 UniProtKB Glycosylation 40 40 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08989 UniProtKB Glycosylation 68 68 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08989 UniProtKB Glycosylation 150 150 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08989 UniProtKB Glycosylation 220 220 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08989 UniProtKB Glycosylation 304 304 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08989 UniProtKB Glycosylation 367 367 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08989 UniProtKB Glycosylation 442 442 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08989 UniProtKB Glycosylation 448 448 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CX20 1 1796 +P0CX20 UniProtKB Chain 1 1796 . . . ID=PRO_0000102201;Note=Y' element ATP-dependent helicase protein 1 copy 1 +P0CX20 UniProtKB Domain 797 974 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P0CX20 UniProtKB Domain 1031 1180 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P0CX20 UniProtKB Nucleotide binding 810 817 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +##sequence-region P0CX21 1 1796 +P0CX21 UniProtKB Chain 1 1796 . . . ID=PRO_0000409756;Note=Y' element ATP-dependent helicase protein 1 copy 5 +P0CX21 UniProtKB Domain 797 974 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P0CX21 UniProtKB Domain 1031 1180 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P0CX21 UniProtKB Nucleotide binding 810 817 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +##sequence-region P42844 1 174 +P42844 UniProtKB Transit peptide 1 47 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15719019;Dbxref=PMID:15719019 +P42844 UniProtKB Chain 48 174 . . . ID=PRO_0000203367;Note=Mitochondrial protein import protein ZIM17 +P42844 UniProtKB Zinc finger 64 159 . . . Note=DNL-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00834 +P42844 UniProtKB Metal binding 75 75 . . . Note=Zinc +P42844 UniProtKB Metal binding 78 78 . . . Note=Zinc +P42844 UniProtKB Metal binding 100 100 . . . Note=Zinc +P42844 UniProtKB Metal binding 103 103 . . . Note=Zinc +P42844 UniProtKB Mutagenesis 106 107 . . . Note=In TIM15-2RH%3B Abolishes interaction with SSC1%2C and leads to self-aggregation of mtHSP70 and accumulation of uncleaved precursor proteins. RH->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17571076;Dbxref=PMID:17571076 +P42844 UniProtKB Mutagenesis 111 111 . . . Note=Abolishes interaction with SSC1%2C and leads to self-aggregation of mtHSP70 and accumulation of uncleaved precursor proteins. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17571076;Dbxref=PMID:17571076 +P42844 UniProtKB Mutagenesis 133 137 . . . Note=Temperature sensitive%3B only partly prevents self-aggregation of mtHSP70 and leads to accumulation of uncleaved precursor proteins at high temperatures. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17571076;Dbxref=PMID:17571076 +P42844 UniProtKB Mutagenesis 140 148 . . . Note=In TIM15-5DE%3B no effect. DLEFEDIPD->ALAFAAIPA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17571076;Dbxref=PMID:17571076 +P42844 UniProtKB Beta strand 68 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z +P42844 UniProtKB Turn 76 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z +P42844 UniProtKB Beta strand 80 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z +P42844 UniProtKB Helix 88 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z +P42844 UniProtKB Beta strand 94 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z +P42844 UniProtKB Beta strand 106 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z +P42844 UniProtKB Helix 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z +P42844 UniProtKB Helix 123 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z +P42844 UniProtKB Beta strand 135 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z +P42844 UniProtKB Beta strand 140 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z +P42844 UniProtKB Helix 148 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z +P42844 UniProtKB Beta strand 155 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2Z +##sequence-region Q8TGS0 1 48 +Q8TGS0 UniProtKB Chain 1 48 . . . ID=PRO_0000237660;Note=Uncharacterized protein YOR161C-C +Q8TGS0 UniProtKB Transmembrane 20 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08543 1 101 +Q08543 UniProtKB Chain 1 101 . . . ID=PRO_0000299720;Note=Putative uncharacterized protein YOR170W +##sequence-region Q08604 1 109 +Q08604 UniProtKB Chain 1 109 . . . ID=PRO_0000299722;Note=Putative uncharacterized protein YOR199W +Q08604 UniProtKB Transmembrane 78 98 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08604 UniProtKB Compositional bias 9 12 . . . Note=Poly-Lys +##sequence-region Q08748 1 1289 +Q08748 UniProtKB Chain 1 1289 . . . ID=PRO_0000245284;Note=Uncharacterized protein YOR296W +Q08748 UniProtKB Domain 615 733 . . . Note=MHD1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00587 +Q08748 UniProtKB Domain 843 947 . . . Note=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 +Q08748 UniProtKB Domain 1044 1184 . . . Note=MHD2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00588 +##sequence-region Q12444 1 126 +Q12444 UniProtKB Chain 1 126 . . . ID=PRO_0000299734;Note=Putative uncharacterized protein YOR309C +Q12444 UniProtKB Compositional bias 44 83 . . . Note=Arg/Lys-rich +##sequence-region Q08816 1 343 +Q08816 UniProtKB Chain 1 343 . . . ID=PRO_0000245290;Note=Uncharacterized protein YOR352W +Q08816 UniProtKB Modified residue 69 69 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08816 UniProtKB Modified residue 105 105 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08816 UniProtKB Modified residue 108 108 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08816 UniProtKB Modified residue 342 342 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q08909 1 290 +Q08909 UniProtKB Chain 1 290 . . . ID=PRO_0000244636;Note=Uncharacterized protein YOR385W +##sequence-region Q8TGJ0 1 55 +Q8TGJ0 UniProtKB Chain 1 55 . . . ID=PRO_0000240708;Note=Uncharacterized protein YOR394C-A +##sequence-region Q8TGL4 1 86 +Q8TGL4 UniProtKB Chain 1 86 . . . ID=PRO_0000299718;Note=Putative uncharacterized protein YOR161W-B +##sequence-region Q8TGL3 1 69 +Q8TGL3 UniProtKB Chain 1 69 . . . ID=PRO_0000299721;Note=Putative uncharacterized protein YOR186C-A +##sequence-region Q08259 1 102 +Q08259 UniProtKB Chain 1 102 . . . ID=PRO_0000299695;Note=Uncharacterized protein YOL118C +##sequence-region Q12070 1 107 +Q12070 UniProtKB Signal peptide 1 34 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12070 UniProtKB Chain 35 107 . . . ID=PRO_0000299703;Note=Putative uncharacterized protein YOR024W +##sequence-region Q08900 1 122 +Q08900 UniProtKB Chain 1 122 . . . ID=PRO_0000262745;Note=Uncharacterized membrane protein YOR376W +Q08900 UniProtKB Topological domain 1 24 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12524434,ECO:0000305|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258 +Q08900 UniProtKB Transmembrane 25 45 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08900 UniProtKB Topological domain 46 57 . . . Note=Extracellular;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12524434,ECO:0000305|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258 +Q08900 UniProtKB Transmembrane 58 78 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08900 UniProtKB Topological domain 79 122 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12524434,ECO:0000269|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258 +##sequence-region Q12274 1 175 +Q12274 UniProtKB Chain 1 175 . . . ID=PRO_0000237654;Note=Uncharacterized protein YOR097C +Q12274 UniProtKB Transmembrane 21 41 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12274 UniProtKB Transmembrane 50 70 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A5Z2X5 1 72 +A5Z2X5 UniProtKB Chain 1 72 . . . ID=PRO_0000306772;Note=UPF0495 protein YPR010C-A +A5Z2X5 UniProtKB Transmembrane 20 42 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04203 1 84 +Q04203 UniProtKB Chain 1 84 . . . ID=PRO_0000299814;Note=Putative uncharacterized protein YPR012W +Q04203 UniProtKB Transmembrane 10 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12531 1 247 +Q12531 UniProtKB Chain 1 247 . . . ID=PRO_0000255975;Note=Zinc finger protein YPR015C +Q12531 UniProtKB Zinc finger 185 207 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q12531 UniProtKB Zinc finger 213 237 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q12531 UniProtKB Sequence conflict 184 184 . . . Note=R->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02606 1 381 +Q02606 UniProtKB Chain 1 381 . . . ID=PRO_0000240703;Note=Uncharacterized protein YPL014W +##sequence-region Q12492 1 139 +Q12492 UniProtKB Chain 1 139 . . . ID=PRO_0000299819;Note=Uncharacterized protein YPR064W +Q12492 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12492 UniProtKB Transmembrane 119 139 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12492 UniProtKB Compositional bias 118 138 . . . Note=Cys-rich +##sequence-region P0C5R6 1 56 +P0C5R6 UniProtKB Chain 1 56 . . . ID=PRO_0000309064;Note=Putative uncharacterized protein YPR074W-A +##sequence-region Q02872 1 168 +Q02872 UniProtKB Chain 1 168 . . . ID=PRO_0000238647;Note=Uncharacterized protein YPL108W +##sequence-region Q06107 1 315 +Q06107 UniProtKB Chain 1 315 . . . ID=PRO_0000242487;Note=Uncharacterized TLC domain-containing protein YPR114W +Q06107 UniProtKB Topological domain 1 38 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06107 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06107 UniProtKB Topological domain 60 101 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06107 UniProtKB Transmembrane 102 122 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06107 UniProtKB Topological domain 123 144 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06107 UniProtKB Transmembrane 145 165 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06107 UniProtKB Topological domain 166 170 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06107 UniProtKB Transmembrane 171 190 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06107 UniProtKB Topological domain 191 225 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06107 UniProtKB Transmembrane 226 246 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06107 UniProtKB Topological domain 247 264 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06107 UniProtKB Transmembrane 265 285 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06107 UniProtKB Topological domain 286 315 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06107 UniProtKB Domain 95 302 . . . Note=TLC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00205 +##sequence-region Q12414 1 1755 +Q12414 UniProtKB Chain 1 1755 . . . ID=PRO_0000279169;Note=Transposon Ty1-PL Gag-Pol polyprotein +Q12414 UniProtKB Chain 1 401 . . . ID=PRO_0000279170;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12414 UniProtKB Chain 402 582 . . . ID=PRO_0000279171;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12414 UniProtKB Chain 583 1217 . . . ID=PRO_0000279172;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12414 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279173;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12414 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12414 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +Q12414 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +Q12414 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12414 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q12414 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12414 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q12414 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q12414 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12414 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12414 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12414 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12414 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12414 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12414 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12414 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12414 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12414 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12414 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12414 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region Q08916 1 105 +Q08916 UniProtKB Chain 1 105 . . . ID=PRO_0000299754;Note=Putative uncharacterized protein YPL142C +##sequence-region P0C5R7 1 72 +P0C5R7 UniProtKB Chain 1 72 . . . ID=PRO_0000309065;Note=Putative uncharacterized protein YPR169W-A +P0C5R7 UniProtKB Transmembrane 11 31 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06595 1 470 +Q06595 UniProtKB Chain 1 470 . . . ID=PRO_0000257819;Note=Maltose fermentation regulatory protein YPR196W +Q06595 UniProtKB DNA binding 8 34 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +Q06595 UniProtKB Motif 41 49 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08964 1 1102 +Q08964 UniProtKB Chain 1 1102 . . . ID=PRO_0000242161;Note=Putative ISWI chromatin-remodeling complex subunit YPL216W +Q08964 UniProtKB Domain 23 131 . . . Note=WAC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00475 +Q08964 UniProtKB Domain 375 435 . . . Note=DDT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00063 +Q08964 UniProtKB Coiled coil 673 743 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CL31 1 191 +P0CL31 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL31 UniProtKB Chain 18 191 . . . ID=PRO_0000406008;Note=Putative uncharacterized protein YPL283W-A +P0CL31 UniProtKB Transmembrane 168 188 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL31 UniProtKB Compositional bias 13 159 . . . Note=Gly/Ser-rich +##sequence-region Q12010 1 308 +Q12010 UniProtKB Chain 1 308 . . . ID=PRO_0000235929;Note=Probable vacuolar amino acid transporter YPQ1 +Q12010 UniProtKB Topological domain 1 12 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12010 UniProtKB Transmembrane 13 33 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12010 UniProtKB Topological domain 34 44 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12010 UniProtKB Transmembrane 45 65 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12010 UniProtKB Topological domain 66 68 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12010 UniProtKB Transmembrane 69 89 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12010 UniProtKB Topological domain 90 167 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12010 UniProtKB Transmembrane 168 188 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12010 UniProtKB Topological domain 189 205 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12010 UniProtKB Transmembrane 206 226 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12010 UniProtKB Topological domain 227 244 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12010 UniProtKB Transmembrane 245 265 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12010 UniProtKB Topological domain 266 277 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12010 UniProtKB Transmembrane 278 298 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12010 UniProtKB Topological domain 299 308 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12010 UniProtKB Domain 10 76 . . . Note=PQ-loop 1 +Q12010 UniProtKB Domain 211 274 . . . Note=PQ-loop 2 +Q12010 UniProtKB Glycosylation 9 9 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12010 UniProtKB Glycosylation 189 189 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12010 UniProtKB Glycosylation 275 275 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region O13559 1 1382 +O13559 UniProtKB Chain 1 1382 . . . ID=PRO_0000102204;Note=Y' element ATP-dependent helicase protein 1 copy 4 +O13559 UniProtKB Domain 383 560 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +O13559 UniProtKB Domain 617 766 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +O13559 UniProtKB Nucleotide binding 396 403 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +##sequence-region P32793 1 468 +P32793 UniProtKB Chain 1 468 . . . ID=PRO_0000202887;Note=Protein YSC84 +P32793 UniProtKB Domain 409 468 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P32793 UniProtKB Compositional bias 222 307 . . . Note=Asp-rich +P32793 UniProtKB Modified residue 301 301 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P32793 UniProtKB Modified residue 311 311 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32793 UniProtKB Beta strand 413 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A08 +P32793 UniProtKB Beta strand 435 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A08 +P32793 UniProtKB Beta strand 447 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A08 +P32793 UniProtKB Beta strand 456 461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A08 +P32793 UniProtKB Helix 462 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A08 +P32793 UniProtKB Beta strand 465 467 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A08 +##sequence-region P0C074 1 85 +P0C074 UniProtKB Chain 1 85 . . . ID=PRO_0000097203;Note=RDS3 complex subunit 10 +##sequence-region P26725 1 428 +P26725 UniProtKB Chain 1 428 . . . ID=PRO_0000208250;Note=Probable mannosyltransferase YUR1 +P26725 UniProtKB Topological domain 1 3 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P26725 UniProtKB Transmembrane 4 24 . . . Note=Helical%3B Signal-anchor for type II membrane protein +P26725 UniProtKB Topological domain 25 428 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P26725 UniProtKB Region 25 88 . . . Note=Stem region;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26725 UniProtKB Region 89 428 . . . Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26725 UniProtKB Active site 313 313 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P26725 UniProtKB Glycosylation 77 77 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P26725 UniProtKB Glycosylation 82 82 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P26725 UniProtKB Glycosylation 92 92 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P26725 UniProtKB Glycosylation 167 167 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P26725 UniProtKB Glycosylation 414 414 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53735 1 605 +P53735 UniProtKB Chain 1 605 . . . ID=PRO_0000203477;Note=Protein ZRG17 +P53735 UniProtKB Topological domain 1 225 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53735 UniProtKB Transmembrane 226 246 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53735 UniProtKB Topological domain 247 254 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53735 UniProtKB Transmembrane 255 275 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53735 UniProtKB Topological domain 276 287 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53735 UniProtKB Transmembrane 288 308 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53735 UniProtKB Topological domain 309 309 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53735 UniProtKB Transmembrane 310 330 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53735 UniProtKB Topological domain 331 363 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53735 UniProtKB Transmembrane 364 384 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53735 UniProtKB Topological domain 385 399 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53735 UniProtKB Transmembrane 400 420 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53735 UniProtKB Topological domain 421 422 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53735 UniProtKB Transmembrane 423 443 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53735 UniProtKB Topological domain 444 545 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53735 UniProtKB Transmembrane 546 566 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53735 UniProtKB Topological domain 567 605 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53735 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53735 UniProtKB Modified residue 131 131 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P53735 UniProtKB Modified residue 498 498 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53735 UniProtKB Sequence conflict 239 239 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P20107 1 442 +P20107 UniProtKB Chain 1 442 . . . ID=PRO_0000206103;Note=Zinc/cadmium resistance protein +P20107 UniProtKB Topological domain 1 9 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20107 UniProtKB Transmembrane 10 26 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20107 UniProtKB Topological domain 27 41 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20107 UniProtKB Transmembrane 42 58 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20107 UniProtKB Topological domain 59 79 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20107 UniProtKB Transmembrane 80 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20107 UniProtKB Topological domain 97 112 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20107 UniProtKB Transmembrane 113 129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20107 UniProtKB Topological domain 130 239 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20107 UniProtKB Transmembrane 240 256 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20107 UniProtKB Topological domain 257 269 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20107 UniProtKB Transmembrane 270 286 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20107 UniProtKB Topological domain 287 442 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20107 UniProtKB Compositional bias 141 145 . . . Note=His-rich (could be involved in coordination of zinc or cadmium ions) +P20107 UniProtKB Compositional bias 163 167 . . . Note=His-rich (could be involved in coordination of zinc or cadmium ions) +P20107 UniProtKB Compositional bias 216 220 . . . Note=His-rich (could be involved in coordination of zinc or cadmium ions) +P20107 UniProtKB Modified residue 387 387 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P20107 UniProtKB Modified residue 393 393 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P20107 UniProtKB Modified residue 397 397 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P20107 UniProtKB Cross-link 357 357 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P20107 UniProtKB Sequence conflict 414 414 . . . Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20107 UniProtKB Sequence conflict 417 417 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32804 1 376 +P32804 UniProtKB Chain 1 376 . . . ID=PRO_0000068768;Note=Zinc-regulated transporter 1 +P32804 UniProtKB Topological domain 1 50 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32804 UniProtKB Transmembrane 51 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32804 UniProtKB Topological domain 72 80 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32804 UniProtKB Transmembrane 81 101 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32804 UniProtKB Topological domain 102 122 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32804 UniProtKB Transmembrane 123 143 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32804 UniProtKB Topological domain 144 216 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32804 UniProtKB Transmembrane 217 237 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32804 UniProtKB Topological domain 238 242 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32804 UniProtKB Transmembrane 243 263 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32804 UniProtKB Topological domain 264 278 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32804 UniProtKB Transmembrane 279 299 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32804 UniProtKB Topological domain 300 310 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32804 UniProtKB Transmembrane 311 331 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32804 UniProtKB Topological domain 332 354 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32804 UniProtKB Transmembrane 355 375 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32804 UniProtKB Topological domain 376 376 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32804 UniProtKB Region 232 233 . . . Note=Heavy metals binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P34240 1 503 +P34240 UniProtKB Chain 1 503 . . . ID=PRO_0000203140;Note=Zinc-regulated transporter 3 +P34240 UniProtKB Transmembrane 8 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34240 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34240 UniProtKB Transmembrane 75 95 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34240 UniProtKB Transmembrane 336 356 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34240 UniProtKB Transmembrane 371 391 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34240 UniProtKB Transmembrane 398 418 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34240 UniProtKB Transmembrane 438 458 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34240 UniProtKB Transmembrane 482 502 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34240 UniProtKB Compositional bias 102 139 . . . Note=His-rich +P34240 UniProtKB Compositional bias 153 158 . . . Note=Poly-Ser +P34240 UniProtKB Compositional bias 322 325 . . . Note=Poly-His +P34240 UniProtKB Compositional bias 464 467 . . . Note=Poly-His +P34240 UniProtKB Modified residue 178 178 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P34240 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P0CX14 1 1859 +P0CX14 UniProtKB Chain 1 1859 . . . ID=PRO_0000102203;Note=Y' element ATP-dependent helicase protein 1 copy 3 +P0CX14 UniProtKB Domain 861 1038 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P0CX14 UniProtKB Domain 1095 1244 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P0CX14 UniProtKB Nucleotide binding 874 881 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +##sequence-region Q06681 1 1438 +Q06681 UniProtKB Chain 1 1438 . . . ID=PRO_0000253815;Note=Membrane-anchored lipid-binding protein YSP2 +Q06681 UniProtKB Topological domain 1 1277 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06681 UniProtKB Transmembrane 1278 1298 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06681 UniProtKB Topological domain 1299 1438 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06681 UniProtKB Domain 648 716 . . . Note=GRAM;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06681 UniProtKB Domain 851 1018 . . . Note=VASt 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01114 +Q06681 UniProtKB Domain 1059 1225 . . . Note=VASt 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01114 +Q06681 UniProtKB Compositional bias 219 232 . . . Note=Asn-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00003 +Q06681 UniProtKB Compositional bias 770 815 . . . Note=Asp-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00004 +Q06681 UniProtKB Modified residue 13 13 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950 +Q06681 UniProtKB Modified residue 411 411 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06681 UniProtKB Modified residue 596 596 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06681 UniProtKB Modified residue 1032 1032 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06681 UniProtKB Glycosylation 1306 1306 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +Q06681 UniProtKB Glycosylation 1373 1373 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +Q06681 UniProtKB Glycosylation 1430 1430 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +Q06681 UniProtKB Mutagenesis 1205 1205 . . . Note=Reduces the ability to bind sterol. G->A%2CT;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26001273;Dbxref=PMID:26001273 +Q06681 UniProtKB Mutagenesis 1205 1205 . . . Note=Abolishes the ability to bind sterol. G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26001273;Dbxref=PMID:26001273 +##sequence-region P40341 1 825 +P40341 UniProtKB Chain 1 825 . . . ID=PRO_0000084676;Note=Mitochondrial respiratory chain complexes assembly protein YTA12 +P40341 UniProtKB Transmembrane 178 194 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40341 UniProtKB Transmembrane 294 311 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40341 UniProtKB Nucleotide binding 388 395 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40341 UniProtKB Active site 614 614 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40341 UniProtKB Metal binding 613 613 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40341 UniProtKB Metal binding 617 617 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40341 UniProtKB Metal binding 689 689 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40341 UniProtKB Mutagenesis 614 614 . . . Note=Abolishes proteolytic activity%3B impairs synthesis of respiratory chain proteins COB and COX1. No effect on m-AAA protease assembly. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9707443;Dbxref=PMID:9707443 +P40341 UniProtKB Sequence conflict 195 195 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40341 UniProtKB Sequence conflict 349 350 . . . Note=DV->EL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40341 UniProtKB Sequence conflict 653 653 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P31383 1 635 +P31383 UniProtKB Chain 1 635 . . . ID=PRO_0000071414;Note=Protein phosphatase PP2A regulatory subunit A +P31383 UniProtKB Repeat 34 72 . . . Note=HEAT 1 +P31383 UniProtKB Repeat 73 111 . . . Note=HEAT 2 +P31383 UniProtKB Repeat 112 150 . . . Note=HEAT 3 +P31383 UniProtKB Repeat 151 189 . . . Note=HEAT 4 +P31383 UniProtKB Repeat 190 228 . . . Note=HEAT 5 +P31383 UniProtKB Repeat 229 273 . . . Note=HEAT 6 +P31383 UniProtKB Repeat 274 316 . . . Note=HEAT 7 +P31383 UniProtKB Repeat 317 356 . . . Note=HEAT 8 +P31383 UniProtKB Repeat 357 395 . . . Note=HEAT 9 +P31383 UniProtKB Repeat 396 434 . . . Note=HEAT 10 +P31383 UniProtKB Repeat 435 473 . . . Note=HEAT 11 +P31383 UniProtKB Repeat 474 512 . . . Note=HEAT 12 +P31383 UniProtKB Repeat 513 553 . . . Note=HEAT 13 +P31383 UniProtKB Repeat 554 598 . . . Note=HEAT 14 +P31383 UniProtKB Repeat 599 632 . . . Note=HEAT 15 +P31383 UniProtKB Sequence conflict 336 336 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31383 UniProtKB Sequence conflict 356 356 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31383 UniProtKB Sequence conflict 366 366 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31383 UniProtKB Sequence conflict 611 611 . . . Note=C->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08361 1 143 +Q08361 UniProtKB Chain 1 143 . . . ID=PRO_0000070370;Note=Putative aryl-alcohol dehydrogenase AAD15 +##sequence-region P43547 1 212 +P43547 UniProtKB Chain 1 212 . . . ID=PRO_0000070367;Note=Putative aryl-alcohol dehydrogenase AAD6 +P43547 UniProtKB Active site 76 76 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43547 UniProtKB Sequence conflict 208 208 . . . Note=V->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P15891 1 592 +P15891 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.4;Dbxref=PMID:22814378 +P15891 UniProtKB Chain 2 592 . . . ID=PRO_0000064429;Note=Actin-binding protein +P15891 UniProtKB Domain 7 136 . . . Note=ADF-H;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00599 +P15891 UniProtKB Repeat 200 209 . . . Note=1 +P15891 UniProtKB Repeat 436 445 . . . Note=2 +P15891 UniProtKB Domain 532 592 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P15891 UniProtKB Repeat 566 575 . . . Note=3 +P15891 UniProtKB Region 200 575 . . . Note=3 X 10 AA approximate repeats (acidic) +P15891 UniProtKB Compositional bias 518 522 . . . Note=Poly-Pro +P15891 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.4;Dbxref=PMID:22814378 +P15891 UniProtKB Modified residue 165 165 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P15891 UniProtKB Modified residue 167 167 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P15891 UniProtKB Modified residue 169 169 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +P15891 UniProtKB Modified residue 181 181 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P15891 UniProtKB Modified residue 183 183 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P15891 UniProtKB Modified residue 313 313 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P15891 UniProtKB Modified residue 365 365 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P15891 UniProtKB Modified residue 389 389 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P15891 UniProtKB Modified residue 458 458 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P15891 UniProtKB Modified residue 481 481 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P15891 UniProtKB Cross-link 464 464 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P15891 UniProtKB Mutagenesis 21 21 . . . Note=In ABP1-1%3B moderately reduces actin binding and partially reduces ARP2/3 complex activation%3B when associated with A-24. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15872087;Dbxref=PMID:15872087 +P15891 UniProtKB Mutagenesis 24 24 . . . Note=In ABP1-1%3B moderately reduces actin binding and partially reduces ARP2/3 complex activation%3B when associated with A-21. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15872087;Dbxref=PMID:15872087 +P15891 UniProtKB Mutagenesis 80 80 . . . Note=In ABP1-2%3B strongly reduces actin binding and abolishes ARP2/3 complex activation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15872087;Dbxref=PMID:15872087 +P15891 UniProtKB Mutagenesis 94 94 . . . Note=In ABP1-3%3B reduces actin binding and abolishes ARP2/3 complex activation%3B when associated with A-96. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15872087;Dbxref=PMID:15872087 +P15891 UniProtKB Mutagenesis 96 96 . . . Note=In ABP1-3%3B reduces actin binding and abolishes ARP2/3 complex activation%3B when associated with A-94. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15872087;Dbxref=PMID:15872087 +P15891 UniProtKB Mutagenesis 122 122 . . . Note=In ABP1-4%3B no effect%3B when associated with A-125. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15872087;Dbxref=PMID:15872087 +P15891 UniProtKB Mutagenesis 125 125 . . . Note=In ABP1-4%3B no effect%3B when associated with A-122. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15872087;Dbxref=PMID:15872087 +P15891 UniProtKB Mutagenesis 134 134 . . . Note=In ABP1-5%3B moderately reduces actin binding and abolishes ARP2/3 complex activation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15872087;Dbxref=PMID:15872087 +P15891 UniProtKB Mutagenesis 201 203 . . . Note=Abolishes ARP2/3 complex activation%2C but not actin binding. DDW->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11331312;Dbxref=PMID:11331312 +P15891 UniProtKB Mutagenesis 437 439 . . . Note=Abolishes ARP2/3 complex activation%2C but not actin binding. DDW->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11331312;Dbxref=PMID:11331312 +P15891 UniProtKB Mutagenesis 569 569 . . . Note=Abolishes protein binding. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11668184;Dbxref=PMID:11668184 +P15891 UniProtKB Sequence conflict 58 58 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15891 UniProtKB Sequence conflict 312 312 . . . Note=K->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15891 UniProtKB Helix 12 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ +P15891 UniProtKB Beta strand 32 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ +P15891 UniProtKB Beta strand 43 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ +P15891 UniProtKB Helix 52 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ +P15891 UniProtKB Beta strand 65 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ +P15891 UniProtKB Beta strand 80 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ +P15891 UniProtKB Helix 93 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ +P15891 UniProtKB Beta strand 115 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ +P15891 UniProtKB Helix 123 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ +P15891 UniProtKB Helix 128 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HQZ +P15891 UniProtKB Beta strand 537 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JO8 +P15891 UniProtKB Beta strand 546 550 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RPN +P15891 UniProtKB Beta strand 558 563 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JO8 +P15891 UniProtKB Beta strand 566 574 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JO8 +P15891 UniProtKB Turn 575 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JO8 +P15891 UniProtKB Beta strand 580 584 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JO8 +P15891 UniProtKB Helix 585 587 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JO8 +P15891 UniProtKB Beta strand 588 590 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JO8 +##sequence-region P39970 1 489 +P39970 UniProtKB Chain 1 489 . . . ID=PRO_0000076537;Note=ATF/CREB activator 1 +P39970 UniProtKB Domain 384 447 . . . Note=bZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P39970 UniProtKB Region 386 406 . . . Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P39970 UniProtKB Region 412 419 . . . Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P39970 UniProtKB Compositional bias 258 267 . . . Note=Poly-Ser +##sequence-region P32316 1 526 +P32316 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1970569;Dbxref=PMID:1970569 +P32316 UniProtKB Chain 2 526 . . . ID=PRO_0000215524;Note=Acetyl-CoA hydrolase +P32316 UniProtKB Region 277 281 . . . Note=Coenzyme A binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:B3EY95 +P32316 UniProtKB Active site 302 302 . . . Note=5-glutamyl coenzyme A thioester intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:B3EY95 +P32316 UniProtKB Binding site 392 392 . . . Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:B3EY95 +P32316 UniProtKB Binding site 396 396 . . . Note=Coenzyme A%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:B3EY95 +P32316 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1970569;Dbxref=PMID:1970569 +P32316 UniProtKB Modified residue 350 350 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P32316 UniProtKB Sequence conflict 308 308 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32316 UniProtKB Sequence conflict 320 320 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32316 UniProtKB Sequence conflict 363 364 . . . Note=LG->FP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q01574 1 713 +Q01574 UniProtKB Chain 1 713 . . . ID=PRO_0000208420;Note=Acetyl-coenzyme A synthetase 1 +Q01574 UniProtKB Nucleotide binding 443 445 . . . Note=ATP +Q01574 UniProtKB Nucleotide binding 467 472 . . . Note=ATP +Q01574 UniProtKB Region 248 251 . . . Note=Coenzyme A binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01574 UniProtKB Motif 711 713 . . . Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01574 UniProtKB Binding site 367 367 . . . Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01574 UniProtKB Binding site 559 559 . . . Note=ATP +Q01574 UniProtKB Binding site 574 574 . . . Note=ATP +Q01574 UniProtKB Binding site 582 582 . . . Note=Coenzyme A%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01574 UniProtKB Binding site 585 585 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01574 UniProtKB Binding site 650 650 . . . Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01574 UniProtKB Sequence conflict 34 34 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01574 UniProtKB Sequence conflict 328 328 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01574 UniProtKB Helix 75 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 87 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 133 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 139 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 148 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 162 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 166 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 191 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 200 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 215 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 225 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 238 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 255 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 271 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 287 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 293 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 316 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 323 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 328 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 335 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 356 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 366 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 374 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 381 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 397 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 408 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 414 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 427 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 438 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 448 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 461 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 465 467 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Turn 472 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 478 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Turn 483 485 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 503 506 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 508 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 520 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 540 547 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 549 551 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 554 563 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 569 571 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 581 583 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 588 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 601 607 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 619 624 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 641 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Turn 655 657 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Beta strand 660 664 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 678 683 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Helix 702 709 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +Q01574 UniProtKB Turn 710 712 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RY2 +##sequence-region Q00362 1 526 +Q00362 UniProtKB Chain 1 526 . . . ID=PRO_0000071442;Note=Protein phosphatase PP2A regulatory subunit B +Q00362 UniProtKB Repeat 23 62 . . . Note=WD 1 +Q00362 UniProtKB Repeat 82 123 . . . Note=WD 2 +Q00362 UniProtKB Repeat 182 220 . . . Note=WD 3 +Q00362 UniProtKB Repeat 231 271 . . . Note=WD 4 +Q00362 UniProtKB Repeat 290 328 . . . Note=WD 5 +Q00362 UniProtKB Repeat 345 386 . . . Note=WD 6 +Q00362 UniProtKB Repeat 495 525 . . . Note=WD 7 +Q00362 UniProtKB Compositional bias 416 419 . . . Note=Poly-Ser +Q00362 UniProtKB Modified residue 124 124 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q00362 UniProtKB Sequence conflict 500 500 . . . Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47096 1 177 +P47096 UniProtKB Chain 1 177 . . . ID=PRO_0000064375;Note=3-hydroxyanthranilate 3%2C4-dioxygenase +P47096 UniProtKB Metal binding 49 49 . . . Note=Iron%3B catalytic +P47096 UniProtKB Metal binding 55 55 . . . Note=Iron%3B catalytic +P47096 UniProtKB Metal binding 97 97 . . . Note=Iron%3B catalytic +P47096 UniProtKB Metal binding 126 126 . . . Note=Divalent metal cation +P47096 UniProtKB Metal binding 129 129 . . . Note=Divalent metal cation +P47096 UniProtKB Metal binding 163 163 . . . Note=Divalent metal cation +P47096 UniProtKB Metal binding 166 166 . . . Note=Divalent metal cation +P47096 UniProtKB Binding site 45 45 . . . Note=Dioxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03019 +P47096 UniProtKB Binding site 55 55 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03019 +P47096 UniProtKB Binding site 101 101 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03019 +P47096 UniProtKB Binding site 111 111 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03019 +P47096 UniProtKB Modified residue 176 176 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P47096 UniProtKB Helix 9 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Helix 17 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Beta strand 21 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Beta strand 26 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Beta strand 32 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Beta strand 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Beta strand 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Beta strand 55 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Beta strand 64 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Beta strand 72 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Beta strand 77 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Beta strand 87 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Beta strand 97 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Beta strand 106 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Beta strand 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Beta strand 121 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Turn 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Beta strand 132 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Beta strand 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Helix 145 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Helix 158 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +P47096 UniProtKB Turn 164 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZVF +##sequence-region P42884 1 376 +P42884 UniProtKB Chain 1 376 . . . ID=PRO_0000070369;Note=Putative aryl-alcohol dehydrogenase AAD14 +P42884 UniProtKB Nucleotide binding 236 246 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42884 UniProtKB Active site 76 76 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42884 UniProtKB Binding site 151 151 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42884 UniProtKB Site 103 103 . . . Note=Lowers pKa of active site Tyr;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P32357 1 355 +P32357 UniProtKB Chain 1 355 . . . ID=PRO_0000209705;Note=A1 cistron-splicing factor AAR2 +P32357 UniProtKB Region 261 282 . . . Note=Leucine-zipper +P32357 UniProtKB Compositional bias 332 341 . . . Note=Asp/Glu-rich (acidic) +P32357 UniProtKB Modified residue 253 253 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21764848;Dbxref=PMID:21764848 +P32357 UniProtKB Modified residue 274 274 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21764848;Dbxref=PMID:21764848 +P32357 UniProtKB Modified residue 328 328 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21764848;Dbxref=PMID:21764848 +P32357 UniProtKB Modified residue 331 331 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21764848;Dbxref=PMID:21764848 +P32357 UniProtKB Modified residue 345 345 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21764848;Dbxref=PMID:21764848 +P32357 UniProtKB Mutagenesis 253 253 . . . Note=No effect on interaction with PRP8. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21764848;Dbxref=PMID:21764848 +P32357 UniProtKB Mutagenesis 253 253 . . . Note=Disrupts interaction with PRP8. S->D%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21764848;Dbxref=PMID:21764848 +P32357 UniProtKB Beta strand 2 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Beta strand 13 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Beta strand 20 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Beta strand 32 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Beta strand 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBS +P32357 UniProtKB Beta strand 42 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Beta strand 51 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Helix 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Beta strand 66 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Turn 73 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Beta strand 77 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Helix 86 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Beta strand 102 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Helix 113 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Helix 123 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Beta strand 136 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Turn 147 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Beta strand 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ILI +P32357 UniProtKB Helix 172 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Beta strand 183 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ILH +P32357 UniProtKB Turn 186 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Helix 194 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Helix 202 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Helix 207 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Helix 217 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Helix 237 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Helix 258 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Helix 277 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Helix 280 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Helix 286 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Turn 297 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Helix 303 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Helix 314 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P32357 UniProtKB Beta strand 345 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +##sequence-region P47146 1 123 +P47146 UniProtKB Chain 1 123 . . . ID=PRO_0000203111;Note=Aberrant microtubules protein 1 +##sequence-region Q12031 1 575 +Q12031 UniProtKB Chain 1 575 . . . ID=PRO_0000068800;Note=Mitochondrial 2-methylisocitrate lyase +Q12031 UniProtKB Active site 238 238 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P07248 1 1323 +P07248 UniProtKB Chain 1 1323 . . . ID=PRO_0000046801;Note=Regulatory protein ADR1 +P07248 UniProtKB Zinc finger 104 126 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P07248 UniProtKB Zinc finger 132 155 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P07248 UniProtKB Modified residue 54 54 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07248 UniProtKB Modified residue 188 188 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07248 UniProtKB Modified residue 193 193 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07248 UniProtKB Modified residue 230 230 . . . Note=Phosphoserine%3B by PKA%3B in vitro;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:1549108;Dbxref=PMID:17287358,PMID:19779198,PMID:1549108 +P07248 UniProtKB Modified residue 258 258 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07248 UniProtKB Modified residue 259 259 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07248 UniProtKB Modified residue 299 299 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07248 UniProtKB Modified residue 323 323 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P07248 UniProtKB Modified residue 325 325 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07248 UniProtKB Modified residue 327 327 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P07248 UniProtKB Mutagenesis 106 106 . . . Note=Suppresses activity. C->Y +P07248 UniProtKB Mutagenesis 109 109 . . . Note=Suppresses activity. C->Y +P07248 UniProtKB Mutagenesis 114 114 . . . Note=Lowers activity. A->V +P07248 UniProtKB Mutagenesis 118 118 . . . Note=Suppresses activity. H->Y +P07248 UniProtKB Mutagenesis 122 122 . . . Note=Suppresses activity. H->Y +P07248 UniProtKB Mutagenesis 134 134 . . . Note=Suppresses activity. C->Y +P07248 UniProtKB Mutagenesis 142 142 . . . Note=Lowers activity. T->I +P07248 UniProtKB Sequence conflict 1216 1216 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07248 UniProtKB Beta strand 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ARF +P07248 UniProtKB Turn 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ARD +P07248 UniProtKB Beta strand 111 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ARF +P07248 UniProtKB Helix 116 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ARD +P07248 UniProtKB Beta strand 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ADR +P07248 UniProtKB Turn 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAA +P07248 UniProtKB Beta strand 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAA +P07248 UniProtKB Helix 145 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAA +P07248 UniProtKB Turn 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ADR +##sequence-region P39925 1 761 +P39925 UniProtKB Chain 1 761 . . . ID=PRO_0000084670;Note=Mitochondrial respiratory chain complexes assembly protein AFG3 +P39925 UniProtKB Transmembrane 116 136 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39925 UniProtKB Transmembrane 224 244 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39925 UniProtKB Nucleotide binding 328 335 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39925 UniProtKB Active site 559 559 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39925 UniProtKB Metal binding 558 558 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39925 UniProtKB Metal binding 562 562 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39925 UniProtKB Metal binding 634 634 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39925 UniProtKB Mutagenesis 559 559 . . . Note=Abolishes proteolytic activity%3B impairs synthesis of respiratory chain proteins COB and COX1. No effect on m-AAA protease assembly. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9707443;Dbxref=PMID:9707443 +P39925 UniProtKB Sequence conflict 411 411 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38903 1 757 +P38903 UniProtKB Chain 1 757 . . . ID=PRO_0000071471;Note=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform +P38903 UniProtKB Compositional bias 16 22 . . . Note=Poly-Ser +P38903 UniProtKB Compositional bias 46 51 . . . Note=Poly-Ser +P38903 UniProtKB Compositional bias 98 110 . . . Note=Poly-Ser +P38903 UniProtKB Compositional bias 143 147 . . . Note=Poly-Ser +P38903 UniProtKB Compositional bias 202 213 . . . Note=Poly-Asn +P38903 UniProtKB Modified residue 242 242 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38903 UniProtKB Modified residue 257 257 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38903 UniProtKB Sequence conflict 95 95 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38903 UniProtKB Sequence conflict 529 529 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38903 UniProtKB Sequence conflict 581 581 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47129 1 309 +P47129 UniProtKB Chain 1 309 . . . ID=PRO_0000203104;Note=Assembly-complementing factor 4 +P47129 UniProtKB Modified residue 44 44 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P47129 UniProtKB Modified residue 71 71 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P47129 UniProtKB Modified residue 74 74 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P47129 UniProtKB Modified residue 78 78 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P47129 UniProtKB Modified residue 165 165 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P47129 UniProtKB Modified residue 288 288 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P14164 1 731 +P14164 UniProtKB Chain 1 731 . . . ID=PRO_0000064807;Note=ARS-binding factor 1 +P14164 UniProtKB Region 624 628 . . . Note=C-terminal sequence 1 +P14164 UniProtKB Region 639 662 . . . Note=C-terminal sequence 2 +P14164 UniProtKB Compositional bias 94 294 . . . Note=Asn-rich +P14164 UniProtKB Compositional bias 449 510 . . . Note=Asn-rich +P14164 UniProtKB Modified residue 189 189 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14164 UniProtKB Modified residue 193 193 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14164 UniProtKB Modified residue 467 467 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P14164 UniProtKB Modified residue 554 554 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14164 UniProtKB Modified residue 618 618 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14164 UniProtKB Modified residue 624 624 . . . Note=Phosphoserine%3B by PKC;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14164 UniProtKB Modified residue 720 720 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:7608180;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:7608180 +P14164 UniProtKB Cross-link 18 18 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P14164 UniProtKB Mutagenesis 57 57 . . . Note=Loss of DNA binding. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2686983;Dbxref=PMID:2686983 +P14164 UniProtKB Mutagenesis 71 71 . . . Note=Loss of DNA binding. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2686983;Dbxref=PMID:2686983 +P14164 UniProtKB Mutagenesis 625 625 . . . Note=Leads to mislocalization into the cytoplasm. K->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15522095;Dbxref=PMID:15522095 +P14164 UniProtKB Mutagenesis 720 720 . . . Note=Strongly reduces phosphorylation by CK2. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7608180;Dbxref=PMID:7608180 +P14164 UniProtKB Sequence conflict 125 125 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14164 UniProtKB Sequence conflict 128 128 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14164 UniProtKB Sequence conflict 128 128 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14164 UniProtKB Sequence conflict 128 128 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14164 UniProtKB Sequence conflict 148 148 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14164 UniProtKB Sequence conflict 148 148 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14164 UniProtKB Sequence conflict 148 148 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14164 UniProtKB Sequence conflict 279 280 . . . Note=NT->TN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14164 UniProtKB Sequence conflict 279 280 . . . Note=NT->TN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14164 UniProtKB Sequence conflict 279 280 . . . Note=NT->TN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14164 UniProtKB Sequence conflict 690 690 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14164 UniProtKB Sequence conflict 690 690 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14164 UniProtKB Sequence conflict 690 690 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40535 1 587 +P40535 UniProtKB Chain 1 587 . . . ID=PRO_0000076530;Note=ATF/CREB activator 2 +P40535 UniProtKB Domain 425 488 . . . Note=bZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P40535 UniProtKB Region 427 447 . . . Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P40535 UniProtKB Region 453 467 . . . Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P40535 UniProtKB Modified residue 171 171 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40535 UniProtKB Modified residue 179 179 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40535 UniProtKB Modified residue 399 399 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P40535 UniProtKB Modified residue 557 557 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40535 UniProtKB Modified residue 559 559 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P31787 1 87 +P31787 UniProtKB Chain 1 87 . . . ID=PRO_0000214013;Note=Acyl-CoA-binding protein +P31787 UniProtKB Domain 2 87 . . . Note=ACB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00573 +P31787 UniProtKB Region 29 33 . . . Note=Acyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P31787 UniProtKB Binding site 51 51 . . . Note=Acyl-CoA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P31787 UniProtKB Binding site 55 55 . . . Note=Acyl-CoA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P31787 UniProtKB Binding site 74 74 . . . Note=Acyl-CoA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P31787 UniProtKB Cross-link 51 51 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P31787 UniProtKB Cross-link 72 72 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P31787 UniProtKB Helix 3 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ST7 +P31787 UniProtKB Helix 22 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ST7 +P31787 UniProtKB Helix 50 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ST7 +P31787 UniProtKB Turn 61 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ST7 +P31787 UniProtKB Helix 66 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ST7 +##sequence-region P53930 1 226 +P53930 UniProtKB Chain 1 226 . . . ID=PRO_0000215934;Note=Protein AF-9 homolog +P53930 UniProtKB Domain 15 123 . . . Note=YEATS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00376 +P53930 UniProtKB Coiled coil 187 224 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53930 UniProtKB Sequence conflict 65 65 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53930 UniProtKB Beta strand 8 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FK3 +P53930 UniProtKB Beta strand 14 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS +P53930 UniProtKB Beta strand 41 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS +P53930 UniProtKB Helix 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS +P53930 UniProtKB Turn 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS +P53930 UniProtKB Beta strand 59 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS +P53930 UniProtKB Beta strand 70 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS +P53930 UniProtKB Beta strand 74 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS +P53930 UniProtKB Beta strand 79 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS +P53930 UniProtKB Beta strand 93 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS +P53930 UniProtKB Helix 102 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS +P53930 UniProtKB Beta strand 109 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS +P53930 UniProtKB Beta strand 145 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS +P53930 UniProtKB Helix 160 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RLS +##sequence-region P32317 1 509 +P32317 UniProtKB Chain 1 509 . . . ID=PRO_0000064477;Note=Protein AFG1 +P32317 UniProtKB Nucleotide binding 126 133 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32317 UniProtKB Sequence conflict 210 210 . . . Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32317 UniProtKB Sequence conflict 210 210 . . . Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32317 UniProtKB Sequence conflict 373 373 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32317 UniProtKB Sequence conflict 373 373 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32317 UniProtKB Sequence conflict 399 399 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32323 1 725 +P32323 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32323 UniProtKB Chain 25 699 . . . ID=PRO_0000020641;Note=A-agglutinin anchorage subunit +P32323 UniProtKB Propeptide 700 725 . . . ID=PRO_0000296627;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32323 UniProtKB Repeat 53 149 . . . Note=1-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 182 188 . . . Note=2-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 189 195 . . . Note=2-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 196 202 . . . Note=2-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 203 209 . . . Note=2-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 210 216 . . . Note=2-5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 217 223 . . . Note=2-6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 224 230 . . . Note=2-7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 231 237 . . . Note=2-8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 238 244 . . . Note=2-9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 245 251 . . . Note=2-10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 252 258 . . . Note=2-11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 259 265 . . . Note=2-12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 266 272 . . . Note=2-13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 273 279 . . . Note=2-14;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 280 286 . . . Note=2-15;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 287 293 . . . Note=2-16;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 294 300 . . . Note=2-17;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 301 307 . . . Note=2-18;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Repeat 395 493 . . . Note=1-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32323 UniProtKB Region 53 493 . . . Note=2 X approximate repeats +P32323 UniProtKB Region 182 307 . . . Note=18 X approximate tandem repeats%2C Ser/Thr-rich +P32323 UniProtKB Lipidation 699 699 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32323 UniProtKB Disulfide bond 133 133 . . . Note=Interchain (with AGA2);Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11278672;Dbxref=PMID:11278672 +P32323 UniProtKB Disulfide bond 136 136 . . . Note=Interchain (with AGA2);Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11278672;Dbxref=PMID:11278672 +##sequence-region Q12482 1 902 +Q12482 UniProtKB Chain 1 902 . . . ID=PRO_0000227601;Note=Mitochondrial aspartate-glutamate transporter AGC1 +Q12482 UniProtKB Transmembrane 534 554 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12482 UniProtKB Transmembrane 591 611 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12482 UniProtKB Transmembrane 622 642 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12482 UniProtKB Transmembrane 681 702 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12482 UniProtKB Transmembrane 731 751 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12482 UniProtKB Transmembrane 786 806 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12482 UniProtKB Repeat 528 614 . . . Note=Solcar 1 +Q12482 UniProtKB Repeat 622 710 . . . Note=Solcar 2 +Q12482 UniProtKB Repeat 725 813 . . . Note=Solcar 3 +##sequence-region Q04412 1 482 +Q04412 UniProtKB Chain 1 482 . . . ID=PRO_0000074222;Note=ADP-ribosylation factor GTPase-activating protein effector protein 1 +Q04412 UniProtKB Domain 170 297 . . . Note=Arf-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288 +Q04412 UniProtKB Zinc finger 186 210 . . . Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288 +##sequence-region P38090 1 596 +P38090 UniProtKB Chain 1 596 . . . ID=PRO_0000054143;Note=General amino acid permease AGP2 +P38090 UniProtKB Topological domain 1 94 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Transmembrane 95 115 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Topological domain 116 117 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Transmembrane 118 138 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Topological domain 139 165 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Transmembrane 166 186 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Topological domain 187 199 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Transmembrane 200 220 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Topological domain 221 227 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Transmembrane 228 248 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Topological domain 249 288 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Transmembrane 289 309 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Topological domain 310 326 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Transmembrane 327 347 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Topological domain 348 379 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Transmembrane 380 400 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Topological domain 401 427 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Transmembrane 428 448 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Topological domain 449 459 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Transmembrane 460 480 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Topological domain 481 505 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Transmembrane 506 526 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Topological domain 527 534 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Transmembrane 535 555 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38090 UniProtKB Topological domain 556 596 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P03876 1 854 +P03876 UniProtKB Chain 1 854 . . . ID=PRO_0000196881;Note=Putative COX1/OXI3 intron 2 protein +P03876 UniProtKB Domain 329 613 . . . Note=Reverse transcriptase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405 +P03876 UniProtKB Sequence conflict 236 236 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03876 UniProtKB Sequence conflict 724 724 . . . Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12471 1 397 +Q12471 UniProtKB Chain 1 397 . . . ID=PRO_0000179977;Note=6-phosphofructo-2-kinase 2 +Q12471 UniProtKB Nucleotide binding 103 110 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12471 UniProtKB Region 85 305 . . . Note=6-phosphofructo-2-kinase +Q12471 UniProtKB Active site 197 197 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12471 UniProtKB Active site 235 235 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12471 UniProtKB Binding site 269 269 . . . Note=Fructose-6-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12471 UniProtKB Cross-link 55 55 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P53319 1 492 +P53319 UniProtKB Chain 1 492 . . . ID=PRO_0000090076;Note=6-phosphogluconate dehydrogenase%2C decarboxylating 2 +P53319 UniProtKB Nucleotide binding 12 17 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53319 UniProtKB Nucleotide binding 35 37 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53319 UniProtKB Nucleotide binding 77 79 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53319 UniProtKB Region 131 133 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53319 UniProtKB Region 188 189 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53319 UniProtKB Active site 185 185 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53319 UniProtKB Active site 192 192 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53319 UniProtKB Binding site 105 105 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53319 UniProtKB Binding site 105 105 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53319 UniProtKB Binding site 193 193 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53319 UniProtKB Binding site 262 262 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53319 UniProtKB Binding site 289 289 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53319 UniProtKB Binding site 449 449 . . . Note=Substrate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53319 UniProtKB Binding site 455 455 . . . Note=Substrate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P23542 1 418 +P23542 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:1859361,ECO:0000269|PubMed:2199266;Dbxref=PMID:22814378,PMID:1859361,PMID:2199266 +P23542 UniProtKB Chain 2 418 . . . ID=PRO_0000123875;Note=Aspartate aminotransferase%2C cytoplasmic +P23542 UniProtKB Binding site 38 38 . . . Note=Aspartate%3B via amide nitrogen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9655342;Dbxref=PMID:9655342 +P23542 UniProtKB Binding site 135 135 . . . Note=Aspartate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9655342;Dbxref=PMID:9655342 +P23542 UniProtKB Binding site 188 188 . . . Note=Aspartate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9655342;Dbxref=PMID:9655342 +P23542 UniProtKB Binding site 387 387 . . . Note=Aspartate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9655342;Dbxref=PMID:9655342 +P23542 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:1859361;Dbxref=PMID:22814378,PMID:1859361 +P23542 UniProtKB Modified residue 255 255 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9655342;Dbxref=PMID:9655342 +P23542 UniProtKB Modified residue 389 389 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P23542 UniProtKB Sequence conflict 95 95 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23542 UniProtKB Sequence conflict 95 95 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23542 UniProtKB Sequence conflict 413 414 . . . Note=TI->AT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23542 UniProtKB Sequence conflict 413 414 . . . Note=TI->AT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23542 UniProtKB Turn 3 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Helix 18 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Helix 51 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Helix 77 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Helix 93 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Beta strand 100 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Helix 107 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Beta strand 128 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Helix 138 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Turn 144 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Beta strand 149 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Turn 157 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Helix 164 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Beta strand 179 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Turn 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Helix 196 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Beta strand 212 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Turn 220 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Beta strand 223 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Helix 227 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Helix 232 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Turn 241 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Beta strand 247 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Turn 254 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Helix 260 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Beta strand 264 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Helix 277 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Turn 294 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Helix 301 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Helix 314 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Helix 353 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Beta strand 359 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Helix 368 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Beta strand 386 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Helix 390 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Turn 395 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +P23542 UniProtKB Helix 398 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAA +##sequence-region Q07622 1 623 +Q07622 UniProtKB Chain 1 623 . . . ID=PRO_0000242166;Note=Activator of C kinase protein 1 +Q07622 UniProtKB Repeat 318 361 . . . Note=Sel1-like 1 +Q07622 UniProtKB Repeat 408 444 . . . Note=Sel1-like 2 +Q07622 UniProtKB Repeat 495 531 . . . Note=Sel1-like 3 +Q07622 UniProtKB Repeat 576 611 . . . Note=Sel1-like 4 +Q07622 UniProtKB Compositional bias 68 76 . . . Note=Poly-Ser +Q07622 UniProtKB Cross-link 184 184 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q07622 UniProtKB Cross-link 191 191 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q03771 1 387 +Q03771 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q03771 UniProtKB Chain 2 387 . . . ID=PRO_0000253808;Note=Assembly chaperone of RPL4 +Q03771 UniProtKB Repeat 42 75 . . . Note=TPR 1 +Q03771 UniProtKB Repeat 163 196 . . . Note=TPR 2 +Q03771 UniProtKB Repeat 224 257 . . . Note=TPR 3 +Q03771 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region Q07747 1 329 +Q07747 UniProtKB Chain 1 329 . . . ID=PRO_0000070366;Note=Probable aryl-alcohol dehydrogenase AAD4 +Q07747 UniProtKB Nucleotide binding 190 200 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07747 UniProtKB Active site 30 30 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07747 UniProtKB Binding site 105 105 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07747 UniProtKB Site 57 57 . . . Note=Lowers pKa of active site Tyr;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P08521 1 25 +P08521 UniProtKB Peptide 1 25 . . . ID=PRO_0000043974;Note=Arginine attenuator peptide +P08521 UniProtKB Mutagenesis 13 13 . . . Note=Eliminates arginine-specific stalling of ribosomes at the termination codon. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3555844;Dbxref=PMID:3555844 +##sequence-region P21192 1 770 +P21192 UniProtKB Chain 1 770 . . . ID=PRO_0000046800;Note=Metallothionein expression activator +P21192 UniProtKB Zinc finger 603 627 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P21192 UniProtKB Zinc finger 633 657 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P21192 UniProtKB Zinc finger 662 685 . . . Note=C2H2-type 3%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P21192 UniProtKB Modified residue 80 80 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198 +P21192 UniProtKB Modified residue 122 122 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P21192 UniProtKB Modified residue 247 247 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P21192 UniProtKB Modified residue 249 249 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P21192 UniProtKB Modified residue 253 253 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P21192 UniProtKB Modified residue 259 259 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P21192 UniProtKB Modified residue 385 385 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P21192 UniProtKB Modified residue 392 392 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P21192 UniProtKB Modified residue 483 483 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P21192 UniProtKB Modified residue 486 486 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P21192 UniProtKB Modified residue 501 501 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P21192 UniProtKB Modified residue 564 564 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P21192 UniProtKB Modified residue 709 709 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P21192 UniProtKB Modified residue 714 714 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P47182 1 288 +P47182 UniProtKB Chain 1 288 . . . ID=PRO_0000070368;Note=Putative aryl-alcohol dehydrogenase AAD10 +##sequence-region P25612 1 363 +P25612 UniProtKB Chain 1 363 . . . ID=PRO_0000070365;Note=Putative aryl-alcohol dehydrogenase AAD3 +##sequence-region P37898 1 856 +P37898 UniProtKB Chain 1 856 . . . ID=PRO_0000095105;Note=Alanine/arginine aminopeptidase +P37898 UniProtKB Region 264 268 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P37898 UniProtKB Active site 301 301 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P37898 UniProtKB Metal binding 300 300 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P37898 UniProtKB Metal binding 304 304 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P37898 UniProtKB Metal binding 323 323 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P37898 UniProtKB Binding site 132 132 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P37898 UniProtKB Site 386 386 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P37898 UniProtKB Sequence conflict 550 569 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37898 UniProtKB Sequence conflict 646 646 . . . Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P28240 1 557 +P28240 UniProtKB Chain 1 557 . . . ID=PRO_0000068799;Note=Isocitrate lyase +P28240 UniProtKB Region 106 108 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WKK7 +P28240 UniProtKB Region 218 219 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WKK7 +P28240 UniProtKB Region 437 441 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WKK7 +P28240 UniProtKB Active site 217 217 . . . Note=Proton acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28240 UniProtKB Metal binding 179 179 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WKK7 +P28240 UniProtKB Binding site 254 254 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WKK7 +P28240 UniProtKB Binding site 471 471 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WKK7 +P28240 UniProtKB Modified residue 53 53 . . . Note=Phosphothreonine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28240 UniProtKB Mutagenesis 53 53 . . . Note=Abolishes short-term enzyme inactivation by glucose addition. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8641464;Dbxref=PMID:8641464 +P28240 UniProtKB Mutagenesis 216 216 . . . Note=Reduces activity by 45%25%3B when associated with L-220. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8923733;Dbxref=PMID:8923733 +P28240 UniProtKB Mutagenesis 220 220 . . . Note=Reduces activity by 45%25%3B when associated with R-216. M->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8923733;Dbxref=PMID:8923733 +##sequence-region P38720 1 489 +P38720 UniProtKB Chain 1 489 . . . ID=PRO_0000090075;Note=6-phosphogluconate dehydrogenase%2C decarboxylating 1 +P38720 UniProtKB Nucleotide binding 9 14 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38720 UniProtKB Nucleotide binding 32 34 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38720 UniProtKB Nucleotide binding 74 76 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38720 UniProtKB Region 128 130 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38720 UniProtKB Region 185 186 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38720 UniProtKB Active site 182 182 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38720 UniProtKB Active site 189 189 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38720 UniProtKB Binding site 102 102 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38720 UniProtKB Binding site 102 102 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38720 UniProtKB Binding site 190 190 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38720 UniProtKB Binding site 259 259 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38720 UniProtKB Binding site 286 286 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38720 UniProtKB Binding site 446 446 . . . Note=Substrate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38720 UniProtKB Binding site 452 452 . . . Note=Substrate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38720 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38720 UniProtKB Beta strand 4 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 12 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Beta strand 28 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Beta strand 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 36 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Turn 44 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Beta strand 49 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 57 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Beta strand 69 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 78 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Beta strand 96 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 105 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Beta strand 121 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 130 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Beta strand 139 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 149 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Beta strand 166 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 177 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 211 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Turn 223 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 229 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Beta strand 245 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 248 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 261 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 277 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 292 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 315 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 354 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Beta strand 363 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 370 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 388 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 392 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 420 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 439 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Helix 458 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +P38720 UniProtKB Beta strand 463 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P4Q +##sequence-region Q02895 1 342 +Q02895 UniProtKB Chain 1 342 . . . ID=PRO_0000238634;Note=Putative aryl-alcohol dehydrogenase AAD16 +##sequence-region Q01802 1 451 +Q01802 UniProtKB Binding site 52 52 . . . Note=Aspartate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01802 UniProtKB Binding site 155 155 . . . Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01802 UniProtKB Binding site 216 216 . . . Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01802 UniProtKB Binding site 423 423 . . . Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01802 UniProtKB Modified residue 286 286 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01802 UniProtKB Sequence conflict 41 41 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01802 UniProtKB Sequence conflict 414 414 . . . Note=Y->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08641 1 628 +Q08641 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9467951;Dbxref=PMID:9467951 +Q08641 UniProtKB Chain 2 628 . . . ID=PRO_0000204458;Note=tRNA(Thr) (cytosine(32)-N(3))-methyltransferase +Q08641 UniProtKB Modified residue 93 93 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q08641 UniProtKB Modified residue 150 150 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q08641 UniProtKB Modified residue 321 321 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q08641 UniProtKB Modified residue 326 326 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q08641 UniProtKB Modified residue 347 347 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P47177 1 404 +P47177 UniProtKB Chain 1 404 . . . ID=PRO_0000203128;Note=Putative nitronate monooxygenase +P47177 UniProtKB Nucleotide binding 41 43 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47177 UniProtKB Nucleotide binding 270 272 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47177 UniProtKB Nucleotide binding 293 294 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47177 UniProtKB Active site 224 224 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47177 UniProtKB Binding site 224 224 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47177 UniProtKB Sequence conflict 402 402 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40433 1 827 +P40433 UniProtKB Chain 1 827 . . . ID=PRO_0000179976;Note=6-phosphofructo-2-kinase 1 +P40433 UniProtKB Nucleotide binding 190 197 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40433 UniProtKB Active site 277 277 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40433 UniProtKB Active site 309 309 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40433 UniProtKB Active site 404 404 . . . Note=Phosphoserine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40433 UniProtKB Active site 497 497 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40433 UniProtKB Active site 565 565 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40433 UniProtKB Binding site 343 343 . . . Note=Fructose-6-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40433 UniProtKB Modified residue 92 92 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40433 UniProtKB Modified residue 157 157 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40433 UniProtKB Modified residue 644 644 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40433 UniProtKB Modified residue 652 652 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40433 UniProtKB Modified residue 659 659 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P40433 UniProtKB Modified residue 667 667 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40433 UniProtKB Sequence conflict 382 382 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40433 UniProtKB Sequence conflict 477 477 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P12904 1 322 +P12904 UniProtKB Chain 1 322 . . . ID=PRO_0000204389;Note=5'-AMP-activated protein kinase subunit gamma +P12904 UniProtKB Domain 37 97 . . . Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +P12904 UniProtKB Domain 118 181 . . . Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +P12904 UniProtKB Domain 194 253 . . . Note=CBS 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +P12904 UniProtKB Domain 262 322 . . . Note=CBS 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +P12904 UniProtKB Nucleotide binding 166 169 . . . Note=ADP 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q10343 +P12904 UniProtKB Nucleotide binding 221 222 . . . Note=AMP%2C ADP or ATP 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22019086;Dbxref=PMID:22019086 +P12904 UniProtKB Nucleotide binding 291 293 . . . Note=ADP 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q10343 +P12904 UniProtKB Nucleotide binding 309 312 . . . Note=AMP%2C ADP or ATP 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22019086;Dbxref=PMID:22019086 +P12904 UniProtKB Binding site 146 146 . . . Note=ADP 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q10343 +P12904 UniProtKB Binding site 195 195 . . . Note=AMP%2C ADP or ATP 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22019086;Dbxref=PMID:22019086 +P12904 UniProtKB Binding site 200 200 . . . Note=AMP%2C ADP or ATP 2%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22019086;Dbxref=PMID:22019086 +P12904 UniProtKB Mutagenesis 63 63 . . . Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. V->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591 +P12904 UniProtKB Mutagenesis 136 136 . . . Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591 +P12904 UniProtKB Mutagenesis 145 145 . . . Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591 +P12904 UniProtKB Mutagenesis 146 146 . . . Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. R->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591 +P12904 UniProtKB Mutagenesis 166 166 . . . Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. T->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591 +P12904 UniProtKB Mutagenesis 177 177 . . . Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. N->A%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591 +P12904 UniProtKB Mutagenesis 242 242 . . . Note=Decreases SNF1-activation efficiency%3B when associated with A-291 and E-293. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17223533;Dbxref=PMID:17223533 +P12904 UniProtKB Mutagenesis 251 251 . . . Note=Leads to resistance to 2-deoxyglucose. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591 +P12904 UniProtKB Mutagenesis 291 291 . . . Note=Decreases SNF1-activation efficiency%3B when associated with E-242 and E-293. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17223533;Dbxref=PMID:17223533 +P12904 UniProtKB Mutagenesis 293 293 . . . Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17223533,ECO:0000269|PubMed:18474591;Dbxref=PMID:17223533,PMID:18474591 +P12904 UniProtKB Mutagenesis 293 293 . . . Note=Decreases SNF1-activation efficiency%3B when associated with E-242 and A-291. H->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17223533,ECO:0000269|PubMed:18474591;Dbxref=PMID:17223533,PMID:18474591 +P12904 UniProtKB Helix 8 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P12904 UniProtKB Helix 31 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P12904 UniProtKB Beta strand 37 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P12904 UniProtKB Helix 50 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P12904 UniProtKB Beta strand 65 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P12904 UniProtKB Turn 70 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P12904 UniProtKB Beta strand 74 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P12904 UniProtKB Helix 81 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P12904 UniProtKB Helix 95 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P12904 UniProtKB Helix 106 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P12904 UniProtKB Helix 132 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P12904 UniProtKB Beta strand 145 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P12904 UniProtKB Turn 154 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P12904 UniProtKB Beta strand 159 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P12904 UniProtKB Helix 167 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P12904 UniProtKB Helix 179 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV +P12904 UniProtKB Helix 182 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC +P12904 UniProtKB Helix 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC +P12904 UniProtKB Helix 208 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC +P12904 UniProtKB Beta strand 221 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC +P12904 UniProtKB Beta strand 231 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC +P12904 UniProtKB Helix 238 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC +P12904 UniProtKB Helix 249 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P12904 UniProtKB Helix 257 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC +P12904 UniProtKB Beta strand 272 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P12904 UniProtKB Helix 280 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC +P12904 UniProtKB Beta strand 293 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC +P12904 UniProtKB Beta strand 302 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC +P12904 UniProtKB Helix 310 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NYC +##sequence-region Q02486 1 183 +Q02486 UniProtKB Transit peptide 1 26 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1881919;Dbxref=PMID:1881919 +Q02486 UniProtKB Chain 27 183 . . . ID=PRO_0000013477;Note=ARS-binding factor 2%2C mitochondrial +Q02486 UniProtKB DNA binding 43 111 . . . Note=HMG box 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267 +Q02486 UniProtKB DNA binding 116 183 . . . Note=HMG box 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267 +Q02486 UniProtKB Helix 30 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH0 +Q02486 UniProtKB Helix 49 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH0 +Q02486 UniProtKB Helix 70 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH0 +Q02486 UniProtKB Helix 86 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH0 +Q02486 UniProtKB Helix 122 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH0 +Q02486 UniProtKB Helix 143 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH0 +Q02486 UniProtKB Helix 159 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH0 +##sequence-region Q00955 1 2233 +Q00955 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +Q00955 UniProtKB Chain 2 2233 . . . ID=PRO_0000146770;Note=Acetyl-CoA carboxylase +Q00955 UniProtKB Domain 58 567 . . . Note=Biotin carboxylation +Q00955 UniProtKB Domain 216 408 . . . Note=ATP-grasp;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 +Q00955 UniProtKB Domain 694 768 . . . Note=Biotinyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066 +Q00955 UniProtKB Domain 1486 1822 . . . Note=CoA carboxyltransferase N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01136 +Q00955 UniProtKB Domain 1826 2141 . . . Note=CoA carboxyltransferase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01137 +Q00955 UniProtKB Nucleotide binding 256 261 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 +Q00955 UniProtKB Region 1486 2141 . . . Note=Carboxyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01138 +Q00955 UniProtKB Region 1627 1629 . . . Note=Acetyl-CoA binding +Q00955 UniProtKB Active site 383 383 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00955 UniProtKB Metal binding 365 365 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00955 UniProtKB Metal binding 379 379 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00955 UniProtKB Metal binding 379 379 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00955 UniProtKB Metal binding 381 381 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00955 UniProtKB Binding site 1731 1731 . . . Note=Coenzyme A +Q00955 UniProtKB Binding site 1998 1998 . . . Note=Acetyl-CoA%3B via amide nitrogen +Q00955 UniProtKB Binding site 2034 2034 . . . Note=Coenzyme A +Q00955 UniProtKB Binding site 2036 2036 . . . Note=Coenzyme A +Q00955 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +Q00955 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q00955 UniProtKB Modified residue 735 735 . . . Note=N6-biotinyllysine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250,ECO:0000255|PROSITE-ProRule:PRU01066 +Q00955 UniProtKB Modified residue 790 790 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00955 UniProtKB Modified residue 1148 1148 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198 +Q00955 UniProtKB Modified residue 1157 1157 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +Q00955 UniProtKB Modified residue 1162 1162 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00955 UniProtKB Mutagenesis 1705 1705 . . . Note=Raises KM for malonyl-CoA by a factor of 20. L->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12663926;Dbxref=PMID:12663926 +Q00955 UniProtKB Mutagenesis 1731 1731 . . . Note=Raises KM for malonyl-CoA by a factor of 15. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12663926;Dbxref=PMID:12663926 +Q00955 UniProtKB Mutagenesis 1738 1738 . . . Note=Does not affect catalytic activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12663926;Dbxref=PMID:12663926 +Q00955 UniProtKB Mutagenesis 1954 1954 . . . Note=Raises KM for malonyl-CoA by a factor of 70. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12663926;Dbxref=PMID:12663926 +Q00955 UniProtKB Mutagenesis 1994 1994 . . . Note=Does not affect catalytic activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12663926;Dbxref=PMID:12663926 +Q00955 UniProtKB Mutagenesis 2026 2026 . . . Note=Does not affect catalytic activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12663926;Dbxref=PMID:12663926 +Q00955 UniProtKB Mutagenesis 2036 2036 . . . Note=Affects only slightly binding of Co-A. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12663926;Dbxref=PMID:12663926 +Q00955 UniProtKB Sequence conflict 1523 1523 . . . Note=W->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00955 UniProtKB Sequence conflict 1755 1755 . . . Note=I->IWYRCL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00955 UniProtKB Sequence conflict 1761 1766 . . . Note=AINKML->ESTNA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00955 UniProtKB Helix 22 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 30 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Beta strand 35 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 45 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Beta strand 61 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 68 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Beta strand 91 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 100 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 108 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Beta strand 113 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 124 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Turn 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 131 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Beta strand 144 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Turn 152 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 158 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Beta strand 171 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 177 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 186 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Turn 204 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Turn 215 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 224 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 228 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 235 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Beta strand 247 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Turn 258 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Beta strand 262 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 268 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Beta strand 287 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Beta strand 297 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Turn 307 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W93 +Q00955 UniProtKB Beta strand 311 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Beta strand 326 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 339 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Beta strand 360 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Turn 370 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Beta strand 375 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 388 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 399 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 412 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 416 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 439 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Beta strand 452 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Beta strand 466 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W93 +Q00955 UniProtKB Beta strand 472 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Beta strand 484 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Beta strand 503 515 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 516 530 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Beta strand 531 536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSK +Q00955 UniProtKB Helix 541 547 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 550 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 561 565 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W96 +Q00955 UniProtKB Helix 577 605 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Helix 612 615 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Beta strand 618 624 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Beta strand 626 636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Beta strand 638 648 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Beta strand 650 657 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Beta strand 659 661 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Beta strand 663 669 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Beta strand 671 675 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Beta strand 682 687 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Beta strand 690 695 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Beta strand 702 704 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Beta strand 709 716 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Beta strand 727 733 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Beta strand 736 741 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Beta strand 746 750 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Beta strand 763 767 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Helix 772 774 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Beta strand 793 795 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I6E +Q00955 UniProtKB Helix 798 813 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0 +Q00955 UniProtKB Helix 818 833 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0 +Q00955 UniProtKB Helix 838 850 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0 +Q00955 UniProtKB Helix 851 853 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0 +Q00955 UniProtKB Helix 856 871 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0 +Q00955 UniProtKB Helix 878 889 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0 +Q00955 UniProtKB Turn 892 894 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0 +Q00955 UniProtKB Beta strand 896 898 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0 +Q00955 UniProtKB Helix 900 913 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0 +Q00955 UniProtKB Turn 914 916 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0 +Q00955 UniProtKB Helix 918 937 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0 +Q00955 UniProtKB Helix 938 940 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Beta strand 942 944 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSL +Q00955 UniProtKB Helix 947 957 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Helix 962 972 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0 +Q00955 UniProtKB Helix 975 995 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0 +Q00955 UniProtKB Helix 997 1002 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0 +Q00955 UniProtKB Helix 1004 1011 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0 +Q00955 UniProtKB Helix 1016 1018 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0 +Q00955 UniProtKB Helix 1019 1030 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CS0 +Q00955 UniProtKB Helix 1037 1052 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1054 1056 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Beta strand 1057 1059 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1062 1066 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSA +Q00955 UniProtKB Helix 1069 1076 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Helix 1083 1086 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Helix 1087 1090 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Turn 1095 1097 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Helix 1098 1109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Turn 1110 1112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1113 1122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1124 1134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Helix 1138 1140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I6E +Q00955 UniProtKB Beta strand 1155 1157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSL +Q00955 UniProtKB Helix 1158 1160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSL +Q00955 UniProtKB Beta strand 1167 1170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I6E +Q00955 UniProtKB Beta strand 1173 1178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Helix 1183 1185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Helix 1186 1194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1220 1225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Helix 1235 1255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1258 1265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1268 1270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1274 1279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Turn 1280 1283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Helix 1287 1289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Helix 1294 1300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Helix 1303 1305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1308 1313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1320 1327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1334 1342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1349 1351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Helix 1353 1372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1378 1380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I6E +Q00955 UniProtKB Beta strand 1382 1389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Helix 1397 1403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Turn 1404 1408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Helix 1409 1411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Helix 1412 1418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1420 1430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Turn 1432 1434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1437 1445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1447 1450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I6E +Q00955 UniProtKB Beta strand 1453 1461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1463 1465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1467 1474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Turn 1477 1480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TRC +Q00955 UniProtKB Beta strand 1482 1484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 1490 1493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 1495 1502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 1508 1510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 1511 1526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 1534 1536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1537 1544 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1546 1548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OD2 +Q00955 UniProtKB Beta strand 1550 1553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1561 1571 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1580 1587 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 1592 1594 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 1598 1614 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1618 1622 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Turn 1633 1638 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1640 1645 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 1649 1651 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1653 1658 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 1660 1668 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 1672 1674 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1675 1682 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1685 1693 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1696 1698 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 1702 1719 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1724 1728 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 1735 1742 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1745 1749 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1754 1757 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 1759 1766 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 1775 1778 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 1780 1783 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Turn 1784 1787 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1788 1795 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 1796 1807 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1812 1816 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSK +Q00955 UniProtKB Beta strand 1827 1829 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CTE +Q00955 UniProtKB Beta strand 1837 1839 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8X +Q00955 UniProtKB Helix 1843 1848 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1850 1852 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1855 1857 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1867 1870 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1877 1884 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1887 1894 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1899 1903 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1909 1911 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OD4 +Q00955 UniProtKB Beta strand 1915 1919 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 1926 1940 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Turn 1941 1943 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1947 1950 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1953 1956 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CTE +Q00955 UniProtKB Helix 1960 1964 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 1967 1979 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1985 1989 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 1994 1996 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8X +Q00955 UniProtKB Helix 1997 2000 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Turn 2001 2003 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 2005 2008 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Turn 2009 2011 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 2012 2017 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 2021 2025 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8X +Q00955 UniProtKB Helix 2027 2034 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 2039 2047 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 2049 2058 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 2059 2063 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CTB +Q00955 UniProtKB Helix 2065 2072 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 2078 2095 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 2100 2106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 2108 2113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 2115 2117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 2118 2139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Beta strand 2142 2144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 2148 2157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Helix 2168 2186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WZ8 +Q00955 UniProtKB Turn 2189 2191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TVU +Q00955 UniProtKB Turn 2196 2199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UYV +Q00955 UniProtKB Turn 2203 2205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UYR +Q00955 UniProtKB Helix 2206 2215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CTE +Q00955 UniProtKB Helix 2223 2233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CTE +##sequence-region P40529 1 298 +P40529 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40529 UniProtKB Chain 2 298 . . . ID=PRO_0000074228;Note=ADP-ribosylation factor GTPase-activating protein effector protein 2 +P40529 UniProtKB Domain 8 130 . . . Note=Arf-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288 +P40529 UniProtKB Zinc finger 23 47 . . . Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288 +P40529 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40529 UniProtKB Modified residue 180 180 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40529 UniProtKB Modified residue 183 183 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40529 UniProtKB Modified residue 207 207 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P52923 1 378 +P52923 UniProtKB Chain 1 378 . . . ID=PRO_0000203486;Note=Apoptosis-inducing factor 1 +P52923 UniProtKB Transmembrane 7 25 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52923 UniProtKB Nucleotide binding 12 16 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52923 UniProtKB Binding site 51 51 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52923 UniProtKB Binding site 56 56 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52923 UniProtKB Binding site 283 283 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P23180 1 465 +P23180 UniProtKB Transit peptide 1 16 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23180 UniProtKB Chain 17 465 . . . ID=PRO_0000207092;Note=Probable oxidoreductase AIM17 +P23180 UniProtKB Metal binding 246 246 . . . Note=Iron%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23180 UniProtKB Metal binding 248 248 . . . Note=Iron%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23180 UniProtKB Metal binding 428 428 . . . Note=Iron%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38884 1 321 +P38884 UniProtKB Transit peptide 1 72 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38884 UniProtKB Chain 73 321 . . . ID=PRO_0000202939;Note=Altered inheritance of mitochondria protein 18%2C mitochondrial +##sequence-region P40451 1 204 +P40451 UniProtKB Chain 1 204 . . . ID=PRO_0000202953;Note=Altered inheritance of mitochondria protein 20 +P40451 UniProtKB Transmembrane 6 26 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32858 1 118 +P32858 UniProtKB Chain 1 118 . . . ID=PRO_0000203183;Note=Altered inheritance of mitochondria protein 26%2C mitochondrial +P32858 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32858 UniProtKB Transmembrane 41 61 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32858 UniProtKB Transmembrane 98 118 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03673 1 198 +Q03673 UniProtKB Transit peptide 1 55 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03673 UniProtKB Chain 56 198 . . . ID=PRO_0000203268;Note=Altered inheritance of mitochondria protein 34%2C mitochondrial +Q03673 UniProtKB Transmembrane 172 187 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03673 UniProtKB Domain 69 103 . . . Note=SAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00186 +##sequence-region Q03798 1 255 +Q03798 UniProtKB Transit peptide 1 40 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03798 UniProtKB Chain 41 255 . . . ID=PRO_0000203312;Note=Altered inheritance of mitochondria protein 36%2C mitochondrial +Q03798 UniProtKB Transmembrane 64 82 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12032 1 185 +Q12032 UniProtKB Transit peptide 1 53 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12032 UniProtKB Chain 54 185 . . . ID=PRO_0000237666;Note=Altered inheritance of mitochondria protein 41%2C mitochondrial +##sequence-region P38305 1 123 +P38305 UniProtKB Chain 1 123 . . . ID=PRO_0000202507;Note=Altered inheritance of mitochondria protein 4 +##sequence-region P46680 1 615 +P46680 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P46680 UniProtKB Chain 2 615 . . . ID=PRO_0000050841;Note=Actin-interacting protein 1 +P46680 UniProtKB Repeat 2 45 . . . Note=WD 1;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914 +P46680 UniProtKB Repeat 46 94 . . . Note=WD 2;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914 +P46680 UniProtKB Repeat 95 146 . . . Note=WD 3;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914 +P46680 UniProtKB Repeat 147 189 . . . Note=WD 4;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914 +P46680 UniProtKB Repeat 190 235 . . . Note=WD 5;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914 +P46680 UniProtKB Repeat 236 280 . . . Note=WD 6;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914 +P46680 UniProtKB Repeat 281 325 . . . Note=WD 7;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914 +P46680 UniProtKB Repeat 326 363 . . . Note=WD 8;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914 +P46680 UniProtKB Repeat 364 399 . . . Note=WD 9;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914 +P46680 UniProtKB Repeat 400 433 . . . Note=WD 10;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914 +P46680 UniProtKB Repeat 434 473 . . . Note=WD 11;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914 +P46680 UniProtKB Repeat 474 516 . . . Note=WD 12;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914 +P46680 UniProtKB Repeat 517 569 . . . Note=WD 13;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914 +P46680 UniProtKB Repeat 570 611 . . . Note=WD 14;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00221,ECO:0000269|PubMed:12807914;Dbxref=PMID:12807914 +P46680 UniProtKB Compositional bias 363 366 . . . Note=Poly-Ser +P46680 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P46680 UniProtKB Beta strand 4 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Turn 28 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 32 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 40 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 55 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Turn 61 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 67 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 80 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 88 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Turn 99 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 103 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 119 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 128 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 141 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Turn 147 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 152 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 163 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 170 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 175 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Turn 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 184 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Turn 190 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 193 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 201 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 209 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 221 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 231 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Turn 236 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 241 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 256 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 274 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Turn 281 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 285 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Helix 297 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 301 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 311 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 321 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 328 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 342 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Turn 347 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 351 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 359 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Turn 362 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 366 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 375 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 387 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Turn 391 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 394 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 400 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 409 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 416 424 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 427 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Turn 434 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 439 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 449 454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 456 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Turn 464 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 469 473 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 476 482 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 491 496 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 500 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 512 516 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Turn 517 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 521 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 534 539 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 555 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 565 571 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 577 579 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 587 594 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 597 602 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +P46680 UniProtKB Beta strand 607 612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGU +##sequence-region P52893 1 592 +P52893 UniProtKB Modified residue 77 77 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P52893 UniProtKB Modified residue 412 412 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P47019 1 175 +P47019 UniProtKB Chain 1 175 . . . ID=PRO_0000203041;Note=Ribosome biogenesis protein ALB1 +##sequence-region P40047 1 520 +P40047 UniProtKB Transit peptide 1 23 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40047 UniProtKB Chain 24 520 . . . ID=PRO_0000007166;Note=Aldehyde dehydrogenase 5%2C mitochondrial +P40047 UniProtKB Nucleotide binding 266 271 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40047 UniProtKB Active site 288 288 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008 +P40047 UniProtKB Active site 322 322 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008 +P40047 UniProtKB Site 190 190 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40047 UniProtKB Sequence conflict 48 48 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40047 UniProtKB Sequence conflict 90 90 . . . Note=A->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40047 UniProtKB Sequence conflict 93 104 . . . Note=AFETKWSIVEPE->LLKRSVYCRAG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40047 UniProtKB Sequence conflict 411 411 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53178 1 202 +P53178 UniProtKB Chain 1 202 . . . ID=PRO_0000215605;Note=UDP-N-acetylglucosamine transferase subunit ALG13 +P53178 UniProtKB Beta strand 9 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +P53178 UniProtKB Beta strand 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KS6 +P53178 UniProtKB Helix 20 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +P53178 UniProtKB Helix 29 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +P53178 UniProtKB Turn 37 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +P53178 UniProtKB Beta strand 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +P53178 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +P53178 UniProtKB Helix 58 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +P53178 UniProtKB Beta strand 65 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KS6 +P53178 UniProtKB Turn 73 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KS6 +P53178 UniProtKB Beta strand 83 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +P53178 UniProtKB Turn 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +P53178 UniProtKB Beta strand 91 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +P53178 UniProtKB Beta strand 99 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +P53178 UniProtKB Helix 103 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +P53178 UniProtKB Beta strand 114 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +P53178 UniProtKB Helix 120 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +P53178 UniProtKB Beta strand 133 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KS6 +P53178 UniProtKB Helix 145 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +P53178 UniProtKB Beta strand 157 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KS6 +P53178 UniProtKB Turn 166 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +P53178 UniProtKB Helix 169 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +P53178 UniProtKB Beta strand 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +P53178 UniProtKB Helix 192 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JZC +##sequence-region P38179 1 458 +P38179 UniProtKB Chain 1 458 . . . ID=PRO_0000080565;Note=Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1%2C3-mannosyltransferase +P38179 UniProtKB Topological domain 1 41 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Topological domain 63 95 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Transmembrane 96 116 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Topological domain 117 137 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Transmembrane 138 158 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Topological domain 159 171 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Transmembrane 172 192 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Topological domain 193 216 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Transmembrane 217 237 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Topological domain 238 242 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Transmembrane 243 263 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Topological domain 264 302 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Transmembrane 303 323 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Topological domain 324 345 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Transmembrane 346 366 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Topological domain 367 381 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Transmembrane 382 402 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Topological domain 403 415 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Transmembrane 416 436 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Topological domain 437 458 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38179 UniProtKB Mutagenesis 275 275 . . . Note=In ALG3-1%3B leads to an underglycosylation of secretory proteins. A->V +P38179 UniProtKB Sequence conflict 86 86 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38179 UniProtKB Sequence conflict 187 198 . . . Note=LGAIVASRCHQR->FRGYRGQQVPSA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38179 UniProtKB Sequence conflict 266 266 . . . Note=S->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06497 1 328 +Q06497 UniProtKB Chain 1 328 . . . ID=PRO_0000227603;Note=Peroxisomal adenine nucleotide transporter 1 +Q06497 UniProtKB Transmembrane 1 21 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06497 UniProtKB Transmembrane 78 98 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06497 UniProtKB Transmembrane 128 148 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06497 UniProtKB Transmembrane 185 202 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06497 UniProtKB Transmembrane 226 246 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06497 UniProtKB Transmembrane 277 297 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06497 UniProtKB Repeat 1 101 . . . Note=Solcar 1 +Q06497 UniProtKB Repeat 122 208 . . . Note=Solcar 2 +Q06497 UniProtKB Repeat 220 304 . . . Note=Solcar 3 +##sequence-region P38856 1 637 +P38856 UniProtKB Chain 1 637 . . . ID=PRO_0000202930;Note=Clathrin coat assembly protein AP180A +P38856 UniProtKB Domain 1 126 . . . Note=ENTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243 +P38856 UniProtKB Region 587 637 . . . Note=Clathrin-binding +P38856 UniProtKB Compositional bias 560 579 . . . Note=Poly-Gln +##sequence-region Q12028 1 832 +Q12028 UniProtKB Chain 1 832 . . . ID=PRO_0000193764;Note=AP-1 complex subunit gamma-1 +Q12028 UniProtKB Domain 733 832 . . . Note=GAE +##sequence-region P38065 1 1025 +P38065 UniProtKB Chain 1 1025 . . . ID=PRO_0000193737;Note=AP-2 complex subunit alpha +P38065 UniProtKB Modified residue 727 727 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38065 UniProtKB Modified residue 733 733 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P53886 1 1748 +P53886 UniProtKB Chain 1 1748 . . . ID=PRO_0000215875;Note=Anaphase-promoting complex subunit 1 +P53886 UniProtKB Compositional bias 353 357 . . . Note=Poly-Gln +P53886 UniProtKB Modified residue 1462 1462 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53886 UniProtKB Sequence conflict 1547 1547 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12440 1 853 +Q12440 UniProtKB Chain 1 853 . . . ID=PRO_0000119814;Note=Anaphase-promoting complex subunit 2 +Q12440 UniProtKB Helix 775 792 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LDD +Q12440 UniProtKB Beta strand 794 796 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LDD +Q12440 UniProtKB Helix 797 807 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LDD +Q12440 UniProtKB Helix 810 812 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LDD +Q12440 UniProtKB Helix 819 831 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LDD +Q12440 UniProtKB Beta strand 834 836 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LDD +Q12440 UniProtKB Turn 839 841 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LDD +Q12440 UniProtKB Beta strand 842 845 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LDD +##sequence-region Q12449 1 350 +Q12449 UniProtKB Chain 1 350 . . . ID=PRO_0000215822;Note=Hsp90 co-chaperone AHA1 +Q12449 UniProtKB Mutagenesis 53 53 . . . Note=No effect on Hsp90 ATPase activity but reduces Hsp90 binding affinity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14739935;Dbxref=PMID:14739935 +Q12449 UniProtKB Mutagenesis 53 53 . . . Note=Decreases activation of Hsp90 ATPase activity and substantially reduces Hsp90 binding affinity. D->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14739935;Dbxref=PMID:14739935 +Q12449 UniProtKB Mutagenesis 59 59 . . . Note=Decreases activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14739935;Dbxref=PMID:14739935 +Q12449 UniProtKB Mutagenesis 60 60 . . . Note=Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14739935;Dbxref=PMID:14739935 +Q12449 UniProtKB Mutagenesis 62 62 . . . Note=Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14739935;Dbxref=PMID:14739935 +Q12449 UniProtKB Sequence conflict 28 28 . . . Note=L->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12449 UniProtKB Helix 17 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +Q12449 UniProtKB Beta strand 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USV +Q12449 UniProtKB Beta strand 41 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +Q12449 UniProtKB Beta strand 49 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +Q12449 UniProtKB Beta strand 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USV +Q12449 UniProtKB Beta strand 68 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +Q12449 UniProtKB Beta strand 82 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USV +Q12449 UniProtKB Beta strand 88 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +Q12449 UniProtKB Helix 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +Q12449 UniProtKB Beta strand 110 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +Q12449 UniProtKB Helix 123 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +Q12449 UniProtKB Helix 132 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USU +##sequence-region Q9ZZX0 1 354 +Q9ZZX0 UniProtKB Chain 1 354 . . . ID=PRO_0000270561;Note=Intron-encoded DNA endonuclease aI5 beta +##sequence-region P47015 1 356 +P47015 UniProtKB Transit peptide 1 32 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47015 UniProtKB Chain 33 356 . . . ID=PRO_0000203039;Note=Altered inheritance of mitochondria protein 23%2C mitochondrial +##sequence-region P36154 1 155 +P36154 UniProtKB Chain 1 155 . . . ID=PRO_0000203221;Note=Altered inheritance rate of mitochondria protein 29 +P36154 UniProtKB Modified residue 78 78 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36154 UniProtKB Sequence conflict 153 153 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08223 1 395 +Q08223 UniProtKB Transmembrane 156 176 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07716 1 390 +Q07716 UniProtKB Signal peptide 1 26 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07716 UniProtKB Chain 27 390 . . . ID=PRO_0000242484;Note=Altered inheritance of mitochondria protein 6 +Q07716 UniProtKB Sequence conflict 44 44 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47771 1 506 +P47771 UniProtKB Chain 1 506 . . . ID=PRO_0000056439;Note=Aldehyde dehydrogenase [NAD(P)+] 1 +P47771 UniProtKB Active site 268 268 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008 +P47771 UniProtKB Active site 302 302 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008 +P47771 UniProtKB Site 169 169 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47771 UniProtKB Sequence conflict 23 23 . . . Note=L->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47771 UniProtKB Sequence conflict 462 462 . . . Note=S->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47771 UniProtKB Sequence conflict 486 488 . . . Note=QSG->DNV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47771 UniProtKB Sequence conflict 497 497 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47771 UniProtKB Sequence conflict 500 501 . . . Note=IN->MD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P54114 1 506 +P54114 UniProtKB Chain 1 506 . . . ID=PRO_0000056440;Note=Aldehyde dehydrogenase [NAD(P)+] 2 +P54114 UniProtKB Active site 268 268 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008 +P54114 UniProtKB Active site 302 302 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008 +P54114 UniProtKB Site 169 169 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P46367 1 519 +P46367 UniProtKB Transit peptide 1 24 . . . Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1989592,ECO:0000269|PubMed:9150920;Dbxref=PMID:1989592,PMID:9150920 +P46367 UniProtKB Chain 25 519 . . . ID=PRO_0000007165;Note=Potassium-activated aldehyde dehydrogenase%2C mitochondrial +P46367 UniProtKB Nucleotide binding 268 273 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46367 UniProtKB Active site 290 290 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008 +P46367 UniProtKB Active site 324 324 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008 +P46367 UniProtKB Site 192 192 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46367 UniProtKB Modified residue 96 96 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46367 UniProtKB Modified residue 216 216 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P46367 UniProtKB Modified residue 500 500 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:19779198;Dbxref=PMID:17761666,PMID:19779198 +P46367 UniProtKB Sequence conflict 51 51 . . . Note=N->NN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46367 UniProtKB Sequence conflict 63 63 . . . Note=E->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38242 1 237 +P38242 UniProtKB Chain 1 237 . . . ID=PRO_0000123818;Note=UDP-N-acetylglucosamine transferase subunit ALG14 +P38242 UniProtKB Topological domain 1 7 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17686769;Dbxref=PMID:17686769 +P38242 UniProtKB Transmembrane 8 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38242 UniProtKB Topological domain 29 237 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17686769;Dbxref=PMID:17686769 +##sequence-region P40350 1 334 +P40350 UniProtKB Chain 1 334 . . . ID=PRO_0000059097;Note=Dolichyl-phosphate beta-glucosyltransferase +P40350 UniProtKB Topological domain 1 12 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40350 UniProtKB Transmembrane 13 33 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40350 UniProtKB Topological domain 34 334 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40350 UniProtKB Glycosylation 83 83 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40350 UniProtKB Glycosylation 119 119 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40351 1 577 +P40351 UniProtKB Chain 1 577 . . . ID=PRO_0000174168;Note=Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1%2C3-glucosyltransferase +P40351 UniProtKB Topological domain 1 42 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Transmembrane 43 63 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Topological domain 64 92 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Transmembrane 93 113 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Topological domain 114 139 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Transmembrane 140 160 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Topological domain 161 168 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Transmembrane 169 189 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Topological domain 190 219 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Transmembrane 220 240 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Topological domain 241 266 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Transmembrane 267 287 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Topological domain 288 307 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Transmembrane 308 328 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Topological domain 329 382 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Transmembrane 383 403 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Topological domain 404 419 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Transmembrane 420 440 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Topological domain 441 447 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Transmembrane 448 468 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Topological domain 469 470 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Transmembrane 471 491 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Topological domain 492 504 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Transmembrane 505 525 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Topological domain 526 543 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Transmembrane 544 564 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40351 UniProtKB Topological domain 565 577 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43633 1 760 +P43633 UniProtKB Chain 1 760 . . . ID=PRO_0000064557;Note=Serine/threonine-protein kinase Haspin homolog ALK1 +P43633 UniProtKB Domain 468 760 . . . Note=Protein kinase +P43633 UniProtKB Nucleotide binding 474 482 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43633 UniProtKB Motif 200 202 . . . Note=KEN box +P43633 UniProtKB Motif 224 232 . . . Note=D box +P43633 UniProtKB Compositional bias 94 449 . . . Note=Ser-rich +P43633 UniProtKB Compositional bias 240 245 . . . Note=Poly-Gln +P43633 UniProtKB Compositional bias 264 269 . . . Note=Poly-Ser +P43633 UniProtKB Compositional bias 351 356 . . . Note=Poly-Ser +P43633 UniProtKB Binding site 510 510 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43633 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43633 UniProtKB Modified residue 79 79 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43633 UniProtKB Mutagenesis 606 610 . . . Note=Reduces strongly kinase activity. EHRNL->AAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16855400;Dbxref=PMID:16855400 +P43633 UniProtKB Sequence conflict 758 760 . . . Note=LYK->AL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32459 1 195 +P32459 UniProtKB Chain 1 195 . . . ID=PRO_0000120562;Note=Ureidoglycolate lyase +##sequence-region Q08269 1 859 +Q08269 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q08269 UniProtKB Chain 2 859 . . . ID=PRO_0000201535;Note=Magnesium transporter ALR1 +Q08269 UniProtKB Transmembrane 744 764 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08269 UniProtKB Transmembrane 773 793 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08269 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q08269 UniProtKB Modified residue 77 77 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q08269 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08269 UniProtKB Modified residue 185 185 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08269 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08269 UniProtKB Modified residue 220 220 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q08269 UniProtKB Modified residue 221 221 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q08269 UniProtKB Modified residue 236 236 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q08269 UniProtKB Modified residue 242 242 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q08269 UniProtKB Modified residue 850 850 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q08269 UniProtKB Sequence conflict 13 13 . . . Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P14904 1 514 +P14904 UniProtKB Propeptide 1 45 . . . ID=PRO_0000026806;Note=Required for vacuolar localization. Mediates aggregation and vesicle formation in Cvt pathway;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2651436,ECO:0000269|PubMed:8521804,ECO:0000269|PubMed:8601598;Dbxref=PMID:2651436,PMID:8521804,PMID:8601598 +P14904 UniProtKB Chain 46 514 . . . ID=PRO_0000026807;Note=Vacuolar aminopeptidase 1 +P14904 UniProtKB Metal binding 132 132 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0 +P14904 UniProtKB Metal binding 303 303 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0 +P14904 UniProtKB Metal binding 303 303 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0 +P14904 UniProtKB Metal binding 340 340 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0 +P14904 UniProtKB Metal binding 385 385 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0 +P14904 UniProtKB Metal binding 479 479 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0 +P14904 UniProtKB Binding site 210 210 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0 +P14904 UniProtKB Binding site 339 339 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0 +P14904 UniProtKB Binding site 385 385 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0 +P14904 UniProtKB Binding site 388 388 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9ULA0 +P14904 UniProtKB Site 45 46 . . . Note=Cleavage%3B by protease B (PrB/PRB1);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1400574;Dbxref=PMID:1400574 +P14904 UniProtKB Modified residue 356 356 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14904 UniProtKB Glycosylation 107 107 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P14904 UniProtKB Glycosylation 110 110 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P14904 UniProtKB Glycosylation 448 448 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P14904 UniProtKB Sequence conflict 233 233 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14904 UniProtKB Sequence conflict 323 323 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14904 UniProtKB Sequence conflict 328 328 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14904 UniProtKB Sequence conflict 369 369 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14904 UniProtKB Helix 1 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGE +P14904 UniProtKB Helix 34 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH9 +P14904 UniProtKB Beta strand 45 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH9 +P14904 UniProtKB Helix 48 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Helix 66 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Turn 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 100 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Turn 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 110 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Helix 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 127 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 136 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 157 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Helix 166 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 173 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 190 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Helix 209 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Helix 213 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Turn 221 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 228 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Helix 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Turn 250 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R8F +P14904 UniProtKB Helix 257 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Helix 271 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 274 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 288 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 296 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Helix 302 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Turn 324 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 330 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Helix 339 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Helix 349 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Helix 353 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Helix 372 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 380 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Helix 395 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 411 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 418 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Helix 424 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 442 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Helix 457 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 467 472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 474 477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Beta strand 480 486 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Helix 489 508 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGF +P14904 UniProtKB Helix 509 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JH9 +##sequence-region P47064 1 194 +P47064 UniProtKB Chain 1 194 . . . ID=PRO_0000193822;Note=AP-3 complex subunit sigma +##sequence-region P60010 1 375 +P60010 UniProtKB Chain 1 375 . . . ID=PRO_0000089051;Note=Actin +P60010 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:1885608;Dbxref=PMID:22814378,PMID:1885608 +P60010 UniProtKB Cross-link 191 191 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P60010 UniProtKB Natural variant 143 143 . . . Note=In strain: CBS 1907. Y->F +P60010 UniProtKB Sequence conflict 178 178 . . . Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P60010 UniProtKB Sequence conflict 308 308 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P60010 UniProtKB Beta strand 8 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Beta strand 14 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Beta strand 28 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Beta strand 35 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Turn 45 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YVN +P60010 UniProtKB Helix 56 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Beta strand 65 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Beta strand 70 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YVN +P60010 UniProtKB Beta strand 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YVN +P60010 UniProtKB Helix 79 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Turn 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Beta strand 103 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 113 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Beta strand 130 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 137 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Beta strand 148 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Beta strand 160 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 172 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Beta strand 176 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 182 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Turn 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 203 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 223 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Turn 229 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Beta strand 234 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Beta strand 238 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Beta strand 247 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 253 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 258 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 264 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 274 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 287 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Beta strand 297 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 302 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 309 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Turn 333 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 338 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 350 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Beta strand 356 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 359 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 367 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +P60010 UniProtKB Helix 370 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAG +##sequence-region P25371 1 1049 +P25371 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Chain 26 1049 . . . ID=PRO_0000000257;Note=Probable ATP-dependent permease +P25371 UniProtKB Topological domain 26 324 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Transmembrane 325 345 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Topological domain 346 463 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Transmembrane 464 481 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Topological domain 482 793 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Transmembrane 794 814 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Topological domain 815 828 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Transmembrane 829 849 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Topological domain 850 877 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Transmembrane 878 898 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Topological domain 899 909 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Transmembrane 910 930 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Topological domain 931 937 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Transmembrane 938 958 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Topological domain 959 1000 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Transmembrane 1001 1021 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Topological domain 1022 1024 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Transmembrane 1025 1045 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Topological domain 1046 1049 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Domain 384 631 . . . Note=ABC transporter;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P25371 UniProtKB Domain 793 1044 . . . Note=ABC transmembrane type-2 +P25371 UniProtKB Nucleotide binding 423 430 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P25371 UniProtKB Modified residue 659 659 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P25371 UniProtKB Modified residue 702 702 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P25371 UniProtKB Glycosylation 50 50 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Glycosylation 114 114 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Glycosylation 165 165 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Glycosylation 221 221 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Glycosylation 935 935 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25371 UniProtKB Sequence conflict 29 29 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25613 1 283 +P25613 UniProtKB Chain 1 283 . . . ID=PRO_0000135706;Note=Accumulation of dyads protein 2 +P25613 UniProtKB Topological domain 1 89 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25613 UniProtKB Transmembrane 90 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25613 UniProtKB Topological domain 111 120 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25613 UniProtKB Transmembrane 121 141 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25613 UniProtKB Topological domain 142 151 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25613 UniProtKB Transmembrane 152 172 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25613 UniProtKB Topological domain 173 185 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25613 UniProtKB Transmembrane 186 206 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25613 UniProtKB Topological domain 207 208 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25613 UniProtKB Transmembrane 209 229 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25613 UniProtKB Topological domain 230 240 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25613 UniProtKB Transmembrane 241 261 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25613 UniProtKB Topological domain 262 283 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P33304 1 620 +P33304 UniProtKB Chain 1 620 . . . ID=PRO_0000064485;Note=Protein AFR1 +P33304 UniProtKB Modified residue 472 472 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P33304 UniProtKB Modified residue 526 526 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region P22149 1 690 +P22149 UniProtKB Chain 1 690 . . . ID=PRO_0000064487;Note=Iron-regulated transcriptional activator AFT1 +P22149 UniProtKB Natural variant 291 291 . . . Note=In allele AFT1-1UP%3B which is constitutively activated. C->F +P22149 UniProtKB Sequence conflict 8 8 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 71 71 . . . Note=I->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 136 136 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 236 236 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 329 329 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 378 378 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 416 416 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 416 416 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 468 468 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 507 507 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 507 507 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 538 538 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 538 538 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 568 568 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 568 568 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 579 579 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 579 579 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 644 644 . . . Note=H->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 644 644 . . . Note=H->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 649 649 . . . Note=H->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22149 UniProtKB Sequence conflict 649 649 . . . Note=H->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P87275 1 137 +P87275 UniProtKB Chain 1 137 . . . ID=PRO_0000202641;Note=Altered inheritance of mitochondria protein 11 +P87275 UniProtKB Transmembrane 20 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P87275 UniProtKB Transmembrane 66 88 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53109 1 570 +P53109 UniProtKB Chain 1 570 . . . ID=PRO_0000202731;Note=Probable metalloreductase AIM14 +P53109 UniProtKB Topological domain 1 20 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53109 UniProtKB Transmembrane 21 41 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53109 UniProtKB Topological domain 42 69 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53109 UniProtKB Transmembrane 70 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53109 UniProtKB Topological domain 91 141 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53109 UniProtKB Transmembrane 142 162 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53109 UniProtKB Topological domain 163 176 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53109 UniProtKB Transmembrane 177 197 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53109 UniProtKB Topological domain 198 373 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53109 UniProtKB Transmembrane 374 394 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53109 UniProtKB Topological domain 395 570 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53109 UniProtKB Domain 101 219 . . . Note=Ferric oxidoreductase +P53109 UniProtKB Domain 250 388 . . . Note=FAD-binding FR-type +##sequence-region P47140 1 327 +P47140 UniProtKB Chain 1 327 . . . ID=PRO_0000203109;Note=Altered inheritance rate of mitochondria protein 25 +##sequence-region P39721 1 246 +P39721 UniProtKB Chain 1 246 . . . ID=PRO_0000202423;Note=Protein AIM2 +##sequence-region Q04689 1 311 +Q04689 UniProtKB Chain 1 311 . . . ID=PRO_0000203255;Note=Altered inheritance of mitochondria protein 32 +##sequence-region P53730 1 551 +P53730 UniProtKB Chain 1 551 . . . ID=PRO_0000215786;Note=Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1%2C6-mannosyltransferase +P53730 UniProtKB Topological domain 1 2 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Transmembrane 3 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Topological domain 24 61 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Transmembrane 62 82 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Topological domain 83 89 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Transmembrane 90 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Topological domain 111 136 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Transmembrane 137 157 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Topological domain 158 178 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Transmembrane 179 199 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Topological domain 200 202 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Transmembrane 203 223 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Topological domain 224 227 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Transmembrane 228 248 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Topological domain 249 275 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Transmembrane 276 296 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Topological domain 297 303 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Transmembrane 304 324 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Topological domain 325 331 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Transmembrane 332 352 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Topological domain 353 365 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Transmembrane 366 386 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Topological domain 387 417 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Transmembrane 418 438 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53730 UniProtKB Topological domain 439 551 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43636 1 503 +P43636 UniProtKB Chain 1 503 . . . ID=PRO_0000080271;Note=Alpha-1%2C3/1%2C6-mannosyltransferase ALG2 +P43636 UniProtKB Transmembrane 64 84 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43636 UniProtKB Transmembrane 112 132 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43636 UniProtKB Transmembrane 443 463 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43636 UniProtKB Glycosylation 170 170 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43636 UniProtKB Glycosylation 303 303 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43636 UniProtKB Glycosylation 371 371 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43636 UniProtKB Glycosylation 400 400 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43636 UniProtKB Mutagenesis 335 335 . . . Note=Severly affects activity%2C especially the second mannosylation step. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16878994;Dbxref=PMID:16878994 +P43636 UniProtKB Mutagenesis 343 343 . . . Note=No activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16878994;Dbxref=PMID:16878994 +P43636 UniProtKB Sequence conflict 8 8 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43636 UniProtKB Sequence conflict 237 238 . . . Note=KA->NG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43636 UniProtKB Sequence conflict 302 302 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43636 UniProtKB Sequence conflict 457 457 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43636 UniProtKB Sequence conflict 470 503 . . . Note=FLFMATFMVLYFKNYLWGIYWAFVFALSYPYEEI->SYLWPLLWYYILRTTYGEFTGHLYSLSPTLMKKYNVYLNKQCIPPEEKIIYIGEEISKCK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32789 1 676 +P32789 UniProtKB Chain 1 676 . . . ID=PRO_0000202464;Note=Serine/threonine-protein kinase Haspin homolog ALK2 +P32789 UniProtKB Domain 383 672 . . . Note=Protein kinase +P32789 UniProtKB Nucleotide binding 389 397 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32789 UniProtKB Motif 116 118 . . . Note=KEN box +P32789 UniProtKB Motif 150 158 . . . Note=D box +P32789 UniProtKB Compositional bias 29 309 . . . Note=Ser-rich +P32789 UniProtKB Binding site 430 430 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32789 UniProtKB Mutagenesis 528 532 . . . Note=Reduces strongly kinase activity. EHRNL->AAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16855400;Dbxref=PMID:16855400 +##sequence-region P43553 1 858 +P43553 UniProtKB Chain 1 858 . . . ID=PRO_0000201536;Note=Magnesium transporter ALR2 +P43553 UniProtKB Topological domain 1 741 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43553 UniProtKB Transmembrane 742 762 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43553 UniProtKB Topological domain 763 771 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43553 UniProtKB Transmembrane 772 792 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43553 UniProtKB Topological domain 793 858 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47029 1 1046 +P47029 UniProtKB Chain 1 1046 . . . ID=PRO_0000203049;Note=Arrestin-related trafficking adapter 3 +P47029 UniProtKB Modified residue 155 155 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P47029 UniProtKB Modified residue 162 162 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P47029 UniProtKB Modified residue 213 213 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P47029 UniProtKB Modified residue 586 586 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47029 UniProtKB Modified residue 826 826 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47029 UniProtKB Modified residue 838 838 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P47029 UniProtKB Modified residue 900 900 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P47029 UniProtKB Modified residue 1022 1022 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47029 UniProtKB Modified residue 1023 1023 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47029 UniProtKB Sequence conflict 852 852 . . . Note=P->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P50082 1 593 +P50082 UniProtKB Chain 1 593 . . . ID=PRO_0000050842;Note=Meiosis-specific APC/C activator protein AMA1 +P50082 UniProtKB Repeat 226 264 . . . Note=WD 1 +P50082 UniProtKB Repeat 271 310 . . . Note=WD 2 +P50082 UniProtKB Repeat 323 364 . . . Note=WD 3 +P50082 UniProtKB Repeat 388 427 . . . Note=WD 4 +P50082 UniProtKB Repeat 432 474 . . . Note=WD 5 +P50082 UniProtKB Repeat 525 564 . . . Note=WD 6 +P50082 UniProtKB Motif 29 35 . . . Note=C-box;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50082 UniProtKB Compositional bias 94 100 . . . Note=Poly-Ser +##sequence-region P38285 1 549 +P38285 UniProtKB Chain 1 549 . . . ID=PRO_0000202500;Note=Antagonist of mitotic exit network protein 1 +##sequence-region P40502 1 157 +P40502 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40502 UniProtKB Chain 2 157 . . . ID=PRO_0000202977;Note=Altered inheritance of mitochondria protein 19%2C mitochondrial +P40502 UniProtKB Transmembrane 31 48 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40502 UniProtKB Transmembrane 80 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40502 UniProtKB Transmembrane 103 119 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40502 UniProtKB Transmembrane 131 147 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40502 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P40563 1 679 +P40563 UniProtKB Chain 1 679 . . . ID=PRO_0000203003;Note=Altered inheritance of mitochondria protein 21 +P40563 UniProtKB Region 383 396 . . . Note=Interaction with SH3 domain of ABP1 +P40563 UniProtKB Modified residue 18 18 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P40563 UniProtKB Modified residue 36 36 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40563 UniProtKB Modified residue 58 58 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P40563 UniProtKB Modified residue 70 70 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40563 UniProtKB Modified residue 85 85 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P40563 UniProtKB Modified residue 104 104 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40563 UniProtKB Modified residue 183 183 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P40563 UniProtKB Modified residue 206 206 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40563 UniProtKB Modified residue 231 231 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40563 UniProtKB Modified residue 277 277 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40563 UniProtKB Modified residue 284 284 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40563 UniProtKB Modified residue 324 324 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40563 UniProtKB Modified residue 552 552 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40563 UniProtKB Modified residue 576 576 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40563 UniProtKB Modified residue 620 620 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40563 UniProtKB Modified residue 623 623 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40563 UniProtKB Modified residue 625 625 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40563 UniProtKB Modified residue 627 627 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40563 UniProtKB Modified residue 667 667 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40563 UniProtKB Modified residue 671 671 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40563 UniProtKB Modified residue 675 675 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40563 UniProtKB Modified residue 678 678 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P40053 1 627 +P40053 UniProtKB Transit peptide 1 43 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40053 UniProtKB Chain 44 627 . . . ID=PRO_0000202637;Note=Altered inheritance of mitochondria protein 9%2C mitochondrial +##sequence-region P25335 1 343 +P25335 UniProtKB Chain 1 343 . . . ID=PRO_0000205914;Note=Allantoicase +P25335 UniProtKB Sequence conflict 93 93 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25335 UniProtKB Sequence conflict 134 135 . . . Note=WV->SL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25335 UniProtKB Beta strand 2 4 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Helix 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Helix 9 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Turn 17 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Helix 28 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 33 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Helix 45 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 69 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 82 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 89 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 93 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 106 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 111 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 135 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 148 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 162 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 174 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Helix 201 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 206 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Helix 218 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 224 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Helix 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 233 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 246 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 257 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 270 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 275 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 297 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 311 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 323 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +P25335 UniProtKB Beta strand 337 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O59 +##sequence-region Q00776 1 475 +Q00776 UniProtKB Chain 1 475 . . . ID=PRO_0000193778;Note=AP-1 complex subunit mu-1-I +Q00776 UniProtKB Domain 175 473 . . . Note=MHD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00404 +Q00776 UniProtKB Sequence conflict 214 214 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00776 UniProtKB Sequence conflict 216 216 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00776 UniProtKB Sequence conflict 222 222 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00776 UniProtKB Sequence conflict 433 433 . . . Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00776 UniProtKB Sequence conflict 440 440 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00776 UniProtKB Sequence conflict 450 450 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P35181 1 156 +P35181 UniProtKB Chain 1 156 . . . ID=PRO_0000193803;Note=AP-1 complex subunit sigma-1 +##sequence-region P16550 1 321 +P16550 UniProtKB Chain 1 321 . . . ID=PRO_0000064611;Note=Protein APA1 +P16550 UniProtKB Region 93 94 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108 +P16550 UniProtKB Region 151 154 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108 +P16550 UniProtKB Region 273 275 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108 +P16550 UniProtKB Active site 158 158 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108 +P16550 UniProtKB Binding site 54 54 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108 +P16550 UniProtKB Binding site 145 145 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108 +P16550 UniProtKB Binding site 160 160 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108 +P16550 UniProtKB Binding site 280 280 . . . Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108 +P16550 UniProtKB Binding site 284 284 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108 +P16550 UniProtKB Site 160 160 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22108 +P16550 UniProtKB Modified residue 60 60 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P16550 UniProtKB Sequence conflict 100 100 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38281 1 316 +P38281 UniProtKB Chain 1 316 . . . ID=PRO_0000202497;Note=Actin patches distal protein 1 +##sequence-region P40532 1 138 +P40532 UniProtKB Chain 1 138 . . . ID=PRO_0000202992;Note=Nuclear membrane organization protein APQ12 +P40532 UniProtKB Topological domain 1 39 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40532 UniProtKB Transmembrane 40 58 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40532 UniProtKB Topological domain 59 67 . . . Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40532 UniProtKB Transmembrane 68 84 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40532 UniProtKB Topological domain 85 138 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53909 1 347 +P53909 UniProtKB Chain 1 347 . . . ID=PRO_0000194360;Note=Adenine deaminase +P53909 UniProtKB Active site 207 207 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03145 +P53909 UniProtKB Metal binding 16 16 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03145 +P53909 UniProtKB Metal binding 18 18 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03145 +P53909 UniProtKB Metal binding 204 204 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03145 +P53909 UniProtKB Metal binding 285 285 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03145 +P53909 UniProtKB Binding site 286 286 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03145 +P53909 UniProtKB Site 228 228 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03145 +P53909 UniProtKB Mutagenesis 69 69 . . . Note=In aah1-2%3B impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885 +P53909 UniProtKB Mutagenesis 72 72 . . . Note=In aah1-3%3B impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885 +P53909 UniProtKB Mutagenesis 219 219 . . . Note=In aah1-4%3B impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885 +P53909 UniProtKB Mutagenesis 237 237 . . . Note=In aah1-6%3B impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885 +P53909 UniProtKB Mutagenesis 329 329 . . . Note=In aah1-7%3B impairs AAH1 degradation during postdiauxic growth. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885 +##sequence-region Q2V2Q1 1 113 +Q2V2Q1 UniProtKB Chain 1 113 . . . ID=PRO_0000248450;Note=Antisense of depressing factor protein 1 +##sequence-region P00330 1 348 +P00330 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:320000;Dbxref=PMID:320000 +P00330 UniProtKB Chain 2 348 . . . ID=PRO_0000160730;Note=Alcohol dehydrogenase 1 +P00330 UniProtKB Nucleotide binding 178 184 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00330 UniProtKB Nucleotide binding 269 271 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00330 UniProtKB Metal binding 44 44 . . . Note=Zinc 1%3B catalytic +P00330 UniProtKB Metal binding 67 67 . . . Note=Zinc 1%3B catalytic +P00330 UniProtKB Metal binding 98 98 . . . Note=Zinc 2 +P00330 UniProtKB Metal binding 101 101 . . . Note=Zinc 2 +P00330 UniProtKB Metal binding 104 104 . . . Note=Zinc 2 +P00330 UniProtKB Metal binding 112 112 . . . Note=Zinc 2 +P00330 UniProtKB Metal binding 154 154 . . . Note=Zinc 1%3B catalytic +P00330 UniProtKB Binding site 202 202 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00330 UniProtKB Binding site 207 207 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00330 UniProtKB Binding site 341 341 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00330 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:320000;Dbxref=PMID:320000 +P00330 UniProtKB Modified residue 213 213 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P00330 UniProtKB Modified residue 223 223 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P00330 UniProtKB Modified residue 279 279 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00330 UniProtKB Modified residue 316 316 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198 +P00330 UniProtKB Cross-link 226 226 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00330 UniProtKB Cross-link 234 234 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00330 UniProtKB Cross-link 287 287 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00330 UniProtKB Cross-link 319 319 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00330 UniProtKB Natural variant 236 236 . . . Note=T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:320000;Dbxref=PMID:320000 +P00330 UniProtKB Sequence conflict 21 21 . . . Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00330 UniProtKB Sequence conflict 21 21 . . . Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00330 UniProtKB Sequence conflict 59 59 . . . Note=V->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00330 UniProtKB Sequence conflict 148 148 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00330 UniProtKB Sequence conflict 152 152 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00330 UniProtKB Sequence conflict 237 237 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00330 UniProtKB Sequence conflict 314 314 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00330 UniProtKB Sequence conflict 338 338 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00330 UniProtKB Beta strand 5 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 20 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 33 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Helix 45 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 61 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 68 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 88 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 93 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 99 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Helix 102 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Helix 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Turn 119 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 125 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Turn 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 137 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Helix 146 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Helix 150 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Helix 155 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 173 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Turn 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Helix 184 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 197 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Helix 207 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 218 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Turn 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Helix 228 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 240 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Helix 250 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 260 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 276 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Helix 281 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 290 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Helix 299 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 318 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Helix 323 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Helix 326 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +P00330 UniProtKB Beta strand 339 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W6Z +##sequence-region P00331 1 348 +P00331 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P00331 UniProtKB Chain 2 348 . . . ID=PRO_0000160731;Note=Alcohol dehydrogenase 2 +P00331 UniProtKB Nucleotide binding 178 184 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00331 UniProtKB Nucleotide binding 269 271 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00331 UniProtKB Metal binding 44 44 . . . Note=Zinc 1%3B catalytic +P00331 UniProtKB Metal binding 67 67 . . . Note=Zinc 1%3B catalytic +P00331 UniProtKB Metal binding 98 98 . . . Note=Zinc 2 +P00331 UniProtKB Metal binding 101 101 . . . Note=Zinc 2 +P00331 UniProtKB Metal binding 104 104 . . . Note=Zinc 2 +P00331 UniProtKB Metal binding 112 112 . . . Note=Zinc 2 +P00331 UniProtKB Metal binding 154 154 . . . Note=Zinc 1%3B catalytic +P00331 UniProtKB Binding site 202 202 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00331 UniProtKB Binding site 207 207 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00331 UniProtKB Binding site 341 341 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00331 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P00331 UniProtKB Modified residue 213 213 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330 +P00331 UniProtKB Modified residue 223 223 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330 +P00331 UniProtKB Modified residue 279 279 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330 +P00331 UniProtKB Modified residue 316 316 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330 +P00331 UniProtKB Cross-link 226 226 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330 +P00331 UniProtKB Cross-link 234 234 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330 +P00331 UniProtKB Cross-link 287 287 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330 +P00331 UniProtKB Cross-link 319 319 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330 +P00331 UniProtKB Sequence conflict 16 16 . . . Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00331 UniProtKB Sequence conflict 31 31 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00331 UniProtKB Sequence conflict 233 233 . . . Note=V->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P10127 1 382 +P10127 UniProtKB Chain 1 382 . . . ID=PRO_0000087817;Note=Alcohol dehydrogenase 4 +P10127 UniProtKB Sequence conflict 60 60 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10127 UniProtKB Sequence conflict 88 88 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10127 UniProtKB Sequence conflict 310 310 . . . Note=F->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10127 UniProtKB Sequence conflict 339 339 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10127 UniProtKB Sequence conflict 348 348 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04894 1 360 +Q04894 UniProtKB Chain 1 360 . . . ID=PRO_0000160734;Note=NADP-dependent alcohol dehydrogenase 6 +Q04894 UniProtKB Nucleotide binding 187 192 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04894 UniProtKB Nucleotide binding 275 277 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04894 UniProtKB Metal binding 46 46 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04894 UniProtKB Metal binding 68 68 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04894 UniProtKB Metal binding 100 100 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04894 UniProtKB Metal binding 103 103 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04894 UniProtKB Metal binding 106 106 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04894 UniProtKB Metal binding 114 114 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04894 UniProtKB Metal binding 163 163 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04894 UniProtKB Binding site 215 215 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04894 UniProtKB Binding site 348 348 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04894 UniProtKB Modified residue 131 131 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04894 UniProtKB Modified residue 315 315 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25377 +Q04894 UniProtKB Modified residue 359 359 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q04894 UniProtKB Turn 3 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 7 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 22 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 35 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Helix 47 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Turn 54 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 70 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 90 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 95 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1N +Q04894 UniProtKB Helix 104 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Helix 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 118 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 134 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Helix 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Helix 155 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Helix 159 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Helix 164 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 182 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Helix 190 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 205 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Helix 216 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 225 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Helix 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Helix 236 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 244 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 254 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PS0 +Q04894 UniProtKB Turn 259 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Helix 262 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 266 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 284 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Helix 288 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 295 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Helix 304 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 323 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Helix 330 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Beta strand 346 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +Q04894 UniProtKB Helix 355 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PIW +##sequence-region P47143 1 340 +P47143 UniProtKB Chain 1 340 . . . ID=PRO_0000080062;Note=Adenosine kinase +P47143 UniProtKB Active site 293 293 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q01976 1 231 +Q01976 UniProtKB Chain 1 231 . . . ID=PRO_0000057050;Note=ADP-ribose pyrophosphatase +Q01976 UniProtKB Domain 75 214 . . . Note=Nudix hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00794 +Q01976 UniProtKB Region 64 65 . . . Note=Substrate binding%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01976 UniProtKB Motif 116 137 . . . Note=Nudix box +Q01976 UniProtKB Metal binding 115 115 . . . Note=Magnesium 1%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01976 UniProtKB Metal binding 131 131 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01976 UniProtKB Metal binding 131 131 . . . Note=Magnesium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01976 UniProtKB Metal binding 135 135 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01976 UniProtKB Metal binding 135 135 . . . Note=Magnesium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01976 UniProtKB Metal binding 185 185 . . . Note=Magnesium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01976 UniProtKB Binding site 46 46 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01976 UniProtKB Binding site 69 69 . . . Note=Substrate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01976 UniProtKB Binding site 103 103 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01976 UniProtKB Binding site 117 117 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01976 UniProtKB Binding site 152 152 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q01976 UniProtKB Alternative sequence 1 19 . . . ID=VSP_058126;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P18239 1 318 +P18239 UniProtKB Chain 1 318 . . . ID=PRO_0000090594;Note=ADP%2CATP carrier protein 2 +P18239 UniProtKB Transmembrane 20 54 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18239 UniProtKB Transmembrane 91 115 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18239 UniProtKB Transmembrane 123 157 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18239 UniProtKB Transmembrane 192 219 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18239 UniProtKB Transmembrane 224 258 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18239 UniProtKB Transmembrane 287 312 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18239 UniProtKB Repeat 21 114 . . . Note=Solcar 1 +P18239 UniProtKB Repeat 125 217 . . . Note=Solcar 2 +P18239 UniProtKB Repeat 225 311 . . . Note=Solcar 3 +P18239 UniProtKB Motif 252 257 . . . Note=Substrate recognition;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18239 UniProtKB Binding site 96 96 . . . Note=Nucleotide;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18239 UniProtKB Sequence conflict 58 58 . . . Note=L->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18239 UniProtKB Sequence conflict 65 65 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18239 UniProtKB Sequence conflict 68 68 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18239 UniProtKB Sequence conflict 71 71 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18239 UniProtKB Sequence conflict 79 79 . . . Note=T->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18239 UniProtKB Sequence conflict 83 83 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18239 UniProtKB Sequence conflict 113 113 . . . Note=A->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18239 UniProtKB Sequence conflict 124 124 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18239 UniProtKB Helix 25 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G +P18239 UniProtKB Helix 54 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G +P18239 UniProtKB Helix 70 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G +P18239 UniProtKB Helix 84 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G +P18239 UniProtKB Helix 90 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G +P18239 UniProtKB Helix 97 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G +P18239 UniProtKB Helix 119 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G +P18239 UniProtKB Helix 123 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G +P18239 UniProtKB Helix 173 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G +P18239 UniProtKB Turn 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G +P18239 UniProtKB Helix 193 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G +P18239 UniProtKB Helix 229 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G +P18239 UniProtKB Helix 246 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G +P18239 UniProtKB Turn 258 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G +P18239 UniProtKB Helix 268 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G +P18239 UniProtKB Helix 281 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G +P18239 UniProtKB Helix 288 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9G +P18239 UniProtKB Beta strand 313 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9H +##sequence-region P18238 1 307 +P18238 UniProtKB Chain 1 307 . . . ID=PRO_0000090595;Note=ADP%2CATP carrier protein 3 +P18238 UniProtKB Transmembrane 9 43 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18238 UniProtKB Transmembrane 80 104 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18238 UniProtKB Transmembrane 112 146 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18238 UniProtKB Transmembrane 181 208 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18238 UniProtKB Transmembrane 213 247 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18238 UniProtKB Transmembrane 276 301 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18238 UniProtKB Repeat 10 103 . . . Note=Solcar 1 +P18238 UniProtKB Repeat 114 206 . . . Note=Solcar 2 +P18238 UniProtKB Repeat 214 300 . . . Note=Solcar 3 +P18238 UniProtKB Motif 241 246 . . . Note=Substrate recognition;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18238 UniProtKB Binding site 85 85 . . . Note=Nucleotide;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18238 UniProtKB Helix 5 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q +P18238 UniProtKB Helix 31 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q +P18238 UniProtKB Helix 43 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q +P18238 UniProtKB Helix 59 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q +P18238 UniProtKB Helix 73 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q +P18238 UniProtKB Helix 79 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q +P18238 UniProtKB Turn 108 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9J +P18238 UniProtKB Helix 112 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q +P18238 UniProtKB Helix 162 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q +P18238 UniProtKB Helix 175 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q +P18238 UniProtKB Turn 179 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q +P18238 UniProtKB Helix 182 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q +P18238 UniProtKB Helix 217 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q +P18238 UniProtKB Helix 235 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q +P18238 UniProtKB Turn 247 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q +P18238 UniProtKB Helix 257 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q +P18238 UniProtKB Helix 270 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q +P18238 UniProtKB Helix 277 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9Q +P18238 UniProtKB Beta strand 302 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C9J +##sequence-region Q07732 1 790 +Q07732 UniProtKB Chain 1 790 . . . ID=PRO_0000064461;Note=Accumulates dyads protein 3 +Q07732 UniProtKB Coiled coil 241 328 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07732 UniProtKB Coiled coil 361 430 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07732 UniProtKB Coiled coil 477 498 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07732 UniProtKB Coiled coil 540 658 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07732 UniProtKB Sequence conflict 569 569 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32493 1 518 +P32493 UniProtKB Transit peptide 1 19 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32493 UniProtKB Chain 20 518 . . . ID=PRO_0000021791;Note=ATPase expression protein 1%2C mitochondrial +P32493 UniProtKB Sequence conflict 51 51 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32493 UniProtKB Sequence conflict 51 51 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32493 UniProtKB Sequence conflict 113 113 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32493 UniProtKB Sequence conflict 113 113 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32493 UniProtKB Sequence conflict 159 159 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32493 UniProtKB Sequence conflict 159 159 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32493 UniProtKB Sequence conflict 197 197 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32493 UniProtKB Sequence conflict 197 197 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32493 UniProtKB Sequence conflict 212 212 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32493 UniProtKB Sequence conflict 212 212 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32493 UniProtKB Sequence conflict 225 225 . . . Note=Y->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32493 UniProtKB Sequence conflict 225 225 . . . Note=Y->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32493 UniProtKB Sequence conflict 240 240 . . . Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32493 UniProtKB Sequence conflict 240 240 . . . Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32493 UniProtKB Sequence conflict 295 295 . . . Note=K->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32493 UniProtKB Sequence conflict 295 295 . . . Note=K->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32493 UniProtKB Sequence conflict 392 392 . . . Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32493 UniProtKB Sequence conflict 392 392 . . . Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P22136 1 580 +P22136 UniProtKB Transit peptide 1 40 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22136 UniProtKB Chain 41 580 . . . ID=PRO_0000002536;Note=ATPase expression protein 2%2C mitochondrial +P22136 UniProtKB Mutagenesis 413 413 . . . Note=Suppresses a T-to-C nucleotide transition mutation in the 5' untranslated region of OLI1 mRNA localized 16 nucleotides upstream of the OLI1 reading frame. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10101162;Dbxref=PMID:10101162 +P22136 UniProtKB Sequence conflict 214 214 . . . Note=G->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22136 UniProtKB Sequence conflict 481 481 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08957 1 416 +Q08957 UniProtKB Chain 1 416 . . . ID=PRO_0000227599;Note=Iron-regulated transcriptional activator AFT2 +Q08957 UniProtKB Helix 54 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG +Q08957 UniProtKB Helix 57 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG +Q08957 UniProtKB Helix 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG +Q08957 UniProtKB Beta strand 72 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG +Q08957 UniProtKB Beta strand 81 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG +Q08957 UniProtKB Beta strand 112 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG +Q08957 UniProtKB Turn 119 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG +Q08957 UniProtKB Beta strand 123 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG +Q08957 UniProtKB Helix 139 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG +Q08957 UniProtKB Helix 146 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG +Q08957 UniProtKB Helix 161 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LMG +##sequence-region P43548 1 558 +P43548 UniProtKB Chain 1 558 . . . ID=PRO_0000054144;Note=General amino acid permease AGP3 +P43548 UniProtKB Topological domain 1 57 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Transmembrane 58 78 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Topological domain 79 81 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Transmembrane 82 102 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Topological domain 103 126 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Transmembrane 127 147 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Topological domain 148 168 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Transmembrane 169 189 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Topological domain 190 193 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Transmembrane 194 214 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Topological domain 215 241 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Transmembrane 242 262 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Topological domain 263 280 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Transmembrane 281 301 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Topological domain 302 324 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Transmembrane 325 345 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Topological domain 346 375 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Transmembrane 376 396 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Topological domain 397 402 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Transmembrane 403 423 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Topological domain 424 446 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Transmembrane 447 467 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Topological domain 468 480 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Transmembrane 481 501 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43548 UniProtKB Topological domain 502 558 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P25649 1 128 +P25649 UniProtKB Chain 1 128 . . . ID=PRO_0000202575;Note=ADA histone acetyltransferase complex component 2 +##sequence-region P29589 1 182 +P29589 UniProtKB Chain 1 182 . . . ID=PRO_0000064511;Note=Hexose transport activator protein +##sequence-region P38266 1 947 +P38266 UniProtKB Chain 1 947 . . . ID=PRO_0000202486;Note=Altered inheritance of mitochondria protein 3 +P38266 UniProtKB Compositional bias 95 398 . . . Note=Gln-rich +P38266 UniProtKB Compositional bias 371 447 . . . Note=Pro-rich +P38266 UniProtKB Compositional bias 862 907 . . . Note=Pro-rich +P38266 UniProtKB Modified residue 57 57 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38266 UniProtKB Modified residue 58 58 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38266 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38266 UniProtKB Modified residue 476 476 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38266 UniProtKB Modified residue 729 729 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P38266 UniProtKB Modified residue 861 861 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38266 UniProtKB Sequence conflict 515 515 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38266 UniProtKB Sequence conflict 515 515 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q99299 1 758 +Q99299 UniProtKB Chain 1 758 . . . ID=PRO_0000203491;Note=Altered inheritance of mitochondria protein 44 +Q99299 UniProtKB Coiled coil 648 711 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99299 UniProtKB Compositional bias 253 263 . . . Note=Poly-Ser +Q99299 UniProtKB Compositional bias 652 658 . . . Note=Poly-Glu +Q99299 UniProtKB Compositional bias 664 669 . . . Note=Poly-Glu +Q99299 UniProtKB Compositional bias 686 690 . . . Note=Poly-Glu +Q99299 UniProtKB Modified residue 25 25 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38885 1 310 +P38885 UniProtKB Transit peptide 1 20 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38885 UniProtKB Chain 21 310 . . . ID=PRO_0000202940;Note=Altered inheritance of mitochondria protein 46%2C mitochondrial +##sequence-region P53954 1 548 +P53954 UniProtKB Chain 1 548 . . . ID=PRO_0000080280;Note=GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1%2C2-mannosyltransferase +P53954 UniProtKB Topological domain 1 20 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53954 UniProtKB Transmembrane 21 41 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53954 UniProtKB Topological domain 42 548 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53954 UniProtKB Compositional bias 84 87 . . . Note=Poly-Gly +P53954 UniProtKB Compositional bias 543 546 . . . Note=Poly-Glu +P53954 UniProtKB Glycosylation 262 262 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53954 UniProtKB Glycosylation 393 393 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53954 UniProtKB Glycosylation 480 480 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53954 UniProtKB Glycosylation 490 490 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53954 UniProtKB Mutagenesis 84 84 . . . Note=No effect. G->A%2CP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19929855;Dbxref=PMID:19929855 +P53954 UniProtKB Mutagenesis 85 85 . . . Note=No effect. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19929855;Dbxref=PMID:19929855 +P53954 UniProtKB Mutagenesis 85 85 . . . Note=No activity. G->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19929855;Dbxref=PMID:19929855 +P53954 UniProtKB Mutagenesis 87 87 . . . Note=No effect. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19929855;Dbxref=PMID:19929855 +P53954 UniProtKB Mutagenesis 87 87 . . . Note=No activity. G->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19929855;Dbxref=PMID:19929855 +P53954 UniProtKB Mutagenesis 319 319 . . . Note=Almost no activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19929855;Dbxref=PMID:19929855 +P53954 UniProtKB Mutagenesis 405 405 . . . Note=Almost no activity. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16878994,ECO:0000269|PubMed:19929855;Dbxref=PMID:16878994,PMID:19929855 +P53954 UniProtKB Mutagenesis 406 406 . . . Note=Almost no activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19929855;Dbxref=PMID:19929855 +P53954 UniProtKB Mutagenesis 407 407 . . . Note=Impaired activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19929855;Dbxref=PMID:19929855 +P53954 UniProtKB Mutagenesis 413 413 . . . Note=No effect. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16878994,ECO:0000269|PubMed:19929855;Dbxref=PMID:16878994,PMID:19929855 +##sequence-region Q12001 1 544 +Q12001 UniProtKB Chain 1 544 . . . ID=PRO_0000174161;Note=Dolichyl pyrophosphate Man9GlcNAc2 alpha-1%2C3-glucosyltransferase +Q12001 UniProtKB Topological domain 1 35 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Transmembrane 36 56 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Topological domain 57 104 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Transmembrane 105 125 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Topological domain 126 145 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Transmembrane 146 166 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Topological domain 167 171 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Transmembrane 172 192 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Topological domain 193 223 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Transmembrane 224 244 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Topological domain 245 263 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Transmembrane 264 284 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Topological domain 285 332 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Transmembrane 333 353 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Topological domain 354 356 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Transmembrane 357 377 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Topological domain 378 398 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Transmembrane 399 419 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Topological domain 420 425 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Transmembrane 426 446 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Topological domain 447 481 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Transmembrane 482 502 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Topological domain 503 508 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Transmembrane 509 529 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Topological domain 530 544 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12001 UniProtKB Sequence conflict 203 203 . . . Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53868 1 555 +P53868 UniProtKB Chain 1 555 . . . ID=PRO_0000215789;Note=Alpha-1%2C2-mannosyltransferase ALG9 +P53868 UniProtKB Topological domain 1 7 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53868 UniProtKB Transmembrane 8 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53868 UniProtKB Topological domain 29 62 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53868 UniProtKB Transmembrane 63 83 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53868 UniProtKB Topological domain 84 86 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53868 UniProtKB Transmembrane 87 107 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53868 UniProtKB Topological domain 108 113 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53868 UniProtKB Transmembrane 114 134 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53868 UniProtKB Topological domain 135 176 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53868 UniProtKB Transmembrane 177 197 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53868 UniProtKB Topological domain 198 213 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53868 UniProtKB Transmembrane 214 234 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53868 UniProtKB Topological domain 235 268 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53868 UniProtKB Transmembrane 269 289 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53868 UniProtKB Topological domain 290 316 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53868 UniProtKB Transmembrane 317 337 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53868 UniProtKB Topological domain 338 349 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53868 UniProtKB Transmembrane 350 370 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53868 UniProtKB Topological domain 371 555 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38313 1 324 +P38313 UniProtKB Chain 1 324 . . . ID=PRO_0000064578;Note=Central kinetochore subunit AME1 +P38313 UniProtKB Coiled coil 199 263 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38313 UniProtKB Modified residue 41 41 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38313 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38313 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38313 UniProtKB Modified residue 59 59 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38313 UniProtKB Modified residue 101 101 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P39533 1 789 +P39533 UniProtKB Transit peptide 1 14 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39533 UniProtKB Chain 15 789 . . . ID=PRO_0000076649;Note=Homocitrate dehydratase%2C mitochondrial +P39533 UniProtKB Region 189 191 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39533 UniProtKB Region 672 673 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39533 UniProtKB Metal binding 385 385 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39533 UniProtKB Metal binding 448 448 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39533 UniProtKB Metal binding 451 451 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39533 UniProtKB Binding site 96 96 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39533 UniProtKB Binding site 476 476 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39533 UniProtKB Binding site 481 481 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39533 UniProtKB Mutagenesis 610 610 . . . Note=Reduces catalytic activity towards homoaconitate by 45%25 and increases the activity towards aconitate by a factor 116. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23106124;Dbxref=PMID:23106124 +##sequence-region P52910 1 683 +P52910 UniProtKB Chain 1 683 . . . ID=PRO_0000208421;Note=Acetyl-coenzyme A synthetase 2 +P52910 UniProtKB Nucleotide binding 401 403 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52910 UniProtKB Nucleotide binding 425 430 . . . Note=AMP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52910 UniProtKB Nucleotide binding 425 430 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52910 UniProtKB Region 206 209 . . . Note=Coenzyme A binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52910 UniProtKB Binding site 325 325 . . . Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52910 UniProtKB Binding site 516 516 . . . Note=AMP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52910 UniProtKB Binding site 516 516 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52910 UniProtKB Binding site 531 531 . . . Note=AMP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52910 UniProtKB Binding site 531 531 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52910 UniProtKB Binding site 539 539 . . . Note=Coenzyme A%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52910 UniProtKB Binding site 542 542 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52910 UniProtKB Binding site 612 612 . . . Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52910 UniProtKB Modified residue 679 679 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P52910 UniProtKB Cross-link 506 506 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region P48360 1 493 +P48360 UniProtKB Nucleotide binding 177 180 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165 +P48360 UniProtKB Nucleotide binding 223 224 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165 +P48360 UniProtKB Nucleotide binding 414 416 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165 +P48360 UniProtKB Binding site 26 26 . . . Note=FAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165 +P48360 UniProtKB Binding site 48 48 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165 +P48360 UniProtKB Binding site 56 56 . . . Note=FAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165 +P48360 UniProtKB Binding site 100 100 . . . Note=FAD%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165 +P48360 UniProtKB Binding site 235 235 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165 +P48360 UniProtKB Binding site 407 407 . . . Note=FAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165 +P48360 UniProtKB Binding site 414 414 . . . Note=NADP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08165 +P48360 UniProtKB Sequence conflict 33 33 . . . Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P48360 UniProtKB Sequence conflict 132 132 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25376 1 633 +P25376 UniProtKB Chain 1 633 . . . ID=PRO_0000054142;Note=General amino acid permease AGP1 +P25376 UniProtKB Topological domain 1 124 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Transmembrane 125 145 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Topological domain 146 148 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Transmembrane 149 169 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Topological domain 170 197 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Transmembrane 198 218 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Topological domain 219 231 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Transmembrane 232 252 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Topological domain 253 260 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Transmembrane 261 281 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Topological domain 282 313 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Transmembrane 314 334 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Topological domain 335 352 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Transmembrane 353 373 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Topological domain 374 402 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Transmembrane 403 425 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Topological domain 426 452 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Transmembrane 453 473 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Topological domain 474 477 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Transmembrane 478 498 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Topological domain 499 531 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Transmembrane 532 552 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Topological domain 553 560 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Transmembrane 561 581 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Topological domain 582 633 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25376 UniProtKB Modified residue 6 6 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P48813 +P25376 UniProtKB Lipidation 633 633 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25376 UniProtKB Cross-link 11 11 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P48813 +##sequence-region P10869 1 527 +P10869 UniProtKB Chain 1 527 . . . ID=PRO_0000066690;Note=Aspartokinase +P10869 UniProtKB Domain 367 440 . . . Note=ACT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01007 +P10869 UniProtKB Domain 442 527 . . . Note=ACT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01007 +P10869 UniProtKB Modified residue 333 333 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region Q08548 1 619 +Q08548 UniProtKB Chain 1 619 . . . ID=PRO_0000245257;Note=Lysophospholipid acyltransferase +Q08548 UniProtKB Topological domain 1 19 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08548 UniProtKB Transmembrane 20 39 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08548 UniProtKB Topological domain 40 51 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08548 UniProtKB Transmembrane 52 72 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08548 UniProtKB Topological domain 73 92 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08548 UniProtKB Transmembrane 93 113 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08548 UniProtKB Topological domain 114 231 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08548 UniProtKB Transmembrane 232 252 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08548 UniProtKB Topological domain 253 274 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08548 UniProtKB Transmembrane 275 295 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08548 UniProtKB Topological domain 296 429 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08548 UniProtKB Transmembrane 430 450 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08548 UniProtKB Topological domain 451 456 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08548 UniProtKB Transmembrane 457 477 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08548 UniProtKB Topological domain 478 619 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08548 UniProtKB Coiled coil 545 593 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08548 UniProtKB Active site 382 382 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08548 UniProtKB Modified residue 513 513 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q08548 UniProtKB Modified residue 605 605 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198 +Q08548 UniProtKB Modified residue 610 610 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08548 UniProtKB Modified residue 615 615 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P36117 1 915 +P36117 UniProtKB Chain 1 915 . . . ID=PRO_0000203200;Note=Arrestin-related trafficking adapter 6 +P36117 UniProtKB Modified residue 220 220 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P22580 1 549 +P22580 UniProtKB Chain 1 549 . . . ID=PRO_0000105130;Note=Probable amidase +P22580 UniProtKB Active site 132 132 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22580 UniProtKB Active site 209 209 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22580 UniProtKB Active site 233 233 . . . Note=Acyl-ester intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22580 UniProtKB Sequence conflict 525 525 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38113 1 351 +P38113 UniProtKB Chain 1 351 . . . ID=PRO_0000160733;Note=Alcohol dehydrogenase 5 +P38113 UniProtKB Nucleotide binding 181 187 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38113 UniProtKB Nucleotide binding 272 274 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38113 UniProtKB Metal binding 47 47 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38113 UniProtKB Metal binding 70 70 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38113 UniProtKB Metal binding 101 101 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38113 UniProtKB Metal binding 104 104 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38113 UniProtKB Metal binding 107 107 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38113 UniProtKB Metal binding 115 115 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38113 UniProtKB Metal binding 183 183 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38113 UniProtKB Binding site 205 205 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38113 UniProtKB Binding site 210 210 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38113 UniProtKB Binding site 344 344 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38113 UniProtKB Modified residue 226 226 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330 +P38113 UniProtKB Modified residue 282 282 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330 +P38113 UniProtKB Modified residue 319 319 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330 +P38113 UniProtKB Cross-link 229 229 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330 +P38113 UniProtKB Cross-link 237 237 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330 +P38113 UniProtKB Cross-link 290 290 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00330 +##sequence-region P04710 1 309 +P04710 UniProtKB Chain 1 309 . . . ID=PRO_0000090593;Note=ADP%2CATP carrier protein 1 +P04710 UniProtKB Transmembrane 10 44 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04710 UniProtKB Transmembrane 81 105 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04710 UniProtKB Transmembrane 114 148 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04710 UniProtKB Transmembrane 183 210 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04710 UniProtKB Transmembrane 215 249 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04710 UniProtKB Transmembrane 278 303 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04710 UniProtKB Repeat 11 104 . . . Note=Solcar 1 +P04710 UniProtKB Repeat 116 208 . . . Note=Solcar 2 +P04710 UniProtKB Repeat 216 302 . . . Note=Solcar 3 +P04710 UniProtKB Motif 243 248 . . . Note=Substrate recognition;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04710 UniProtKB Binding site 86 86 . . . Note=Nucleotide;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P47127 1 394 +P47127 UniProtKB Transit peptide 1 111 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47127 UniProtKB Chain 112 394 . . . ID=PRO_0000203103;Note=Altered inheritance of mitochondria protein 24%2C mitochondrial +##sequence-region Q12013 1 749 +Q12013 UniProtKB Chain 1 749 . . . ID=PRO_0000212936;Note=Probable palmitoyltransferase AKR2 +Q12013 UniProtKB Topological domain 1 306 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12013 UniProtKB Transmembrane 307 327 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12013 UniProtKB Transmembrane 328 348 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12013 UniProtKB Topological domain 349 360 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12013 UniProtKB Transmembrane 361 381 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12013 UniProtKB Topological domain 382 392 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12013 UniProtKB Transmembrane 393 413 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12013 UniProtKB Topological domain 414 489 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12013 UniProtKB Transmembrane 490 510 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12013 UniProtKB Topological domain 511 546 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12013 UniProtKB Transmembrane 547 567 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12013 UniProtKB Topological domain 568 749 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12013 UniProtKB Repeat 49 79 . . . Note=ANK 1 +Q12013 UniProtKB Repeat 83 112 . . . Note=ANK 2 +Q12013 UniProtKB Repeat 117 146 . . . Note=ANK 3 +Q12013 UniProtKB Repeat 150 183 . . . Note=ANK 4 +Q12013 UniProtKB Repeat 189 218 . . . Note=ANK 5 +Q12013 UniProtKB Repeat 222 251 . . . Note=ANK 6 +Q12013 UniProtKB Domain 446 496 . . . Note=DHHC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00067 +Q12013 UniProtKB Active site 476 476 . . . Note=S-palmitoyl cysteine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12013 UniProtKB Glycosylation 534 534 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P52892 1 507 +P52892 UniProtKB Chain 1 507 . . . ID=PRO_0000123937;Note=Probable alanine aminotransferase +P52892 UniProtKB Modified residue 327 327 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52892 UniProtKB Sequence conflict 420 420 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P14540 1 359 +P14540 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8935650;Dbxref=PMID:8935650 +P14540 UniProtKB Chain 2 359 . . . ID=PRO_0000178762;Note=Fructose-bisphosphate aldolase +P14540 UniProtKB Region 266 268 . . . Note=Dihydroxyacetone phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14540 UniProtKB Region 287 290 . . . Note=Dihydroxyacetone phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14540 UniProtKB Active site 110 110 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14540 UniProtKB Metal binding 111 111 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14540 UniProtKB Metal binding 145 145 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14540 UniProtKB Metal binding 175 175 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14540 UniProtKB Metal binding 227 227 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14540 UniProtKB Metal binding 265 265 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14540 UniProtKB Binding site 63 63 . . . Note=Glyceraldehyde 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14540 UniProtKB Binding site 228 228 . . . Note=Dihydroxyacetone phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14540 UniProtKB Modified residue 11 11 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950 +P14540 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14540 UniProtKB Modified residue 63 63 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14540 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P14540 UniProtKB Modified residue 83 83 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14540 UniProtKB Modified residue 96 96 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14540 UniProtKB Modified residue 147 147 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P14540 UniProtKB Modified residue 150 150 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P14540 UniProtKB Modified residue 179 179 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P14540 UniProtKB Modified residue 268 268 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P14540 UniProtKB Modified residue 290 290 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P14540 UniProtKB Modified residue 310 310 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P14540 UniProtKB Modified residue 313 313 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P14540 UniProtKB Cross-link 27 27 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P14540 UniProtKB Cross-link 73 73 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P14540 UniProtKB Cross-link 85 85 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P14540 UniProtKB Cross-link 308 308 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P50076 1 525 +P50076 UniProtKB Chain 1 525 . . . ID=PRO_0000215463;Note=Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1%2C2-glucosyltransferase +P50076 UniProtKB Transmembrane 36 56 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50076 UniProtKB Transmembrane 95 115 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50076 UniProtKB Transmembrane 128 148 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50076 UniProtKB Transmembrane 151 171 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50076 UniProtKB Transmembrane 188 208 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50076 UniProtKB Transmembrane 214 234 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50076 UniProtKB Transmembrane 257 277 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50076 UniProtKB Transmembrane 295 315 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50076 UniProtKB Transmembrane 334 354 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50076 UniProtKB Transmembrane 376 396 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50076 UniProtKB Transmembrane 424 444 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50076 UniProtKB Transmembrane 448 468 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50076 UniProtKB Transmembrane 493 513 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50076 UniProtKB Glycosylation 31 31 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50076 UniProtKB Glycosylation 278 278 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50076 UniProtKB Glycosylation 372 372 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50076 UniProtKB Sequence conflict 266 266 . . . Note=I->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P50076 UniProtKB Sequence conflict 266 266 . . . Note=I->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32375 1 460 +P32375 UniProtKB Chain 1 460 . . . ID=PRO_0000165939;Note=Allantoinase +P32375 UniProtKB Metal binding 70 70 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32375 UniProtKB Metal binding 72 72 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32375 UniProtKB Metal binding 157 157 . . . Note=Zinc 1%3B via carbamate group;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32375 UniProtKB Metal binding 157 157 . . . Note=Zinc 2%3B via carbamate group;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32375 UniProtKB Metal binding 193 193 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32375 UniProtKB Metal binding 250 250 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32375 UniProtKB Metal binding 323 323 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32375 UniProtKB Modified residue 157 157 . . . Note=N6-carboxylysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32375 UniProtKB Sequence conflict 438 460 . . . Note=VVYTNANGVSKTPLGQTLLDSRR->WYIRMPTESRKHHWVKLCLILDVKLKLQIFIKEIL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P54783 1 526 +P54783 UniProtKB Chain 1 526 . . . ID=PRO_0000128171;Note=D-arabinono-1%2C4-lactone oxidase +P54783 UniProtKB Domain 19 193 . . . Note=FAD-binding PCMH-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00718 +P54783 UniProtKB Modified residue 56 56 . . . Note=Pros-8alpha-FAD histidine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P54783 UniProtKB Sequence conflict 417 417 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38971 1 573 +P38971 UniProtKB Chain 1 573 . . . ID=PRO_0000054145;Note=Basic amino-acid permease +P38971 UniProtKB Topological domain 1 73 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Transmembrane 74 93 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Topological domain 94 95 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Transmembrane 96 116 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Topological domain 117 153 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Transmembrane 154 174 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Topological domain 175 179 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Transmembrane 180 200 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Topological domain 201 209 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Transmembrane 210 230 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Topological domain 231 265 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Transmembrane 266 286 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Topological domain 287 306 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Transmembrane 307 327 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Topological domain 328 359 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Transmembrane 360 380 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Topological domain 381 403 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Transmembrane 404 424 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Topological domain 425 431 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Transmembrane 432 452 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Topological domain 453 477 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Transmembrane 478 498 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Topological domain 499 510 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Transmembrane 511 531 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Topological domain 532 573 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38971 UniProtKB Modified residue 39 39 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32487 +P38971 UniProtKB Sequence conflict 51 51 . . . Note=D->DD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38971 UniProtKB Sequence conflict 126 126 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38971 UniProtKB Sequence conflict 260 260 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38971 UniProtKB Sequence conflict 517 517 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38971 UniProtKB Sequence conflict 548 548 . . . Note=R->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08981 1 209 +Q08981 UniProtKB Chain 1 209 . . . ID=PRO_0000268174;Note=APC/C-CDH1 modulator 1 +Q08981 UniProtKB Modified residue 48 48 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q08981 UniProtKB Modified residue 161 161 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +Q08981 UniProtKB Modified residue 202 202 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +Q08981 UniProtKB Helix 68 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +Q08981 UniProtKB Helix 95 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +Q08981 UniProtKB Helix 103 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +##sequence-region P13711 1 748 +P13711 UniProtKB Chain 1 748 . . . ID=PRO_0000204704;Note=Acyl-coenzyme A oxidase +P13711 UniProtKB Sequence conflict 443 443 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32463 1 125 +P32463 UniProtKB Transit peptide 1 36 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32463 UniProtKB Chain 37 125 . . . ID=PRO_0000000566;Note=Acyl carrier protein%2C mitochondrial +P32463 UniProtKB Domain 43 122 . . . Note=Carrier;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00258 +P32463 UniProtKB Modified residue 82 82 . . . Note=O-(pantetheine 4'-phosphoryl)serine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00258 +##sequence-region Q02336 1 434 +Q02336 UniProtKB Chain 1 434 . . . ID=PRO_0000197082;Note=Transcriptional adapter 2 +Q02336 UniProtKB Domain 60 112 . . . Note=SANT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00624 +Q02336 UniProtKB Domain 349 434 . . . Note=SWIRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00247 +Q02336 UniProtKB Zinc finger 1 48 . . . Note=ZZ-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00228 +Q02336 UniProtKB Helix 358 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ELJ +Q02336 UniProtKB Beta strand 367 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ELJ +Q02336 UniProtKB Helix 371 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ELJ +Q02336 UniProtKB Helix 384 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ELJ +Q02336 UniProtKB Helix 407 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ELJ +Q02336 UniProtKB Helix 418 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ELJ +##sequence-region P07246 1 375 +P07246 UniProtKB Transit peptide 1 27 . . . Note=Mitochondrion +P07246 UniProtKB Chain 28 375 . . . ID=PRO_0000000879;Note=Alcohol dehydrogenase 3%2C mitochondrial +P07246 UniProtKB Nucleotide binding 205 211 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07246 UniProtKB Nucleotide binding 296 298 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07246 UniProtKB Metal binding 71 71 . . . Note=Zinc 1%3B catalytic +P07246 UniProtKB Metal binding 94 94 . . . Note=Zinc 1%3B catalytic +P07246 UniProtKB Metal binding 125 125 . . . Note=Zinc 2 +P07246 UniProtKB Metal binding 128 128 . . . Note=Zinc 2 +P07246 UniProtKB Metal binding 131 131 . . . Note=Zinc 2 +P07246 UniProtKB Metal binding 139 139 . . . Note=Zinc 2 +P07246 UniProtKB Metal binding 181 181 . . . Note=Zinc 1%3B catalytic +P07246 UniProtKB Binding site 229 229 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07246 UniProtKB Binding site 234 234 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07246 UniProtKB Binding site 368 368 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07246 UniProtKB Sequence conflict 10 10 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07246 UniProtKB Sequence conflict 45 45 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25377 1 361 +P25377 UniProtKB Chain 1 361 . . . ID=PRO_0000160735;Note=NADP-dependent alcohol dehydrogenase 7 +P25377 UniProtKB Nucleotide binding 188 193 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25377 UniProtKB Nucleotide binding 276 278 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25377 UniProtKB Metal binding 46 46 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25377 UniProtKB Metal binding 68 68 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25377 UniProtKB Metal binding 100 100 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25377 UniProtKB Metal binding 103 103 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25377 UniProtKB Metal binding 106 106 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25377 UniProtKB Metal binding 114 114 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25377 UniProtKB Metal binding 164 164 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25377 UniProtKB Binding site 216 216 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25377 UniProtKB Binding site 349 349 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25377 UniProtKB Modified residue 132 132 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04894 +P25377 UniProtKB Modified residue 316 316 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region Q12184 1 172 +Q12184 UniProtKB Domain 61 163 . . . Note=2Fe-2S ferredoxin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00465 +Q12184 UniProtKB Metal binding 98 98 . . . Note=Iron-sulfur (2Fe-2S);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00465 +Q12184 UniProtKB Metal binding 104 104 . . . Note=Iron-sulfur (2Fe-2S);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00465 +Q12184 UniProtKB Metal binding 107 107 . . . Note=Iron-sulfur (2Fe-2S);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00465 +Q12184 UniProtKB Metal binding 144 144 . . . Note=Iron-sulfur (2Fe-2S);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00465 +Q12184 UniProtKB Beta strand 61 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD +Q12184 UniProtKB Beta strand 72 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD +Q12184 UniProtKB Helix 83 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD +Q12184 UniProtKB Beta strand 101 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD +Q12184 UniProtKB Beta strand 108 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD +Q12184 UniProtKB Turn 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD +Q12184 UniProtKB Turn 124 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD +Q12184 UniProtKB Helix 128 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD +Q12184 UniProtKB Beta strand 133 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD +Q12184 UniProtKB Beta strand 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD +Q12184 UniProtKB Turn 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD +Q12184 UniProtKB Helix 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJE +Q12184 UniProtKB Beta strand 156 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJD +##sequence-region P38872 1 237 +P38872 UniProtKB Chain 1 237 . . . ID=PRO_0000064460;Note=Prospore formation at selected spindle poles protein 1 +##sequence-region Q05955 1 493 +Q05955 UniProtKB Chain 1 493 . . . ID=PRO_0000064462;Note=Accumulates dyads protein 4 +##sequence-region Q12089 1 606 +Q12089 UniProtKB Chain 1 606 . . . ID=PRO_0000064466;Note=ATPase expression protein 3 +Q12089 UniProtKB Repeat 220 254 . . . Note=PPR 1 +Q12089 UniProtKB Repeat 397 432 . . . Note=PPR 2 +Q12089 UniProtKB Repeat 433 467 . . . Note=PPR 3 +##sequence-region Q99222 1 893 +Q99222 UniProtKB Chain 1 893 . . . ID=PRO_0000066256;Note=ARF3-interacting protein 1 +Q99222 UniProtKB Domain 28 335 . . . Note=uDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00304 +Q99222 UniProtKB Domain 365 492 . . . Note=cDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00304 +Q99222 UniProtKB Domain 494 640 . . . Note=dDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00304 +Q99222 UniProtKB Region 25 488 . . . Note=Interaction with active ARF3 +Q99222 UniProtKB Coiled coil 152 172 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99222 UniProtKB Coiled coil 872 892 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99222 UniProtKB Mutagenesis 38 41 . . . Note=Abolishes interaction with ARF3. KLGP->AAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18397879;Dbxref=PMID:18397879 +##sequence-region P32781 1 87 +P32781 UniProtKB Signal peptide 1 18 . . . . +P32781 UniProtKB Chain 19 87 . . . ID=PRO_0000020642;Note=A-agglutinin-binding subunit +P32781 UniProtKB Glycosylation 22 22 . . . Note=O-linked (Man...) threonine +P32781 UniProtKB Glycosylation 30 30 . . . Note=O-linked (Man...) serine +P32781 UniProtKB Glycosylation 32 32 . . . Note=O-linked (Man...) threonine +P32781 UniProtKB Glycosylation 39 39 . . . Note=O-linked (Man...) serine +P32781 UniProtKB Glycosylation 63 63 . . . Note=O-linked (Man...) threonine +P32781 UniProtKB Glycosylation 66 66 . . . Note=O-linked (Man...) serine +P32781 UniProtKB Glycosylation 75 75 . . . Note=O-linked (Man...) threonine +P32781 UniProtKB Disulfide bond 25 25 . . . Note=Interchain (with AGA1);Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32781 UniProtKB Disulfide bond 68 68 . . . Note=Interchain (with AGA1);Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32781 UniProtKB Mutagenesis 25 25 . . . Note=Abolishes agglutination%3B when associated with S-68. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7957044;Dbxref=PMID:7957044 +P32781 UniProtKB Mutagenesis 68 68 . . . Note=Abolishes agglutination%3B when associated with S-25. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7957044;Dbxref=PMID:7957044 +##sequence-region P38628 1 557 +P38628 UniProtKB Chain 1 557 . . . ID=PRO_0000148019;Note=Phosphoacetylglucosamine mutase +P38628 UniProtKB Region 395 397 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P4V2 +P38628 UniProtKB Region 522 526 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P4V2 +P38628 UniProtKB Active site 67 67 . . . Note=Phosphoserine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P4V2 +P38628 UniProtKB Metal binding 67 67 . . . Note=Magnesium%3B via phosphate group;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P4V2 +P38628 UniProtKB Metal binding 298 298 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P4V2 +P38628 UniProtKB Metal binding 300 300 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P4V2 +P38628 UniProtKB Metal binding 302 302 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P4V2 +P38628 UniProtKB Binding site 531 531 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9P4V2 +P38628 UniProtKB Modified residue 67 67 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38628 UniProtKB Sequence conflict 15 15 . . . Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38628 UniProtKB Sequence conflict 196 196 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38628 UniProtKB Sequence conflict 406 406 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P43567 1 385 +P43567 UniProtKB Chain 1 385 . . . ID=PRO_0000150239;Note=Alanine--glyoxylate aminotransferase 1 +P43567 UniProtKB Binding site 354 354 . . . Note=Substrate +P43567 UniProtKB Modified residue 201 201 . . . Note=N6-(pyridoxal phosphate)lysine +P43567 UniProtKB Beta strand 10 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Helix 18 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Helix 34 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Helix 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Beta strand 60 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Helix 70 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Beta strand 88 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Helix 96 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Beta strand 111 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Helix 126 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Beta strand 139 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Turn 148 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Helix 156 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Beta strand 170 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Turn 177 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Turn 187 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Beta strand 193 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Beta strand 209 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Helix 216 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Helix 225 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Helix 238 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Helix 261 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Helix 279 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Turn 299 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Beta strand 304 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Beta strand 309 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Beta strand 319 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Helix 326 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Turn 346 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Helix 349 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Beta strand 352 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Helix 359 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +P43567 UniProtKB Helix 369 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKW +##sequence-region Q04516 1 312 +Q04516 UniProtKB Chain 1 312 . . . ID=PRO_0000167629;Note=Uncharacterized oxidoreductase AIM33 +Q04516 UniProtKB Topological domain 1 14 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04516 UniProtKB Transmembrane 15 35 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04516 UniProtKB Topological domain 36 41 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04516 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04516 UniProtKB Topological domain 63 179 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04516 UniProtKB Transmembrane 180 200 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04516 UniProtKB Topological domain 201 312 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04516 UniProtKB Domain 70 173 . . . Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716 +##sequence-region Q12476 1 344 +Q12476 UniProtKB Chain 1 344 . . . ID=PRO_0000227604;Note=Protein AIR2 +Q12476 UniProtKB Zinc finger 61 78 . . . Note=CCHC-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +Q12476 UniProtKB Zinc finger 99 116 . . . Note=CCHC-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +Q12476 UniProtKB Zinc finger 162 179 . . . Note=CCHC-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +Q12476 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12476 UniProtKB Modified residue 49 49 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12476 UniProtKB Beta strand 19 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +Q12476 UniProtKB Helix 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +Q12476 UniProtKB Helix 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +Q12476 UniProtKB Helix 36 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +Q12476 UniProtKB Beta strand 67 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI +Q12476 UniProtKB Turn 73 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI +Q12476 UniProtKB Turn 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI +Q12476 UniProtKB Turn 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI +Q12476 UniProtKB Turn 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI +Q12476 UniProtKB Helix 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI +Q12476 UniProtKB Beta strand 101 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI +Q12476 UniProtKB Beta strand 107 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI +Q12476 UniProtKB Turn 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI +Q12476 UniProtKB Beta strand 124 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +Q12476 UniProtKB Beta strand 129 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +Q12476 UniProtKB Helix 133 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +Q12476 UniProtKB Helix 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +Q12476 UniProtKB Beta strand 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLI +Q12476 UniProtKB Beta strand 165 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +Q12476 UniProtKB Beta strand 170 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +Q12476 UniProtKB Helix 174 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +##sequence-region P21147 1 510 +P21147 UniProtKB Chain 1 510 . . . ID=PRO_0000185406;Note=Acyl-CoA desaturase 1 +P21147 UniProtKB Topological domain 1 112 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21147 UniProtKB Transmembrane 113 133 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21147 UniProtKB Topological domain 134 138 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21147 UniProtKB Transmembrane 139 159 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21147 UniProtKB Topological domain 160 255 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21147 UniProtKB Transmembrane 256 276 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21147 UniProtKB Topological domain 277 280 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21147 UniProtKB Transmembrane 281 301 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21147 UniProtKB Topological domain 302 510 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21147 UniProtKB Domain 409 487 . . . Note=Cytochrome b5 heme-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279 +P21147 UniProtKB Motif 161 166 . . . Note=Histidine box-1;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21147 UniProtKB Motif 198 202 . . . Note=Histidine box-2;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21147 UniProtKB Motif 335 339 . . . Note=Histidine box-3;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21147 UniProtKB Metal binding 161 161 . . . Note=Iron 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13516 +P21147 UniProtKB Metal binding 166 166 . . . Note=Iron 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13516 +P21147 UniProtKB Metal binding 198 198 . . . Note=Iron 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13516 +P21147 UniProtKB Metal binding 201 201 . . . Note=Iron 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13516 +P21147 UniProtKB Metal binding 202 202 . . . Note=Iron 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13516 +P21147 UniProtKB Metal binding 306 306 . . . Note=Iron 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13516 +P21147 UniProtKB Metal binding 335 335 . . . Note=Iron 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13516 +P21147 UniProtKB Metal binding 338 338 . . . Note=Iron 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13516 +P21147 UniProtKB Metal binding 339 339 . . . Note=Iron 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13516 +P21147 UniProtKB Metal binding 444 444 . . . Note=Iron (heme axial ligand);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279 +P21147 UniProtKB Metal binding 470 470 . . . Note=Iron (heme axial ligand);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279 +P21147 UniProtKB Sequence conflict 67 67 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21147 UniProtKB Sequence conflict 304 304 . . . Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P19414 1 778 +P19414 UniProtKB Transit peptide 1 16 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975908;Dbxref=PMID:15975908 +P19414 UniProtKB Chain 17 778 . . . ID=PRO_0000000547;Note=Aconitate hydratase%2C mitochondrial +P19414 UniProtKB Region 188 190 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19414 UniProtKB Region 667 668 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19414 UniProtKB Metal binding 382 382 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19414 UniProtKB Metal binding 445 445 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19414 UniProtKB Metal binding 448 448 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19414 UniProtKB Binding site 95 95 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19414 UniProtKB Binding site 471 471 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19414 UniProtKB Binding site 476 476 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19414 UniProtKB Binding site 604 604 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19414 UniProtKB Modified residue 391 391 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P19414 UniProtKB Modified residue 409 409 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P19414 UniProtKB Modified residue 556 556 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P19414 UniProtKB Mutagenesis 604 604 . . . Note=Strongly diminishes the catalytic activity towards both known substrates%2C aconitate and homoaconitate. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23106124;Dbxref=PMID:23106124 +P19414 UniProtKB Sequence conflict 527 549 . . . Note=DGLPQRGYDAGENTYQAPPADRS->RWFASKEVMMLVRTLTKLHLQTVA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03233 1 198 +Q03233 UniProtKB Chain 1 198 . . . ID=PRO_0000203321;Note=Alpha1-proteinase inhibitor-degradation deficient protein 37 +Q03233 UniProtKB Modified residue 79 79 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P32794 1 780 +P32794 UniProtKB Chain 1 780 . . . ID=PRO_0000084592;Note=ATPase family gene 2 protein +P32794 UniProtKB Nucleotide binding 286 293 . . . Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32794 UniProtKB Nucleotide binding 557 564 . . . Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12433 1 566 +Q12433 UniProtKB Chain 1 566 . . . ID=PRO_0000227804;Note=Protein AHC1 +Q12433 UniProtKB Modified residue 282 282 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12433 UniProtKB Modified residue 505 505 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +##sequence-region P38013 1 176 +P38013 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4 +P38013 UniProtKB Chain 2 176 . . . ID=PRO_0000056610;Note=Peroxiredoxin AHP1 +P38013 UniProtKB Domain 9 176 . . . Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +P38013 UniProtKB Active site 62 62 . . . Note=Cysteine sulfenic acid (-SOH) intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:22474296;Dbxref=PMID:22474296 +P38013 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4 +P38013 UniProtKB Modified residue 28 28 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38013 UniProtKB Modified residue 59 59 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38013 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38013 UniProtKB Disulfide bond 31 31 . . . Note=Interchain (with C-31 in TRX2)%3B transient;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22474296;Dbxref=PMID:22474296 +P38013 UniProtKB Disulfide bond 31 31 . . . Note=Interchain (with C-62)%3B in linked form;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4DSQ,ECO:0000244|PDB:4OWY,ECO:0000269|PubMed:22474296;Dbxref=PMID:22474296 +P38013 UniProtKB Disulfide bond 62 62 . . . Note=Interchain (with C-31)%3B in linked form;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4DSQ,ECO:0000244|PDB:4OWY,ECO:0000269|PubMed:22474296;Dbxref=PMID:22474296 +P38013 UniProtKB Cross-link 32 32 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in URM1);Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:21209336;Dbxref=PMID:21209336 +P38013 UniProtKB Cross-link 48 48 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38013 UniProtKB Cross-link 113 113 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38013 UniProtKB Mutagenesis 31 31 . . . Note=Abolishes catalytic activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22474296;Dbxref=PMID:22474296 +P38013 UniProtKB Mutagenesis 32 32 . . . Note=Prevents urmylation of AHP1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21209336;Dbxref=PMID:21209336 +P38013 UniProtKB Mutagenesis 62 62 . . . Note=Abolishes catalytic activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22474296;Dbxref=PMID:22474296 +P38013 UniProtKB Mutagenesis 120 120 . . . Note=No effect on tert-butyl hydroperoxide consumption. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22474296;Dbxref=PMID:22474296 +P38013 UniProtKB Sequence conflict 21 21 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38013 UniProtKB Sequence conflict 65 65 . . . Note=S->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38013 UniProtKB Sequence conflict 87 87 . . . Note=I->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38013 UniProtKB Turn 3 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Beta strand 15 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Beta strand 23 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Beta strand 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OWY +P38013 UniProtKB Helix 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Beta strand 35 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Helix 39 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Beta strand 47 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Helix 60 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Helix 67 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Beta strand 85 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Helix 94 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Beta strand 110 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Helix 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Helix 121 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Beta strand 129 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Beta strand 136 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Beta strand 141 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Beta strand 150 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Turn 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +P38013 UniProtKB Helix 169 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H86 +##sequence-region P03875 1 834 +P03875 UniProtKB Chain 1 834 . . . ID=PRO_0000196880;Note=Putative COX1/OXI3 intron 1 protein +P03875 UniProtKB Domain 296 577 . . . Note=Reverse transcriptase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405 +P03875 UniProtKB Sequence conflict 118 118 . . . Note=F->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03875 UniProtKB Sequence conflict 118 118 . . . Note=F->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12156 1 149 +Q12156 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12156 UniProtKB Chain 2 149 . . . ID=PRO_0000244441;Note=Protein AIM7 +Q12156 UniProtKB Domain 3 147 . . . Note=ADF-H;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00599 +Q12156 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12156 UniProtKB Modified residue 137 137 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P40507 1 360 +P40507 UniProtKB Chain 1 360 . . . ID=PRO_0000202979;Note=Protein AIR1 +P40507 UniProtKB Zinc finger 74 91 . . . Note=CCHC-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +P40507 UniProtKB Zinc finger 112 129 . . . Note=CCHC-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +P40507 UniProtKB Zinc finger 134 151 . . . Note=CCHC-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +P40507 UniProtKB Zinc finger 173 190 . . . Note=CCHC-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +P40507 UniProtKB Modified residue 37 37 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P39010 1 764 +P39010 UniProtKB Chain 1 764 . . . ID=PRO_0000212934;Note=Palmitoyltransferase AKR1 +P39010 UniProtKB Topological domain 1 321 . . . Note=Cytoplasmic +P39010 UniProtKB Transmembrane 322 341 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39010 UniProtKB Topological domain 342 346 . . . Note=Lumenal +P39010 UniProtKB Transmembrane 347 364 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39010 UniProtKB Topological domain 365 384 . . . Note=Cytoplasmic +P39010 UniProtKB Transmembrane 385 405 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39010 UniProtKB Topological domain 406 418 . . . Note=Lumenal +P39010 UniProtKB Transmembrane 419 439 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39010 UniProtKB Topological domain 440 513 . . . Note=Cytoplasmic +P39010 UniProtKB Transmembrane 514 534 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39010 UniProtKB Topological domain 535 570 . . . Note=Lumenal +P39010 UniProtKB Transmembrane 571 591 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39010 UniProtKB Topological domain 592 764 . . . Note=Cytoplasmic +P39010 UniProtKB Repeat 72 102 . . . Note=ANK 1 +P39010 UniProtKB Repeat 108 137 . . . Note=ANK 2 +P39010 UniProtKB Repeat 142 171 . . . Note=ANK 3 +P39010 UniProtKB Repeat 175 204 . . . Note=ANK 4 +P39010 UniProtKB Repeat 213 242 . . . Note=ANK 5 +P39010 UniProtKB Repeat 246 275 . . . Note=ANK 6 +P39010 UniProtKB Domain 470 520 . . . Note=DHHC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00067 +P39010 UniProtKB Active site 500 500 . . . Note=S-palmitoyl cysteine intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12370247;Dbxref=PMID:12370247 +P39010 UniProtKB Modified residue 51 51 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P39010 UniProtKB Modified residue 57 57 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P39010 UniProtKB Mutagenesis 497 498 . . . Note=Abolishes YCK2 palmitoylation. DH->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12370247;Dbxref=PMID:12370247 +P39010 UniProtKB Mutagenesis 500 500 . . . Note=Abolishes YCK2 palmitoylation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12370247;Dbxref=PMID:12370247 +##sequence-region P38207 1 520 +P38207 UniProtKB Chain 1 520 . . . ID=PRO_0000200020;Note=DNA-(apurinic or apyrimidinic site) lyase 2 +P38207 UniProtKB Active site 181 181 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38207 UniProtKB Active site 222 222 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38207 UniProtKB Metal binding 59 59 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38207 UniProtKB Metal binding 222 222 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38207 UniProtKB Metal binding 224 224 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38207 UniProtKB Metal binding 353 353 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38207 UniProtKB Site 224 224 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38207 UniProtKB Site 328 328 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38207 UniProtKB Site 354 354 . . . Note=Interaction with DNA substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38207 UniProtKB Sequence conflict 15 15 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12354 1 227 +Q12354 UniProtKB Chain 1 227 . . . ID=PRO_0000229015;Note=Acyl-protein thioesterase 1 +Q12354 UniProtKB Active site 119 119 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12354 UniProtKB Active site 173 173 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12354 UniProtKB Active site 207 207 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q08702 1 217 +Q08702 UniProtKB Chain 1 217 . . . ID=PRO_0000109802;Note=Aprataxin-like protein +Q08702 UniProtKB Domain 6 139 . . . Note=HIT +Q08702 UniProtKB Region 34 38 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74859 +Q08702 UniProtKB Region 121 132 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74859 +Q08702 UniProtKB Region 144 148 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74859 +Q08702 UniProtKB Active site 130 130 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74859 +Q08702 UniProtKB Metal binding 188 188 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74859 +Q08702 UniProtKB Metal binding 191 191 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74859 +Q08702 UniProtKB Metal binding 205 205 . . . Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74859 +Q08702 UniProtKB Metal binding 209 209 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74859 +Q08702 UniProtKB Site 10 10 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74859 +Q08702 UniProtKB Sequence conflict 80 80 . . . Note=I->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08702 UniProtKB Sequence conflict 157 157 . . . Note=F->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04212 1 335 +Q04212 UniProtKB Chain 1 335 . . . ID=PRO_0000070372;Note=D-arabinose 1-dehydrogenase +Q04212 UniProtKB Nucleotide binding 221 287 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04212 UniProtKB Active site 58 58 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04212 UniProtKB Binding site 124 124 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04212 UniProtKB Site 86 86 . . . Note=Lowers pKa of active site Tyr;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38724 1 620 +P38724 UniProtKB Chain 1 620 . . . ID=PRO_0000084863;Note=Siderophore iron transporter ARN2 +P38724 UniProtKB Transmembrane 71 93 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38724 UniProtKB Transmembrane 106 128 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38724 UniProtKB Transmembrane 135 152 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38724 UniProtKB Transmembrane 162 184 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38724 UniProtKB Transmembrane 191 213 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38724 UniProtKB Transmembrane 223 245 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38724 UniProtKB Transmembrane 286 308 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38724 UniProtKB Transmembrane 318 335 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38724 UniProtKB Transmembrane 355 377 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38724 UniProtKB Transmembrane 392 414 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38724 UniProtKB Transmembrane 421 438 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38724 UniProtKB Transmembrane 448 470 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38724 UniProtKB Transmembrane 491 513 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38724 UniProtKB Transmembrane 561 578 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38840 1 513 +P38840 UniProtKB Chain 1 513 . . . ID=PRO_0000064679;Note=Aromatic amino acid aminotransferase 2 +P38840 UniProtKB Modified residue 90 90 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38840 UniProtKB Modified residue 92 92 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38840 UniProtKB Sequence conflict 460 460 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04549 1 284 +Q04549 UniProtKB Chain 1 284 . . . ID=PRO_0000089130;Note=Actin-like protein ARP10 +##sequence-region P80428 1 489 +P80428 UniProtKB Chain 1 489 . . . ID=PRO_0000089103;Note=Actin-related protein 4 +P80428 UniProtKB Modified residue 349 349 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P80428 UniProtKB Mutagenesis 23 23 . . . Note=Lethal%3B when associated with D-161. Formamide-%2C hydroxyurea and UV-hypersensitivity%2C suppressor of TY phenotype%3B when associated with A-159. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14622406;Dbxref=PMID:14622406 +P80428 UniProtKB Mutagenesis 155 155 . . . Note=No histone acetyltransferase activity at 37 degrees Celsius. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10911987;Dbxref=PMID:10911987 +P80428 UniProtKB Mutagenesis 159 159 . . . Note=Formamide-%2C hydroxyurea and UV-hypersensitivity%2C suppressor of TY phenotype%3B when associated with S-23. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14622406;Dbxref=PMID:14622406 +P80428 UniProtKB Mutagenesis 161 161 . . . Note=Formamide-%2C hydroxyurea and UV-hypersensitivity%2C destabilization of ARP4%2C suppressor of TY phenotype and elevated levels of MSN2/MSN4-regulated genes. Lethal%3B when associated with A-23. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14622406;Dbxref=PMID:14622406 +P80428 UniProtKB Mutagenesis 187 187 . . . Note=Defect in promoter association and change in chromatin structure. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11937627;Dbxref=PMID:11937627 +P80428 UniProtKB Mutagenesis 455 455 . . . Note=No histone acetyltransferase activity at 37 degrees Celsius. Defect in promoter association and change in chromatin structure. G->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10911987,ECO:0000269|PubMed:11937627;Dbxref=PMID:10911987,PMID:11937627 +P80428 UniProtKB Beta strand 9 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Beta strand 17 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Beta strand 23 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Beta strand 37 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Helix 59 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Beta strand 67 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Beta strand 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Helix 83 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Beta strand 107 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Helix 118 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Beta strand 135 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Helix 142 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Beta strand 153 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Beta strand 165 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Helix 177 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QB0 +P80428 UniProtKB Beta strand 181 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Helix 187 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Turn 198 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QB0 +P80428 UniProtKB Beta strand 209 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Beta strand 213 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Helix 227 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Helix 238 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Helix 254 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Helix 258 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Beta strand 268 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QB0 +P80428 UniProtKB Beta strand 273 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QB0 +P80428 UniProtKB Beta strand 277 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QB0 +P80428 UniProtKB Helix 282 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Turn 291 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Turn 297 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Beta strand 308 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QB0 +P80428 UniProtKB Helix 385 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Helix 398 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Beta strand 408 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Helix 413 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Helix 420 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Helix 446 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Helix 451 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Helix 463 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Beta strand 469 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QB0 +P80428 UniProtKB Helix 472 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +P80428 UniProtKB Turn 479 485 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +##sequence-region P40467 1 964 +P40467 UniProtKB Chain 1 964 . . . ID=PRO_0000114997;Note=Activator of stress genes 1 +P40467 UniProtKB DNA binding 21 47 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P40467 UniProtKB Compositional bias 832 837 . . . Note=Poly-Asn +P40467 UniProtKB Compositional bias 840 869 . . . Note=Poly-Asn +P40467 UniProtKB Compositional bias 875 887 . . . Note=Poly-Asn +P40467 UniProtKB Modified residue 166 166 . . . Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40467 UniProtKB Modified residue 186 186 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40467 UniProtKB Modified residue 963 963 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40467 UniProtKB Natural variant 77 77 . . . Note=In strain: SK1. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P40467 UniProtKB Natural variant 149 149 . . . Note=In strain: SK1. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P40467 UniProtKB Natural variant 353 353 . . . Note=In strain: SK1. I->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P40467 UniProtKB Natural variant 682 682 . . . Note=In strain: SK1. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P40467 UniProtKB Natural variant 707 707 . . . Note=In strain: SK1. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P40467 UniProtKB Natural variant 770 770 . . . Note=In strain: SK1. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P40467 UniProtKB Natural variant 811 811 . . . Note=In strain: SK1. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P40467 UniProtKB Natural variant 852 852 . . . Note=In strain: SK1. D->NDNNN +P40467 UniProtKB Natural variant 887 887 . . . Note=In strain: SK1. N->NN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P40467 UniProtKB Natural variant 926 933 . . . Note=In strain: SK1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +##sequence-region P34233 1 588 +P34233 UniProtKB Chain 1 588 . . . ID=PRO_0000083492;Note=Transcriptional regulatory protein ASH1 +P34233 UniProtKB Zinc finger 499 526 . . . Note=GATA-type%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00094 +P34233 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34233 UniProtKB Modified residue 465 465 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q06834 1 288 +Q06834 UniProtKB Chain 1 288 . . . ID=PRO_0000055760;Note=Alcohol-sensitive RING finger protein 1 +Q06834 UniProtKB Zinc finger 4 48 . . . Note=RING-type 1%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +Q06834 UniProtKB Zinc finger 121 168 . . . Note=RING-type 2%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +##sequence-region P49435 1 187 +P49435 UniProtKB Chain 1 187 . . . ID=PRO_0000149517;Note=Adenine phosphoribosyltransferase 1 +P49435 UniProtKB Nucleotide binding 133 137 . . . Note=AMP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P49435 UniProtKB Modified residue 68 68 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P49435 UniProtKB Mutagenesis 69 69 . . . Note=4-fold decrease in activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055 +P49435 UniProtKB Mutagenesis 89 89 . . . Note=2-fold decrease in activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055 +P49435 UniProtKB Mutagenesis 90 90 . . . Note=30-fold decrease in activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055 +P49435 UniProtKB Mutagenesis 93 93 . . . Note=Small increase in activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055 +P49435 UniProtKB Mutagenesis 103 103 . . . Note=4-fold increase in activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055 +P49435 UniProtKB Mutagenesis 106 106 . . . Note=1 million-fold decrease in activity. E->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055 +P49435 UniProtKB Mutagenesis 106 106 . . . Note=2-fold decrease in activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055 +P49435 UniProtKB Mutagenesis 107 107 . . . Note=2/3-fold decrease in activity. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055 +P49435 UniProtKB Mutagenesis 107 107 . . . Note=Small decrease in activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055 +P49435 UniProtKB Mutagenesis 108 108 . . . Note=Small decrease in activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055 +P49435 UniProtKB Mutagenesis 108 108 . . . Note=2/3-fold decrease in activity. G->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11535055;Dbxref=PMID:11535055 +P49435 UniProtKB Sequence conflict 37 37 . . . Note=P->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P49435 UniProtKB Helix 2 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q +P49435 UniProtKB Beta strand 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q +P49435 UniProtKB Beta strand 27 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q +P49435 UniProtKB Helix 31 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q +P49435 UniProtKB Helix 37 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q +P49435 UniProtKB Beta strand 62 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q +P49435 UniProtKB Turn 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q +P49435 UniProtKB Helix 70 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q +P49435 UniProtKB Beta strand 84 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q +P49435 UniProtKB Beta strand 96 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q +P49435 UniProtKB Beta strand 109 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q +P49435 UniProtKB Beta strand 124 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q +P49435 UniProtKB Helix 136 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q +P49435 UniProtKB Beta strand 151 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q +P49435 UniProtKB Helix 162 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2P +P49435 UniProtKB Helix 166 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2P +P49435 UniProtKB Beta strand 174 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G2Q +##sequence-region P07347 1 238 +P07347 UniProtKB Chain 1 238 . . . ID=PRO_0000074529;Note=N-terminal acetyltransferase A complex catalytic subunit ARD1 +P07347 UniProtKB Domain 35 195 . . . Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532 +P07347 UniProtKB Sequence conflict 37 37 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07347 UniProtKB Beta strand 3 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Helix 10 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Helix 13 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Helix 27 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY +P07347 UniProtKB Helix 30 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Turn 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Beta strand 45 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Helix 66 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY +P07347 UniProtKB Turn 70 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY +P07347 UniProtKB Beta strand 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Beta strand 90 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Helix 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNX +P07347 UniProtKB Beta strand 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNW +P07347 UniProtKB Beta strand 112 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Helix 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Beta strand 126 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Helix 129 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Beta strand 148 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Helix 159 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Turn 167 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Beta strand 172 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Beta strand 187 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Helix 196 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Helix 201 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P07347 UniProtKB Turn 205 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY +P07347 UniProtKB Beta strand 220 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY +P07347 UniProtKB Helix 224 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY +##sequence-region P18544 1 423 +P18544 UniProtKB Modified residue 276 276 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53974 1 638 +P53974 UniProtKB Chain 1 638 . . . ID=PRO_0000085635;Note=Actin-regulating kinase 1 +P53974 UniProtKB Domain 22 298 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53974 UniProtKB Nucleotide binding 28 36 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53974 UniProtKB Region 602 615 . . . Note=Interaction with SH3 domain of ABP1 +P53974 UniProtKB Active site 159 159 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P53974 UniProtKB Binding site 56 56 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53974 UniProtKB Modified residue 478 478 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P53974 UniProtKB Modified residue 522 522 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53974 UniProtKB Modified residue 535 535 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53974 UniProtKB Mutagenesis 56 56 . . . Note=Abolishes protein kinase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10087264;Dbxref=PMID:10087264 +##sequence-region P38116 1 183 +P38116 UniProtKB Initiator methionine 1 1 . . . Note=Removed +P38116 UniProtKB Chain 2 183 . . . ID=PRO_0000207421;Note=ADP-ribosylation factor-like protein 1 +P38116 UniProtKB Nucleotide binding 25 32 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38116 UniProtKB Nucleotide binding 68 72 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38116 UniProtKB Nucleotide binding 127 130 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38116 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9388248;Dbxref=PMID:9388248 +P38116 UniProtKB Helix 3 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ +P38116 UniProtKB Helix 10 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ +P38116 UniProtKB Beta strand 19 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ +P38116 UniProtKB Helix 31 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ +P38116 UniProtKB Beta strand 41 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ +P38116 UniProtKB Beta strand 54 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ +P38116 UniProtKB Beta strand 62 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ +P38116 UniProtKB Helix 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ +P38116 UniProtKB Turn 82 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ +P38116 UniProtKB Beta strand 86 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ +P38116 UniProtKB Turn 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ +P38116 UniProtKB Helix 101 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ +P38116 UniProtKB Beta strand 121 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ +P38116 UniProtKB Helix 137 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ +P38116 UniProtKB Turn 144 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ +P38116 UniProtKB Beta strand 154 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ +P38116 UniProtKB Helix 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ +P38116 UniProtKB Helix 167 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MOZ +##sequence-region P38696 1 384 +P38696 UniProtKB Chain 1 384 . . . ID=PRO_0000089066;Note=Centractin +P38696 UniProtKB Mutagenesis 2 2 . . . Note=Temperature-sensitive%3B when associated with A-6. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903 +P38696 UniProtKB Mutagenesis 6 6 . . . Note=Temperature-sensitive%3B when associated with A-2. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903 +P38696 UniProtKB Mutagenesis 46 46 . . . Note=Strongly reduces interaction with JNM1. Reduces nuclear migration in mitosis%3B when associated with 48-A-A-49. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535 +P38696 UniProtKB Mutagenesis 48 49 . . . Note=Strongly reduces interaction with JNM1. Reduces nuclear migration in mitosis%3B when associated with A-46. DK->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535 +P38696 UniProtKB Mutagenesis 73 73 . . . Note=Reduces spindle formation%3B when associated with A-75. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535 +P38696 UniProtKB Mutagenesis 75 75 . . . Note=Reduces spindle formation%3B when associated with A-73. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535 +P38696 UniProtKB Mutagenesis 79 80 . . . Note=Reduces nuclear migration in mitosis. KH->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535 +P38696 UniProtKB Mutagenesis 84 85 . . . Note=Reduces spindle formation. Strongly reduces interaction with JNM1. Reduces nuclear migration in mitosis%3B when associated with A-87. ED->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535 +P38696 UniProtKB Mutagenesis 87 87 . . . Note=Reduces spindle formation. Reduces nuclear migration in mitosis%3B when associated with 84-A-A-85. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535 +P38696 UniProtKB Mutagenesis 108 109 . . . Note=Reduces nuclear migration in mitosis. EH->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535 +P38696 UniProtKB Mutagenesis 133 133 . . . Note=Lethal. Strongly reduces interaction with JNM1%3B when associated with A-136. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903 +P38696 UniProtKB Mutagenesis 136 136 . . . Note=Lethal. Strongly reduces interaction with JNM1%3B when associated with A-133. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903 +P38696 UniProtKB Mutagenesis 162 162 . . . Note=Reduces spindle formation. Reduces nuclear migration in mitosis%3B when associated with A-165. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535 +P38696 UniProtKB Mutagenesis 165 165 . . . Note=Reduces spindle formation. Reduces nuclear migration in mitosis%3B when associated with A-162. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535 +P38696 UniProtKB Mutagenesis 185 185 . . . Note=Temperature-sensitive. Strongly reduces interaction with JNM1%3B when associated with A-187. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903 +P38696 UniProtKB Mutagenesis 187 187 . . . Note=Temperature-sensitive. Strongly reduces interaction with JNM1%3B when associated with A-185. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903 +P38696 UniProtKB Mutagenesis 214 216 . . . Note=Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis. Alters complex assembly%3B when associated with A-219. ERE->AAA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535 +P38696 UniProtKB Mutagenesis 219 219 . . . Note=Lethal%3B when associated with 214-A--A-216. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903 +P38696 UniProtKB Mutagenesis 222 224 . . . Note=Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis. KEK->AAA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535 +P38696 UniProtKB Mutagenesis 233 238 . . . Note=Temperature-sensitive. Strongly reduces interaction with JNM1. KKEEEK->AAAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903 +P38696 UniProtKB Mutagenesis 233 235 . . . Note=Reduces spindle formation. KKE->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535 +P38696 UniProtKB Mutagenesis 236 238 . . . Note=Reduces spindle formation. EEK->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535 +P38696 UniProtKB Mutagenesis 251 251 . . . Note=Lethal and dominant cold-sensitive. Reduces nuclear migration in mitosis%3B when associated with A-254. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535 +P38696 UniProtKB Mutagenesis 254 254 . . . Note=Lethal and dominant cold-sensitive. Reduces nuclear migration in mitosis%3B when associated with A-251. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535 +P38696 UniProtKB Mutagenesis 263 264 . . . Note=Reduces spindle formation. DR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535 +P38696 UniProtKB Mutagenesis 266 266 . . . Note=Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis%3B when associated with A-269. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535 +P38696 UniProtKB Mutagenesis 269 269 . . . Note=Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis%3B when associated with A-266. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535 +P38696 UniProtKB Mutagenesis 294 294 . . . Note=Reduces nuclear migration in mitosis%3B when associated with A-296 and A-298. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535 +P38696 UniProtKB Mutagenesis 296 296 . . . Note=Reduces nuclear migration in mitosis%3B when associated with A-294 and A-298. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535 +P38696 UniProtKB Mutagenesis 298 298 . . . Note=Reduces nuclear migration in mitosis%3B when associated with A-294 and A-296. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535 +P38696 UniProtKB Mutagenesis 321 322 . . . Note=Lethal. Strongly reduces interaction with JNM1. DR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903 +P38696 UniProtKB Mutagenesis 326 326 . . . Note=Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1%3B when associated with A-328. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535 +P38696 UniProtKB Mutagenesis 328 328 . . . Note=Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1%3B when associated with A-326. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535 +P38696 UniProtKB Mutagenesis 336 336 . . . Note=Strongly reduces interaction with JNM1%3B when associated with A-338. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903 +P38696 UniProtKB Mutagenesis 338 338 . . . Note=Strongly reduces interaction with JNM1%3B when associated with A-336. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903 +P38696 UniProtKB Mutagenesis 344 346 . . . Note=Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1. ERK->AAA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535 +P38696 UniProtKB Mutagenesis 368 369 . . . Note=Reduces nuclear migration in mitosis%3B when associated with A-371. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16415535;Dbxref=PMID:16415535 +P38696 UniProtKB Mutagenesis 369 369 . . . Note=Lethal. Strongly reduces interaction with JNM1%3B when associated with A-371. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903 +P38696 UniProtKB Mutagenesis 371 371 . . . Note=Lethal. Strongly reduces interaction with JNM1%3B when associated with A-369. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535 +P38696 UniProtKB Mutagenesis 371 371 . . . Note=Reduces nuclear migration in mitosis%3B when associated with 368-A-A-369. D->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15975903,ECO:0000269|PubMed:16415535;Dbxref=PMID:15975903,PMID:16415535 +P38696 UniProtKB Mutagenesis 374 375 . . . Note=Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1%3B when associated with A-378. ED->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903 +P38696 UniProtKB Mutagenesis 378 378 . . . Note=Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1%3B when associated with 374-A-A-375. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15975903;Dbxref=PMID:15975903 +P38696 UniProtKB Sequence conflict 3 3 . . . Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06597 1 130 +Q06597 UniProtKB Chain 1 130 . . . ID=PRO_0000064439;Note=Arsenical-resistance protein 2 +Q06597 UniProtKB Domain 17 124 . . . Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173 +##sequence-region P40994 1 183 +P40994 UniProtKB Initiator methionine 1 1 . . . Note=Removed +P40994 UniProtKB Chain 2 183 . . . ID=PRO_0000207420;Note=ADP-ribosylation factor 3 +P40994 UniProtKB Nucleotide binding 24 31 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40994 UniProtKB Nucleotide binding 67 71 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40994 UniProtKB Nucleotide binding 126 129 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40994 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q04728 1 441 +Q04728 UniProtKB Transit peptide 1 8 . . . Note=Mitochondrion;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03124,ECO:0000269|PubMed:7705341;Dbxref=PMID:7705341 +Q04728 UniProtKB Chain 9 214 . . . ID=PRO_0000002283;Note=Arginine biosynthesis bifunctional protein ArgJ alpha chain;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124 +Q04728 UniProtKB Chain 215 441 . . . ID=PRO_0000002284;Note=Arginine biosynthesis bifunctional protein ArgJ beta chain;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124 +Q04728 UniProtKB Active site 215 215 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124 +Q04728 UniProtKB Binding site 177 177 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124 +Q04728 UniProtKB Binding site 204 204 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124 +Q04728 UniProtKB Binding site 215 215 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124 +Q04728 UniProtKB Binding site 301 301 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124 +Q04728 UniProtKB Binding site 436 436 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124 +Q04728 UniProtKB Binding site 441 441 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124 +Q04728 UniProtKB Site 136 136 . . . Note=Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124 +Q04728 UniProtKB Site 137 137 . . . Note=Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03124 +Q04728 UniProtKB Site 214 215 . . . Note=Cleavage%3B by autolysis +Q04728 UniProtKB Mutagenesis 215 215 . . . Note=Blocks autocatalytic processing of the precursor protein. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10753950;Dbxref=PMID:10753950 +##sequence-region P07249 1 177 +P07249 UniProtKB Chain 1 177 . . . ID=PRO_0000199438;Note=Arginine metabolism regulation protein I +P07249 UniProtKB Domain 80 134 . . . Note=MADS-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00251 +P07249 UniProtKB Mutagenesis 94 94 . . . Note=Decreases the physical interaction with ARG82. Abolishes the physical interaction with ARG82 and impairs function%3B when associated with D-95 and R-103. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10632874;Dbxref=PMID:10632874 +P07249 UniProtKB Mutagenesis 95 95 . . . Note=Decreases the physical interaction with ARG82. Abolishes the physical interaction with ARG82 and impairs function%3B when associated with G-94 and R-103. H->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10632874;Dbxref=PMID:10632874 +P07249 UniProtKB Mutagenesis 103 103 . . . Note=Abolishes the physical interaction with ARG82 and impairs function%3B when associated with G-94 and D-95. H->R +P07249 UniProtKB Mutagenesis 109 109 . . . Note=Decreases the physical interaction with ARG82. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10632874;Dbxref=PMID:10632874 +P07249 UniProtKB Mutagenesis 115 115 . . . Note=Decreases the physical interaction with ARG82. L->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10632874;Dbxref=PMID:10632874 +P07249 UniProtKB Mutagenesis 148 148 . . . Note=Decreases the physical interaction with ARG82. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10632874;Dbxref=PMID:10632874 +##sequence-region P38731 1 627 +P38731 UniProtKB Chain 1 627 . . . ID=PRO_0000084862;Note=Siderophore iron transporter ARN1 +P38731 UniProtKB Topological domain 1 70 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Transmembrane 71 91 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Topological domain 92 110 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Transmembrane 111 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Topological domain 132 135 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Topological domain 157 167 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Transmembrane 168 188 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Topological domain 189 197 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Transmembrane 198 218 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Topological domain 219 231 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Transmembrane 232 252 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Topological domain 253 290 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Transmembrane 291 311 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Topological domain 312 323 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Transmembrane 324 344 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Topological domain 345 367 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Transmembrane 368 388 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Topological domain 389 398 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Transmembrane 399 419 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Topological domain 420 424 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Transmembrane 425 445 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Topological domain 446 454 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Transmembrane 455 475 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Topological domain 476 563 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Transmembrane 564 584 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38731 UniProtKB Topological domain 585 627 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53090 1 500 +P53090 UniProtKB Chain 1 500 . . . ID=PRO_0000064678;Note=Aromatic/aminoadipate aminotransferase 1 +P53090 UniProtKB Modified residue 100 100 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53090 UniProtKB Helix 10 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 15 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 24 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Turn 30 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Beta strand 37 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Beta strand 53 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Beta strand 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Beta strand 78 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 89 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 99 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 112 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Beta strand 133 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 141 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Beta strand 158 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 167 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Beta strand 179 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 192 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Beta strand 211 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Turn 220 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 228 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Beta strand 244 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 252 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 263 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 277 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 288 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Beta strand 293 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Beta strand 297 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Turn 304 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 309 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Beta strand 314 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 320 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Turn 332 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 339 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Beta strand 395 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 406 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Turn 410 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 420 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 441 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 456 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Beta strand 466 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +P53090 UniProtKB Helix 478 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE5 +##sequence-region P32449 1 370 +P32449 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32449 UniProtKB Chain 2 370 . . . ID=PRO_0000140851;Note=Phospho-2-dehydro-3-deoxyheptonate aldolase%2C tyrosine-inhibited +P32449 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32449 UniProtKB Beta strand 25 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Helix 34 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Helix 45 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Beta strand 68 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Helix 81 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Turn 99 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Beta strand 102 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Beta strand 115 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Turn 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Beta strand 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Helix 134 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Turn 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Beta strand 155 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Beta strand 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Helix 165 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Helix 169 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Beta strand 173 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Turn 179 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Helix 185 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Beta strand 198 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Helix 209 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Beta strand 223 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Beta strand 231 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Beta strand 244 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Helix 259 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Beta strand 276 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Helix 282 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Helix 289 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Helix 292 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Beta strand 309 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Beta strand 319 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Helix 330 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF6 +P32449 UniProtKB Beta strand 339 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +P32449 UniProtKB Helix 347 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF8 +##sequence-region P53946 1 755 +P53946 UniProtKB Chain 1 755 . . . ID=PRO_0000089104;Note=Actin-related protein 5 +P53946 UniProtKB Modified residue 7 7 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53946 UniProtKB Modified residue 24 24 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53946 UniProtKB Modified residue 383 383 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53946 UniProtKB Cross-link 12 12 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q12386 1 881 +Q12386 UniProtKB Chain 1 881 . . . ID=PRO_0000089128;Note=Actin-like protein ARP8 +Q12386 UniProtKB Nucleotide binding 502 505 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12386 UniProtKB Compositional bias 22 27 . . . Note=Poly-Asp +Q12386 UniProtKB Modified residue 65 65 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12386 UniProtKB Modified residue 70 70 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12386 UniProtKB Helix 265 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 268 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 275 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 285 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 289 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 295 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 299 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 305 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 321 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 352 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM7 +Q12386 UniProtKB Beta strand 357 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 367 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 386 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Turn 394 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 397 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 402 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 418 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 434 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 442 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 449 454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 460 472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 477 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 484 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 498 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 508 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 520 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 524 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 530 543 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 556 569 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 574 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 579 586 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 589 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 593 602 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 603 609 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 610 612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 615 619 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 628 631 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Turn 640 642 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 651 657 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 662 664 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 668 686 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 703 716 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 720 722 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 723 727 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 730 734 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 735 738 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM7 +Q12386 UniProtKB Helix 742 753 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Turn 757 759 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 763 778 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Beta strand 786 788 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Turn 793 797 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM7 +Q12386 UniProtKB Helix 798 817 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 838 840 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 841 849 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 853 858 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 862 868 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +Q12386 UniProtKB Helix 869 874 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AM6 +##sequence-region Q05123 1 467 +Q05123 UniProtKB Chain 1 467 . . . ID=PRO_0000089129;Note=Actin-like protein ARP9 +Q05123 UniProtKB Mutagenesis 337 337 . . . Note=Impaired heterodimerization with ARP7%3B when associated with L-338. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12805231;Dbxref=PMID:12805231 +Q05123 UniProtKB Mutagenesis 338 338 . . . Note=Impaired heterodimerization with ARP7%3B when associated with V-337. G->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12805231;Dbxref=PMID:12805231 +Q05123 UniProtKB Helix 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Beta strand 10 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Beta strand 16 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Beta strand 27 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Beta strand 35 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Beta strand 41 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Beta strand 51 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Helix 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Beta strand 62 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Beta strand 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Helix 76 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Turn 101 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Beta strand 111 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Helix 121 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Beta strand 139 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Helix 145 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Beta strand 157 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Beta strand 169 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Turn 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Beta strand 185 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Helix 191 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Helix 207 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Helix 224 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE +Q05123 UniProtKB Beta strand 229 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE +Q05123 UniProtKB Beta strand 251 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE +Q05123 UniProtKB Helix 276 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Beta strand 282 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Beta strand 291 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Helix 296 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Helix 303 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Helix 323 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Beta strand 333 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Helix 338 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Helix 345 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Helix 363 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Helix 379 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE +Q05123 UniProtKB Beta strand 401 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Helix 417 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Turn 425 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Helix 428 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Beta strand 448 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Helix 451 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q05123 UniProtKB Helix 458 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +##sequence-region P38328 1 384 +P38328 UniProtKB Chain 1 384 . . . ID=PRO_0000050859;Note=Actin-related protein 2/3 complex subunit 1 +P38328 UniProtKB Repeat 61 99 . . . Note=WD 1 +P38328 UniProtKB Repeat 105 146 . . . Note=WD 2 +P38328 UniProtKB Repeat 151 190 . . . Note=WD 3 +P38328 UniProtKB Repeat 212 251 . . . Note=WD 4 +P38328 UniProtKB Repeat 349 383 . . . Note=WD 5 +##sequence-region P53731 1 342 +P53731 UniProtKB Chain 1 342 . . . ID=PRO_0000124041;Note=Actin-related protein 2/3 complex subunit 2 +P53731 UniProtKB Modified residue 155 155 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53731 UniProtKB Modified residue 324 324 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P32447 1 279 +P32447 UniProtKB Chain 1 279 . . . ID=PRO_0000064695;Note=Histone chaperone ASF1 +P32447 UniProtKB Region 1 155 . . . Note=Interaction with histone H3%2C histone H4%2C RAD53 and the RF-C complex +P32447 UniProtKB Region 1 143 . . . Note=Interaction with HIR1 +P32447 UniProtKB Coiled coil 192 243 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32447 UniProtKB Compositional bias 170 242 . . . Note=Asp/Glu-rich (highly acidic) +P32447 UniProtKB Mutagenesis 6 6 . . . Note=Enhances transcriptional silencing. L->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17081973;Dbxref=PMID:17081973 +P32447 UniProtKB Mutagenesis 36 37 . . . Note=Abrogates stimulation of replication-independent chromatin assembly by the HIR complex and abrogates telomeric silencing. HD->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14680630,ECO:0000269|PubMed:16303565;Dbxref=PMID:14680630,PMID:16303565 +P32447 UniProtKB Mutagenesis 37 37 . . . Note=Reduces transcriptional silencing%3B when associated with R-39. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15840725;Dbxref=PMID:15840725 +P32447 UniProtKB Mutagenesis 39 39 . . . Note=Reduces transcriptional silencing%3B when associated with R-37. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15840725;Dbxref=PMID:15840725 +P32447 UniProtKB Mutagenesis 45 45 . . . Note=Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to camptothecin. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16627621;Dbxref=PMID:16627621 +P32447 UniProtKB Mutagenesis 48 48 . . . Note=Abrogates interaction with histone H3 and histone H4 and enhances transcriptional silencing. Reduces acetylation of histone H3 on 'K-9' and 'K-56'%3B when associated with E-145 or E-147. S->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17081973,ECO:0000269|PubMed:17107956;Dbxref=PMID:17081973,PMID:17107956 +P32447 UniProtKB Mutagenesis 53 54 . . . Note=Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to camptothecin. HD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16627621;Dbxref=PMID:16627621 +P32447 UniProtKB Mutagenesis 54 54 . . . Note=Reduces transcriptional silencing. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15840725;Dbxref=PMID:15840725 +P32447 UniProtKB Mutagenesis 94 94 . . . Note=Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin%2C camptothecin%2C HU and MMS%3B when associated with D-96. V->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15840725,ECO:0000269|PubMed:16627621,ECO:0000269|PubMed:17081973,ECO:0000269|PubMed:17107956;Dbxref=PMID:15840725,PMID:16627621,PMID:17081973,PMID:17107956 +P32447 UniProtKB Mutagenesis 94 94 . . . Note=Abrogates interaction with histone H3 and histone H4%2C abrogates transcriptional silencing%2C reduces acetylation of histone H3 on 'K-9' and 'K-56' and enhances sensitivity to HU and MMS. V->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15840725,ECO:0000269|PubMed:16627621,ECO:0000269|PubMed:17081973,ECO:0000269|PubMed:17107956;Dbxref=PMID:15840725,PMID:16627621,PMID:17081973,PMID:17107956 +P32447 UniProtKB Mutagenesis 96 96 . . . Note=Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin%2C camptothecin%2C HU and MMS%3B when associated with D-94. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16627621;Dbxref=PMID:16627621 +P32447 UniProtKB Mutagenesis 108 108 . . . Note=Reduces transcriptional silencing. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15840725;Dbxref=PMID:15840725 +P32447 UniProtKB Mutagenesis 109 109 . . . Note=Reduces interaction with histone H3 and histone H4%2C enhances transcriptional silencing and reduces transcriptional activation. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17081973;Dbxref=PMID:17081973 +P32447 UniProtKB Mutagenesis 112 112 . . . Note=Abrogates interaction with histone H3 and histone H4 and enhances transcriptional silencing. Abrogates transcriptional silencing%2C reduces transcriptional activation%2C reduces acetylation of histone H3 on 'K-9' and 'K-56' and enhances sensitivity to HU and MMS%3B when associated with E-145 or E-147. Y->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16627621,ECO:0000269|PubMed:17081973,ECO:0000269|PubMed:17107956;Dbxref=PMID:16627621,PMID:17081973,PMID:17107956 +P32447 UniProtKB Mutagenesis 112 112 . . . Note=Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin%2C camptothecin%2C HU and MMS. Y->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16627621,ECO:0000269|PubMed:17081973,ECO:0000269|PubMed:17107956;Dbxref=PMID:16627621,PMID:17081973,PMID:17107956 +P32447 UniProtKB Mutagenesis 145 145 . . . Note=Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin%2C camptothecin%2C HU and MMS%3B when associated with A-147. R->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16627621,ECO:0000269|PubMed:17081973,ECO:0000269|PubMed:17107956;Dbxref=PMID:16627621,PMID:17081973,PMID:17107956 +P32447 UniProtKB Mutagenesis 145 145 . . . Note=Abrogates interaction with histone H3 and histone H4%2C abrogates transcriptional silencing%2C reduces transcriptional activation%2C reduces acetylation of histone H3 on 'K-9' and 'K-56' and enhances sensitivity to HU and MMS%3B when associated with R-48%3B E-112 or E-147. R->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16627621,ECO:0000269|PubMed:17081973,ECO:0000269|PubMed:17107956;Dbxref=PMID:16627621,PMID:17081973,PMID:17107956 +P32447 UniProtKB Mutagenesis 146 146 . . . Note=Reduces interaction with histone H3 and histone H4%2C enhances transcriptional silencing and reduces transcriptional activation. V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17081973;Dbxref=PMID:17081973 +P32447 UniProtKB Mutagenesis 147 147 . . . Note=Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin%2C camptothecin%2C HU and MMS%3B when associated with A-145. T->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16627621,ECO:0000269|PubMed:17081973,ECO:0000269|PubMed:17107956;Dbxref=PMID:16627621,PMID:17081973,PMID:17107956 +P32447 UniProtKB Mutagenesis 147 147 . . . Note=Enhances transcriptional silencing. Abrogates interaction with histone H3 and histone H4%2C abrogates transcriptional silencing%2C reduces transcriptional activation%2C reduces acetylation of histone H3 on 'K-9' and 'K-56' and enhances sensitivity to HU and MMS%3B when associated with R-48%3B A-112 or E-145. T->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16627621,ECO:0000269|PubMed:17081973,ECO:0000269|PubMed:17107956;Dbxref=PMID:16627621,PMID:17081973,PMID:17107956 +P32447 UniProtKB Mutagenesis 152 152 . . . Note=Impairs interaction with histone H3 and RAD53 and enhances silencing at telomeres and mating-type loci. V->VVFLHY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16582440;Dbxref=PMID:16582440 +P32447 UniProtKB Beta strand 3 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC +P32447 UniProtKB Beta strand 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC +P32447 UniProtKB Beta strand 22 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC +P32447 UniProtKB Beta strand 38 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC +P32447 UniProtKB Helix 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HUE +P32447 UniProtKB Beta strand 55 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC +P32447 UniProtKB Beta strand 67 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC +P32447 UniProtKB Helix 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC +P32447 UniProtKB Helix 87 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC +P32447 UniProtKB Beta strand 93 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC +P32447 UniProtKB Beta strand 104 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC +P32447 UniProtKB Helix 120 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC +P32447 UniProtKB Helix 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC +P32447 UniProtKB Beta strand 135 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC +P32447 UniProtKB Beta strand 145 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ROC +P32447 UniProtKB Turn 155 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HUE +##sequence-region P38986 1 381 +P38986 UniProtKB Chain 1 381 . . . ID=PRO_0000171091;Note=L-asparaginase 1 +P38986 UniProtKB Domain 54 378 . . . Note=Asparaginase/glutaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01068 +P38986 UniProtKB Region 141 142 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38986 UniProtKB Active site 64 64 . . . Note=O-isoaspartyl threonine intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10099,ECO:0000255|PROSITE-ProRule:PRU10100 +P38986 UniProtKB Binding site 110 110 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38986 UniProtKB Modified residue 350 350 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38986 UniProtKB Mutagenesis 176 176 . . . Note=Almost no activity. A->V +##sequence-region P40024 1 610 +P40024 UniProtKB Chain 1 610 . . . ID=PRO_0000093463;Note=ABC transporter ATP-binding protein ARB1 +P40024 UniProtKB Domain 82 323 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P40024 UniProtKB Domain 393 610 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P40024 UniProtKB Nucleotide binding 114 121 . . . Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P40024 UniProtKB Nucleotide binding 428 435 . . . Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P40024 UniProtKB Modified residue 43 43 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40024 UniProtKB Modified residue 65 65 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40024 UniProtKB Modified residue 196 196 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40024 UniProtKB Modified residue 446 446 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P11076 1 181 +P11076 UniProtKB Initiator methionine 1 1 . . . Note=Removed +P11076 UniProtKB Chain 2 181 . . . ID=PRO_0000207418;Note=ADP-ribosylation factor 1 +P11076 UniProtKB Nucleotide binding 25 32 . . . Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20601958;Dbxref=PMID:20601958 +P11076 UniProtKB Nucleotide binding 126 129 . . . Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20601958;Dbxref=PMID:20601958 +P11076 UniProtKB Nucleotide binding 160 161 . . . Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20601958;Dbxref=PMID:20601958 +P11076 UniProtKB Binding site 48 48 . . . Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20601958;Dbxref=PMID:20601958 +P11076 UniProtKB Binding site 70 70 . . . Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20601958;Dbxref=PMID:20601958 +P11076 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19141284,ECO:0000269|PubMed:20601958;Dbxref=PMID:19141284,PMID:20601958 +P11076 UniProtKB Cross-link 127 127 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P11076 UniProtKB Beta strand 4 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K5U +P11076 UniProtKB Helix 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KSQ +P11076 UniProtKB Turn 14 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KSQ +P11076 UniProtKB Beta strand 19 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ +P11076 UniProtKB Turn 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KSQ +P11076 UniProtKB Helix 30 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ +P11076 UniProtKB Beta strand 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K5U +P11076 UniProtKB Beta strand 49 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ +P11076 UniProtKB Beta strand 61 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ +P11076 UniProtKB Helix 72 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ +P11076 UniProtKB Helix 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ +P11076 UniProtKB Helix 79 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ +P11076 UniProtKB Beta strand 86 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ +P11076 UniProtKB Beta strand 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ +P11076 UniProtKB Helix 100 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ +P11076 UniProtKB Helix 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ +P11076 UniProtKB Beta strand 120 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ +P11076 UniProtKB Helix 136 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ +P11076 UniProtKB Helix 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ +P11076 UniProtKB Beta strand 153 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ +P11076 UniProtKB Turn 160 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ +P11076 UniProtKB Helix 166 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJZ +P11076 UniProtKB Turn 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KSQ +##sequence-region P00812 1 333 +P00812 UniProtKB Chain 1 333 . . . ID=PRO_0000173711;Note=Arginase +P00812 UniProtKB Region 148 152 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53608 +P00812 UniProtKB Region 159 161 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53608 +P00812 UniProtKB Metal binding 123 123 . . . Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00742 +P00812 UniProtKB Metal binding 146 146 . . . Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00742 +P00812 UniProtKB Metal binding 146 146 . . . Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00742 +P00812 UniProtKB Metal binding 148 148 . . . Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00742 +P00812 UniProtKB Metal binding 150 150 . . . Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00742 +P00812 UniProtKB Metal binding 256 256 . . . Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00742 +P00812 UniProtKB Metal binding 256 256 . . . Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00742 +P00812 UniProtKB Metal binding 258 258 . . . Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00742 +P00812 UniProtKB Binding site 205 205 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53608 +P00812 UniProtKB Binding site 270 270 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53608 +P00812 UniProtKB Binding site 301 301 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53608 +P00812 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P00812 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00812 UniProtKB Modified residue 77 77 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00812 UniProtKB Modified residue 270 270 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P08566 1 1588 +P08566 UniProtKB Chain 1 1588 . . . ID=PRO_0000140862;Note=Pentafunctional AROM polypeptide +P08566 UniProtKB Nucleotide binding 43 45 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Nucleotide binding 78 81 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Nucleotide binding 109 111 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Nucleotide binding 134 135 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Nucleotide binding 174 177 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Nucleotide binding 895 902 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Region 1 392 . . . Note=3-dehydroquinate synthase +P08566 UniProtKB Region 189 192 . . . Note=Substrate binding 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Region 272 276 . . . Note=Substrate binding 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Region 405 871 . . . Note=EPSP synthase +P08566 UniProtKB Region 890 1080 . . . Note=Shikimate kinase +P08566 UniProtKB Region 1081 1293 . . . Note=3-dehydroquinase +P08566 UniProtKB Region 1306 1588 . . . Note=Shikimate dehydrogenase +P08566 UniProtKB Active site 268 268 . . . Note=Proton acceptor%3B for 3-dehydroquinate synthase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Active site 283 283 . . . Note=Proton acceptor%3B for 3-dehydroquinate synthase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Active site 853 853 . . . Note=For EPSP synthase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Active site 1198 1198 . . . Note=Proton acceptor%3B for 3-dehydroquinate dehydratase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Active site 1227 1227 . . . Note=Schiff-base intermediate with substrate%3B for 3-dehydroquinate dehydratase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Metal binding 189 189 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Metal binding 279 279 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Metal binding 295 295 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Binding site 114 114 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Binding site 125 125 . . . Note=Substrate 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Binding site 141 141 . . . Note=Substrate 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Binding site 147 147 . . . Note=Substrate 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Binding site 156 156 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Binding site 157 157 . . . Note=Substrate 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Binding site 185 185 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Binding site 258 258 . . . Note=Substrate 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Binding site 279 279 . . . Note=Substrate 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Binding site 295 295 . . . Note=Substrate 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +P08566 UniProtKB Binding site 364 364 . . . Note=Substrate 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03143 +##sequence-region P15274 1 810 +P15274 UniProtKB Chain 1 810 . . . ID=PRO_0000194414;Note=AMP deaminase +P15274 UniProtKB Region 433 438 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15274 UniProtKB Region 708 711 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15274 UniProtKB Active site 652 652 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10104 +P15274 UniProtKB Metal binding 362 362 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15274 UniProtKB Metal binding 364 364 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15274 UniProtKB Metal binding 630 630 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15274 UniProtKB Metal binding 707 707 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15274 UniProtKB Binding site 364 364 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15274 UniProtKB Binding site 633 633 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15274 UniProtKB Modified residue 19 19 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P15274 UniProtKB Modified residue 58 58 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P15274 UniProtKB Modified residue 61 61 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P15274 UniProtKB Modified residue 138 138 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950 +P15274 UniProtKB Sequence conflict 568 568 . . . Note=F->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08951 1 932 +Q08951 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q08951 UniProtKB Chain 2 932 . . . ID=PRO_0000227676;Note=AP-3 complex subunit delta +Q08951 UniProtKB Repeat 157 194 . . . Note=HEAT 1 +Q08951 UniProtKB Repeat 196 231 . . . Note=HEAT 2 +Q08951 UniProtKB Repeat 233 269 . . . Note=HEAT 3 +Q08951 UniProtKB Repeat 270 307 . . . Note=HEAT 4 +Q08951 UniProtKB Repeat 310 346 . . . Note=HEAT 5 +Q08951 UniProtKB Repeat 347 384 . . . Note=HEAT 6 +Q08951 UniProtKB Repeat 386 425 . . . Note=HEAT 7 +Q08951 UniProtKB Repeat 427 466 . . . Note=HEAT 8 +Q08951 UniProtKB Repeat 490 527 . . . Note=HEAT 9 +Q08951 UniProtKB Repeat 528 564 . . . Note=HEAT 10 +Q08951 UniProtKB Repeat 570 601 . . . Note=HEAT 11 +Q08951 UniProtKB Repeat 602 638 . . . Note=HEAT 12 +Q08951 UniProtKB Coiled coil 858 878 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08951 UniProtKB Compositional bias 784 791 . . . Note=Poly-Lys +Q08951 UniProtKB Compositional bias 897 916 . . . Note=Poly-Lys +Q08951 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q08951 UniProtKB Modified residue 700 700 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08951 UniProtKB Modified residue 727 727 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q08951 UniProtKB Modified residue 767 767 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q08951 UniProtKB Modified residue 770 770 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08951 UniProtKB Modified residue 773 773 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08951 UniProtKB Modified residue 798 798 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q08951 UniProtKB Modified residue 888 888 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q08951 UniProtKB Modified residue 918 918 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P22108 1 325 +P22108 UniProtKB Chain 1 325 . . . ID=PRO_0000064613;Note=Diadenosine 5'%2C5'''-P1%2CP4-tetraphosphate phosphorylase 2 +P22108 UniProtKB Region 92 93 . . . Note=Substrate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156 +P22108 UniProtKB Region 154 157 . . . Note=Substrate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156 +P22108 UniProtKB Region 277 279 . . . Note=Substrate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156 +P22108 UniProtKB Active site 161 161 . . . Note=Nucleophile;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156 +P22108 UniProtKB Binding site 53 53 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156 +P22108 UniProtKB Binding site 148 148 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156 +P22108 UniProtKB Binding site 163 163 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156 +P22108 UniProtKB Binding site 284 284 . . . Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156 +P22108 UniProtKB Binding site 288 288 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156 +P22108 UniProtKB Mutagenesis 161 161 . . . Note=Completely abolishes catalytic activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23628156;Dbxref=PMID:23628156 +P22108 UniProtKB Helix 6 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Beta strand 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5W +P22108 UniProtKB Beta strand 29 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Turn 36 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Beta strand 41 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Helix 48 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Turn 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Helix 73 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Beta strand 76 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Beta strand 81 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Beta strand 101 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Helix 117 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Beta strand 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Beta strand 143 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Turn 151 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Beta strand 161 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Helix 174 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Beta strand 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5V +P22108 UniProtKB Beta strand 197 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Beta strand 204 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Helix 212 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Helix 217 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Turn 233 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Beta strand 249 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Beta strand 255 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Turn 270 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Helix 278 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Beta strand 284 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Helix 290 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Helix 301 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +P22108 UniProtKB Helix 320 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I5T +##sequence-region Q04601 1 652 +Q04601 UniProtKB Chain 1 652 . . . ID=PRO_0000064623;Note=Anaphase-promoting complex subunit 4 +##sequence-region Q08683 1 685 +Q08683 UniProtKB Chain 1 685 . . . ID=PRO_0000064625;Note=Anaphase-promoting complex subunit 5 +Q08683 UniProtKB Compositional bias 497 500 . . . Note=Poly-Ser +##sequence-region Q12107 1 265 +Q12107 UniProtKB Chain 1 265 . . . ID=PRO_0000064626;Note=Anaphase-promoting complex subunit 9 +##sequence-region P53933 1 587 +P53933 UniProtKB Chain 1 587 . . . ID=PRO_0000076180;Note=Phosphatidate phosphatase APP1 +P53933 UniProtKB Region 467 483 . . . Note=Interaction with SH3 domain of ABP1 +P53933 UniProtKB Motif 281 285 . . . Note=DXDXT motif +P53933 UniProtKB Compositional bias 469 475 . . . Note=Poly-Pro +P53933 UniProtKB Mutagenesis 281 281 . . . Note=Abolishes PAP activity. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23071111;Dbxref=PMID:23071111 +##sequence-region P47036 1 138 +P47036 UniProtKB Chain 1 138 . . . ID=PRO_0000203053;Note=Putative uncharacterized protein APQ13 +P47036 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36973 1 181 +P36973 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P36973 UniProtKB Chain 2 181 . . . ID=PRO_0000149518;Note=Adenine phosphoribosyltransferase 2 +P36973 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P36973 UniProtKB Sequence conflict 57 57 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25628 1 610 +P25628 UniProtKB Chain 1 610 . . . ID=PRO_0000207648;Note=Sterol O-acyltransferase 1 +P25628 UniProtKB Transmembrane 182 202 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25628 UniProtKB Transmembrane 229 249 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25628 UniProtKB Transmembrane 264 284 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25628 UniProtKB Transmembrane 371 391 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25628 UniProtKB Transmembrane 409 429 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25628 UniProtKB Transmembrane 535 555 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25628 UniProtKB Transmembrane 590 610 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25628 UniProtKB Active site 547 547 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25628 UniProtKB Modified residue 21 21 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P25628 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P53111 1 347 +P53111 UniProtKB Chain 1 347 . . . ID=PRO_0000215578;Note=NADPH-dependent aldehyde reductase ARI1 +##sequence-region P36090 1 516 +P36090 UniProtKB Chain 1 516 . . . ID=PRO_0000203181;Note=Uncharacterized protein ANR2 +P36090 UniProtKB Domain 31 185 . . . Note=uDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00304 +P36090 UniProtKB Domain 211 365 . . . Note=cDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00304 +P36090 UniProtKB Domain 367 513 . . . Note=dDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00304 +P36090 UniProtKB Lipidation 511 511 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36090 UniProtKB Lipidation 516 516 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P46682 1 809 +P46682 UniProtKB Chain 1 809 . . . ID=PRO_0000193757;Note=AP-3 complex subunit beta +P46682 UniProtKB Repeat 37 76 . . . Note=HEAT 1 +P46682 UniProtKB Repeat 112 151 . . . Note=HEAT 2 +P46682 UniProtKB Repeat 153 186 . . . Note=HEAT 3 +P46682 UniProtKB Repeat 187 224 . . . Note=HEAT 4 +P46682 UniProtKB Repeat 524 561 . . . Note=HEAT 5 +P46682 UniProtKB Compositional bias 771 789 . . . Note=Asp/Glu-rich (acidic) +P46682 UniProtKB Modified residue 693 693 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46682 UniProtKB Modified residue 698 698 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P46682 UniProtKB Modified residue 724 724 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46682 UniProtKB Modified residue 726 726 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P46682 UniProtKB Sequence conflict 27 35 . . . Note=TSKLGESSY->PLSWVNPP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46682 UniProtKB Sequence conflict 724 724 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46682 UniProtKB Sequence conflict 798 802 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12157 1 165 +Q12157 UniProtKB Chain 1 165 . . . ID=PRO_0000055751;Note=Anaphase-promoting complex subunit 11 +Q12157 UniProtKB Zinc finger 52 95 . . . Note=RING-type%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +Q12157 UniProtKB Mutagenesis 10 10 . . . Note=In APC11-13%3B G2/M cell cycle arrest at 37 degrees Celsius. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10888670;Dbxref=PMID:10888670 +Q12157 UniProtKB Mutagenesis 41 41 . . . Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10888670;Dbxref=PMID:10888670 +Q12157 UniProtKB Mutagenesis 44 44 . . . Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10888670;Dbxref=PMID:10888670 +Q12157 UniProtKB Mutagenesis 81 81 . . . Note=Loss of function. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10888670;Dbxref=PMID:10888670 +Q12157 UniProtKB Mutagenesis 91 91 . . . Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10888670;Dbxref=PMID:10888670 +##sequence-region Q04413 1 109 +Q04413 UniProtKB Chain 1 109 . . . ID=PRO_0000299768;Note=Uncharacterized protein API2 +##sequence-region P04076 1 463 +P04076 UniProtKB Chain 1 463 . . . ID=PRO_0000137727;Note=Argininosuccinate lyase +P04076 UniProtKB Modified residue 27 27 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P04076 UniProtKB Sequence conflict 103 103 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P08019 1 549 +P08019 UniProtKB Chain 1 549 . . . ID=PRO_0000186120;Note=Glucoamylase%2C intracellular sporulation-specific +P08019 UniProtKB Active site 261 261 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10051 +P08019 UniProtKB Active site 264 264 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10051 +P08019 UniProtKB Binding site 198 198 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08019 UniProtKB Sequence conflict 184 184 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08019 UniProtKB Sequence conflict 504 549 . . . Note=HVGTDGELSEQFNKYTGFMQGAQHLTWSYTSFWDAYQIRQEVLQSL->TWEQTGN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32629 1 500 +P32629 UniProtKB Chain 1 500 . . . ID=PRO_0000193668;Note=Mannan polymerase II complex ANP1 subunit +P32629 UniProtKB Topological domain 1 15 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32629 UniProtKB Transmembrane 16 27 . . . Note=Helical%3B Signal-anchor for type II membrane protein +P32629 UniProtKB Topological domain 28 500 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32629 UniProtKB Compositional bias 446 473 . . . Note=Gln-rich +P32629 UniProtKB Sequence conflict 220 224 . . . Note=HHDKD->QSGQGN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32629 UniProtKB Sequence conflict 220 224 . . . Note=HHDKD->QSGQGN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32629 UniProtKB Sequence conflict 313 313 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32629 UniProtKB Sequence conflict 313 313 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32629 UniProtKB Sequence conflict 313 313 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32629 UniProtKB Sequence conflict 313 313 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32629 UniProtKB Sequence conflict 472 500 . . . Note=PQGKPLDDNDKNKKKHPKEVPLDFDPDRN->RRGNLLMTTTRTRKNILKKFH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32629 UniProtKB Sequence conflict 472 500 . . . Note=PQGKPLDDNDKNKKKHPKEVPLDFDPDRN->RRGNLLMTTTRTRKNILKKFH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38832 1 159 +P38832 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38832 UniProtKB Chain 21 137 . . . ID=PRO_0000203777;Note=Probable GPI-anchored protein ANS1 +P38832 UniProtKB Propeptide 138 159 . . . ID=PRO_0000402190;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38832 UniProtKB Repeat 101 114 . . . Note=PIR1/2/3 +P38832 UniProtKB Lipidation 137 137 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38153 1 483 +P38153 UniProtKB Chain 1 483 . . . ID=PRO_0000193794;Note=AP-3 complex subunit mu +P38153 UniProtKB Domain 211 482 . . . Note=MHD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00404 +P38153 UniProtKB Sequence conflict 35 36 . . . Note=QS->RT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38153 UniProtKB Sequence conflict 35 36 . . . Note=QS->RT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P37302 1 537 +P37302 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37302 UniProtKB Propeptide 22 56 . . . ID=PRO_0000026847;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37302 UniProtKB Chain 57 537 . . . ID=PRO_0000026848;Note=Aminopeptidase Y +P37302 UniProtKB Active site 358 358 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561 +P37302 UniProtKB Metal binding 314 314 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561 +P37302 UniProtKB Metal binding 326 326 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561 +P37302 UniProtKB Metal binding 326 326 . . . Note=Zinc 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561 +P37302 UniProtKB Metal binding 359 359 . . . Note=Zinc 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561 +P37302 UniProtKB Metal binding 387 387 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561 +P37302 UniProtKB Metal binding 472 472 . . . Note=Zinc 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561 +P37302 UniProtKB Site 471 471 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561 +P37302 UniProtKB Glycosylation 85 85 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37302 UniProtKB Glycosylation 96 96 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37302 UniProtKB Glycosylation 115 115 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37302 UniProtKB Glycosylation 150 150 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37302 UniProtKB Glycosylation 162 162 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37302 UniProtKB Glycosylation 371 371 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37302 UniProtKB Glycosylation 427 427 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37302 UniProtKB Glycosylation 480 480 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37302 UniProtKB Sequence conflict 14 15 . . . Note=YA->LR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53940 1 528 +P53940 UniProtKB Chain 1 528 . . . ID=PRO_0000071155;Note=J domain-containing protein APJ1 +P53940 UniProtKB Domain 4 73 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +P53940 UniProtKB Repeat 206 213 . . . Note=CXXCXGXG motif +P53940 UniProtKB Repeat 218 225 . . . Note=CXXCXGXG motif +P53940 UniProtKB Repeat 246 253 . . . Note=CXXCXGXG motif +P53940 UniProtKB Repeat 262 269 . . . Note=CXXCXGXG motif +P53940 UniProtKB Zinc finger 193 274 . . . Note=CR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00546 +##sequence-region P38700 1 605 +P38700 UniProtKB Chain 1 605 . . . ID=PRO_0000193793;Note=Adaptin medium chain homolog APM2 +P38700 UniProtKB Domain 269 604 . . . Note=MHD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00404 +##sequence-region P22936 1 367 +P22936 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3056935;Dbxref=PMID:3056935 +P22936 UniProtKB Chain 2 367 . . . ID=PRO_0000190898;Note=DNA-(apurinic or apyrimidinic site) lyase 1 +P22936 UniProtKB Metal binding 83 83 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22936 UniProtKB Metal binding 123 123 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22936 UniProtKB Metal binding 158 158 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22936 UniProtKB Metal binding 158 158 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22936 UniProtKB Metal binding 192 192 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22936 UniProtKB Metal binding 195 195 . . . Note=Zinc 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22936 UniProtKB Metal binding 229 229 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22936 UniProtKB Metal binding 242 242 . . . Note=Zinc 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22936 UniProtKB Metal binding 244 244 . . . Note=Zinc 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22936 UniProtKB Metal binding 274 274 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22936 UniProtKB Modified residue 356 356 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P22936 UniProtKB Sequence conflict 239 239 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53943 1 586 +P53943 UniProtKB Chain 1 586 . . . ID=PRO_0000173443;Note=Probable transporter AQR1 +P53943 UniProtKB Topological domain 1 99 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Transmembrane 100 120 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Topological domain 121 139 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Transmembrane 140 160 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Topological domain 161 166 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Transmembrane 167 187 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Topological domain 188 188 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Transmembrane 189 209 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Topological domain 210 225 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Transmembrane 226 246 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Topological domain 247 255 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Transmembrane 256 276 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Topological domain 277 334 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Transmembrane 335 355 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Topological domain 356 374 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Transmembrane 375 395 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Topological domain 396 433 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Transmembrane 434 454 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Topological domain 455 459 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Transmembrane 460 480 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Topological domain 481 523 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Transmembrane 524 544 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Topological domain 545 586 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53943 UniProtKB Sequence conflict 174 174 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CD90 1 149 +P0CD90 UniProtKB Chain 1 149 . . . ID=PRO_0000391651;Note=Aquaporin-like protein 2 +P0CD90 UniProtKB Topological domain 1 47 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CD90 UniProtKB Transmembrane 48 68 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD90 UniProtKB Topological domain 69 89 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CD90 UniProtKB Transmembrane 90 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD90 UniProtKB Topological domain 111 149 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q04371 1 470 +Q04371 UniProtKB Chain 1 470 . . . ID=PRO_0000203271;Note=Protein-glutamate O-methyltransferase +Q04371 UniProtKB Binding site 259 259 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H993 +Q04371 UniProtKB Binding site 292 292 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H993 +Q04371 UniProtKB Helix 15 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 23 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Beta strand 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 47 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 77 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 88 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Beta strand 103 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 106 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Turn 125 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 134 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 145 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 175 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 191 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 196 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 204 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 210 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Beta strand 223 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 228 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Beta strand 248 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 258 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Beta strand 277 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Turn 289 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 295 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Turn 308 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 319 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Beta strand 339 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 346 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 354 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Beta strand 363 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 366 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Beta strand 377 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 383 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 402 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 407 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Beta strand 416 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 434 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Beta strand 444 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Helix 450 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Beta strand 456 458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +Q04371 UniProtKB Beta strand 460 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PT1 +##sequence-region Q06408 1 635 +Q06408 UniProtKB Chain 1 635 . . . ID=PRO_0000090835;Note=Transaminated amino acid decarboxylase +Q06408 UniProtKB Cross-link 588 588 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region Q04052 1 950 +Q04052 UniProtKB Chain 1 950 . . . ID=PRO_0000114938;Note=Transcriptional activator ARO80 +Q04052 UniProtKB DNA binding 25 58 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +Q04052 UniProtKB Compositional bias 921 943 . . . Note=Asn-rich +##sequence-region P38080 1 1108 +P38080 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38080 UniProtKB Chain 2 1108 . . . ID=PRO_0000085603;Note=Serine/threonine-protein kinase AKL1 +P38080 UniProtKB Domain 35 319 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38080 UniProtKB Nucleotide binding 41 49 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38080 UniProtKB Active site 181 181 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P38080 UniProtKB Binding site 70 70 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38080 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38080 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38080 UniProtKB Modified residue 407 407 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38080 UniProtKB Modified residue 471 471 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38080 UniProtKB Modified residue 504 504 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38080 UniProtKB Modified residue 541 541 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38080 UniProtKB Modified residue 574 574 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38080 UniProtKB Modified residue 801 801 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38080 UniProtKB Modified residue 846 846 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38080 UniProtKB Modified residue 953 953 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38080 UniProtKB Modified residue 960 960 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38080 UniProtKB Modified residue 1048 1048 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38080 UniProtKB Modified residue 1072 1072 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38080 UniProtKB Cross-link 1008 1008 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P38080 UniProtKB Cross-link 1046 1046 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region P54115 1 500 +P54115 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9392076;Dbxref=PMID:9392076 +P54115 UniProtKB Chain 2 500 . . . ID=PRO_0000056441;Note=Magnesium-activated aldehyde dehydrogenase%2C cytosolic +P54115 UniProtKB Nucleotide binding 249 254 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P54115 UniProtKB Active site 272 272 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007 +P54115 UniProtKB Active site 306 306 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007 +P54115 UniProtKB Site 173 173 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P54115 UniProtKB Cross-link 3 3 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P54115 UniProtKB Cross-link 142 142 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P54115 UniProtKB Cross-link 196 196 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P54115 UniProtKB Sequence conflict 121 121 . . . Note=L->FK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P16661 1 449 +P16661 UniProtKB Chain 1 449 . . . ID=PRO_0000080259;Note=Chitobiosyldiphosphodolichol beta-mannosyltransferase +P16661 UniProtKB Topological domain 1 7 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16661 UniProtKB Transmembrane 8 34 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16661 UniProtKB Topological domain 35 449 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16661 UniProtKB Region 435 449 . . . Note=Required for oligomerization +P16661 UniProtKB Motif 21 32 . . . Note=Dolichol recognition;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16661 UniProtKB Glycosylation 88 88 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16661 UniProtKB Glycosylation 199 199 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16661 UniProtKB Glycosylation 425 425 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16661 UniProtKB Mutagenesis 278 278 . . . Note=Abolishes enzymatic activity. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15044395;Dbxref=PMID:15044395 +P16661 UniProtKB Mutagenesis 310 310 . . . Note=Abolishes enzymatic activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15044395;Dbxref=PMID:15044395 +P16661 UniProtKB Mutagenesis 356 356 . . . Note=Abolishes enzymatic activity. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15044395;Dbxref=PMID:15044395 +P16661 UniProtKB Mutagenesis 363 363 . . . Note=No effect on enzymatic activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15044395;Dbxref=PMID:15044395 +P16661 UniProtKB Mutagenesis 370 370 . . . Note=No effect on enzymatic activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15044395;Dbxref=PMID:15044395 +##sequence-region P36000 1 726 +P36000 UniProtKB Chain 1 726 . . . ID=PRO_0000193753;Note=AP-1 complex subunit beta-1 +##sequence-region P19880 1 650 +P19880 UniProtKB Chain 1 650 . . . ID=PRO_0000076521;Note=AP-1-like transcription factor YAP1 +P19880 UniProtKB Domain 64 127 . . . Note=bZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P19880 UniProtKB Region 67 90 . . . Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P19880 UniProtKB Region 92 120 . . . Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P19880 UniProtKB Region 220 378 . . . Note=Transcription activation 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8182076;Dbxref=PMID:8182076 +P19880 UniProtKB Region 303 315 . . . Note=n-CRD;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15318225;Dbxref=PMID:15318225 +P19880 UniProtKB Region 430 537 . . . Note=Transcription activation 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8182076;Dbxref=PMID:8182076 +P19880 UniProtKB Region 598 629 . . . Note=c-CRD;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15318225;Dbxref=PMID:15318225 +P19880 UniProtKB Motif 35 42 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00768 +P19880 UniProtKB Motif 68 75 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00768 +P19880 UniProtKB Motif 614 621 . . . Note=Nuclear export signal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9857197;Dbxref=PMID:9857197 +P19880 UniProtKB Compositional bias 411 414 . . . Note=Poly-Asn +P19880 UniProtKB Compositional bias 517 521 . . . Note=Poly-Asp +P19880 UniProtKB Modified residue 9 9 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P19880 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198 +P19880 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P19880 UniProtKB Modified residue 165 165 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P19880 UniProtKB Modified residue 204 204 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P19880 UniProtKB Modified residue 372 372 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P19880 UniProtKB Modified residue 528 528 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P19880 UniProtKB Disulfide bond 303 598 . . . Note=In peroxide stress-induced nuclear retained form%3B alternate;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1SSE,ECO:0000269|PubMed:12437921,ECO:0000269|PubMed:14556629,ECO:0000269|PubMed:15318225,ECO:0000269|PubMed:17707237;Dbxref=PMID:12437921,PMID:14556629,PMID:15318225,PMID:17707237 +P19880 UniProtKB Disulfide bond 310 629 . . . Note=In peroxide stress-induced nuclear retained form%3B alternate;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1SSE,ECO:0000269|PubMed:14556629,ECO:0000269|PubMed:15318225,ECO:0000269|PubMed:17707237;Dbxref=PMID:14556629,PMID:15318225,PMID:17707237 +P19880 UniProtKB Disulfide bond 598 629 . . . Note=In diamide-induced nuclear retained form%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11509657;Dbxref=PMID:11509657 +P19880 UniProtKB Disulfide bond 598 620 . . . Note=In diamide-induced nuclear retained form;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11509657;Dbxref=PMID:11509657 +P19880 UniProtKB Disulfide bond 598 598 . . . Note=Interchain (with C-36 in HYR1)%3B transient%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12437921,ECO:0000269|PubMed:14556629,ECO:0000269|PubMed:17720812;Dbxref=PMID:12437921,PMID:14556629,PMID:17720812 +P19880 UniProtKB Disulfide bond 620 629 . . . Note=In diamide-induced nuclear retained form;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11509657;Dbxref=PMID:11509657 +P19880 UniProtKB Mutagenesis 78 78 . . . Note=Dominant negative transcription activator. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8182076;Dbxref=PMID:8182076 +P19880 UniProtKB Mutagenesis 598 598 . . . Note=Does not alter nuclear location and transcription activation. Constitutively cytoplasmic%3B when associated with A-620 and T-629. C->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9130715;Dbxref=PMID:9130715 +P19880 UniProtKB Mutagenesis 620 620 . . . Note=Does not alter nuclear location and transcription activation. Constitutively cytoplasmic%3B when associated with T-598 and T-629. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9130715;Dbxref=PMID:9130715 +P19880 UniProtKB Mutagenesis 620 620 . . . Note=Constitutive nuclear location and transcription activation. C->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9130715;Dbxref=PMID:9130715 +P19880 UniProtKB Mutagenesis 629 629 . . . Note=Does not alter nuclear location and transcription activation. Constitutively cytoplasmic%3B when associated with T-598 and T-620. C->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9130715;Dbxref=PMID:9130715 +P19880 UniProtKB Sequence conflict 316 316 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19880 UniProtKB Sequence conflict 586 586 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19880 UniProtKB Sequence conflict 648 648 . . . Note=H->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19880 UniProtKB Helix 289 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SSE +P19880 UniProtKB Beta strand 292 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SSE +P19880 UniProtKB Beta strand 298 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SSE +P19880 UniProtKB Helix 301 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SSE +P19880 UniProtKB Helix 598 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SSE +P19880 UniProtKB Helix 616 623 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SSE +P19880 UniProtKB Turn 624 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SSE +P19880 UniProtKB Helix 638 646 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SSE +##sequence-region P27351 1 700 +P27351 UniProtKB Chain 1 700 . . . ID=PRO_0000193755;Note=AP-2 complex subunit beta +P27351 UniProtKB Modified residue 649 649 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P27351 UniProtKB Modified residue 652 652 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P27351 UniProtKB Modified residue 683 683 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P27351 UniProtKB Sequence conflict 55 55 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27351 UniProtKB Sequence conflict 484 484 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27351 UniProtKB Sequence conflict 504 504 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27351 UniProtKB Sequence conflict 521 521 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27351 UniProtKB Sequence conflict 629 629 . . . Note=F->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q99186 1 491 +Q99186 UniProtKB Chain 1 491 . . . ID=PRO_0000193780;Note=AP-2 complex subunit mu +Q99186 UniProtKB Domain 209 490 . . . Note=MHD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00404 +Q99186 UniProtKB Modified residue 179 179 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q99186 UniProtKB Modified residue 180 180 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q99186 UniProtKB Modified residue 181 181 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P53068 1 250 +P53068 UniProtKB Chain 1 250 . . . ID=PRO_0000174016;Note=Anaphase-promoting complex subunit DOC1 +P53068 UniProtKB Domain 60 246 . . . Note=DOC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00614 +P53068 UniProtKB Mutagenesis 94 94 . . . Note=In DOC1-1%3B G2/M cell cycle arrest at 37 degrees Celsius. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9348530;Dbxref=PMID:9348530 +P53068 UniProtKB Beta strand 31 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Helix 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Turn 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Helix 62 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Beta strand 79 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Helix 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Beta strand 88 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Helix 101 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Beta strand 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Beta strand 117 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Beta strand 135 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Helix 142 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Helix 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Beta strand 149 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Turn 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Beta strand 165 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Beta strand 176 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Beta strand 193 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Beta strand 213 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +P53068 UniProtKB Beta strand 217 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GQP +##sequence-region P0CD91 1 305 +P0CD91 UniProtKB Chain 1 305 . . . ID=PRO_0000064076;Note=Aquaporin-1 +P0CD91 UniProtKB Topological domain 1 48 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD91 UniProtKB Transmembrane 49 69 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD91 UniProtKB Topological domain 70 91 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD91 UniProtKB Transmembrane 92 112 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD91 UniProtKB Topological domain 113 136 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD91 UniProtKB Transmembrane 137 157 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD91 UniProtKB Topological domain 158 176 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD91 UniProtKB Transmembrane 177 197 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD91 UniProtKB Topological domain 198 203 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD91 UniProtKB Transmembrane 204 224 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD91 UniProtKB Topological domain 225 248 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD91 UniProtKB Transmembrane 249 269 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD91 UniProtKB Topological domain 270 305 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD91 UniProtKB Motif 118 120 . . . Note=NPA 1 +P0CD91 UniProtKB Motif 230 232 . . . Note=NPA 2 +P0CD91 UniProtKB Mutagenesis 121 121 . . . Note=Restores water permeability%3B when associated with P-255. M->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9765289;Dbxref=PMID:9765289 +P0CD91 UniProtKB Mutagenesis 255 255 . . . Note=Restores water permeability%3B when associated with V-121. T->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9765289;Dbxref=PMID:9765289 +##sequence-region P38115 1 344 +P38115 UniProtKB Chain 1 344 . . . ID=PRO_0000124610;Note=D-arabinose dehydrogenase [NAD(P)+] heavy chain +P38115 UniProtKB Nucleotide binding 241 295 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38115 UniProtKB Active site 71 71 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38115 UniProtKB Binding site 131 131 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38115 UniProtKB Site 100 100 . . . Note=Lowers pKa of active site Tyr;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38115 UniProtKB Modified residue 151 151 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P38115 UniProtKB Sequence conflict 56 62 . . . Note=AAIKAGY->LQSKLDN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38115 UniProtKB Sequence conflict 71 73 . . . Note=YET->SR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38115 UniProtKB Helix 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Beta strand 23 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Beta strand 32 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Helix 44 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Helix 50 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Beta strand 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Helix 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Helix 74 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Helix 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Beta strand 96 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Helix 103 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Helix 109 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Beta strand 126 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Helix 167 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Beta strand 185 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJC +P38115 UniProtKB Beta strand 189 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Helix 196 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Beta strand 211 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Helix 224 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Beta strand 236 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Helix 249 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Helix 254 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Helix 267 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Helix 289 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Helix 303 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Helix 324 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +P38115 UniProtKB Helix 339 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IJR +##sequence-region P46672 1 376 +P46672 UniProtKB Chain 1 376 . . . ID=PRO_0000087409;Note=tRNA-aminoacylation cofactor ARC1 +P46672 UniProtKB Domain 205 307 . . . Note=tRNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00209 +P46672 UniProtKB Region 22 46 . . . Note=Interaction with methionyl-tRNA synthetase MES1 +P46672 UniProtKB Region 52 61 . . . Note=Interaction with glutamyl-tRNA synthetase GUS1 +P46672 UniProtKB Region 91 121 . . . Note=Interaction with glutamyl-tRNA synthetase GUS1 +P46672 UniProtKB Mutagenesis 26 26 . . . Note=Abolishes interaction with MES1. A->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16914447;Dbxref=PMID:16914447 +P46672 UniProtKB Mutagenesis 100 100 . . . Note=Abolishes interaction with GUS1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16914447;Dbxref=PMID:16914447 +P46672 UniProtKB Sequence conflict 137 149 . . . Note=PAGGAADAAAKAD->LRVALLMLQQGS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46672 UniProtKB Sequence conflict 181 182 . . . Note=KK->LL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46672 UniProtKB Helix 3 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQT +P46672 UniProtKB Helix 12 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRK +P46672 UniProtKB Helix 22 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQT +P46672 UniProtKB Helix 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQT +P46672 UniProtKB Helix 44 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQT +P46672 UniProtKB Helix 65 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQT +P46672 UniProtKB Helix 88 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQT +P46672 UniProtKB Helix 96 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQT +P46672 UniProtKB Turn 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQT +P46672 UniProtKB Helix 206 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +P46672 UniProtKB Beta strand 211 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +P46672 UniProtKB Beta strand 229 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +P46672 UniProtKB Beta strand 242 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +P46672 UniProtKB Turn 249 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +P46672 UniProtKB Helix 254 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +P46672 UniProtKB Beta strand 261 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +P46672 UniProtKB Beta strand 271 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +P46672 UniProtKB Beta strand 276 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +P46672 UniProtKB Beta strand 284 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +P46672 UniProtKB Beta strand 291 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +P46672 UniProtKB Beta strand 305 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +P46672 UniProtKB Helix 322 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +P46672 UniProtKB Helix 326 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +P46672 UniProtKB Helix 331 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +P46672 UniProtKB Beta strand 334 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +P46672 UniProtKB Beta strand 341 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +P46672 UniProtKB Beta strand 354 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +P46672 UniProtKB Beta strand 374 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R1J +##sequence-region P53309 1 568 +P53309 UniProtKB Chain 1 568 . . . ID=PRO_0000202856;Note=Clathrin coat assembly protein AP180B +P53309 UniProtKB Domain 1 127 . . . Note=ENTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243 +P53309 UniProtKB Compositional bias 379 383 . . . Note=Poly-Gln +P53309 UniProtKB Compositional bias 464 467 . . . Note=Poly-Gln +P53309 UniProtKB Compositional bias 551 560 . . . Note=Poly-Gln +P53309 UniProtKB Modified residue 449 449 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53309 UniProtKB Cross-link 282 282 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q00381 1 147 +Q00381 UniProtKB Chain 1 147 . . . ID=PRO_0000193814;Note=AP-2 complex subunit sigma +##sequence-region P24813 1 409 +P24813 UniProtKB Chain 1 409 . . . ID=PRO_0000076522;Note=AP-1-like transcription factor YAP2 +P24813 UniProtKB Domain 43 106 . . . Note=bZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P24813 UniProtKB Region 46 69 . . . Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P24813 UniProtKB Region 71 99 . . . Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P24813 UniProtKB Region 356 387 . . . Note=c-CRD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19880 +P24813 UniProtKB Motif 17 24 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00768 +P24813 UniProtKB Motif 47 54 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00768 +P24813 UniProtKB Motif 372 379 . . . Note=Nuclear export signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19880 +P24813 UniProtKB Mutagenesis 356 356 . . . Note=Only partially accumulates in the nucleus in response to cadmium. Does not accumulate in the nucleus%3B when associated with A-387. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17187783;Dbxref=PMID:17187783 +P24813 UniProtKB Mutagenesis 378 378 . . . Note=No effect. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17187783;Dbxref=PMID:17187783 +P24813 UniProtKB Mutagenesis 387 387 . . . Note=Only partially accumulates in the nucleus in response to cadmium. Does not accumulate in the nucleus%3B when associated with A-356. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17187783;Dbxref=PMID:17187783 +P24813 UniProtKB Mutagenesis 391 391 . . . Note=Does not accumulate in the nucleus in response to cadmium. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17187783;Dbxref=PMID:17187783 +P24813 UniProtKB Sequence conflict 36 36 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24813 UniProtKB Sequence conflict 90 90 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24813 UniProtKB Sequence conflict 102 102 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24813 UniProtKB Sequence conflict 125 125 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24813 UniProtKB Sequence conflict 131 131 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24813 UniProtKB Sequence conflict 142 142 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24813 UniProtKB Sequence conflict 145 145 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24813 UniProtKB Sequence conflict 327 327 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24813 UniProtKB Sequence conflict 337 337 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24813 UniProtKB Sequence conflict 347 347 . . . Note=S->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24813 UniProtKB Sequence conflict 354 354 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q8TGM5 1 67 +Q8TGM5 UniProtKB Chain 1 67 . . . ID=PRO_0000262871;Note=Putative uncharacterized protein ART3 +##sequence-region Q03862 1 593 +Q03862 UniProtKB Chain 1 593 . . . ID=PRO_0000148999;Note=Probable metalloprotease ARX1 +##sequence-region P22768 1 420 +P22768 UniProtKB Chain 1 420 . . . ID=PRO_0000148559;Note=Argininosuccinate synthase +P22768 UniProtKB Nucleotide binding 9 17 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22768 UniProtKB Nucleotide binding 114 122 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22768 UniProtKB Binding site 35 35 . . . Note=ATP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22768 UniProtKB Binding site 86 86 . . . Note=Citrulline;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22768 UniProtKB Binding site 91 91 . . . Note=Citrulline;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22768 UniProtKB Binding site 118 118 . . . Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22768 UniProtKB Binding site 122 122 . . . Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22768 UniProtKB Binding site 122 122 . . . Note=Citrulline;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22768 UniProtKB Binding site 123 123 . . . Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22768 UniProtKB Binding site 126 126 . . . Note=Citrulline;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22768 UniProtKB Binding site 179 179 . . . Note=Citrulline;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22768 UniProtKB Binding site 188 188 . . . Note=Citrulline;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22768 UniProtKB Binding site 273 273 . . . Note=Citrulline;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22768 UniProtKB Binding site 285 285 . . . Note=Citrulline;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22768 UniProtKB Sequence conflict 27 28 . . . Note=GY->AT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22768 UniProtKB Sequence conflict 27 28 . . . Note=GY->AT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22768 UniProtKB Sequence conflict 48 49 . . . Note=EK->VL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22768 UniProtKB Sequence conflict 48 49 . . . Note=EK->VL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22768 UniProtKB Sequence conflict 61 64 . . . Note=VDCR->GGLS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22768 UniProtKB Sequence conflict 169 169 . . . Note=P->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22768 UniProtKB Sequence conflict 316 316 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22768 UniProtKB Sequence conflict 329 332 . . . Note=SYFT->FLLH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22768 UniProtKB Sequence conflict 329 332 . . . Note=SYFT->FLLH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22768 UniProtKB Sequence conflict 329 332 . . . Note=SYFT->FLLH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P13586 1 950 +P13586 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P13586 UniProtKB Chain 2 950 . . . ID=PRO_0000046231;Note=Calcium-transporting ATPase 1 +P13586 UniProtKB Topological domain 2 92 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13586 UniProtKB Transmembrane 93 111 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13586 UniProtKB Topological domain 112 116 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13586 UniProtKB Transmembrane 117 133 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13586 UniProtKB Topological domain 134 288 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13586 UniProtKB Transmembrane 289 309 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13586 UniProtKB Topological domain 310 323 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13586 UniProtKB Transmembrane 324 344 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13586 UniProtKB Topological domain 345 814 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13586 UniProtKB Transmembrane 815 835 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13586 UniProtKB Topological domain 836 844 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13586 UniProtKB Transmembrane 845 862 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13586 UniProtKB Topological domain 863 884 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13586 UniProtKB Transmembrane 885 905 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13586 UniProtKB Topological domain 906 909 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13586 UniProtKB Transmembrane 910 930 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13586 UniProtKB Topological domain 931 950 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13586 UniProtKB Active site 371 371 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13586 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P13586 UniProtKB Modified residue 227 227 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q12675 1 1612 +Q12675 UniProtKB Chain 1 1612 . . . ID=PRO_0000046234;Note=Phospholipid-transporting ATPase DNF2 +Q12675 UniProtKB Topological domain 1 252 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Transmembrane 253 273 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Topological domain 274 277 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Transmembrane 278 298 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Topological domain 299 598 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Transmembrane 599 619 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Topological domain 620 639 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Transmembrane 640 660 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Topological domain 661 1231 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Transmembrane 1232 1252 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Topological domain 1253 1262 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Transmembrane 1263 1283 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Topological domain 1284 1313 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Transmembrane 1314 1334 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Topological domain 1335 1350 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Transmembrane 1351 1371 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Topological domain 1372 1377 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Transmembrane 1378 1398 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Topological domain 1399 1418 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Transmembrane 1419 1439 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Topological domain 1440 1612 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12675 UniProtKB Active site 712 712 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12675 UniProtKB Modified residue 70 70 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12675 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12675 UniProtKB Modified residue 389 389 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12675 UniProtKB Modified residue 392 392 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12675 UniProtKB Modified residue 396 396 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12675 UniProtKB Modified residue 403 403 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12675 UniProtKB Modified residue 406 406 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12675 UniProtKB Modified residue 782 782 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12675 UniProtKB Modified residue 1542 1542 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +Q12675 UniProtKB Modified residue 1592 1592 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12675 UniProtKB Cross-link 938 938 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P40527 1 1151 +P40527 UniProtKB Chain 1 1151 . . . ID=PRO_0000046236;Note=Probable phospholipid-transporting ATPase NEO1 +P40527 UniProtKB Topological domain 1 184 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Transmembrane 185 205 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Topological domain 206 209 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Transmembrane 210 230 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Topological domain 231 367 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Transmembrane 368 388 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Topological domain 389 416 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Transmembrane 417 437 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Topological domain 438 438 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Transmembrane 439 459 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Topological domain 460 947 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Transmembrane 948 968 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Topological domain 969 970 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Transmembrane 971 991 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Topological domain 992 1020 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Transmembrane 1021 1041 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Topological domain 1042 1052 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Transmembrane 1053 1073 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Topological domain 1074 1078 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Transmembrane 1079 1099 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Topological domain 1100 1109 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Transmembrane 1110 1130 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Topological domain 1131 1151 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40527 UniProtKB Region 1131 1151 . . . Note=Required for endosomal targeting +P40527 UniProtKB Active site 503 503 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40527 UniProtKB Modified residue 102 102 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40527 UniProtKB Modified residue 551 551 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P16639 1 503 +P16639 UniProtKB Chain 1 503 . . . ID=PRO_0000195092;Note=Arginyl-tRNA--protein transferase 1 +P16639 UniProtKB Sequence conflict 122 122 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16639 UniProtKB Sequence conflict 122 122 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16639 UniProtKB Sequence conflict 402 402 . . . Note=Y->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38316 1 186 +P38316 UniProtKB Chain 1 186 . . . ID=PRO_0000212485;Note=Ubiquitin-like protein ATG12 +P38316 UniProtKB Cross-link 186 186 . . . Note=Glycyl lysine isopeptide (Gly-Lys) (interchain with K-149 in ATG5) +P38316 UniProtKB Mutagenesis 106 106 . . . Note=Decreases protein stability. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16874032;Dbxref=PMID:16874032 +P38316 UniProtKB Mutagenesis 108 108 . . . Note=Decreases protein stability. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16874032;Dbxref=PMID:16874032 +P38316 UniProtKB Mutagenesis 149 149 . . . Note=Impairs conjugation to ATG5 and autophagic activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16874032;Dbxref=PMID:16874032 +P38316 UniProtKB Mutagenesis 154 154 . . . Note=Impairs conjugation to ATG5 and autophagic activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16874032;Dbxref=PMID:16874032 +P38316 UniProtKB Mutagenesis 186 186 . . . Note=Strong decrease of conjugation with ATG5. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9759731;Dbxref=PMID:9759731 +P38316 UniProtKB Beta strand 103 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W1S +P38316 UniProtKB Beta strand 121 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W1S +P38316 UniProtKB Helix 130 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W1S +P38316 UniProtKB Beta strand 147 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W1S +P38316 UniProtKB Turn 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W1S +P38316 UniProtKB Helix 162 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W1S +P38316 UniProtKB Beta strand 174 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W1S +##sequence-region Q06628 1 738 +Q06628 UniProtKB Chain 1 738 . . . ID=PRO_0000157972;Note=Autophagy-related protein 13 +Q06628 UniProtKB Region 432 520 . . . Note=Interaction with ATG1 +Q06628 UniProtKB Compositional bias 306 338 . . . Note=Poly-Gln +Q06628 UniProtKB Compositional bias 622 625 . . . Note=Poly-Asp +Q06628 UniProtKB Compositional bias 699 708 . . . Note=Poly-Asn +Q06628 UniProtKB Modified residue 344 344 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19805182;Dbxref=PMID:19805182 +Q06628 UniProtKB Modified residue 348 348 . . . Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911 +Q06628 UniProtKB Modified residue 355 355 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06628 UniProtKB Modified residue 437 437 . . . Note=Phosphoserine%3B by TORC1 and PKA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19805182,ECO:0000269|PubMed:19995911;Dbxref=PMID:19805182,PMID:19995911 +Q06628 UniProtKB Modified residue 438 438 . . . Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911 +Q06628 UniProtKB Modified residue 461 461 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06628 UniProtKB Modified residue 496 496 . . . Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911 +Q06628 UniProtKB Modified residue 535 535 . . . Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911 +Q06628 UniProtKB Modified residue 541 541 . . . Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911 +Q06628 UniProtKB Modified residue 554 554 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06628 UniProtKB Modified residue 581 581 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19805182;Dbxref=PMID:19805182 +Q06628 UniProtKB Modified residue 646 646 . . . Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911 +Q06628 UniProtKB Modified residue 649 649 . . . Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:19995911;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198,PMID:19995911 +Q06628 UniProtKB Mutagenesis 344 344 . . . Note=Decreases phosphorylation by PKA. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19805182;Dbxref=PMID:19805182 +Q06628 UniProtKB Mutagenesis 348 348 . . . Note=Leads to constitutive activation of autophagy%3B when associated with A-437%3B A-438%3B A-496%3B A-535%3B A-541%3B A-646 and A-649. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911 +Q06628 UniProtKB Mutagenesis 437 437 . . . Note=Decreases phosphorylation by PKA. Leads to constitutive activation of autophagy%3B when associated with A-348%3B A-438%3B A-496%3B A-535%3B A-541%3B A-646 and A-649. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19805182,ECO:0000269|PubMed:19995911;Dbxref=PMID:19805182,PMID:19995911 +Q06628 UniProtKB Mutagenesis 438 438 . . . Note=Leads to constitutive activation of autophagy%3B when associated with A-348%3B A-437%3B A-496%3B A-535%3B A-541%3B A-646 and A-649. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911 +Q06628 UniProtKB Mutagenesis 468 468 . . . Note=Impairs binding to ATG1%3B when associated with A-469. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22885598;Dbxref=PMID:22885598 +Q06628 UniProtKB Mutagenesis 469 469 . . . Note=Impairs binding to ATG1%3B when associated with A-468. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22885598;Dbxref=PMID:22885598 +Q06628 UniProtKB Mutagenesis 496 496 . . . Note=Leads to constitutive activation of autophagy%3B when associated with A-348%3B A-437%3B A-438%3B A-535%3B A-541%3B A-646 and A-649. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911 +Q06628 UniProtKB Mutagenesis 535 535 . . . Note=Leads to constitutive activation of autophagy%3B when associated with A-348%3B A-437%3B A-438%3B A-496%3B A-541%3B A-646 and A-649. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911 +Q06628 UniProtKB Mutagenesis 541 541 . . . Note=Leads to constitutive activation of autophagy%3B when associated with A-348%3B A-437%3B A-438%3B A-496%3B A-535%3B A-646 and A-649. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911 +Q06628 UniProtKB Mutagenesis 581 581 . . . Note=Decreases phosphorylation by PKA. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19805182;Dbxref=PMID:19805182 +Q06628 UniProtKB Mutagenesis 646 646 . . . Note=Leads to constitutive activation of autophagy%3B when associated with A-348%3B A-437%3B A-438%3B A-496%3B A-535%3B A-541 and A-649. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911 +Q06628 UniProtKB Mutagenesis 649 649 . . . Note=Leads to constitutive activation of autophagy%3B when associated with A-348%3B A-437%3B A-438%3B A-496%3B A-535%3B A-541%2C and A-646. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995911;Dbxref=PMID:19995911 +##sequence-region Q06671 1 453 +Q06671 UniProtKB Chain 1 453 . . . ID=PRO_0000064727;Note=Autophagy-related protein 23 +Q06671 UniProtKB Coiled coil 144 213 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06671 UniProtKB Coiled coil 272 302 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P46989 1 271 +P46989 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46989 UniProtKB Chain 20 271 . . . ID=PRO_0000001780;Note=Autophagy-related protein 27 +P46989 UniProtKB Topological domain 20 199 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17135291;Dbxref=PMID:17135291 +P46989 UniProtKB Transmembrane 200 220 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46989 UniProtKB Topological domain 221 271 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17135291;Dbxref=PMID:17135291 +P46989 UniProtKB Mutagenesis 188 193 . . . Note=Abolishes the binding of phosphatidylinositol 3-phosphate and the cytoplasm to vacuole transport. KKPAKK->AAPAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12186856;Dbxref=PMID:12186856 +##sequence-region P01097 1 85 +P01097 UniProtKB Transit peptide 1 22 . . . Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2138617,ECO:0000269|PubMed:6458601;Dbxref=PMID:2138617,PMID:6458601 +P01097 UniProtKB Chain 23 85 . . . ID=PRO_0000002554;Note=ATPase inhibitor%2C mitochondrial +P01097 UniProtKB Coiled coil 41 84 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P01097 UniProtKB Mutagenesis 41 41 . . . Note=No loss of inhibitory activity. K->Q%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10705452;Dbxref=PMID:10705452 +P01097 UniProtKB Turn 24 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P01097 UniProtKB Helix 38 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +##sequence-region P21306 1 62 +P21306 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1985960;Dbxref=PMID:1985960 +P21306 UniProtKB Chain 2 62 . . . ID=PRO_0000071667;Note=ATP synthase subunit epsilon%2C mitochondrial +P21306 UniProtKB Modified residue 52 52 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P21306 UniProtKB Turn 4 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P21306 UniProtKB Helix 11 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P21306 UniProtKB Helix 28 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P21306 UniProtKB Helix 33 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P21306 UniProtKB Beta strand 44 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +##sequence-region P00830 1 511 +P00830 UniProtKB Transit peptide 1 33 . . . Note=Mitochondrion +P00830 UniProtKB Chain 34 511 . . . ID=PRO_0000002454;Note=ATP synthase subunit beta%2C mitochondrial +P00830 UniProtKB Nucleotide binding 190 197 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00830 UniProtKB Modified residue 112 112 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P00830 UniProtKB Modified residue 237 237 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P00830 UniProtKB Modified residue 373 373 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P00830 UniProtKB Sequence conflict 201 201 . . . Note=Q->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00830 UniProtKB Sequence conflict 218 218 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00830 UniProtKB Sequence conflict 218 218 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00830 UniProtKB Sequence conflict 232 237 . . . Note=REMKET->HEMEDS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00830 UniProtKB Sequence conflict 260 260 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00830 UniProtKB Sequence conflict 287 288 . . . Note=FI->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00830 UniProtKB Sequence conflict 354 358 . . . Note=APATT->SPSTS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00830 UniProtKB Sequence conflict 365 366 . . . Note=TT->SS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00830 UniProtKB Sequence conflict 365 366 . . . Note=TT->SS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00830 UniProtKB Sequence conflict 469 473 . . . Note=DTVAS->RTRCL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00830 UniProtKB Sequence conflict 489 489 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00830 UniProtKB Sequence conflict 501 501 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00830 UniProtKB Sequence conflict 508 508 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00830 UniProtKB Beta strand 43 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Beta strand 53 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Beta strand 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XOK +P00830 UniProtKB Beta strand 69 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Beta strand 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Beta strand 79 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Beta strand 91 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Beta strand 108 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Beta strand 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Beta strand 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Beta strand 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HLD +P00830 UniProtKB Beta strand 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPD +P00830 UniProtKB Beta strand 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Beta strand 147 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEE +P00830 UniProtKB Helix 172 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Beta strand 180 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEH +P00830 UniProtKB Beta strand 184 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Beta strand 192 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPD +P00830 UniProtKB Helix 196 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Turn 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Beta strand 211 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEE +P00830 UniProtKB Beta strand 215 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 224 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Turn 236 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Beta strand 242 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OFN +P00830 UniProtKB Beta strand 247 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 259 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Beta strand 283 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 292 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 303 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 311 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 318 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Beta strand 332 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEE +P00830 UniProtKB Beta strand 335 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 346 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 353 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 359 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Beta strand 363 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 370 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Turn 383 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 393 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 398 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 426 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HLD +P00830 UniProtKB Helix 431 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 455 458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 467 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Turn 480 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 487 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Turn 490 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P00830 UniProtKB Helix 496 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +##sequence-region P05626 1 244 +P05626 UniProtKB Transit peptide 1 35 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2883007;Dbxref=PMID:2883007 +P05626 UniProtKB Chain 36 244 . . . ID=PRO_0000002524;Note=ATP synthase subunit 4%2C mitochondrial +P05626 UniProtKB Modified residue 144 144 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P05626 UniProtKB Sequence conflict 11 11 . . . Note=A->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05626 UniProtKB Sequence conflict 172 172 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05626 UniProtKB Sequence conflict 172 172 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07879 1 167 +Q07879 UniProtKB Chain 1 167 . . . ID=PRO_0000096190;Note=Ubiquitin-like-conjugating enzyme ATG10 +Q07879 UniProtKB Active site 133 133 . . . Note=Glycyl thioester intermediate +Q07879 UniProtKB Mutagenesis 26 26 . . . Note=No effect on conjugating activity. Normal autophagic activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10508157;Dbxref=PMID:10508157 +Q07879 UniProtKB Mutagenesis 133 133 . . . Note=Complete loss of covalent binding to ATG12. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10508157;Dbxref=PMID:10508157 +Q07879 UniProtKB Mutagenesis 133 133 . . . Note=Strong decrease of binding to ATG12. No more formation of ATG12-ATG5 conjugate. Defect in autophagy. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10508157;Dbxref=PMID:10508157 +Q07879 UniProtKB Mutagenesis 137 137 . . . Note=No effect on conjugating activity. Normal autophagic activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10508157;Dbxref=PMID:10508157 +Q07879 UniProtKB Helix 4 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR +Q07879 UniProtKB Turn 17 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR +Q07879 UniProtKB Beta strand 26 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR +Q07879 UniProtKB Beta strand 33 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GSK +Q07879 UniProtKB Beta strand 38 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR +Q07879 UniProtKB Helix 46 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GSK +Q07879 UniProtKB Beta strand 61 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR +Q07879 UniProtKB Turn 71 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR +Q07879 UniProtKB Beta strand 75 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR +Q07879 UniProtKB Beta strand 91 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR +Q07879 UniProtKB Helix 99 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR +Q07879 UniProtKB Turn 107 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR +Q07879 UniProtKB Beta strand 115 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR +Q07879 UniProtKB Beta strand 125 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR +Q07879 UniProtKB Helix 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR +Q07879 UniProtKB Helix 146 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR +Q07879 UniProtKB Helix 150 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR +Q07879 UniProtKB Helix 159 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EBR +##sequence-region Q07528 1 640 +Q07528 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q07528 UniProtKB Chain 2 640 . . . ID=PRO_0000213824;Note=Autophagy-related protein 20 +Q07528 UniProtKB Domain 140 301 . . . Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147 +Q07528 UniProtKB Coiled coil 475 512 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07528 UniProtKB Coiled coil 562 593 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07528 UniProtKB Binding site 192 192 . . . Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07528 UniProtKB Binding site 194 194 . . . Note=Phosphatidylinositol 3-phosphate%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07528 UniProtKB Binding site 218 218 . . . Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07528 UniProtKB Binding site 267 267 . . . Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07528 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q07528 UniProtKB Modified residue 361 361 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07528 UniProtKB Modified residue 363 363 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07528 UniProtKB Mutagenesis 193 193 . . . Note=Abolishes the intracellular punctate localization and decreases the cytoplasm to vacuole transport. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12048214;Dbxref=PMID:12048214 +##sequence-region Q12421 1 196 +Q12421 UniProtKB Chain 1 196 . . . ID=PRO_0000076210;Note=Autophagy-related protein 31 +##sequence-region Q99325 1 256 +Q99325 UniProtKB Signal peptide 1 16 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99325 UniProtKB Chain 17 256 . . . ID=PRO_0000245280;Note=Autophagy-related protein 40 +Q99325 UniProtKB Topological domain 17 67 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99325 UniProtKB Transmembrane 68 88 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99325 UniProtKB Topological domain 89 256 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99325 UniProtKB Motif 242 245 . . . Note=ATG8-binding;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26040717;Dbxref=PMID:26040717 +Q99325 UniProtKB Mutagenesis 242 242 . . . Note=Impairs interaction with ATG8 and decreases subsequent reticulophagy%3B when associated with A-245. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26040717;Dbxref=PMID:26040717 +Q99325 UniProtKB Mutagenesis 245 245 . . . Note=Impairs interaction with ATG8 and decreases subsequent reticulophagy%3B when associated with A-245. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26040717;Dbxref=PMID:26040717 +##sequence-region P48016 1 1211 +P48016 UniProtKB Region 513 514 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:D6XZ22 +P48016 UniProtKB Region 711 712 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:D6XZ22 +P48016 UniProtKB Active site 644 644 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:D6XZ22 +P48016 UniProtKB Glycosylation 28 28 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 32 32 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 98 98 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 207 207 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 238 238 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 247 247 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 255 255 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 259 259 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 325 325 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 370 370 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 376 376 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 488 488 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 539 539 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 568 568 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 628 628 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 638 638 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 696 696 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 705 705 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 879 879 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 897 897 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 910 910 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 972 972 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 990 990 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 1031 1031 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 1049 1049 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 1064 1064 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 1147 1147 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Glycosylation 1157 1157 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48016 UniProtKB Sequence conflict 1168 1211 . . . Note=LQVGDKGNTDWRKTRYIVVAVQGVYDDYDDDNKGATIKEIVLND->FAGG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12233 1 115 +Q12233 UniProtKB Chain 1 115 . . . ID=PRO_0000071696;Note=ATP synthase subunit g%2C mitochondrial +Q12233 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +Q12233 UniProtKB Modified residue 3 3 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +Q12233 UniProtKB Modified residue 62 62 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +Q12233 UniProtKB Mutagenesis 62 62 . . . Note=No effect on ATP synthase dimerization. S->A +Q12233 UniProtKB Mutagenesis 62 62 . . . Note=Inhibits ATP synthase dimerization. S->E +##sequence-region P38111 1 2368 +P38111 UniProtKB Chain 1 2368 . . . ID=PRO_0000088836;Note=Serine/threonine-protein kinase MEC1 +P38111 UniProtKB Domain 1399 1944 . . . Note=FAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534 +P38111 UniProtKB Domain 2082 2368 . . . Note=PI3K/PI4K;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00269 +P38111 UniProtKB Domain 2336 2368 . . . Note=FATC;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534,ECO:0000255|PROSITE-ProRule:PRU00535 +P38111 UniProtKB Region 2140 2368 . . . Note=Binding to the RPA complex +P38111 UniProtKB Mutagenesis 225 225 . . . Note=In MEC1-101%3B impairs both the G1/S and intra-S damage checkpoints but not the G2/M damage checkpoint%3B when associated with P-552 and S-781. V->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11359899;Dbxref=PMID:11359899 +P38111 UniProtKB Mutagenesis 552 552 . . . Note=In MEC1-101%3B impairs both the G1/S and intra-S damage checkpoints but not the G2/M damage checkpoint%3B when associated with S-225 and S-781. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11359899;Dbxref=PMID:11359899 +P38111 UniProtKB Mutagenesis 781 781 . . . Note=In MEC1-101%3B impairs both the G1/S and intra-S damage checkpoints but not the G2/M damage checkpoint%3B when associated with S-225 and P-552. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11359899;Dbxref=PMID:11359899 +P38111 UniProtKB Mutagenesis 1179 1179 . . . Note=In MEC1-100%3B impairs both the G1/S and intra-S damage checkpoints but not the G2/M damage checkpoint%3B when associated with S-1700. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11359899;Dbxref=PMID:11359899 +P38111 UniProtKB Mutagenesis 1700 1700 . . . Note=In MEC1-100%3B impairs both the G1/S and intra-S damage checkpoints but not the G2/M damage checkpoint%3B when associated with S-1179. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11359899;Dbxref=PMID:11359899 +P38111 UniProtKB Mutagenesis 2224 2224 . . . Note=Impairs kinase activity%3B when associated with K-2229. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11095737,ECO:0000269|PubMed:11359899;Dbxref=PMID:11095737,PMID:11359899 +P38111 UniProtKB Mutagenesis 2229 2229 . . . Note=Impairs kinase activity%3B when associated with A-2224. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11095737;Dbxref=PMID:11095737 +P38111 UniProtKB Mutagenesis 2243 2243 . . . Note=Impairs kinase activity. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11359899;Dbxref=PMID:11359899 +P38111 UniProtKB Mutagenesis 2360 2362 . . . Note=In MEC1-85%3B disrupts interaction with RFA1 and severely impairs kinase activity. MYI->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16148046;Dbxref=PMID:16148046 +P38111 UniProtKB Mutagenesis 2367 2368 . . . Note=In MEC1-87%3B decreases the level of MEC1 and impairs viability. FW->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16148046;Dbxref=PMID:16148046 +P38111 UniProtKB Sequence conflict 197 197 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38111 UniProtKB Sequence conflict 716 716 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38111 UniProtKB Sequence conflict 1255 1255 . . . Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38111 UniProtKB Sequence conflict 1276 1276 . . . Note=L->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08409 1 1394 +Q08409 UniProtKB Chain 1 1394 . . . ID=PRO_0000093434;Note=ATP-dependent permease AUS1 +Q08409 UniProtKB Topological domain 1 420 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08409 UniProtKB Transmembrane 421 443 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08409 UniProtKB Transmembrane 468 490 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08409 UniProtKB Transmembrane 497 519 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08409 UniProtKB Transmembrane 529 551 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08409 UniProtKB Transmembrane 558 575 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08409 UniProtKB Transmembrane 636 658 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08409 UniProtKB Topological domain 659 1080 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08409 UniProtKB Transmembrane 1081 1103 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08409 UniProtKB Transmembrane 1107 1129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08409 UniProtKB Transmembrane 1156 1178 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08409 UniProtKB Transmembrane 1193 1215 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08409 UniProtKB Transmembrane 1224 1246 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08409 UniProtKB Transmembrane 1346 1368 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08409 UniProtKB Topological domain 1369 1394 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08409 UniProtKB Domain 33 273 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q08409 UniProtKB Domain 751 978 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q08409 UniProtKB Nucleotide binding 782 789 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +##sequence-region Q12500 1 764 +Q12500 UniProtKB Chain 1 764 . . . ID=PRO_0000247424;Note=Late secretory pathway protein AVL9 +Q12500 UniProtKB Domain 10 173 . . . Note=uDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00304 +Q12500 UniProtKB Domain 195 360 . . . Note=cDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00304 +Q12500 UniProtKB Domain 362 464 . . . Note=dDENN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00304 +Q12500 UniProtKB Compositional bias 603 682 . . . Note=Asp-rich +Q12500 UniProtKB Modified residue 519 519 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12500 UniProtKB Modified residue 524 524 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q05933 1 178 +Q05933 UniProtKB Chain 1 178 . . . ID=PRO_0000124048;Note=Actin-related protein 2/3 complex subunit 3 +Q05933 UniProtKB Cross-link 29 29 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P0CX79 1 362 +P0CX79 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3042786;Dbxref=PMID:3042786 +P0CX79 UniProtKB Chain 26 362 . . . ID=PRO_0000410443;Note=L-asparaginase 2-4 +P0CX79 UniProtKB Domain 33 359 . . . Note=Asparaginase/glutaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01068 +P0CX79 UniProtKB Region 122 123 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX79 UniProtKB Active site 43 43 . . . Note=O-isoaspartyl threonine intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10099,ECO:0000255|PROSITE-ProRule:PRU10100 +P0CX79 UniProtKB Binding site 89 89 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX79 UniProtKB Glycosylation 29 29 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX79 UniProtKB Glycosylation 93 93 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX79 UniProtKB Glycosylation 239 239 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX79 UniProtKB Natural variant 26 55 . . . Note=Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3042786;Dbxref=PMID:3042786 +##sequence-region P39945 1 430 +P39945 UniProtKB Chain 1 430 . . . ID=PRO_0000064711;Note=Protein AST2 +##sequence-region P53296 1 535 +P53296 UniProtKB Chain 1 535 . . . ID=PRO_0000064721;Note=Alcohol O-acetyltransferase 2 +P53296 UniProtKB Sequence conflict 179 179 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12527 1 1178 +Q12527 UniProtKB Chain 1 1178 . . . ID=PRO_0000124554;Note=Autophagy-related protein 11 +Q12527 UniProtKB Coiled coil 538 572 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12527 UniProtKB Coiled coil 696 850 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12527 UniProtKB Compositional bias 598 610 . . . Note=Asn-rich +Q12527 UniProtKB Compositional bias 1050 1099 . . . Note=Ser-rich +##sequence-region P38270 1 344 +P38270 UniProtKB Chain 1 344 . . . ID=PRO_0000212453;Note=Autophagy-related protein 14 +P38270 UniProtKB Region 3 18 . . . Note=Cysteine repeats;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38270 UniProtKB Coiled coil 25 156 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P25641 1 520 +P25641 UniProtKB Chain 1 520 . . . ID=PRO_0000090372;Note=Putative lipase ATG15 +P25641 UniProtKB Topological domain 1 14 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12499386;Dbxref=PMID:12499386 +P25641 UniProtKB Transmembrane 15 35 . . . Note=Helical%3B Signal-anchor for type II membrane protein +P25641 UniProtKB Topological domain 36 520 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12499386;Dbxref=PMID:12499386 +P25641 UniProtKB Active site 332 332 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10037 +P25641 UniProtKB Glycosylation 173 173 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25641 UniProtKB Glycosylation 202 202 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25641 UniProtKB Glycosylation 208 208 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25641 UniProtKB Mutagenesis 332 332 . . . Note=Loss of function. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11085977,ECO:0000269|PubMed:11566994;Dbxref=PMID:11085977,PMID:11566994 +##sequence-region Q03818 1 150 +Q03818 UniProtKB Chain 1 150 . . . ID=PRO_0000218595;Note=Autophagy protein 16 +Q03818 UniProtKB Coiled coil 58 130 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03818 UniProtKB Mutagenesis 35 35 . . . Note=Impairs interaction with ATG5and autophagy. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17192262;Dbxref=PMID:17192262 +Q03818 UniProtKB Mutagenesis 46 46 . . . Note=Impairs interaction with ATG5and autophagy. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17192262;Dbxref=PMID:17192262 +Q03818 UniProtKB Mutagenesis 101 101 . . . Note=Significantly reduces autophagic activity%3B when associated with A-102. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19889643;Dbxref=PMID:19889643 +Q03818 UniProtKB Mutagenesis 102 102 . . . Note=Significantly reduces autophagic activity%3B when associated with A-101. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19889643;Dbxref=PMID:19889643 +Q03818 UniProtKB Mutagenesis 104 104 . . . Note=Significantly reduces autophagic activity%3B when associated with A-108 and A-112. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19889643;Dbxref=PMID:19889643 +Q03818 UniProtKB Mutagenesis 108 108 . . . Note=Significantly reduces autophagic activity%3B when associated with A-104 and A-112. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19889643;Dbxref=PMID:19889643 +Q03818 UniProtKB Mutagenesis 112 112 . . . Note=Significantly reduces autophagic activity%3B when associated with A-104 and A-108. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19889643;Dbxref=PMID:19889643 +Q03818 UniProtKB Helix 23 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q03818 UniProtKB Helix 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q03818 UniProtKB Turn 48 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q03818 UniProtKB Helix 61 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A7O +##sequence-region Q06410 1 417 +Q06410 UniProtKB Chain 1 417 . . . ID=PRO_0000124566;Note=Autophagy-related protein 17 +Q06410 UniProtKB Coiled coil 146 221 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06410 UniProtKB Coiled coil 353 384 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06410 UniProtKB Mutagenesis 24 24 . . . Note=Decreases affinity for ATG13. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15743910;Dbxref=PMID:15743910 +##sequence-region P35193 1 415 +P35193 UniProtKB Chain 1 415 . . . ID=PRO_0000064722;Note=Autophagy-related protein 19 +P35193 UniProtKB Region 21 28 . . . Note=ATG11-binding +P35193 UniProtKB Region 254 367 . . . Note=AMS1-binding +P35193 UniProtKB Region 406 415 . . . Note=ATG8-binding +P35193 UniProtKB Coiled coil 157 187 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35193 UniProtKB Motif 412 415 . . . Note=WXXL +P35193 UniProtKB Modified residue 136 136 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P35193 UniProtKB Modified residue 141 141 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35193 UniProtKB Modified residue 243 243 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P35193 UniProtKB Cross-link 213 213 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16186126;Dbxref=PMID:16186126 +P35193 UniProtKB Cross-link 216 216 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16186126;Dbxref=PMID:16186126 +P35193 UniProtKB Mutagenesis 412 412 . . . Note=Impairs vacuolar transport of LAP4. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19021777;Dbxref=PMID:19021777 +P35193 UniProtKB Mutagenesis 415 415 . . . Note=Impairs vacuolar transport of LAP4. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19021777;Dbxref=PMID:19021777 +P35193 UniProtKB Sequence conflict 412 412 . . . Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35193 UniProtKB Helix 161 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JGE +P35193 UniProtKB Beta strand 262 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZB +P35193 UniProtKB Beta strand 272 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZB +P35193 UniProtKB Beta strand 281 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZB +P35193 UniProtKB Beta strand 295 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZB +P35193 UniProtKB Beta strand 318 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZB +P35193 UniProtKB Beta strand 335 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZB +P35193 UniProtKB Beta strand 342 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZB +P35193 UniProtKB Beta strand 352 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZB +##sequence-region P53104 1 897 +P53104 UniProtKB Chain 1 897 . . . ID=PRO_0000085655;Note=Serine/threonine-protein kinase ATG1 +P53104 UniProtKB Domain 24 325 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53104 UniProtKB Nucleotide binding 30 38 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53104 UniProtKB Region 880 886 . . . Note=Required for Cvt trafficking +P53104 UniProtKB Motif 429 432 . . . Note=LIR +P53104 UniProtKB Compositional bias 542 548 . . . Note=Poly-Gln +P53104 UniProtKB Active site 172 172 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P53104 UniProtKB Binding site 54 54 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53104 UniProtKB Modified residue 34 34 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Modified residue 129 129 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Modified residue 226 226 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20439775;Dbxref=PMID:20439775 +P53104 UniProtKB Modified residue 304 304 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Modified residue 365 365 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Modified residue 390 390 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:21460632;Dbxref=PMID:18407956,PMID:21460632 +P53104 UniProtKB Modified residue 508 508 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17699586;Dbxref=PMID:17699586 +P53104 UniProtKB Modified residue 515 515 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17699586,ECO:0000269|PubMed:21460632;Dbxref=PMID:17699586,PMID:21460632 +P53104 UniProtKB Modified residue 533 533 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Modified residue 551 551 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Modified residue 552 552 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Modified residue 590 590 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Modified residue 621 621 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Modified residue 635 635 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53104 UniProtKB Modified residue 638 638 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53104 UniProtKB Modified residue 647 647 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53104 UniProtKB Modified residue 677 677 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000269|PubMed:21460632;Dbxref=PMID:15665377,PMID:21460632 +P53104 UniProtKB Modified residue 680 680 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Modified residue 683 683 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Modified residue 769 769 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Modified residue 783 783 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Mutagenesis 34 34 . . . Note=Impairs kinase activity. S->D%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Mutagenesis 54 54 . . . Note=Defect in the Cvt pathway. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10995454,ECO:0000269|PubMed:12589048,ECO:0000269|PubMed:23549786;Dbxref=PMID:10995454,PMID:12589048,PMID:23549786 +P53104 UniProtKB Mutagenesis 102 102 . . . Note=Enables the binding of the inhibitor of the kinase activity 1-NA-PP1. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12589048;Dbxref=PMID:12589048 +P53104 UniProtKB Mutagenesis 211 211 . . . Note=Loss of cell viability under starvation. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23549786,ECO:0000269|PubMed:9224897;Dbxref=PMID:23549786,PMID:9224897 +P53104 UniProtKB Mutagenesis 226 226 . . . Note=Leads to constitutive autophosphorylation activity. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20439775;Dbxref=PMID:20439775 +P53104 UniProtKB Mutagenesis 237 237 . . . Note=Loss of cell viability under starvation. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9224897;Dbxref=PMID:9224897 +P53104 UniProtKB Mutagenesis 429 429 . . . Note=Impairs interaction with ATG8 and decreases autophagy efficiency%3B when associated with A-432. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22778255;Dbxref=PMID:22778255 +P53104 UniProtKB Mutagenesis 432 432 . . . Note=Impairs interaction with ATG8 and decreases autophagy efficiency%3B when associated with A-429. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22778255;Dbxref=PMID:22778255 +P53104 UniProtKB Mutagenesis 508 508 . . . Note=Impairs autophagic activity%3B when associated with A-515. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17699586;Dbxref=PMID:17699586 +P53104 UniProtKB Mutagenesis 515 515 . . . Note=Impairs autophagic activity%3B when associated with A-508. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17699586;Dbxref=PMID:17699586 +P53104 UniProtKB Mutagenesis 551 551 . . . Note=Decreases autophagic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Mutagenesis 552 552 . . . Note=Decreases autophagic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Mutagenesis 621 621 . . . Note=Decreases autophagic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Mutagenesis 677 677 . . . Note=Decreases autophagic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Mutagenesis 680 680 . . . Note=Decreases autophagic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Mutagenesis 683 683 . . . Note=Decreases autophagic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Mutagenesis 769 769 . . . Note=Decreases autophagic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Mutagenesis 783 783 . . . Note=Decreases autophagic activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460632;Dbxref=PMID:21460632 +P53104 UniProtKB Mutagenesis 884 884 . . . Note=No effect. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12589048;Dbxref=PMID:12589048 +P53104 UniProtKB Mutagenesis 886 886 . . . Note=Cvt pathway specific block. L->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12589048;Dbxref=PMID:12589048 +##sequence-region Q06159 1 398 +Q06159 UniProtKB Chain 1 398 . . . ID=PRO_0000268627;Note=Autophagy-related protein 39 +Q06159 UniProtKB Transmembrane 148 164 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06159 UniProtKB Motif 8 11 . . . Note=ATG8-binding;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26040717;Dbxref=PMID:26040717 +Q06159 UniProtKB Motif 52 59 . . . Note=ATG11-binding;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26040717;Dbxref=PMID:26040717 +Q06159 UniProtKB Mutagenesis 52 59 . . . Note=Impairs interaction with ATG8 and decreases subsequent reticulophagy. DVLSNTSS->AAAAAAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26040717;Dbxref=PMID:26040717 +##sequence-region P53867 1 494 +P53867 UniProtKB Chain 1 494 . . . ID=PRO_0000215870;Note=Cysteine protease ATG4 +P53867 UniProtKB Active site 147 147 . . . Note=Nucleophile +P53867 UniProtKB Active site 322 322 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53867 UniProtKB Active site 324 324 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53867 UniProtKB Modified residue 488 488 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53867 UniProtKB Mutagenesis 147 147 . . . Note=Abolishes the proteolytic activity and decreases autophagy. C->S%2CA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11038174;Dbxref=PMID:11038174 +##sequence-region Q12380 1 294 +Q12380 UniProtKB Chain 1 294 . . . ID=PRO_0000219010;Note=Autophagy protein 5 +Q12380 UniProtKB Cross-link 149 149 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ATG12) +Q12380 UniProtKB Mutagenesis 149 149 . . . Note=Loss of conjugation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9759731;Dbxref=PMID:9759731 +Q12380 UniProtKB Helix 1 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Beta strand 12 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Helix 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Helix 30 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Beta strand 34 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Helix 45 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Helix 49 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Helix 57 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Beta strand 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Turn 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W1S +Q12380 UniProtKB Beta strand 71 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Beta strand 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Beta strand 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYM +Q12380 UniProtKB Helix 87 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Turn 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYM +Q12380 UniProtKB Beta strand 115 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Beta strand 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYM +Q12380 UniProtKB Helix 139 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Beta strand 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Helix 160 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Helix 167 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Helix 182 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Beta strand 202 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Beta strand 208 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Helix 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Helix 233 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Turn 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Beta strand 248 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Beta strand 255 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Helix 263 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +Q12380 UniProtKB Beta strand 277 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYO +##sequence-region P53722 1 227 +P53722 UniProtKB Chain 1 227 . . . ID=PRO_0000203472;Note=Mitochondrial inner membrane protease ATP23 +P53722 UniProtKB Active site 125 125 . . . . +P53722 UniProtKB Metal binding 124 124 . . . Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53722 UniProtKB Metal binding 128 128 . . . Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53722 UniProtKB Mutagenesis 124 124 . . . Note=Abolishes proteolytic processing of ATP6%2C but still promotes assembly of the ATP6 precursor into the ATPase CF(0) particle. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17135288;Dbxref=PMID:17135288 +P53722 UniProtKB Mutagenesis 125 125 . . . Note=Abolishes proteolytic processing of ATP6%2C but still promotes assembly of the ATP6 precursor into the ATPase CF(0) particle. E->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17135288,ECO:0000269|PubMed:17135290;Dbxref=PMID:17135288,PMID:17135290 +P53722 UniProtKB Mutagenesis 128 128 . . . Note=Abolishes proteolytic processing of ATP6%2C but still promotes assembly of the ATP6 precursor into the ATPase CF(0) particle. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17135288;Dbxref=PMID:17135288 +##sequence-region Q12092 1 213 +Q12092 UniProtKB Chain 1 213 . . . ID=PRO_0000232994;Note=Autophagy-related protein 29 +Q12092 UniProtKB Modified residue 106 106 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12092 UniProtKB Modified residue 187 187 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12092 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40458 1 529 +P40458 UniProtKB Chain 1 529 . . . ID=PRO_0000086920;Note=Autophagy-related protein 32 +P40458 UniProtKB Transmembrane 390 414 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40458 UniProtKB Modified residue 114 114 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21757540;Dbxref=PMID:21757540 +P40458 UniProtKB Modified residue 119 119 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21757540;Dbxref=PMID:21757540 +P40458 UniProtKB Mutagenesis 114 114 . . . Note=Abolishes mitophagy and impairs interaction with ATG11. S->A%2CN%2CG%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21757540;Dbxref=PMID:21757540 +P40458 UniProtKB Mutagenesis 119 119 . . . Note=Decreases mitophagy and impairs interaction with ATG11. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21757540;Dbxref=PMID:21757540 +##sequence-region P46983 1 293 +P46983 UniProtKB Chain 1 293 . . . ID=PRO_0000203020;Note=Autophagy-related protein 36 +##sequence-region Q12048 1 136 +Q12048 UniProtKB Chain 1 136 . . . ID=PRO_0000270559;Note=Autophagy-related protein 41 +Q12048 UniProtKB Region 127 136 . . . Note=ATG9-binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26565778;Dbxref=PMID:26565778 +##sequence-region P38862 1 630 +P38862 UniProtKB Chain 1 630 . . . ID=PRO_0000212822;Note=Ubiquitin-like modifier-activating enzyme ATG7 +P38862 UniProtKB Region 591 630 . . . Note=Homodimerization +P38862 UniProtKB Motif 331 336 . . . Note=GXGXXG motif +P38862 UniProtKB Active site 507 507 . . . Note=Glycyl thioester intermediate +P38862 UniProtKB Mutagenesis 333 333 . . . Note=Loss of interaction with ATG8 and ATG12%2C and no more ATG12-ATG5 conjugate. Defect in Cvt pathway and autophagy. G->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10233150,ECO:0000269|PubMed:11100732;Dbxref=PMID:10233150,PMID:11100732 +P38862 UniProtKB Mutagenesis 443 443 . . . Note=Loss of interaction with ATG8. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22055191;Dbxref=PMID:22055191 +P38862 UniProtKB Mutagenesis 466 466 . . . Note=Loss of interaction with ATG8%3B when associated with F-486 and A-490. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22055191;Dbxref=PMID:22055191 +P38862 UniProtKB Mutagenesis 486 486 . . . Note=Loss of interaction with ATG8%3B when associated with A-466 and A-490. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22055191;Dbxref=PMID:22055191 +P38862 UniProtKB Mutagenesis 490 490 . . . Note=Loss of interaction with ATG8%3B when associated with A-466 and F-486. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22055191;Dbxref=PMID:22055191 +P38862 UniProtKB Mutagenesis 507 507 . . . Note=Loss of interaction with ATG8 and ATG12 and no more formation of ATG12-ATG5 conjugate. Defect in Cvt pathway and autophagy. C->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10233150,ECO:0000269|PubMed:11100732,ECO:0000269|PubMed:15277523;Dbxref=PMID:10233150,PMID:11100732,PMID:15277523 +P38862 UniProtKB Mutagenesis 507 507 . . . Note=Instead of the formation of an intermediate complex with a thiol ester bond between ATG7 (E1-like enzyme) and ATG8 (substrate) or between ATG7 and ATG12 (substrate)%2C a stable complex with an O-ester bond is formed. No more formation of ATG12-ATG5 conjugate. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10233150,ECO:0000269|PubMed:11100732,ECO:0000269|PubMed:15277523;Dbxref=PMID:10233150,PMID:11100732,PMID:15277523 +P38862 UniProtKB Mutagenesis 550 550 . . . Note=Loss of interaction with ATG8. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22055191;Dbxref=PMID:22055191 +P38862 UniProtKB Beta strand 12 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Helix 19 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Turn 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7G +P38862 UniProtKB Beta strand 36 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Beta strand 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VH2 +P38862 UniProtKB Beta strand 56 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Helix 64 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Beta strand 68 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GSL +P38862 UniProtKB Beta strand 78 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Helix 90 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Helix 98 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Helix 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Beta strand 123 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Turn 131 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Beta strand 135 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Beta strand 151 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Helix 159 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Helix 165 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Beta strand 179 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Beta strand 189 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Helix 194 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Beta strand 202 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Helix 219 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Beta strand 235 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Beta strand 243 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Beta strand 248 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Beta strand 263 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7F +P38862 UniProtKB Beta strand 269 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Beta strand 279 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Beta strand 284 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7H +P38862 UniProtKB Helix 289 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUJ +P38862 UniProtKB Helix 294 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Helix 319 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Beta strand 326 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Helix 334 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Beta strand 350 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Turn 364 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Helix 372 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Beta strand 376 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VH1 +P38862 UniProtKB Helix 379 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Beta strand 391 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GSK +P38862 UniProtKB Beta strand 395 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Helix 413 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Beta strand 431 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Beta strand 438 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VH4 +P38862 UniProtKB Helix 441 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Helix 444 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Beta strand 456 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Beta strand 464 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Helix 486 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Beta strand 490 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Beta strand 494 496 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VH1 +P38862 UniProtKB Turn 498 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Helix 504 508 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Helix 513 529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Beta strand 537 540 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Beta strand 547 552 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Turn 553 556 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Beta strand 557 561 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Turn 570 572 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Helix 574 583 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Helix 585 593 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Helix 595 602 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Helix 604 612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38862 UniProtKB Helix 616 618 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LI5 +P38862 UniProtKB Helix 627 629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LI5 +##sequence-region P38182 1 117 +P38182 UniProtKB Chain 1 116 . . . ID=PRO_0000017242;Note=Autophagy-related protein 8 +P38182 UniProtKB Propeptide 117 117 . . . ID=PRO_0000017243;Note=Removed in mature form +P38182 UniProtKB Site 116 117 . . . Note=Cleavage%3B by ATG4 +P38182 UniProtKB Lipidation 116 116 . . . Note=Phosphatidylethanolamine amidated glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11100732;Dbxref=PMID:11100732 +P38182 UniProtKB Mutagenesis 26 26 . . . Note=No effect on autophagic activity. K->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20428927;Dbxref=PMID:20428927 +P38182 UniProtKB Mutagenesis 28 28 . . . Note=Impairs ATG19-binding and autophagic activity. R->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19021777,ECO:0000269|PubMed:19398890;Dbxref=PMID:19021777,PMID:19398890 +P38182 UniProtKB Mutagenesis 48 48 . . . Note=Impairs autophagic activity. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19398890;Dbxref=PMID:19398890 +P38182 UniProtKB Mutagenesis 49 49 . . . Note=Impairs ATG19-binding%2C PE-conjugation%2C and autophagic activity. Y->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16680092,ECO:0000269|PubMed:19398890;Dbxref=PMID:16680092,PMID:19398890 +P38182 UniProtKB Mutagenesis 50 50 . . . Note=Impairs ATG19-binding and autophagic activity. L->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16680092,ECO:0000269|PubMed:19398890;Dbxref=PMID:16680092,PMID:19398890 +P38182 UniProtKB Mutagenesis 52 52 . . . Note=Significantly decreases ATG19-binding and autophagic activity. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19021777;Dbxref=PMID:19021777 +P38182 UniProtKB Mutagenesis 55 55 . . . Note=Impairs autophagic activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19398890;Dbxref=PMID:19398890 +P38182 UniProtKB Mutagenesis 67 67 . . . Note=Significantly decreases ATG19-binding and autophagic activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19021777;Dbxref=PMID:19021777 +P38182 UniProtKB Mutagenesis 77 77 . . . Note=Impairs interaction with ATG4%2C cleavage by ATG4%2C PAS localization%2C and autophagic activity%3B when associated with A-79. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16680092;Dbxref=PMID:16680092 +P38182 UniProtKB Mutagenesis 79 79 . . . Note=Impairs interaction with ATG4%2C cleavage by ATG4%2C PAS localization%2C and autophagic activity%3B when associated with A-77. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16680092;Dbxref=PMID:16680092 +P38182 UniProtKB Mutagenesis 116 116 . . . Note=No cleaving of the C-terminal R-117 by ATG4. Defect in Cvt pathway and autophagy. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11038174;Dbxref=PMID:11038174 +P38182 UniProtKB Mutagenesis 117 117 . . . Note=Normal processing after G-116 by ATG4. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11038174;Dbxref=PMID:11038174 +P38182 UniProtKB Helix 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VH3 +P38182 UniProtKB Helix 11 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38182 UniProtKB Beta strand 26 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38182 UniProtKB Beta strand 37 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KWC +P38182 UniProtKB Beta strand 48 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38182 UniProtKB Helix 57 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38182 UniProtKB Beta strand 76 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38182 UniProtKB Beta strand 87 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KWC +P38182 UniProtKB Helix 91 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +P38182 UniProtKB Beta strand 105 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RUI +##sequence-region Q12691 1 1091 +Q12691 UniProtKB Chain 1 1091 . . . ID=PRO_0000046244;Note=Sodium transport ATPase 5 +Q12691 UniProtKB Topological domain 1 63 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Transmembrane 64 84 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Topological domain 85 90 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Transmembrane 91 111 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Topological domain 112 282 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Transmembrane 283 303 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Topological domain 304 312 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Transmembrane 313 333 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Topological domain 334 815 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Transmembrane 816 836 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Topological domain 837 848 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Transmembrane 849 869 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Topological domain 870 885 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Transmembrane 886 906 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Topological domain 907 943 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Transmembrane 944 964 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Topological domain 965 991 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Transmembrane 992 1012 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Topological domain 1013 1021 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Transmembrane 1022 1042 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Topological domain 1043 1091 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12691 UniProtKB Active site 369 369 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P32453 1 318 +P32453 UniProtKB Transit peptide 1 40 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32453 UniProtKB Chain 41 318 . . . ID=PRO_0000002535;Note=Protein ATP11%2C mitochondrial +P32453 UniProtKB Modified residue 109 109 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region P00854 1 259 +P00854 UniProtKB Propeptide 1 10 . . . ID=PRO_0000002626;Note=Removed in mature form;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2894987;Dbxref=PMID:2894987 +P00854 UniProtKB Chain 11 259 . . . ID=PRO_0000002627;Note=ATP synthase subunit a +P00854 UniProtKB Transmembrane 36 56 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00854 UniProtKB Transmembrane 92 112 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00854 UniProtKB Transmembrane 125 145 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00854 UniProtKB Transmembrane 150 170 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00854 UniProtKB Transmembrane 191 211 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00854 UniProtKB Transmembrane 216 236 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00854 UniProtKB Natural variant 171 171 . . . Note=In strain: D273-10B/A1. I->M +P00854 UniProtKB Natural variant 177 177 . . . Note=In strain: D273-10B/A1. F->I +P00854 UniProtKB Natural variant 231 231 . . . Note=In strain: D273-10B/A1. M->I +P00854 UniProtKB Natural variant 241 241 . . . Note=In strain: D273-10B/A1. G->S +P00854 UniProtKB Natural variant 245 245 . . . Note=In strain: D273-10B/A1. A->T +P00854 UniProtKB Natural variant 255 256 . . . Note=In strain: D273-10B/A1. AV->TL +##sequence-region Q12165 1 160 +Q12165 UniProtKB Transit peptide 1 22 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8026496;Dbxref=PMID:8026496 +Q12165 UniProtKB Chain 23 160 . . . ID=PRO_0000002671;Note=ATP synthase subunit delta%2C mitochondrial +Q12165 UniProtKB Beta strand 34 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +Q12165 UniProtKB Beta strand 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OFN +Q12165 UniProtKB Beta strand 51 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +Q12165 UniProtKB Beta strand 56 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +Q12165 UniProtKB Beta strand 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +Q12165 UniProtKB Beta strand 70 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +Q12165 UniProtKB Beta strand 78 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +Q12165 UniProtKB Beta strand 86 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +Q12165 UniProtKB Beta strand 95 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +Q12165 UniProtKB Turn 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +Q12165 UniProtKB Beta strand 104 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +Q12165 UniProtKB Beta strand 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OFN +Q12165 UniProtKB Helix 115 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +Q12165 UniProtKB Helix 120 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +Q12165 UniProtKB Beta strand 136 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +Q12165 UniProtKB Helix 140 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +##sequence-region Q06405 1 101 +Q06405 UniProtKB Transit peptide 1 6 . . . Note=Mitochondrion +Q06405 UniProtKB Chain 7 101 . . . ID=PRO_0000002637;Note=ATP synthase subunit f%2C mitochondrial +##sequence-region P31386 1 333 +P31386 UniProtKB Chain 1 333 . . . ID=PRO_0000206648;Note=Protein ATS1 +P31386 UniProtKB Repeat 1 53 . . . Note=RCC1 1 +P31386 UniProtKB Repeat 55 104 . . . Note=RCC1 2 +P31386 UniProtKB Repeat 146 197 . . . Note=RCC1 3 +P31386 UniProtKB Repeat 286 333 . . . Note=RCC1 4 +P31386 UniProtKB Sequence conflict 305 305 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31386 UniProtKB Sequence conflict 305 305 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31386 UniProtKB Sequence conflict 305 305 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31386 UniProtKB Sequence conflict 305 305 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31386 UniProtKB Beta strand 3 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 16 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 23 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4D4O +P31386 UniProtKB Beta strand 38 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 45 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 57 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 76 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 89 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 96 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 108 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 115 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4D4O +P31386 UniProtKB Beta strand 132 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 140 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 148 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 158 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 165 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 182 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 189 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 201 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Helix 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 217 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 224 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 231 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Turn 237 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 241 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 263 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 270 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 281 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4D4O +P31386 UniProtKB Beta strand 287 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 296 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4D4Q +P31386 UniProtKB Beta strand 311 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 321 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +P31386 UniProtKB Beta strand 326 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +##sequence-region P38636 1 73 +P38636 UniProtKB Chain 1 73 . . . ID=PRO_0000212535;Note=Metal homeostasis factor ATX1 +P38636 UniProtKB Domain 5 69 . . . Note=HMA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P38636 UniProtKB Metal binding 15 15 . . . Note=Copper +P38636 UniProtKB Metal binding 18 18 . . . Note=Copper +P38636 UniProtKB Sequence conflict 8 8 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38636 UniProtKB Beta strand 5 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CC8 +P38636 UniProtKB Helix 16 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CC8 +P38636 UniProtKB Turn 28 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CC8 +P38636 UniProtKB Beta strand 32 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CC8 +P38636 UniProtKB Turn 40 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CC8 +P38636 UniProtKB Beta strand 44 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CC8 +P38636 UniProtKB Helix 53 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CC8 +P38636 UniProtKB Turn 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K7R +P38636 UniProtKB Beta strand 67 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CC8 +##sequence-region P40851 1 1208 +P40851 UniProtKB Chain 1 1208 . . . ID=PRO_0000074417;Note=Putative protease AXL1 +P40851 UniProtKB Active site 71 71 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10096 +P40851 UniProtKB Metal binding 68 68 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10096 +P40851 UniProtKB Metal binding 72 72 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10096 +P40851 UniProtKB Metal binding 156 156 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10096 +P40851 UniProtKB Modified residue 262 262 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P40851 UniProtKB Sequence conflict 113 113 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06541 1 321 +Q06541 UniProtKB Chain 1 321 . . . ID=PRO_0000228135;Note=Protein ARV1 +Q06541 UniProtKB Transmembrane 179 199 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06541 UniProtKB Transmembrane 214 234 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06541 UniProtKB Transmembrane 248 270 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06541 UniProtKB Transmembrane 272 292 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06541 UniProtKB Glycosylation 296 296 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06822 1 443 +Q06822 UniProtKB Chain 1 443 . . . ID=PRO_0000252299;Note=ASTRA-associated protein 1 +Q06822 UniProtKB Repeat 23 67 . . . Note=WD 1 +Q06822 UniProtKB Repeat 71 110 . . . Note=WD 2 +Q06822 UniProtKB Repeat 258 295 . . . Note=WD 3 +Q06822 UniProtKB Repeat 318 359 . . . Note=WD 4 +##sequence-region P46993 1 209 +P46993 UniProtKB Chain 1 209 . . . ID=PRO_0000203025;Note=Protein ASG7 +P46993 UniProtKB Topological domain 1 49 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46993 UniProtKB Transmembrane 50 70 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46993 UniProtKB Topological domain 71 184 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46993 UniProtKB Transmembrane 185 205 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46993 UniProtKB Topological domain 206 209 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46993 UniProtKB Modified residue 121 121 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P46993 UniProtKB Modified residue 123 123 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P46993 UniProtKB Modified residue 125 125 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P46993 UniProtKB Modified residue 153 153 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region P54074 1 624 +P54074 UniProtKB Chain 1 624 . . . ID=PRO_0000203295;Note=Protein ASI1 +P54074 UniProtKB Topological domain 1 69 . . . Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54074 UniProtKB Transmembrane 70 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54074 UniProtKB Topological domain 91 116 . . . Note=Nuclear;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54074 UniProtKB Transmembrane 117 137 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54074 UniProtKB Topological domain 138 152 . . . Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54074 UniProtKB Transmembrane 153 173 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54074 UniProtKB Topological domain 174 209 . . . Note=Nuclear;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54074 UniProtKB Transmembrane 210 230 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54074 UniProtKB Topological domain 231 273 . . . Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54074 UniProtKB Transmembrane 274 294 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54074 UniProtKB Topological domain 295 624 . . . Note=Nuclear;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54074 UniProtKB Zinc finger 568 608 . . . Note=RING-type%3B atypical +P54074 UniProtKB Glycosylation 2 2 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16735580,ECO:0000269|PubMed:17085444;Dbxref=PMID:16735580,PMID:17085444 +P54074 UniProtKB Glycosylation 19 19 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16735580,ECO:0000269|PubMed:17085444;Dbxref=PMID:16735580,PMID:17085444 +P54074 UniProtKB Glycosylation 29 29 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16735580,ECO:0000269|PubMed:17085444;Dbxref=PMID:16735580,PMID:17085444 +P54074 UniProtKB Mutagenesis 583 583 . . . Note=In ASI1-21HA%3B when associated with S-585%3B abolishes function. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16735580;Dbxref=PMID:16735580 +P54074 UniProtKB Mutagenesis 585 585 . . . Note=In ASI1-21HA%3B when associated with S-583%3B abolishes function. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16735580;Dbxref=PMID:16735580 +##sequence-region P48361 1 1146 +P48361 UniProtKB Chain 1 1146 . . . ID=PRO_0000064699;Note=Activator of SKN7 protein 10 +P48361 UniProtKB Domain 482 606 . . . Note=PH +P48361 UniProtKB Compositional bias 22 26 . . . Note=Poly-Gly +P48361 UniProtKB Compositional bias 625 628 . . . Note=Poly-Ser +P48361 UniProtKB Compositional bias 933 938 . . . Note=Poly-Asn +P48361 UniProtKB Compositional bias 958 961 . . . Note=Poly-Gln +P48361 UniProtKB Compositional bias 972 975 . . . Note=Poly-Ser +P48361 UniProtKB Modified residue 344 344 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P48361 UniProtKB Modified residue 793 793 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P48361 UniProtKB Modified residue 808 808 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P48361 UniProtKB Modified residue 944 944 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48361 UniProtKB Modified residue 969 969 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48361 UniProtKB Modified residue 1017 1017 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P48361 UniProtKB Modified residue 1070 1070 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +P48361 UniProtKB Modified residue 1095 1095 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48361 UniProtKB Modified residue 1098 1098 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48361 UniProtKB Sequence conflict 57 57 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P48361 UniProtKB Sequence conflict 346 346 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P48361 UniProtKB Sequence conflict 464 464 . . . Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P48361 UniProtKB Sequence conflict 467 467 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P48361 UniProtKB Sequence conflict 603 603 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P48361 UniProtKB Sequence conflict 906 906 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32660 1 1571 +P32660 UniProtKB Chain 1 1571 . . . ID=PRO_0000046235;Note=Phospholipid-transporting ATPase DNF1 +P32660 UniProtKB Topological domain 1 214 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Transmembrane 215 235 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Topological domain 236 239 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Transmembrane 240 260 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Topological domain 261 553 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Transmembrane 554 574 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Topological domain 575 594 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Transmembrane 595 615 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Topological domain 616 1188 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Transmembrane 1189 1209 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Topological domain 1210 1219 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Transmembrane 1220 1240 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Topological domain 1241 1270 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Transmembrane 1271 1291 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Topological domain 1292 1307 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Transmembrane 1308 1328 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Topological domain 1329 1334 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Transmembrane 1335 1355 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Topological domain 1356 1375 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Transmembrane 1376 1396 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Topological domain 1397 1571 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32660 UniProtKB Active site 667 667 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32660 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +P32660 UniProtKB Modified residue 70 70 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32660 UniProtKB Modified residue 81 81 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32660 UniProtKB Modified residue 85 85 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32660 UniProtKB Modified residue 92 92 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32660 UniProtKB Modified residue 94 94 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32660 UniProtKB Modified residue 104 104 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32660 UniProtKB Modified residue 109 109 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32660 UniProtKB Modified residue 351 351 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32660 UniProtKB Modified residue 354 354 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12675 +P32660 UniProtKB Modified residue 358 358 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12675 +P32660 UniProtKB Modified residue 365 365 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32660 UniProtKB Modified residue 368 368 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12675 +P32660 UniProtKB Modified residue 1506 1506 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P32660 UniProtKB Modified residue 1551 1551 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32660 UniProtKB Modified residue 1552 1552 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32660 UniProtKB Modified residue 1563 1563 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32660 UniProtKB Cross-link 895 895 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12675 +##sequence-region Q12674 1 1656 +Q12674 UniProtKB Chain 1 1656 . . . ID=PRO_0000046237;Note=Probable phospholipid-transporting ATPase DNF3 +Q12674 UniProtKB Topological domain 1 164 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q12674 UniProtKB Transmembrane 165 185 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12674 UniProtKB Topological domain 186 451 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12674 UniProtKB Transmembrane 452 472 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12674 UniProtKB Topological domain 473 495 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q12674 UniProtKB Transmembrane 496 516 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12674 UniProtKB Topological domain 517 1157 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12674 UniProtKB Transmembrane 1158 1178 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12674 UniProtKB Topological domain 1179 1318 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q12674 UniProtKB Transmembrane 1319 1339 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12674 UniProtKB Topological domain 1340 1365 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12674 UniProtKB Transmembrane 1366 1386 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12674 UniProtKB Topological domain 1387 1395 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q12674 UniProtKB Transmembrane 1396 1416 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12674 UniProtKB Topological domain 1417 1432 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12674 UniProtKB Transmembrane 1433 1453 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12674 UniProtKB Topological domain 1454 1473 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q12674 UniProtKB Transmembrane 1474 1494 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12674 UniProtKB Topological domain 1495 1656 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +Q12674 UniProtKB Active site 566 566 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12674 UniProtKB Modified residue 627 627 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q03153 1 612 +Q03153 UniProtKB Transit peptide 1 14 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03153 UniProtKB Chain 15 612 . . . ID=PRO_0000203288;Note=ATPase synthesis protein 25%2C mitochondrial +##sequence-region P30902 1 174 +P30902 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1832157;Dbxref=PMID:1832157 +P30902 UniProtKB Chain 2 174 . . . ID=PRO_0000071681;Note=ATP synthase subunit d%2C mitochondrial +P30902 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1832157;Dbxref=PMID:1832157 +##sequence-region P00856 1 48 +P00856 UniProtKB Chain 1 48 . . . ID=PRO_0000195607;Note=ATP synthase protein 8 +P00856 UniProtKB Transmembrane 13 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12406 1 477 +Q12406 UniProtKB Chain 1 477 . . . ID=PRO_0000089122;Note=Actin-related protein 7 +Q12406 UniProtKB Mutagenesis 19 19 . . . Note=Impaired heterodimerization with ARP9. Temperature-sensitive phenotype. Moderate suppressor of Ty phenotype. A->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12805231,ECO:0000269|PubMed:9844636;Dbxref=PMID:12805231,PMID:9844636 +Q12406 UniProtKB Mutagenesis 33 33 . . . Note=Impaired heterodimerization with ARP9. Temperature-sensitive phenotype. Moderate suppressor of Ty phenotype. S->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12805231,ECO:0000269|PubMed:9844636;Dbxref=PMID:12805231,PMID:9844636 +Q12406 UniProtKB Mutagenesis 396 396 . . . Note=Temperature-sensitive phenotype. Moderate suppressor of Ty phenotype. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9844636;Dbxref=PMID:9844636 +Q12406 UniProtKB Mutagenesis 411 411 . . . Note=Impaired heterodimerization with ARP9. Temperature-sensitive phenotype. Moderate suppressor of Ty phenotype. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12805231,ECO:0000269|PubMed:9844636;Dbxref=PMID:12805231,PMID:9844636 +Q12406 UniProtKB Beta strand 8 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Beta strand 14 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Beta strand 24 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Beta strand 28 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Beta strand 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE +Q12406 UniProtKB Beta strand 45 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE +Q12406 UniProtKB Helix 51 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Beta strand 66 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Beta strand 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE +Q12406 UniProtKB Helix 80 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Turn 99 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE +Q12406 UniProtKB Beta strand 104 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Beta strand 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE +Q12406 UniProtKB Helix 116 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Turn 128 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Beta strand 134 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 141 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Turn 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Beta strand 152 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Beta strand 164 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 186 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 198 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 217 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 227 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 243 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 283 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Beta strand 287 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 293 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Beta strand 297 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 303 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 316 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 325 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 329 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Turn 339 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 344 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE +Q12406 UniProtKB Helix 381 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Beta strand 391 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 397 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 404 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Beta strand 423 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WEE +Q12406 UniProtKB Helix 429 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 435 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 449 451 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Beta strand 454 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +Q12406 UniProtKB Helix 457 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +##sequence-region P40518 1 154 +P40518 UniProtKB Chain 1 154 . . . ID=PRO_0000124059;Note=Actin-related protein 2/3 complex subunit 5 +P40518 UniProtKB Modified residue 142 142 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q06598 1 404 +Q06598 UniProtKB Chain 1 404 . . . ID=PRO_0000064440;Note=Arsenical-resistance protein 3 +Q06598 UniProtKB Topological domain 1 34 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482 +Q06598 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06598 UniProtKB Topological domain 56 69 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482 +Q06598 UniProtKB Transmembrane 70 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06598 UniProtKB Topological domain 91 113 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482 +Q06598 UniProtKB Transmembrane 114 134 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06598 UniProtKB Topological domain 135 141 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482 +Q06598 UniProtKB Transmembrane 142 162 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06598 UniProtKB Topological domain 163 169 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482 +Q06598 UniProtKB Transmembrane 170 190 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06598 UniProtKB Topological domain 191 216 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482 +Q06598 UniProtKB Transmembrane 217 237 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06598 UniProtKB Topological domain 238 245 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482 +Q06598 UniProtKB Transmembrane 246 266 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06598 UniProtKB Topological domain 267 280 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482 +Q06598 UniProtKB Transmembrane 281 301 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06598 UniProtKB Topological domain 302 343 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482 +Q06598 UniProtKB Transmembrane 344 364 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06598 UniProtKB Topological domain 365 369 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482 +Q06598 UniProtKB Transmembrane 370 390 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06598 UniProtKB Topological domain 391 404 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9374482;Dbxref=PMID:9374482 +Q06598 UniProtKB Glycosylation 201 201 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +Q06598 UniProtKB Glycosylation 365 365 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +Q06598 UniProtKB Mutagenesis 90 90 . . . Note=Leads to ER retention and arsenite sensitivity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24291645;Dbxref=PMID:24291645 +Q06598 UniProtKB Mutagenesis 117 117 . . . Note=Impairs cell membrane localization%2C and leads to arsenite sensitivity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064 +Q06598 UniProtKB Mutagenesis 150 150 . . . Note=Leads to ER retention%2C protein unstability and arsenite sensitivity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064 +Q06598 UniProtKB Mutagenesis 151 151 . . . Note=Leads to complete loss of metalloid transport function. C->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24291645;Dbxref=PMID:24291645 +Q06598 UniProtKB Mutagenesis 158 158 . . . Note=Impairs cell membrane localization%2C and leads to arsenite sensitivity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064 +Q06598 UniProtKB Mutagenesis 169 169 . . . Note=Greatly reduces arsenite efflux. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24291645;Dbxref=PMID:24291645 +Q06598 UniProtKB Mutagenesis 176 176 . . . Note=Leads to ER retention%2C protein unstability and arsenite sensitivity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064 +Q06598 UniProtKB Mutagenesis 192 192 . . . Note=Results in moderate reduction of arsenite transport capacities and sorting perturbations. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24291645;Dbxref=PMID:24291645 +Q06598 UniProtKB Mutagenesis 230 230 . . . Note=Leads to ER retention%2C protein unstability and arsenite sensitivity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064 +Q06598 UniProtKB Mutagenesis 266 266 . . . Note=Impairs arsenite resistance. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064 +Q06598 UniProtKB Mutagenesis 283 283 . . . Note=Does not alter the arsenite/proton exchange across the plasma membrane. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24291645;Dbxref=PMID:24291645 +Q06598 UniProtKB Mutagenesis 290 290 . . . Note=Leads to ER retention%2C protein unstability and arsenite sensitivity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064 +Q06598 UniProtKB Mutagenesis 316 316 . . . Note=Results in moderate reduction of arsenite transport capacities and sorting perturbations. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24291645;Dbxref=PMID:24291645 +Q06598 UniProtKB Mutagenesis 318 318 . . . Note=Results in moderate reduction of arsenite transport capacities and sorting perturbations. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24291645;Dbxref=PMID:24291645 +Q06598 UniProtKB Mutagenesis 333 333 . . . Note=Results in moderate reduction of arsenite transport capacities and sorting perturbations. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24291645;Dbxref=PMID:24291645 +Q06598 UniProtKB Mutagenesis 344 344 . . . Note=Results in moderate reduction of arsenite transport capacities and sorting perturbations. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24291645;Dbxref=PMID:24291645 +Q06598 UniProtKB Mutagenesis 345 345 . . . Note=Leads to ER retention%2C protein unstability and arsenite sensitivity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064 +Q06598 UniProtKB Mutagenesis 349 349 . . . Note=Impairs arsenite resistance. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064 +Q06598 UniProtKB Mutagenesis 351 351 . . . Note=Leads to ER retention%2C protein unstability and arsenite sensitivity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064 +Q06598 UniProtKB Mutagenesis 352 352 . . . Note=Impairs arsenite resistance. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064 +Q06598 UniProtKB Mutagenesis 353 353 . . . Note=Impairs arsenite resistance. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064 +Q06598 UniProtKB Mutagenesis 380 380 . . . Note=Impairs arsenite resistance. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26123064;Dbxref=PMID:26123064 +##sequence-region Q8TGM7 1 61 +Q8TGM7 UniProtKB Chain 1 61 . . . ID=PRO_0000262870;Note=Putative uncharacterized protein ART2 +##sequence-region P35734 1 292 +P35734 UniProtKB Chain 1 292 . . . ID=PRO_0000211317;Note=DASH complex subunit ASK1 +P35734 UniProtKB Modified residue 26 26 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:12408861;Dbxref=PMID:18407956,PMID:12408861 +P35734 UniProtKB Modified residue 118 118 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12408861;Dbxref=PMID:12408861 +P35734 UniProtKB Modified residue 134 134 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:12408861;Dbxref=PMID:17330950,PMID:19779198,PMID:12408861 +P35734 UniProtKB Modified residue 140 140 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12408861;Dbxref=PMID:12408861 +P35734 UniProtKB Modified residue 155 155 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P35734 UniProtKB Modified residue 156 156 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P35734 UniProtKB Modified residue 200 200 . . . Note=Phosphoserine%3B by IPL1;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:12408861;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:12408861 +P35734 UniProtKB Modified residue 216 216 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35734 UniProtKB Modified residue 250 250 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12408861;Dbxref=PMID:12408861 +P35734 UniProtKB Sequence conflict 14 14 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35734 UniProtKB Sequence conflict 14 14 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P35183 1 429 +P35183 UniProtKB Chain 1 429 . . . ID=PRO_0000064710;Note=Protein AST1 +P35183 UniProtKB Sequence conflict 326 429 . . . Note=TVGDYVANYKEDIFDSWDNPSANARKMFGSIIWSYNYTHYYFDPNAKTASANNDWIEQCGDFLKNGTVKCVVDKVYDWKDHKEAFSYMATQRAQGKLIMNVEKF->HCR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40353 1 525 +P40353 UniProtKB Chain 1 525 . . . ID=PRO_0000064720;Note=Alcohol O-acetyltransferase 1 +P40353 UniProtKB Sequence conflict 84 84 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40353 UniProtKB Sequence conflict 391 391 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53855 1 1592 +P53855 UniProtKB Chain 1 1592 . . . ID=PRO_0000215836;Note=Autophagy-related protein 2 +P53855 UniProtKB Coiled coil 1049 1075 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53855 UniProtKB Modified residue 236 236 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53855 UniProtKB Mutagenesis 83 83 . . . Note=Leads to a severely reduced activity of autophagy and a dispersed localization in the cytoplasm. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11382761;Dbxref=PMID:11382761 +##sequence-region Q12292 1 412 +Q12292 UniProtKB Chain 1 412 . . . ID=PRO_0000235927;Note=Autophagy-related protein 34 +Q12292 UniProtKB Region 246 348 . . . Note=AMS1-binding +Q12292 UniProtKB Beta strand 251 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZK +Q12292 UniProtKB Beta strand 263 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZK +Q12292 UniProtKB Beta strand 269 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZK +Q12292 UniProtKB Beta strand 278 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZK +Q12292 UniProtKB Beta strand 284 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZK +Q12292 UniProtKB Beta strand 303 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZK +Q12292 UniProtKB Beta strand 322 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZK +Q12292 UniProtKB Beta strand 330 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZK +Q12292 UniProtKB Beta strand 338 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KZK +##sequence-region Q05789 1 226 +Q05789 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q05789 UniProtKB Chain 2 226 . . . ID=PRO_0000203237;Note=Autophagy-related protein 38 +Q05789 UniProtKB Coiled coil 52 85 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05789 UniProtKB Coiled coil 161 215 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05789 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q05789 UniProtKB Helix 125 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KC1 +Q05789 UniProtKB Helix 129 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KC1 +Q05789 UniProtKB Helix 156 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KC1 +Q05789 UniProtKB Helix 164 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KC1 +##sequence-region Q01896 1 1091 +Q01896 UniProtKB Chain 1 1091 . . . ID=PRO_0000046243;Note=Sodium transport ATPase 2 +Q01896 UniProtKB Topological domain 1 63 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Transmembrane 64 84 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Topological domain 85 90 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Transmembrane 91 111 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Topological domain 112 282 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Transmembrane 283 303 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Topological domain 304 312 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Transmembrane 313 333 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Topological domain 334 815 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Transmembrane 816 836 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Topological domain 837 848 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Transmembrane 849 869 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Topological domain 870 885 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Transmembrane 886 906 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Topological domain 907 943 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Transmembrane 944 964 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Topological domain 965 991 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Transmembrane 992 1012 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Topological domain 1013 1021 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Transmembrane 1022 1042 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Topological domain 1043 1091 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01896 UniProtKB Active site 369 369 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P22135 1 325 +P22135 UniProtKB Transit peptide 1 32 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22135 UniProtKB Chain 33 325 . . . ID=PRO_0000002421;Note=Protein ATP12%2C mitochondrial +P22135 UniProtKB Sequence conflict 48 48 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38360 1 1216 +P38360 UniProtKB Chain 1 1216 . . . ID=PRO_0000046317;Note=P-type cation-transporting ATPase +P38360 UniProtKB Topological domain 1 556 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38360 UniProtKB Transmembrane 557 578 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38360 UniProtKB Topological domain 579 592 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38360 UniProtKB Transmembrane 593 612 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38360 UniProtKB Topological domain 613 620 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38360 UniProtKB Transmembrane 621 641 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38360 UniProtKB Topological domain 642 659 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38360 UniProtKB Transmembrane 660 680 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38360 UniProtKB Topological domain 681 808 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38360 UniProtKB Transmembrane 809 831 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38360 UniProtKB Topological domain 832 847 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38360 UniProtKB Transmembrane 848 865 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38360 UniProtKB Topological domain 866 1161 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38360 UniProtKB Transmembrane 1162 1181 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38360 UniProtKB Topological domain 1182 1190 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38360 UniProtKB Transmembrane 1191 1209 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38360 UniProtKB Topological domain 1210 1216 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38360 UniProtKB Domain 411 474 . . . Note=HMA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P38360 UniProtKB Region 250 350 . . . Note=Metal-responding degradation signal +P38360 UniProtKB Active site 903 903 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38360 UniProtKB Metal binding 421 421 . . . Note=Copper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P38360 UniProtKB Metal binding 424 424 . . . Note=Copper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P38360 UniProtKB Metal binding 1107 1107 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P38360 UniProtKB Metal binding 1111 1111 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P38360 UniProtKB Mutagenesis 298 298 . . . Note=Abolishes copper resistance but not cadmium resistance%3B when associated with A-300. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18753133;Dbxref=PMID:18753133 +P38360 UniProtKB Mutagenesis 300 300 . . . Note=Abolishes copper resistance but not cadmium resistance%3B when associated with A-298. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18753133;Dbxref=PMID:18753133 +P38360 UniProtKB Mutagenesis 311 311 . . . Note=Abolishes cadmium resistance yet retains the ability to confer copper resistance%3B when associated with A-312. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18753133;Dbxref=PMID:18753133 +P38360 UniProtKB Mutagenesis 312 312 . . . Note=Abolishes cadmium resistance yet retains the ability to confer copper resistance%3B when associated with A-311. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18753133;Dbxref=PMID:18753133 +P38360 UniProtKB Mutagenesis 970 970 . . . Note=Confers localization to the plasma membrane and cadmium transport function. R->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10743563,ECO:0000269|PubMed:17107946;Dbxref=PMID:10743563,PMID:17107946 +P38360 UniProtKB Sequence conflict 382 382 . . . Note=H->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38360 UniProtKB Sequence conflict 382 382 . . . Note=H->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32450 1 94 +P32450 UniProtKB Chain 1 94 . . . ID=PRO_0000064762;Note=Ammonia regulation of amino acid uptake protein +P32450 UniProtKB Repeat 48 57 . . . . +P32450 UniProtKB Repeat 58 67 . . . . +P32450 UniProtKB Compositional bias 41 94 . . . Note=Arg/His/Lys-rich (basic) +##sequence-region P36107 1 401 +P36107 UniProtKB Chain 1 401 . . . ID=PRO_0000064766;Note=Inositol phosphorylceramide synthase catalytic subunit AUR1 +P36107 UniProtKB Topological domain 1 41 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36107 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36107 UniProtKB Topological domain 63 64 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36107 UniProtKB Transmembrane 65 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36107 UniProtKB Topological domain 86 87 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36107 UniProtKB Transmembrane 88 108 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36107 UniProtKB Topological domain 109 155 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36107 UniProtKB Transmembrane 156 176 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36107 UniProtKB Topological domain 177 178 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36107 UniProtKB Transmembrane 179 199 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36107 UniProtKB Topological domain 200 245 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36107 UniProtKB Transmembrane 246 266 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36107 UniProtKB Topological domain 267 268 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36107 UniProtKB Transmembrane 269 289 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36107 UniProtKB Topological domain 290 291 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36107 UniProtKB Transmembrane 292 312 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36107 UniProtKB Topological domain 313 401 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36107 UniProtKB Modified residue 392 392 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P36107 UniProtKB Modified residue 395 395 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P36107 UniProtKB Glycosylation 132 132 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36107 UniProtKB Mutagenesis 137 137 . . . Note=AbA resistant%3B when associated with Y-157. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8593016;Dbxref=PMID:8593016 +P36107 UniProtKB Mutagenesis 157 157 . . . Note=AbA resistant%3B when associated with F-137. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8593016;Dbxref=PMID:8593016 +P36107 UniProtKB Mutagenesis 158 158 . . . Note=In AUR1-1%3B AbA resistant. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8668135;Dbxref=PMID:8668135 +P36107 UniProtKB Mutagenesis 294 294 . . . Note=Abolishes catalytic activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10888667;Dbxref=PMID:10888667 +##sequence-region P39981 1 480 +P39981 UniProtKB Chain 1 480 . . . ID=PRO_0000093835;Note=Vacuolar amino acid transporter 2 +P39981 UniProtKB Transmembrane 72 92 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39981 UniProtKB Transmembrane 95 115 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39981 UniProtKB Transmembrane 145 165 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39981 UniProtKB Transmembrane 214 234 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39981 UniProtKB Transmembrane 263 283 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39981 UniProtKB Transmembrane 297 317 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39981 UniProtKB Transmembrane 338 358 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39981 UniProtKB Transmembrane 394 414 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39981 UniProtKB Transmembrane 447 467 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36062 1 692 +P36062 UniProtKB Chain 1 692 . . . ID=PRO_0000093836;Note=Vacuolar amino acid transporter 3 +P36062 UniProtKB Transmembrane 302 322 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36062 UniProtKB Transmembrane 329 349 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36062 UniProtKB Transmembrane 374 394 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36062 UniProtKB Transmembrane 412 432 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36062 UniProtKB Transmembrane 443 463 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36062 UniProtKB Transmembrane 483 503 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36062 UniProtKB Transmembrane 519 539 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36062 UniProtKB Transmembrane 561 581 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36062 UniProtKB Transmembrane 607 627 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36062 UniProtKB Transmembrane 630 650 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36062 UniProtKB Transmembrane 665 685 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36062 UniProtKB Compositional bias 261 276 . . . Note=Poly-Glu +P36062 UniProtKB Modified residue 59 59 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P36062 UniProtKB Modified residue 119 119 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36062 UniProtKB Modified residue 121 121 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P36062 UniProtKB Modified residue 165 165 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P53629 1 642 +P53629 UniProtKB Chain 1 642 . . . ID=PRO_0000207651;Note=Sterol O-acyltransferase 2 +P53629 UniProtKB Transmembrane 215 235 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53629 UniProtKB Transmembrane 292 312 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53629 UniProtKB Transmembrane 404 424 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53629 UniProtKB Transmembrane 442 462 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53629 UniProtKB Transmembrane 485 505 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53629 UniProtKB Transmembrane 567 587 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53629 UniProtKB Transmembrane 622 642 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53629 UniProtKB Active site 579 579 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53629 UniProtKB Modified residue 175 175 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53629 UniProtKB Modified residue 176 176 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53629 UniProtKB Sequence conflict 80 80 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53629 UniProtKB Sequence conflict 184 184 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53629 UniProtKB Sequence conflict 211 211 . . . Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53629 UniProtKB Sequence conflict 612 612 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P19146 1 181 +P19146 UniProtKB Initiator methionine 1 1 . . . Note=Removed +P19146 UniProtKB Chain 2 181 . . . ID=PRO_0000207419;Note=ADP-ribosylation factor 2 +P19146 UniProtKB Nucleotide binding 25 32 . . . Note=GTP +P19146 UniProtKB Nucleotide binding 126 129 . . . Note=GTP +P19146 UniProtKB Nucleotide binding 160 161 . . . Note=GTP +P19146 UniProtKB Binding site 48 48 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19146 UniProtKB Binding site 70 70 . . . Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19146 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19146 UniProtKB Cross-link 127 127 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11076 +P19146 UniProtKB Helix 10 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3 +P19146 UniProtKB Beta strand 18 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3 +P19146 UniProtKB Helix 30 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3 +P19146 UniProtKB Beta strand 43 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3 +P19146 UniProtKB Beta strand 51 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3 +P19146 UniProtKB Beta strand 61 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3 +P19146 UniProtKB Helix 76 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3 +P19146 UniProtKB Beta strand 86 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3 +P19146 UniProtKB Helix 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3 +P19146 UniProtKB Helix 100 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3 +P19146 UniProtKB Helix 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3 +P19146 UniProtKB Beta strand 120 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3 +P19146 UniProtKB Helix 136 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3 +P19146 UniProtKB Helix 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3 +P19146 UniProtKB Beta strand 153 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3 +P19146 UniProtKB Turn 160 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3 +P19146 UniProtKB Helix 166 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MR3 +##sequence-region P14843 1 370 +P14843 UniProtKB Chain 1 370 . . . ID=PRO_0000140849;Note=Phospho-2-dehydro-3-deoxyheptonate aldolase%2C phenylalanine-inhibited +##sequence-region P32448 1 525 +P32448 UniProtKB Chain 1 525 . . . ID=PRO_0000064696;Note=Anti-silencing protein 2 +##sequence-region P53895 1 289 +P53895 UniProtKB Chain 1 289 . . . ID=PRO_0000203414;Note=Protein ASI2 +P53895 UniProtKB Topological domain 1 222 . . . Note=Nuclear;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53895 UniProtKB Transmembrane 223 243 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53895 UniProtKB Topological domain 244 247 . . . Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53895 UniProtKB Transmembrane 248 268 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53895 UniProtKB Topological domain 269 289 . . . Note=Nuclear;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04489 1 525 +Q04489 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04489 UniProtKB Chain 2 525 . . . ID=PRO_0000056940;Note=Asparagine synthetase domain-containing protein YML096W +Q04489 UniProtKB Domain 2 209 . . . Note=Glutamine amidotransferase type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609 +Q04489 UniProtKB Domain 210 523 . . . Note=Asparagine synthetase +Q04489 UniProtKB Active site 2 2 . . . Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P49089 1 572 +P49089 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49089 UniProtKB Chain 2 572 . . . ID=PRO_0000056917;Note=Asparagine synthetase [glutamine-hydrolyzing] 1 +P49089 UniProtKB Domain 2 186 . . . Note=Glutamine amidotransferase type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609 +P49089 UniProtKB Domain 194 546 . . . Note=Asparagine synthetase +P49089 UniProtKB Nucleotide binding 366 367 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49089 UniProtKB Region 49 53 . . . Note=Glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49089 UniProtKB Region 74 76 . . . Note=Glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49089 UniProtKB Active site 2 2 . . . Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49089 UniProtKB Binding site 97 97 . . . Note=Glutamine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49089 UniProtKB Binding site 233 233 . . . Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49089 UniProtKB Binding site 292 292 . . . Note=ATP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49089 UniProtKB Site 368 368 . . . Note=Important for beta-aspartyl-AMP intermediate formation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49089 UniProtKB Modified residue 265 265 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P49089 UniProtKB Modified residue 509 509 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P49090 1 572 +P49090 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49090 UniProtKB Chain 2 572 . . . ID=PRO_0000056918;Note=Asparagine synthetase [glutamine-hydrolyzing] 2 +P49090 UniProtKB Domain 2 186 . . . Note=Glutamine amidotransferase type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609 +P49090 UniProtKB Domain 194 545 . . . Note=Asparagine synthetase +P49090 UniProtKB Nucleotide binding 365 366 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49090 UniProtKB Region 49 53 . . . Note=Glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49090 UniProtKB Region 74 76 . . . Note=Glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49090 UniProtKB Active site 2 2 . . . Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49090 UniProtKB Binding site 97 97 . . . Note=Glutamine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49090 UniProtKB Binding site 233 233 . . . Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49090 UniProtKB Binding site 291 291 . . . Note=ATP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49090 UniProtKB Site 367 367 . . . Note=Important for beta-aspartyl-AMP intermediate formation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49090 UniProtKB Sequence conflict 560 560 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P43601 1 500 +P43601 UniProtKB Chain 1 500 . . . ID=PRO_0000050874;Note=Autophagy-related protein 18 +P43601 UniProtKB Repeat 243 283 . . . Note=WD 1 +P43601 UniProtKB Repeat 288 327 . . . Note=WD 2 +P43601 UniProtKB Region 284 287 . . . Note=Necessary for proper localization to vacuole membrane +P43601 UniProtKB Motif 284 288 . . . Note=FRRGT-motif;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:16876790;Dbxref=PMID:16876790 +P43601 UniProtKB Modified residue 354 354 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P43601 UniProtKB Mutagenesis 73 76 . . . Note=Slight reduction of PIP2 binding. RRLR->SSLS +P43601 UniProtKB Mutagenesis 264 264 . . . Note=Impairs membrane-association. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491 +P43601 UniProtKB Mutagenesis 268 268 . . . Note=Impairs membrane-association. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491 +P43601 UniProtKB Mutagenesis 271 271 . . . Note=Impairs membrane-association. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491 +P43601 UniProtKB Mutagenesis 285 286 . . . Note=Loss of recruitment to vacuole membrane. RR->GG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491 +P43601 UniProtKB Mutagenesis 285 286 . . . Note=40-fold decrease of affinity to PIP2. RR->TT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491 +P43601 UniProtKB Mutagenesis 285 285 . . . Note=Impairs membrane-association. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491 +P43601 UniProtKB Mutagenesis 286 286 . . . Note=Impairs membrane-association. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491 +P43601 UniProtKB Mutagenesis 311 311 . . . Note=Impairs membrane-association. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491 +P43601 UniProtKB Mutagenesis 313 313 . . . Note=Impairs membrane-association. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491 +P43601 UniProtKB Mutagenesis 315 315 . . . Note=Impairs membrane-association. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22753491;Dbxref=PMID:22753491 +##sequence-region Q02887 1 496 +Q02887 UniProtKB Chain 1 496 . . . ID=PRO_0000050882;Note=Autophagy-related protein 21 +Q02887 UniProtKB Repeat 294 334 . . . Note=WD 1 +Q02887 UniProtKB Repeat 346 385 . . . Note=WD 2 +Q02887 UniProtKB Repeat 448 488 . . . Note=WD 3 +Q02887 UniProtKB Motif 342 346 . . . Note=FRRGT-motif +Q02887 UniProtKB Compositional bias 77 80 . . . Note=Poly-Glu +Q02887 UniProtKB Modified residue 213 213 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02887 UniProtKB Modified residue 237 237 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q02887 UniProtKB Mutagenesis 343 344 . . . Note=Loss of aminopeptidase I precursor maturation and no more association with vacuole and punctate structures. RR->KK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15155809;Dbxref=PMID:15155809 +##sequence-region P25568 1 528 +P25568 UniProtKB Chain 1 528 . . . ID=PRO_0000207629;Note=Autophagy-related protein 22 +P25568 UniProtKB Topological domain 1 98 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Transmembrane 99 119 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Topological domain 120 130 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Transmembrane 131 151 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Topological domain 152 153 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Transmembrane 154 174 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Topological domain 175 210 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Transmembrane 211 231 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Topological domain 232 241 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Transmembrane 242 262 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Topological domain 263 318 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Transmembrane 319 339 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Topological domain 340 352 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Transmembrane 353 373 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Topological domain 374 388 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Transmembrane 389 409 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Topological domain 410 417 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Transmembrane 418 438 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Topological domain 439 485 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Transmembrane 486 506 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Topological domain 507 528 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25568 UniProtKB Modified residue 278 278 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q06485 1 197 +Q06485 UniProtKB Chain 1 197 . . . ID=PRO_0000247213;Note=Autophagy-related protein 33 +Q06485 UniProtKB Transmembrane 10 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06485 UniProtKB Transmembrane 52 72 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06485 UniProtKB Transmembrane 78 98 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06485 UniProtKB Transmembrane 172 192 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06485 UniProtKB Modified residue 127 127 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06485 UniProtKB Modified residue 129 129 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40344 1 310 +P40344 UniProtKB Chain 1 310 . . . ID=PRO_0000213586;Note=Autophagy-related protein 3 +P40344 UniProtKB Region 1 7 . . . Note=PE-binding +P40344 UniProtKB Region 83 163 . . . Note=Flexible region +P40344 UniProtKB Region 238 285 . . . Note=Handle region +P40344 UniProtKB Motif 270 273 . . . Note=ATG8 interaction motif (AIM) +P40344 UniProtKB Active site 234 234 . . . Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40344 UniProtKB Modified residue 19 19 . . . Note=N6-acetyllysine%3B by ESA1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22539722;Dbxref=PMID:22539722 +P40344 UniProtKB Modified residue 48 48 . . . Note=N6-acetyllysine%3B by ESA1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22539722;Dbxref=PMID:22539722 +P40344 UniProtKB Mutagenesis 213 213 . . . Note=Decreases ATG8-PE comjugation and autophagy. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23503366;Dbxref=PMID:23503366 +P40344 UniProtKB Mutagenesis 234 234 . . . Note=Loss of interaction with ATG8 and defect in autophagy and Cvt pathway. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11100732,ECO:0000269|PubMed:15277523;Dbxref=PMID:11100732,PMID:15277523 +P40344 UniProtKB Mutagenesis 234 234 . . . Note=Instead of the formation of an intermediate complex with a thiol ester bond between ATG3 (E2-like enzyme) and ATG8 (substrate)%2C a stable complex with an O-ester bond is formed. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11100732,ECO:0000269|PubMed:15277523;Dbxref=PMID:11100732,PMID:15277523 +P40344 UniProtKB Mutagenesis 270 270 . . . Note=Decreases interaction with ATG8. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20615880;Dbxref=PMID:20615880 +P40344 UniProtKB Mutagenesis 272 272 . . . Note=Decreases interaction with ATG8. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20615880;Dbxref=PMID:20615880 +P40344 UniProtKB Mutagenesis 273 273 . . . Note=Decreases interaction with ATG8. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20615880;Dbxref=PMID:20615880 +P40344 UniProtKB Helix 22 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT +P40344 UniProtKB Helix 30 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT +P40344 UniProtKB Beta strand 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GSL +P40344 UniProtKB Helix 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GSL +P40344 UniProtKB Beta strand 69 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT +P40344 UniProtKB Turn 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT +P40344 UniProtKB Helix 135 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7G +P40344 UniProtKB Beta strand 167 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT +P40344 UniProtKB Turn 177 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT +P40344 UniProtKB Beta strand 181 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT +P40344 UniProtKB Helix 198 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT +P40344 UniProtKB Turn 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT +P40344 UniProtKB Helix 210 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT +P40344 UniProtKB Beta strand 214 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT +P40344 UniProtKB Beta strand 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT +P40344 UniProtKB Beta strand 227 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT +P40344 UniProtKB Beta strand 235 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT +P40344 UniProtKB Helix 239 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT +P40344 UniProtKB Helix 283 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT +P40344 UniProtKB Helix 286 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DYT +##sequence-region P32907 1 282 +P32907 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P32907 UniProtKB Chain 2 282 . . . ID=PRO_0000135701;Note=Ammonia transport outward protein 2 +P32907 UniProtKB Topological domain 2 86 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32907 UniProtKB Transmembrane 87 107 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32907 UniProtKB Topological domain 108 119 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32907 UniProtKB Transmembrane 120 140 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32907 UniProtKB Topological domain 141 150 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32907 UniProtKB Transmembrane 151 171 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32907 UniProtKB Topological domain 172 184 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32907 UniProtKB Transmembrane 185 205 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32907 UniProtKB Topological domain 206 207 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32907 UniProtKB Transmembrane 208 228 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32907 UniProtKB Topological domain 229 238 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32907 UniProtKB Transmembrane 239 259 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32907 UniProtKB Topological domain 260 282 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32907 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P32907 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P32907 UniProtKB Modified residue 7 7 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P32907 UniProtKB Modified residue 21 21 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P32907 UniProtKB Modified residue 22 22 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P32907 UniProtKB Modified residue 28 28 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P32907 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +##sequence-region Q12349 1 124 +Q12349 UniProtKB Transit peptide 1 32 . . . Note=Mitochondrion +Q12349 UniProtKB Chain 33 124 . . . ID=PRO_0000002525;Note=ATP synthase subunit H%2C mitochondrial +##sequence-region P32454 1 952 +P32454 UniProtKB Transit peptide 1 52 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32454 UniProtKB Chain 53 952 . . . ID=PRO_0000095104;Note=Aminopeptidase 2%2C mitochondrial +P32454 UniProtKB Region 360 364 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32454 UniProtKB Active site 397 397 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P32454 UniProtKB Metal binding 396 396 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P32454 UniProtKB Metal binding 400 400 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P32454 UniProtKB Metal binding 419 419 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P32454 UniProtKB Binding site 228 228 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32454 UniProtKB Site 482 482 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32454 UniProtKB Glycosylation 381 381 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32454 UniProtKB Glycosylation 713 713 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32454 UniProtKB Sequence conflict 73 73 . . . Note=R->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32454 UniProtKB Sequence conflict 92 93 . . . Note=LL->FI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32454 UniProtKB Sequence conflict 255 255 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32454 UniProtKB Sequence conflict 533 533 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P05085 1 880 +P05085 UniProtKB Chain 1 880 . . . ID=PRO_0000114937;Note=Arginine metabolism regulation protein II +P05085 UniProtKB DNA binding 21 48 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P05085 UniProtKB Sequence conflict 4 4 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05085 UniProtKB Sequence conflict 129 129 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05085 UniProtKB Sequence conflict 283 283 . . . Note=F->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05085 UniProtKB Sequence conflict 345 345 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05085 UniProtKB Sequence conflict 366 366 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05085 UniProtKB Sequence conflict 549 549 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05085 UniProtKB Sequence conflict 597 597 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05085 UniProtKB Sequence conflict 665 665 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05085 UniProtKB Sequence conflict 869 869 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32381 1 391 +P32381 UniProtKB Chain 1 391 . . . ID=PRO_0000089077;Note=Actin-related protein 2 +P32381 UniProtKB Nucleotide binding 159 161 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32381 UniProtKB Nucleotide binding 213 217 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32381 UniProtKB Nucleotide binding 304 309 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32381 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P47117 1 449 +P47117 UniProtKB Chain 1 449 . . . ID=PRO_0000089090;Note=Actin-related protein 3 +##sequence-region Q12509 1 438 +Q12509 UniProtKB Chain 1 438 . . . ID=PRO_0000089121;Note=Actin-like protein ARP6 +##sequence-region P33204 1 171 +P33204 UniProtKB Chain 1 171 . . . ID=PRO_0000124053;Note=Actin-related protein 2/3 complex subunit 4 +##sequence-region P53244 1 586 +P53244 UniProtKB Chain 1 586 . . . ID=PRO_0000202804;Note=Arrestin-related trafficking adapter 5 +P53244 UniProtKB Compositional bias 199 204 . . . Note=Poly-Ser +P53244 UniProtKB Cross-link 364 364 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P53983 1 676 +P53983 UniProtKB Chain 1 676 . . . ID=PRO_0000203467;Note=Protein ASI3 +P53983 UniProtKB Topological domain 1 78 . . . Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53983 UniProtKB Transmembrane 79 99 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53983 UniProtKB Topological domain 100 126 . . . Note=Nuclear;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53983 UniProtKB Transmembrane 127 147 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53983 UniProtKB Topological domain 148 156 . . . Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53983 UniProtKB Transmembrane 157 177 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53983 UniProtKB Topological domain 178 181 . . . Note=Nuclear;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53983 UniProtKB Transmembrane 182 202 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53983 UniProtKB Topological domain 203 277 . . . Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53983 UniProtKB Transmembrane 278 298 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53983 UniProtKB Topological domain 299 676 . . . Note=Nuclear;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53983 UniProtKB Zinc finger 624 664 . . . Note=RING-type%3B atypical +P53983 UniProtKB Glycosylation 24 24 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53983 UniProtKB Glycosylation 34 34 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53983 UniProtKB Glycosylation 46 46 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53983 UniProtKB Glycosylation 66 66 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53983 UniProtKB Sequence conflict 1 15 . . . Note=MSTNILQHVKQLLHN->MLSNCSIT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53983 UniProtKB Sequence conflict 1 15 . . . Note=MSTNILQHVKQLLHN->MLSNCSIT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CZ17 1 362 +P0CZ17 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3042786;Dbxref=PMID:3042786 +P0CZ17 UniProtKB Chain 26 362 . . . ID=PRO_0000002362;Note=L-asparaginase 2-1 +P0CZ17 UniProtKB Domain 33 359 . . . Note=Asparaginase/glutaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01068 +P0CZ17 UniProtKB Region 122 123 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CZ17 UniProtKB Active site 43 43 . . . Note=O-isoaspartyl threonine intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10099,ECO:0000255|PROSITE-ProRule:PRU10100 +P0CZ17 UniProtKB Binding site 89 89 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CZ17 UniProtKB Glycosylation 29 29 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CZ17 UniProtKB Glycosylation 93 93 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CZ17 UniProtKB Glycosylation 239 239 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CZ17 UniProtKB Natural variant 26 55 . . . Note=Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3042786;Dbxref=PMID:3042786 +P0CZ17 UniProtKB Sequence conflict 31 31 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38929 1 1173 +P38929 UniProtKB Chain 1 1173 . . . ID=PRO_0000046232;Note=Calcium-transporting ATPase 2 +P38929 UniProtKB Topological domain 1 114 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Transmembrane 115 139 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Topological domain 140 152 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Transmembrane 153 173 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Topological domain 174 349 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Transmembrane 350 368 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Topological domain 369 388 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Transmembrane 389 409 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Topological domain 410 899 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Transmembrane 900 922 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Topological domain 923 929 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Transmembrane 930 950 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Topological domain 951 976 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Transmembrane 977 998 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Topological domain 999 1010 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Transmembrane 1011 1029 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Topological domain 1030 1065 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Transmembrane 1066 1086 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Topological domain 1087 1099 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Transmembrane 1100 1120 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Topological domain 1121 1173 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38929 UniProtKB Active site 445 445 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P39524 1 1355 +P39524 UniProtKB Chain 1 1355 . . . ID=PRO_0000046233;Note=Probable phospholipid-transporting ATPase DRS2 +P39524 UniProtKB Topological domain 1 221 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Transmembrane 222 242 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Topological domain 243 246 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Transmembrane 247 267 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Topological domain 268 449 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Transmembrane 450 470 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Topological domain 471 490 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Transmembrane 491 511 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Topological domain 512 1012 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Transmembrane 1013 1033 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Topological domain 1034 1043 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Transmembrane 1044 1064 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Topological domain 1065 1094 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Transmembrane 1095 1115 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Topological domain 1116 1131 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Transmembrane 1132 1152 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Topological domain 1153 1161 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Transmembrane 1162 1182 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Topological domain 1183 1202 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Transmembrane 1203 1223 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Topological domain 1224 1355 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39524 UniProtKB Active site 560 560 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39524 UniProtKB Modified residue 102 102 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P39524 UniProtKB Sequence conflict 45 46 . . . Note=AN->GY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39524 UniProtKB Sequence conflict 45 46 . . . Note=AN->GY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39524 UniProtKB Sequence conflict 450 450 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39524 UniProtKB Sequence conflict 450 450 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39524 UniProtKB Sequence conflict 674 674 . . . Note=P->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39524 UniProtKB Sequence conflict 674 674 . . . Note=P->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39524 UniProtKB Sequence conflict 891 892 . . . Note=NT->KS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39524 UniProtKB Sequence conflict 891 892 . . . Note=NT->KS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39524 UniProtKB Sequence conflict 953 954 . . . Note=GD->AS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39524 UniProtKB Sequence conflict 953 954 . . . Note=GD->AS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39524 UniProtKB Sequence conflict 987 987 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39524 UniProtKB Sequence conflict 987 987 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39986 1 1215 +P39986 UniProtKB Chain 1 1215 . . . ID=PRO_0000046349;Note=Manganese-transporting ATPase 1 +P39986 UniProtKB Topological domain 1 21 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Transmembrane 22 43 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Topological domain 44 49 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Transmembrane 50 72 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Topological domain 73 191 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Transmembrane 192 214 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Topological domain 215 217 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Transmembrane 218 236 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Topological domain 237 399 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Transmembrane 400 419 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Topological domain 420 432 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Transmembrane 433 454 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Topological domain 455 993 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Transmembrane 994 1013 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Topological domain 1014 1020 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Transmembrane 1021 1037 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Topological domain 1038 1055 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Transmembrane 1056 1079 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Topological domain 1080 1099 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Transmembrane 1100 1122 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Topological domain 1123 1133 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Transmembrane 1134 1153 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Topological domain 1154 1170 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Transmembrane 1171 1193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Topological domain 1194 1215 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39986 UniProtKB Active site 487 487 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39986 UniProtKB Metal binding 816 816 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39986 UniProtKB Metal binding 820 820 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39986 UniProtKB Modified residue 324 324 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39986 UniProtKB Modified residue 936 936 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39986 UniProtKB Mutagenesis 487 487 . . . Note=Loss of ATPase activity and transport function. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24392018;Dbxref=PMID:24392018 +##sequence-region Q01217 1 863 +Q01217 UniProtKB Transit peptide 1 65 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01217 UniProtKB Chain 66 532 . . . ID=PRO_0000002073;Note=Acetylglutamate kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01217 UniProtKB Chain 533 863 . . . ID=PRO_0000002074;Note=N-acetyl-gamma-glutamyl-phosphate reductase;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01217 UniProtKB Domain 353 505 . . . Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532 +Q01217 UniProtKB Active site 675 675 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10010 +Q01217 UniProtKB Modified residue 359 359 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q01217 UniProtKB Helix 68 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Helix 81 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Beta strand 100 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Helix 106 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Helix 113 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Beta strand 130 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Helix 137 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Helix 162 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Beta strand 190 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Beta strand 195 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Helix 205 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Beta strand 209 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Helix 220 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Beta strand 231 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Beta strand 237 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZG +Q01217 UniProtKB Beta strand 244 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Helix 250 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Beta strand 264 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Beta strand 271 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZF +Q01217 UniProtKB Turn 278 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Beta strand 286 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Helix 289 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Beta strand 300 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZG +Q01217 UniProtKB Helix 304 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Beta strand 326 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Helix 331 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Helix 334 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Beta strand 340 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7 +Q01217 UniProtKB Beta strand 345 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZZH +Q01217 UniProtKB Beta strand 355 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7 +Q01217 UniProtKB Helix 360 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7 +Q01217 UniProtKB Helix 366 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7 +Q01217 UniProtKB Turn 377 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7 +Q01217 UniProtKB Beta strand 380 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7 +Q01217 UniProtKB Helix 386 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7 +Q01217 UniProtKB Beta strand 398 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7 +Q01217 UniProtKB Beta strand 407 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7 +Q01217 UniProtKB Beta strand 415 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7 +Q01217 UniProtKB Beta strand 420 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7 +Q01217 UniProtKB Helix 428 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7 +Q01217 UniProtKB Helix 435 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7 +Q01217 UniProtKB Beta strand 448 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7 +Q01217 UniProtKB Helix 461 467 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7 +Q01217 UniProtKB Beta strand 469 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7 +Q01217 UniProtKB Beta strand 477 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7 +Q01217 UniProtKB Helix 487 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AB7 +##sequence-region Q02804 1 198 +Q02804 UniProtKB Chain 1 198 . . . ID=PRO_0000207422;Note=ADP-ribosylation factor-like protein 3 +Q02804 UniProtKB Nucleotide binding 24 31 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02804 UniProtKB Nucleotide binding 74 78 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02804 UniProtKB Nucleotide binding 133 136 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02804 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15077113,ECO:0000269|PubMed:15077114;Dbxref=PMID:15077113,PMID:15077114 +Q02804 UniProtKB Cross-link 50 50 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P28777 1 376 +P28777 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P28777 UniProtKB Chain 2 376 . . . ID=PRO_0000140704;Note=Chorismate synthase +P28777 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P28777 UniProtKB Beta strand 6 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Beta strand 18 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Beta strand 30 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R52 +P28777 UniProtKB Helix 36 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Helix 40 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Beta strand 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R52 +P28777 UniProtKB Beta strand 67 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Beta strand 79 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Helix 130 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Beta strand 150 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Helix 170 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Helix 181 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Helix 195 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Beta strand 217 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Turn 233 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Helix 238 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Beta strand 254 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R52 +P28777 UniProtKB Turn 258 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Helix 262 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Helix 268 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Beta strand 293 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Beta strand 304 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Helix 342 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +P28777 UniProtKB Helix 347 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R53 +##sequence-region P18634 1 518 +P18634 UniProtKB Chain 1 518 . . . ID=PRO_0000203235;Note=Arrestin-related trafficking adapter 10 +P18634 UniProtKB Cross-link 118 118 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P50275 1 885 +P50275 UniProtKB Chain 1 885 . . . ID=PRO_0000064694;Note=Anaphase spindle elongation protein +P50275 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P0CX77 1 362 +P0CX77 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3042786;Dbxref=PMID:3042786 +P0CX77 UniProtKB Chain 26 362 . . . ID=PRO_0000410441;Note=L-asparaginase 2-2 +P0CX77 UniProtKB Domain 33 359 . . . Note=Asparaginase/glutaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01068 +P0CX77 UniProtKB Region 122 123 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX77 UniProtKB Active site 43 43 . . . Note=O-isoaspartyl threonine intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10099,ECO:0000255|PROSITE-ProRule:PRU10100 +P0CX77 UniProtKB Binding site 89 89 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX77 UniProtKB Glycosylation 29 29 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX77 UniProtKB Glycosylation 93 93 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX77 UniProtKB Glycosylation 239 239 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX77 UniProtKB Natural variant 26 55 . . . Note=Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3042786;Dbxref=PMID:3042786 +P0CX77 UniProtKB Sequence conflict 243 243 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CX78 1 362 +P0CX78 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3042786;Dbxref=PMID:3042786 +P0CX78 UniProtKB Chain 26 362 . . . ID=PRO_0000410442;Note=L-asparaginase 2-3 +P0CX78 UniProtKB Domain 33 359 . . . Note=Asparaginase/glutaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01068 +P0CX78 UniProtKB Region 122 123 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX78 UniProtKB Active site 43 43 . . . Note=O-isoaspartyl threonine intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10099,ECO:0000255|PROSITE-ProRule:PRU10100 +P0CX78 UniProtKB Binding site 89 89 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX78 UniProtKB Glycosylation 29 29 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX78 UniProtKB Glycosylation 93 93 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX78 UniProtKB Glycosylation 239 239 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX78 UniProtKB Natural variant 26 55 . . . Note=Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3042786;Dbxref=PMID:3042786 +##sequence-region P40416 1 690 +P40416 UniProtKB Transit peptide 1 26 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40416 UniProtKB Chain 27 690 . . . ID=PRO_0000000258;Note=Iron-sulfur clusters transporter ATM1%2C mitochondrial +P40416 UniProtKB Topological domain 27 110 . . . Note=Mitochondrial matrix +P40416 UniProtKB Transmembrane 111 132 . . . Note=Helical +P40416 UniProtKB Topological domain 133 155 . . . Note=Mitochondrial intermembrane +P40416 UniProtKB Transmembrane 156 179 . . . Note=Helical +P40416 UniProtKB Topological domain 180 228 . . . Note=Mitochondrial matrix +P40416 UniProtKB Transmembrane 229 252 . . . Note=Helical +P40416 UniProtKB Topological domain 253 253 . . . Note=Mitochondrial intermembrane +P40416 UniProtKB Transmembrane 254 274 . . . Note=Helical +P40416 UniProtKB Topological domain 275 340 . . . Note=Mitochondrial matrix +P40416 UniProtKB Transmembrane 341 359 . . . Note=Helical +P40416 UniProtKB Topological domain 360 374 . . . Note=Mitochondrial intermembrane +P40416 UniProtKB Transmembrane 375 396 . . . Note=Helical +P40416 UniProtKB Topological domain 397 690 . . . Note=Mitochondrial matrix +P40416 UniProtKB Domain 111 401 . . . Note=ABC transmembrane type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P40416 UniProtKB Domain 436 672 . . . Note=ABC transporter;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P40416 UniProtKB Nucleotide binding 469 480 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P40416 UniProtKB Region 280 284 . . . Note=Glutathione binding +P40416 UniProtKB Region 343 346 . . . Note=Glutathione binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40416 UniProtKB Binding site 393 393 . . . Note=Glutathione%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40416 UniProtKB Binding site 445 445 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40416 UniProtKB Mutagenesis 475 475 . . . Note=Loss of function%3B significant decrease in ATP-binding%3B no homodimerization. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15225610;Dbxref=PMID:15225610 +P40416 UniProtKB Mutagenesis 598 598 . . . Note=Loss of function%3B slight decrease in ATP-binding. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15225610;Dbxref=PMID:15225610 +P40416 UniProtKB Mutagenesis 666 690 . . . Note=Impairs protein stability. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24604199;Dbxref=PMID:24604199 +P40416 UniProtKB Sequence conflict 23 23 . . . Note=I->IRNHS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40416 UniProtKB Beta strand 103 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYH +P40416 UniProtKB Helix 106 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 110 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 128 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 152 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 203 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 212 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Turn 216 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 229 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 236 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 256 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 305 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 315 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Beta strand 367 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYH +P40416 UniProtKB Helix 373 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 383 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 387 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Turn 390 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 397 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Turn 412 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Beta strand 430 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Beta strand 436 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Beta strand 451 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Beta strand 464 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 475 477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 478 482 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Beta strand 489 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 500 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 505 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Beta strand 512 515 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Beta strand 523 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 526 530 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 531 533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 539 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 552 557 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 561 563 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Beta strand 565 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 575 589 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Beta strand 592 598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 605 618 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Beta strand 620 623 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Beta strand 625 631 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 633 636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Beta strand 640 646 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Beta strand 649 654 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 656 661 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +P40416 UniProtKB Helix 666 690 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MYC +##sequence-region P81450 1 59 +P81450 UniProtKB Chain 1 59 . . . ID=PRO_0000071697;Note=ATP synthase subunit J%2C mitochondrial +P81450 UniProtKB Transmembrane 9 25 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06321 1 1198 +Q06321 UniProtKB Chain 1 1198 . . . ID=PRO_0000215616;Note=Sterol 3-beta-glucosyltransferase +Q06321 UniProtKB Domain 187 236 . . . Note=GRAM 1 +Q06321 UniProtKB Domain 238 336 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +Q06321 UniProtKB Domain 570 636 . . . Note=GRAM 2 +Q06321 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06321 UniProtKB Modified residue 693 693 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06321 UniProtKB Beta strand 741 745 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 750 765 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Beta strand 769 774 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 776 778 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 779 784 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Beta strand 788 791 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 797 805 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 810 839 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Beta strand 842 846 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 848 850 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 853 860 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Beta strand 864 870 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Beta strand 876 878 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 891 919 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 928 931 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 933 935 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Beta strand 938 940 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Turn 944 946 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Beta strand 957 959 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 975 986 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Beta strand 990 995 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Beta strand 998 1000 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 1004 1017 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Beta strand 1020 1025 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Beta strand 1028 1031 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Beta strand 1048 1050 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 1056 1059 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 1060 1062 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Beta strand 1063 1068 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 1072 1080 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Beta strand 1085 1087 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 1093 1103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Beta strand 1106 1109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 1115 1127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 1129 1144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +Q06321 UniProtKB Helix 1147 1169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GL5 +##sequence-region Q12142 1 997 +Q12142 UniProtKB Chain 1 997 . . . ID=PRO_0000119839;Note=Autophagy-related protein 9 +Q12142 UniProtKB Topological domain 1 318 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q12142 UniProtKB Transmembrane 319 339 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12142 UniProtKB Topological domain 340 376 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q12142 UniProtKB Transmembrane 377 397 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12142 UniProtKB Topological domain 398 538 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q12142 UniProtKB Transmembrane 539 559 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12142 UniProtKB Topological domain 560 620 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q12142 UniProtKB Transmembrane 621 641 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12142 UniProtKB Topological domain 642 656 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q12142 UniProtKB Transmembrane 657 677 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12142 UniProtKB Topological domain 678 723 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q12142 UniProtKB Transmembrane 724 744 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12142 UniProtKB Topological domain 745 997 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q12142 UniProtKB Compositional bias 907 978 . . . Note=Asn-rich +Q12142 UniProtKB Modified residue 143 143 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12142 UniProtKB Modified residue 144 144 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12142 UniProtKB Modified residue 787 787 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12142 UniProtKB Mutagenesis 192 192 . . . Note=Aboloshes interaction with ATG11 and disrupts Cvt%2C but not bulk autophagy. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17178909;Dbxref=PMID:17178909 +##sequence-region P38110 1 2787 +P38110 UniProtKB Chain 1 2787 . . . ID=PRO_0000088839;Note=Serine/threonine-protein kinase TEL1 +P38110 UniProtKB Domain 1734 2326 . . . Note=FAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534 +P38110 UniProtKB Domain 2461 2787 . . . Note=PI3K/PI4K;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00269 +P38110 UniProtKB Domain 2755 2787 . . . Note=FATC;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534,ECO:0000255|PROSITE-ProRule:PRU00535 +P38110 UniProtKB Mutagenesis 1319 1319 . . . Note=In TEL1-11%3B short telomere phenotype and impairs DNA-damage checkpoint function at 37 degrees Celsius. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16228207;Dbxref=PMID:16228207 +P38110 UniProtKB Mutagenesis 2611 2612 . . . Note=Short telomere phenotype in vivo and impairs kinase activity in vitro%3B when associated with K-2616 and E-2631. GD->DA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11095737,ECO:0000269|PubMed:7671310;Dbxref=PMID:11095737,PMID:7671310 +P38110 UniProtKB Mutagenesis 2616 2616 . . . Note=Short telomere phenotype in vivo and impairs kinase activity in vitro%3B when associated with D-2611-2612-A and E-2631. N->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11095737,ECO:0000269|PubMed:7671310;Dbxref=PMID:11095737,PMID:7671310 +P38110 UniProtKB Mutagenesis 2631 2631 . . . Note=Short telomere phenotype in vivo and impairs kinase activity in vitro%3B when associated with D-2611-2612-A and K-2616. D->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11095737,ECO:0000269|PubMed:7671310;Dbxref=PMID:11095737,PMID:7671310 +P38110 UniProtKB Sequence conflict 64 64 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38110 UniProtKB Sequence conflict 164 164 . . . Note=C->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38110 UniProtKB Sequence conflict 1190 1190 . . . Note=F->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38110 UniProtKB Sequence conflict 1412 1412 . . . Note=C->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38110 UniProtKB Sequence conflict 1412 1412 . . . Note=C->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P13587 1 1091 +P13587 UniProtKB Chain 1 1091 . . . ID=PRO_0000046242;Note=Sodium transport ATPase 1 +P13587 UniProtKB Topological domain 1 63 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Transmembrane 64 84 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Topological domain 85 90 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Transmembrane 91 111 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Topological domain 112 282 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Transmembrane 283 303 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Topological domain 304 312 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Transmembrane 313 333 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Topological domain 334 815 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Transmembrane 816 836 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Topological domain 837 848 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Transmembrane 849 869 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Topological domain 870 885 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Transmembrane 886 906 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Topological domain 907 943 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Transmembrane 944 964 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Topological domain 965 991 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Transmembrane 992 1012 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Topological domain 1013 1021 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Transmembrane 1022 1042 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Topological domain 1043 1091 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13587 UniProtKB Active site 369 369 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q12359 1 275 +Q12359 UniProtKB Chain 1 275 . . . ID=PRO_0000135707;Note=Ammonia transport outward protein 3 +Q12359 UniProtKB Topological domain 1 84 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12359 UniProtKB Transmembrane 85 105 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12359 UniProtKB Topological domain 106 120 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12359 UniProtKB Transmembrane 121 141 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12359 UniProtKB Topological domain 142 181 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12359 UniProtKB Transmembrane 182 202 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12359 UniProtKB Topological domain 203 207 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12359 UniProtKB Transmembrane 208 228 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12359 UniProtKB Topological domain 229 236 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12359 UniProtKB Transmembrane 237 257 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12359 UniProtKB Topological domain 258 275 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12359 UniProtKB Modified residue 4 4 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +##sequence-region P18496 1 279 +P18496 UniProtKB Chain 1 279 . . . ID=PRO_0000071727;Note=Mitochondrial ATPase complex subunit ATP10 +P18496 UniProtKB Sequence conflict 224 224 . . . Note=C->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P81451 1 68 +P81451 UniProtKB Chain 1 68 . . . ID=PRO_0000071699;Note=ATP synthase subunit K%2C mitochondrial +P81451 UniProtKB Transmembrane 15 31 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P61829 1 76 +P61829 UniProtKB Chain 1 76 . . . ID=PRO_0000112240;Note=ATP synthase subunit 9%2C mitochondrial +P61829 UniProtKB Transmembrane 14 34 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P61829 UniProtKB Transmembrane 52 72 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P61829 UniProtKB Site 59 59 . . . Note=Reversibly protonated during proton transport;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P61829 UniProtKB Modified residue 1 1 . . . Note=N-formylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2894987;Dbxref=PMID:2894987 +P61829 UniProtKB Natural variant 46 46 . . . Note=In strain: DS400/A3 and KL14-4A. T->L +P61829 UniProtKB Natural variant 53 53 . . . Note=In strain: DS400/A3%2C DS401 and oligomycin-resistant mutant. L->F +P61829 UniProtKB Natural variant 57 57 . . . Note=In oligomycin-resistant mutant and cross-resistance to venturicidin. L->V +P61829 UniProtKB Natural variant 65 65 . . . Note=In oligomycin-resistant mutant. C->S +P61829 UniProtKB Helix 2 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F4S +P61829 UniProtKB Helix 15 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F4S +P61829 UniProtKB Helix 19 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F4S +P61829 UniProtKB Helix 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F4S +P61829 UniProtKB Helix 44 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F4S +##sequence-region P22035 1 811 +P22035 UniProtKB Chain 1 811 . . . ID=PRO_0000197085;Note=Myb-like DNA-binding protein BAS1 +P22035 UniProtKB Domain 34 110 . . . Note=Myb-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00133 +P22035 UniProtKB Domain 111 165 . . . Note=HTH myb-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +P22035 UniProtKB Domain 166 218 . . . Note=HTH myb-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +P22035 UniProtKB DNA binding 138 161 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +P22035 UniProtKB DNA binding 191 214 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +##sequence-region Q05029 1 724 +Q05029 UniProtKB Chain 1 724 . . . ID=PRO_0000203335;Note=Protein BCH1 +Q05029 UniProtKB Region 711 724 . . . Note=CHS5-binding +Q05029 UniProtKB Helix 18 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Beta strand 37 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Beta strand 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q66 +Q05029 UniProtKB Helix 102 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Beta strand 123 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q66 +Q05029 UniProtKB Beta strand 131 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Beta strand 136 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Turn 142 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Beta strand 146 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Beta strand 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Beta strand 159 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 190 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Turn 207 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Beta strand 223 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q66 +Q05029 UniProtKB Helix 228 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Beta strand 233 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 237 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 245 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 252 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Beta strand 266 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 270 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 285 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 300 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 303 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 316 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 341 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 366 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 384 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 400 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 463 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Turn 469 472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 475 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 493 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 539 564 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 575 588 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 592 601 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 608 630 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 638 665 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 672 684 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 687 697 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 700 709 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q05029 UniProtKB Helix 711 716 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +##sequence-region P35817 1 686 +P35817 UniProtKB Chain 1 686 . . . ID=PRO_0000211176;Note=Bromodomain-containing factor 1 +P35817 UniProtKB Domain 165 237 . . . Note=Bromo 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 +P35817 UniProtKB Domain 332 404 . . . Note=Bromo 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 +P35817 UniProtKB Domain 518 598 . . . Note=NET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00857 +P35817 UniProtKB Coiled coil 460 499 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35817 UniProtKB Modified residue 270 270 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P35817 UniProtKB Modified residue 429 429 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P35817 UniProtKB Modified residue 615 615 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P35817 UniProtKB Modified residue 659 659 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P35817 UniProtKB Mutagenesis 187 187 . . . Note=Impairs interaction with histones H3 and H4%3B when associated with F-354. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12620225;Dbxref=PMID:12620225 +P35817 UniProtKB Mutagenesis 354 354 . . . Note=Impairs interaction with histones H3 and H4%3B when associated with F-187. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12620225;Dbxref=PMID:12620225 +P35817 UniProtKB Sequence conflict 8 8 . . . Note=Q->LC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35817 UniProtKB Sequence conflict 93 94 . . . Note=GA->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35817 UniProtKB Sequence conflict 94 94 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35817 UniProtKB Sequence conflict 282 282 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35817 UniProtKB Sequence conflict 385 385 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35817 UniProtKB Sequence conflict 493 493 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39714 1 382 +P39714 UniProtKB Chain 1 382 . . . ID=PRO_0000160788;Note=(R%2CR)-butanediol dehydrogenase +P39714 UniProtKB Metal binding 39 39 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39714 UniProtKB Metal binding 73 73 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39714 UniProtKB Metal binding 103 103 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39714 UniProtKB Metal binding 120 120 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39714 UniProtKB Metal binding 123 123 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39714 UniProtKB Metal binding 131 131 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39714 UniProtKB Metal binding 173 173 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39714 UniProtKB Modified residue 63 63 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39714 UniProtKB Sequence conflict 322 322 . . . Note=D->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P50273 1 684 +P50273 UniProtKB Transit peptide 1 56 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50273 UniProtKB Chain 57 684 . . . ID=PRO_0000072452;Note=Mitochondrial translation factor ATP22 +##sequence-region P07251 1 545 +P07251 UniProtKB Transit peptide 1 35 . . . Note=Mitochondrion +P07251 UniProtKB Chain 36 545 . . . ID=PRO_0000002433;Note=ATP synthase subunit alpha%2C mitochondrial +P07251 UniProtKB Nucleotide binding 206 213 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07251 UniProtKB Site 407 407 . . . Note=Required for activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07251 UniProtKB Modified residue 57 57 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P07251 UniProtKB Modified residue 178 178 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P07251 UniProtKB Mutagenesis 291 291 . . . Note=In ATP1-2%3B growth-defect. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10744740;Dbxref=PMID:10744740 +P07251 UniProtKB Mutagenesis 383 383 . . . Note=In ATP1-1%3B growth-defect. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10744740;Dbxref=PMID:10744740 +P07251 UniProtKB Sequence conflict 311 313 . . . Note=QAV->ASL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07251 UniProtKB Sequence conflict 321 321 . . . Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07251 UniProtKB Sequence conflict 340 340 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07251 UniProtKB Sequence conflict 340 340 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07251 UniProtKB Sequence conflict 385 385 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07251 UniProtKB Sequence conflict 459 459 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07251 UniProtKB Sequence conflict 479 483 . . . Note=VPLIY->SMII;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07251 UniProtKB Sequence conflict 490 493 . . . Note=LDGI->SGWY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07251 UniProtKB Turn 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 65 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 75 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 88 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 97 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 108 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 124 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 144 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 161 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 173 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEE +P07251 UniProtKB Beta strand 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEE +P07251 UniProtKB Helix 188 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 203 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 208 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPD +P07251 UniProtKB Helix 212 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 224 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 228 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Turn 232 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 237 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 247 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Turn 259 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 263 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 266 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 277 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 300 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 308 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 328 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 335 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 347 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Turn 351 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 357 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 367 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 374 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 383 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 391 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Turn 404 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Beta strand 408 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 412 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 418 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 438 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 449 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 475 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Turn 488 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 495 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 498 512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 514 523 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P07251 UniProtKB Helix 528 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +##sequence-region P09457 1 212 +P09457 UniProtKB Transit peptide 1 17 . . . Note=Mitochondrion +P09457 UniProtKB Chain 18 212 . . . ID=PRO_0000002656;Note=ATP synthase subunit 5%2C mitochondrial +##sequence-region P13090 1 542 +P13090 UniProtKB Chain 1 542 . . . ID=PRO_0000173367;Note=Aminotriazole resistance protein +P13090 UniProtKB Topological domain 1 108 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Transmembrane 109 129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Topological domain 130 136 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Transmembrane 137 157 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Topological domain 158 172 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Topological domain 194 198 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Transmembrane 199 219 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Topological domain 220 231 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Transmembrane 232 252 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Topological domain 253 262 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Transmembrane 263 283 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Topological domain 284 295 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Transmembrane 296 316 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Topological domain 317 333 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Transmembrane 334 354 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Topological domain 355 371 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Transmembrane 372 392 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Topological domain 393 399 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Transmembrane 400 420 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Topological domain 421 429 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Transmembrane 430 450 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Topological domain 451 505 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Transmembrane 506 526 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Topological domain 527 542 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Glycosylation 394 394 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Glycosylation 471 471 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13090 UniProtKB Sequence conflict 531 542 . . . Note=ARAAAEYDCTVA->QELLQNTIALWLSGKRY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12067 1 313 +Q12067 UniProtKB Chain 1 313 . . . ID=PRO_0000064758;Note=Metal homeostasis factor ATX2 +Q12067 UniProtKB Topological domain 1 2 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12067 UniProtKB Transmembrane 3 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12067 UniProtKB Topological domain 24 67 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12067 UniProtKB Transmembrane 68 88 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12067 UniProtKB Topological domain 89 103 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12067 UniProtKB Transmembrane 104 124 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12067 UniProtKB Topological domain 125 154 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12067 UniProtKB Transmembrane 155 175 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12067 UniProtKB Topological domain 176 183 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12067 UniProtKB Transmembrane 184 204 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12067 UniProtKB Topological domain 205 217 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12067 UniProtKB Transmembrane 218 238 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12067 UniProtKB Topological domain 239 251 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12067 UniProtKB Transmembrane 252 272 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12067 UniProtKB Topological domain 273 285 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12067 UniProtKB Transmembrane 286 306 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12067 UniProtKB Topological domain 307 313 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12128 1 409 +Q12128 UniProtKB Chain 1 409 . . . ID=PRO_0000064810;Note=Rho-GTPase-activating protein BAG7 +Q12128 UniProtKB Domain 76 235 . . . Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172 +Q12128 UniProtKB Compositional bias 319 326 . . . Note=Poly-His +##sequence-region Q01389 1 1478 +Q01389 UniProtKB Chain 1 1478 . . . ID=PRO_0000085662;Note=Serine/threonine-protein kinase BCK1/SLK1/SSP31 +Q01389 UniProtKB Domain 1175 1440 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q01389 UniProtKB Nucleotide binding 1181 1189 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q01389 UniProtKB Active site 1303 1303 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q01389 UniProtKB Binding site 1204 1204 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q01389 UniProtKB Modified residue 407 407 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q01389 UniProtKB Modified residue 411 411 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q01389 UniProtKB Modified residue 491 491 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q01389 UniProtKB Modified residue 747 747 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q01389 UniProtKB Modified residue 816 816 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q01389 UniProtKB Modified residue 1058 1058 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q01389 UniProtKB Modified residue 1061 1061 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q01389 UniProtKB Modified residue 1134 1134 . . . Note=Phosphoserine%3B by PKC;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01389 UniProtKB Mutagenesis 1119 1119 . . . Note=In BCK1-19%3B Dominant active. T->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1729597;Dbxref=PMID:1729597 +Q01389 UniProtKB Mutagenesis 1120 1120 . . . Note=In BCK1-11%3B Dominant active. I->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1729597;Dbxref=PMID:1729597 +Q01389 UniProtKB Mutagenesis 1120 1120 . . . Note=In BCK1-16%3B Dominant active. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1729597;Dbxref=PMID:1729597 +Q01389 UniProtKB Mutagenesis 1146 1146 . . . Note=In BCK1-10%3B Dominant active. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1729597;Dbxref=PMID:1729597 +Q01389 UniProtKB Mutagenesis 1174 1174 . . . Note=In BCK1-20%3B Dominant active. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1729597;Dbxref=PMID:1729597 +Q01389 UniProtKB Sequence conflict 59 59 . . . Note=F->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01389 UniProtKB Sequence conflict 79 79 . . . Note=E->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01389 UniProtKB Sequence conflict 264 264 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01389 UniProtKB Sequence conflict 279 279 . . . Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01389 UniProtKB Sequence conflict 703 714 . . . Note=RYPQTPSYYYDR->STPKPRVITMTE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01389 UniProtKB Sequence conflict 795 795 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01389 UniProtKB Sequence conflict 802 802 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01389 UniProtKB Sequence conflict 808 808 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01389 UniProtKB Sequence conflict 903 903 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01389 UniProtKB Sequence conflict 919 919 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01389 UniProtKB Sequence conflict 960 960 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01389 UniProtKB Sequence conflict 962 962 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32839 1 456 +P32839 UniProtKB Chain 1 456 . . . ID=PRO_0000084777;Note=Mitochondrial chaperone BCS1 +P32839 UniProtKB Topological domain 1 44 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8599931;Dbxref=PMID:8599931 +P32839 UniProtKB Transmembrane 45 68 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32839 UniProtKB Topological domain 69 456 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8599931;Dbxref=PMID:8599931 +P32839 UniProtKB Nucleotide binding 267 274 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32839 UniProtKB Motif 69 83 . . . Note=Mitochondrial-targeting signal +P32839 UniProtKB Sequence conflict 119 119 . . . Note=N->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32839 UniProtKB Sequence conflict 267 267 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32839 UniProtKB Sequence conflict 349 349 . . . Note=L->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32839 UniProtKB Sequence conflict 351 351 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39713 1 417 +P39713 UniProtKB Chain 1 417 . . . ID=PRO_0000160897;Note=Probable diacetyl reductase [(R)-acetoin forming] 2 +P39713 UniProtKB Metal binding 39 39 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39713 UniProtKB Metal binding 64 64 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39713 UniProtKB Metal binding 120 120 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39713 UniProtKB Metal binding 123 123 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39713 UniProtKB Metal binding 131 131 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39713 UniProtKB Metal binding 173 173 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39713 UniProtKB Modified residue 63 63 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P39714 +##sequence-region Q08347 1 646 +Q08347 UniProtKB Chain 1 646 . . . ID=PRO_0000227682;Note=Alkyl/aryl-sulfatase BDS1 +Q08347 UniProtKB Metal binding 162 162 . . . Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25910 +Q08347 UniProtKB Metal binding 164 164 . . . Note=Zinc%3B via pros nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25910 +Q08347 UniProtKB Metal binding 166 166 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25910 +Q08347 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P38077 1 311 +P38077 UniProtKB Transit peptide 1 33 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7929329;Dbxref=PMID:7929329 +P38077 UniProtKB Chain 34 311 . . . ID=PRO_0000002691;Note=ATP synthase subunit gamma%2C mitochondrial +P38077 UniProtKB Natural variant 207 207 . . . Note=In strain: D273-10B/A1. S->I +P38077 UniProtKB Natural variant 308 308 . . . Note=In allele ATP3a. S->F +P38077 UniProtKB Mutagenesis 273 273 . . . Note=Lower activity. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7929329;Dbxref=PMID:7929329 +P38077 UniProtKB Mutagenesis 297 297 . . . Note=In ATP3-5%3B dominant suppressor of the slow-growth phenotype of yme1 strains lacking mitochondrial DNA. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7498726;Dbxref=PMID:7498726 +P38077 UniProtKB Mutagenesis 303 303 . . . Note=In ATP3-1%3B dominant suppressor of the slow-growth phenotype of yme1 strains lacking mitochondrial DNA. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7498726;Dbxref=PMID:7498726 +P38077 UniProtKB Helix 36 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P38077 UniProtKB Helix 83 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P38077 UniProtKB Beta strand 105 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P38077 UniProtKB Helix 120 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P38077 UniProtKB Beta strand 139 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P38077 UniProtKB Helix 145 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P38077 UniProtKB Helix 156 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P38077 UniProtKB Beta strand 159 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P38077 UniProtKB Beta strand 167 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P38077 UniProtKB Helix 173 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P38077 UniProtKB Helix 189 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P38077 UniProtKB Beta strand 193 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P38077 UniProtKB Beta strand 203 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P38077 UniProtKB Beta strand 209 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P38077 UniProtKB Helix 218 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P38077 UniProtKB Helix 227 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P38077 UniProtKB Beta strand 234 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +P38077 UniProtKB Helix 239 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZIA +##sequence-region P81449 1 96 +P81449 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9857174;Dbxref=PMID:9857174 +P81449 UniProtKB Chain 2 96 . . . ID=PRO_0000071689;Note=ATP synthase subunit e%2C mitochondrial +P81449 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9857174;Dbxref=PMID:9857174 +##sequence-region Q12226 1 474 +Q12226 UniProtKB Chain 1 474 . . . ID=PRO_0000076181;Note=Trichothecene 3-O-acetyltransferase +##sequence-region P41815 1 604 +P41815 UniProtKB Chain 1 604 . . . ID=PRO_0000054147;Note=Valine amino-acid permease +P41815 UniProtKB Topological domain 1 95 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Transmembrane 96 116 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Topological domain 117 119 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Transmembrane 120 140 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Topological domain 141 169 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Transmembrane 170 190 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Topological domain 191 206 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Transmembrane 207 227 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Topological domain 228 238 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Transmembrane 239 259 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Topological domain 260 284 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Transmembrane 285 305 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Topological domain 306 323 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Transmembrane 324 344 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Topological domain 345 377 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Transmembrane 378 398 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Topological domain 399 423 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Transmembrane 424 444 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Topological domain 445 449 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Transmembrane 450 470 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Topological domain 471 502 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Transmembrane 503 523 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Topological domain 524 531 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Transmembrane 532 552 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Topological domain 553 604 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41815 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38084 +P41815 UniProtKB Modified residue 79 79 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38084 +P41815 UniProtKB Sequence conflict 573 575 . . . Note=VYD->GLR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47068 1 1157 +P47068 UniProtKB Chain 1 1157 . . . ID=PRO_0000064839;Note=Myosin tail region-interacting protein MTI1 +P47068 UniProtKB Domain 5 69 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P47068 UniProtKB Coiled coil 234 301 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47068 UniProtKB Coiled coil 356 430 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47068 UniProtKB Compositional bias 278 412 . . . Note=Glu-rich +P47068 UniProtKB Compositional bias 674 830 . . . Note=Pro-rich +P47068 UniProtKB Modified residue 103 103 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P47068 UniProtKB Modified residue 158 158 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198 +P47068 UniProtKB Modified residue 166 166 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P47068 UniProtKB Modified residue 565 565 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P47068 UniProtKB Modified residue 621 621 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P47068 UniProtKB Modified residue 631 631 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198 +P47068 UniProtKB Modified residue 634 634 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P47068 UniProtKB Modified residue 636 636 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47068 UniProtKB Modified residue 638 638 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198 +P47068 UniProtKB Modified residue 647 647 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P47068 UniProtKB Modified residue 850 850 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47068 UniProtKB Modified residue 889 889 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P47068 UniProtKB Modified residue 894 894 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P47068 UniProtKB Modified residue 895 895 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P47068 UniProtKB Cross-link 1012 1012 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P47068 UniProtKB Beta strand 6 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TG0 +P47068 UniProtKB Beta strand 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WDX +P47068 UniProtKB Beta strand 31 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TG0 +P47068 UniProtKB Beta strand 39 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TG0 +P47068 UniProtKB Beta strand 54 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TG0 +P47068 UniProtKB Helix 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TG0 +P47068 UniProtKB Beta strand 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TG0 +##sequence-region Q08236 1 1176 +Q08236 UniProtKB Chain 1 1176 . . . ID=PRO_0000218771;Note=Target of rapamycin complex 2 subunit AVO1 +Q08236 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q08236 UniProtKB Modified residue 140 140 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q08236 UniProtKB Modified residue 144 144 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q08236 UniProtKB Modified residue 400 400 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08236 UniProtKB Modified residue 509 509 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08236 UniProtKB Modified residue 510 510 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08236 UniProtKB Modified residue 552 552 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q08236 UniProtKB Beta strand 1069 1090 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ULB +Q08236 UniProtKB Beta strand 1093 1097 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ULB +Q08236 UniProtKB Beta strand 1112 1115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ULB +Q08236 UniProtKB Helix 1116 1118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ULB +Q08236 UniProtKB Beta strand 1119 1124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ULB +Q08236 UniProtKB Beta strand 1131 1136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ULB +Q08236 UniProtKB Beta strand 1145 1153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ULB +Q08236 UniProtKB Helix 1154 1173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ULB +##sequence-region P47082 1 602 +P47082 UniProtKB Chain 1 602 . . . ID=PRO_0000093834;Note=Vacuolar amino acid transporter 1 +P47082 UniProtKB Topological domain 1 208 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Transmembrane 209 231 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Topological domain 232 240 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Transmembrane 241 261 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Topological domain 262 286 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Transmembrane 287 307 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Topological domain 308 321 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Transmembrane 322 342 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Topological domain 343 344 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Transmembrane 345 365 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Topological domain 366 389 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Transmembrane 390 410 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Topological domain 411 429 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Transmembrane 430 450 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Topological domain 451 466 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Transmembrane 467 487 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Topological domain 488 517 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Transmembrane 518 538 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Topological domain 539 543 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Transmembrane 544 564 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Topological domain 565 580 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Transmembrane 581 601 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Topological domain 602 602 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47082 UniProtKB Modified residue 8 8 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47082 UniProtKB Modified residue 15 15 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47082 UniProtKB Modified residue 35 35 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47082 UniProtKB Modified residue 181 181 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P47082 UniProtKB Modified residue 187 187 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P38176 1 459 +P38176 UniProtKB Chain 1 459 . . . ID=PRO_0000093838;Note=Vacuolar amino acid transporter 5 +P38176 UniProtKB Transmembrane 8 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38176 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38176 UniProtKB Transmembrane 82 102 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38176 UniProtKB Transmembrane 131 151 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38176 UniProtKB Transmembrane 161 181 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38176 UniProtKB Transmembrane 206 226 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38176 UniProtKB Transmembrane 240 260 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38176 UniProtKB Transmembrane 278 298 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38176 UniProtKB Transmembrane 364 384 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38176 UniProtKB Transmembrane 386 406 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38176 UniProtKB Transmembrane 434 454 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P50080 1 613 +P50080 UniProtKB Chain 1 613 . . . ID=PRO_0000173426;Note=Azole resistance protein 1 +P50080 UniProtKB Topological domain 1 70 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Transmembrane 71 91 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Topological domain 92 102 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Transmembrane 103 123 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Topological domain 124 134 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Transmembrane 135 155 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Topological domain 156 163 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Transmembrane 164 184 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Topological domain 185 189 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Transmembrane 190 210 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Topological domain 211 221 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Transmembrane 222 242 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Topological domain 243 298 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Transmembrane 299 319 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Topological domain 320 329 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Transmembrane 330 350 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Topological domain 351 375 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Transmembrane 376 396 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Topological domain 397 414 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Transmembrane 415 435 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Topological domain 436 443 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Transmembrane 444 464 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Topological domain 465 472 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Transmembrane 473 493 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Topological domain 494 581 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Transmembrane 582 602 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50080 UniProtKB Topological domain 603 613 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38084 1 609 +P38084 UniProtKB Chain 1 609 . . . ID=PRO_0000054146;Note=Leu/Val/Ile amino-acid permease +P38084 UniProtKB Topological domain 1 99 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Transmembrane 100 120 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Topological domain 121 123 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Transmembrane 124 144 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Topological domain 145 173 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Transmembrane 174 194 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Topological domain 195 210 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Transmembrane 211 231 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Topological domain 232 235 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Transmembrane 236 256 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Topological domain 257 289 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Transmembrane 290 310 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Topological domain 311 328 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Transmembrane 329 349 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Topological domain 350 374 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Transmembrane 375 395 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Topological domain 396 427 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Transmembrane 428 448 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Topological domain 449 451 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Transmembrane 452 472 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Topological domain 473 500 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Transmembrane 501 521 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Topological domain 522 536 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Transmembrane 537 557 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Topological domain 558 609 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38084 UniProtKB Modified residue 3 3 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38084 UniProtKB Modified residue 15 15 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38084 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38084 UniProtKB Modified residue 19 19 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38084 UniProtKB Modified residue 21 21 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38084 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38084 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38084 UniProtKB Modified residue 84 84 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38084 UniProtKB Sequence conflict 139 139 . . . Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38084 UniProtKB Sequence conflict 203 203 . . . Note=W->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39960 1 2167 +P39960 UniProtKB Chain 1 2167 . . . ID=PRO_0000068858;Note=GTPase-activating protein BEM2/IPL2 +P39960 UniProtKB Domain 592 859 . . . Note=Ras-GEF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00168 +P39960 UniProtKB Domain 1846 1948 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +P39960 UniProtKB Domain 1967 2165 . . . Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172 +P39960 UniProtKB Compositional bias 16 25 . . . Note=Poly-Ser +P39960 UniProtKB Compositional bias 35 43 . . . Note=Poly-Ser +P39960 UniProtKB Compositional bias 58 63 . . . Note=Poly-His +P39960 UniProtKB Compositional bias 198 208 . . . Note=Poly-Asn +P39960 UniProtKB Compositional bias 253 260 . . . Note=Poly-Ser +P39960 UniProtKB Compositional bias 1161 1165 . . . Note=Poly-Thr +P39960 UniProtKB Modified residue 129 129 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P39960 UniProtKB Modified residue 283 283 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P39960 UniProtKB Modified residue 1012 1012 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950 +P39960 UniProtKB Modified residue 1016 1016 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P39960 UniProtKB Modified residue 1038 1038 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39960 UniProtKB Modified residue 1046 1046 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950 +P39960 UniProtKB Modified residue 1054 1054 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P39960 UniProtKB Modified residue 1128 1128 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39960 UniProtKB Cross-link 27 27 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P36149 1 193 +P36149 UniProtKB Chain 1 193 . . . ID=PRO_0000211578;Note=Trafficking protein particle complex subunit BET3 +P36149 UniProtKB Lipidation 80 80 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15692564;Dbxref=PMID:15692564 +P36149 UniProtKB Mutagenesis 80 80 . . . Note=Loss of palmitoylation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15692564;Dbxref=PMID:15692564 +##sequence-region P47134 1 954 +P47134 UniProtKB Chain 1 954 . . . ID=PRO_0000122388;Note=Protein BIR1 +P47134 UniProtKB Repeat 20 117 . . . Note=BIR 1 +P47134 UniProtKB Repeat 153 241 . . . Note=BIR 2 +P47134 UniProtKB Metal binding 208 208 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00029 +P47134 UniProtKB Metal binding 211 211 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00029 +P47134 UniProtKB Metal binding 228 228 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00029 +P47134 UniProtKB Metal binding 237 237 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00029 +P47134 UniProtKB Modified residue 477 477 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47134 UniProtKB Modified residue 508 508 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P47134 UniProtKB Modified residue 552 552 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47134 UniProtKB Modified residue 587 587 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P47134 UniProtKB Modified residue 751 751 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47134 UniProtKB Modified residue 765 765 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P47041 1 543 +P47041 UniProtKB Chain 1 543 . . . ID=PRO_0000203060;Note=Target of rapamycin complex 2 subunit BIT61 +P47041 UniProtKB Modified residue 58 58 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47041 UniProtKB Modified residue 59 59 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47041 UniProtKB Modified residue 139 139 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47041 UniProtKB Modified residue 144 144 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region Q99177 1 341 +Q99177 UniProtKB Chain 1 341 . . . ID=PRO_0000239636;Note=Pre-mRNA-splicing factor BRR1 +##sequence-region P53062 1 197 +P53062 UniProtKB Chain 1 197 . . . ID=PRO_0000202707;Note=Nucleus export protein BRR6 +P53062 UniProtKB Transmembrane 54 74 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53062 UniProtKB Transmembrane 161 181 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08235 1 291 +Q08235 UniProtKB Chain 1 291 . . . ID=PRO_0000120235;Note=Ribosome biogenesis protein BRX1 +Q08235 UniProtKB Domain 31 232 . . . Note=Brix;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00034 +Q08235 UniProtKB Modified residue 285 285 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q08235 UniProtKB Sequence conflict 161 161 . . . Note=G->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08235 UniProtKB Sequence conflict 161 161 . . . Note=G->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q05611 1 235 +Q05611 UniProtKB Chain 1 235 . . . ID=PRO_0000064993;Note=Bypass of stop codon protein 2 +Q05611 UniProtKB Transmembrane 68 88 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05611 UniProtKB Modified residue 177 177 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q08280 1 497 +Q08280 UniProtKB Chain 1 497 . . . ID=PRO_0000084864;Note=Bypass of stop codon protein 6 +Q08280 UniProtKB Topological domain 1 72 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Transmembrane 73 93 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Topological domain 94 144 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Transmembrane 145 165 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Topological domain 166 167 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Transmembrane 168 188 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Topological domain 189 205 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Transmembrane 206 226 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Topological domain 227 232 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Transmembrane 233 253 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Topological domain 254 300 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Transmembrane 301 321 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Topological domain 322 340 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Transmembrane 341 361 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Topological domain 362 373 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Transmembrane 374 394 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Topological domain 395 397 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Transmembrane 398 418 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Topological domain 419 439 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Transmembrane 440 460 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Topological domain 461 462 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Transmembrane 463 483 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Topological domain 484 497 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Modified residue 37 37 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +Q08280 UniProtKB Modified residue 41 41 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q08280 UniProtKB Glycosylation 49 49 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08280 UniProtKB Sequence conflict 472 472 . . . Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47176 1 376 +P47176 UniProtKB Chain 1 376 . . . ID=PRO_0000103302;Note=Branched-chain-amino-acid aminotransferase%2C cytosolic +P47176 UniProtKB Modified residue 202 202 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47176 UniProtKB Sequence conflict 148 149 . . . Note=IG->MA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47176 UniProtKB Sequence conflict 194 195 . . . Note=WP->CA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47176 UniProtKB Sequence conflict 224 224 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47176 UniProtKB Sequence conflict 313 313 . . . Note=F->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P15703 1 313 +P15703 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8935650,ECO:0000269|PubMed:9748433;Dbxref=PMID:8935650,PMID:9748433 +P15703 UniProtKB Chain 24 313 . . . ID=PRO_0000011896;Note=Glucan 1%2C3-beta-glucosidase +P15703 UniProtKB Active site 233 233 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15703 UniProtKB Active site 292 292 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15703 UniProtKB Glycosylation 202 202 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15703 UniProtKB Glycosylation 284 284 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P50277 1 480 +P50277 UniProtKB Chain 1 480 . . . ID=PRO_0000120378;Note=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase +P50277 UniProtKB Region 65 66 . . . Note=7-keto-8-aminopelargonic acid binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50277 UniProtKB Region 126 127 . . . Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50277 UniProtKB Binding site 26 26 . . . Note=7-keto-8-aminopelargonic acid;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50277 UniProtKB Binding site 270 270 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50277 UniProtKB Binding site 314 314 . . . Note=7-keto-8-aminopelargonic acid;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50277 UniProtKB Binding site 350 350 . . . Note=7-keto-8-aminopelargonic acid%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50277 UniProtKB Binding site 352 352 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50277 UniProtKB Binding site 441 441 . . . Note=7-keto-8-aminopelargonic acid;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50277 UniProtKB Modified residue 314 314 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50277 UniProtKB Natural variant 229 229 . . . Note=In strain: ATCC 28383 and ATCC 204626. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16269718;Dbxref=PMID:16269718 +P50277 UniProtKB Natural variant 295 295 . . . Note=In strain: ATCC 28383 and ATCC 204626. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16269718;Dbxref=PMID:16269718 +P50277 UniProtKB Natural variant 384 384 . . . Note=In strain: ATCC 28383 and ATCC 204626. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16269718;Dbxref=PMID:16269718 +P50277 UniProtKB Sequence conflict 140 140 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08965 1 1183 +Q08965 UniProtKB Chain 1 1183 . . . ID=PRO_0000195006;Note=Ribosome biogenesis protein BMS1 +Q08965 UniProtKB Domain 68 234 . . . Note=Bms1-type G +Q08965 UniProtKB Nucleotide binding 76 83 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08965 UniProtKB Modified residue 438 438 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08965 UniProtKB Modified residue 478 478 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q08965 UniProtKB Modified residue 492 492 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08965 UniProtKB Modified residue 504 504 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08965 UniProtKB Modified residue 516 516 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08965 UniProtKB Modified residue 518 518 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08965 UniProtKB Modified residue 523 523 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08965 UniProtKB Modified residue 574 574 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08965 UniProtKB Modified residue 578 578 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q08965 UniProtKB Helix 549 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08965 UniProtKB Helix 560 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08965 UniProtKB Helix 618 624 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08965 UniProtKB Helix 629 634 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +##sequence-region P47039 1 444 +P47039 UniProtKB Chain 1 444 . . . ID=PRO_0000123930;Note=Probable kynurenine--oxoglutarate transaminase BNA3 +P47039 UniProtKB Modified residue 271 271 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47039 UniProtKB Helix 24 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 34 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 70 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 83 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 95 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Turn 106 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 115 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Beta strand 118 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 123 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Beta strand 141 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 152 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Beta strand 162 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 172 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Beta strand 184 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 188 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Beta strand 199 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Turn 209 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 217 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Beta strand 233 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Turn 239 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 252 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 257 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Beta strand 263 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 269 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Beta strand 281 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 288 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 307 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 325 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Beta strand 355 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 377 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Beta strand 380 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 384 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 403 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 409 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Beta strand 418 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 427 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +P47039 UniProtKB Helix 437 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B46 +##sequence-region P40450 1 1375 +P40450 UniProtKB Chain 1 1375 . . . ID=PRO_0000194900;Note=BNI1-related protein 1 +P40450 UniProtKB Domain 94 490 . . . Note=GBD/FH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00579 +P40450 UniProtKB Domain 659 851 . . . Note=FH1 +P40450 UniProtKB Domain 868 1290 . . . Note=FH2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00774 +P40450 UniProtKB Domain 1302 1336 . . . Note=DAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00577 +P40450 UniProtKB Coiled coil 520 601 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40450 UniProtKB Compositional bias 659 839 . . . Note=Pro-rich +P40450 UniProtKB Compositional bias 1332 1335 . . . Note=Arg/Lys-rich (basic) +P40450 UniProtKB Modified residue 621 621 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40450 UniProtKB Modified residue 751 751 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q07457 1 700 +Q07457 UniProtKB Chain 1 700 . . . ID=PRO_0000055857;Note=E3 ubiquitin-protein ligase BRE1 +Q07457 UniProtKB Zinc finger 648 687 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +Q07457 UniProtKB Coiled coil 126 406 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07457 UniProtKB Coiled coil 555 620 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07457 UniProtKB Mutagenesis 663 663 . . . Note=Abolishes ability to monoubiquitinate histone H2B. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12535539;Dbxref=PMID:12535539 +Q07457 UniProtKB Mutagenesis 665 665 . . . Note=Abolishes ability to monoubiquitinate histone H2B. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12535539;Dbxref=PMID:12535539 +Q07457 UniProtKB Helix 633 646 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R7E +Q07457 UniProtKB Turn 649 651 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R7E +Q07457 UniProtKB Beta strand 652 655 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R7E +Q07457 UniProtKB Beta strand 658 660 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R7E +Q07457 UniProtKB Turn 661 663 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R7E +Q07457 UniProtKB Helix 669 677 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R7E +Q07457 UniProtKB Turn 684 686 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R7E +Q07457 UniProtKB Helix 692 694 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R7E +Q07457 UniProtKB Beta strand 695 697 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R7E +##sequence-region Q07660 1 1125 +Q07660 UniProtKB Chain 1 1125 . . . ID=PRO_0000239634;Note=Protein BRE4 +Q07660 UniProtKB Topological domain 1 143 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Transmembrane 144 164 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Topological domain 165 176 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Transmembrane 177 194 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Topological domain 195 198 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Transmembrane 199 219 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Topological domain 220 227 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Transmembrane 228 248 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Topological domain 249 254 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Transmembrane 255 275 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Topological domain 276 284 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Transmembrane 285 305 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Topological domain 306 706 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Transmembrane 707 727 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Topological domain 728 750 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Transmembrane 751 771 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Topological domain 772 780 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Transmembrane 781 801 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Topological domain 802 843 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Transmembrane 844 864 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Topological domain 865 1125 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07660 UniProtKB Glycosylation 830 830 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12140 1 328 +Q12140 UniProtKB Chain 1 328 . . . ID=PRO_0000064992;Note=Bypass of stop codon protein 1 +Q12140 UniProtKB Domain 1 155 . . . Note=Flo11;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01168 +Q12140 UniProtKB Compositional bias 161 317 . . . Note=Ser/Thr-rich +##sequence-region P53755 1 489 +P53755 UniProtKB Chain 1 489 . . . ID=PRO_0000064995;Note=Bypass of stop codon protein 5 +P53755 UniProtKB Modified residue 111 111 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53755 UniProtKB Modified residue 350 350 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53755 UniProtKB Sequence conflict 209 209 . . . Note=Y->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06604 1 576 +Q06604 UniProtKB Chain 1 576 . . . ID=PRO_0000228137;Note=Protein BSP1 +Q06604 UniProtKB Modified residue 46 46 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q06604 UniProtKB Modified residue 79 79 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06604 UniProtKB Modified residue 88 88 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06604 UniProtKB Modified residue 185 185 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06604 UniProtKB Modified residue 220 220 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06604 UniProtKB Modified residue 309 309 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q06604 UniProtKB Modified residue 320 320 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region P25627 1 275 +P25627 UniProtKB Chain 1 275 . . . ID=PRO_0000204459;Note=18S rRNA (guanine(1575)-N(7))-methyltransferase +P25627 UniProtKB Motif 257 264 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25627 UniProtKB Mutagenesis 57 57 . . . Note=Fails to ctalyze the N-7 methylation of the G1575 residue. G->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18332120,ECO:0000269|PubMed:23233232;Dbxref=PMID:18332120,PMID:23233232 +P25627 UniProtKB Mutagenesis 57 57 . . . Note=Can only partially restore the slow-growth phenotype and the random budding pattern of a null mutant. G->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18332120,ECO:0000269|PubMed:23233232;Dbxref=PMID:18332120,PMID:23233232 +P25627 UniProtKB Mutagenesis 77 77 . . . Note=No effect on growth and budding pattern. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18332120,ECO:0000269|PubMed:23233232;Dbxref=PMID:18332120,PMID:23233232 +P25627 UniProtKB Mutagenesis 77 77 . . . Note=Fails to ctalyze the N-7 methylation of the G1575 residue. D->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18332120,ECO:0000269|PubMed:23233232;Dbxref=PMID:18332120,PMID:23233232 +P25627 UniProtKB Helix 16 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTU +P25627 UniProtKB Helix 25 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT +P25627 UniProtKB Beta strand 50 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT +P25627 UniProtKB Helix 60 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT +P25627 UniProtKB Beta strand 72 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT +P25627 UniProtKB Helix 80 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT +P25627 UniProtKB Turn 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT +P25627 UniProtKB Beta strand 92 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT +P25627 UniProtKB Helix 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT +P25627 UniProtKB Beta strand 111 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT +P25627 UniProtKB Helix 120 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT +P25627 UniProtKB Helix 133 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT +P25627 UniProtKB Beta strand 148 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT +P25627 UniProtKB Helix 163 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT +P25627 UniProtKB Beta strand 179 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT +P25627 UniProtKB Turn 190 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT +P25627 UniProtKB Beta strand 194 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QTT +##sequence-region P50944 1 713 +P50944 UniProtKB Chain 1 713 . . . ID=PRO_0000093837;Note=Vacuolar amino acid transporter 4 +P50944 UniProtKB Topological domain 1 242 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Transmembrane 243 263 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Topological domain 264 301 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Transmembrane 302 322 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Topological domain 323 326 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Transmembrane 327 347 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Topological domain 348 373 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Transmembrane 374 394 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Topological domain 395 410 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Transmembrane 411 431 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Topological domain 432 438 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Transmembrane 439 459 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Topological domain 460 483 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Transmembrane 484 504 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Topological domain 505 515 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Transmembrane 516 536 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Topological domain 537 561 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Transmembrane 562 582 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Topological domain 583 621 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Transmembrane 622 642 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Topological domain 643 648 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Transmembrane 649 669 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Topological domain 670 692 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Transmembrane 693 711 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Topological domain 712 713 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50944 UniProtKB Modified residue 88 88 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P50944 UniProtKB Modified residue 130 130 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P50944 UniProtKB Modified residue 165 165 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region P40501 1 490 +P40501 UniProtKB Chain 1 490 . . . ID=PRO_0000093840;Note=Vacuolar amino acid transporter 7 +P40501 UniProtKB Topological domain 1 6 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Topological domain 28 34 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Topological domain 56 84 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Transmembrane 85 105 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Topological domain 106 108 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Transmembrane 109 129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Topological domain 130 143 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Transmembrane 144 164 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Topological domain 165 190 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Transmembrane 191 211 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Topological domain 212 221 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Transmembrane 222 242 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Topological domain 243 264 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Transmembrane 265 285 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Topological domain 286 397 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Transmembrane 398 418 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Topological domain 419 428 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Transmembrane 429 449 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Topological domain 450 463 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Transmembrane 464 484 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40501 UniProtKB Topological domain 485 490 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P41696 1 914 +P41696 UniProtKB Chain 1 914 . . . ID=PRO_0000046802;Note=Asparagine-rich zinc finger protein AZF1 +P41696 UniProtKB Zinc finger 593 615 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P41696 UniProtKB Zinc finger 621 643 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P41696 UniProtKB Zinc finger 649 671 . . . Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P41696 UniProtKB Zinc finger 677 702 . . . Note=C2H2-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P41696 UniProtKB Compositional bias 136 143 . . . Note=Poly-Gln +P41696 UniProtKB Compositional bias 146 154 . . . Note=Poly-Gln +P41696 UniProtKB Compositional bias 362 381 . . . Note=Poly-Asn +P41696 UniProtKB Compositional bias 856 860 . . . Note=Poly-Ser +P41696 UniProtKB Compositional bias 861 868 . . . Note=Poly-Asn +P41696 UniProtKB Modified residue 61 61 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P41696 UniProtKB Modified residue 286 286 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P41696 UniProtKB Modified residue 325 325 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q12365 1 385 +Q12365 UniProtKB Chain 1 385 . . . ID=PRO_0000064840;Note=Spindle pole component BBP1 +Q12365 UniProtKB Coiled coil 229 355 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12365 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12365 UniProtKB Modified residue 73 73 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12365 UniProtKB Modified residue 115 115 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region Q3E793 1 110 +Q3E793 UniProtKB Chain 1 110 . . . ID=PRO_0000248409;Note=BolA-like protein 1 +Q3E793 UniProtKB Mutagenesis 56 56 . . . Note=No effect. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27532773;Dbxref=PMID:27532773 +Q3E793 UniProtKB Mutagenesis 56 56 . . . Note=Partial loss of function. H->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27532773;Dbxref=PMID:27532773 +Q3E793 UniProtKB Mutagenesis 93 93 . . . Note=Loss of function. H->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27532773;Dbxref=PMID:27532773 +##sequence-region P38928 1 823 +P38928 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Chain 23 823 . . . ID=PRO_0000020773;Note=Axial budding pattern protein 2 +P38928 UniProtKB Topological domain 23 508 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Transmembrane 509 529 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Topological domain 530 823 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Modified residue 642 642 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38928 UniProtKB Modified residue 673 673 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38928 UniProtKB Modified residue 676 676 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38928 UniProtKB Glycosylation 41 41 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Glycosylation 50 50 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Glycosylation 96 96 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Glycosylation 117 117 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Glycosylation 163 163 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Glycosylation 260 260 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Glycosylation 266 266 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Glycosylation 304 304 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Glycosylation 324 324 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Glycosylation 359 359 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Glycosylation 382 382 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Glycosylation 389 389 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Glycosylation 403 403 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Glycosylation 447 447 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Glycosylation 451 451 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38928 UniProtKB Glycosylation 495 495 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36122 1 765 +P36122 UniProtKB Chain 1 765 . . . ID=PRO_0000203204;Note=Protein BCH2 +P36122 UniProtKB Region 735 765 . . . Note=CHS5-binding +##sequence-region P33306 1 851 +P33306 UniProtKB Chain 1 851 . . . ID=PRO_0000064883;Note=Protein BCK2 +P33306 UniProtKB Modified residue 334 334 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P33306 UniProtKB Modified residue 757 757 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P33306 UniProtKB Modified residue 761 761 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33306 UniProtKB Sequence conflict 4 5 . . . Note=NS->HC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33306 UniProtKB Sequence conflict 100 100 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33306 UniProtKB Sequence conflict 167 167 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33306 UniProtKB Sequence conflict 812 812 . . . Note=F->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33306 UniProtKB Sequence conflict 827 827 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07442 1 638 +Q07442 UniProtKB Chain 1 638 . . . ID=PRO_0000239629;Note=Bromodomain-containing factor 2 +Q07442 UniProtKB Domain 150 222 . . . Note=Bromo 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 +Q07442 UniProtKB Domain 337 409 . . . Note=Bromo 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 +Q07442 UniProtKB Domain 506 590 . . . Note=NET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00857 +Q07442 UniProtKB Coiled coil 468 537 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07442 UniProtKB Modified residue 264 264 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region P53858 1 892 +P53858 UniProtKB Chain 1 892 . . . ID=PRO_0000064959;Note=Protein BNI4 +P53858 UniProtKB Compositional bias 122 129 . . . Note=Poly-Glu +P53858 UniProtKB Compositional bias 290 293 . . . Note=Poly-Lys +P53858 UniProtKB Compositional bias 321 324 . . . Note=Poly-Ser +P53858 UniProtKB Compositional bias 344 349 . . . Note=Poly-Ser +P53858 UniProtKB Modified residue 43 43 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53858 UniProtKB Modified residue 133 133 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53858 UniProtKB Modified residue 281 281 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53858 UniProtKB Modified residue 364 364 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P53858 UniProtKB Modified residue 394 394 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53858 UniProtKB Modified residue 410 410 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53858 UniProtKB Modified residue 476 476 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53858 UniProtKB Modified residue 500 500 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53858 UniProtKB Modified residue 503 503 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53858 UniProtKB Modified residue 618 618 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53858 UniProtKB Modified residue 703 703 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53858 UniProtKB Modified residue 746 746 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53858 UniProtKB Modified residue 825 825 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P53958 1 396 +P53958 UniProtKB Chain 1 396 . . . ID=PRO_0000203456;Note=Protein BOP3 +##sequence-region Q06338 1 283 +Q06338 UniProtKB Chain 1 283 . . . ID=PRO_0000239628;Note=Protein BCP1 +Q06338 UniProtKB Modified residue 205 205 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06338 UniProtKB Modified residue 209 209 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P47113 1 574 +P47113 UniProtKB Chain 1 574 . . . ID=PRO_0000064913;Note=Mitotic check point protein BFA1 +P47113 UniProtKB Compositional bias 193 201 . . . Note=Poly-Glu +P47113 UniProtKB Compositional bias 265 268 . . . Note=Poly-Ser +P47113 UniProtKB Modified residue 317 317 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40013 1 344 +P40013 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40013 UniProtKB Chain 2 344 . . . ID=PRO_0000213432;Note=Protein BIM1 +P40013 UniProtKB Domain 8 107 . . . Note=Calponin-homology (CH) +P40013 UniProtKB Domain 188 281 . . . Note=EB1 C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00576 +P40013 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40013 UniProtKB Modified residue 157 157 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P40013 UniProtKB Helix 9 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX +P40013 UniProtKB Helix 27 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX +P40013 UniProtKB Helix 34 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX +P40013 UniProtKB Helix 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX +P40013 UniProtKB Helix 59 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX +P40013 UniProtKB Helix 84 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX +P40013 UniProtKB Turn 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX +P40013 UniProtKB Helix 92 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX +P40013 UniProtKB Helix 117 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX +P40013 UniProtKB Turn 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QJX +P40013 UniProtKB Helix 182 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E61 +P40013 UniProtKB Helix 260 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E61 +##sequence-region P38346 1 545 +P38346 UniProtKB Chain 1 545 . . . ID=PRO_0000202530;Note=Probable target of rapamycin complex 2 subunit BIT2 +P38346 UniProtKB Sequence conflict 152 153 . . . Note=SG->RA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P35727 1 113 +P35727 UniProtKB Chain 1 113 . . . ID=PRO_0000203176;Note=Biogenesis of lysosome-related organelles complex 1 subunit BLI1 +P35727 UniProtKB Coiled coil 57 97 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40471 1 297 +P40471 UniProtKB Chain 1 297 . . . ID=PRO_0000054520;Note=NADPH-dependent 1-acyldihydroxyacetone phosphate reductase +P40471 UniProtKB Nucleotide binding 13 37 . . . Note=NAD or NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40471 UniProtKB Active site 157 157 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001 +P40471 UniProtKB Binding site 144 144 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P29366 1 551 +P29366 UniProtKB Chain 1 551 . . . ID=PRO_0000064908;Note=Bud emergence protein 1 +P29366 UniProtKB Domain 72 132 . . . Note=SH3 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P29366 UniProtKB Domain 155 217 . . . Note=SH3 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P29366 UniProtKB Domain 278 404 . . . Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147 +P29366 UniProtKB Domain 478 551 . . . Note=PB1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01081 +P29366 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P29366 UniProtKB Modified residue 47 47 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P29366 UniProtKB Modified residue 255 255 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P29366 UniProtKB Modified residue 258 258 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P29366 UniProtKB Modified residue 458 458 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +P29366 UniProtKB Modified residue 461 461 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956 +P29366 UniProtKB Beta strand 160 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV +P29366 UniProtKB Beta strand 170 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV +P29366 UniProtKB Beta strand 178 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV +P29366 UniProtKB Turn 189 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV +P29366 UniProtKB Beta strand 192 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV +P29366 UniProtKB Beta strand 198 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV +P29366 UniProtKB Beta strand 205 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV +P29366 UniProtKB Beta strand 217 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV +P29366 UniProtKB Helix 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQW +P29366 UniProtKB Helix 227 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV +P29366 UniProtKB Turn 232 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV +P29366 UniProtKB Helix 239 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV +P29366 UniProtKB Turn 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RQV +P29366 UniProtKB Beta strand 283 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V +P29366 UniProtKB Beta strand 297 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V +P29366 UniProtKB Beta strand 311 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V +P29366 UniProtKB Helix 318 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V +P29366 UniProtKB Turn 333 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V +P29366 UniProtKB Helix 363 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V +P29366 UniProtKB Helix 385 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V +P29366 UniProtKB Helix 391 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V +P29366 UniProtKB Beta strand 401 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V +P29366 UniProtKB Beta strand 406 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6V +P29366 UniProtKB Beta strand 479 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IP9 +P29366 UniProtKB Beta strand 490 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IP9 +P29366 UniProtKB Helix 500 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IP9 +P29366 UniProtKB Beta strand 516 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IP9 +P29366 UniProtKB Beta strand 523 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IP9 +P29366 UniProtKB Helix 533 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IP9 +P29366 UniProtKB Beta strand 546 550 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IP9 +##sequence-region P39011 1 633 +P39011 UniProtKB Chain 1 633 . . . ID=PRO_0000064910;Note=Bud emergence protein 4 +##sequence-region Q03630 1 159 +Q03630 UniProtKB Chain 1 159 . . . ID=PRO_0000211565;Note=Trafficking protein particle complex subunit BET5 +##sequence-region P38813 1 335 +P38813 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38813 UniProtKB Chain 18 335 . . . ID=PRO_0000014327;Note=Protein BIG1 +P38813 UniProtKB Topological domain 20 275 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38813 UniProtKB Transmembrane 276 296 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38813 UniProtKB Topological domain 297 335 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38813 UniProtKB Glycosylation 24 24 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38813 UniProtKB Glycosylation 144 144 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53744 1 561 +P53744 UniProtKB Chain 1 561 . . . ID=PRO_0000054282;Note=7-keto 8-aminopelargonic acid transporter +P53744 UniProtKB Topological domain 1 49 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Transmembrane 50 70 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Topological domain 71 77 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Transmembrane 78 98 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Topological domain 99 160 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Transmembrane 161 181 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Topological domain 182 204 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Transmembrane 205 225 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Topological domain 226 230 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Transmembrane 231 251 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Topological domain 252 281 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Transmembrane 282 302 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Topological domain 303 321 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Transmembrane 322 342 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Topological domain 343 369 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Transmembrane 370 390 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Topological domain 391 439 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Transmembrane 440 460 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Topological domain 461 461 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Transmembrane 462 482 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Topological domain 483 507 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Transmembrane 508 528 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Topological domain 529 540 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Transmembrane 541 560 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53744 UniProtKB Topological domain 561 561 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43583 1 2143 +P43583 UniProtKB Chain 1 2143 . . . ID=PRO_0000076182;Note=Proteasome activator BLM10 +P43583 UniProtKB Repeat 1316 1355 . . . Note=HEAT 1 +P43583 UniProtKB Repeat 1779 1814 . . . Note=HEAT 2 +P43583 UniProtKB Repeat 1902 1941 . . . Note=HEAT 3 +P43583 UniProtKB Repeat 1985 2023 . . . Note=HEAT 4 +P43583 UniProtKB Region 1648 1732 . . . Note=Bromodomain-like (BRDL) +P43583 UniProtKB Motif 2141 2143 . . . Note=YYX motif +P43583 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P43583 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P43583 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P43583 UniProtKB Modified residue 62 62 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +P43583 UniProtKB Modified residue 64 64 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P43583 UniProtKB Modified residue 66 66 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43583 UniProtKB Modified residue 1041 1041 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198 +P43583 UniProtKB Mutagenesis 1663 1664 . . . Note=Abolihes binding to acetylated histones. YN->HD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23706739;Dbxref=PMID:23706739 +P43583 UniProtKB Mutagenesis 2139 2139 . . . Note=Does not affect binding to the proteasome. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22025621;Dbxref=PMID:22025621 +P43583 UniProtKB Mutagenesis 2140 2140 . . . Note=Abolishes binding to the proteasome. S->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22025621;Dbxref=PMID:22025621 +P43583 UniProtKB Mutagenesis 2141 2143 . . . Note=Loss of function. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20227375;Dbxref=PMID:20227375 +P43583 UniProtKB Mutagenesis 2141 2141 . . . Note=Does not affect viability in the presence of cycloheximide. Y->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22025621;Dbxref=PMID:22025621 +P43583 UniProtKB Mutagenesis 2142 2142 . . . Note=Loss of function%3B abolishes binding to the proteasome. Y->A%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22025621;Dbxref=PMID:22025621 +P43583 UniProtKB Mutagenesis 2142 2142 . . . Note=Abolishes binding to the proteasome. Y->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22025621;Dbxref=PMID:22025621 +P43583 UniProtKB Mutagenesis 2143 2143 . . . Note=Does not affect viability in the presence of cycloheximide. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22025621;Dbxref=PMID:22025621 +P43583 UniProtKB Helix 81 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 97 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 122 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 126 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 133 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 240 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 249 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 257 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 280 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 300 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 313 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 321 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 329 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 339 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 342 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 364 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 367 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 375 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 380 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 383 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 405 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 408 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 415 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 422 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 444 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 465 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 488 496 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 505 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 508 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 531 552 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 553 559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 563 565 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 568 586 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 591 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 612 627 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 628 633 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 635 646 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 649 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 658 661 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 662 671 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 678 693 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 709 712 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 714 725 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 730 732 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 739 747 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 748 750 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 751 765 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 773 787 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 791 806 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 813 815 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 819 831 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 833 835 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 836 852 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 853 856 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 861 863 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 866 868 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 869 882 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 883 885 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 886 890 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 893 905 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 910 916 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 919 928 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 937 941 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 953 956 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 957 960 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 962 964 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 974 997 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1009 1023 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1026 1029 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1032 1035 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 1158 1161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 1162 1165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1167 1193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1199 1211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 1215 1217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1231 1238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1249 1266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1276 1288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1293 1307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 1308 1310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1313 1330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1335 1343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1347 1352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1353 1355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1357 1369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 1374 1377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 1378 1380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1381 1390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1404 1406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1408 1410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1420 1427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1430 1451 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1460 1471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1481 1488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1489 1493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1496 1506 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1508 1519 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1523 1526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 1527 1530 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 1536 1541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 1544 1546 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1547 1554 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 1577 1582 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1593 1603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1608 1620 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 1621 1625 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1630 1643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1652 1654 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1655 1661 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1668 1681 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 1690 1692 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1693 1708 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1716 1730 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1733 1735 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1737 1743 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1764 1774 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1782 1787 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1795 1810 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1820 1828 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 1831 1834 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1843 1856 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1858 1861 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 1869 1873 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1875 1890 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1893 1895 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1896 1899 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1900 1902 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1903 1907 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 1908 1911 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1919 1923 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1929 1934 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 1936 1938 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1942 1951 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 1955 1958 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 1961 1963 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1964 1978 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 1979 1981 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1986 1989 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 1991 1994 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 1995 1999 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 2004 2019 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 2024 2034 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Turn 2039 2041 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 2045 2054 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 2056 2069 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 2081 2090 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Beta strand 2093 2095 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 2099 2102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 2104 2113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 2118 2121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 2122 2124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +P43583 UniProtKB Helix 2131 2133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V7O +##sequence-region P47040 1 408 +P47040 UniProtKB Signal peptide 1 30 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47040 UniProtKB Chain 31 408 . . . ID=PRO_0000020836;Note=Protein BTN1 +P47040 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47040 UniProtKB Transmembrane 80 100 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47040 UniProtKB Transmembrane 128 148 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47040 UniProtKB Transmembrane 150 170 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47040 UniProtKB Transmembrane 238 258 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47040 UniProtKB Transmembrane 323 343 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47040 UniProtKB Transmembrane 369 389 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47040 UniProtKB Natural variant 181 181 . . . Note=In strain: K289-3A. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9753630;Dbxref=PMID:9753630 +P47040 UniProtKB Natural variant 328 328 . . . Note=In strain: K289-3A. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9753630;Dbxref=PMID:9753630 +P47040 UniProtKB Sequence conflict 162 162 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P41695 1 1021 +P41695 UniProtKB Chain 1 1021 . . . ID=PRO_0000085676;Note=Checkpoint serine/threonine-protein kinase BUB1 +P41695 UniProtKB Domain 47 212 . . . Note=BUB1 N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00822 +P41695 UniProtKB Domain 705 1021 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P41695 UniProtKB Nucleotide binding 711 719 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P41695 UniProtKB Active site 833 833 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P41695 UniProtKB Binding site 733 733 . . . Note=ATP +P41695 UniProtKB Mutagenesis 733 733 . . . Note=Loss of activity. K->R +P41695 UniProtKB Sequence conflict 531 531 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41695 UniProtKB Beta strand 307 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BL0 +P41695 UniProtKB Beta strand 317 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3S +P41695 UniProtKB Helix 323 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3S +P41695 UniProtKB Beta strand 330 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BL0 +P41695 UniProtKB Helix 336 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3S +##sequence-region P39988 1 312 +P39988 UniProtKB Chain 1 312 . . . ID=PRO_0000213348;Note=Putative pyridoxal kinase BUD16 +P39988 UniProtKB Nucleotide binding 183 184 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39988 UniProtKB Nucleotide binding 211 223 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39988 UniProtKB Binding site 9 9 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39988 UniProtKB Binding site 44 44 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39988 UniProtKB Binding site 122 122 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39988 UniProtKB Binding site 224 224 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q04347 1 519 +Q04347 UniProtKB Chain 1 519 . . . ID=PRO_0000065014;Note=Bud site selection protein 22 +Q04347 UniProtKB Coiled coil 426 470 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04347 UniProtKB Modified residue 257 257 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +Q04347 UniProtKB Modified residue 367 367 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q04347 UniProtKB Modified residue 371 371 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q04347 UniProtKB Modified residue 375 375 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q04347 UniProtKB Sequence conflict 497 497 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P85052 1 153 +P85052 UniProtKB Chain 1 153 . . . ID=PRO_0000270625;Note=Bud site selection protein 25 +##sequence-region P33314 1 1104 +P33314 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P33314 UniProtKB Chain 2 1104 . . . ID=PRO_0000056656;Note=Inhibitory regulator protein BUD2/CLA2 +P33314 UniProtKB Domain 322 425 . . . Note=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 +P33314 UniProtKB Domain 505 721 . . . Note=Ras-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00167 +P33314 UniProtKB Compositional bias 496 499 . . . Note=Poly-Ser +P33314 UniProtKB Compositional bias 1096 1099 . . . Note=Poly-Lys +P33314 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P33314 UniProtKB Modified residue 854 854 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P33314 UniProtKB Sequence conflict 437 437 . . . Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47136 1 1447 +P47136 UniProtKB Chain 1 1447 . . . ID=PRO_0000065017;Note=Bud site selection protein 4 +P47136 UniProtKB Domain 1302 1413 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +P47136 UniProtKB Region 768 879 . . . Note=Interaction with IQG1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12446742;Dbxref=PMID:12446742 +P47136 UniProtKB Compositional bias 181 189 . . . Note=Asp/Glu-rich (acidic) +P47136 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47136 UniProtKB Modified residue 78 78 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47136 UniProtKB Modified residue 81 81 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47136 UniProtKB Modified residue 91 91 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47136 UniProtKB Modified residue 96 96 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47136 UniProtKB Modified residue 167 167 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47136 UniProtKB Modified residue 365 365 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47136 UniProtKB Modified residue 367 367 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47136 UniProtKB Modified residue 511 511 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47136 UniProtKB Modified residue 616 616 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47136 UniProtKB Modified residue 805 805 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47136 UniProtKB Modified residue 811 811 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47136 UniProtKB Sequence conflict 340 340 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P41697 1 788 +P41697 UniProtKB Chain 1 788 . . . ID=PRO_0000065018;Note=Bud site selection protein 6 +P41697 UniProtKB Coiled coil 573 628 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41697 UniProtKB Modified residue 12 12 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P41697 UniProtKB Modified residue 233 233 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P41697 UniProtKB Modified residue 327 327 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P41697 UniProtKB Modified residue 342 342 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956 +P41697 UniProtKB Sequence conflict 376 376 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41697 UniProtKB Sequence conflict 384 385 . . . Note=NA->KP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41697 UniProtKB Sequence conflict 434 434 . . . Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41697 UniProtKB Sequence conflict 441 441 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41697 UniProtKB Sequence conflict 454 454 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41697 UniProtKB Sequence conflict 565 568 . . . Note=ELGD->SH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41697 UniProtKB Sequence conflict 742 742 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41697 UniProtKB Sequence conflict 764 788 . . . Note=FEEVERIRKQKDEANLRAYFGPGFT->LKK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41697 UniProtKB Helix 555 594 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OKQ +P41697 UniProtKB Helix 600 676 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OKQ +P41697 UniProtKB Helix 701 713 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WYB +P41697 UniProtKB Helix 719 733 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WYB +P41697 UniProtKB Turn 734 737 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WYB +##sequence-region P38822 1 633 +P38822 UniProtKB Chain 1 633 . . . ID=PRO_0000065033;Note=Protein BZZ1 +P38822 UniProtKB Domain 5 271 . . . Note=F-BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01077 +P38822 UniProtKB Domain 493 555 . . . Note=SH3 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P38822 UniProtKB Domain 577 633 . . . Note=SH3 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P38822 UniProtKB Coiled coil 138 210 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38822 UniProtKB Modified residue 327 327 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38822 UniProtKB Modified residue 463 463 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38822 UniProtKB Modified residue 472 472 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38822 UniProtKB Modified residue 476 476 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38822 UniProtKB Sequence conflict 196 196 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38822 UniProtKB Beta strand 520 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUU +P38822 UniProtKB Beta strand 527 536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUU +P38822 UniProtKB Turn 537 540 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUU +P38822 UniProtKB Beta strand 541 546 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUU +P38822 UniProtKB Helix 547 549 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUU +P38822 UniProtKB Beta strand 582 584 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A28 +P38822 UniProtKB Beta strand 603 608 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A28 +P38822 UniProtKB Beta strand 612 620 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A28 +P38822 UniProtKB Beta strand 623 628 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A28 +P38822 UniProtKB Helix 629 631 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A28 +##sequence-region Q04749 1 426 +Q04749 UniProtKB Chain 1 426 . . . ID=PRO_0000067247;Note=Target of rapamycin complex 2 subunit AVO2 +Q04749 UniProtKB Repeat 4 33 . . . Note=ANK 1 +Q04749 UniProtKB Repeat 39 68 . . . Note=ANK 2 +Q04749 UniProtKB Repeat 74 104 . . . Note=ANK 3 +Q04749 UniProtKB Repeat 108 137 . . . Note=ANK 4 +Q04749 UniProtKB Repeat 141 171 . . . Note=ANK 5 +Q04749 UniProtKB Modified residue 315 315 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04749 UniProtKB Modified residue 350 350 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P40074 1 448 +P40074 UniProtKB Chain 1 448 . . . ID=PRO_0000093839;Note=Vacuolar amino acid transporter 6 +P40074 UniProtKB Topological domain 1 7 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Transmembrane 8 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Topological domain 29 32 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Topological domain 54 80 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Transmembrane 81 101 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Topological domain 102 125 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Transmembrane 126 146 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Topological domain 147 150 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Transmembrane 151 171 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Topological domain 172 195 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Transmembrane 196 216 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Topological domain 217 229 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Transmembrane 230 250 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Topological domain 251 267 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Transmembrane 268 288 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Topological domain 289 357 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Transmembrane 358 378 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Topological domain 379 381 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Transmembrane 382 402 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Topological domain 403 424 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Transmembrane 425 445 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Topological domain 446 448 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40074 UniProtKB Modified residue 344 344 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P12630 1 587 +P12630 UniProtKB Signal peptide 1 24 . . . . +P12630 UniProtKB Chain 25 587 . . . ID=PRO_0000025834;Note=Barrierpepsin +P12630 UniProtKB Domain 45 393 . . . Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103 +P12630 UniProtKB Active site 63 63 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +P12630 UniProtKB Active site 287 287 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +P12630 UniProtKB Glycosylation 84 84 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12630 UniProtKB Glycosylation 90 90 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12630 UniProtKB Glycosylation 268 268 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12630 UniProtKB Glycosylation 308 308 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12630 UniProtKB Glycosylation 366 366 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12630 UniProtKB Glycosylation 398 398 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12630 UniProtKB Glycosylation 468 468 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12630 UniProtKB Glycosylation 503 503 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12630 UniProtKB Glycosylation 551 551 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12630 UniProtKB Disulfide bond 322 358 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q12186 1 476 +Q12186 UniProtKB Chain 1 476 . . . ID=PRO_0000234564;Note=Branchpoint-bridging protein +Q12186 UniProtKB Domain 153 219 . . . Note=KH +Q12186 UniProtKB Zinc finger 271 288 . . . Note=CCHC-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +Q12186 UniProtKB Zinc finger 297 314 . . . Note=CCHC-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +Q12186 UniProtKB Compositional bias 363 474 . . . Note=Pro-rich +Q12186 UniProtKB Modified residue 93 93 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12186 UniProtKB Modified residue 95 95 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12186 UniProtKB Modified residue 100 100 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12186 UniProtKB Modified residue 382 382 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12186 UniProtKB Mutagenesis 60 60 . . . Note=In MSL5-2%3B temperature-sensitive%3B growth defect%3B when associated with N-72 and S-155. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10775271;Dbxref=PMID:10775271 +Q12186 UniProtKB Mutagenesis 72 72 . . . Note=In MSL5-2%3B temperature-sensitive%3B growth defect%3B when associated with G-60 and S-155. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10775271;Dbxref=PMID:10775271 +Q12186 UniProtKB Mutagenesis 155 155 . . . Note=In MSL5-2%3B temperature-sensitive%3B growth defect%3B when associated with G-60 and N-72. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10775271;Dbxref=PMID:10775271 +Q12186 UniProtKB Mutagenesis 195 195 . . . Note=In MSL5-5%3B cold-sensitive%3B growth defect%3B when associated with V-258. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10775271;Dbxref=PMID:10775271 +Q12186 UniProtKB Mutagenesis 230 230 . . . Note=In msl-5%3B loss of function. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9150140;Dbxref=PMID:9150140 +Q12186 UniProtKB Mutagenesis 258 258 . . . Note=In MSL5-5%3B cold-sensitive%3B growth defect%3B when associated with D-195. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10775271;Dbxref=PMID:10775271 +Q12186 UniProtKB Beta strand 148 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN +Q12186 UniProtKB Turn 156 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN +Q12186 UniProtKB Helix 164 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN +Q12186 UniProtKB Helix 171 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN +Q12186 UniProtKB Helix 174 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN +Q12186 UniProtKB Beta strand 186 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN +Q12186 UniProtKB Helix 201 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN +Q12186 UniProtKB Turn 206 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN +Q12186 UniProtKB Beta strand 212 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN +Q12186 UniProtKB Helix 224 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN +Q12186 UniProtKB Helix 250 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WAN +##sequence-region P38891 1 393 +P38891 UniProtKB Transit peptide 1 16 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38891 UniProtKB Chain 17 393 . . . ID=PRO_0000001281;Note=Branched-chain-amino-acid aminotransferase%2C mitochondrial +P38891 UniProtKB Modified residue 219 219 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38891 UniProtKB Modified residue 315 315 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P38772 1 366 +P38772 UniProtKB Chain 1 366 . . . ID=PRO_0000173558;Note=Box C/D snoRNA protein 1 +P38772 UniProtKB Zinc finger 5 39 . . . Note=HIT-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00453 +P38772 UniProtKB Modified residue 330 330 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38772 UniProtKB Beta strand 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N94 +P38772 UniProtKB Turn 18 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N94 +P38772 UniProtKB Helix 27 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N94 +P38772 UniProtKB Beta strand 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N94 +##sequence-region P32873 1 1128 +P32873 UniProtKB Chain 1 1128 . . . ID=PRO_0000056728;Note=GTPase-activating protein BEM3 +P32873 UniProtKB Domain 634 741 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +P32873 UniProtKB Domain 913 1128 . . . Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172 +P32873 UniProtKB Modified residue 254 254 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P22804 1 142 +P22804 UniProtKB Chain 1 142 . . . ID=PRO_0000206892;Note=Protein transport protein BET1 +P22804 UniProtKB Topological domain 1 117 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22804 UniProtKB Transmembrane 118 141 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22804 UniProtKB Topological domain 142 142 . . . Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22804 UniProtKB Domain 52 114 . . . Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202 +P22804 UniProtKB Helix 52 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +##sequence-region Q06631 1 534 +Q06631 UniProtKB Chain 1 534 . . . ID=PRO_0000056634;Note=Protein BFR2 +Q06631 UniProtKB Coiled coil 86 161 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06631 UniProtKB Modified residue 41 41 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06631 UniProtKB Modified residue 44 44 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06631 UniProtKB Modified residue 366 366 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06631 UniProtKB Modified residue 372 372 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06631 UniProtKB Modified residue 379 379 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06631 UniProtKB Sequence conflict 451 451 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P11709 1 440 +P11709 UniProtKB Chain 1 440 . . . ID=PRO_0000083513;Note=Nuclear fusion protein BIK1 +P11709 UniProtKB Domain 26 69 . . . Note=CAP-Gly;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00045 +P11709 UniProtKB Coiled coil 190 397 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P11709 UniProtKB Motif 416 429 . . . Note=CCHC-box +P11709 UniProtKB Modified residue 95 95 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P11709 UniProtKB Modified residue 110 110 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +##sequence-region P32451 1 375 +P32451 UniProtKB Transit peptide 1 16 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32451 UniProtKB Chain 17 375 . . . ID=PRO_0000185567;Note=Biotin synthase%2C mitochondrial +P32451 UniProtKB Metal binding 99 99 . . . Note=Iron-sulfur 1 (4Fe-4S-S-AdoMet);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32451 UniProtKB Metal binding 103 103 . . . Note=Iron-sulfur 1 (4Fe-4S-S-AdoMet);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32451 UniProtKB Metal binding 106 106 . . . Note=Iron-sulfur 1 (4Fe-4S-S-AdoMet);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32451 UniProtKB Metal binding 143 143 . . . Note=Iron-sulfur 2 (2Fe-2S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32451 UniProtKB Metal binding 176 176 . . . Note=Iron-sulfur 2 (2Fe-2S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32451 UniProtKB Metal binding 236 236 . . . Note=Iron-sulfur 2 (2Fe-2S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32451 UniProtKB Metal binding 314 314 . . . Note=Iron-sulfur 2 (2Fe-2S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32451 UniProtKB Sequence conflict 348 349 . . . Note=MC->IY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40493 1 336 +P40493 UniProtKB Chain 1 336 . . . ID=PRO_0000202971;Note=25S rRNA (uridine(2634)-N(3))-methyltransferase +P40493 UniProtKB Mutagenesis 182 182 . . . Note=Abolishes methyltransferase activity. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24335083;Dbxref=PMID:24335083 +##sequence-region P39724 1 118 +P39724 UniProtKB Chain 1 118 . . . ID=PRO_0000201239;Note=BolA-like protein 3 +P39724 UniProtKB Mutagenesis 64 64 . . . Note=Partial loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27532773;Dbxref=PMID:27532773 +P39724 UniProtKB Mutagenesis 101 101 . . . Note=Loss of function. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27532773;Dbxref=PMID:27532773 +P39724 UniProtKB Mutagenesis 101 101 . . . Note=Dominant negative mutant%3B displays respiratory defects that are higher than the BOL1 BOL3 double mutant. H->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27532773;Dbxref=PMID:27532773 +##sequence-region P26449 1 341 +P26449 UniProtKB Chain 1 341 . . . ID=PRO_0000050890;Note=Cell cycle arrest protein BUB3 +P26449 UniProtKB Repeat 9 48 . . . Note=WD 1 +P26449 UniProtKB Repeat 54 96 . . . Note=WD 2 +P26449 UniProtKB Repeat 97 137 . . . Note=WD 3 +P26449 UniProtKB Repeat 144 185 . . . Note=WD 4 +P26449 UniProtKB Repeat 191 233 . . . Note=WD 5 +P26449 UniProtKB Repeat 249 288 . . . Note=WD 6 +P26449 UniProtKB Repeat 292 329 . . . Note=WD 7 +P26449 UniProtKB Mutagenesis 2 2 . . . Note=Abolishes checkpoint function. Benomyl-sensitive phenotype. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329 +P26449 UniProtKB Mutagenesis 31 31 . . . Note=Abolishes checkpoint function and interaction with MAD2%2C MAD3 and CDC20. Benomyl-sensitive phenotype. W->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11726501;Dbxref=PMID:11726501 +P26449 UniProtKB Mutagenesis 120 120 . . . Note=Abolishes checkpoint function and interaction with MAD2%2C MAD3 and CDC20. Benomyl-sensitive phenotype. W->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11726501;Dbxref=PMID:11726501 +P26449 UniProtKB Mutagenesis 188 188 . . . Note=Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329 +P26449 UniProtKB Mutagenesis 191 191 . . . Note=Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329 +P26449 UniProtKB Mutagenesis 192 192 . . . Note=Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329 +P26449 UniProtKB Mutagenesis 193 193 . . . Note=Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329 +P26449 UniProtKB Mutagenesis 217 217 . . . Note=Abolishes checkpoint function. Benomyl-sensitive phenotype. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329 +P26449 UniProtKB Mutagenesis 226 226 . . . Note=Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329 +P26449 UniProtKB Mutagenesis 242 242 . . . Note=Abolishes checkpoint function. Benomyl-sensitive phenotype. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329 +P26449 UniProtKB Mutagenesis 276 276 . . . Note=Abolishes checkpoint function. Lowers interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329 +P26449 UniProtKB Mutagenesis 278 278 . . . Note=Abolishes checkpoint function. No effect on interaction with BUB1. Lowers interaction with MAD3. Benomyl-sensitive phenotype. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15644329;Dbxref=PMID:15644329 +P26449 UniProtKB Beta strand 2 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 14 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Helix 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 25 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 33 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Turn 42 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 46 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 59 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 81 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 86 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 104 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Turn 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 114 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 122 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Helix 129 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 133 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3S +P26449 UniProtKB Beta strand 137 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 144 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 153 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 160 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 171 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3T +P26449 UniProtKB Beta strand 186 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 196 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Helix 204 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 208 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 216 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 236 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 241 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3S +P26449 UniProtKB Beta strand 249 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3S +P26449 UniProtKB Beta strand 254 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Turn 261 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 266 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 275 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Turn 280 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 284 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 293 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 304 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Helix 315 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 320 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +P26449 UniProtKB Beta strand 332 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFQ +##sequence-region Q08492 1 214 +Q08492 UniProtKB Chain 1 214 . . . ID=PRO_0000065013;Note=Bud site selection protein 21 +Q08492 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08492 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q08492 UniProtKB Modified residue 65 65 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q08492 UniProtKB Modified residue 144 144 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region Q05949 1 395 +Q05949 UniProtKB Chain 1 395 . . . ID=PRO_0000076186;Note=Protein BUR2 +Q05949 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P40580 1 263 +P40580 UniProtKB Chain 1 263 . . . ID=PRO_0000054871;Note=Benzil reductase ((S)-benzoin forming) IRC24 +P40580 UniProtKB Nucleotide binding 6 30 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40580 UniProtKB Active site 157 157 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001 +P40580 UniProtKB Binding site 144 144 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P09440 1 975 +P09440 UniProtKB Transit peptide 1 34 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3528153;Dbxref=PMID:3528153 +P09440 UniProtKB Chain 35 975 . . . ID=PRO_0000034052;Note=C-1-tetrahydrofolate synthase%2C mitochondrial +P09440 UniProtKB Nucleotide binding 201 203 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09440 UniProtKB Nucleotide binding 408 415 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09440 UniProtKB Region 35 343 . . . Note=Methylenetetrahydrofolate dehydrogenase and cyclohydrolase +P09440 UniProtKB Region 83 87 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09440 UniProtKB Region 130 132 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09440 UniProtKB Region 301 305 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09440 UniProtKB Region 344 975 . . . Note=Formyltetrahydrofolate synthetase +P09440 UniProtKB Binding site 226 226 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P43569 1 289 +P43569 UniProtKB Chain 1 289 . . . ID=PRO_0000093464;Note=CCR4-associated factor 16 +P43569 UniProtKB Domain 7 249 . . . Note=ABC transporter;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P43569 UniProtKB Nucleotide binding 41 48 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +##sequence-region P53615 1 221 +P53615 UniProtKB Chain 1 221 . . . ID=PRO_0000077468;Note=Carbonic anhydrase +P53615 UniProtKB Metal binding 57 57 . . . Note=Zinc;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3EYX,ECO:0000269|PubMed:19852838;Dbxref=PMID:19852838 +P53615 UniProtKB Metal binding 59 59 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61517 +P53615 UniProtKB Metal binding 112 112 . . . Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3EYX,ECO:0000269|PubMed:19852838;Dbxref=PMID:19852838 +P53615 UniProtKB Metal binding 115 115 . . . Note=Zinc;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3EYX,ECO:0000269|PubMed:19852838;Dbxref=PMID:19852838 +P53615 UniProtKB Sequence conflict 39 39 . . . Note=L->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53615 UniProtKB Helix 18 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Helix 37 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Beta strand 51 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Helix 64 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Beta strand 73 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Helix 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Helix 89 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Beta strand 105 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Helix 116 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Helix 126 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Helix 130 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Helix 135 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Helix 142 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Helix 152 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Helix 161 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Helix 184 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Beta strand 196 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Turn 204 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Beta strand 209 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +P53615 UniProtKB Beta strand 217 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EYX +##sequence-region P07252 1 654 +P07252 UniProtKB Chain 1 654 . . . ID=PRO_0000089378;Note=Cytochrome B pre-mRNA-processing protein 1 +##sequence-region P0C155 1 581 +P0C155 UniProtKB Chain 1 581 . . . ID=PRO_0000226147;Note=Putative carboxypeptidase YOL153C +P0C155 UniProtKB Topological domain 1 29 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C155 UniProtKB Transmembrane 30 46 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C155 UniProtKB Topological domain 47 581 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C155 UniProtKB Active site 172 172 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C155 UniProtKB Active site 241 241 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C155 UniProtKB Metal binding 170 170 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C155 UniProtKB Metal binding 207 207 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C155 UniProtKB Metal binding 207 207 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C155 UniProtKB Metal binding 242 242 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C155 UniProtKB Metal binding 270 270 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C155 UniProtKB Metal binding 550 550 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0C155 UniProtKB Glycosylation 54 54 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C155 UniProtKB Glycosylation 76 76 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C155 UniProtKB Glycosylation 335 335 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C155 UniProtKB Glycosylation 428 428 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0C155 UniProtKB Cross-link 17 17 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27614 +##sequence-region P27614 1 576 +P27614 UniProtKB Chain 1 576 . . . ID=PRO_0000185271;Note=Carboxypeptidase S +P27614 UniProtKB Topological domain 1 19 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27614 UniProtKB Transmembrane 20 40 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27614 UniProtKB Topological domain 41 576 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27614 UniProtKB Active site 170 170 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P27614 UniProtKB Active site 239 239 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P27614 UniProtKB Metal binding 168 168 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P27614 UniProtKB Metal binding 205 205 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P27614 UniProtKB Metal binding 205 205 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P27614 UniProtKB Metal binding 240 240 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P27614 UniProtKB Metal binding 268 268 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P27614 UniProtKB Metal binding 547 547 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P27614 UniProtKB Glycosylation 88 88 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27614 UniProtKB Glycosylation 176 176 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27614 UniProtKB Glycosylation 228 228 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27614 UniProtKB Glycosylation 381 381 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27614 UniProtKB Glycosylation 525 525 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27614 UniProtKB Cross-link 8 8 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P27614 UniProtKB Sequence conflict 387 387 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P00729 1 532 +P00729 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00729 UniProtKB Propeptide 21 111 . . . ID=PRO_0000004293;Note=Mediates translocation across the endoplasmic reticulum%2C renders the enzyme inactive during transit%2C and targets the molecule to the vacuole;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|Ref.4,ECO:0000305|PubMed:3028649;Dbxref=PMID:3028649 +P00729 UniProtKB Chain 112 532 . . . ID=PRO_0000004294;Note=Carboxypeptidase Y +P00729 UniProtKB Motif 24 27 . . . Note=Vacuolar targeting signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3028649;Dbxref=PMID:3028649 +P00729 UniProtKB Active site 257 257 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7727362,ECO:0000269|Ref.5;Dbxref=PMID:7727362 +P00729 UniProtKB Active site 449 449 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7727362;Dbxref=PMID:7727362 +P00729 UniProtKB Active site 508 508 . . . Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:2639680,ECO:0000305|PubMed:7727362;Dbxref=PMID:2639680,PMID:7727362 +P00729 UniProtKB Binding site 452 452 . . . Note=Substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|Ref.5 +P00729 UniProtKB Binding site 509 509 . . . Note=Substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|Ref.5 +P00729 UniProtKB Glycosylation 124 124 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28189789;Dbxref=PMID:28189789 +P00729 UniProtKB Glycosylation 198 198 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15713484,ECO:0000269|PubMed:28189789,ECO:0000269|PubMed:7727362;Dbxref=PMID:15713484,PMID:28189789,PMID:7727362 +P00729 UniProtKB Glycosylation 279 279 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15713484,ECO:0000269|PubMed:28189789,ECO:0000269|PubMed:7727362;Dbxref=PMID:15713484,PMID:28189789,PMID:7727362 +P00729 UniProtKB Glycosylation 479 479 . . . Note=N-linked (GlcNAc...) (high mannose) asparagine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15713484,ECO:0000269|PubMed:28189789,ECO:0000269|PubMed:7727362;Dbxref=PMID:15713484,PMID:28189789,PMID:7727362 +P00729 UniProtKB Disulfide bond 167 409 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15713484,ECO:0000269|PubMed:7727362;Dbxref=PMID:15713484,PMID:7727362 +P00729 UniProtKB Disulfide bond 304 318 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15713484,ECO:0000269|PubMed:7727362;Dbxref=PMID:15713484,PMID:7727362 +P00729 UniProtKB Disulfide bond 328 351 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15713484,ECO:0000269|PubMed:7727362;Dbxref=PMID:15713484,PMID:7727362 +P00729 UniProtKB Disulfide bond 335 344 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15713484,ECO:0000269|PubMed:7727362;Dbxref=PMID:15713484,PMID:7727362 +P00729 UniProtKB Disulfide bond 373 379 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15713484,ECO:0000269|PubMed:7727362;Dbxref=PMID:15713484,PMID:7727362 +P00729 UniProtKB Mutagenesis 508 508 . . . Note=Inactivates enzyme. H->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7904479;Dbxref=PMID:7904479 +P00729 UniProtKB Sequence conflict 260 261 . . . Note=GH->HG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00729 UniProtKB Sequence conflict 389 389 . . . Note=Y->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00729 UniProtKB Sequence conflict 529 529 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00729 UniProtKB Helix 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Beta strand 119 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Beta strand 129 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Turn 135 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Beta strand 139 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Turn 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Beta strand 157 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Turn 164 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 170 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Turn 174 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Beta strand 178 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Turn 184 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Beta strand 187 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 195 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Beta strand 199 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Beta strand 214 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 224 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 242 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YSC +P00729 UniProtKB Turn 245 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Beta strand 251 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 259 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Beta strand 282 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 292 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 296 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 299 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Beta strand 307 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 315 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 341 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 357 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Beta strand 368 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Beta strand 375 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 382 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 393 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Beta strand 403 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +P00729 UniProtKB Helix 411 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Turn 419 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 422 424 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 428 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Beta strand 441 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 454 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 469 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Beta strand 478 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Turn 483 485 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Beta strand 487 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Beta strand 498 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 510 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Helix 515 526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +P00729 UniProtKB Turn 527 529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CPY +##sequence-region P14905 1 389 +P14905 UniProtKB Chain 1 389 . . . ID=PRO_0000089382;Note=Cytochrome B translational activator protein CBS2 +##sequence-region P34730 1 273 +P34730 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P34730 UniProtKB Chain 2 273 . . . ID=PRO_0000058716;Note=Protein BMH2 +P34730 UniProtKB Compositional bias 245 261 . . . Note=Poly-Gln +P34730 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P34730 UniProtKB Sequence conflict 119 119 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P34730 UniProtKB Sequence conflict 174 174 . . . Note=G->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38041 1 980 +P38041 UniProtKB Chain 1 980 . . . ID=PRO_0000064968;Note=Protein BOB1 +P38041 UniProtKB Domain 13 77 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P38041 UniProtKB Domain 228 292 . . . Note=SAM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00184 +P38041 UniProtKB Domain 776 895 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +P38041 UniProtKB Modified residue 104 104 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38041 UniProtKB Modified residue 106 106 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38041 UniProtKB Modified residue 128 128 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38041 UniProtKB Modified residue 151 151 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38041 UniProtKB Modified residue 158 158 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38041 UniProtKB Modified residue 209 209 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198 +P38041 UniProtKB Modified residue 393 393 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38041 UniProtKB Modified residue 412 412 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38041 UniProtKB Modified residue 525 525 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38041 UniProtKB Modified residue 528 528 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38041 UniProtKB Modified residue 589 589 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38041 UniProtKB Modified residue 590 590 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38041 UniProtKB Modified residue 593 593 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38041 UniProtKB Modified residue 644 644 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38041 UniProtKB Modified residue 655 655 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38041 UniProtKB Modified residue 735 735 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38041 UniProtKB Modified residue 919 919 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region P48558 1 297 +P48558 UniProtKB Chain 1 297 . . . ID=PRO_0000203369;Note=Bax inhibitor 1 +P48558 UniProtKB Topological domain 1 53 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48558 UniProtKB Transmembrane 54 74 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48558 UniProtKB Topological domain 75 85 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48558 UniProtKB Transmembrane 86 106 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48558 UniProtKB Topological domain 107 146 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48558 UniProtKB Transmembrane 147 167 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48558 UniProtKB Topological domain 168 171 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48558 UniProtKB Transmembrane 172 192 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48558 UniProtKB Topological domain 193 208 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48558 UniProtKB Transmembrane 209 229 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48558 UniProtKB Topological domain 230 239 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48558 UniProtKB Transmembrane 240 260 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48558 UniProtKB Topological domain 261 270 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48558 UniProtKB Transmembrane 271 291 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48558 UniProtKB Topological domain 292 297 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48558 UniProtKB Sequence conflict 84 84 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53836 1 1060 +P53836 UniProtKB Chain 1 1060 . . . ID=PRO_0000203378;Note=CCR4-NOT transcriptional complex subunit CAF120 +P53836 UniProtKB Domain 75 204 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +P53836 UniProtKB Compositional bias 886 1030 . . . Note=Pro-rich +P53836 UniProtKB Modified residue 491 491 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53836 UniProtKB Modified residue 510 510 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P53836 UniProtKB Modified residue 518 518 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P53836 UniProtKB Modified residue 538 538 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P53836 UniProtKB Modified residue 556 556 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P53836 UniProtKB Modified residue 871 871 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53836 UniProtKB Modified residue 885 885 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P39101 1 391 +P39101 UniProtKB Chain 1 391 . . . ID=PRO_0000071119;Note=Protein CAJ1 +P39101 UniProtKB Domain 4 73 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +P39101 UniProtKB Cross-link 132 132 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P17555 1 526 +P17555 UniProtKB Chain 1 526 . . . ID=PRO_0000205706;Note=Adenylyl cyclase-associated protein +P17555 UniProtKB Domain 369 504 . . . Note=C-CAP/cofactor C-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00659 +P17555 UniProtKB Region 1 168 . . . Note=Adenyl cyclase-binding +P17555 UniProtKB Region 354 361 . . . Note=Interaction with SH3 domain of ABP1 +P17555 UniProtKB Region 370 526 . . . Note=Dimerization and actin-binding +P17555 UniProtKB Motif 169 369 . . . Note=SH3-binding +P17555 UniProtKB Compositional bias 262 300 . . . Note=Ala/Pro/Ser-rich +P17555 UniProtKB Compositional bias 277 282 . . . Note=Poly-Pro +P17555 UniProtKB Modified residue 454 454 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P17555 UniProtKB Beta strand 371 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z +P17555 UniProtKB Beta strand 378 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z +P17555 UniProtKB Beta strand 391 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z +P17555 UniProtKB Beta strand 400 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z +P17555 UniProtKB Beta strand 417 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z +P17555 UniProtKB Beta strand 435 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z +P17555 UniProtKB Beta strand 439 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z +P17555 UniProtKB Beta strand 456 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z +P17555 UniProtKB Beta strand 464 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z +P17555 UniProtKB Turn 473 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z +P17555 UniProtKB Beta strand 478 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z +P17555 UniProtKB Beta strand 485 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z +P17555 UniProtKB Helix 495 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z +P17555 UniProtKB Beta strand 500 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z +P17555 UniProtKB Beta strand 508 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z +P17555 UniProtKB Beta strand 516 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K4Z +##sequence-region P06787 1 147 +P06787 UniProtKB Chain 1 147 . . . ID=PRO_0000198328;Note=Calmodulin +P06787 UniProtKB Domain 8 43 . . . Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P06787 UniProtKB Domain 44 79 . . . Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P06787 UniProtKB Domain 81 116 . . . Note=EF-hand 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P06787 UniProtKB Domain 117 147 . . . Note=EF-hand 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P06787 UniProtKB Calcium binding 21 32 . . . Note=1 +P06787 UniProtKB Calcium binding 57 68 . . . Note=2 +P06787 UniProtKB Calcium binding 94 105 . . . Note=3 +P06787 UniProtKB Modified residue 82 82 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06787 UniProtKB Modified residue 102 102 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P06787 UniProtKB Mutagenesis 21 21 . . . Note=Highly reduced affinity for Ca(2+). D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2044154;Dbxref=PMID:2044154 +P06787 UniProtKB Mutagenesis 32 32 . . . Note=Highly reduced affinity for Ca(2+). E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2044154;Dbxref=PMID:2044154 +P06787 UniProtKB Mutagenesis 57 57 . . . Note=Highly reduced affinity for Ca(2+). D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2044154;Dbxref=PMID:2044154 +P06787 UniProtKB Mutagenesis 68 68 . . . Note=Highly reduced affinity for Ca(2+). E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2044154;Dbxref=PMID:2044154 +P06787 UniProtKB Mutagenesis 94 94 . . . Note=Highly reduced affinity for Ca(2+). D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2044154;Dbxref=PMID:2044154 +P06787 UniProtKB Mutagenesis 105 105 . . . Note=Highly reduced affinity for Ca(2+). E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2044154;Dbxref=PMID:2044154 +P06787 UniProtKB Helix 7 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F54 +P06787 UniProtKB Beta strand 25 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F54 +P06787 UniProtKB Helix 30 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F54 +P06787 UniProtKB Helix 46 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F54 +P06787 UniProtKB Beta strand 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LKJ +P06787 UniProtKB Beta strand 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F54 +P06787 UniProtKB Helix 66 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F54 +P06787 UniProtKB Helix 82 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LKJ +P06787 UniProtKB Beta strand 95 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LKJ +P06787 UniProtKB Beta strand 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LKJ +P06787 UniProtKB Helix 103 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LKJ +P06787 UniProtKB Helix 119 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LKJ +P06787 UniProtKB Beta strand 132 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LKJ +P06787 UniProtKB Helix 138 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LKJ +##sequence-region P27825 1 502 +P27825 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27825 UniProtKB Chain 20 502 . . . ID=PRO_0000004208;Note=Calnexin homolog +P27825 UniProtKB Topological domain 20 481 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27825 UniProtKB Transmembrane 482 502 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27825 UniProtKB Repeat 250 261 . . . Note=1-1 +P27825 UniProtKB Repeat 267 278 . . . Note=1-2 +P27825 UniProtKB Repeat 286 297 . . . Note=1-3 +P27825 UniProtKB Repeat 305 316 . . . Note=1-4 +P27825 UniProtKB Repeat 320 330 . . . Note=2-1 +P27825 UniProtKB Repeat 339 349 . . . Note=2-2 +P27825 UniProtKB Repeat 353 363 . . . Note=2-3 +P27825 UniProtKB Repeat 367 377 . . . Note=2-4 +P27825 UniProtKB Region 248 381 . . . Note=P domain (Extended arm);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P27825 UniProtKB Region 250 316 . . . Note=4 X approximate repeats +P27825 UniProtKB Region 320 377 . . . Note=4 X approximate repeats +P27825 UniProtKB Binding site 131 131 . . . Note=Carbohydrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P27825 UniProtKB Glycosylation 25 25 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27825 UniProtKB Glycosylation 104 104 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27825 UniProtKB Glycosylation 296 296 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27825 UniProtKB Glycosylation 416 416 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27825 UniProtKB Glycosylation 425 425 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27825 UniProtKB Disulfide bond 125 161 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P27825 UniProtKB Disulfide bond 332 338 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P04817 1 590 +P04817 UniProtKB Chain 1 590 . . . ID=PRO_0000054148;Note=Arginine permease CAN1 +P04817 UniProtKB Transmembrane 93 113 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04817 UniProtKB Transmembrane 117 137 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04817 UniProtKB Transmembrane 172 192 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04817 UniProtKB Transmembrane 199 219 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04817 UniProtKB Transmembrane 235 255 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04817 UniProtKB Transmembrane 283 303 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04817 UniProtKB Transmembrane 324 344 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04817 UniProtKB Transmembrane 377 397 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04817 UniProtKB Transmembrane 420 440 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04817 UniProtKB Transmembrane 449 469 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04817 UniProtKB Transmembrane 498 518 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04817 UniProtKB Transmembrane 524 544 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04817 UniProtKB Modified residue 54 54 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32487 +P04817 UniProtKB Modified residue 66 66 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32487 +P04817 UniProtKB Mutagenesis 113 113 . . . Note=In CAN1-343%3B confers citrulline transport activity in GAP1-deleted cells. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604 +P04817 UniProtKB Mutagenesis 148 148 . . . Note=In CAN1-337%3B confers citrulline transport activity in GAP1-deleted cells and leads to sensitivity to L-glutamic acid alpha-hydroxamate%2C alpha-aminoisobutyrate%2C 3-chloro-L-alanine%2C L-ethionine%2C L-allylglycine%2C and D-histidine%2C but not sensitivity to L-aspartic acid alpha-hydroxamate or p-fluoro-L-phenylalanine. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604 +P04817 UniProtKB Mutagenesis 149 149 . . . Note=In CAN1-315%3B confers citrulline transport activity in GAP1-deleted cells. V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604 +P04817 UniProtKB Mutagenesis 152 152 . . . Note=In CAN1-342%3B confers citrulline transport activity in GAP1-deleted cells. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604 +P04817 UniProtKB Mutagenesis 173 173 . . . Note=In CAN1-306%3B confers citrulline transport activity in GAP1-deleted cells. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604 +P04817 UniProtKB Mutagenesis 173 173 . . . Note=In CAN1-327%3B confers citrulline transport activity in GAP1-deleted cells. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604 +P04817 UniProtKB Mutagenesis 308 308 . . . Note=In CAN1-341%3B confers citrulline transport activity in GAP1-deleted cells. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604 +P04817 UniProtKB Mutagenesis 313 313 . . . Note=In CAN1-329%3B confers citrulline transport activity in GAP1-deleted cells and leads to sensitivity to L-glutamic acid alpha-hydroxamate%2C alpha-aminoisobutyrate%2C 3-chloro-L-alanine%2C L-ethionine%2C L-allylglycine%2C and D-histidine%2C L-aspartic acid alpha-hydroxamate and p-fluoro-L-phenylalanine. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604 +P04817 UniProtKB Mutagenesis 354 355 . . . Note=In CAN1-318%3B confers citrulline transport activity in GAP1-deleted cells. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604 +P04817 UniProtKB Mutagenesis 356 356 . . . Note=In CAN1-340%3B confers citrulline transport activity in GAP1-deleted cells. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604 +P04817 UniProtKB Mutagenesis 356 356 . . . Note=In CAN1-339%3B confers citrulline transport activity in GAP1-deleted cells. Y->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604 +P04817 UniProtKB Mutagenesis 451 451 . . . Note=In CAN1-328%3B confers citrulline transport activity in GAP1-deleted cells. W->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604 +P04817 UniProtKB Mutagenesis 451 451 . . . Note=In CAN1-316%3B confers citrulline transport activity in GAP1-deleted cells. W->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604 +P04817 UniProtKB Mutagenesis 451 451 . . . Note=In CAN1-335%3B confers citrulline transport activity in GAP1-deleted cells. W->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604 +P04817 UniProtKB Mutagenesis 461 461 . . . Note=In CAN1-307%3B confers citrulline transport activity in GAP1-deleted cells. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11746604;Dbxref=PMID:11746604 +P04817 UniProtKB Sequence conflict 534 534 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P28495 1 268 +P28495 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P28495 UniProtKB Chain 2 268 . . . ID=PRO_0000208646;Note=F-actin-capping protein subunit alpha +P28495 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P28495 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P34237 1 679 +P34237 UniProtKB Chain 1 679 . . . ID=PRO_0000071795;Note=Protein CASP +P34237 UniProtKB Topological domain 1 614 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34237 UniProtKB Transmembrane 615 635 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34237 UniProtKB Topological domain 636 679 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34237 UniProtKB Coiled coil 14 90 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34237 UniProtKB Coiled coil 178 341 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34237 UniProtKB Coiled coil 385 444 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34237 UniProtKB Coiled coil 492 540 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34237 UniProtKB Modified residue 364 364 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198 +P34237 UniProtKB Modified residue 450 450 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P34237 UniProtKB Modified residue 453 453 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34237 UniProtKB Modified residue 555 555 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34237 UniProtKB Mutagenesis 619 619 . . . Note=Retained in the endoplasmic reticulum. Y->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12429822;Dbxref=PMID:12429822 +P34237 UniProtKB Mutagenesis 624 624 . . . Note=No effect on subcellular location. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12429822;Dbxref=PMID:12429822 +##sequence-region P15202 1 515 +P15202 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P15202 UniProtKB Chain 2 515 . . . ID=PRO_0000084928;Note=Peroxisomal catalase A +P15202 UniProtKB Motif 513 515 . . . Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15202 UniProtKB Active site 70 70 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9931255;Dbxref=PMID:9931255 +P15202 UniProtKB Active site 143 143 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9931255;Dbxref=PMID:9931255 +P15202 UniProtKB Metal binding 355 355 . . . Note=Iron (heme axial ligand);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9931255;Dbxref=PMID:9931255 +P15202 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P15202 UniProtKB Sequence conflict 131 131 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15202 UniProtKB Beta strand 31 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Beta strand 36 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Turn 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 50 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Beta strand 72 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Turn 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Beta strand 101 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Beta strand 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Beta strand 119 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Beta strand 126 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Beta strand 136 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 155 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Turn 167 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 174 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 184 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 190 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Beta strand 202 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 206 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Beta strand 217 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Beta strand 226 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 244 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 257 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Beta strand 273 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 283 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Beta strand 289 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Turn 302 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Beta strand 308 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 322 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Turn 326 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Beta strand 340 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 346 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 367 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 371 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Turn 395 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Beta strand 425 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Beta strand 429 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Beta strand 438 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 441 454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 459 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 476 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +P15202 UniProtKB Helix 491 501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A4E +##sequence-region P53630 1 237 +P53630 UniProtKB Chain 1 237 . . . ID=PRO_0000188006;Note=Dethiobiotin synthetase +P53630 UniProtKB Nucleotide binding 18 26 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q06071 1 122 +Q06071 UniProtKB Chain 1 122 . . . ID=PRO_0000247218;Note=Biogenesis of lysosome-related organelles complex 1 subunit BLS1 +Q06071 UniProtKB Modified residue 33 33 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q01532 1 483 +Q01532 UniProtKB Transit peptide 1 30 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01532 UniProtKB Chain 31 482 . . . ID=PRO_0000050554;Note=Cysteine proteinase 1%2C mitochondrial +Q01532 UniProtKB Propeptide 483 483 . . . ID=PRO_0000292865;Note=Removed in mature form%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7638617;Dbxref=PMID:7638617 +Q01532 UniProtKB Active site 102 102 . . . . +Q01532 UniProtKB Active site 398 398 . . . . +Q01532 UniProtKB Active site 421 421 . . . . +Q01532 UniProtKB Alternative sequence 1 29 . . . ID=VSP_026453;Note=In isoform Cytoplasmic. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01532 UniProtKB Mutagenesis 102 102 . . . Note=Abolishes peptidase activity%2C which also hinders autocatalytic processing of the enzyme to the mature form. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9374524;Dbxref=PMID:9374524 +Q01532 UniProtKB Mutagenesis 271 274 . . . Note=In GAL6DB%3B disrupts nucleic acid-binding activity%2C but retains normal peptidase activity. KDKK->ADAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9374524;Dbxref=PMID:9374524 +Q01532 UniProtKB Mutagenesis 398 398 . . . Note=Abolishes Hcy-thiolactonase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16769724;Dbxref=PMID:16769724 +Q01532 UniProtKB Mutagenesis 479 479 . . . Note=Results in the abnormal cleavage of 3 C-terminal residues instead of only 1 during autocatalytic processing. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9546396;Dbxref=PMID:9546396 +Q01532 UniProtKB Sequence conflict 187 187 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01532 UniProtKB Helix 36 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Helix 50 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Helix 64 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Helix 71 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Beta strand 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Beta strand 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GCB +Q01532 UniProtKB Helix 102 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Helix 128 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Turn 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Helix 158 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Helix 174 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Helix 189 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Helix 197 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Helix 203 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Beta strand 229 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A6R +Q01532 UniProtKB Helix 232 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Beta strand 264 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Beta strand 275 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Helix 282 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Beta strand 296 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Beta strand 311 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Beta strand 326 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Helix 333 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Beta strand 350 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Turn 356 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Turn 362 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Helix 374 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Helix 385 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Beta strand 398 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Turn 409 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Beta strand 414 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Turn 425 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E03 +Q01532 UniProtKB Beta strand 432 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Helix 437 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Beta strand 444 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Helix 451 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Helix 456 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Beta strand 470 472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E01 +Q01532 UniProtKB Helix 477 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A6R +##sequence-region P29311 1 267 +P29311 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P29311 UniProtKB Chain 2 267 . . . ID=PRO_0000058715;Note=Protein BMH1 +P29311 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P29311 UniProtKB Modified residue 89 89 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P29311 UniProtKB Cross-link 76 76 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P29311 UniProtKB Sequence conflict 197 197 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29311 UniProtKB Sequence conflict 197 197 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29311 UniProtKB Sequence conflict 263 267 . . . Note=GEAPK->VKHQSKYSDKSKEKLLKKRKKKERGCNNL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P48445 1 690 +P48445 UniProtKB Chain 1 690 . . . ID=PRO_0000064981;Note=Biotin--protein ligase +P48445 UniProtKB Domain 378 606 . . . Note=BPL/LPL catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01067 +##sequence-region P48582 1 844 +P48582 UniProtKB Chain 1 844 . . . ID=PRO_0000218872;Note=Vacuolar-sorting protein BRO1 +P48582 UniProtKB Domain 4 400 . . . Note=BRO1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00526 +P48582 UniProtKB Coiled coil 547 583 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48582 UniProtKB Modified residue 740 740 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P48582 UniProtKB Sequence conflict 359 359 . . . Note=C->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P48582 UniProtKB Helix 18 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Turn 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Helix 35 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Helix 41 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Helix 60 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Helix 82 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Beta strand 92 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Beta strand 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Beta strand 107 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Helix 113 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Turn 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Beta strand 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Helix 141 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Helix 167 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Helix 171 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Helix 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Helix 203 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Turn 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Beta strand 233 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Helix 239 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Helix 270 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Helix 286 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Turn 290 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Helix 298 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Beta strand 318 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Helix 330 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +P48582 UniProtKB Helix 344 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZB1 +##sequence-region P32639 1 2163 +P32639 UniProtKB Chain 1 2163 . . . ID=PRO_0000102086;Note=Pre-mRNA-splicing helicase BRR2 +P32639 UniProtKB Domain 508 692 . . . Note=Helicase ATP-binding 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P32639 UniProtKB Domain 718 921 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P32639 UniProtKB Domain 998 1308 . . . Note=SEC63 1 +P32639 UniProtKB Domain 1357 1533 . . . Note=Helicase ATP-binding 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P32639 UniProtKB Domain 1846 2160 . . . Note=SEC63 2 +P32639 UniProtKB Nucleotide binding 521 528 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P32639 UniProtKB Nucleotide binding 1370 1377 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P32639 UniProtKB Motif 634 637 . . . Note=DEIH box +P32639 UniProtKB Motif 1474 1477 . . . Note=DDAH box +P32639 UniProtKB Compositional bias 1570 1575 . . . Note=Poly-Ala +P32639 UniProtKB Modified residue 403 403 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32639 UniProtKB Mutagenesis 858 858 . . . Note=Reduces spliceosomal pre-mRNA splicing. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23124065;Dbxref=PMID:23124065 +P32639 UniProtKB Mutagenesis 938 938 . . . Note=Strongly reduced unwinding of U4/U6 snRNA. W->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19716790;Dbxref=PMID:19716790 +P32639 UniProtKB Mutagenesis 1107 1107 . . . Note=Reduced ATP-dependent RNA helicase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19525970;Dbxref=PMID:19525970 +P32639 UniProtKB Mutagenesis 1110 1110 . . . Note=Abolishes unwinding of U4/U6 snRNA. R->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19716790;Dbxref=PMID:19716790 +P32639 UniProtKB Helix 114 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 133 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 137 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Turn 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 164 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 176 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 263 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 267 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M52 +P32639 UniProtKB Turn 285 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 292 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 306 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Turn 320 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 330 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 340 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M52 +P32639 UniProtKB Turn 344 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 347 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 353 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Turn 362 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 370 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Turn 378 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Turn 382 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 388 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 429 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 453 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 458 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 480 482 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 485 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Turn 493 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 501 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 517 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 523 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BGD +P32639 UniProtKB Helix 527 540 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 545 550 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 556 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 564 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Turn 579 582 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 585 587 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 591 593 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 596 601 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 603 607 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 609 617 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 619 621 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 622 625 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 628 633 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 636 640 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 644 656 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 659 662 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 666 673 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 677 683 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 688 690 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 691 693 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 696 698 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 699 701 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BGD +P32639 UniProtKB Beta strand 703 710 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 715 735 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 740 743 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 747 762 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Turn 767 770 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 776 785 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 791 798 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 801 804 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 806 808 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BGD +P32639 UniProtKB Helix 810 821 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 826 830 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 833 836 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 842 848 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 851 854 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 855 857 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 859 862 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 865 873 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 874 876 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BGD +P32639 UniProtKB Turn 878 880 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 882 891 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 892 894 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 895 901 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Turn 902 904 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 912 915 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 916 925 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 932 939 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 943 950 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Turn 952 956 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 960 963 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Turn 964 966 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 967 983 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 986 990 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Turn 991 994 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 995 999 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1000 1008 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1012 1021 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1028 1036 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1039 1041 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Turn 1048 1050 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1051 1059 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1069 1071 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BGD +P32639 UniProtKB Helix 1072 1084 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1092 1119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1122 1137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1141 1143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BGD +P32639 UniProtKB Helix 1145 1148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1154 1163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1168 1171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1178 1182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Turn 1186 1190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1191 1196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1202 1224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1230 1233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1237 1244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1246 1248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1250 1259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1261 1263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1266 1275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1278 1282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1286 1297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1301 1307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1331 1333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1337 1340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1344 1347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M52 +P32639 UniProtKB Helix 1350 1354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1356 1360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1366 1369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1372 1375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M52 +P32639 UniProtKB Helix 1376 1389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1395 1398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1402 1416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Turn 1417 1421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1424 1426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1432 1441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1443 1447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1449 1455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1456 1461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1463 1466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1470 1474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1476 1480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1482 1502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1507 1513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1519 1525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1529 1531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1532 1534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1537 1539 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BGD +P32639 UniProtKB Beta strand 1544 1553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1555 1558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M52 +P32639 UniProtKB Helix 1561 1576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1581 1587 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1588 1603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Turn 1604 1606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1614 1622 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1627 1629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1630 1634 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1637 1640 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1642 1644 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1646 1657 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1660 1667 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1668 1670 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1671 1673 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1677 1683 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1686 1689 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Turn 1690 1693 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1694 1697 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1700 1707 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1714 1716 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1718 1725 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1726 1737 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1746 1749 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1750 1759 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1766 1773 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1777 1782 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1786 1789 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Helix 1796 1816 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1819 1823 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1843 1846 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1847 1849 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Helix 1860 1869 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Helix 1876 1884 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Helix 1887 1891 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Helix 1898 1906 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Beta strand 1909 1911 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Beta strand 1915 1917 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P32639 UniProtKB Beta strand 1919 1921 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Helix 1922 1935 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Helix 1941 1967 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Helix 1973 1985 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Beta strand 1989 1991 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BGD +P32639 UniProtKB Helix 1993 1996 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Helix 2002 2010 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Helix 2016 2021 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Helix 2024 2030 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Helix 2035 2047 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Beta strand 2051 2057 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Helix 2060 2062 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Beta strand 2067 2079 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Beta strand 2099 2105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Helix 2106 2108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Beta strand 2110 2117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Beta strand 2121 2131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Beta strand 2135 2148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +P32639 UniProtKB Beta strand 2154 2163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IM1 +##sequence-region O13558 1 102 +O13558 UniProtKB Chain 1 102 . . . ID=PRO_0000299769;Note=Putative uncharacterized protein BSC3 +##sequence-region Q07992 1 125 +Q07992 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07992 UniProtKB Chain 20 125 . . . ID=PRO_0000299772;Note=Putative uncharacterized protein BUD28 +##sequence-region Q12064 1 193 +Q12064 UniProtKB Signal peptide 1 14 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12064 UniProtKB Chain 15 193 . . . ID=PRO_0000299773;Note=Putative uncharacterized protein BUD30 +Q12064 UniProtKB Compositional bias 2 58 . . . Note=Ser-rich +##sequence-region P25558 1 1636 +P25558 UniProtKB Chain 1 1636 . . . ID=PRO_0000065016;Note=Bud site selection protein 3 +P25558 UniProtKB Modified residue 766 766 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25558 UniProtKB Modified residue 1045 1045 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25558 UniProtKB Modified residue 1063 1063 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P25558 UniProtKB Modified residue 1075 1075 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P25558 UniProtKB Modified residue 1134 1134 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P25558 UniProtKB Modified residue 1149 1149 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25558 UniProtKB Modified residue 1157 1157 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P25558 UniProtKB Modified residue 1160 1160 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P25558 UniProtKB Modified residue 1228 1228 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25558 UniProtKB Modified residue 1254 1254 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P25558 UniProtKB Modified residue 1257 1257 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P25558 UniProtKB Modified residue 1390 1390 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25558 UniProtKB Modified residue 1412 1412 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P25558 UniProtKB Modified residue 1429 1429 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25558 UniProtKB Modified residue 1440 1440 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P25558 UniProtKB Modified residue 1443 1443 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P25558 UniProtKB Modified residue 1501 1501 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25558 UniProtKB Modified residue 1549 1549 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25558 UniProtKB Modified residue 1589 1589 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25558 UniProtKB Modified residue 1614 1614 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P25558 UniProtKB Cross-link 792 792 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25558 UniProtKB Cross-link 963 963 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q12191 1 341 +Q12191 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12191 UniProtKB Chain 2 341 . . . ID=PRO_0000270973;Note=Binder of USO1 and GRH1 protein 1 +Q12191 UniProtKB Coiled coil 2 41 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12191 UniProtKB Coiled coil 188 272 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12191 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12191 UniProtKB Modified residue 87 87 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12191 UniProtKB Modified residue 170 170 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12191 UniProtKB Modified residue 292 292 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q03758 1 920 +Q03758 UniProtKB Chain 1 920 . . . ID=PRO_0000203241;Note=Ubiquitin ligase-binding protein BUL2 +Q03758 UniProtKB Motif 129 133 . . . Note=PY-motif +Q03758 UniProtKB Modified residue 22 22 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03758 UniProtKB Modified residue 557 557 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region P12962 1 161 +P12962 UniProtKB Chain 1 161 . . . ID=PRO_0000084163;Note=Cap-associated protein CAF20 +P12962 UniProtKB Modified residue 78 78 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P12962 UniProtKB Modified residue 91 91 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P12962 UniProtKB Modified residue 99 99 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P12962 UniProtKB Modified residue 101 101 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P12962 UniProtKB Modified residue 102 102 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P12962 UniProtKB Modified residue 154 154 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P12962 UniProtKB Mutagenesis 4 4 . . . Note=Reduces interaction with eIF4E/TIF45. Prevents pseudohyphal growth. Further reduces interaction with eIF4E/TIF45%3B when associated with A-9. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17083129;Dbxref=PMID:17083129 +P12962 UniProtKB Mutagenesis 9 9 . . . Note=Further reduces interaction with eIF4E/TIF45%3B when associated with A-4. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17083129;Dbxref=PMID:17083129 +##sequence-region P03965 1 1118 +P03965 UniProtKB Chain 1 1118 . . . ID=PRO_0000145091;Note=Carbamoyl-phosphate synthase arginine-specific large chain +P03965 UniProtKB Domain 154 346 . . . Note=ATP-grasp 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 +P03965 UniProtKB Domain 698 890 . . . Note=ATP-grasp 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 +P03965 UniProtKB Nucleotide binding 174 229 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 +P03965 UniProtKB Nucleotide binding 321 371 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 +P03965 UniProtKB Metal binding 303 303 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P03965 UniProtKB Metal binding 317 317 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P03965 UniProtKB Metal binding 317 317 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P03965 UniProtKB Metal binding 319 319 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P03965 UniProtKB Metal binding 848 848 . . . Note=Manganese 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P03965 UniProtKB Metal binding 861 861 . . . Note=Manganese 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38278 1 337 +P38278 UniProtKB Chain 1 337 . . . ID=PRO_0000202494;Note=25S rRNA (adenine(2142)-N(1))-methyltransferase +P38278 UniProtKB Mutagenesis 180 180 . . . Note=Abolishes methyltransferase activity. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23558746;Dbxref=PMID:23558746 +P38278 UniProtKB Sequence conflict 312 312 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38278 UniProtKB Sequence conflict 312 312 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12291 1 365 +Q12291 UniProtKB Chain 1 365 . . . ID=PRO_0000247230;Note=25S rRNA (uridine(2843)-N(3))-methyltransferase +Q12291 UniProtKB Mutagenesis 294 294 . . . Note=Abolishes methyltransferase activity. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24335083;Dbxref=PMID:24335083 +##sequence-region P53890 1 448 +P53890 UniProtKB Chain 1 448 . . . ID=PRO_0000203411;Note=Bud neck protein 5 +P53890 UniProtKB Modified residue 70 70 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53890 UniProtKB Modified residue 179 179 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P53890 UniProtKB Modified residue 194 194 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53890 UniProtKB Modified residue 257 257 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53890 UniProtKB Modified residue 270 270 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53890 UniProtKB Modified residue 273 273 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53890 UniProtKB Modified residue 274 274 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53890 UniProtKB Modified residue 332 332 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53890 UniProtKB Modified residue 340 340 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53890 UniProtKB Modified residue 344 344 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P53890 UniProtKB Modified residue 346 346 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53890 UniProtKB Modified residue 350 350 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P39969 1 1040 +P39969 UniProtKB Chain 1 1040 . . . ID=PRO_0000064970;Note=Protein BOI2 +P39969 UniProtKB Domain 43 107 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P39969 UniProtKB Domain 266 330 . . . Note=SAM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00184 +P39969 UniProtKB Domain 768 887 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +P39969 UniProtKB Modified residue 18 18 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P39969 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39969 UniProtKB Modified residue 28 28 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P39969 UniProtKB Modified residue 450 450 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P39969 UniProtKB Modified residue 519 519 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P39969 UniProtKB Modified residue 523 523 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P39969 UniProtKB Modified residue 546 546 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P39969 UniProtKB Modified residue 652 652 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P39969 UniProtKB Sequence conflict 733 733 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P43132 1 505 +P43132 UniProtKB Chain 1 505 . . . ID=PRO_0000064987;Note=COMPASS component BRE2 +P43132 UniProtKB Modified residue 227 227 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P43132 UniProtKB Helix 483 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RT4 +##sequence-region P53841 1 131 +P53841 UniProtKB Chain 1 131 . . . ID=PRO_0000064994;Note=Bypass of stop codon protein 4 +P53841 UniProtKB Natural variant 3 3 . . . Note=In strain: XH1549. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18493065;Dbxref=PMID:18493065 +P53841 UniProtKB Natural variant 6 6 . . . Note=In strain: AS2.101%2C AS2.1406%2C AS2.179%2C AS2.7%2C AS2.724%2C AS2.771%2C AS2.820 and AS2.93. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18493065;Dbxref=PMID:18493065 +P53841 UniProtKB Natural variant 9 10 . . . Note=In strain: XH1549. NK->T +P53841 UniProtKB Natural variant 16 16 . . . Note=In strain: XH1549. I->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18493065;Dbxref=PMID:18493065 +P53841 UniProtKB Natural variant 19 19 . . . Note=In strain: XH1549. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18493065;Dbxref=PMID:18493065 +P53841 UniProtKB Natural variant 22 22 . . . Note=In strain: XH1549. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18493065;Dbxref=PMID:18493065 +P53841 UniProtKB Natural variant 32 32 . . . Note=In strain: XH1549. V->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18493065;Dbxref=PMID:18493065 +P53841 UniProtKB Natural variant 42 42 . . . Note=In strain: AS2.101%2C AS2.1406%2C AS2.179%2C AS2.7%2C AS2.724%2C AS2.771%2C AS2.820%2C AS2.93 and XH1549. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18493065;Dbxref=PMID:18493065 +P53841 UniProtKB Natural variant 92 92 . . . Note=In strain: AS2.724 and AS2.820. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18493065;Dbxref=PMID:18493065 +##sequence-region P38356 1 321 +P38356 UniProtKB Chain 1 321 . . . ID=PRO_0000064996;Note=Metal homeostatis protein BSD2 +P38356 UniProtKB Topological domain 1 178 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38356 UniProtKB Transmembrane 179 199 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38356 UniProtKB Topological domain 200 211 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38356 UniProtKB Transmembrane 212 232 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38356 UniProtKB Topological domain 233 280 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38356 UniProtKB Transmembrane 281 301 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38356 UniProtKB Topological domain 302 321 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38356 UniProtKB Cross-link 312 312 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38356 UniProtKB Mutagenesis 149 149 . . . Note=Reverses the aerobic defects of yeast strains lacking superoxide dismutase (SOD). Associated with elevated copper ion accumulation and increased sensitivity to the toxic effects of copper and cadmium. Exhibits no additional sensitivity to manganese. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7935419;Dbxref=PMID:7935419 +##sequence-region O94143 1 102 +O94143 UniProtKB Chain 1 102 . . . ID=PRO_0000299770;Note=Putative uncharacterized protein BUD19 +##sequence-region Q08004 1 166 +Q08004 UniProtKB Chain 1 166 . . . ID=PRO_0000046803;Note=Bud site selection protein 20 +Q08004 UniProtKB Zinc finger 49 73 . . . Note=C2H2-type +##sequence-region Q03783 1 95 +Q03783 UniProtKB Chain 1 95 . . . ID=PRO_0000299771;Note=Putative uncharacterized protein BUD26 +Q03783 UniProtKB Transmembrane 21 43 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03783 UniProtKB Transmembrane 68 87 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43573 1 796 +P43573 UniProtKB Chain 1 796 . . . ID=PRO_0000153693;Note=Bud site selection protein 27 +P43573 UniProtKB Coiled coil 81 121 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43573 UniProtKB Modified residue 580 580 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P53323 1 261 +P53323 UniProtKB Chain 1 261 . . . ID=PRO_0000088189;Note=EKC/KEOPS complex subunit BUD32 +P53323 UniProtKB Domain 16 261 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53323 UniProtKB Nucleotide binding 22 30 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53323 UniProtKB Active site 161 161 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10028 +P53323 UniProtKB Binding site 43 43 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53323 UniProtKB Modified residue 187 187 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12023889;Dbxref=PMID:12023889 +P53323 UniProtKB Modified residue 189 189 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12023889;Dbxref=PMID:12023889 +P53323 UniProtKB Mutagenesis 187 187 . . . Note=Reduced kinase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12023889;Dbxref=PMID:12023889 +P53323 UniProtKB Mutagenesis 189 189 . . . Note=Reduced kinase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12023889;Dbxref=PMID:12023889 +P53323 UniProtKB Helix 5 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +P53323 UniProtKB Beta strand 20 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +P53323 UniProtKB Beta strand 29 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +P53323 UniProtKB Beta strand 37 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +P53323 UniProtKB Beta strand 49 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +P53323 UniProtKB Helix 73 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +P53323 UniProtKB Beta strand 94 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +P53323 UniProtKB Turn 99 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +P53323 UniProtKB Beta strand 103 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +P53323 UniProtKB Helix 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +P53323 UniProtKB Beta strand 118 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWA +P53323 UniProtKB Helix 122 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +P53323 UniProtKB Helix 136 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +P53323 UniProtKB Beta strand 166 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +P53323 UniProtKB Beta strand 175 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +P53323 UniProtKB Helix 192 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +P53323 UniProtKB Helix 214 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +P53323 UniProtKB Helix 233 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +##sequence-region P41698 1 603 +P41698 UniProtKB Chain 1 603 . . . ID=PRO_0000065020;Note=Bud site selection protein 8 +P41698 UniProtKB Topological domain 1 515 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41698 UniProtKB Transmembrane 516 536 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41698 UniProtKB Topological domain 537 577 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41698 UniProtKB Transmembrane 578 598 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41698 UniProtKB Topological domain 599 603 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41698 UniProtKB Compositional bias 84 95 . . . Note=Poly-Ser +P41698 UniProtKB Glycosylation 92 92 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41698 UniProtKB Glycosylation 110 110 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41698 UniProtKB Glycosylation 211 211 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41698 UniProtKB Glycosylation 240 240 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41698 UniProtKB Glycosylation 271 271 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41698 UniProtKB Glycosylation 333 333 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41698 UniProtKB Glycosylation 396 396 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41698 UniProtKB Glycosylation 423 423 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41698 UniProtKB Sequence conflict 140 140 . . . Note=R->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41698 UniProtKB Sequence conflict 145 145 . . . Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41698 UniProtKB Sequence conflict 221 221 . . . Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41698 UniProtKB Sequence conflict 350 350 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41698 UniProtKB Sequence conflict 354 354 . . . Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41698 UniProtKB Sequence conflict 422 422 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41698 UniProtKB Sequence conflict 602 602 . . . Note=R->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53226 1 547 +P53226 UniProtKB Chain 1 547 . . . ID=PRO_0000065021;Note=Bud site selection protein 9 +P53226 UniProtKB Topological domain 1 460 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53226 UniProtKB Transmembrane 461 481 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53226 UniProtKB Topological domain 482 521 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53226 UniProtKB Transmembrane 522 542 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53226 UniProtKB Topological domain 543 547 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53226 UniProtKB Modified residue 112 112 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53226 UniProtKB Modified residue 189 189 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53226 UniProtKB Glycosylation 83 83 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53226 UniProtKB Glycosylation 139 139 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53226 UniProtKB Glycosylation 142 142 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53226 UniProtKB Glycosylation 221 221 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53226 UniProtKB Glycosylation 259 259 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53226 UniProtKB Glycosylation 263 263 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53226 UniProtKB Glycosylation 289 289 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53226 UniProtKB Glycosylation 299 299 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53226 UniProtKB Glycosylation 340 340 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53226 UniProtKB Sequence conflict 16 16 . . . Note=K->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53226 UniProtKB Sequence conflict 27 27 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53226 UniProtKB Sequence conflict 132 132 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53226 UniProtKB Sequence conflict 249 249 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53226 UniProtKB Sequence conflict 260 260 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53226 UniProtKB Sequence conflict 298 298 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53226 UniProtKB Sequence conflict 321 321 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53226 UniProtKB Sequence conflict 345 345 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53226 UniProtKB Sequence conflict 406 406 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53226 UniProtKB Sequence conflict 451 451 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53226 UniProtKB Sequence conflict 480 480 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53226 UniProtKB Sequence conflict 545 545 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P48524 1 976 +P48524 UniProtKB Chain 1 976 . . . ID=PRO_0000065022;Note=Ubiquitin ligase-binding protein BUL1 +P48524 UniProtKB Motif 156 160 . . . Note=PY-motif +P48524 UniProtKB Compositional bias 631 640 . . . Note=Poly-Ser +P48524 UniProtKB Compositional bias 868 876 . . . Note=Poly-Ser +P48524 UniProtKB Modified residue 58 58 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P48524 UniProtKB Modified residue 70 70 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P48524 UniProtKB Mutagenesis 157 157 . . . Note=Abolishes interaction with RSP5 and reduces HSE-mediated gene expression%3B when associated with A-158. P->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12821147,ECO:0000269|PubMed:9931424;Dbxref=PMID:12821147,PMID:9931424 +P48524 UniProtKB Mutagenesis 158 158 . . . Note=Abolishes interaction with RSP5 and reduces HSE-mediated gene expression%3B when associated with Q-157. P->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12821147,ECO:0000269|PubMed:9931424;Dbxref=PMID:12821147,PMID:9931424 +P48524 UniProtKB Sequence conflict 35 35 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P48524 UniProtKB Sequence conflict 773 775 . . . Note=YDD->ISN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P48524 UniProtKB Sequence conflict 963 963 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P07245 1 946 +P07245 UniProtKB Chain 1 946 . . . ID=PRO_0000199326;Note=C-1-tetrahydrofolate synthase%2C cytoplasmic +P07245 UniProtKB Nucleotide binding 169 171 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07245 UniProtKB Nucleotide binding 384 391 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07245 UniProtKB Region 1 319 . . . Note=Methylenetetrahydrofolate dehydrogenase and cyclohydrolase +P07245 UniProtKB Region 51 55 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07245 UniProtKB Region 98 100 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07245 UniProtKB Region 277 281 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07245 UniProtKB Region 320 946 . . . Note=Formyltetrahydrofolate synthetase +P07245 UniProtKB Binding site 194 194 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07245 UniProtKB Modified residue 176 176 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P07245 UniProtKB Modified residue 318 318 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07245 UniProtKB Modified residue 322 322 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07245 UniProtKB Mutagenesis 11 11 . . . Note=Almost no effect on activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2541774;Dbxref=PMID:2541774 +P07245 UniProtKB Mutagenesis 144 144 . . . Note=Cyclohydrolase activity is reduced 20-fold. Dehydrogenase Km is increased 7-fold. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2541774;Dbxref=PMID:2541774 +P07245 UniProtKB Mutagenesis 257 257 . . . Note=Cyclohydrolase activity is increased 2-fold. Dehydrogenase Km is increased 2-fold. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2541774;Dbxref=PMID:2541774 +##sequence-region P36076 1 571 +P36076 UniProtKB Chain 1 571 . . . ID=PRO_0000182039;Note=Coenzyme A biosynthesis protein 3 +P36076 UniProtKB Compositional bias 508 570 . . . Note=Asp/Glu-rich (highly acidic) +P36076 UniProtKB Modified residue 42 42 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956 +P36076 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P36076 UniProtKB Modified residue 121 121 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P36076 UniProtKB Modified residue 124 124 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P36076 UniProtKB Modified residue 264 264 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36076 UniProtKB Mutagenesis 478 478 . . . Note=Abolishes PPCDC activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19915539;Dbxref=PMID:19915539 +##sequence-region Q03941 1 241 +Q03941 UniProtKB Chain 1 241 . . . ID=PRO_0000173043;Note=Dephospho-CoA kinase CAB5 +Q03941 UniProtKB Domain 3 211 . . . Note=DPCK +Q03941 UniProtKB Nucleotide binding 8 15 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P13517 1 287 +P13517 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P13517 UniProtKB Chain 2 287 . . . ID=PRO_0000204642;Note=F-actin-capping protein subunit beta +P13517 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P13517 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P13517 UniProtKB Modified residue 92 92 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13517 UniProtKB Sequence conflict 140 140 . . . Note=F->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13517 UniProtKB Sequence conflict 146 147 . . . Note=FK->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P07258 1 411 +P07258 UniProtKB Chain 1 411 . . . ID=PRO_0000112372;Note=Carbamoyl-phosphate synthase arginine-specific small chain +P07258 UniProtKB Domain 185 376 . . . Note=Glutamine amidotransferase type-1 +P07258 UniProtKB Active site 264 264 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07258 UniProtKB Active site 349 349 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07258 UniProtKB Active site 351 351 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38995 1 1004 +P38995 UniProtKB Chain 1 1004 . . . ID=PRO_0000046318;Note=Copper-transporting ATPase +P38995 UniProtKB Topological domain 1 262 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Transmembrane 263 283 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Topological domain 284 303 . . . Note=Lumenal%2C vesicle;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Transmembrane 304 324 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Topological domain 325 335 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Transmembrane 336 356 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Topological domain 357 370 . . . Note=Lumenal%2C vesicle;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Transmembrane 371 391 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Topological domain 392 528 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Transmembrane 529 549 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Topological domain 550 577 . . . Note=Lumenal%2C vesicle;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Transmembrane 578 598 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Topological domain 599 901 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Transmembrane 902 924 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Topological domain 925 927 . . . Note=Lumenal%2C vesicle;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Transmembrane 928 950 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Topological domain 951 1004 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38995 UniProtKB Domain 3 68 . . . Note=HMA 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P38995 UniProtKB Domain 81 147 . . . Note=HMA 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P38995 UniProtKB Active site 627 627 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38995 UniProtKB Metal binding 13 13 . . . Note=Copper +P38995 UniProtKB Metal binding 16 16 . . . Note=Copper +P38995 UniProtKB Metal binding 91 91 . . . Note=Copper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P38995 UniProtKB Metal binding 94 94 . . . Note=Copper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P38995 UniProtKB Metal binding 838 838 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P38995 UniProtKB Metal binding 842 842 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P38995 UniProtKB Beta strand 2 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ +P38995 UniProtKB Helix 14 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ +P38995 UniProtKB Beta strand 27 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ +P38995 UniProtKB Turn 37 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ +P38995 UniProtKB Beta strand 41 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ +P38995 UniProtKB Beta strand 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVS +P38995 UniProtKB Helix 52 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ +P38995 UniProtKB Beta strand 66 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FVQ +##sequence-region Q02948 1 557 +Q02948 UniProtKB Chain 1 557 . . . ID=PRO_0000218559;Note=Vacuolar protein sorting-associated protein 30 +Q02948 UniProtKB Region 320 539 . . . Note=BARA +Q02948 UniProtKB Region 515 540 . . . Note=Required for membrane-association%2C autophagic function during starvation and normal autophagosome morphology;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23878393;Dbxref=PMID:23878393 +Q02948 UniProtKB Coiled coil 189 322 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02948 UniProtKB Modified residue 142 142 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q02948 UniProtKB Turn 322 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7 +Q02948 UniProtKB Beta strand 329 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7 +Q02948 UniProtKB Beta strand 335 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7 +Q02948 UniProtKB Beta strand 341 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7 +Q02948 UniProtKB Helix 353 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7 +Q02948 UniProtKB Beta strand 379 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7 +Q02948 UniProtKB Helix 387 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7 +Q02948 UniProtKB Beta strand 391 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7 +Q02948 UniProtKB Beta strand 413 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7 +Q02948 UniProtKB Helix 435 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7 +Q02948 UniProtKB Beta strand 502 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7 +Q02948 UniProtKB Helix 513 537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VP7 +##sequence-region P38934 1 470 +P38934 UniProtKB Chain 1 470 . . . ID=PRO_0000064919;Note=Nuclear segregation protein BFR1 +P38934 UniProtKB Coiled coil 17 178 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38934 UniProtKB Coiled coil 237 281 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38934 UniProtKB Coiled coil 398 469 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38934 UniProtKB Modified residue 260 260 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38934 UniProtKB Modified residue 336 336 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +P38934 UniProtKB Modified residue 369 369 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q06333 1 122 +Q06333 UniProtKB Chain 1 122 . . . ID=PRO_0000253844;Note=Biogenesis of lysosome-related organelles complex 1 subunit CNL1 +Q06333 UniProtKB Coiled coil 63 95 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04199 1 468 +Q04199 UniProtKB Chain 1 468 . . . ID=PRO_0000050894;Note=Chromatin assembly factor 1 subunit p60 +Q04199 UniProtKB Repeat 11 52 . . . Note=WD 1 +Q04199 UniProtKB Repeat 69 108 . . . Note=WD 2 +Q04199 UniProtKB Repeat 143 182 . . . Note=WD 3 +Q04199 UniProtKB Repeat 185 224 . . . Note=WD 4 +Q04199 UniProtKB Repeat 371 413 . . . Note=WD 5 +##sequence-region Q06150 1 570 +Q06150 UniProtKB Chain 1 570 . . . ID=PRO_0000247176;Note=Protein BOP2 +Q06150 UniProtKB Modified residue 383 383 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P53741 1 515 +P53741 UniProtKB Chain 1 515 . . . ID=PRO_0000194803;Note=UBP3-associated protein BRE5 +P53741 UniProtKB Domain 8 140 . . . Note=NTF2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00137 +P53741 UniProtKB Domain 418 494 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P53741 UniProtKB Modified residue 187 187 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P53741 UniProtKB Modified residue 282 282 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53741 UniProtKB Modified residue 336 336 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P53741 UniProtKB Modified residue 340 340 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53741 UniProtKB Modified residue 398 398 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P53741 UniProtKB Helix 5 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY +P53741 UniProtKB Helix 24 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY +P53741 UniProtKB Beta strand 31 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY +P53741 UniProtKB Beta strand 56 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY +P53741 UniProtKB Helix 62 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY +P53741 UniProtKB Helix 73 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY +P53741 UniProtKB Beta strand 79 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY +P53741 UniProtKB Helix 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY +P53741 UniProtKB Beta strand 97 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY +P53741 UniProtKB Beta strand 114 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY +P53741 UniProtKB Beta strand 131 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QIY +##sequence-region P43571 1 1029 +P43571 UniProtKB Chain 1 1029 . . . ID=PRO_0000202676;Note=GPI inositol-deacylase +P43571 UniProtKB Transmembrane 57 77 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Transmembrane 708 728 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Transmembrane 749 769 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Transmembrane 804 824 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Transmembrane 872 892 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Transmembrane 920 940 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Transmembrane 957 977 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Transmembrane 985 1005 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Transmembrane 1008 1028 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Active site 236 236 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43571 UniProtKB Glycosylation 19 19 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Glycosylation 295 295 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Glycosylation 302 302 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Glycosylation 447 447 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Glycosylation 456 456 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Glycosylation 485 485 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Glycosylation 565 565 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Glycosylation 651 651 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Glycosylation 668 668 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Glycosylation 694 694 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43571 UniProtKB Glycosylation 918 918 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36130 1 643 +P36130 UniProtKB Chain 1 643 . . . ID=PRO_0000051478;Note=CCR4-associated factor 4 +P36130 UniProtKB Repeat 317 357 . . . Note=WD 1 +P36130 UniProtKB Repeat 360 400 . . . Note=WD 2 +P36130 UniProtKB Repeat 422 461 . . . Note=WD 3 +P36130 UniProtKB Repeat 479 526 . . . Note=WD 4 +P36130 UniProtKB Repeat 527 566 . . . Note=WD 5 +P36130 UniProtKB Repeat 568 603 . . . Note=WD 6 +P36130 UniProtKB Repeat 614 643 . . . Note=WD 7 +P36130 UniProtKB Region 1 274 . . . Note=Required for interaction with FIS1 and MDV1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16009724;Dbxref=PMID:16009724 +P36130 UniProtKB Region 74 126 . . . Note=Sufficient for interaction with FIS1 +P36130 UniProtKB Coiled coil 160 255 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36130 UniProtKB Mutagenesis 85 86 . . . Note=Abolishes interaction with FIS1. FR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17998537;Dbxref=PMID:17998537 +P36130 UniProtKB Mutagenesis 88 88 . . . Note=Abolishes interaction with FIS1. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17998537;Dbxref=PMID:17998537 +P36130 UniProtKB Mutagenesis 110 110 . . . Note=Abolishes interaction with FIS1. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17998537;Dbxref=PMID:17998537 +P36130 UniProtKB Mutagenesis 111 111 . . . Note=Abolishes interaction with FIS1. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17998537;Dbxref=PMID:17998537 +P36130 UniProtKB Mutagenesis 114 114 . . . Note=Abolishes interaction with FIS1. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17998537;Dbxref=PMID:17998537 +P36130 UniProtKB Sequence conflict 94 95 . . . Note=QR->HG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36130 UniProtKB Helix 83 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PQR +P36130 UniProtKB Turn 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PQR +P36130 UniProtKB Beta strand 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PQR +P36130 UniProtKB Helix 110 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PQR +##sequence-region P41832 1 1953 +P41832 UniProtKB Chain 1 1953 . . . ID=PRO_0000194899;Note=Protein BNI1 +P41832 UniProtKB Domain 174 696 . . . Note=GBD/FH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00579 +P41832 UniProtKB Domain 1053 1337 . . . Note=FH1 +P41832 UniProtKB Domain 1348 1766 . . . Note=FH2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00774 +P41832 UniProtKB Domain 1792 1826 . . . Note=DAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00577 +P41832 UniProtKB Coiled coil 712 807 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41832 UniProtKB Coiled coil 864 894 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41832 UniProtKB Coiled coil 928 981 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41832 UniProtKB Coiled coil 1732 1811 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41832 UniProtKB Compositional bias 64 67 . . . Note=Poly-Ser +P41832 UniProtKB Compositional bias 1053 1057 . . . Note=Poly-Ser +P41832 UniProtKB Compositional bias 1239 1250 . . . Note=Poly-Pro +P41832 UniProtKB Compositional bias 1278 1291 . . . Note=Poly-Pro +P41832 UniProtKB Compositional bias 1303 1309 . . . Note=Poly-Pro +P41832 UniProtKB Compositional bias 1751 1754 . . . Note=Poly-Glu +P41832 UniProtKB Modified residue 311 311 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P41832 UniProtKB Modified residue 325 325 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P41832 UniProtKB Modified residue 1085 1085 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P41832 UniProtKB Modified residue 1170 1170 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P41832 UniProtKB Modified residue 1338 1338 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P41832 UniProtKB Modified residue 1344 1344 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P41832 UniProtKB Modified residue 1918 1918 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P41832 UniProtKB Sequence conflict 938 938 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41832 UniProtKB Sequence conflict 938 938 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41832 UniProtKB Sequence conflict 938 938 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41832 UniProtKB Sequence conflict 1430 1430 . . . Note=G->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41832 UniProtKB Beta strand 1371 1373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1378 1388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1391 1398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Beta strand 1400 1402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1405 1413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Turn 1414 1416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1423 1432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1434 1436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1441 1449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Turn 1450 1452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1453 1456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1459 1464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1468 1471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1475 1480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1482 1484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1494 1496 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1504 1506 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y64 +P41832 UniProtKB Helix 1509 1516 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Turn 1517 1524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1525 1535 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1538 1560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1563 1579 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1582 1584 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1591 1596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Beta strand 1597 1599 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Beta strand 1603 1608 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX4 +P41832 UniProtKB Helix 1609 1620 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1622 1626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1627 1630 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1632 1637 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Helix 1642 1665 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Turn 1667 1669 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Turn 1671 1673 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y64 +P41832 UniProtKB Helix 1680 1715 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +P41832 UniProtKB Beta strand 1720 1722 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y64 +P41832 UniProtKB Helix 1723 1757 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UX5 +##sequence-region P50084 1 137 +P50084 UniProtKB Chain 1 137 . . . ID=PRO_0000202851;Note=Protein BNS1 +##sequence-region P53838 1 576 +P53838 UniProtKB Chain 1 576 . . . ID=PRO_0000079243;Note=Boron transporter 1 +P53838 UniProtKB Topological domain 1 84 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Transmembrane 85 105 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Topological domain 106 116 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Transmembrane 117 134 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Topological domain 135 140 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Transmembrane 141 160 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Topological domain 161 165 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Transmembrane 166 186 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Topological domain 187 192 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Transmembrane 193 213 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Topological domain 214 235 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Transmembrane 236 256 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Topological domain 257 274 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Transmembrane 275 295 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Topological domain 296 329 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Transmembrane 330 350 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Topological domain 351 373 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Transmembrane 374 394 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Topological domain 395 438 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Transmembrane 439 459 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Topological domain 460 495 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Transmembrane 496 516 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Topological domain 517 518 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Transmembrane 519 539 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53838 UniProtKB Topological domain 540 576 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P25385 1 244 +P25385 UniProtKB Chain 1 244 . . . ID=PRO_0000207557;Note=Protein transport protein BOS1 +P25385 UniProtKB Topological domain 1 222 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25385 UniProtKB Transmembrane 223 240 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25385 UniProtKB Topological domain 241 244 . . . Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25385 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P14772 1 1559 +P14772 UniProtKB Chain 1 1559 . . . ID=PRO_0000093448;Note=Bile pigment transporter 1 +P14772 UniProtKB Topological domain 1 29 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14772 UniProtKB Transmembrane 30 50 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Topological domain 51 84 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14772 UniProtKB Transmembrane 85 105 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Topological domain 106 110 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14772 UniProtKB Transmembrane 111 127 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Topological domain 128 139 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14772 UniProtKB Transmembrane 140 160 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Topological domain 161 178 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14772 UniProtKB Transmembrane 179 199 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Topological domain 200 283 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14772 UniProtKB Transmembrane 284 304 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Topological domain 305 333 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14772 UniProtKB Transmembrane 334 354 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Topological domain 355 410 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14772 UniProtKB Transmembrane 411 431 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Topological domain 432 434 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14772 UniProtKB Transmembrane 435 455 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Topological domain 456 518 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14772 UniProtKB Transmembrane 519 539 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Topological domain 540 560 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14772 UniProtKB Transmembrane 561 581 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Topological domain 582 972 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14772 UniProtKB Transmembrane 973 993 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Topological domain 994 1030 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14772 UniProtKB Transmembrane 1031 1052 . . . Note=Helical%3B Name%3D13;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Topological domain 1053 1095 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14772 UniProtKB Transmembrane 1096 1116 . . . Note=Helical%3B Name%3D14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Topological domain 1117 1117 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14772 UniProtKB Transmembrane 1118 1138 . . . Note=Helical%3B Name%3D15;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Topological domain 1139 1209 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14772 UniProtKB Transmembrane 1210 1230 . . . Note=Helical%3B Name%3D16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Topological domain 1231 1235 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14772 UniProtKB Transmembrane 1236 1256 . . . Note=Helical%3B Name%3D17;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Topological domain 1257 1559 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14772 UniProtKB Domain 292 578 . . . Note=ABC transmembrane type-1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Domain 639 871 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P14772 UniProtKB Domain 980 1265 . . . Note=ABC transmembrane type-1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P14772 UniProtKB Domain 1302 1553 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P14772 UniProtKB Nucleotide binding 672 679 . . . Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P14772 UniProtKB Nucleotide binding 1336 1343 . . . Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P14772 UniProtKB Modified residue 645 645 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P14772 UniProtKB Modified residue 885 885 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14772 UniProtKB Modified residue 889 889 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14772 UniProtKB Modified residue 893 893 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14772 UniProtKB Modified residue 895 895 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14772 UniProtKB Modified residue 916 916 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P14772 UniProtKB Modified residue 927 927 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P14772 UniProtKB Modified residue 931 931 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P14772 UniProtKB Modified residue 934 934 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P14772 UniProtKB Glycosylation 1011 1011 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38770 1 471 +P38770 UniProtKB Chain 1 471 . . . ID=PRO_0000202892;Note=Nucleus export protein BRL1 +P38770 UniProtKB Topological domain 1 299 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38770 UniProtKB Transmembrane 300 320 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38770 UniProtKB Topological domain 321 407 . . . Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38770 UniProtKB Transmembrane 408 428 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38770 UniProtKB Topological domain 429 471 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53194 1 125 +P53194 UniProtKB Chain 1 125 . . . ID=PRO_0000202777;Note=Uncharacterized protein BRP1 +##sequence-region P53286 1 410 +P53286 UniProtKB Chain 1 410 . . . ID=PRO_0000065007;Note=Protein BTN2 +P53286 UniProtKB Coiled coil 243 330 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53286 UniProtKB Compositional bias 215 301 . . . Note=Glu-rich +##sequence-region P53727 1 317 +P53727 UniProtKB Chain 1 317 . . . ID=PRO_0000213349;Note=Putative pyridoxal kinase BUD17 +P53727 UniProtKB Nucleotide binding 190 191 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53727 UniProtKB Nucleotide binding 220 232 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53727 UniProtKB Binding site 16 16 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53727 UniProtKB Binding site 128 128 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53727 UniProtKB Binding site 233 233 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53727 UniProtKB Sequence conflict 93 93 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25337 1 157 +P25337 UniProtKB Chain 1 157 . . . ID=PRO_0000193902;Note=Pre-mRNA-splicing factor BUD31 +P25337 UniProtKB Motif 2 11 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25337 UniProtKB Helix 16 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P25337 UniProtKB Helix 42 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P25337 UniProtKB Helix 75 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P25337 UniProtKB Beta strand 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MY1 +P25337 UniProtKB Helix 89 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P25337 UniProtKB Turn 99 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P25337 UniProtKB Turn 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P25337 UniProtKB Beta strand 114 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P25337 UniProtKB Helix 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P25337 UniProtKB Helix 126 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P25337 UniProtKB Turn 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P25300 1 642 +P25300 UniProtKB Chain 1 642 . . . ID=PRO_0000068859;Note=Bud site selection protein 5 +P25300 UniProtKB Domain 224 339 . . . Note=N-terminal Ras-GEF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00135 +P25300 UniProtKB Domain 412 640 . . . Note=Ras-GEF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00168 +P25300 UniProtKB Sequence conflict 110 110 . . . Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25300 UniProtKB Sequence conflict 111 111 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25300 UniProtKB Sequence conflict 225 225 . . . Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25300 UniProtKB Sequence conflict 401 401 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25300 UniProtKB Sequence conflict 401 401 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25300 UniProtKB Sequence conflict 481 481 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25300 UniProtKB Sequence conflict 481 481 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08754 1 746 +Q08754 UniProtKB Chain 1 746 . . . ID=PRO_0000065019;Note=Bud site selection protein 7 +Q08754 UniProtKB Region 733 746 . . . Note=CHS5-binding +##sequence-region P23293 1 657 +P23293 UniProtKB Chain 1 657 . . . ID=PRO_0000085687;Note=Serine/threonine-protein kinase BUR1 +P23293 UniProtKB Domain 60 366 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P23293 UniProtKB Nucleotide binding 66 74 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P23293 UniProtKB Active site 195 195 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P23293 UniProtKB Binding site 89 89 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P23293 UniProtKB Modified residue 240 240 . . . Note=Phosphothreonine%3B by CAK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12215532;Dbxref=PMID:12215532 +P23293 UniProtKB Modified residue 400 400 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P23293 UniProtKB Modified residue 405 405 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P23293 UniProtKB Modified residue 417 417 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P23293 UniProtKB Modified residue 634 634 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P23293 UniProtKB Mutagenesis 107 107 . . . Note=Loss of kinase activity in vitro. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12972617;Dbxref=PMID:12972617 +P23293 UniProtKB Mutagenesis 213 213 . . . Note=Loss of kinase activity in vitro. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12972617;Dbxref=PMID:12972617 +P23293 UniProtKB Mutagenesis 240 240 . . . Note=No phosphorylation of SGV1. T->A%2CD%2CE;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12215532,ECO:0000269|PubMed:12972617;Dbxref=PMID:12215532,PMID:12972617 +##sequence-region P36106 1 594 +P36106 UniProtKB Chain 1 594 . . . ID=PRO_0000203191;Note=Transcription factor BYE1 +P36106 UniProtKB Domain 254 365 . . . Note=TFIIS central;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00651 +P36106 UniProtKB Zinc finger 72 134 . . . Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 +P36106 UniProtKB Modified residue 177 177 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36106 UniProtKB Helix 234 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P36106 UniProtKB Helix 254 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P36106 UniProtKB Helix 272 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P36106 UniProtKB Helix 285 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P36106 UniProtKB Helix 302 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P36106 UniProtKB Beta strand 317 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BXX +P36106 UniProtKB Helix 320 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P36106 UniProtKB Helix 332 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P36106 UniProtKB Helix 346 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P36106 UniProtKB Turn 360 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +##sequence-region Q05791 1 360 +Q05791 UniProtKB Chain 1 360 . . . ID=PRO_0000227684;Note=Cell division cycle protein 123 +Q05791 UniProtKB Mutagenesis 274 274 . . . Note=Reduces the interaction with DMA1. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15319434;Dbxref=PMID:15319434 +##sequence-region P32797 1 924 +P32797 UniProtKB Chain 1 924 . . . ID=PRO_0000089441;Note=Cell division control protein 13 +P32797 UniProtKB DNA binding 500 686 . . . Note=OB +P32797 UniProtKB Modified residue 306 306 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32797 UniProtKB Modified residue 308 308 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32797 UniProtKB Modified residue 333 333 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32797 UniProtKB Mutagenesis 50 50 . . . Note=Increase in length of X' and Y' telomeres. Disrupts interaction with POL1 but not FUN12. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792 +P32797 UniProtKB Mutagenesis 72 72 . . . Note=Disrupts interaction with POL1 and FUN12. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792 +P32797 UniProtKB Mutagenesis 124 124 . . . Note=Disrupts interaction with POL1 but not FUN12. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792 +P32797 UniProtKB Mutagenesis 149 149 . . . Note=Disrupts interaction with POL1 but not FUN12. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792 +P32797 UniProtKB Mutagenesis 228 228 . . . Note=Disrupts interaction with POL1 but not FUN12. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792 +P32797 UniProtKB Mutagenesis 243 243 . . . Note=Disrupts interaction with POL1 and FUN12. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792 +P32797 UniProtKB Mutagenesis 392 392 . . . Note=Disrupts interaction with POL1 but not FUN12. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792 +P32797 UniProtKB Mutagenesis 523 523 . . . Note=Increase in length of X' and Y' telomeres. Disrupts interaction with POL1 but not FUN12. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792 +P32797 UniProtKB Sequence conflict 40 40 . . . Note=L->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32797 UniProtKB Helix 21 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ +P32797 UniProtKB Beta strand 32 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ +P32797 UniProtKB Beta strand 48 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ +P32797 UniProtKB Beta strand 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NWT +P32797 UniProtKB Beta strand 70 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ +P32797 UniProtKB Helix 79 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ +P32797 UniProtKB Beta strand 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ +P32797 UniProtKB Helix 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ +P32797 UniProtKB Beta strand 125 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ +P32797 UniProtKB Beta strand 138 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ +P32797 UniProtKB Helix 151 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ +P32797 UniProtKB Helix 178 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ +P32797 UniProtKB Beta strand 197 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ +P32797 UniProtKB Helix 203 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ +P32797 UniProtKB Helix 211 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ +P32797 UniProtKB Helix 348 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE +P32797 UniProtKB Beta strand 359 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE +P32797 UniProtKB Helix 377 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE +P32797 UniProtKB Beta strand 381 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE +P32797 UniProtKB Beta strand 385 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE +P32797 UniProtKB Beta strand 394 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE +P32797 UniProtKB Turn 403 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE +P32797 UniProtKB Beta strand 406 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE +P32797 UniProtKB Helix 415 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE +P32797 UniProtKB Helix 424 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE +P32797 UniProtKB Helix 429 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE +P32797 UniProtKB Turn 437 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE +P32797 UniProtKB Beta strand 444 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE +P32797 UniProtKB Beta strand 463 472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HCE +P32797 UniProtKB Turn 510 512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL +P32797 UniProtKB Beta strand 521 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL +P32797 UniProtKB Beta strand 531 533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL +P32797 UniProtKB Beta strand 539 544 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL +P32797 UniProtKB Beta strand 565 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL +P32797 UniProtKB Turn 571 573 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL +P32797 UniProtKB Beta strand 575 580 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL +P32797 UniProtKB Helix 581 592 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL +P32797 UniProtKB Beta strand 595 597 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL +P32797 UniProtKB Helix 599 602 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL +P32797 UniProtKB Beta strand 617 624 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL +P32797 UniProtKB Beta strand 626 629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL +P32797 UniProtKB Beta strand 631 634 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL +P32797 UniProtKB Beta strand 642 644 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL +P32797 UniProtKB Helix 645 648 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL +P32797 UniProtKB Helix 653 668 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL +P32797 UniProtKB Helix 670 675 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL +P32797 UniProtKB Helix 677 680 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KXL +##sequence-region P25656 1 391 +P25656 UniProtKB Chain 1 391 . . . ID=PRO_0000207670;Note=Cell division control protein 50 +P25656 UniProtKB Topological domain 1 44 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25656 UniProtKB Transmembrane 45 65 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25656 UniProtKB Topological domain 66 331 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25656 UniProtKB Transmembrane 332 352 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25656 UniProtKB Topological domain 353 391 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25656 UniProtKB Glycosylation 199 199 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25656 UniProtKB Glycosylation 216 216 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25656 UniProtKB Glycosylation 237 237 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25656 UniProtKB Glycosylation 288 288 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25656 UniProtKB Glycosylation 329 329 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P09119 1 513 +P09119 UniProtKB Chain 1 513 . . . ID=PRO_0000150977;Note=Cell division control protein 6 +P09119 UniProtKB Nucleotide binding 108 115 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P09119 UniProtKB Region 1 47 . . . Note=Interaction with CDC4%3B required for degradation;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9312054;Dbxref=PMID:9312054 +P09119 UniProtKB Motif 27 33 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8892760;Dbxref=PMID:8892760 +P09119 UniProtKB Modified residue 368 368 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P09119 UniProtKB Mutagenesis 29 29 . . . Note=Impairs nuclear localization. K->R%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8892760;Dbxref=PMID:8892760 +P09119 UniProtKB Mutagenesis 114 114 . . . Note=Impairs ORC1-binding and leads to defective association with chromatin. K->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10075735,ECO:0000269|PubMed:9892652;Dbxref=PMID:10075735,PMID:9892652 +P09119 UniProtKB Sequence conflict 3 3 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09119 UniProtKB Sequence conflict 202 202 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09119 UniProtKB Sequence conflict 225 225 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09119 UniProtKB Sequence conflict 272 272 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09119 UniProtKB Sequence conflict 277 277 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09119 UniProtKB Sequence conflict 339 339 . . . Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09119 UniProtKB Sequence conflict 395 396 . . . Note=SK->LQN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09119 UniProtKB Sequence conflict 402 402 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09119 UniProtKB Sequence conflict 410 410 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09119 UniProtKB Sequence conflict 436 436 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53197 1 566 +P53197 UniProtKB Chain 1 566 . . . ID=PRO_0000050904;Note=APC/C activator protein CDH1 +P53197 UniProtKB Repeat 258 298 . . . Note=WD 1 +P53197 UniProtKB Repeat 300 339 . . . Note=WD 2 +P53197 UniProtKB Repeat 342 379 . . . Note=WD 3 +P53197 UniProtKB Repeat 383 422 . . . Note=WD 4 +P53197 UniProtKB Repeat 425 467 . . . Note=WD 5 +P53197 UniProtKB Repeat 469 510 . . . Note=WD 6 +P53197 UniProtKB Repeat 513 552 . . . Note=WD 7 +P53197 UniProtKB Motif 55 61 . . . Note=C-box +P53197 UniProtKB Compositional bias 32 38 . . . Note=Poly-Ser +P53197 UniProtKB Modified residue 213 213 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53197 UniProtKB Mutagenesis 12 12 . . . Note=Abolishes phosphorylation%3B when associated with A-16%3B A-42%3B A-157%3B A-169%3B A-173%3B A-176%3B A-227 and A-239. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9831566;Dbxref=PMID:9831566 +P53197 UniProtKB Mutagenesis 16 16 . . . Note=Abolishes phosphorylation%3B when associated with A-12%3B A-42%3B A-157%3B A-169%3B A-173%3B A-176%3B A-227 and A-239. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9831566;Dbxref=PMID:9831566 +P53197 UniProtKB Mutagenesis 42 42 . . . Note=Abolishes phosphorylation%3B when associated with A-12%3B A-16%3B A-157%3B A-169%3B A-173%3B A-176%3B A-227 and A-239. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9831566;Dbxref=PMID:9831566 +P53197 UniProtKB Mutagenesis 157 157 . . . Note=Abolishes phosphorylation%3B when associated with A-12%3B A-16%3B A-42%3B A-169%3B A-173%3B A-176%3B A-227 and A-239. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9831566;Dbxref=PMID:9831566 +P53197 UniProtKB Mutagenesis 169 169 . . . Note=Abolishes phosphorylation%3B when associated with A-12%3B A-16%3B A-42%3B A-157%3B A-173%3B A-176%3B A-227 and A-239. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9831566;Dbxref=PMID:9831566 +P53197 UniProtKB Mutagenesis 173 173 . . . Note=Abolishes phosphorylation%3B when associated with A-12%3B A-16%3B A-42%3B A-157%3B A-169%3B A-176%3B A-227 and A-239. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9831566;Dbxref=PMID:9831566 +P53197 UniProtKB Mutagenesis 176 176 . . . Note=Abolishes phosphorylation%3B when associated with A-12%3B A-16%3B A-42%3B A-157%3B A-169%3B A-173%3B A-227 and A-239. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9831566;Dbxref=PMID:9831566 +P53197 UniProtKB Mutagenesis 227 227 . . . Note=Abolishes phosphorylation%3B when associated with A-12%3B A-16%3B A-42%3B A-157%3B A-169%3B A-173%3B A-176 and A-239. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9831566;Dbxref=PMID:9831566 +P53197 UniProtKB Mutagenesis 239 239 . . . Note=Abolishes phosphorylation%3B when associated with A-12%3B A-16%3B A-42%3B A-157%3B A-169%3B A-173%3B A-176 and A-227. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9831566;Dbxref=PMID:9831566 +P53197 UniProtKB Beta strand 252 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 269 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 275 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 284 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Turn 290 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 295 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 305 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 314 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 326 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Turn 331 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 335 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 347 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 356 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 366 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 373 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 378 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 388 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 395 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 399 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 409 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 420 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 430 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 437 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 442 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Turn 449 451 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 453 458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Turn 459 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 463 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 474 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 481 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 486 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 497 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 502 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 507 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 518 523 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 527 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Turn 535 537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +P53197 UniProtKB Beta strand 538 543 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BH6 +##sequence-region P47112 1 604 +P47112 UniProtKB Chain 1 604 . . . ID=PRO_0000203095;Note=Cell division cycle protein CDT1 +P47112 UniProtKB Beta strand 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Turn 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Helix 26 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Beta strand 41 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Helix 51 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Turn 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Beta strand 79 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Beta strand 87 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Helix 109 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Helix 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Beta strand 141 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5ME9 +P47112 UniProtKB Beta strand 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Beta strand 149 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Beta strand 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Beta strand 194 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Beta strand 220 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Beta strand 227 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Helix 234 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Beta strand 249 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Helix 253 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5ME9 +P47112 UniProtKB Beta strand 258 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Helix 278 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Helix 291 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Helix 299 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEC +P47112 UniProtKB Beta strand 333 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Helix 340 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEC +P47112 UniProtKB Helix 357 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEC +P47112 UniProtKB Beta strand 370 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEC +P47112 UniProtKB Beta strand 381 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEC +P47112 UniProtKB Helix 391 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEA +P47112 UniProtKB Helix 399 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEC +P47112 UniProtKB Beta strand 417 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEC +P47112 UniProtKB Helix 495 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEB +P47112 UniProtKB Beta strand 525 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEB +P47112 UniProtKB Helix 531 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEB +P47112 UniProtKB Helix 551 564 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEB +P47112 UniProtKB Turn 566 568 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEB +P47112 UniProtKB Beta strand 569 572 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEB +P47112 UniProtKB Beta strand 580 584 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEB +P47112 UniProtKB Helix 588 602 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MEB +##sequence-region Q12453 1 761 +Q12453 UniProtKB Chain 1 761 . . . ID=PRO_0000237655;Note=Cytoplasmic export protein 1 +Q12453 UniProtKB Repeat 385 423 . . . Note=HEAT 1 +Q12453 UniProtKB Repeat 498 534 . . . Note=HEAT 2 +Q12453 UniProtKB Modified residue 754 754 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q12453 UniProtKB Turn 10 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Beta strand 16 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Beta strand 24 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Beta strand 28 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Turn 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Beta strand 43 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Turn 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 56 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Beta strand 77 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Beta strand 89 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 103 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 110 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Turn 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Beta strand 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Beta strand 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Beta strand 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 164 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Turn 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 190 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Turn 205 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 210 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 213 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 226 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 237 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 243 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 253 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 259 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 277 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 287 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 292 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 322 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 325 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 346 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 359 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 378 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 386 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 392 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 398 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 412 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 417 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 423 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 437 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 451 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Beta strand 454 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 458 473 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 478 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 492 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 497 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 504 508 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 509 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +Q12453 UniProtKB Helix 517 540 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VWA +##sequence-region Q06632 1 1357 +Q06632 UniProtKB Chain 1 1357 . . . ID=PRO_0000076203;Note=Protein CFT1 +##sequence-region P13365 1 580 +P13365 UniProtKB Chain 1 580 . . . ID=PRO_0000080413;Note=G1/S-specific cyclin CLN3 +P13365 UniProtKB Sequence conflict 23 23 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53188 1 120 +P53188 UniProtKB Chain 1 120 . . . ID=PRO_0000202773;Note=rRNA-processing protein CGR1 +P53188 UniProtKB Coiled coil 47 106 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P07267 1 405 +P07267 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8840499;Dbxref=PMID:8840499 +P07267 UniProtKB Propeptide 23 76 . . . ID=PRO_0000025873;Note=Activation peptide;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6 +P07267 UniProtKB Chain 77 405 . . . ID=PRO_0000025874;Note=Saccharopepsin +P07267 UniProtKB Domain 91 402 . . . Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103 +P07267 UniProtKB Active site 109 109 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +P07267 UniProtKB Active site 294 294 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +P07267 UniProtKB Glycosylation 144 144 . . . Note=N-linked (GlcNAc...) asparagine +P07267 UniProtKB Glycosylation 345 345 . . . Note=N-linked (GlcNAc...) asparagine +P07267 UniProtKB Disulfide bond 122 127 . . . . +P07267 UniProtKB Disulfide bond 328 361 . . . . +P07267 UniProtKB Mutagenesis 294 294 . . . Note=Inactivation. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1959673;Dbxref=PMID:1959673 +P07267 UniProtKB Beta strand 79 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Turn 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 90 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Turn 98 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 102 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 115 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Helix 125 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Helix 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 142 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 155 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 171 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Helix 186 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 195 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Helix 203 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Helix 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Helix 213 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 224 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Helix 235 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 240 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Helix 252 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 255 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Turn 267 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 271 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 282 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 290 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 300 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Helix 304 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 317 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FQ8 +P07267 UniProtKB Beta strand 322 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Helix 328 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 337 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 344 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Turn 350 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 353 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 360 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 365 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Turn 372 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 376 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Helix 382 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 388 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Turn 394 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +P07267 UniProtKB Beta strand 398 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +##sequence-region P39113 1 1433 +P39113 UniProtKB Chain 1 1433 . . . ID=PRO_0000114940;Note=Regulatory protein CAT8 +P39113 UniProtKB DNA binding 70 97 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P39113 UniProtKB Compositional bias 208 212 . . . Note=Poly-Pro +P39113 UniProtKB Compositional bias 972 976 . . . Note=Poly-Asn +P39113 UniProtKB Sequence conflict 303 303 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39113 UniProtKB Sequence conflict 747 747 . . . Note=K->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39113 UniProtKB Sequence conflict 768 768 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39113 UniProtKB Sequence conflict 999 1002 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39113 UniProtKB Sequence conflict 1008 1008 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39113 UniProtKB Sequence conflict 1016 1016 . . . Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39113 UniProtKB Sequence conflict 1019 1019 . . . Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39113 UniProtKB Sequence conflict 1061 1061 . . . Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39113 UniProtKB Sequence conflict 1072 1074 . . . Note=TDA->ADS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39113 UniProtKB Sequence conflict 1092 1092 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39113 UniProtKB Sequence conflict 1100 1100 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39113 UniProtKB Sequence conflict 1120 1120 . . . Note=M->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39113 UniProtKB Sequence conflict 1162 1162 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P35203 1 478 +P35203 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7957085;Dbxref=PMID:7957085 +P35203 UniProtKB Chain 2 478 . . . ID=PRO_0000089370;Note=Centromere DNA-binding protein complex CBF3 subunit C +P35203 UniProtKB Compositional bias 198 222 . . . Note=Asp/Glu-rich (acidic) +P35203 UniProtKB Compositional bias 216 229 . . . Note=Ser-rich +##sequence-region P32582 1 507 +P32582 UniProtKB Chain 1 507 . . . ID=PRO_0000167135;Note=Cystathionine beta-synthase +P32582 UniProtKB Domain 373 432 . . . Note=CBS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +P32582 UniProtKB Region 196 200 . . . Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32582 UniProtKB Binding site 84 84 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32582 UniProtKB Binding site 289 289 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32582 UniProtKB Modified residue 53 53 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32582 UniProtKB Modified residue 134 134 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32582 UniProtKB Modified residue 350 350 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32582 UniProtKB Modified residue 424 424 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32582 UniProtKB Natural variant 504 504 . . . Note=In strain: UCD932. S->N +P32582 UniProtKB Sequence conflict 2 2 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32582 UniProtKB Sequence conflict 8 8 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32582 UniProtKB Sequence conflict 63 63 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32582 UniProtKB Sequence conflict 104 104 . . . Note=L->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32582 UniProtKB Sequence conflict 129 129 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32582 UniProtKB Sequence conflict 163 163 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32582 UniProtKB Sequence conflict 407 407 . . . Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32582 UniProtKB Sequence conflict 436 437 . . . Note=GK->VE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32582 UniProtKB Sequence conflict 441 441 . . . Note=F->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32582 UniProtKB Sequence conflict 481 481 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P21269 1 546 +P21269 UniProtKB Alternative sequence 1 17 . . . ID=VSP_018699;Note=In isoform Cytoplasmic+nuclear 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21269 UniProtKB Alternative sequence 1 9 . . . ID=VSP_018698;Note=In isoform Cytoplasmic+nuclear 1. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06703 1 312 +Q06703 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06703 UniProtKB Chain 26 312 . . . ID=PRO_0000024827;Note=Chitin deacetylase 2 +Q06703 UniProtKB Domain 118 307 . . . Note=NodB homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01014 +Q06703 UniProtKB Glycosylation 142 142 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06703 UniProtKB Glycosylation 181 181 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06703 UniProtKB Glycosylation 199 199 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06703 UniProtKB Glycosylation 246 246 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06703 UniProtKB Glycosylation 263 263 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P27636 1 974 +P27636 UniProtKB Chain 1 974 . . . ID=PRO_0000085717;Note=Cell division control protein 15 +P27636 UniProtKB Domain 25 272 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P27636 UniProtKB Nucleotide binding 31 39 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P27636 UniProtKB Region 360 702 . . . Note=Self association domain +P27636 UniProtKB Region 751 974 . . . Note=Auto-inhibitory domain +P27636 UniProtKB Active site 146 146 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P27636 UniProtKB Binding site 54 54 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P27636 UniProtKB Modified residue 561 561 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22031224;Dbxref=PMID:22031224 +P27636 UniProtKB Modified residue 567 567 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:22031224;Dbxref=PMID:19779198,PMID:22031224 +P27636 UniProtKB Modified residue 870 870 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22031224;Dbxref=PMID:22031224 +P27636 UniProtKB Sequence conflict 316 316 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27636 UniProtKB Sequence conflict 316 316 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27636 UniProtKB Sequence conflict 316 316 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27636 UniProtKB Sequence conflict 316 316 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27636 UniProtKB Sequence conflict 321 321 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27636 UniProtKB Sequence conflict 321 321 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27636 UniProtKB Sequence conflict 321 321 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27636 UniProtKB Sequence conflict 321 321 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27636 UniProtKB Sequence conflict 900 902 . . . Note=KDV->NGC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27636 UniProtKB Sequence conflict 900 902 . . . Note=KDV->NGC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40986 1 491 +P40986 UniProtKB Chain 1 491 . . . ID=PRO_0000089444;Note=Cell division control protein 1 +P40986 UniProtKB Topological domain 1 39 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40986 UniProtKB Transmembrane 40 60 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40986 UniProtKB Topological domain 61 391 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40986 UniProtKB Transmembrane 392 412 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40986 UniProtKB Topological domain 413 465 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40986 UniProtKB Transmembrane 466 486 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40986 UniProtKB Topological domain 487 491 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40986 UniProtKB Compositional bias 8 38 . . . Note=Lys-rich +P40986 UniProtKB Metal binding 95 95 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40986 UniProtKB Metal binding 144 144 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40986 UniProtKB Metal binding 144 144 . . . Note=Divalent metal cation 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40986 UniProtKB Metal binding 183 183 . . . Note=Divalent metal cation 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40986 UniProtKB Metal binding 323 323 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40986 UniProtKB Sequence conflict 439 439 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40986 UniProtKB Sequence conflict 478 478 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P04821 1 1589 +P04821 UniProtKB Chain 1 1589 . . . ID=PRO_0000068863;Note=Cell division control protein 25 +P04821 UniProtKB Transmembrane 1452 1473 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04821 UniProtKB Domain 58 128 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P04821 UniProtKB Domain 1117 1247 . . . Note=N-terminal Ras-GEF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00135 +P04821 UniProtKB Domain 1305 1542 . . . Note=Ras-GEF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00168 +P04821 UniProtKB Modified residue 151 151 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04821 UniProtKB Modified residue 154 154 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04821 UniProtKB Modified residue 423 423 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P04821 UniProtKB Modified residue 580 580 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04821 UniProtKB Modified residue 596 596 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04821 UniProtKB Modified residue 632 632 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04821 UniProtKB Modified residue 635 635 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04821 UniProtKB Modified residue 649 649 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04821 UniProtKB Sequence conflict 497 497 . . . Note=I->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04821 UniProtKB Sequence conflict 954 963 . . . Note=PVGHHEPFKN->LSVIMNLSR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25694 1 835 +P25694 UniProtKB Chain 1 835 . . . ID=PRO_0000084587;Note=Cell division control protein 48 +P25694 UniProtKB Nucleotide binding 257 263 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 +P25694 UniProtKB Binding site 358 358 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 +P25694 UniProtKB Binding site 394 394 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55072 +P25694 UniProtKB Modified residue 472 472 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25694 UniProtKB Modified residue 519 519 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P25694 UniProtKB Modified residue 735 735 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P25694 UniProtKB Modified residue 770 770 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950 +P25694 UniProtKB Cross-link 305 305 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25694 UniProtKB Cross-link 322 322 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25694 UniProtKB Cross-link 346 346 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25694 UniProtKB Cross-link 522 522 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25694 UniProtKB Cross-link 539 539 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25694 UniProtKB Cross-link 594 594 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P25694 UniProtKB Cross-link 673 673 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region P06243 1 507 +P06243 UniProtKB Chain 1 507 . . . ID=PRO_0000085766;Note=Cell division control protein 7 +P06243 UniProtKB Domain 33 469 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P06243 UniProtKB Nucleotide binding 39 47 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P06243 UniProtKB Active site 163 163 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P06243 UniProtKB Binding site 76 76 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +##sequence-region P53829 1 373 +P53829 UniProtKB Chain 1 373 . . . ID=PRO_0000203375;Note=Protein CAF40 +##sequence-region P43568 1 368 +P43568 UniProtKB Chain 1 368 . . . ID=PRO_0000085690;Note=Serine/threonine-protein kinase CAK1 +P43568 UniProtKB Domain 1 368 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P43568 UniProtKB Active site 156 156 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +##sequence-region P53223 1 239 +P53223 UniProtKB Chain 1 239 . . . ID=PRO_0000215629;Note=Dolichyldiphosphatase +P53223 UniProtKB Topological domain 1 34 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53223 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53223 UniProtKB Topological domain 56 131 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53223 UniProtKB Transmembrane 132 152 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53223 UniProtKB Topological domain 153 164 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53223 UniProtKB Transmembrane 165 185 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53223 UniProtKB Topological domain 186 239 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40969 1 608 +P40969 UniProtKB Chain 1 608 . . . ID=PRO_0000114941;Note=Centromere DNA-binding protein complex CBF3 subunit B +P40969 UniProtKB DNA binding 14 42 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P40969 UniProtKB Modified residue 575 575 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40969 UniProtKB Helix 58 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Turn 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 75 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Turn 92 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 96 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 108 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 123 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 134 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 154 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 176 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 186 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 200 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 204 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Turn 223 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 231 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Turn 241 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 245 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 250 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 280 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 313 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QUQ +P40969 UniProtKB Helix 338 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Turn 357 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 367 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 394 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 427 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 444 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Turn 447 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 451 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 457 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 480 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 498 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 501 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Beta strand 530 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 536 550 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 555 562 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 589 600 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +P40969 UniProtKB Helix 603 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VEQ +##sequence-region P53894 1 756 +P53894 UniProtKB Chain 1 756 . . . ID=PRO_0000085697;Note=Serine/threonine-protein kinase CBK1 +P53894 UniProtKB Domain 352 672 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53894 UniProtKB Domain 673 754 . . . Note=AGC-kinase C-terminal +P53894 UniProtKB Nucleotide binding 358 366 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53894 UniProtKB Compositional bias 23 34 . . . Note=Poly-Gln +P53894 UniProtKB Compositional bias 160 164 . . . Note=Poly-Ser +P53894 UniProtKB Compositional bias 214 232 . . . Note=Poly-Gln +P53894 UniProtKB Compositional bias 235 250 . . . Note=Poly-Gln +P53894 UniProtKB Active site 475 475 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P53894 UniProtKB Binding site 381 381 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53894 UniProtKB Modified residue 109 109 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53894 UniProtKB Helix 299 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Beta strand 349 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Beta strand 366 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Turn 372 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Beta strand 378 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Beta strand 385 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Beta strand 415 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Beta strand 425 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Helix 437 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Helix 450 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Helix 458 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Beta strand 478 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Helix 557 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Helix 561 563 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Beta strand 582 586 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Helix 591 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Turn 619 621 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Helix 622 625 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Helix 640 649 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Beta strand 656 658 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Beta strand 663 666 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P53894 UniProtKB Helix 679 681 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +##sequence-region P03874 1 630 +P03874 UniProtKB Chain 1 630 . . . ID=PRO_0000089380;Note=Cytochrome B pre-mRNA-processing protein 2 +P03874 UniProtKB Sequence conflict 490 490 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P11433 1 854 +P11433 UniProtKB Chain 1 854 . . . ID=PRO_0000080934;Note=Cell division control protein 24 +P11433 UniProtKB Domain 278 454 . . . Note=DH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00062 +P11433 UniProtKB Domain 478 668 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +P11433 UniProtKB Domain 761 854 . . . Note=PB1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01081 +P11433 UniProtKB Compositional bias 494 600 . . . Note=Ser/Thr-rich +P11433 UniProtKB Compositional bias 681 778 . . . Note=Ser/Thr-rich +P11433 UniProtKB Beta strand 762 768 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1O +P11433 UniProtKB Beta strand 780 784 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PQS +P11433 UniProtKB Helix 792 801 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PQS +P11433 UniProtKB Turn 802 806 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PQS +P11433 UniProtKB Beta strand 817 820 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PQS +P11433 UniProtKB Turn 821 823 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PQS +P11433 UniProtKB Beta strand 824 827 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PQS +P11433 UniProtKB Helix 833 844 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PQS +P11433 UniProtKB Beta strand 848 852 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PQS +##sequence-region P38042 1 758 +P38042 UniProtKB Chain 1 758 . . . ID=PRO_0000106274;Note=Anaphase-promoting complex subunit CDC27 +P38042 UniProtKB Repeat 154 187 . . . Note=TPR 1 +P38042 UniProtKB Repeat 472 505 . . . Note=TPR 2 +P38042 UniProtKB Repeat 540 573 . . . Note=TPR 3 +P38042 UniProtKB Repeat 574 607 . . . Note=TPR 4 +P38042 UniProtKB Repeat 608 641 . . . Note=TPR 5 +P38042 UniProtKB Repeat 642 675 . . . Note=TPR 6 +P38042 UniProtKB Repeat 676 709 . . . Note=TPR 7 +P38042 UniProtKB Repeat 710 743 . . . Note=TPR 8 +P38042 UniProtKB Compositional bias 365 388 . . . Note=Poly-Asn +P38042 UniProtKB Mutagenesis 267 267 . . . Note=Abolishes phosphorylation%3B when associated with A-304%3B A-328%3B A-351 and A-397. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279 +P38042 UniProtKB Mutagenesis 304 304 . . . Note=Abolishes phosphorylation%3B when associated with A-267%3B A-304%3B A-351 and A-397. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279 +P38042 UniProtKB Mutagenesis 328 328 . . . Note=Abolishes phosphorylation%3B when associated with A-267%3B A-304%3B A-328 and A-397. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279 +P38042 UniProtKB Mutagenesis 351 351 . . . Note=Abolishes phosphorylation%3B when associated with A-267%3B A-304%3B A-328 and A-304. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279 +P38042 UniProtKB Mutagenesis 397 397 . . . Note=Abolishes phosphorylation%3B when associated with A-304%3B A-328%3B A-351 and A-397. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279 +P38042 UniProtKB Mutagenesis 613 613 . . . Note=In CDC27-633%3B G2/M cell cycle arrest at 35 degrees Celsius. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1819514;Dbxref=PMID:1819514 +P38042 UniProtKB Mutagenesis 614 614 . . . Note=Abolishes interaction with CDC23. L->GL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7925276;Dbxref=PMID:7925276 +P38042 UniProtKB Sequence conflict 430 430 . . . Note=S->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38042 UniProtKB Sequence conflict 430 430 . . . Note=S->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06549 1 142 +Q06549 UniProtKB Chain 1 142 . . . ID=PRO_0000171685;Note=Cytidine deaminase +Q06549 UniProtKB Domain 9 139 . . . Note=CMP/dCMP-type deaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01083 +Q06549 UniProtKB Region 50 52 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06549 UniProtKB Active site 63 63 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06549 UniProtKB Metal binding 61 61 . . . Note=Zinc%3B catalytic +Q06549 UniProtKB Metal binding 96 96 . . . Note=Zinc%3B catalytic +Q06549 UniProtKB Metal binding 99 99 . . . Note=Zinc%3B catalytic +Q06549 UniProtKB Helix 8 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T +Q06549 UniProtKB Helix 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T +Q06549 UniProtKB Turn 28 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T +Q06549 UniProtKB Beta strand 34 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T +Q06549 UniProtKB Beta strand 45 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T +Q06549 UniProtKB Helix 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T +Q06549 UniProtKB Helix 62 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T +Q06549 UniProtKB Beta strand 81 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T +Q06549 UniProtKB Beta strand 89 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T +Q06549 UniProtKB Helix 97 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T +Q06549 UniProtKB Beta strand 112 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T +Q06549 UniProtKB Beta strand 118 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T +Q06549 UniProtKB Helix 128 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T +Q06549 UniProtKB Helix 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5T +##sequence-region P20438 1 545 +P20438 UniProtKB Chain 1 545 . . . ID=PRO_0000080412;Note=G1/S-specific cyclin CLN2 +P20438 UniProtKB Sequence conflict 440 440 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P24869 1 491 +P24869 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P24869 UniProtKB Chain 2 491 . . . ID=PRO_0000080404;Note=G2/mitotic-specific cyclin-2 +P24869 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P80235 1 687 +P80235 UniProtKB Chain 1 687 . . . ID=PRO_0000210175;Note=Putative mitochondrial carnitine O-acetyltransferase +P80235 UniProtKB Region 446 459 . . . Note=Coenzyme A binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P80235 UniProtKB Active site 346 346 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P80235 UniProtKB Binding site 481 481 . . . Note=Carnitine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P80235 UniProtKB Binding site 494 494 . . . Note=Carnitine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P80235 UniProtKB Modified residue 517 517 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P80235 UniProtKB Sequence conflict 25 25 . . . Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P80235 UniProtKB Sequence conflict 392 392 . . . Note=S->SS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P80235 UniProtKB Sequence conflict 595 596 . . . Note=SF->AS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P80235 UniProtKB Sequence conflict 653 653 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P80235 UniProtKB Sequence conflict 660 660 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32796 1 670 +P32796 UniProtKB Region 465 472 . . . Note=Coenzyme A binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32796 UniProtKB Motif 668 670 . . . Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32796 UniProtKB Active site 378 378 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32796 UniProtKB Binding site 461 461 . . . Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32796 UniProtKB Binding site 494 494 . . . Note=Carnitine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32796 UniProtKB Binding site 498 498 . . . Note=Coenzyme A%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32796 UniProtKB Binding site 507 507 . . . Note=Carnitine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32796 UniProtKB Binding site 597 597 . . . Note=Coenzyme A%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32796 UniProtKB Alternative sequence 1 22 . . . ID=VSP_018690;Note=In isoform Peroxisomal. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32796 UniProtKB Sequence conflict 263 263 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32796 UniProtKB Sequence conflict 308 308 . . . Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25296 1 175 +P25296 UniProtKB Initiator methionine 1 1 . . . Note=Removed +P25296 UniProtKB Chain 2 175 . . . ID=PRO_0000073498;Note=Calcineurin subunit B +P25296 UniProtKB Domain 21 56 . . . Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P25296 UniProtKB Domain 53 88 . . . Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P25296 UniProtKB Domain 90 125 . . . Note=EF-hand 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P25296 UniProtKB Domain 131 166 . . . Note=EF-hand 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P25296 UniProtKB Calcium binding 34 45 . . . Note=1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P25296 UniProtKB Calcium binding 66 77 . . . Note=2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P25296 UniProtKB Calcium binding 103 114 . . . Note=3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P25296 UniProtKB Calcium binding 144 155 . . . Note=4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P25296 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1321337;Dbxref=PMID:1321337 +##sequence-region P07253 1 162 +P07253 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P07253 UniProtKB Chain 2 162 . . . ID=PRO_0000089381;Note=Cytochrome B pre-mRNA-processing protein 6 +P07253 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P07253 UniProtKB Modified residue 97 97 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P07253 UniProtKB Sequence conflict 2 2 . . . Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36038 1 271 +P36038 UniProtKB Chain 1 271 . . . ID=PRO_0000203131;Note=Cytochrome b termination protein 1 +P36038 UniProtKB Sequence conflict 270 270 . . . Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P37366 1 393 +P37366 UniProtKB Chain 1 393 . . . ID=PRO_0000080504;Note=Cyclin CCL1 +##sequence-region P37267 1 147 +P37267 UniProtKB Chain 1 147 . . . ID=PRO_0000020845;Note=Assembly factor CBP4 +P37267 UniProtKB Transmembrane 5 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37267 UniProtKB Sequence conflict 42 42 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P48237 1 864 +P48237 UniProtKB Repeat 319 355 . . . Note=PPR 1 +P48237 UniProtKB Repeat 356 390 . . . Note=PPR 2 +##sequence-region P31384 1 837 +P31384 UniProtKB Chain 1 837 . . . ID=PRO_0000218577;Note=Glucose-repressible alcohol dehydrogenase transcriptional effector +P31384 UniProtKB Repeat 334 356 . . . Note=LRR 1 +P31384 UniProtKB Repeat 358 379 . . . Note=LRR 2 +P31384 UniProtKB Repeat 381 402 . . . Note=LRR 3 +P31384 UniProtKB Repeat 404 426 . . . Note=LRR 4 +P31384 UniProtKB Repeat 427 447 . . . Note=LRR 5 +P31384 UniProtKB Compositional bias 15 24 . . . Note=Poly-Gln +P31384 UniProtKB Compositional bias 77 103 . . . Note=Asn-rich +P31384 UniProtKB Compositional bias 89 103 . . . Note=Poly-Asn +P31384 UniProtKB Compositional bias 190 206 . . . Note=Gln-rich +P31384 UniProtKB Metal binding 556 556 . . . Note=Magnesium +P31384 UniProtKB Modified residue 33 33 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P31384 UniProtKB Modified residue 278 278 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P31384 UniProtKB Modified residue 285 285 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P31384 UniProtKB Mutagenesis 556 556 . . . Note=Loss of activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11889047;Dbxref=PMID:11889047 +P31384 UniProtKB Mutagenesis 713 713 . . . Note=Strongly reduces activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11889047;Dbxref=PMID:11889047 +P31384 UniProtKB Mutagenesis 780 780 . . . Note=Reduces activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11889047;Dbxref=PMID:11889047 +P31384 UniProtKB Mutagenesis 818 818 . . . Note=Loss of activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11889047;Dbxref=PMID:11889047 +P31384 UniProtKB Sequence conflict 544 544 . . . Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31384 UniProtKB Sequence conflict 803 803 . . . Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31384 UniProtKB Turn 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Helix 144 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Helix 155 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Helix 176 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Helix 245 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Beta strand 338 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Helix 351 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Helix 374 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Beta strand 384 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Helix 399 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Beta strand 406 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Helix 441 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Helix 515 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Turn 520 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Helix 528 531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Helix 533 546 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Beta strand 550 554 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Helix 559 563 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Turn 564 566 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Beta strand 600 602 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Helix 800 803 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Beta strand 807 811 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P31384 UniProtKB Beta strand 816 818 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +##sequence-region Q12127 1 133 +Q12127 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10322008;Dbxref=PMID:10322008 +Q12127 UniProtKB Chain 19 112 . . . ID=PRO_0000020879;Note=Covalently-linked cell wall protein 12 +Q12127 UniProtKB Propeptide 113 133 . . . ID=PRO_0000020880;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12127 UniProtKB Repeat 75 88 . . . Note=1 +Q12127 UniProtKB Repeat 91 103 . . . Note=2 +Q12127 UniProtKB Lipidation 112 112 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12127 UniProtKB Glycosylation 21 21 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17315267;Dbxref=PMID:17315267 +Q12127 UniProtKB Glycosylation 23 23 . . . Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243 +Q12127 UniProtKB Glycosylation 24 24 . . . Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243 +Q12127 UniProtKB Glycosylation 26 26 . . . Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243 +Q12127 UniProtKB Glycosylation 28 28 . . . Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243 +Q12127 UniProtKB Glycosylation 31 31 . . . Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243 +Q12127 UniProtKB Glycosylation 32 32 . . . Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243 +Q12127 UniProtKB Glycosylation 33 33 . . . Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243 +Q12127 UniProtKB Glycosylation 36 36 . . . Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243 +Q12127 UniProtKB Glycosylation 38 38 . . . Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243 +Q12127 UniProtKB Glycosylation 39 39 . . . Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243 +Q12127 UniProtKB Glycosylation 46 46 . . . Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243 +Q12127 UniProtKB Glycosylation 48 48 . . . Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15165243;Dbxref=PMID:15165243 +Q12127 UniProtKB Glycosylation 81 81 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17315267;Dbxref=PMID:17315267 +Q12127 UniProtKB Glycosylation 97 97 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17315267;Dbxref=PMID:17315267 +Q12127 UniProtKB Cross-link 80 80 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P32457 1 520 +P32457 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +P32457 UniProtKB Chain 2 520 . . . ID=PRO_0000173496;Note=Cell division control protein 3 +P32457 UniProtKB Domain 116 411 . . . Note=Septin-type G +P32457 UniProtKB Nucleotide binding 126 133 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32457 UniProtKB Nucleotide binding 287 295 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32457 UniProtKB Coiled coil 427 508 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32457 UniProtKB Binding site 207 207 . . . Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32457 UniProtKB Binding site 344 344 . . . Note=GTP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32457 UniProtKB Binding site 360 360 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32457 UniProtKB Site 415 415 . . . Note=Not sumoylated +P32457 UniProtKB Site 443 443 . . . Note=Not sumoylated +P32457 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +P32457 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P32457 UniProtKB Modified residue 9 9 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P32457 UniProtKB Modified residue 47 47 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32457 UniProtKB Modified residue 60 60 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32457 UniProtKB Modified residue 77 77 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32457 UniProtKB Modified residue 175 175 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32457 UniProtKB Modified residue 468 468 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32457 UniProtKB Modified residue 509 509 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32457 UniProtKB Cross-link 4 4 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) +P32457 UniProtKB Cross-link 11 11 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) +P32457 UniProtKB Cross-link 30 30 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) +P32457 UniProtKB Cross-link 63 63 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15166219,ECO:0000269|PubMed:15542864;Dbxref=PMID:15166219,PMID:15542864 +P32457 UniProtKB Cross-link 287 287 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) +P32457 UniProtKB Mutagenesis 4 4 . . . Note=Abolishes sumoylation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10579719;Dbxref=PMID:10579719 +P32457 UniProtKB Mutagenesis 11 11 . . . Note=Abolishes sumoylation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10579719;Dbxref=PMID:10579719 +P32457 UniProtKB Mutagenesis 287 287 . . . Note=Abolishes sumoylation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10579719;Dbxref=PMID:10579719 +P32457 UniProtKB Mutagenesis 415 415 . . . Note=No effect on sumoylation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10579719;Dbxref=PMID:10579719 +P32457 UniProtKB Mutagenesis 443 443 . . . Note=No effect on sumoylation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10579719;Dbxref=PMID:10579719 +P32457 UniProtKB Sequence conflict 431 431 . . . Note=Q->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06697 1 393 +Q06697 UniProtKB Chain 1 393 . . . ID=PRO_0000238580;Note=Cell division control protein 73 +Q06697 UniProtKB Modified residue 114 114 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06697 UniProtKB Modified residue 150 150 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06697 UniProtKB Beta strand 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46 +Q06697 UniProtKB Beta strand 248 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DM4 +Q06697 UniProtKB Turn 252 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46 +Q06697 UniProtKB Helix 255 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46 +Q06697 UniProtKB Helix 267 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46 +Q06697 UniProtKB Beta strand 276 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46 +Q06697 UniProtKB Beta strand 287 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46 +Q06697 UniProtKB Beta strand 291 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46 +Q06697 UniProtKB Helix 305 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46 +Q06697 UniProtKB Beta strand 311 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46 +Q06697 UniProtKB Helix 320 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46 +Q06697 UniProtKB Beta strand 326 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46 +Q06697 UniProtKB Helix 331 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46 +Q06697 UniProtKB Beta strand 338 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46 +Q06697 UniProtKB Helix 352 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46 +Q06697 UniProtKB Beta strand 357 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46 +Q06697 UniProtKB Helix 369 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DM4 +Q06697 UniProtKB Helix 372 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V46 +##sequence-region P41733 1 394 +P41733 UniProtKB Chain 1 394 . . . ID=PRO_0000121398;Note=GPI transamidase component GAB1 +P41733 UniProtKB Topological domain 1 135 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41733 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41733 UniProtKB Topological domain 157 160 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41733 UniProtKB Transmembrane 161 181 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41733 UniProtKB Topological domain 182 190 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41733 UniProtKB Transmembrane 191 211 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41733 UniProtKB Topological domain 212 224 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41733 UniProtKB Transmembrane 225 245 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41733 UniProtKB Topological domain 246 250 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41733 UniProtKB Transmembrane 251 271 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41733 UniProtKB Topological domain 272 297 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41733 UniProtKB Transmembrane 298 318 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41733 UniProtKB Topological domain 319 324 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41733 UniProtKB Transmembrane 325 345 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41733 UniProtKB Topological domain 346 351 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41733 UniProtKB Transmembrane 352 372 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41733 UniProtKB Topological domain 373 394 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41733 UniProtKB Region 235 255 . . . Note=May be involved in recognition of long-chain fatty acids in GPI;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P17106 1 351 +P17106 UniProtKB Chain 1 351 . . . ID=PRO_0000127161;Note=Centromere-binding protein 1 +P17106 UniProtKB Domain 222 270 . . . Note=bHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981 +P17106 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P17106 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P17106 UniProtKB Modified residue 48 48 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P17106 UniProtKB Modified residue 84 84 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P17106 UniProtKB Modified residue 138 138 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P17106 UniProtKB Sequence conflict 144 144 . . . Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17106 UniProtKB Sequence conflict 168 168 . . . Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17106 UniProtKB Sequence conflict 262 262 . . . Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17106 UniProtKB Sequence conflict 262 262 . . . Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17106 UniProtKB Sequence conflict 262 262 . . . Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03702 1 353 +Q03702 UniProtKB Metal binding 293 293 . . . Note=Magnesium +Q03702 UniProtKB Metal binding 294 294 . . . Note=Magnesium +Q03702 UniProtKB Mutagenesis 79 79 . . . Note=>200-fold decrease in activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168 +Q03702 UniProtKB Mutagenesis 145 145 . . . Note=>200-fold decrease in activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168 +Q03702 UniProtKB Mutagenesis 146 146 . . . Note=100-fold decrease in activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168 +Q03702 UniProtKB Mutagenesis 147 147 . . . Note=70-fold decrease in activity. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168 +Q03702 UniProtKB Mutagenesis 150 150 . . . Note=4-fold decrease in activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168 +Q03702 UniProtKB Mutagenesis 231 231 . . . Note=>200-fold decrease in activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168 +Q03702 UniProtKB Mutagenesis 231 231 . . . Note=47-fold decrease in activity. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168 +Q03702 UniProtKB Mutagenesis 291 291 . . . Note=>200-fold decrease in activity. K->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168 +Q03702 UniProtKB Mutagenesis 292 292 . . . Note=80-fold decrease in activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168 +Q03702 UniProtKB Mutagenesis 293 293 . . . Note=>200-fold decrease in activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168 +Q03702 UniProtKB Mutagenesis 294 294 . . . Note=>200-fold decrease in activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10825168;Dbxref=PMID:10825168 +##sequence-region P38273 1 704 +P38273 UniProtKB Chain 1 704 . . . ID=PRO_0000202491;Note=Vacuolar fusion protein CCZ1 +##sequence-region Q06702 1 301 +Q06702 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06702 UniProtKB Chain 25 301 . . . ID=PRO_0000024826;Note=Chitin deacetylase 1 +Q06702 UniProtKB Domain 108 288 . . . Note=NodB homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01014 +Q06702 UniProtKB Glycosylation 26 26 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06702 UniProtKB Glycosylation 50 50 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06702 UniProtKB Glycosylation 68 68 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06702 UniProtKB Glycosylation 189 189 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P25342 1 322 +P25342 UniProtKB Chain 1 322 . . . ID=PRO_0000173498;Note=Cell division control protein 10 +P25342 UniProtKB Domain 29 302 . . . Note=Septin-type G +P25342 UniProtKB Nucleotide binding 39 46 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25342 UniProtKB Nucleotide binding 180 188 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25342 UniProtKB Binding site 74 74 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25342 UniProtKB Binding site 100 100 . . . Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25342 UniProtKB Binding site 236 236 . . . Note=GTP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25342 UniProtKB Binding site 251 251 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25342 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P25342 UniProtKB Modified residue 216 216 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +##sequence-region P32468 1 407 +P32468 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32468 UniProtKB Chain 2 407 . . . ID=PRO_0000173500;Note=Cell division control protein 12 +P32468 UniProtKB Domain 31 314 . . . Note=Septin-type G +P32468 UniProtKB Nucleotide binding 41 48 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32468 UniProtKB Nucleotide binding 180 188 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32468 UniProtKB Coiled coil 344 406 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32468 UniProtKB Binding site 75 75 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32468 UniProtKB Binding site 101 101 . . . Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32468 UniProtKB Binding site 247 247 . . . Note=GTP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32468 UniProtKB Binding site 263 263 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32468 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P09798 1 840 +P09798 UniProtKB Chain 1 840 . . . ID=PRO_0000106269;Note=Anaphase-promoting complex subunit CDC16 +P09798 UniProtKB Repeat 229 260 . . . Note=TPR 1 +P09798 UniProtKB Repeat 263 288 . . . Note=TPR 2 +P09798 UniProtKB Repeat 296 319 . . . Note=TPR 3 +P09798 UniProtKB Repeat 357 388 . . . Note=TPR 4 +P09798 UniProtKB Repeat 393 416 . . . Note=TPR 5 +P09798 UniProtKB Repeat 426 454 . . . Note=TPR 6 +P09798 UniProtKB Repeat 464 492 . . . Note=TPR 7 +P09798 UniProtKB Repeat 499 526 . . . Note=TPR 8 +P09798 UniProtKB Repeat 531 560 . . . Note=TPR 9 +P09798 UniProtKB Repeat 565 593 . . . Note=TPR 10 +P09798 UniProtKB Repeat 600 628 . . . Note=TPR 11 +P09798 UniProtKB Repeat 633 665 . . . Note=TPR 12 +P09798 UniProtKB Repeat 671 703 . . . Note=TPR 13 +P09798 UniProtKB Repeat 708 737 . . . Note=TPR 14 +P09798 UniProtKB Compositional bias 209 220 . . . Note=Poly-Thr +P09798 UniProtKB Mutagenesis 44 44 . . . Note=Abolishes phosphorylation%3B when associated with A-59%3B A-95%3B A-103%3B A-115 and A-406. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279 +P09798 UniProtKB Mutagenesis 59 59 . . . Note=Abolishes phosphorylation%3B when associated with A-44%3B A-95%3B A-103%3B A-115 and A-406. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279 +P09798 UniProtKB Mutagenesis 95 95 . . . Note=Abolishes phosphorylation%3B when associated with A-44%3B A-59%3B A-103%3B A-115 and A-406. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279 +P09798 UniProtKB Mutagenesis 103 103 . . . Note=Abolishes phosphorylation%3B when associated with A-44%3B A-59%3B A-95%3B A-115 and A-406. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279 +P09798 UniProtKB Mutagenesis 115 115 . . . Note=Abolishes phosphorylation%3B when associated with A-44%3B A-59%3B A-95%3B A-103 and A-406. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279 +P09798 UniProtKB Mutagenesis 406 406 . . . Note=Abolishes phosphorylation%3B when associated with A-44%3B A-59%3B A-95%3B A-103 and A-115. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10871279;Dbxref=PMID:10871279 +P09798 UniProtKB Mutagenesis 482 482 . . . Note=In CDC16-264%3B G2/M cell cycle arrest at 36 degrees Celsius. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9660930;Dbxref=PMID:9660930 +P09798 UniProtKB Mutagenesis 530 530 . . . Note=In CDC16-183%3B G2/M cell cycle arrest at 37 degrees Celsius. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12928868;Dbxref=PMID:12928868 +P09798 UniProtKB Mutagenesis 557 557 . . . Note=In CDC16-1%3B G2/M cell cycle arrest at 36 degrees Celsius. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9660930;Dbxref=PMID:9660930 +##sequence-region P16522 1 626 +P16522 UniProtKB Chain 1 626 . . . ID=PRO_0000106272;Note=Anaphase-promoting complex subunit CDC23 +P16522 UniProtKB Repeat 215 248 . . . Note=TPR 1 +P16522 UniProtKB Repeat 295 328 . . . Note=TPR 2 +P16522 UniProtKB Repeat 329 362 . . . Note=TPR 3 +P16522 UniProtKB Repeat 363 396 . . . Note=TPR 4 +P16522 UniProtKB Repeat 397 430 . . . Note=TPR 5 +P16522 UniProtKB Repeat 431 464 . . . Note=TPR 6 +P16522 UniProtKB Repeat 465 498 . . . Note=TPR 7 +P16522 UniProtKB Repeat 499 532 . . . Note=TPR 8 +P16522 UniProtKB Repeat 536 569 . . . Note=TPR 9 +P16522 UniProtKB Modified residue 59 59 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:10871279;Dbxref=PMID:18407956,PMID:10871279 +P16522 UniProtKB Mutagenesis 39 39 . . . Note=In CDC23-50%3B G2/M cell cycle arrest at 37 degrees Celsius. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 42 42 . . . Note=In CDC23-54%3B G2/M cell cycle arrest at 37 degrees Celsius. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 80 80 . . . Note=In CDC23-44%3B G2/M cell cycle arrest at 37 degrees Celsius. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 85 85 . . . Note=In CDC23-51%3B G2/M cell cycle arrest at 37 degrees Celsius. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 93 93 . . . Note=In CDC23-52%3B G2/M cell cycle arrest at 37 degrees Celsius. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 94 94 . . . Note=In CDC23-4%3B G2/M cell cycle arrest at 36 degrees Celsius. T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 103 103 . . . Note=In CDC23-40%3B G2/M cell cycle arrest at 37 degrees Celsius%3B when associated with V-573. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 114 114 . . . Note=In CDC23-53%3B G2/M cell cycle arrest at 37 degrees Celsius. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 114 114 . . . Note=In CDC23-41%3B G2/M cell cycle arrest at 37 degrees Celsius. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 123 123 . . . Note=In CDC23-6%3B G2/M cell cycle arrest at 36 degrees Celsius. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 213 213 . . . Note=In CDC23-47%3B G2/M cell cycle arrest at 37 degrees Celsius%3B when associated with W-583. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 306 306 . . . Note=In CDC23-49%3B G2/M cell cycle arrest at 37 degrees Celsius%3B when associated with P-326. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 326 326 . . . Note=In CDC23-49%3B G2/M cell cycle arrest at 37 degrees Celsius%3B when associated with E-306. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 398 398 . . . Note=In CDC23-37%3B G2/M cell cycle arrest at 30 degrees Celsius. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 404 404 . . . Note=In CDC23-39%3B G2/M cell cycle arrest at 37 degrees Celsius. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 439 439 . . . Note=In CDC23-2%3B G2/M cell cycle arrest at 36 degrees Celsius. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 472 472 . . . Note=In CDC23-1%3B G2/M cell cycle arrest at 36 degrees Celsius. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 485 485 . . . Note=In CDC23-56%3B G2/M cell cycle arrest at 37 degrees Celsius. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 573 573 . . . Note=In CDC23-40%3B G2/M cell cycle arrest at 37 degrees Celsius%3B when associated with R-103. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8423787;Dbxref=PMID:8423787 +P16522 UniProtKB Mutagenesis 583 626 . . . Note=In CDC23-47%3B G2/M cell cycle arrest at 37 degrees Celsius%3B when associated with G-213. Missing +##sequence-region P06704 1 161 +P06704 UniProtKB Chain 1 161 . . . ID=PRO_0000073577;Note=Cell division control protein 31 +P06704 UniProtKB Domain 20 55 . . . Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P06704 UniProtKB Domain 56 91 . . . Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P06704 UniProtKB Domain 93 128 . . . Note=EF-hand 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P06704 UniProtKB Domain 129 161 . . . Note=EF-hand 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P06704 UniProtKB Calcium binding 33 44 . . . Note=1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P06704 UniProtKB Calcium binding 142 153 . . . Note=2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P06704 UniProtKB Modified residue 130 130 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P06704 UniProtKB Sequence conflict 77 77 . . . Note=K->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06704 UniProtKB Sequence conflict 110 110 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06704 UniProtKB Turn 10 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB +P06704 UniProtKB Helix 19 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB +P06704 UniProtKB Beta strand 36 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB +P06704 UniProtKB Helix 42 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB +P06704 UniProtKB Helix 58 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB +P06704 UniProtKB Beta strand 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB +P06704 UniProtKB Helix 78 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB +P06704 UniProtKB Helix 94 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB +P06704 UniProtKB Beta strand 110 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB +P06704 UniProtKB Helix 115 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB +P06704 UniProtKB Helix 131 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB +P06704 UniProtKB Beta strand 143 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB +P06704 UniProtKB Helix 151 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB +##sequence-region P53082 1 120 +P53082 UniProtKB Chain 1 120 . . . ID=PRO_0000201232;Note=BolA-like protein 2 +##sequence-region P25356 1 2167 +P25356 UniProtKB Chain 1 2167 . . . ID=PRO_0000050887;Note=Beige protein homolog 1 +P25356 UniProtKB Domain 1368 1499 . . . Note=BEACH-type PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01119 +P25356 UniProtKB Domain 1545 1839 . . . Note=BEACH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00026 +P25356 UniProtKB Repeat 1927 1965 . . . Note=WD 1 +P25356 UniProtKB Repeat 1976 2015 . . . Note=WD 2 +P25356 UniProtKB Repeat 2017 2054 . . . Note=WD 3 +P25356 UniProtKB Repeat 2072 2111 . . . Note=WD 4 +P25356 UniProtKB Repeat 2129 2167 . . . Note=WD 5 +P25356 UniProtKB Cross-link 1667 1667 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25356 UniProtKB Sequence conflict 1893 1893 . . . Note=F->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P26448 1 306 +P26448 UniProtKB Chain 1 306 . . . ID=PRO_0000208008;Note=Mitotic check point protein BUB2 +P26448 UniProtKB Domain 37 235 . . . Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163 +##sequence-region P27637 1 709 +P27637 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P27637 UniProtKB Chain 2 707 . . . ID=PRO_0000065012;Note=Bud site selection protein 14 +P27637 UniProtKB Domain 259 320 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P27637 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P27637 UniProtKB Modified residue 159 159 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P27637 UniProtKB Modified residue 160 160 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P27637 UniProtKB Modified residue 162 162 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P27637 UniProtKB Modified residue 177 177 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P27637 UniProtKB Modified residue 212 212 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P27637 UniProtKB Modified residue 222 222 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P27637 UniProtKB Modified residue 376 376 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P27637 UniProtKB Modified residue 378 378 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P27637 UniProtKB Modified residue 401 401 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P27637 UniProtKB Modified residue 507 507 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P27637 UniProtKB Modified residue 655 655 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P27637 UniProtKB Modified residue 658 658 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P27637 UniProtKB Modified residue 670 670 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P27637 UniProtKB Sequence conflict 439 439 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27637 UniProtKB Sequence conflict 439 439 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27637 UniProtKB Sequence conflict 573 595 . . . Note=KDISQYIHAKSKIEETTNVENTE->RTFTYIMQNRKLRDNKRGKHR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27637 UniProtKB Sequence conflict 573 595 . . . Note=KDISQYIHAKSKIEETTNVENTE->RTFTYIMQNRKLRDNKRGKHR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27637 UniProtKB Sequence conflict 609 609 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27637 UniProtKB Sequence conflict 609 609 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47158 1 497 +P47158 UniProtKB Transit peptide 1 27 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47158 UniProtKB Chain 28 497 . . . ID=PRO_0000203117;Note=Putative transferase CAF17%2C mitochondrial +##sequence-region P53934 1 400 +P53934 UniProtKB Chain 1 400 . . . ID=PRO_0000203441;Note=Carnosine N-methyltransferase +P53934 UniProtKB Natural variant 42 42 . . . Note=In strain: SK1. A->E +P53934 UniProtKB Natural variant 154 154 . . . Note=In strain: SK1. V->M +P53934 UniProtKB Natural variant 317 317 . . . Note=In strain: SK1. E->D +##sequence-region P06115 1 562 +P06115 UniProtKB Chain 1 562 . . . ID=PRO_0000084929;Note=Catalase T +P06115 UniProtKB Active site 64 64 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10013 +P06115 UniProtKB Active site 137 137 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10013 +P06115 UniProtKB Metal binding 351 351 . . . Note=Iron (heme axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06115 UniProtKB Sequence conflict 429 429 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06115 UniProtKB Sequence conflict 539 539 . . . Note=C->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32504 1 956 +P32504 UniProtKB Chain 1 956 . . . ID=PRO_0000089369;Note=Centromere DNA-binding protein complex CBF3 subunit A +P32504 UniProtKB Modified residue 566 566 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32504 UniProtKB Modified residue 706 706 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32504 UniProtKB Sequence conflict 418 418 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32504 UniProtKB Sequence conflict 774 774 . . . Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32504 UniProtKB Helix 45 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Turn 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 82 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Turn 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 108 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 148 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 184 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Turn 198 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Turn 202 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 208 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 228 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 236 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Beta strand 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Beta strand 249 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Beta strand 266 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 278 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 282 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Turn 298 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 309 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Turn 314 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 318 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Beta strand 321 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 335 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 356 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Beta strand 368 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 371 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 380 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 390 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 396 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 401 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 429 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 438 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 447 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 452 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 483 486 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 488 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 493 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 504 506 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Turn 518 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 521 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +P32504 UniProtKB Helix 527 531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ACO +##sequence-region P33322 1 483 +P33322 UniProtKB Chain 1 483 . . . ID=PRO_0000121982;Note=H/ACA ribonucleoprotein complex subunit 4 +P33322 UniProtKB Domain 266 341 . . . Note=PUA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00161 +P33322 UniProtKB Repeat 434 436 . . . Note=1 +P33322 UniProtKB Repeat 437 439 . . . Note=2 +P33322 UniProtKB Repeat 440 442 . . . Note=3 +P33322 UniProtKB Repeat 443 445 . . . Note=4 +P33322 UniProtKB Repeat 446 448 . . . Note=5 +P33322 UniProtKB Repeat 449 451 . . . Note=6 +P33322 UniProtKB Repeat 452 454 . . . Note=7 +P33322 UniProtKB Repeat 455 457 . . . Note=8 +P33322 UniProtKB Repeat 458 460 . . . Note=9 +P33322 UniProtKB Repeat 461 463 . . . Note=10 +P33322 UniProtKB Region 434 463 . . . Note=10 X 3 AA tandem repeats of K-K-[DE] +P33322 UniProtKB Active site 95 95 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33322 UniProtKB Modified residue 47 47 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33322 UniProtKB Modified residue 378 378 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P33322 UniProtKB Cross-link 9 9 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P33322 UniProtKB Cross-link 267 267 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P33322 UniProtKB Mutagenesis 65 65 . . . Note=Reduced pseudouridylation of rRNA and reduced snoRNA levels. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523634;Dbxref=PMID:10523634 +P33322 UniProtKB Mutagenesis 94 94 . . . Note=Reduced pseudouridylation of rRNA. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523634;Dbxref=PMID:10523634 +P33322 UniProtKB Mutagenesis 95 95 . . . Note=Reduced pseudouridylation of rRNA. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523634;Dbxref=PMID:10523634 +P33322 UniProtKB Helix 24 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Helix 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Beta strand 32 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Helix 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Helix 53 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Beta strand 60 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Beta strand 68 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Helix 72 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Beta strand 88 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Beta strand 94 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UAI +P33322 UniProtKB Beta strand 99 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Helix 107 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Helix 113 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Beta strand 121 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Helix 138 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Beta strand 148 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Beta strand 165 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Turn 179 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Beta strand 183 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Helix 196 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Beta strand 211 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Helix 233 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Helix 250 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Beta strand 256 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UAI +P33322 UniProtKB Helix 259 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Beta strand 268 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Helix 273 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Helix 276 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Beta strand 283 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Helix 287 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Beta strand 290 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Beta strand 302 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Beta strand 312 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Helix 322 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Beta strand 329 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P33322 UniProtKB Helix 355 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZV0 +##sequence-region P14066 1 229 +P14066 UniProtKB Transit peptide 1 25 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1657414;Dbxref=PMID:1657414 +P14066 UniProtKB Chain 26 229 . . . ID=PRO_0000020850;Note=Cytochrome b translational activator protein CBS1%2C mitochondrial +P14066 UniProtKB Mutagenesis 98 98 . . . Note=Loss of function%2C causes respiratory deficiency. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10669873;Dbxref=PMID:10669873 +P14066 UniProtKB Mutagenesis 100 100 . . . Note=In CBS1-1%2C which is respiratory deficient. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10669873;Dbxref=PMID:10669873 +P14066 UniProtKB Mutagenesis 124 124 . . . Note=Loss of function%2C causes respiratory deficiency. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10669873;Dbxref=PMID:10669873 +P14066 UniProtKB Mutagenesis 129 129 . . . Note=Loss of function%2C causes respiratory deficiency. F->S%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10669873;Dbxref=PMID:10669873 +##sequence-region P50077 1 2039 +P50077 UniProtKB Chain 1 2039 . . . ID=PRO_0000054106;Note=Calcium-channel protein CCH1 +P50077 UniProtKB Transmembrane 346 366 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 384 404 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 563 583 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 658 678 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 691 711 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 766 786 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 809 829 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 841 861 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 904 924 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 942 962 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 978 998 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 1207 1227 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 1247 1267 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 1277 1297 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 1340 1360 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 1408 1428 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 1452 1472 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 1529 1549 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 1554 1574 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 1596 1616 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 1618 1638 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 1654 1674 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Transmembrane 1748 1768 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50077 UniProtKB Domain 1787 1822 . . . Note=EF-hand;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P50077 UniProtKB Modified residue 284 284 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P50077 UniProtKB Sequence conflict 1185 1185 . . . Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P50077 UniProtKB Sequence conflict 1203 1203 . . . Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P00431 1 361 +P00431 UniProtKB Transit peptide 1 67 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6257176;Dbxref=PMID:6257176 +P00431 UniProtKB Chain 68 361 . . . ID=PRO_0000023634;Note=Cytochrome c peroxidase%2C mitochondrial +P00431 UniProtKB Active site 119 119 . . . Note=Proton acceptor +P00431 UniProtKB Active site 258 258 . . . Note=Tryptophan radical intermediate +P00431 UniProtKB Metal binding 242 242 . . . Note=Iron (heme axial ligand) +P00431 UniProtKB Site 115 115 . . . Note=Transition state stabilizer +P00431 UniProtKB Modified residue 220 220 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P00431 UniProtKB Natural variant 33 33 . . . Note=In allele 2. A->AA +P00431 UniProtKB Natural variant 120 120 . . . Note=In allele 2. T->I +P00431 UniProtKB Natural variant 219 219 . . . Note=In allele 2. D->G +P00431 UniProtKB Mutagenesis 258 258 . . . Note=Substantially diminished activity. W->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2851317;Dbxref=PMID:2851317 +P00431 UniProtKB Sequence conflict 41 41 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00431 UniProtKB Sequence conflict 62 62 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00431 UniProtKB Sequence conflict 145 146 . . . Note=ND->DN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00431 UniProtKB Sequence conflict 231 231 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00431 UniProtKB Sequence conflict 273 273 . . . Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00431 UniProtKB Helix 83 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Turn 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IA8 +P00431 UniProtKB Helix 103 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Helix 110 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Turn 126 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Beta strand 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Helix 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Helix 141 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Helix 147 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Turn 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Helix 153 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Beta strand 167 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B0Z +P00431 UniProtKB Helix 171 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Helix 202 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Turn 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MKR +P00431 UniProtKB Helix 218 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Turn 227 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Helix 232 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Helix 240 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Beta strand 244 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Helix 249 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Beta strand 256 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Beta strand 262 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M23 +P00431 UniProtKB Helix 268 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Beta strand 278 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Beta strand 284 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PCC +P00431 UniProtKB Beta strand 288 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Turn 293 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMT +P00431 UniProtKB Beta strand 296 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CMT +P00431 UniProtKB Helix 300 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Helix 309 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Helix 322 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +P00431 UniProtKB Beta strand 345 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCN +P00431 UniProtKB Helix 356 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E2O +##sequence-region Q7LHD1 1 136 +Q7LHD1 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q7LHD1 UniProtKB Chain 19 115 . . . ID=PRO_0000226148;Note=Putative covalently bound cell wall protein 22 +Q7LHD1 UniProtKB Propeptide 116 136 . . . ID=PRO_0000226149;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q7LHD1 UniProtKB Compositional bias 23 114 . . . Note=Thr-rich +Q7LHD1 UniProtKB Lipidation 115 115 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q7LHD1 UniProtKB Glycosylation 21 21 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q7LHD1 UniProtKB Glycosylation 82 82 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P21560 1 335 +P21560 UniProtKB Transit peptide 1 38 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21560 UniProtKB Chain 39 335 . . . ID=PRO_0000004775;Note=Protein CBP3%2C mitochondrial +P21560 UniProtKB Transmembrane 152 169 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P19073 1 191 +P19073 UniProtKB Chain 1 188 . . . ID=PRO_0000198955;Note=Cell division control protein 42 +P19073 UniProtKB Propeptide 189 191 . . . ID=PRO_0000281285;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19073 UniProtKB Nucleotide binding 10 17 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19073 UniProtKB Nucleotide binding 57 61 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19073 UniProtKB Nucleotide binding 115 118 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19073 UniProtKB Motif 32 40 . . . Note=Effector region;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19073 UniProtKB Modified residue 188 188 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19073 UniProtKB Lipidation 188 188 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19073 UniProtKB Mutagenesis 12 12 . . . Note=Enhances interaction with RGA1. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9178507;Dbxref=PMID:9178507 +P19073 UniProtKB Mutagenesis 58 58 . . . Note=Temperature-sensitive mutant. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9178507;Dbxref=PMID:9178507 +P19073 UniProtKB Mutagenesis 61 61 . . . Note=Enhances interaction with RGA1. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9178507;Dbxref=PMID:9178507 +P19073 UniProtKB Mutagenesis 71 71 . . . Note=Temperature-sensitive mutant. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9178507;Dbxref=PMID:9178507 +P19073 UniProtKB Mutagenesis 97 97 . . . Note=Temperature-sensitive mutant. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9178507;Dbxref=PMID:9178507 +P19073 UniProtKB Mutagenesis 118 118 . . . Note=Dramatically reduces interaction with RGA1. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9178507;Dbxref=PMID:9178507 +P19073 UniProtKB Mutagenesis 142 142 . . . Note=In CDC42-1%3B temperature-sensitive mutant. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9178507;Dbxref=PMID:9178507 +P19073 UniProtKB Mutagenesis 188 188 . . . Note=Enhances interaction with RGA1. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9178507;Dbxref=PMID:9178507 +P19073 UniProtKB Sequence conflict 189 189 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32458 1 415 +P32458 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +P32458 UniProtKB Chain 2 415 . . . ID=PRO_0000173499;Note=Cell division control protein 11 +P32458 UniProtKB Domain 19 298 . . . Note=Septin-type G +P32458 UniProtKB Nucleotide binding 29 36 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32458 UniProtKB Nucleotide binding 172 180 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32458 UniProtKB Coiled coil 354 414 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32458 UniProtKB Motif 12 19 . . . Note=Basic motif +P32458 UniProtKB Binding site 92 92 . . . Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32458 UniProtKB Binding site 230 230 . . . Note=GTP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32458 UniProtKB Binding site 247 247 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32458 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +P32458 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P32458 UniProtKB Modified residue 305 305 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P32458 UniProtKB Modified residue 327 327 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950 +P32458 UniProtKB Cross-link 412 412 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) +P32458 UniProtKB Mutagenesis 12 16 . . . Note=Loss of function%3B abolishes association with PI(4)P and PI(5)P. RKRKH->QQEQQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665577;Dbxref=PMID:12665577 +P32458 UniProtKB Mutagenesis 12 16 . . . Note=Loss of function%3B strongly decreases association with PI(4)P and PI(5)P. RKRKH->QQQQQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665577;Dbxref=PMID:12665577 +P32458 UniProtKB Mutagenesis 29 29 . . . Note=Abolishes GTP-binding%3B no strong effect in vivo. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665577;Dbxref=PMID:12665577 +P32458 UniProtKB Mutagenesis 32 32 . . . Note=Abolishes GTP-binding%3B no strong effect in vivo. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665577;Dbxref=PMID:12665577 +P32458 UniProtKB Mutagenesis 34 34 . . . Note=Abolishes GTP-binding%3B no strong effect in vivo. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665577;Dbxref=PMID:12665577 +P32458 UniProtKB Mutagenesis 35 35 . . . Note=Abolishes GTP-binding%3B no strong effect in vivo. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665577;Dbxref=PMID:12665577 +P32458 UniProtKB Mutagenesis 40 40 . . . Note=Temperature-sensitive%3B no effect at 23 degrees Celsius but loss of function at 37 degrees Celsius%3B abolishes interaction with itself. N->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665577;Dbxref=PMID:12665577 +P32458 UniProtKB Mutagenesis 230 230 . . . Note=Temperature-sensitive%3B no effect at 23 degrees Celsius but loss of function at 37 degrees Celsius. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665577;Dbxref=PMID:12665577 +P32458 UniProtKB Mutagenesis 412 412 . . . Note=Abolishes sumoylation in vitro. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10579719;Dbxref=PMID:10579719 +P32458 UniProtKB Beta strand 23 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Beta strand 31 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Turn 36 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Beta strand 69 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Beta strand 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Beta strand 85 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Helix 104 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Beta strand 137 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Beta strand 145 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Helix 151 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Turn 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Beta strand 166 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Helix 173 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Helix 178 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Beta strand 206 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Helix 213 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Beta strand 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Beta strand 263 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Helix 269 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +P32458 UniProtKB Helix 287 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AR1 +##sequence-region P14724 1 124 +P14724 UniProtKB Chain 1 124 . . . ID=PRO_0000089446;Note=Anaphase-promoting complex subunit CDC26 +P14724 UniProtKB Compositional bias 53 77 . . . Note=Asp-rich +P14724 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14724 UniProtKB Sequence conflict 50 50 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14724 UniProtKB Sequence conflict 121 124 . . . Note=IREE->TARNNSISAYAHAHAHAHASTFTFTYKISSL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P06101 1 506 +P06101 UniProtKB Chain 1 506 . . . ID=PRO_0000195067;Note=Hsp90 co-chaperone Cdc37 +P06101 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:17220467;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198,PMID:17220467 +P06101 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P06101 UniProtKB Modified residue 367 367 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P06101 UniProtKB Modified residue 466 466 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P06101 UniProtKB Modified residue 484 484 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P06101 UniProtKB Mutagenesis 14 14 . . . Note=Leads to osmosensitivity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17220467;Dbxref=PMID:17220467 +P06101 UniProtKB Sequence conflict 169 169 . . . Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12018 1 815 +Q12018 UniProtKB Chain 1 815 . . . ID=PRO_0000119805;Note=Cell division control protein 53 +Q12018 UniProtKB Region 9 280 . . . Note=Required for interaction with SKP1/CBF3D and F-box protein +Q12018 UniProtKB Region 448 748 . . . Note=Required for interaction with CDC34/UBC3 +Q12018 UniProtKB Cross-link 760 760 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13616 +Q12018 UniProtKB Mutagenesis 488 488 . . . Note=Prevents CDC34/UBC3 interaction. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9499404;Dbxref=PMID:9499404 +Q12018 UniProtKB Helix 735 762 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2P +Q12018 UniProtKB Beta strand 763 766 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2P +Q12018 UniProtKB Helix 767 778 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2P +Q12018 UniProtKB Turn 779 781 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2P +Q12018 UniProtKB Helix 786 798 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2P +Q12018 UniProtKB Beta strand 801 804 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2P +Q12018 UniProtKB Beta strand 808 813 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2P +##sequence-region P38910 1 106 +P38910 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38910 UniProtKB Chain 2 106 . . . ID=PRO_0000174922;Note=10 kDa heat shock protein%2C mitochondrial +P38910 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38910 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38910 UniProtKB Sequence conflict 82 82 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47818 1 322 +P47818 UniProtKB Chain 1 322 . . . ID=PRO_0000089394;Note=Protein CCC1 +P47818 UniProtKB Topological domain 1 99 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47818 UniProtKB Transmembrane 100 120 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47818 UniProtKB Topological domain 121 129 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47818 UniProtKB Transmembrane 130 150 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47818 UniProtKB Topological domain 151 236 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47818 UniProtKB Transmembrane 237 257 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47818 UniProtKB Topological domain 258 259 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47818 UniProtKB Transmembrane 260 280 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47818 UniProtKB Topological domain 281 300 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47818 UniProtKB Transmembrane 301 321 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47818 UniProtKB Topological domain 322 322 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47818 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47818 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47818 UniProtKB Modified residue 68 68 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P47818 UniProtKB Modified residue 71 71 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P47818 UniProtKB Modified residue 83 83 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P06182 1 269 +P06182 UniProtKB Chain 1 269 . . . ID=PRO_0000121718;Note=Cytochrome c heme lyase +P06182 UniProtKB Repeat 25 30 . . . Note=HRM 1 +P06182 UniProtKB Repeat 41 46 . . . Note=HRM 2 +##sequence-region P40202 1 249 +P40202 UniProtKB Chain 1 249 . . . ID=PRO_0000213542;Note=Superoxide dismutase 1 copper chaperone +P40202 UniProtKB Domain 7 70 . . . Note=HMA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P40202 UniProtKB Metal binding 16 16 . . . Note=Zinc%3B shared with apo-SOD1;Ontology_term=ECO:0000244,ECO:0000255,ECO:0000269;evidence=ECO:0000244|PDB:1JK9,ECO:0000255|PROSITE-ProRule:PRU00280,ECO:0000269|PubMed:11524675;Dbxref=PMID:11524675 +P40202 UniProtKB Metal binding 17 17 . . . Note=Copper 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P40202 UniProtKB Metal binding 20 20 . . . Note=Copper 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P40202 UniProtKB Metal binding 229 229 . . . Note=Copper 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P40202 UniProtKB Metal binding 231 231 . . . Note=Copper 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00280 +P40202 UniProtKB Disulfide bond 27 64 . . . Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1QUP,ECO:0000269|PubMed:7557423;Dbxref=PMID:7557423 +P40202 UniProtKB Disulfide bond 229 229 . . . Note=Interchain (with C-58 in apo-SOD1);Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1JK9,ECO:0000269|PubMed:24374639;Dbxref=PMID:24374639 +P40202 UniProtKB Helix 3 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QUP +P40202 UniProtKB Beta strand 7 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QUP +P40202 UniProtKB Beta strand 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK9 +P40202 UniProtKB Helix 20 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QUP +P40202 UniProtKB Beta strand 34 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QUP +P40202 UniProtKB Turn 41 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QUP +P40202 UniProtKB Beta strand 45 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QUP +P40202 UniProtKB Helix 54 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QUP +P40202 UniProtKB Beta strand 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QUP +P40202 UniProtKB Beta strand 79 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8 +P40202 UniProtKB Beta strand 100 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8 +P40202 UniProtKB Beta strand 113 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8 +P40202 UniProtKB Beta strand 127 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8 +P40202 UniProtKB Helix 142 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8 +P40202 UniProtKB Beta strand 148 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8 +P40202 UniProtKB Beta strand 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8 +P40202 UniProtKB Beta strand 161 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8 +P40202 UniProtKB Turn 165 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8 +P40202 UniProtKB Beta strand 169 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8 +P40202 UniProtKB Helix 182 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8 +P40202 UniProtKB Turn 185 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8 +P40202 UniProtKB Beta strand 188 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8 +P40202 UniProtKB Helix 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8 +P40202 UniProtKB Beta strand 202 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK9 +P40202 UniProtKB Beta strand 208 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJ8 +P40202 UniProtKB Beta strand 216 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QUP +P40202 UniProtKB Helix 236 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK9 +##sequence-region O13547 1 238 +O13547 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10322008;Dbxref=PMID:10322008 +O13547 UniProtKB Chain 23 217 . . . ID=PRO_0000020881;Note=Covalently-linked cell wall protein 14 +O13547 UniProtKB Propeptide 218 238 . . . ID=PRO_0000020882;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13547 UniProtKB Compositional bias 77 215 . . . Note=Ser-rich +O13547 UniProtKB Lipidation 217 217 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13547 UniProtKB Glycosylation 87 87 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13547 UniProtKB Cross-link 161 161 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q00684 1 551 +Q00684 UniProtKB Chain 1 551 . . . ID=PRO_0000094875;Note=Tyrosine-protein phosphatase CDC14 +Q00684 UniProtKB Active site 283 283 . . . Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10044 +Q00684 UniProtKB Modified residue 467 467 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q00684 UniProtKB Mutagenesis 253 253 . . . Note=Inactivates catalytic activity and leads to substrate retention. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21127052;Dbxref=PMID:21127052 +Q00684 UniProtKB Mutagenesis 280 280 . . . Note=Leads to temperature sensitivity. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21784165;Dbxref=PMID:21784165 +Q00684 UniProtKB Mutagenesis 283 283 . . . Note=Inactivates catalytic activity and leads to substrate retention. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21127052;Dbxref=PMID:21127052 +Q00684 UniProtKB Sequence conflict 118 118 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P26309 1 610 +P26309 UniProtKB Chain 1 610 . . . ID=PRO_0000050903;Note=APC/C activator protein CDC20 +P26309 UniProtKB Repeat 257 296 . . . Note=WD 1 +P26309 UniProtKB Repeat 299 338 . . . Note=WD 2 +P26309 UniProtKB Repeat 342 379 . . . Note=WD 3 +P26309 UniProtKB Repeat 383 422 . . . Note=WD 4 +P26309 UniProtKB Repeat 425 467 . . . Note=WD 5 +P26309 UniProtKB Repeat 469 519 . . . Note=WD 6 +P26309 UniProtKB Repeat 523 562 . . . Note=WD 7 +P26309 UniProtKB Motif 17 25 . . . Note=D-box +P26309 UniProtKB Motif 85 101 . . . Note=Bipartite nuclear localization signal +P26309 UniProtKB Motif 144 150 . . . Note=C-box +P26309 UniProtKB Motif 586 592 . . . Note=KEN box;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P26309 UniProtKB Mutagenesis 205 205 . . . Note=Confers spindle checkpoint resistance and diminishes binding to MAD2 and MAD3. Y->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9461437;Dbxref=PMID:9461437 +P26309 UniProtKB Mutagenesis 209 209 . . . Note=Confers spindle checkpoint resistance and diminishes binding to MAD2 and MAD3. P->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9461437;Dbxref=PMID:9461437 +P26309 UniProtKB Mutagenesis 210 210 . . . Note=Confers spindle checkpoint resistance and diminishes binding to MAD2 and MAD3. P->L%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9461437;Dbxref=PMID:9461437 +P26309 UniProtKB Sequence conflict 318 319 . . . Note=IG->MA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region O13297 1 549 +O13297 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +O13297 UniProtKB Chain 2 549 . . . ID=PRO_0000210119;Note=mRNA-capping enzyme subunit beta +O13297 UniProtKB Active site 223 223 . . . Note=N6-GMP-lysine intermediate +O13297 UniProtKB Site 280 280 . . . Note=Essential for dimer formation +O13297 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +O13297 UniProtKB Modified residue 15 15 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +O13297 UniProtKB Modified residue 124 124 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +O13297 UniProtKB Mutagenesis 280 280 . . . Note=Significant growth defects. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788946;Dbxref=PMID:12788946 +O13297 UniProtKB Mutagenesis 520 520 . . . Note=No growth. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788946;Dbxref=PMID:12788946 +O13297 UniProtKB Mutagenesis 523 523 . . . Note=Temperature sensitive growth phenotype. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788946;Dbxref=PMID:12788946 +O13297 UniProtKB Mutagenesis 524 524 . . . Note=Temperature sensitive growth phenotype. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788946;Dbxref=PMID:12788946 +O13297 UniProtKB Sequence conflict 242 242 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +O13297 UniProtKB Helix 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Turn 254 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +O13297 UniProtKB Beta strand 262 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Beta strand 274 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Helix 280 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Turn 298 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Helix 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Beta strand 304 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Beta strand 319 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Beta strand 330 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Beta strand 338 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Helix 345 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Helix 362 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Turn 365 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Beta strand 368 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Beta strand 391 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Beta strand 405 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Beta strand 425 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Beta strand 437 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +O13297 UniProtKB Helix 441 445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Beta strand 446 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8I +O13297 UniProtKB Beta strand 453 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Helix 464 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Beta strand 468 477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Beta strand 488 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Helix 499 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Turn 508 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +O13297 UniProtKB Helix 514 536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8H +##sequence-region P20437 1 546 +P20437 UniProtKB Chain 1 546 . . . ID=PRO_0000080411;Note=G1/S-specific cyclin CLN1 +##sequence-region P29029 1 562 +P29029 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1918080,ECO:0000269|PubMed:9748433;Dbxref=PMID:1918080,PMID:9748433 +P29029 UniProtKB Chain 21 562 . . . ID=PRO_0000011936;Note=Endochitinase +P29029 UniProtKB Region 21 327 . . . Note=Catalytic +P29029 UniProtKB Region 481 562 . . . Note=Chitin-binding%2C high affinity +P29029 UniProtKB Compositional bias 328 480 . . . Note=Ser/Thr-rich +P29029 UniProtKB Active site 157 157 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10053 +P29029 UniProtKB Glycosylation 553 553 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P29029 UniProtKB Natural variant 16 16 . . . Note=In strain: DBY939. L->P +P29029 UniProtKB Natural variant 23 23 . . . Note=In strain: DBY939 and SEY6210. R->S +P29029 UniProtKB Natural variant 321 321 . . . Note=In strain: DBY939. T->S +P29029 UniProtKB Natural variant 336 340 . . . Note=In strain: DBY939. Missing +P29029 UniProtKB Natural variant 399 399 . . . Note=In strain: DBY939. S->A +P29029 UniProtKB Natural variant 433 434 . . . Note=In strain: DBY939. PI->SL +P29029 UniProtKB Natural variant 461 461 . . . Note=In strain: DBY939. T->K +P29029 UniProtKB Natural variant 477 481 . . . Note=In strain: DBY939. Missing +P29029 UniProtKB Sequence conflict 168 168 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29029 UniProtKB Sequence conflict 168 168 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29029 UniProtKB Beta strand 28 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Helix 44 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Beta strand 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Beta strand 54 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Turn 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Helix 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Helix 87 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Beta strand 102 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Beta strand 110 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY4 +P29029 UniProtKB Helix 119 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Turn 143 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Beta strand 150 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Helix 164 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Beta strand 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Beta strand 183 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Beta strand 189 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Turn 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Helix 198 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Beta strand 207 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Beta strand 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Beta strand 219 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY5 +P29029 UniProtKB Helix 226 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Beta strand 243 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Beta strand 254 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Helix 263 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Beta strand 279 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Helix 287 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +P29029 UniProtKB Beta strand 294 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TXE +P29029 UniProtKB Helix 300 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UY2 +##sequence-region P32178 1 256 +P32178 UniProtKB Chain 1 256 . . . ID=PRO_0000119204;Note=Chorismate mutase +P32178 UniProtKB Domain 3 255 . . . Note=Chorismate mutase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00516 +P32178 UniProtKB Mutagenesis 226 226 . . . Note=Constitutively activated and feedback-resistant. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2646272;Dbxref=PMID:2646272 +P32178 UniProtKB Helix 6 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM +P32178 UniProtKB Helix 12 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM +P32178 UniProtKB Helix 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM +P32178 UniProtKB Beta strand 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CSM +P32178 UniProtKB Helix 59 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM +P32178 UniProtKB Helix 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM +P32178 UniProtKB Turn 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM +P32178 UniProtKB Helix 108 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM +P32178 UniProtKB Helix 114 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM +P32178 UniProtKB Helix 126 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM +P32178 UniProtKB Beta strand 130 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM +P32178 UniProtKB Helix 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CSM +P32178 UniProtKB Helix 140 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM +P32178 UniProtKB Helix 161 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM +P32178 UniProtKB Helix 173 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM +P32178 UniProtKB Helix 185 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM +P32178 UniProtKB Helix 195 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM +P32178 UniProtKB Beta strand 212 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CSM +P32178 UniProtKB Helix 227 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM +P32178 UniProtKB Helix 238 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CSM +P32178 UniProtKB Turn 252 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CSM +##sequence-region Q12114 1 671 +Q12114 UniProtKB Chain 1 671 . . . ID=PRO_0000089661;Note=Chitin biosynthesis protein CHS5 +Q12114 UniProtKB Domain 78 168 . . . Note=Fibronectin type-III;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 +Q12114 UniProtKB Domain 166 262 . . . Note=BRCT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033 +Q12114 UniProtKB Compositional bias 279 635 . . . Note=Glu-rich +Q12114 UniProtKB Compositional bias 645 671 . . . Note=Lys-rich +Q12114 UniProtKB Modified residue 305 305 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12114 UniProtKB Modified residue 338 338 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12114 UniProtKB Modified residue 362 362 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12114 UniProtKB Modified residue 365 365 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12114 UniProtKB Modified residue 383 383 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12114 UniProtKB Modified residue 384 384 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12114 UniProtKB Modified residue 573 573 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12114 UniProtKB Modified residue 579 579 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12114 UniProtKB Modified residue 590 590 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12114 UniProtKB Cross-link 584 584 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q12114 UniProtKB Beta strand 4 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q12114 UniProtKB Beta strand 19 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +Q12114 UniProtKB Beta strand 27 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q12114 UniProtKB Turn 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +Q12114 UniProtKB Beta strand 44 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IN3 +Q12114 UniProtKB Helix 57 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +Q12114 UniProtKB Beta strand 84 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8 +Q12114 UniProtKB Beta strand 94 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8 +Q12114 UniProtKB Beta strand 108 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8 +Q12114 UniProtKB Turn 126 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8 +Q12114 UniProtKB Beta strand 131 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8 +Q12114 UniProtKB Beta strand 142 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8 +Q12114 UniProtKB Beta strand 154 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8 +Q12114 UniProtKB Beta strand 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8 +Q12114 UniProtKB Helix 183 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8 +Q12114 UniProtKB Helix 189 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8 +Q12114 UniProtKB Beta strand 205 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8 +Q12114 UniProtKB Beta strand 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8 +Q12114 UniProtKB Helix 227 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8 +Q12114 UniProtKB Helix 243 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8 +Q12114 UniProtKB Helix 258 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8 +Q12114 UniProtKB Helix 266 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8 +Q12114 UniProtKB Helix 279 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8 +##sequence-region P38843 1 316 +P38843 UniProtKB Chain 1 316 . . . ID=PRO_0000202922;Note=Chitin synthase export chaperone +P38843 UniProtKB Transmembrane 62 82 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38843 UniProtKB Transmembrane 99 119 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38843 UniProtKB Transmembrane 130 150 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38843 UniProtKB Transmembrane 170 190 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38843 UniProtKB Transmembrane 200 220 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38843 UniProtKB Transmembrane 233 253 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38843 UniProtKB Transmembrane 266 286 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P35190 1 452 +P35190 UniProtKB Chain 1 452 . . . ID=PRO_0000080503;Note=PHO85 cyclin CLG1 +P35190 UniProtKB Compositional bias 395 401 . . . Note=Poly-Gln +##sequence-region Q03654 1 590 +Q03654 UniProtKB Chain 1 590 . . . ID=PRO_0000197107;Note=Pre-mRNA-splicing factor CEF1 +Q03654 UniProtKB Domain 1 60 . . . Note=HTH myb-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +Q03654 UniProtKB Domain 63 110 . . . Note=HTH myb-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +Q03654 UniProtKB DNA binding 33 56 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +Q03654 UniProtKB DNA binding 84 106 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +Q03654 UniProtKB Region 460 490 . . . Note=Interaction with PRP19 and self-interaction +Q03654 UniProtKB Compositional bias 238 321 . . . Note=Lys-rich +Q03654 UniProtKB Mutagenesis 33 33 . . . Note=No effect. Slower growth and thermosensitivity%3B when associated with G-84. Complete loss of function%3B when associated with G-52 and G-84. Complete loss of function%3B when associated with G-52%3B G-84 and G-102. W->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9632794;Dbxref=PMID:9632794 +Q03654 UniProtKB Mutagenesis 52 52 . . . Note=No effect. Slower growth and thermosensitivity%3B when associated with G-84. Complete loss of function%3B when associated with G-33 and G-84. Complete loss of function%3B when associated with G-33%3B G-84 and G-102. W->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11784857,ECO:0000269|PubMed:9632794;Dbxref=PMID:11784857,PMID:9632794 +Q03654 UniProtKB Mutagenesis 84 84 . . . Note=No effect. Slower growth and thermosensitivity%3B when associated with G-33 or G-52. Complete loss of function%3B when associated with G-33 and G-52 or G-52 and Y-102. Complete loss of function%3B when associated with G-33%3B G-52 and G-102. W->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11784857,ECO:0000269|PubMed:9632794;Dbxref=PMID:11784857,PMID:9632794 +Q03654 UniProtKB Mutagenesis 102 102 . . . Note=No effect. Slower growth and thermosensitivity%3B when associated with G-52 or G-84. Complete loss of function%3B when associated with G-33%3B G-52 and G-84. Y->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9632794;Dbxref=PMID:9632794 +Q03654 UniProtKB Sequence conflict 11 11 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03654 UniProtKB Sequence conflict 192 192 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03654 UniProtKB Helix 15 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q03654 UniProtKB Helix 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q03654 UniProtKB Helix 36 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q03654 UniProtKB Helix 45 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q03654 UniProtKB Helix 67 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q03654 UniProtKB Beta strand 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q03654 UniProtKB Helix 86 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q03654 UniProtKB Helix 95 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q03654 UniProtKB Helix 146 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q03654 UniProtKB Helix 165 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q03654 UniProtKB Turn 213 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q03654 UniProtKB Helix 233 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q03654 UniProtKB Helix 483 581 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q03654 UniProtKB Helix 583 586 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region Q12102 1 859 +Q12102 UniProtKB Chain 1 859 . . . ID=PRO_0000076204;Note=Cleavage factor two protein 2 +Q12102 UniProtKB Beta strand 3 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 10 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 18 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 25 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Turn 35 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 40 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 64 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 70 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 78 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 86 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 91 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 110 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 121 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 131 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Turn 143 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 149 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 163 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 173 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 208 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 223 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 243 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Turn 250 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 253 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 279 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Turn 284 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 288 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 297 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 302 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 310 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Turn 320 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 323 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 328 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 338 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 346 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 362 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 375 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 405 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 631 633 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 640 651 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 653 657 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 666 672 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 673 675 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 679 683 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 687 689 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Helix 692 700 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 704 707 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +Q12102 UniProtKB Beta strand 714 716 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I7X +##sequence-region P24868 1 471 +P24868 UniProtKB Chain 1 471 . . . ID=PRO_0000080403;Note=G2/mitotic-specific cyclin-1 +##sequence-region P24870 1 427 +P24870 UniProtKB Chain 1 427 . . . ID=PRO_0000080405;Note=G2/mitotic-specific cyclin-3 +P24870 UniProtKB Sequence conflict 48 48 . . . Note=D->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P30283 1 435 +P30283 UniProtKB Chain 1 435 . . . ID=PRO_0000080408;Note=S-phase entry cyclin-5 +##sequence-region P43634 1 648 +P43634 UniProtKB Chain 1 648 . . . ID=PRO_0000114942;Note=Activatory protein CHA4 +P43634 UniProtKB DNA binding 44 70 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P43634 UniProtKB Compositional bias 32 35 . . . Note=Poly-Asn +P43634 UniProtKB Compositional bias 48 52 . . . Note=Poly-Arg +P43634 UniProtKB Compositional bias 105 109 . . . Note=Poly-Ser +P43634 UniProtKB Compositional bias 195 198 . . . Note=Poly-Gln +P43634 UniProtKB Compositional bias 302 306 . . . Note=Poly-Ser +P43634 UniProtKB Modified residue 164 164 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P43634 UniProtKB Modified residue 166 166 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P22516 1 861 +P22516 UniProtKB Chain 1 861 . . . ID=PRO_0000055138;Note=ATP-dependent DNA helicase CHL1 +P22516 UniProtKB Domain 6 458 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P22516 UniProtKB Nucleotide binding 42 49 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P22516 UniProtKB Motif 393 396 . . . Note=DEAH box +P22516 UniProtKB Modified residue 86 86 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P22516 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P22516 UniProtKB Mutagenesis 47 47 . . . Note=No ATPase activity%3B increase in chromosome missegregation. G->A%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10931920;Dbxref=PMID:10931920 +P22516 UniProtKB Mutagenesis 48 48 . . . Note=No ATPase activity%3B increase in chromosome missegregation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10931920;Dbxref=PMID:10931920 +##sequence-region Q08032 1 650 +Q08032 UniProtKB Chain 1 650 . . . ID=PRO_0000192819;Note=Cell division control protein 45 +Q08032 UniProtKB Modified residue 453 453 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q08032 UniProtKB Sequence conflict 576 576 . . . Note=T->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P07834 1 779 +P07834 UniProtKB Chain 1 779 . . . ID=PRO_0000050899;Note=Cell division control protein 4 +P07834 UniProtKB Domain 272 319 . . . Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080 +P07834 UniProtKB Repeat 380 408 . . . Note=WD 1 +P07834 UniProtKB Repeat 420 449 . . . Note=WD 2 +P07834 UniProtKB Repeat 461 493 . . . Note=WD 3 +P07834 UniProtKB Repeat 528 556 . . . Note=WD 4 +P07834 UniProtKB Repeat 568 598 . . . Note=WD 5 +P07834 UniProtKB Repeat 630 658 . . . Note=WD 6 +P07834 UniProtKB Repeat 669 698 . . . Note=WD 7 +P07834 UniProtKB Motif 82 85 . . . Note=Nuclear localization signal +P07834 UniProtKB Modified residue 104 104 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07834 UniProtKB Mutagenesis 82 82 . . . Note=Prevents nuclear localization%3B when associated with A-83 and A-85. K->A +P07834 UniProtKB Mutagenesis 83 83 . . . Note=Prevents nuclear localization%3B when associated with A-82 and A-85. R->A +P07834 UniProtKB Mutagenesis 83 83 . . . Note=Prevents nuclear localization. R->G +P07834 UniProtKB Mutagenesis 85 85 . . . Note=Prevents nuclear localization%3B when associated with A-82 and A-83. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11080155;Dbxref=PMID:11080155 +P07834 UniProtKB Sequence conflict 460 460 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07834 UniProtKB Helix 228 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P63 +P07834 UniProtKB Helix 235 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P63 +P07834 UniProtKB Helix 242 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P63 +P07834 UniProtKB Helix 256 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P63 +P07834 UniProtKB Helix 274 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Helix 280 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Helix 292 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Helix 303 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Helix 313 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Turn 328 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Helix 331 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Helix 347 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 373 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 381 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 385 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 394 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 404 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Turn 409 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 413 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 425 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Turn 432 434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKS +P07834 UniProtKB Beta strand 435 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 445 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Turn 450 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 454 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 466 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 478 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 489 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 509 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Helix 516 518 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 522 526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 533 539 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 542 547 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 552 556 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Turn 557 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 561 566 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 573 579 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Turn 580 583 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 584 589 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 594 598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 624 628 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 635 640 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 642 649 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 652 658 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Turn 659 661 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 664 669 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 676 681 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 683 690 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 693 698 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Turn 699 701 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 704 707 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Turn 709 712 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 714 722 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 725 732 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P07834 UniProtKB Beta strand 735 742 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +##sequence-region P32562 1 705 +P32562 UniProtKB Chain 1 705 . . . ID=PRO_0000085762;Note=Cell cycle serine/threonine-protein kinase CDC5/MSD2 +P32562 UniProtKB Domain 82 337 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32562 UniProtKB Domain 520 587 . . . Note=POLO box 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00154 +P32562 UniProtKB Domain 619 692 . . . Note=POLO box 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00154 +P32562 UniProtKB Nucleotide binding 88 96 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32562 UniProtKB Active site 204 204 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P32562 UniProtKB Binding site 110 110 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32562 UniProtKB Modified residue 23 23 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32562 UniProtKB Modified residue 419 419 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region P36012 1 229 +P36012 UniProtKB Chain 1 229 . . . ID=PRO_0000221376;Note=Histone H3-like centromeric protein CSE4 +P36012 UniProtKB Region 132 229 . . . Note=H3-like +P36012 UniProtKB Motif 115 132 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36012 UniProtKB Compositional bias 1 66 . . . Note=Ser-rich +P36012 UniProtKB Mutagenesis 176 176 . . . Note=In CSE4-102%3B impairs nuclear division by disrupting the core centromere structure%3B when associated with T-218. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10891506;Dbxref=PMID:10891506 +P36012 UniProtKB Mutagenesis 194 194 . . . Note=In CSE4-111%3B impairs nuclear division by disrupting the core centromere structure. L->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10891506;Dbxref=PMID:10891506 +P36012 UniProtKB Mutagenesis 197 197 . . . Note=In CSE4-110%3B impairs nuclear division by disrupting the core centromere structure. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10891506;Dbxref=PMID:10891506 +P36012 UniProtKB Mutagenesis 218 218 . . . Note=In CSE4-102%3B impairs nuclear division by disrupting the core centromere structure%3B when associated with S-176. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10891506;Dbxref=PMID:10891506 +P36012 UniProtKB Helix 157 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LY8 +P36012 UniProtKB Helix 180 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LY8 +P36012 UniProtKB Turn 205 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LY8 +P36012 UniProtKB Helix 214 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LY8 +##sequence-region Q03705 1 181 +Q03705 UniProtKB Chain 1 181 . . . ID=PRO_0000203259;Note=EKC/KEOPS complex subunit CGI121 +Q03705 UniProtKB Beta strand 2 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +Q03705 UniProtKB Beta strand 9 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +Q03705 UniProtKB Helix 25 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +Q03705 UniProtKB Turn 31 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW5 +Q03705 UniProtKB Turn 36 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XAH +Q03705 UniProtKB Beta strand 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +Q03705 UniProtKB Helix 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +Q03705 UniProtKB Helix 50 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +Q03705 UniProtKB Beta strand 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +Q03705 UniProtKB Helix 74 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +Q03705 UniProtKB Beta strand 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +Q03705 UniProtKB Helix 88 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +Q03705 UniProtKB Beta strand 104 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +Q03705 UniProtKB Beta strand 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW9 +Q03705 UniProtKB Helix 118 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +Q03705 UniProtKB Beta strand 131 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +Q03705 UniProtKB Helix 138 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +Q03705 UniProtKB Helix 147 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +Q03705 UniProtKB Helix 165 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WW7 +##sequence-region P24871 1 460 +P24871 UniProtKB Chain 1 460 . . . ID=PRO_0000080406;Note=G2/mitotic-specific cyclin-4 +P24871 UniProtKB Sequence conflict 255 255 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24871 UniProtKB Sequence conflict 318 318 . . . Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24871 UniProtKB Sequence conflict 328 328 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38221 1 457 +P38221 UniProtKB Chain 1 457 . . . ID=PRO_0000090722;Note=Phosphatidate cytidylyltransferase +P38221 UniProtKB Transmembrane 71 91 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38221 UniProtKB Transmembrane 154 174 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38221 UniProtKB Transmembrane 188 208 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38221 UniProtKB Transmembrane 214 234 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38221 UniProtKB Transmembrane 255 275 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38221 UniProtKB Transmembrane 330 350 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38221 UniProtKB Mutagenesis 102 102 . . . Note=Reduced enzyme level. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8910557;Dbxref=PMID:8910557 +##sequence-region P39525 1 442 +P39525 UniProtKB Chain 1 442 . . . ID=PRO_0000180356;Note=3-oxoacyl-[acyl-carrier-protein] synthase homolog +P39525 UniProtKB Active site 187 187 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10022 +##sequence-region P40558 1 293 +P40558 UniProtKB Chain 1 293 . . . ID=PRO_0000184952;Note=Cytosolic Fe-S cluster assembly factor CFD1 +P40558 UniProtKB Nucleotide binding 25 32 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03039 +P40558 UniProtKB Metal binding 201 201 . . . Note=Iron-sulfur (4Fe-4S)%3B shared with dimeric partner +P40558 UniProtKB Metal binding 204 204 . . . Note=Iron-sulfur (4Fe-4S)%3B shared with dimeric partner +P40558 UniProtKB Modified residue 291 291 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P40558 UniProtKB Mutagenesis 31 31 . . . Note=Loss of function. K->A +P40558 UniProtKB Mutagenesis 86 86 . . . Note=Loss of function. T->A +P40558 UniProtKB Mutagenesis 182 182 . . . Note=Does not impair function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766 +P40558 UniProtKB Mutagenesis 201 201 . . . Note=Loss of function and disrupts heterotetramer formation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766 +P40558 UniProtKB Mutagenesis 204 204 . . . Note=Loss of function and disrupts heterotetramer formation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766 +P40558 UniProtKB Mutagenesis 207 207 . . . Note=Does not impair function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766 +##sequence-region P32656 1 232 +P32656 UniProtKB Chain 1 232 . . . ID=PRO_0000202657;Note=Glutathione-specific gamma-glutamylcyclotransferase +P32656 UniProtKB Region 10 15 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75223 +P32656 UniProtKB Active site 115 115 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75223 +P32656 UniProtKB Mutagenesis 115 115 . . . Note=Loss of catalytic activity against glutathione. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23070364;Dbxref=PMID:23070364 +P32656 UniProtKB Beta strand 8 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK +P32656 UniProtKB Helix 15 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK +P32656 UniProtKB Beta strand 25 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK +P32656 UniProtKB Beta strand 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK +P32656 UniProtKB Beta strand 54 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK +P32656 UniProtKB Helix 62 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK +P32656 UniProtKB Helix 69 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK +P32656 UniProtKB Helix 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK +P32656 UniProtKB Beta strand 91 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK +P32656 UniProtKB Helix 101 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK +P32656 UniProtKB Turn 115 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWI +P32656 UniProtKB Beta strand 119 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK +P32656 UniProtKB Helix 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK +P32656 UniProtKB Helix 135 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK +P32656 UniProtKB Turn 149 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWI +P32656 UniProtKB Beta strand 154 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK +P32656 UniProtKB Helix 176 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK +P32656 UniProtKB Helix 193 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK +P32656 UniProtKB Helix 219 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HWK +##sequence-region Q05583 1 330 +Q05583 UniProtKB Chain 1 330 . . . ID=PRO_0000253806;Note=Cytosolic iron-sulfur protein assembly protein 1 +Q05583 UniProtKB Repeat 12 53 . . . Note=WD 1 +Q05583 UniProtKB Repeat 56 95 . . . Note=WD 2 +Q05583 UniProtKB Repeat 105 144 . . . Note=WD 3 +Q05583 UniProtKB Repeat 151 190 . . . Note=WD 4 +Q05583 UniProtKB Repeat 195 236 . . . Note=WD 5 +Q05583 UniProtKB Repeat 248 286 . . . Note=WD 6 +Q05583 UniProtKB Repeat 292 330 . . . Note=WD 7 +Q05583 UniProtKB Mutagenesis 127 127 . . . Note=Impaired in cytosolic Fe/S protein assembly. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17937914;Dbxref=PMID:17937914 +Q05583 UniProtKB Beta strand 5 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 17 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 26 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 36 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 42 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 47 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 61 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 70 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 82 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 98 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 110 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 121 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 131 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 144 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 156 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 163 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 177 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 186 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 200 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 208 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 213 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 223 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 237 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 253 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 264 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 273 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 282 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Turn 292 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 298 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 312 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +Q05583 UniProtKB Beta strand 319 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HES +##sequence-region P53280 1 1122 +P53280 UniProtKB Chain 1 1122 . . . ID=PRO_0000202824;Note=Protein CAF130 +P53280 UniProtKB Modified residue 1042 1042 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P32943 1 380 +P32943 UniProtKB Chain 1 380 . . . ID=PRO_0000080409;Note=S-phase entry cyclin-6 +P32943 UniProtKB Sequence conflict 77 77 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32943 UniProtKB Sequence conflict 92 92 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32943 UniProtKB Sequence conflict 109 109 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32943 UniProtKB Sequence conflict 223 223 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P08004 1 1131 +P08004 UniProtKB Chain 1 1131 . . . ID=PRO_0000193727;Note=Chitin synthase 1 +P08004 UniProtKB Transmembrane 795 815 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08004 UniProtKB Transmembrane 833 853 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08004 UniProtKB Transmembrane 866 886 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08004 UniProtKB Transmembrane 914 934 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08004 UniProtKB Transmembrane 942 962 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08004 UniProtKB Transmembrane 1042 1062 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08004 UniProtKB Transmembrane 1101 1121 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08004 UniProtKB Modified residue 34 34 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P08004 UniProtKB Modified residue 35 35 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P08004 UniProtKB Modified residue 270 270 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P08004 UniProtKB Modified residue 299 299 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P08004 UniProtKB Modified residue 318 318 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P08004 UniProtKB Modified residue 328 328 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P08004 UniProtKB Modified residue 358 358 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P08004 UniProtKB Sequence conflict 815 815 . . . Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08004 UniProtKB Sequence conflict 815 815 . . . Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P14180 1 963 +P14180 UniProtKB Chain 1 963 . . . ID=PRO_0000193728;Note=Chitin synthase 2 +P14180 UniProtKB Topological domain 1 643 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14180 UniProtKB Transmembrane 644 664 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14180 UniProtKB Topological domain 665 677 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14180 UniProtKB Transmembrane 678 698 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14180 UniProtKB Topological domain 699 711 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14180 UniProtKB Transmembrane 712 732 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14180 UniProtKB Topological domain 733 743 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14180 UniProtKB Transmembrane 744 764 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14180 UniProtKB Topological domain 765 775 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14180 UniProtKB Transmembrane 776 796 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14180 UniProtKB Topological domain 797 875 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14180 UniProtKB Transmembrane 876 896 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14180 UniProtKB Topological domain 897 905 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14180 UniProtKB Transmembrane 906 926 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14180 UniProtKB Topological domain 927 963 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14180 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14180 UniProtKB Modified residue 82 82 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14180 UniProtKB Modified residue 86 86 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P14180 UniProtKB Modified residue 100 100 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14180 UniProtKB Modified residue 133 133 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P14180 UniProtKB Modified residue 217 217 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P14180 UniProtKB Glycosylation 22 22 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14180 UniProtKB Glycosylation 197 197 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14180 UniProtKB Glycosylation 447 447 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14180 UniProtKB Mutagenesis 197 197 . . . Note=30%25 decrease of activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 312 312 . . . Note=20%25 increase of activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 355 355 . . . Note=10%25 decrease of activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 393 393 . . . Note=5%25 decrease of activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 441 441 . . . Note=Loss of activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 441 441 . . . Note=Loss of activity. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 447 447 . . . Note=80%25 decrease of activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 490 490 . . . Note=70%25 decrease of activity. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 492 492 . . . Note=80%25 decrease of activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 493 493 . . . Note=90%25 decrease of activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 494 494 . . . Note=95%25 decrease of activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 497 497 . . . Note=95%25 decrease of activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 502 502 . . . Note=90%25 decrease of activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 505 505 . . . Note=80%25 decrease of activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 506 506 . . . Note=20%25 increase of activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 508 508 . . . Note=60%25 decrease of activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 509 509 . . . Note=70%25 decrease of activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 514 514 . . . Note=80%25 decrease of activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 515 515 . . . Note=90%25 decrease of activity. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 516 516 . . . Note=95%25 decrease of activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 521 521 . . . Note=Loss of activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 522 522 . . . Note=60%25 decrease of activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 537 537 . . . Note=No change in activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 550 550 . . . Note=85%25 decrease of activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 556 556 . . . Note=95%25 decrease of activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 559 559 . . . Note=95%25 decrease of activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 561 561 . . . Note=Loss of activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 561 561 . . . Note=65%25 decrease of activity. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 561 561 . . . Note=Loss of activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 562 562 . . . Note=Loss of activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 562 562 . . . Note=Loss of activity. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 562 562 . . . Note=Loss of activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 563 563 . . . Note=Loss of activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 563 563 . . . Note=94%25 decrease of activity. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 565 565 . . . Note=95%25 decrease of activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 589 589 . . . Note=70%25 decrease of activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 592 592 . . . Note=70%25 decrease of activity. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 601 601 . . . Note=Loss of activity. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 601 601 . . . Note=Loss of activity. Q->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 602 603 . . . Note=Loss of activity. RR->KK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 602 602 . . . Note=Loss of activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 602 602 . . . Note=95%25 decrease of activity. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 603 603 . . . Note=Loss of activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 603 603 . . . Note=57%25 decrease of activity. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 604 604 . . . Note=Loss of activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 604 604 . . . Note=Loss of activity. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 605 605 . . . Note=Loss of activity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 605 605 . . . Note=Loss of activity. W->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +P14180 UniProtKB Mutagenesis 607 607 . . . Note=95%25 decrease of activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7775457;Dbxref=PMID:7775457 +##sequence-region P38147 1 527 +P38147 UniProtKB Chain 1 527 . . . ID=PRO_0000085857;Note=Serine/threonine-protein kinase CHK1 +P38147 UniProtKB Domain 15 281 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38147 UniProtKB Nucleotide binding 21 29 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38147 UniProtKB Active site 142 142 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P38147 UniProtKB Binding site 45 45 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +##sequence-region P38907 1 458 +P38907 UniProtKB Chain 1 458 . . . ID=PRO_0000089646;Note=Central kinetochore subunit CHL4 +P38907 UniProtKB Beta strand 383 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38907 UniProtKB Beta strand 396 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38907 UniProtKB Helix 409 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38907 UniProtKB Helix 424 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38907 UniProtKB Turn 429 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38907 UniProtKB Beta strand 440 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38907 UniProtKB Beta strand 446 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +##sequence-region P40955 1 746 +P40955 UniProtKB Chain 1 746 . . . ID=PRO_0000089662;Note=Chitin biosynthesis protein CHS6 +P40955 UniProtKB Region 734 746 . . . Note=CHS5-binding +P40955 UniProtKB Helix 32 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Beta strand 45 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 53 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Beta strand 77 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Beta strand 91 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Beta strand 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 107 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Beta strand 131 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Turn 139 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Beta strand 143 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Beta strand 155 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 173 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 194 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 212 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 227 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Turn 237 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Beta strand 245 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 249 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 262 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 265 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 280 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 283 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 298 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 301 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 315 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Beta strand 319 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 327 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 353 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 371 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 387 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Turn 424 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 435 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 450 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Beta strand 459 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 473 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Turn 477 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 489 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Turn 495 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 500 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 509 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Beta strand 517 519 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 522 552 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 585 599 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Beta strand 605 608 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YG8 +P40955 UniProtKB Helix 613 625 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 629 642 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 646 657 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Beta strand 663 665 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 671 687 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 694 707 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 709 718 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +P40955 UniProtKB Helix 724 740 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +##sequence-region P20486 1 150 +P20486 UniProtKB Chain 1 150 . . . ID=PRO_0000206245;Note=Cyclin-dependent kinases regulatory subunit +P20486 UniProtKB Compositional bias 118 133 . . . Note=Poly-Gln +P20486 UniProtKB Helix 15 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2 +P20486 UniProtKB Helix 23 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2 +P20486 UniProtKB Beta strand 37 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2 +P20486 UniProtKB Helix 48 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2 +P20486 UniProtKB Helix 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2 +P20486 UniProtKB Turn 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2 +P20486 UniProtKB Beta strand 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2 +P20486 UniProtKB Helix 71 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2 +P20486 UniProtKB Beta strand 86 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2 +P20486 UniProtKB Beta strand 97 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2 +P20486 UniProtKB Turn 106 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QY2 +##sequence-region P53264 1 445 +P53264 UniProtKB Transit peptide 1 39 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53264 UniProtKB Chain 40 445 . . . ID=PRO_0000202813;Note=Cardiolipin-specific deacylase 1%2C mitochondrial +P53264 UniProtKB Domain 142 430 . . . Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53264 UniProtKB Motif 424 429 . . . Note=HXXXXD motif +##sequence-region P38323 1 520 +P38323 UniProtKB Transit peptide 1 13 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38323 UniProtKB Chain 14 520 . . . ID=PRO_0000160569;Note=ATP-dependent clpX-like chaperone%2C mitochondrial;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38323 UniProtKB Nucleotide binding 140 147 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00499 +P38323 UniProtKB Mutagenesis 174 174 . . . Note=Abrogates unfolding activity of unfoldase. Mildly increased ATPase activity. Reduces ALA synthesis. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25957689;Dbxref=PMID:25957689 +P38323 UniProtKB Mutagenesis 206 206 . . . Note=Blocks ATP hydrolysis. E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:25957689;Dbxref=PMID:25957689 +##sequence-region P33313 1 385 +P33313 UniProtKB Chain 1 385 . . . ID=PRO_0000106279;Note=Hsp70/Hsp90 co-chaperone CNS1 +P33313 UniProtKB Repeat 83 116 . . . Note=TPR 1 +P33313 UniProtKB Repeat 121 154 . . . Note=TPR 2 +P33313 UniProtKB Repeat 155 189 . . . Note=TPR 3 +P33313 UniProtKB Mutagenesis 90 90 . . . Note=In CNS1-1%3B disrupts interaction with Hsp90%2C temperature-sensitive defect impairing Hsp90-dependent function. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788914;Dbxref=PMID:12788914 +P33313 UniProtKB Mutagenesis 140 140 . . . Note=In CNS1-2%3B disrupts interaction with Hsp90%2C temperature-sensitive defect impairing Hsp90-dependent function. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788914;Dbxref=PMID:12788914 +P33313 UniProtKB Mutagenesis 260 260 . . . Note=In CNS1-3%3B temperature-sensitive defect impairing Hsp90-dependent function%3B when associated with G-324 and S-330. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788914;Dbxref=PMID:12788914 +P33313 UniProtKB Mutagenesis 324 324 . . . Note=In CNS1-3%3B temperature-sensitive defect impairing Hsp90-dependent function%3B when associated with G-260 and S-330. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788914;Dbxref=PMID:12788914 +P33313 UniProtKB Mutagenesis 330 330 . . . Note=In CNS1-3%3B temperature-sensitive defect impairing Hsp90-dependent function%3B when associated with G-260 and G-324. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788914;Dbxref=PMID:12788914 +P33313 UniProtKB Sequence conflict 6 13 . . . Note=ANGGYTKP->RQMEDIPNQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q3E823 1 68 +Q3E823 UniProtKB Chain 1 68 . . . ID=PRO_0000238657;Note=Cytochrome c oxidase assembly factor 2 +##sequence-region Q3E7B2 1 85 +Q3E7B2 UniProtKB Chain 1 85 . . . ID=PRO_0000245412;Note=Cytochrome c oxidase assembly factor 3%2C mitochondrial +Q3E7B2 UniProtKB Topological domain 1 26 . . . Note=Mitochondrial matrix +Q3E7B2 UniProtKB Transmembrane 27 49 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E7B2 UniProtKB Topological domain 50 85 . . . Note=Mitochondrial intermembrane +##sequence-region Q3E846 1 104 +Q3E846 UniProtKB Chain 1 104 . . . ID=PRO_0000247793;Note=Cytochrome c oxidase assembly factor 6 +Q3E846 UniProtKB Domain 22 76 . . . Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q3E846 UniProtKB Motif 25 35 . . . Note=Cx9C motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q3E846 UniProtKB Motif 57 68 . . . Note=Cx10C motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q3E846 UniProtKB Disulfide bond 25 68 . . . Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|PROSITE-ProRule:PRU01150,ECO:0000305|PubMed:20922212;Dbxref=PMID:20922212 +Q3E846 UniProtKB Disulfide bond 35 57 . . . Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|PROSITE-ProRule:PRU01150,ECO:0000305|PubMed:20922212;Dbxref=PMID:20922212 +Q3E846 UniProtKB Mutagenesis 25 25 . . . Note=Loss of function. Localizes correctly to the mitochondrion%2C but reduces the steady-state level of the protein in the mitochondrial fraction. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24549041;Dbxref=PMID:24549041 +Q3E846 UniProtKB Mutagenesis 26 26 . . . Note=Loss of function. Localizes correctly to the mitochondrion%2C but severely reduces the steady-state level of the protein in the mitochondrial fraction. W->C +Q3E846 UniProtKB Mutagenesis 35 35 . . . Note=Loss of function. Localizes correctly to the mitochondrion%2C but reduces the steady-state level of the protein in the mitochondrial fraction. C->A +Q3E846 UniProtKB Mutagenesis 57 57 . . . Note=Loss of function. Localizes correctly to the mitochondrion%2C but reduces the steady-state level of the protein in the mitochondrial fraction. C->A +Q3E846 UniProtKB Mutagenesis 68 68 . . . Note=Loss of function. Localizes correctly to the mitochondrion%2C but severely reduces the steady-state level of the protein in the mitochondrial fraction. C->A +##sequence-region Q12309 1 687 +Q12309 UniProtKB Chain 1 687 . . . ID=PRO_0000205753;Note=Pre-mRNA-splicing factor CLF1 +Q12309 UniProtKB Repeat 45 77 . . . Note=HAT 1 +Q12309 UniProtKB Repeat 79 111 . . . Note=HAT 2 +Q12309 UniProtKB Repeat 113 145 . . . Note=HAT 3 +Q12309 UniProtKB Repeat 147 178 . . . Note=HAT 4 +Q12309 UniProtKB Repeat 180 211 . . . Note=HAT 5 +Q12309 UniProtKB Repeat 213 247 . . . Note=HAT 6 +Q12309 UniProtKB Repeat 251 283 . . . Note=HAT 7 +Q12309 UniProtKB Repeat 300 332 . . . Note=HAT 8 +Q12309 UniProtKB Repeat 337 369 . . . Note=HAT 9 +Q12309 UniProtKB Repeat 383 416 . . . Note=HAT 10 +Q12309 UniProtKB Repeat 451 483 . . . Note=HAT 11 +Q12309 UniProtKB Repeat 525 557 . . . Note=HAT 12 +Q12309 UniProtKB Repeat 629 661 . . . Note=HAT 13 +Q12309 UniProtKB Helix 40 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12309 UniProtKB Helix 65 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12309 UniProtKB Helix 81 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12309 UniProtKB Helix 99 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12309 UniProtKB Helix 115 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12309 UniProtKB Helix 133 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12309 UniProtKB Turn 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12309 UniProtKB Helix 149 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12309 UniProtKB Helix 166 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12309 UniProtKB Helix 182 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12309 UniProtKB Helix 199 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12309 UniProtKB Helix 215 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12309 UniProtKB Helix 233 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12309 UniProtKB Helix 240 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12309 UniProtKB Helix 260 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region Q08685 1 445 +Q08685 UniProtKB Chain 1 445 . . . ID=PRO_0000076211;Note=mRNA cleavage and polyadenylation factor CLP1 +Q08685 UniProtKB Nucleotide binding 133 138 . . . Note=ATP;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03035,ECO:0000269|PubMed:17151076;Dbxref=PMID:17151076 +Q08685 UniProtKB Binding site 33 33 . . . Note=ATP;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03035,ECO:0000269|PubMed:17151076;Dbxref=PMID:17151076 +Q08685 UniProtKB Binding site 72 72 . . . Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03035,ECO:0000269|PubMed:17151076;Dbxref=PMID:17151076 +Q08685 UniProtKB Mutagenesis 136 136 . . . Note=Completely abolishes interaction with PCF11. No effect on growth%3B when associated with A-137. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22216186;Dbxref=PMID:22216186 +Q08685 UniProtKB Mutagenesis 137 137 . . . Note=Completely abolishes interaction with PCF11. No effect on growth%3B when associated with A-136. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22216186;Dbxref=PMID:22216186 +Q08685 UniProtKB Mutagenesis 161 161 . . . Note=Compromises interaction with PCF11. No effect on growth. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18648070,ECO:0000269|PubMed:22216186;Dbxref=PMID:18648070,PMID:22216186 +Q08685 UniProtKB Beta strand 24 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 32 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 43 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 65 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 72 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 81 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Turn 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 96 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Helix 103 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 120 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 125 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Helix 136 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Helix 148 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NPI +Q08685 UniProtKB Beta strand 156 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 166 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 172 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 194 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 206 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 212 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Helix 215 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Helix 219 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Helix 241 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 248 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Helix 255 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Helix 263 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 276 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Helix 286 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Helix 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 304 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Helix 318 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Turn 337 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NPI +Q08685 UniProtKB Beta strand 344 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Helix 350 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 355 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Helix 361 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 371 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Helix 378 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 384 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Helix 397 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 405 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Turn 416 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 420 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +Q08685 UniProtKB Beta strand 434 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +##sequence-region P32657 1 1468 +P32657 UniProtKB Chain 1 1468 . . . ID=PRO_0000080237;Note=Chromo domain-containing protein 1 +P32657 UniProtKB Domain 195 257 . . . Note=Chromo 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00053 +P32657 UniProtKB Domain 285 350 . . . Note=Chromo 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00053 +P32657 UniProtKB Domain 388 562 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P32657 UniProtKB Domain 699 860 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P32657 UniProtKB Nucleotide binding 401 408 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P32657 UniProtKB Motif 513 516 . . . Note=DEAH box +P32657 UniProtKB Modified residue 36 36 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P32657 UniProtKB Modified residue 72 72 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32657 UniProtKB Modified residue 987 987 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32657 UniProtKB Modified residue 989 989 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32657 UniProtKB Modified residue 1336 1336 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32657 UniProtKB Modified residue 1364 1364 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32657 UniProtKB Modified residue 1372 1372 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32657 UniProtKB Cross-link 1144 1144 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P32657 UniProtKB Mutagenesis 220 220 . . . Note=No interaction with methylated histone H3 'K-4'. E->L%2CW;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15647753,ECO:0000269|PubMed:17433364;Dbxref=PMID:15647753,PMID:17433364 +P32657 UniProtKB Mutagenesis 222 222 . . . Note=Confers interaction with methylated histone H3 'K-4'. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15647753;Dbxref=PMID:15647753 +P32657 UniProtKB Mutagenesis 314 314 . . . Note=No effect on interaction with methylated histone H3 'K-4'. L->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15647753;Dbxref=PMID:15647753 +P32657 UniProtKB Mutagenesis 316 316 . . . Note=Disrupts interaction with methylated histone H3 'K-4'%3B abrogates histone acetylation activity of SLIK. Y->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15647753;Dbxref=PMID:15647753 +P32657 UniProtKB Beta strand 179 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E +P32657 UniProtKB Turn 190 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DY7 +P32657 UniProtKB Helix 193 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E +P32657 UniProtKB Helix 204 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E +P32657 UniProtKB Beta strand 211 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E +P32657 UniProtKB Helix 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E +P32657 UniProtKB Beta strand 226 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E +P32657 UniProtKB Helix 230 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E +P32657 UniProtKB Beta strand 234 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DY7 +P32657 UniProtKB Helix 239 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E +P32657 UniProtKB Helix 251 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E +P32657 UniProtKB Helix 264 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E +P32657 UniProtKB Beta strand 286 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E +P32657 UniProtKB Beta strand 299 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DY8 +P32657 UniProtKB Beta strand 303 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E +P32657 UniProtKB Beta strand 320 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E +P32657 UniProtKB Helix 324 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E +P32657 UniProtKB Helix 332 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2H1E +P32657 UniProtKB Helix 1012 1025 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0 +P32657 UniProtKB Helix 1029 1031 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TED +P32657 UniProtKB Helix 1032 1037 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0 +P32657 UniProtKB Helix 1046 1091 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0 +P32657 UniProtKB Beta strand 1092 1094 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0 +P32657 UniProtKB Beta strand 1096 1098 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TED +P32657 UniProtKB Beta strand 1101 1103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TED +P32657 UniProtKB Helix 1104 1112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0 +P32657 UniProtKB Beta strand 1119 1122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TED +P32657 UniProtKB Beta strand 1125 1129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TED +P32657 UniProtKB Helix 1130 1150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0 +P32657 UniProtKB Helix 1155 1157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0 +P32657 UniProtKB Beta strand 1171 1173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0 +P32657 UniProtKB Helix 1177 1190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0 +P32657 UniProtKB Helix 1195 1200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0 +P32657 UniProtKB Turn 1202 1204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0 +P32657 UniProtKB Helix 1207 1209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0 +P32657 UniProtKB Helix 1250 1264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0 +P32657 UniProtKB Turn 1265 1268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XB0 +##sequence-region Q06350 1 511 +Q06350 UniProtKB Signal peptide 1 34 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06350 UniProtKB Chain 35 511 . . . ID=PRO_0000011937;Note=Sporulation-specific chitinase 2 +Q06350 UniProtKB Active site 223 223 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10053 +Q06350 UniProtKB Glycosylation 147 147 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06350 UniProtKB Glycosylation 228 228 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06350 UniProtKB Glycosylation 456 456 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06350 UniProtKB Glycosylation 472 472 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P05374 1 869 +P05374 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P05374 UniProtKB Chain 2 869 . . . ID=PRO_0000058304;Note=Phosphatidylethanolamine N-methyltransferase +P05374 UniProtKB Topological domain 2 55 . . . Note=Lumenal;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P05374 UniProtKB Transmembrane 56 76 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217 +P05374 UniProtKB Topological domain 77 86 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P05374 UniProtKB Transmembrane 87 107 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217 +P05374 UniProtKB Topological domain 108 187 . . . Note=Lumenal;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P05374 UniProtKB Transmembrane 188 208 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217 +P05374 UniProtKB Topological domain 209 212 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P05374 UniProtKB Transmembrane 213 233 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217 +P05374 UniProtKB Topological domain 234 258 . . . Note=Lumenal;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P05374 UniProtKB Transmembrane 259 279 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217 +P05374 UniProtKB Topological domain 280 291 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P05374 UniProtKB Transmembrane 292 310 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217 +P05374 UniProtKB Topological domain 311 362 . . . Note=Lumenal;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P05374 UniProtKB Transmembrane 363 383 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217 +P05374 UniProtKB Topological domain 384 389 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P05374 UniProtKB Transmembrane 390 410 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217 +P05374 UniProtKB Topological domain 411 439 . . . Note=Lumenal;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P05374 UniProtKB Transmembrane 440 460 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217 +P05374 UniProtKB Topological domain 461 463 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P05374 UniProtKB Transmembrane 464 484 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217 +P05374 UniProtKB Topological domain 485 534 . . . Note=Lumenal;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P05374 UniProtKB Transmembrane 535 555 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03217 +P05374 UniProtKB Topological domain 556 869 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03217,ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +P05374 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P29465 1 1165 +P29465 UniProtKB Chain 1 1165 . . . ID=PRO_0000193729;Note=Chitin synthase 3 +P29465 UniProtKB Topological domain 1 170 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P29465 UniProtKB Transmembrane 171 191 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P29465 UniProtKB Topological domain 192 202 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P29465 UniProtKB Transmembrane 203 223 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P29465 UniProtKB Topological domain 224 452 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P29465 UniProtKB Transmembrane 453 473 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P29465 UniProtKB Topological domain 474 1006 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P29465 UniProtKB Transmembrane 1007 1027 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P29465 UniProtKB Topological domain 1028 1029 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P29465 UniProtKB Transmembrane 1030 1050 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P29465 UniProtKB Topological domain 1051 1055 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P29465 UniProtKB Transmembrane 1056 1076 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P29465 UniProtKB Topological domain 1077 1080 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P29465 UniProtKB Transmembrane 1081 1101 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P29465 UniProtKB Topological domain 1102 1165 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +P29465 UniProtKB Modified residue 537 537 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P29465 UniProtKB Modified residue 538 538 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P29465 UniProtKB Glycosylation 82 82 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P29465 UniProtKB Glycosylation 114 114 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P29465 UniProtKB Glycosylation 152 152 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P29465 UniProtKB Glycosylation 163 163 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P29465 UniProtKB Glycosylation 303 303 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P29465 UniProtKB Glycosylation 332 332 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P29465 UniProtKB Glycosylation 371 371 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P29465 UniProtKB Cross-link 136 136 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P29465 UniProtKB Mutagenesis 991 991 . . . Note=Reduces catalytic activity by 67%25. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9760183;Dbxref=PMID:9760183 +P29465 UniProtKB Mutagenesis 993 993 . . . Note=Reduces catalytic activity by 89%25. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9760183;Dbxref=PMID:9760183 +P29465 UniProtKB Mutagenesis 994 994 . . . Note=Completely abolishes catalytic activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9760183;Dbxref=PMID:9760183 +P29465 UniProtKB Mutagenesis 995 995 . . . Note=Reduces catalytic activity by 87%25. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9760183;Dbxref=PMID:9760183 +P29465 UniProtKB Mutagenesis 999 999 . . . Note=Reduces catalytic activity by 59%25. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9760183;Dbxref=PMID:9760183 +P29465 UniProtKB Sequence conflict 1163 1163 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29465 UniProtKB Helix 13 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJW +##sequence-region P40019 1 153 +P40019 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40019 UniProtKB Chain 2 153 . . . ID=PRO_0000202623;Note=Histone H2A.Z-specific chaperone CHZ1 +P40019 UniProtKB Region 87 108 . . . Note=Important for H2A.Z-H2B binding +P40019 UniProtKB Compositional bias 32 36 . . . Note=Poly-Arg +P40019 UniProtKB Compositional bias 84 89 . . . Note=Poly-Glu +P40019 UniProtKB Compositional bias 138 150 . . . Note=Asp/Glu-rich (acidic) +P40019 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40019 UniProtKB Modified residue 68 68 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40019 UniProtKB Modified residue 70 70 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40019 UniProtKB Helix 75 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JSS +P40019 UniProtKB Helix 86 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JSS +P40019 UniProtKB Helix 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JSS +P40019 UniProtKB Turn 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JSS +P40019 UniProtKB Helix 116 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JSS +##sequence-region P43635 1 486 +P43635 UniProtKB Transit peptide 1 23 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43635 UniProtKB Chain 24 486 . . . ID=PRO_0000169985;Note=Citrate synthase 3%2C mitochondrial +P43635 UniProtKB Motif 484 486 . . . Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43635 UniProtKB Active site 315 315 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10117 +P43635 UniProtKB Active site 361 361 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10117 +P43635 UniProtKB Active site 419 419 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10117 +##sequence-region Q07897 1 291 +Q07897 UniProtKB Chain 1 291 . . . ID=PRO_0000247153;Note=Protein CMS1 +Q07897 UniProtKB Compositional bias 43 51 . . . Note=Poly-Asp +Q07897 UniProtKB Modified residue 59 59 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region Q01649 1 594 +Q01649 UniProtKB Chain 1 594 . . . ID=PRO_0000089750;Note=Spindle pole body-associated protein CIK1 +Q01649 UniProtKB Coiled coil 81 360 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40987 1 1014 +P40987 UniProtKB Chain 1 1014 . . . ID=PRO_0000089761;Note=Chromosome instability protein 1 +##sequence-region P27895 1 1000 +P27895 UniProtKB Chain 1 1000 . . . ID=PRO_0000125367;Note=Kinesin-like protein CIN8 +P27895 UniProtKB Domain 36 477 . . . Note=Kinesin motor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283 +P27895 UniProtKB Nucleotide binding 128 135 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283 +P27895 UniProtKB Coiled coil 518 615 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27895 UniProtKB Coiled coil 860 904 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27895 UniProtKB Modified residue 972 972 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P27895 UniProtKB Sequence conflict 216 216 . . . Note=D->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27895 UniProtKB Sequence conflict 216 216 . . . Note=D->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27895 UniProtKB Sequence conflict 793 793 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27895 UniProtKB Sequence conflict 793 793 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P48562 1 842 +P48562 UniProtKB Chain 1 842 . . . ID=PRO_0000085865;Note=Serine/threonine-protein kinase CLA4 +P48562 UniProtKB Domain 61 179 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +P48562 UniProtKB Domain 184 197 . . . Note=CRIB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00057 +P48562 UniProtKB Domain 546 825 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P48562 UniProtKB Nucleotide binding 552 560 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P48562 UniProtKB Compositional bias 136 144 . . . Note=Poly-Ser +P48562 UniProtKB Compositional bias 372 387 . . . Note=Poly-Gln +P48562 UniProtKB Active site 693 693 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P48562 UniProtKB Binding site 594 594 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P48562 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48562 UniProtKB Modified residue 46 46 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P48562 UniProtKB Modified residue 351 351 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P48562 UniProtKB Modified residue 367 367 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48562 UniProtKB Modified residue 425 425 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P48562 UniProtKB Sequence conflict 390 390 . . . Note=Y->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P22137 1 1653 +P22137 UniProtKB Chain 1 1653 . . . ID=PRO_0000205785;Note=Clathrin heavy chain +P22137 UniProtKB Repeat 543 689 . . . Note=CHCR 1 +P22137 UniProtKB Repeat 692 834 . . . Note=CHCR 2 +P22137 UniProtKB Repeat 839 978 . . . Note=CHCR 3 +P22137 UniProtKB Repeat 985 1130 . . . Note=CHCR 4 +P22137 UniProtKB Repeat 1134 1275 . . . Note=CHCR 5 +P22137 UniProtKB Repeat 1280 1426 . . . Note=CHCR 6 +P22137 UniProtKB Repeat 1429 1572 . . . Note=CHCR 7 +P22137 UniProtKB Region 1 483 . . . Note=Globular terminal domain +P22137 UniProtKB Region 23 66 . . . Note=WD40-like repeat 1 +P22137 UniProtKB Region 67 107 . . . Note=WD40-like repeat 2 +P22137 UniProtKB Region 108 152 . . . Note=WD40-like repeat 3 +P22137 UniProtKB Region 153 198 . . . Note=WD40-like repeat 4 +P22137 UniProtKB Region 199 263 . . . Note=WD40-like repeat 5 +P22137 UniProtKB Region 264 307 . . . Note=WD40-like repeat 6 +P22137 UniProtKB Region 308 336 . . . Note=WD40-like repeat 7 +P22137 UniProtKB Region 453 469 . . . Note=Binding site for the uncoating ATPase%2C involved in lattice disassembly;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22137 UniProtKB Region 484 527 . . . Note=Flexible linker +P22137 UniProtKB Region 528 1653 . . . Note=Heavy chain arm +P22137 UniProtKB Region 1219 1528 . . . Note=Involved in binding clathrin light chain;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22137 UniProtKB Cross-link 1107 1107 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region D6W196 1 494 +D6W196 UniProtKB Chain 1 494 . . . ID=PRO_0000402277;Note=Truncated non-functional calcium-binding mitochondrial carrier SAL1-1 +D6W196 UniProtKB Transmembrane 231 248 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +D6W196 UniProtKB Transmembrane 307 326 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +D6W196 UniProtKB Transmembrane 355 368 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +D6W196 UniProtKB Transmembrane 409 428 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +D6W196 UniProtKB Transmembrane 458 475 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +D6W196 UniProtKB Domain 11 46 . . . Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +D6W196 UniProtKB Domain 80 115 . . . Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +D6W196 UniProtKB Domain 120 155 . . . Note=EF-hand 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +D6W196 UniProtKB Domain 156 191 . . . Note=EF-hand 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +D6W196 UniProtKB Repeat 225 332 . . . Note=Solcar 1 +D6W196 UniProtKB Repeat 345 434 . . . Note=Solcar 2 +D6W196 UniProtKB Repeat 452 494 . . . Note=Solcar 3%3B truncated +D6W196 UniProtKB Calcium binding 59 70 . . . Note=1 +D6W196 UniProtKB Calcium binding 93 104 . . . Note=2 +D6W196 UniProtKB Calcium binding 155 166 . . . Note=3 +D6W196 UniProtKB Sequence conflict 131 131 . . . Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08058 1 207 +Q08058 UniProtKB Transit peptide 1 39 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08058 UniProtKB Chain 40 207 . . . ID=PRO_0000227688;Note=Coenzyme Q-binding protein COQ10%2C mitochondrial +##sequence-region P53318 1 479 +P53318 UniProtKB Transit peptide 1 17 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03193 +P53318 UniProtKB Chain 18 479 . . . ID=PRO_0000207581;Note=Ubiquinone biosynthesis monooxygenase COQ6%2C mitochondrial +P53318 UniProtKB Mutagenesis 202 202 . . . Note=Accumulates ubiquinone biosynthesis intermediates lacking the C5-ring hydroxyl. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21944752;Dbxref=PMID:21944752 +P53318 UniProtKB Mutagenesis 386 386 . . . Note=Accumulates ubiquinone biosynthesis intermediates lacking the C5-ring hydroxyl%3B when associated with D-388. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21944752;Dbxref=PMID:21944752 +P53318 UniProtKB Mutagenesis 388 388 . . . Note=Accumulates ubiquinone biosynthesis intermediates lacking the C5-ring hydroxyl%3B when associated with A-386. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21944752;Dbxref=PMID:21944752 +P53318 UniProtKB Sequence conflict 60 60 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53318 UniProtKB Sequence conflict 68 68 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53318 UniProtKB Sequence conflict 313 313 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q05779 1 260 +Q05779 UniProtKB Region 189 192 . . . Note=Lipid binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75208 +Q05779 UniProtKB Mutagenesis 135 135 . . . Note=Inability to grow on nonfermentable carbon sources. L->E%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25339443;Dbxref=PMID:25339443 +Q05779 UniProtKB Mutagenesis 174 174 . . . Note=Impaired ability to grow on nonfermentable carbon sources. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25339443;Dbxref=PMID:25339443 +Q05779 UniProtKB Mutagenesis 185 185 . . . Note=Inability to grow on nonfermentable carbon sources. D->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25339443;Dbxref=PMID:25339443 +Q05779 UniProtKB Mutagenesis 188 188 . . . Note=Inability to grow on nonfermentable carbon sources. W->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25339443;Dbxref=PMID:25339443 +Q05779 UniProtKB Mutagenesis 189 189 . . . Note=Impaired ability to grow on nonfermentable carbon sources. Y->D%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25339443;Dbxref=PMID:25339443 +Q05779 UniProtKB Mutagenesis 204 204 . . . Note=Impaired ability to grow on nonfermentable carbon sources. L->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25339443;Dbxref=PMID:25339443 +##sequence-region Q06156 1 1176 +Q06156 UniProtKB Chain 1 1176 . . . ID=PRO_0000095046;Note=Condensin complex subunit 1 +Q06156 UniProtKB Modified residue 464 464 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06156 UniProtKB Modified residue 475 475 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P53079 1 417 +P53079 UniProtKB Chain 1 417 . . . ID=PRO_0000213494;Note=Conserved oligomeric Golgi complex subunit 1 +P53079 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53079 UniProtKB Modified residue 305 305 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38779 1 376 +P38779 UniProtKB Chain 1 376 . . . ID=PRO_0000202895;Note=Proteasome-interacting protein CIC1 +P38779 UniProtKB Region 310 376 . . . Note=Required for interaction with CDC4 +##sequence-region P00890 1 479 +P00890 UniProtKB Transit peptide 1 37 . . . Note=Mitochondrion +P00890 UniProtKB Chain 38 479 . . . ID=PRO_0000005479;Note=Citrate synthase%2C mitochondrial +P00890 UniProtKB Active site 312 312 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10117 +P00890 UniProtKB Active site 358 358 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10117 +P00890 UniProtKB Active site 413 413 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10117 +P00890 UniProtKB Sequence conflict 58 58 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00890 UniProtKB Sequence conflict 78 78 . . . Note=E->EE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q3E7A9 1 73 +Q3E7A9 UniProtKB Chain 1 73 . . . ID=PRO_0000247790;Note=Cx9C motif-containing protein 4%2C mitochondrial +Q3E7A9 UniProtKB Domain 2 44 . . . Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q3E7A9 UniProtKB Motif 5 15 . . . Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q3E7A9 UniProtKB Motif 26 36 . . . Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q3E7A9 UniProtKB Disulfide bond 5 36 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q3E7A9 UniProtKB Disulfide bond 15 26 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +##sequence-region Q12510 1 522 +Q12510 UniProtKB Chain 1 522 . . . ID=PRO_0000240874;Note=DNA damage-binding protein CMR1 +Q12510 UniProtKB Repeat 183 224 . . . Note=WD 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12510 UniProtKB Repeat 239 281 . . . Note=WD 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12510 UniProtKB Repeat 287 327 . . . Note=WD 3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12510 UniProtKB Repeat 331 371 . . . Note=WD 4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12510 UniProtKB Repeat 388 427 . . . Note=WD 5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12510 UniProtKB Repeat 442 481 . . . Note=WD 6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12510 UniProtKB Repeat 482 521 . . . Note=WD 7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12510 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12510 UniProtKB Modified residue 69 69 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q12510 UniProtKB Modified residue 224 224 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q06680 1 1035 +Q06680 UniProtKB Chain 1 1035 . . . ID=PRO_0000095048;Note=Condensin complex subunit 3 +Q06680 UniProtKB Repeat 113 150 . . . Note=HEAT 1 +Q06680 UniProtKB Repeat 153 191 . . . Note=HEAT 2 +Q06680 UniProtKB Repeat 201 239 . . . Note=HEAT 3 +Q06680 UniProtKB Repeat 597 635 . . . Note=HEAT 4 +Q06680 UniProtKB Repeat 827 864 . . . Note=HEAT 5 +Q06680 UniProtKB Modified residue 198 198 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06680 UniProtKB Modified residue 933 933 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06680 UniProtKB Modified residue 981 981 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q06680 UniProtKB Modified residue 1008 1008 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P39110 1 191 +P39110 UniProtKB Chain 1 191 . . . ID=PRO_0000122464;Note=GTP-binding protein CIN4 +P39110 UniProtKB Nucleotide binding 23 30 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39110 UniProtKB Nucleotide binding 69 73 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39110 UniProtKB Nucleotide binding 131 134 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P47001 1 227 +P47001 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10438739;Dbxref=PMID:10438739 +P47001 UniProtKB Propeptide 22 64 . . . ID=PRO_0000033258;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10438739,ECO:0000269|PubMed:12776183,ECO:0000269|PubMed:12898712,ECO:0000269|PubMed:16495216,ECO:0000269|PubMed:9301021,ECO:0000269|PubMed:9748433;Dbxref=PMID:10438739,PMID:12776183,PMID:12898712,PMID:16495216,PMID:9301021,PMID:9748433 +P47001 UniProtKB Chain 65 227 . . . ID=PRO_0000033259;Note=Cell wall mannoprotein CIS3 +P47001 UniProtKB Repeat 65 78 . . . Note=PIR1/2/3 +P47001 UniProtKB Site 64 65 . . . Note=Cleavage%3B by KEX2 +P47001 UniProtKB Site 74 74 . . . Note=Covalent attachment to cell wall glycan +P47001 UniProtKB Glycosylation 68 68 . . . Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216 +P47001 UniProtKB Glycosylation 78 78 . . . Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216 +P47001 UniProtKB Glycosylation 105 105 . . . Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183 +P47001 UniProtKB Glycosylation 106 106 . . . Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183 +P47001 UniProtKB Glycosylation 107 107 . . . Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183 +P47001 UniProtKB Glycosylation 109 109 . . . Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183 +P47001 UniProtKB Glycosylation 111 111 . . . Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183 +P47001 UniProtKB Glycosylation 112 112 . . . Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183 +P47001 UniProtKB Glycosylation 113 113 . . . Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183 +P47001 UniProtKB Glycosylation 114 114 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47001 UniProtKB Glycosylation 116 116 . . . Note=O-linked (Man) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183 +P47001 UniProtKB Glycosylation 117 117 . . . Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183 +P47001 UniProtKB Glycosylation 118 118 . . . Note=O-linked (Man) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12776183;Dbxref=PMID:12776183 +P47001 UniProtKB Mutagenesis 65 65 . . . Note=Does not affect cell wall incorporation. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216 +P47001 UniProtKB Mutagenesis 68 68 . . . Note=Does not affect cell wall incorporation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216 +P47001 UniProtKB Mutagenesis 69 69 . . . Note=Results in complete loss of cell wall incorporation. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216 +P47001 UniProtKB Mutagenesis 72 72 . . . Note=Results in complete loss of cell wall incorporation. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216 +P47001 UniProtKB Mutagenesis 74 74 . . . Note=Results in complete loss of cell wall incorporation. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216 +P47001 UniProtKB Mutagenesis 76 76 . . . Note=Results in complete loss of cell wall incorporation. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216 +P47001 UniProtKB Mutagenesis 78 78 . . . Note=Does not affect cell wall incorporation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216 +P47001 UniProtKB Mutagenesis 79 79 . . . Note=Does not affect cell wall incorporation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216 +P47001 UniProtKB Mutagenesis 82 82 . . . Note=Does not affect cell wall incorporation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16495216;Dbxref=PMID:16495216 +P47001 UniProtKB Mutagenesis 130 130 . . . Note=Does not affect cell wall incorporation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12898712;Dbxref=PMID:12898712 +P47001 UniProtKB Mutagenesis 197 197 . . . Note=Results in the incorporation of KEX2-unprocessed precursor protein into the cell wall. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12898712;Dbxref=PMID:12898712 +P47001 UniProtKB Mutagenesis 208 227 . . . Note=In PIR4t18%3B destabilizes the protein. QNVAEQCSAIHLEAVSLVDC->LDC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12898712;Dbxref=PMID:12898712 +P47001 UniProtKB Mutagenesis 227 227 . . . Note=Does not affect cell wall incorporation. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12898712;Dbxref=PMID:12898712 +P47001 UniProtKB Sequence conflict 43 44 . . . Note=AA->SS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47001 UniProtKB Sequence conflict 68 68 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47001 UniProtKB Sequence conflict 88 88 . . . Note=S->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03690 1 1277 +Q03690 UniProtKB Chain 1 1277 . . . ID=PRO_0000123557;Note=Clustered mitochondria protein 1 +Q03690 UniProtKB Domain 339 596 . . . Note=Clu;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01167 +Q03690 UniProtKB Repeat 704 738 . . . Note=TPR 1 +Q03690 UniProtKB Repeat 1020 1053 . . . Note=TPR 2 +Q03690 UniProtKB Repeat 1148 1181 . . . Note=TPR 3 +Q03690 UniProtKB Modified residue 1247 1247 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P53865 1 581 +P53865 UniProtKB Chain 1 581 . . . ID=PRO_0000089973;Note=Chaotic nuclear migration protein 67 +P53865 UniProtKB Coiled coil 179 252 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53865 UniProtKB Coiled coil 306 363 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53865 UniProtKB Coiled coil 373 451 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53865 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53865 UniProtKB Modified residue 20 20 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53865 UniProtKB Modified residue 72 72 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53865 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53865 UniProtKB Modified residue 89 89 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53865 UniProtKB Modified residue 151 151 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53865 UniProtKB Helix 429 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7 +P53865 UniProtKB Helix 449 451 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7 +P53865 UniProtKB Helix 455 461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7 +P53865 UniProtKB Helix 467 473 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7 +P53865 UniProtKB Helix 475 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7 +P53865 UniProtKB Helix 483 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7 +P53865 UniProtKB Helix 501 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7 +P53865 UniProtKB Helix 504 516 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7 +P53865 UniProtKB Helix 518 533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7 +P53865 UniProtKB Helix 540 554 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7 +P53865 UniProtKB Helix 563 571 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OA7 +##sequence-region P41810 1 973 +P41810 UniProtKB Chain 1 973 . . . ID=PRO_0000193839;Note=Coatomer subunit beta +P41810 UniProtKB Repeat 98 133 . . . Note=HEAT 1 +P41810 UniProtKB Repeat 134 170 . . . Note=HEAT 2 +P41810 UniProtKB Repeat 279 317 . . . Note=HEAT 3 +P41810 UniProtKB Repeat 318 354 . . . Note=HEAT 4 +P41810 UniProtKB Modified residue 181 181 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P41810 UniProtKB Modified residue 540 540 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P41810 UniProtKB Mutagenesis 334 336 . . . Note=Loses ability to recognize arginine (R)-based ER localization signals in proteins. Recognition of C-terminal di-lysine signals present in proteins is unimpaired. DLD->NAN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17954604;Dbxref=PMID:17954604 +P41810 UniProtKB Sequence conflict 412 412 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40509 1 296 +P40509 UniProtKB Chain 1 296 . . . ID=PRO_0000193856;Note=Coatomer subunit epsilon +P40509 UniProtKB Helix 4 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Turn 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Helix 15 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Helix 20 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Helix 31 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Beta strand 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Helix 57 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Helix 73 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Turn 78 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Helix 86 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Helix 102 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Turn 114 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV3 +P40509 UniProtKB Beta strand 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV3 +P40509 UniProtKB Helix 121 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Helix 138 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Helix 154 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Turn 179 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Helix 182 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Helix 197 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Helix 213 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Helix 226 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Turn 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Helix 234 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Beta strand 237 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Helix 240 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Helix 259 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P40509 UniProtKB Helix 273 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +##sequence-region O13525 1 335 +O13525 UniProtKB Transit peptide 1 10 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03111 +O13525 UniProtKB Chain 11 335 . . . ID=PRO_0000006035;Note=Ubiquinone biosynthesis protein COQ4%2C mitochondrial +O13525 UniProtKB Mutagenesis 120 120 . . . Note=In COQ4-3%3B abolishes coenzyme Q biosynthesis%2C but does not affect stability of other COQ polypeptides. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19022396;Dbxref=PMID:19022396 +O13525 UniProtKB Mutagenesis 121 121 . . . Note=In COQ4-2%3B abolishes coenzyme Q biosynthesis%2C but does not affect stability of other COQ polypeptides. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19022396;Dbxref=PMID:19022396 +O13525 UniProtKB Mutagenesis 226 226 . . . Note=In COQ4-1%3B abolishes coenzyme Q biosynthesis%2C but does not affect stability of other COQ polypeptides. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11469793,ECO:0000269|PubMed:19022396;Dbxref=PMID:11469793,PMID:19022396 +##sequence-region P41735 1 233 +P41735 UniProtKB Transit peptide 1 15 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03194 +P41735 UniProtKB Chain 16 233 . . . ID=PRO_0000089330;Note=5-demethoxyubiquinone hydroxylase%2C mitochondrial +P41735 UniProtKB Metal binding 63 63 . . . Note=Iron 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03194 +P41735 UniProtKB Metal binding 95 95 . . . Note=Iron 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03194 +P41735 UniProtKB Metal binding 95 95 . . . Note=Iron 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03194 +P41735 UniProtKB Metal binding 98 98 . . . Note=Iron 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03194 +P41735 UniProtKB Metal binding 147 147 . . . Note=Iron 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03194 +P41735 UniProtKB Metal binding 194 194 . . . Note=Iron 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03194 +P41735 UniProtKB Metal binding 194 194 . . . Note=Iron 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03194 +P41735 UniProtKB Metal binding 197 197 . . . Note=Iron 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03194 +P41735 UniProtKB Mutagenesis 194 194 . . . Note=Lacks ubiquinone and accumulates the intermediate DMQH2%2C causing respiratory deficiency. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624818;Dbxref=PMID:16624818 +##sequence-region Q01519 1 83 +Q01519 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1331057,ECO:0000269|PubMed:1331058;Dbxref=PMID:1331057,PMID:1331058 +Q01519 UniProtKB Chain 2 83 . . . ID=PRO_0000194925;Note=Cytochrome c oxidase subunit 6B +Q01519 UniProtKB Domain 24 67 . . . Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q01519 UniProtKB Motif 27 37 . . . Note=Cx9C motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q01519 UniProtKB Motif 48 59 . . . Note=Cx10C motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q01519 UniProtKB Modified residue 82 82 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +Q01519 UniProtKB Disulfide bond 27 59 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q01519 UniProtKB Disulfide bond 37 48 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +##sequence-region Q03048 1 143 +Q03048 UniProtKB Chain 1 143 . . . ID=PRO_0000214915;Note=Cofilin +Q03048 UniProtKB Domain 5 137 . . . Note=ADF-H;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00599 +Q03048 UniProtKB Modified residue 4 4 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03048 UniProtKB Mutagenesis 105 106 . . . Note=Reduced interaction with PIP2. KD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11747431;Dbxref=PMID:11747431 +Q03048 UniProtKB Mutagenesis 109 110 . . . Note=Defects in actin monomer interaction. RR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11747431;Dbxref=PMID:11747431 +Q03048 UniProtKB Sequence conflict 1 5 . . . Note=MSRSG->MWGKKFIRSQENVKFLCS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03048 UniProtKB Helix 10 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF +Q03048 UniProtKB Beta strand 26 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF +Q03048 UniProtKB Beta strand 36 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF +Q03048 UniProtKB Helix 50 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF +Q03048 UniProtKB Beta strand 63 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF +Q03048 UniProtKB Beta strand 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CFY +Q03048 UniProtKB Beta strand 80 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF +Q03048 UniProtKB Beta strand 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QPV +Q03048 UniProtKB Helix 95 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF +Q03048 UniProtKB Beta strand 117 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF +Q03048 UniProtKB Helix 125 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF +Q03048 UniProtKB Helix 129 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KEF +##sequence-region P53622 1 1201 +P53622 UniProtKB Chain 1 1201 . . . ID=PRO_0000050910;Note=Coatomer subunit alpha +P53622 UniProtKB Repeat 9 39 . . . Note=WD 1 +P53622 UniProtKB Repeat 51 81 . . . Note=WD 2 +P53622 UniProtKB Repeat 93 123 . . . Note=WD 3 +P53622 UniProtKB Repeat 135 165 . . . Note=WD 4 +P53622 UniProtKB Repeat 207 237 . . . Note=WD 5 +P53622 UniProtKB Repeat 251 281 . . . Note=WD 6 +P53622 UniProtKB Sequence conflict 753 753 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53622 UniProtKB Sequence conflict 753 753 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53622 UniProtKB Sequence conflict 905 905 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53622 UniProtKB Sequence conflict 905 905 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53622 UniProtKB Sequence conflict 1006 1006 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53622 UniProtKB Sequence conflict 1006 1006 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53622 UniProtKB Sequence conflict 1027 1028 . . . Note=DA->NT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53622 UniProtKB Sequence conflict 1027 1028 . . . Note=DA->NT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53622 UniProtKB Helix 649 658 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ +P53622 UniProtKB Helix 662 672 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ +P53622 UniProtKB Helix 675 687 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ +P53622 UniProtKB Helix 691 700 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ +P53622 UniProtKB Helix 704 714 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ +P53622 UniProtKB Helix 717 729 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ +P53622 UniProtKB Helix 733 743 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ +P53622 UniProtKB Helix 746 755 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ +P53622 UniProtKB Helix 759 768 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ +P53622 UniProtKB Helix 772 781 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ +P53622 UniProtKB Helix 786 788 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MKQ +P53622 UniProtKB Helix 900 907 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Helix 911 916 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Helix 920 931 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Helix 937 939 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Helix 940 949 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Beta strand 951 954 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Beta strand 957 961 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV3 +P53622 UniProtKB Beta strand 964 967 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Beta strand 969 971 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Beta strand 973 975 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Helix 977 979 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Helix 987 1002 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Helix 1006 1021 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Beta strand 1025 1027 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV3 +P53622 UniProtKB Helix 1029 1055 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Turn 1059 1061 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV3 +P53622 UniProtKB Helix 1062 1071 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Helix 1072 1074 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Helix 1079 1095 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Helix 1099 1110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Helix 1117 1130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Beta strand 1147 1149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Turn 1151 1153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Beta strand 1156 1161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Beta strand 1163 1165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Turn 1167 1169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Beta strand 1172 1174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Helix 1175 1177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Beta strand 1179 1181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV3 +P53622 UniProtKB Beta strand 1183 1186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV2 +P53622 UniProtKB Beta strand 1188 1191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MV3 +##sequence-region P00401 1 534 +P00401 UniProtKB Chain 1 534 . . . ID=PRO_0000183432;Note=Cytochrome c oxidase subunit 1 +P00401 UniProtKB Transmembrane 16 38 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00401 UniProtKB Transmembrane 58 80 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00401 UniProtKB Transmembrane 101 123 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00401 UniProtKB Transmembrane 148 170 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00401 UniProtKB Transmembrane 183 205 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00401 UniProtKB Transmembrane 237 259 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00401 UniProtKB Transmembrane 266 288 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00401 UniProtKB Transmembrane 303 325 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00401 UniProtKB Transmembrane 337 359 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00401 UniProtKB Transmembrane 374 396 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00401 UniProtKB Transmembrane 409 431 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00401 UniProtKB Transmembrane 451 473 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00401 UniProtKB Metal binding 62 62 . . . Note=Iron (heme A axial ligand);Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00401 UniProtKB Metal binding 241 241 . . . Note=Copper B;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00401 UniProtKB Metal binding 245 245 . . . Note=Copper B;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00401 UniProtKB Metal binding 290 290 . . . Note=Copper B;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00401 UniProtKB Metal binding 291 291 . . . Note=Copper B;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00401 UniProtKB Metal binding 376 376 . . . Note=Iron (heme A3 axial ligand);Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00401 UniProtKB Metal binding 378 378 . . . Note=Iron (heme A axial ligand);Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00401 UniProtKB Cross-link 241 245 . . . Note=1'-histidyl-3'-tyrosine (His-Tyr);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00401 UniProtKB Sequence conflict 57 57 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00401 UniProtKB Sequence conflict 69 69 . . . Note=F->CT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00401 UniProtKB Sequence conflict 224 224 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00401 UniProtKB Sequence conflict 328 328 . . . Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00401 UniProtKB Sequence conflict 378 378 . . . Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00401 UniProtKB Sequence conflict 479 485 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00401 UniProtKB Sequence conflict 492 492 . . . Note=N->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00401 UniProtKB Sequence conflict 496 510 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32344 1 111 +P32344 UniProtKB Chain 1 111 . . . ID=PRO_0000097136;Note=Mitochondrial mRNA-processing protein COX24 +P32344 UniProtKB Compositional bias 82 111 . . . Note=Arg/Lys-rich (basic) +##sequence-region P38287 1 376 +P38287 UniProtKB Chain 1 376 . . . ID=PRO_0000079395;Note=Mannosyl phosphorylinositol ceramide synthase CSH1 +P38287 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38287 UniProtKB Transmembrane 274 294 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38287 UniProtKB Modified residue 354 354 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region P43639 1 278 +P43639 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +P43639 UniProtKB Chain 2 278 . . . ID=PRO_0000068257;Note=Casein kinase II subunit beta +P43639 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +P43639 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +##sequence-region P46946 1 345 +P46946 UniProtKB Chain 1 345 . . . ID=PRO_0000097565;Note=DNA endonuclease SAE2 +P46946 UniProtKB Region 21 172 . . . Note=DNA-binding +P46946 UniProtKB Modified residue 143 143 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46946 UniProtKB Modified residue 267 267 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18716619,ECO:0000269|PubMed:20150422;Dbxref=PMID:18716619,PMID:20150422 +P46946 UniProtKB Mutagenesis 72 72 . . . Note=Reduces DNA damage-induced phosphorylation%3B when associated with A-73%2C A-75%2C A-76 and A-90. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15121837;Dbxref=PMID:15121837 +P46946 UniProtKB Mutagenesis 73 73 . . . Note=Reduces DNA damage-induced phosphorylation%3B when associated with A-73%2C A-75%2C A-76 and A-90. Abolishes DNA damage-induced phosphorylation and function in DNA repair%3B when associated with A-90%2C A-249%2C A-279 and A-289. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15121837,ECO:0000269|PubMed:16861895,ECO:0000269|PubMed:18670132;Dbxref=PMID:15121837,PMID:16861895,PMID:18670132 +P46946 UniProtKB Mutagenesis 75 75 . . . Note=Reduces DNA damage-induced phosphorylation%3B when associated with A-72%2C A-75%2C A-76 and A-90. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15121837;Dbxref=PMID:15121837 +P46946 UniProtKB Mutagenesis 76 76 . . . Note=Reduces DNA damage-induced phosphorylation%3B when associated with A-72%2C A-73%2C A-75 and A-90. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15121837;Dbxref=PMID:15121837 +P46946 UniProtKB Mutagenesis 90 90 . . . Note=Reduces DNA damage-induced phosphorylation%3B when associated with A-72%2C A-73%2C A-75 and A-76. Abolishes DNA damage-induced phosphorylation and function in DNA repair%3B when associated with A-73%2C A-249%2C A-279 and A-289. T->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15121837,ECO:0000269|PubMed:16861895,ECO:0000269|PubMed:18670132;Dbxref=PMID:15121837,PMID:16861895,PMID:18670132 +P46946 UniProtKB Mutagenesis 223 223 . . . Note=Leads to camptothecin hypersensitivity and loss of function%3B when associated with A-225. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18716619;Dbxref=PMID:18716619 +P46946 UniProtKB Mutagenesis 225 225 . . . Note=Leads to camptothecin hypersensitivity and loss of function%3B when associated with A-223. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18716619;Dbxref=PMID:18716619 +P46946 UniProtKB Mutagenesis 249 249 . . . Note=Reduces DNA damage-induced phosphorylation%3B when associated with A-278%2C A-279%2C and A-289. Abolishes DNA damage-induced phosphorylation and function in DNA repair%3B when associated with A-73%2C A-90%2C A-279 and A-289. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15121837,ECO:0000269|PubMed:16861895,ECO:0000269|PubMed:18670132;Dbxref=PMID:15121837,PMID:16861895,PMID:18670132 +P46946 UniProtKB Mutagenesis 267 267 . . . Note=Leads to camptothecin hypersensitivity and loss of function. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18716619,ECO:0000269|PubMed:20150422;Dbxref=PMID:18716619,PMID:20150422 +P46946 UniProtKB Mutagenesis 267 267 . . . Note=Leads to constitutive activation of the DNA repair function. S->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18716619,ECO:0000269|PubMed:20150422;Dbxref=PMID:18716619,PMID:20150422 +P46946 UniProtKB Mutagenesis 270 270 . . . Note=Abolishes DNA-binding and endonuclease activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18042458;Dbxref=PMID:18042458 +P46946 UniProtKB Mutagenesis 278 278 . . . Note=Reduces DNA damage-induced phosphorylation%3B when associated with A-249%2C A-279%2C and A-289. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15121837;Dbxref=PMID:15121837 +P46946 UniProtKB Mutagenesis 279 279 . . . Note=Reduces DNA damage-induced phosphorylation%3B when associated with A-249%2C A-278%2C and A-289. Abolishes DNA damage-induced phosphorylation and function in DNA repair%3B when associated with A-73%2C A-90%2C A-249 and A-289. T->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15121837,ECO:0000269|PubMed:16861895,ECO:0000269|PubMed:18670132;Dbxref=PMID:15121837,PMID:16861895,PMID:18670132 +P46946 UniProtKB Mutagenesis 289 289 . . . Note=Reduces DNA damage-induced phosphorylation%3B when associated with A-249%2C A-278%2C and A-279. Abolishes DNA damage-induced phosphorylation and function in DNA repair%3B when associated with A-73%2C A-90%2C A-249 and A-279. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15121837,ECO:0000269|PubMed:16861895,ECO:0000269|PubMed:18670132;Dbxref=PMID:15121837,PMID:16861895,PMID:18670132 +##sequence-region P32074 1 935 +P32074 UniProtKB Chain 1 935 . . . ID=PRO_0000193861;Note=Coatomer subunit gamma +P32074 UniProtKB Repeat 258 296 . . . Note=HEAT 1 +P32074 UniProtKB Repeat 337 372 . . . Note=HEAT 2 +P32074 UniProtKB Repeat 373 410 . . . Note=HEAT 3 +P32074 UniProtKB Repeat 412 449 . . . Note=HEAT 4 +P32074 UniProtKB Repeat 524 562 . . . Note=HEAT 5 +P32074 UniProtKB Modified residue 638 638 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32074 UniProtKB Modified residue 643 643 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32074 UniProtKB Modified residue 653 653 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32074 UniProtKB Cross-link 647 647 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32074 UniProtKB Sequence conflict 353 353 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q05892 1 277 +Q05892 UniProtKB Chain 1 277 . . . ID=PRO_0000268626;Note=MIOREX complex component 2 +##sequence-region P18900 1 473 +P18900 UniProtKB Metal binding 193 193 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18900 UniProtKB Metal binding 193 193 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18900 UniProtKB Metal binding 197 197 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18900 UniProtKB Metal binding 197 197 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18900 UniProtKB Metal binding 364 364 . . . Note=Magnesium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18900 UniProtKB Binding site 84 84 . . . Note=Isopentenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18900 UniProtKB Binding site 87 87 . . . Note=Isopentenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18900 UniProtKB Binding site 186 186 . . . Note=Isopentenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18900 UniProtKB Binding site 202 202 . . . Note=Polyprenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18900 UniProtKB Binding site 203 203 . . . Note=Isopentenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18900 UniProtKB Binding site 323 323 . . . Note=Polyprenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18900 UniProtKB Binding site 324 324 . . . Note=Polyprenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18900 UniProtKB Binding site 361 361 . . . Note=Polyprenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18900 UniProtKB Binding site 378 378 . . . Note=Polyprenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P27697 1 501 +P27697 UniProtKB Transit peptide 1 29 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27697 UniProtKB Chain 30 501 . . . ID=PRO_0000000260;Note=Atypical kinase COQ8%2C mitochondrial +P27697 UniProtKB Domain 188 501 . . . Note=Protein kinase +P27697 UniProtKB Nucleotide binding 303 306 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8NI60 +P27697 UniProtKB Motif 134 137 . . . Note=KxGQ motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8NI60 +P27697 UniProtKB Motif 195 198 . . . Note=AAAS motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8NI60 +P27697 UniProtKB Active site 346 346 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8NI60 +P27697 UniProtKB Binding site 198 198 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8NI60 +P27697 UniProtKB Binding site 216 216 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8NI60 +P27697 UniProtKB Binding site 351 351 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8NI60 +P27697 UniProtKB Binding site 365 365 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8NI60 +P27697 UniProtKB Mutagenesis 89 89 . . . Note=In coq8-2%3B impairs growth on ethanol and/or glycerol as a carbon source%2C but retains steady-state levels of COQ8. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21296186;Dbxref=PMID:21296186 +P27697 UniProtKB Mutagenesis 130 130 . . . Note=In coq8-5%3B impairs growth on ethanol and/or glycerol as a carbon source%2C but retains steady-state levels of COQ8. Impairs coenzyme Q6 biosynthesis. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21296186;Dbxref=PMID:21296186 +P27697 UniProtKB Mutagenesis 134 134 . . . Note=Abolishes coenzyme Q biosynthesis. Able to autophosphorylate in cis. K->A%2CH%2CR%2CS;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25498144,ECO:0000269|PubMed:27499294;Dbxref=PMID:25498144,PMID:27499294 +P27697 UniProtKB Mutagenesis 137 137 . . . Note=Abolishes coenzyme Q biosynthesis. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25498144;Dbxref=PMID:25498144 +P27697 UniProtKB Mutagenesis 197 197 . . . Note=Abolishes coenzyme Q biosynthesis. Able to autophosphorylate in cis. A->G%2CS;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25498144,ECO:0000269|PubMed:27499294;Dbxref=PMID:25498144,PMID:27499294 +P27697 UniProtKB Mutagenesis 197 197 . . . Note=In coq8-3%3B impairs growth on ethanol and/or glycerol as a carbon source%2C but retains steady-state levels of COQ8. Impairs coenzyme Q6 biosynthesis. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21296186;Dbxref=PMID:21296186 +P27697 UniProtKB Mutagenesis 198 198 . . . Note=Decreased coenzyme Q biosynthesis. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25498144;Dbxref=PMID:25498144 +P27697 UniProtKB Mutagenesis 216 216 . . . Note=Impairs coenzyme Q biosynthesis. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21296186;Dbxref=PMID:21296186 +P27697 UniProtKB Mutagenesis 216 216 . . . Note=Abolishes coenzyme Q biosynthesis. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25498144;Dbxref=PMID:25498144 +P27697 UniProtKB Mutagenesis 229 229 . . . Note=In coq8-6%3B impairs growth on ethanol and/or glycerol as a carbon source%2C but retains steady-state levels of COQ8. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21296186;Dbxref=PMID:21296186 +P27697 UniProtKB Mutagenesis 269 269 . . . Note=Abolishes coenzyme Q biosynthesis. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25498144;Dbxref=PMID:25498144 +P27697 UniProtKB Mutagenesis 346 346 . . . Note=Abolishes coenzyme Q biosynthesis. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25498144;Dbxref=PMID:25498144 +P27697 UniProtKB Mutagenesis 346 346 . . . Note=In coq8-2%3B impairs growth on ethanol and/or glycerol as a carbon source%2C but retains steady-state levels of COQ8. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21296186;Dbxref=PMID:21296186 +P27697 UniProtKB Mutagenesis 348 348 . . . Note=In coq8-4%3B impairs growth on ethanol and/or glycerol as a carbon source%2C but retains steady-state levels of COQ8. N->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21296186;Dbxref=PMID:21296186 +P27697 UniProtKB Mutagenesis 351 351 . . . Note=Abolishes coenzyme Q biosynthesis. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25498144;Dbxref=PMID:25498144 +P27697 UniProtKB Mutagenesis 365 365 . . . Note=Abolishes coenzyme Q biosynthesis. Enhanced autophosphorylation in cis. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25498144,ECO:0000269|PubMed:27499294;Dbxref=PMID:25498144,PMID:27499294 +P27697 UniProtKB Mutagenesis 471 471 . . . Note=Abolishes coenzyme Q biosynthesis. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25498144;Dbxref=PMID:25498144 +P27697 UniProtKB Mutagenesis 475 475 . . . Note=In coq8-8%3B impairs growth on ethanol and/or glycerol as a carbon source%2C but retains steady-state levels of COQ8. G->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21296186;Dbxref=PMID:21296186 +##sequence-region P52924 1 374 +P52924 UniProtKB Chain 1 374 . . . ID=PRO_0000207521;Note=Protein COS10 +P52924 UniProtKB Topological domain 1 36 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52924 UniProtKB Transmembrane 37 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52924 UniProtKB Topological domain 60 62 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52924 UniProtKB Transmembrane 63 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52924 UniProtKB Topological domain 86 374 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43542 1 379 +P43542 UniProtKB Chain 1 379 . . . ID=PRO_0000207515;Note=Protein COS4 +P43542 UniProtKB Transmembrane 43 63 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43542 UniProtKB Transmembrane 70 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43542 UniProtKB Transmembrane 233 253 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43542 UniProtKB Transmembrane 255 275 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53344 1 381 +P53344 UniProtKB Chain 1 381 . . . ID=PRO_0000207517;Note=Protein COS6 +P53344 UniProtKB Topological domain 1 42 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53344 UniProtKB Transmembrane 43 63 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53344 UniProtKB Topological domain 64 69 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53344 UniProtKB Transmembrane 70 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53344 UniProtKB Topological domain 91 381 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32798 1 439 +P32798 UniProtKB Chain 1 439 . . . ID=PRO_0000206102;Note=Cobalt uptake protein COT1 +P32798 UniProtKB Transmembrane 10 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32798 UniProtKB Transmembrane 43 60 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32798 UniProtKB Transmembrane 78 100 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32798 UniProtKB Transmembrane 114 133 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32798 UniProtKB Transmembrane 244 265 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32798 UniProtKB Transmembrane 279 295 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32798 UniProtKB Compositional bias 140 148 . . . Note=His-rich (could be involved in coordination of cobalt ions) +P32798 UniProtKB Compositional bias 163 169 . . . Note=His-rich (could be involved in coordination of cobalt ions) +P32798 UniProtKB Modified residue 225 225 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32798 UniProtKB Cross-link 301 301 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14557538;Dbxref=PMID:14557538 +P32798 UniProtKB Sequence conflict 227 227 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32798 UniProtKB Sequence conflict 333 334 . . . Note=HI->RV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32798 UniProtKB Sequence conflict 424 424 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47081 1 118 +P47081 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12287 1 69 +Q12287 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9407107;Dbxref=PMID:9407107 +Q12287 UniProtKB Chain 2 69 . . . ID=PRO_0000213541;Note=Cytochrome c oxidase copper chaperone +Q12287 UniProtKB Domain 23 65 . . . Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q12287 UniProtKB Motif 26 36 . . . Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q12287 UniProtKB Motif 47 57 . . . Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q12287 UniProtKB Metal binding 23 23 . . . Note=Copper;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q14061 +Q12287 UniProtKB Metal binding 24 24 . . . Note=Copper;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q14061 +Q12287 UniProtKB Disulfide bond 26 57 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q12287 UniProtKB Disulfide bond 36 47 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q12287 UniProtKB Beta strand 3 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U97 +Q12287 UniProtKB Beta strand 13 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U96 +Q12287 UniProtKB Beta strand 23 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z2G +Q12287 UniProtKB Helix 28 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U96 +Q12287 UniProtKB Helix 45 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U96 +Q12287 UniProtKB Helix 48 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U96 +Q12287 UniProtKB Turn 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U96 +##sequence-region P04037 1 155 +P04037 UniProtKB Transit peptide 1 25 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6327686;Dbxref=PMID:6327686 +P04037 UniProtKB Chain 26 155 . . . ID=PRO_0000006114;Note=Cytochrome c oxidase subunit 4%2C mitochondrial +P04037 UniProtKB Metal binding 111 111 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00692 +P04037 UniProtKB Metal binding 134 134 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00692 +P04037 UniProtKB Metal binding 137 137 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00692 +P04037 UniProtKB Modified residue 55 55 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P04037 UniProtKB Sequence conflict 26 26 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04037 UniProtKB Sequence conflict 73 73 . . . Note=G->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04037 UniProtKB Beta strand 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR8 +P04037 UniProtKB Beta strand 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ODX +P04037 UniProtKB Beta strand 103 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ODX +P04037 UniProtKB Beta strand 109 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ODX +P04037 UniProtKB Beta strand 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ODX +P04037 UniProtKB Beta strand 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ODX +P04037 UniProtKB Beta strand 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ODX +P04037 UniProtKB Beta strand 140 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ODX +##sequence-region P00424 1 153 +P00424 UniProtKB Transit peptide 1 20 . . . Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:6300105,ECO:0000269|PubMed:6327686;Dbxref=PMID:6300105,PMID:6327686 +P00424 UniProtKB Chain 21 153 . . . ID=PRO_0000006097;Note=Cytochrome c oxidase polypeptide 5A%2C mitochondrial +P00424 UniProtKB Sequence conflict 51 51 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P00425 1 151 +P00425 UniProtKB Transit peptide 1 17 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00425 UniProtKB Chain 18 151 . . . ID=PRO_0000006098;Note=Cytochrome c oxidase polypeptide 5B%2C mitochondrial +##sequence-region P04039 1 78 +P04039 UniProtKB Transit peptide 1 27 . . . Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:6327685,ECO:0000269|PubMed:7851399;Dbxref=PMID:6327685,PMID:7851399 +P04039 UniProtKB Chain 28 74 . . . ID=PRO_0000006173;Note=Cytochrome c oxidase polypeptide VIII%2C mitochondrial +P04039 UniProtKB Propeptide 75 78 . . . ID=PRO_0000006174 +P04039 UniProtKB Sequence conflict 47 47 . . . Note=T->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04039 UniProtKB Sequence conflict 68 68 . . . Note=C->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P10614 1 530 +P10614 UniProtKB Chain 1 530 . . . ID=PRO_0000052012;Note=Lanosterol 14-alpha demethylase +P10614 UniProtKB Topological domain 1 20 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10614 UniProtKB Transmembrane 21 41 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10614 UniProtKB Topological domain 42 530 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10614 UniProtKB Metal binding 470 470 . . . Note=Iron (heme axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P10614 UniProtKB Modified residue 458 458 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P10614 UniProtKB Cross-link 116 116 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P10614 UniProtKB Cross-link 353 353 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P10614 UniProtKB Cross-link 454 454 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P10614 UniProtKB Sequence conflict 433 433 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10614 UniProtKB Sequence conflict 433 433 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10614 UniProtKB Helix 9 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 27 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Beta strand 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Turn 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 69 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 76 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Beta strand 89 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Beta strand 98 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 105 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Turn 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 122 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 144 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 160 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Turn 182 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Turn 186 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Beta strand 190 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 196 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 215 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 225 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 238 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 249 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Beta strand 280 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 283 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 301 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 334 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 349 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 357 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 364 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Beta strand 383 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Beta strand 405 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 410 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Turn 417 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Turn 421 424 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 428 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Beta strand 444 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Beta strand 451 454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 466 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Helix 473 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Beta strand 491 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Beta strand 507 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +P10614 UniProtKB Beta strand 518 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LXJ +##sequence-region P17898 1 393 +P17898 UniProtKB Chain 1 393 . . . ID=PRO_0000056808;Note=Cholinephosphotransferase 1 +P17898 UniProtKB Topological domain 1 40 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17898 UniProtKB Transmembrane 41 61 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17898 UniProtKB Topological domain 62 172 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17898 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17898 UniProtKB Topological domain 194 210 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17898 UniProtKB Transmembrane 211 231 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17898 UniProtKB Topological domain 232 263 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17898 UniProtKB Transmembrane 264 284 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17898 UniProtKB Topological domain 285 285 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17898 UniProtKB Transmembrane 286 306 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17898 UniProtKB Topological domain 307 320 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17898 UniProtKB Transmembrane 321 341 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17898 UniProtKB Topological domain 342 348 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17898 UniProtKB Transmembrane 349 369 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17898 UniProtKB Topological domain 370 393 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P08679 1 460 +P08679 UniProtKB Chain 1 460 . . . ID=PRO_0000169984;Note=Citrate synthase%2C peroxisomal +P08679 UniProtKB Motif 458 460 . . . Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08679 UniProtKB Active site 293 293 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10117 +P08679 UniProtKB Active site 339 339 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10117 +P08679 UniProtKB Active site 394 394 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10117 +P08679 UniProtKB Modified residue 21 21 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P08679 UniProtKB Cross-link 218 218 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P08679 UniProtKB Cross-link 239 239 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P08679 UniProtKB Cross-link 354 354 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P08679 UniProtKB Cross-link 385 385 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region P17891 1 233 +P17891 UniProtKB Chain 1 233 . . . ID=PRO_0000205776;Note=Clathrin light chain +P17891 UniProtKB Region 144 204 . . . Note=Involved in binding clathrin heavy chain;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17891 UniProtKB Coiled coil 125 186 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17891 UniProtKB Modified residue 49 49 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P17891 UniProtKB Modified residue 52 52 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +##sequence-region P53332 1 305 +P53332 UniProtKB Chain 1 305 . . . ID=PRO_0000202870;Note=Phosphopantetheine adenylyltransferase +##sequence-region P43618 1 361 +P43618 UniProtKB Chain 1 361 . . . ID=PRO_0000202697;Note=Kinetochore-associated protein CNN1 +P43618 UniProtKB Sequence conflict 8 8 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43618 UniProtKB Helix 63 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GEQ +##sequence-region P40452 1 197 +P40452 UniProtKB Chain 1 197 . . . ID=PRO_0000202954;Note=Cytochrome c oxidase assembly factor 1 +P40452 UniProtKB Topological domain 1 73 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40452 UniProtKB Transmembrane 74 94 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40452 UniProtKB Topological domain 95 197 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q05809 1 96 +Q05809 UniProtKB Chain 1 96 . . . ID=PRO_0000247207;Note=Cytochrome oxidase assembly factor 4 +Q05809 UniProtKB Domain 36 77 . . . Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q05809 UniProtKB Motif 39 49 . . . Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q05809 UniProtKB Motif 59 69 . . . Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q05809 UniProtKB Disulfide bond 39 69 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q05809 UniProtKB Disulfide bond 49 59 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +##sequence-region P53600 1 189 +P53600 UniProtKB Chain 1 189 . . . ID=PRO_0000193830;Note=Coatomer subunit zeta +##sequence-region P53239 1 316 +P53239 UniProtKB Transmembrane 164 184 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53239 UniProtKB Transmembrane 214 234 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53239 UniProtKB Transmembrane 275 295 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E731 1 98 +Q3E731 UniProtKB Chain 1 98 . . . ID=PRO_0000122292;Note=Cytochrome c oxidase assembly protein COX19 +Q3E731 UniProtKB Domain 27 70 . . . Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q3E731 UniProtKB Motif 30 40 . . . Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q3E731 UniProtKB Motif 52 62 . . . Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q3E731 UniProtKB Disulfide bond 30 62 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q3E731 UniProtKB Disulfide bond 40 52 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q3E731 UniProtKB Mutagenesis 63 63 . . . Note=In COX19-1%3B causes a respiratory-deficient phenotype because of lack of cytochrome c activity. R->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12171940;Dbxref=PMID:12171940 +##sequence-region P00410 1 251 +P00410 UniProtKB Propeptide 1 15 . . . ID=PRO_0000419180;Note=Removed in mature form +P00410 UniProtKB Chain 16 251 . . . ID=PRO_0000006048;Note=Cytochrome c oxidase subunit 2 +P00410 UniProtKB Topological domain 16 42 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00410 UniProtKB Transmembrane 43 64 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00410 UniProtKB Topological domain 65 82 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00410 UniProtKB Transmembrane 83 107 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00410 UniProtKB Topological domain 108 251 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00410 UniProtKB Metal binding 186 186 . . . Note=Copper A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00410 UniProtKB Metal binding 221 221 . . . Note=Copper A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00410 UniProtKB Metal binding 225 225 . . . Note=Copper A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00410 UniProtKB Metal binding 229 229 . . . Note=Copper A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00410 UniProtKB Site 15 16 . . . Note=Cleavage%3B by IMP1 +P00410 UniProtKB Sequence conflict 59 59 . . . Note=Y->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P00420 1 269 +P00420 UniProtKB Chain 1 269 . . . ID=PRO_0000183874;Note=Cytochrome c oxidase subunit 3 +P00420 UniProtKB Transmembrane 16 36 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00420 UniProtKB Transmembrane 45 65 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00420 UniProtKB Transmembrane 90 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00420 UniProtKB Transmembrane 142 162 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00420 UniProtKB Transmembrane 167 187 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00420 UniProtKB Transmembrane 204 224 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00420 UniProtKB Transmembrane 247 267 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00420 UniProtKB Sequence conflict 263 263 . . . Note=V->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00420 UniProtKB Sequence conflict 263 263 . . . Note=V->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P41811 1 889 +P41811 UniProtKB Chain 1 889 . . . ID=PRO_0000050918;Note=Coatomer subunit beta' +P41811 UniProtKB Repeat 11 41 . . . Note=WD 1 +P41811 UniProtKB Repeat 53 83 . . . Note=WD 2 +P41811 UniProtKB Repeat 95 125 . . . Note=WD 3 +P41811 UniProtKB Repeat 138 169 . . . Note=WD 4 +P41811 UniProtKB Repeat 182 214 . . . Note=WD 5 +P41811 UniProtKB Repeat 226 256 . . . Note=WD 6 +P41811 UniProtKB Modified residue 326 326 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P41811 UniProtKB Beta strand 6 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 16 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 23 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 35 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Turn 42 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 46 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 58 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Helix 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 69 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 77 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Turn 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 89 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 100 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 107 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 121 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Turn 126 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 132 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 143 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 155 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 163 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 176 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 189 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 200 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 208 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Turn 215 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 220 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 231 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 238 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 252 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Turn 257 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 262 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 269 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Helix 283 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J82 +P41811 UniProtKB Beta strand 287 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 294 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J73 +P41811 UniProtKB Beta strand 313 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 321 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 327 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 341 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 350 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 360 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 368 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 378 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Turn 384 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 389 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 396 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 404 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 416 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 423 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 438 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 442 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 453 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Turn 458 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 463 467 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 471 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 480 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Turn 490 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 496 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Helix 504 512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 518 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Helix 523 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 526 532 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 537 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 545 549 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 554 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 563 568 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 573 579 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Turn 580 583 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 584 589 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +P41811 UniProtKB Beta strand 594 598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YNP +##sequence-region P27680 1 312 +P27680 UniProtKB Transit peptide 1 32 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03190 +P27680 UniProtKB Chain 33 312 . . . ID=PRO_0000035932;Note=Ubiquinone biosynthesis O-methyltransferase%2C mitochondrial +P27680 UniProtKB Binding site 68 68 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03190 +P27680 UniProtKB Binding site 130 130 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03190 +P27680 UniProtKB Binding site 153 153 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03190 +P27680 UniProtKB Binding site 196 196 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03190 +##sequence-region P49017 1 307 +P49017 UniProtKB Transit peptide 1 19 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03191 +P49017 UniProtKB Chain 20 307 . . . ID=PRO_0000193361;Note=2-methoxy-6-polyprenyl-1%2C4-benzoquinol methylase%2C mitochondrial +P49017 UniProtKB Region 179 180 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03191,ECO:0000269|PubMed:25084328;Dbxref=PMID:25084328 +P49017 UniProtKB Binding site 122 122 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03191,ECO:0000269|PubMed:25084328;Dbxref=PMID:25084328 +P49017 UniProtKB Binding site 148 148 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03191,ECO:0000269|PubMed:25084328;Dbxref=PMID:25084328 +P49017 UniProtKB Binding site 197 197 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03191,ECO:0000269|PubMed:25084328;Dbxref=PMID:25084328 +P49017 UniProtKB Helix 74 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +P49017 UniProtKB Turn 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +P49017 UniProtKB Helix 90 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +P49017 UniProtKB Beta strand 114 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +P49017 UniProtKB Helix 124 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +P49017 UniProtKB Beta strand 143 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +P49017 UniProtKB Helix 151 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +P49017 UniProtKB Beta strand 166 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBW +P49017 UniProtKB Beta strand 173 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +P49017 UniProtKB Turn 180 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +P49017 UniProtKB Beta strand 191 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +P49017 UniProtKB Helix 200 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +P49017 UniProtKB Helix 206 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +P49017 UniProtKB Beta strand 217 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +P49017 UniProtKB Helix 234 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +P49017 UniProtKB Helix 258 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +P49017 UniProtKB Helix 274 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +P49017 UniProtKB Beta strand 286 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +P49017 UniProtKB Helix 295 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +P49017 UniProtKB Beta strand 299 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OBX +##sequence-region P53053 1 380 +P53053 UniProtKB Chain 1 380 . . . ID=PRO_0000207522;Note=Protein COS12 +P53053 UniProtKB Topological domain 1 70 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53053 UniProtKB Transmembrane 71 91 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53053 UniProtKB Topological domain 92 231 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53053 UniProtKB Transmembrane 232 252 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53053 UniProtKB Topological domain 253 257 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53053 UniProtKB Transmembrane 258 278 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53053 UniProtKB Topological domain 279 380 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CX13 1 379 +P0CX13 UniProtKB Chain 1 379 . . . ID=PRO_0000409750;Note=Protein COS3 +P0CX13 UniProtKB Topological domain 1 72 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX13 UniProtKB Transmembrane 73 93 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX13 UniProtKB Topological domain 94 254 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX13 UniProtKB Transmembrane 255 275 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX13 UniProtKB Topological domain 276 379 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07788 1 383 +Q07788 UniProtKB Chain 1 383 . . . ID=PRO_0000207518;Note=Protein COS7 +Q07788 UniProtKB Topological domain 1 42 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07788 UniProtKB Transmembrane 43 63 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07788 UniProtKB Topological domain 64 72 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07788 UniProtKB Transmembrane 73 93 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07788 UniProtKB Topological domain 94 232 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07788 UniProtKB Transmembrane 233 253 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07788 UniProtKB Topological domain 254 254 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07788 UniProtKB Transmembrane 255 275 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07788 UniProtKB Topological domain 276 383 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39103 1 70 +P39103 UniProtKB Chain 1 70 . . . ID=PRO_0000183930;Note=Cytochrome c oxidase assembly protein COX14 +P39103 UniProtKB Transmembrane 17 38 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38170 1 754 +P38170 UniProtKB Chain 1 754 . . . ID=PRO_0000095047;Note=Condensin complex subunit 2 +P38170 UniProtKB Modified residue 245 245 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38170 UniProtKB Modified residue 548 548 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38170 UniProtKB Sequence conflict 517 517 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38170 UniProtKB Sequence conflict 517 517 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06096 1 861 +Q06096 UniProtKB Chain 1 861 . . . ID=PRO_0000213508;Note=Conserved oligomeric Golgi complex subunit 4 +##sequence-region P53195 1 279 +P53195 UniProtKB Chain 1 279 . . . ID=PRO_0000213520;Note=Conserved oligomeric Golgi complex subunit 7 +P53195 UniProtKB Sequence conflict 12 12 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04935 1 205 +Q04935 UniProtKB Transmembrane 91 109 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04935 UniProtKB Transmembrane 116 132 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E7A4 1 109 +Q3E7A4 UniProtKB Chain 1 109 . . . ID=PRO_0000248414;Note=COX assembly mitochondrial protein 2 +Q3E7A4 UniProtKB Domain 10 54 . . . Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q3E7A4 UniProtKB Motif 13 23 . . . Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q3E7A4 UniProtKB Motif 36 46 . . . Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q3E7A4 UniProtKB Disulfide bond 13 46 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q3E7A4 UniProtKB Disulfide bond 23 36 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +##sequence-region P53951 1 403 +P53951 UniProtKB Chain 1 403 . . . ID=PRO_0000213512;Note=Conserved oligomeric Golgi complex subunit 5 +##sequence-region P43621 1 546 +P43621 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8617224;Dbxref=PMID:8617224 +P43621 UniProtKB Chain 2 546 . . . ID=PRO_0000193848;Note=Coatomer subunit delta +P43621 UniProtKB Domain 288 546 . . . Note=MHD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00404 +P43621 UniProtKB Region 190 440 . . . Note=Interaction with DSL1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14504276;Dbxref=PMID:14504276 +P43621 UniProtKB Modified residue 277 277 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P43621 UniProtKB Beta strand 289 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Beta strand 309 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Helix 325 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Beta strand 328 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Helix 343 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Helix 355 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Beta strand 362 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Beta strand 366 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Beta strand 380 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Beta strand 398 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Beta strand 409 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Beta strand 428 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Helix 447 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Turn 451 454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJX +P43621 UniProtKB Beta strand 456 458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Beta strand 463 473 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Beta strand 478 486 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Helix 490 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Beta strand 495 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Beta strand 501 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Beta strand 517 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +P43621 UniProtKB Beta strand 525 529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJX +P43621 UniProtKB Beta strand 533 545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FJZ +##sequence-region P32378 1 372 +P32378 UniProtKB Transit peptide 1 42 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03189 +P32378 UniProtKB Chain 43 372 . . . ID=PRO_0000035921;Note=4-hydroxybenzoate polyprenyltransferase%2C mitochondrial;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03189 +P32378 UniProtKB Transmembrane 92 112 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03189 +P32378 UniProtKB Transmembrane 114 134 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03189 +P32378 UniProtKB Transmembrane 171 191 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03189 +P32378 UniProtKB Transmembrane 193 213 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03189 +P32378 UniProtKB Transmembrane 229 249 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03189 +P32378 UniProtKB Transmembrane 298 318 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03189 +P32378 UniProtKB Transmembrane 352 372 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03189 +P32378 UniProtKB Region 134 156 . . . Note=Allylic polyprenyl diphosphate-binding site;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03189,ECO:0000305|PubMed:1740455;Dbxref=PMID:1740455 +P32378 UniProtKB Compositional bias 29 49 . . . Note=Ser-rich +P32378 UniProtKB Sequence conflict 273 273 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P00427 1 148 +P00427 UniProtKB Transit peptide 1 40 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6290493;Dbxref=PMID:6290493 +P00427 UniProtKB Chain 41 148 . . . ID=PRO_0000006108;Note=Cytochrome c oxidase subunit 6%2C mitochondrial +##sequence-region P21595 1 489 +P21595 UniProtKB Chain 1 489 . . . ID=PRO_0000052042;Note=Cytochrome P450-DIT2 +P21595 UniProtKB Metal binding 435 435 . . . Note=Iron (heme axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21595 UniProtKB Sequence conflict 445 445 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38930 1 258 +P38930 UniProtKB Chain 1 258 . . . ID=PRO_0000068258;Note=Casein kinase II subunit beta' +##sequence-region P40465 1 213 +P40465 UniProtKB Chain 1 213 . . . ID=PRO_0000202960;Note=Chromosome segregation in meiosis protein 2 +P40465 UniProtKB Sequence conflict 18 18 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40465 UniProtKB Helix 3 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQ6 +P40465 UniProtKB Beta strand 8 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +P40465 UniProtKB Helix 17 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +P40465 UniProtKB Beta strand 33 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +P40465 UniProtKB Helix 48 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +P40465 UniProtKB Helix 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +P40465 UniProtKB Helix 63 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +P40465 UniProtKB Beta strand 69 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +P40465 UniProtKB Helix 77 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +P40465 UniProtKB Beta strand 110 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +P40465 UniProtKB Helix 119 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +P40465 UniProtKB Helix 132 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +P40465 UniProtKB Beta strand 155 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +P40465 UniProtKB Helix 167 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +P40465 UniProtKB Helix 171 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +P40465 UniProtKB Beta strand 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +P40465 UniProtKB Helix 199 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +P40465 UniProtKB Beta strand 209 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +##sequence-region Q06705 1 408 +Q06705 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q06705 UniProtKB Chain 2 408 . . . ID=PRO_0000228155;Note=Phosphatidylinositol transfer protein CSR1 +Q06705 UniProtKB Domain 157 317 . . . Note=CRAL-TRIO;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00056 +Q06705 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q06705 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q06705 UniProtKB Sequence conflict 6 6 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47976 1 325 +P47976 UniProtKB Chain 1 325 . . . ID=PRO_0000089173;Note=mRNA decay factor CTH1 +P47976 UniProtKB Zinc finger 204 232 . . . Note=C3H1-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 +P47976 UniProtKB Zinc finger 242 270 . . . Note=C3H1-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 +P47976 UniProtKB Mutagenesis 225 225 . . . Note=Abolishes mRNA binding. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18522836;Dbxref=PMID:18522836 +P47976 UniProtKB Sequence conflict 142 143 . . . Note=EI->RV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03957 1 528 +Q03957 UniProtKB Chain 1 528 . . . ID=PRO_0000085906;Note=CTD kinase subunit alpha +Q03957 UniProtKB Domain 183 469 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03957 UniProtKB Nucleotide binding 189 197 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03957 UniProtKB Motif 37 44 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03957 UniProtKB Compositional bias 506 528 . . . Note=Asn/Asp-rich +Q03957 UniProtKB Active site 306 306 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q03957 UniProtKB Binding site 212 212 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03957 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03957 UniProtKB Modified residue 338 338 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15870265;Dbxref=PMID:15870265 +Q03957 UniProtKB Mutagenesis 324 324 . . . Note=Cold-sensitive. Sensitive to hydroxyurea and UV irradiation. Interferes with ATP-binding. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12684377,ECO:0000269|PubMed:15870265;Dbxref=PMID:12684377,PMID:15870265 +Q03957 UniProtKB Mutagenesis 338 338 . . . Note=Cold-sensitive. Abolishes kinase activity. Delayed growth at early stationary phase. Shows no increase in CTD Ser-2 phosphorylation in the transition from rapid growth to stationary phase. Has compromised transcriptional activation of two stationary-phase genes CTT1 and SPI1. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15870265;Dbxref=PMID:15870265 +##sequence-region P38428 1 203 +P38428 UniProtKB Chain 1 203 . . . ID=PRO_0000203346;Note=Coupling of ubiquitin conjugation to ER degradation protein 1 +P38428 UniProtKB Topological domain 1 6 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9388185;Dbxref=PMID:9388185 +P38428 UniProtKB Transmembrane 7 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38428 UniProtKB Topological domain 24 203 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9388185;Dbxref=PMID:9388185 +P38428 UniProtKB Domain 65 107 . . . Note=CUE;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00468 +P38428 UniProtKB Sequence conflict 48 48 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38428 UniProtKB Helix 67 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MYX +P38428 UniProtKB Helix 82 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MYX +P38428 UniProtKB Helix 95 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MYX +P38428 UniProtKB Turn 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MYX +P38428 UniProtKB Helix 151 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU +P38428 UniProtKB Helix 168 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU +P38428 UniProtKB Helix 173 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU +P38428 UniProtKB Helix 196 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JQU +##sequence-region P40094 1 801 +P40094 UniProtKB Chain 1 801 . . . ID=PRO_0000213503;Note=Conserved oligomeric Golgi complex subunit 3 +P40094 UniProtKB Modified residue 507 507 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40094 UniProtKB Modified residue 647 647 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P53959 1 839 +P53959 UniProtKB Chain 1 839 . . . ID=PRO_0000213517;Note=Conserved oligomeric Golgi complex subunit 6 +##sequence-region Q06440 1 651 +Q06440 UniProtKB Chain 1 651 . . . ID=PRO_0000050940;Note=Coronin-like protein +Q06440 UniProtKB Repeat 79 110 . . . Note=WD 1 +Q06440 UniProtKB Repeat 138 169 . . . Note=WD 2 +Q06440 UniProtKB Repeat 180 210 . . . Note=WD 3 +Q06440 UniProtKB Repeat 226 257 . . . Note=WD 4 +Q06440 UniProtKB Coiled coil 618 650 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06440 UniProtKB Modified residue 441 441 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q06440 UniProtKB Modified residue 454 454 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +Q06440 UniProtKB Modified residue 456 456 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06440 UniProtKB Modified residue 517 517 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q06440 UniProtKB Modified residue 529 529 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q06440 UniProtKB Modified residue 573 573 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06440 UniProtKB Modified residue 579 579 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P53822 1 381 +P53822 UniProtKB Chain 1 381 . . . ID=PRO_0000207513;Note=Protein COS1 +P53822 UniProtKB Topological domain 1 42 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53822 UniProtKB Transmembrane 43 63 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53822 UniProtKB Topological domain 64 72 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53822 UniProtKB Transmembrane 73 93 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53822 UniProtKB Topological domain 94 231 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53822 UniProtKB Transmembrane 232 252 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53822 UniProtKB Topological domain 253 254 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53822 UniProtKB Transmembrane 255 275 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53822 UniProtKB Topological domain 276 381 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47187 1 383 +P47187 UniProtKB Chain 1 383 . . . ID=PRO_0000207516;Note=Protein COS5 +P47187 UniProtKB Topological domain 1 42 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47187 UniProtKB Transmembrane 43 63 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47187 UniProtKB Topological domain 64 72 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47187 UniProtKB Transmembrane 73 93 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47187 UniProtKB Topological domain 94 232 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47187 UniProtKB Transmembrane 233 253 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47187 UniProtKB Topological domain 254 254 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47187 UniProtKB Transmembrane 255 275 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47187 UniProtKB Topological domain 276 383 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38723 1 381 +P38723 UniProtKB Chain 1 381 . . . ID=PRO_0000207519;Note=Protein COS8 +P38723 UniProtKB Topological domain 1 42 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38723 UniProtKB Transmembrane 43 63 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38723 UniProtKB Topological domain 64 72 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38723 UniProtKB Transmembrane 73 93 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38723 UniProtKB Topological domain 94 237 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38723 UniProtKB Transmembrane 238 258 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38723 UniProtKB Topological domain 259 381 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P21592 1 462 +P21592 UniProtKB Transit peptide 1 30 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21592 UniProtKB Chain 31 462 . . . ID=PRO_0000035925;Note=Protoheme IX farnesyltransferase%2C mitochondrial +P21592 UniProtKB Transmembrane 141 165 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21592 UniProtKB Transmembrane 180 198 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21592 UniProtKB Transmembrane 221 239 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21592 UniProtKB Transmembrane 250 268 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21592 UniProtKB Transmembrane 338 356 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21592 UniProtKB Transmembrane 369 386 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21592 UniProtKB Transmembrane 429 453 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40086 1 486 +P40086 UniProtKB Chain 1 486 . . . ID=PRO_0000183933;Note=Cytochrome c oxidase assembly protein COX15 +P40086 UniProtKB Transmembrane 86 106 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40086 UniProtKB Transmembrane 171 191 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40086 UniProtKB Transmembrane 201 221 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40086 UniProtKB Transmembrane 244 264 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40086 UniProtKB Transmembrane 294 314 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40086 UniProtKB Transmembrane 403 423 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40086 UniProtKB Transmembrane 425 445 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P10174 1 60 +P10174 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3013877;Dbxref=PMID:3013877 +P10174 UniProtKB Chain 2 60 . . . ID=PRO_0000183907;Note=Cytochrome c oxidase subunit 7 +P10174 UniProtKB Transmembrane 31 51 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12150 1 2958 +Q12150 UniProtKB Chain 1 2958 . . . ID=PRO_0000228143;Note=Protein CSF1 +Q12150 UniProtKB Topological domain 1 17 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Transmembrane 18 38 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Topological domain 39 2958 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 82 82 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 117 117 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 144 144 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 271 271 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 478 478 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 530 530 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 816 816 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 821 821 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 839 839 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 892 892 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 1309 1309 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 1368 1368 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 1453 1453 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 1785 1785 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 1921 1921 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 2130 2130 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 2146 2146 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 2280 2280 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 2337 2337 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 2520 2520 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 2578 2578 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 2719 2719 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12150 UniProtKB Glycosylation 2869 2869 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P15790 1 372 +P15790 UniProtKB Chain 1 372 . . . ID=PRO_0000085889;Note=Casein kinase II subunit alpha +P15790 UniProtKB Domain 40 363 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P15790 UniProtKB Nucleotide binding 46 54 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P15790 UniProtKB Active site 195 195 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P15790 UniProtKB Binding site 69 69 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P15790 UniProtKB Beta strand 10 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 15 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 21 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FI1 +P15790 UniProtKB Beta strand 37 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Beta strand 53 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Turn 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Beta strand 65 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 76 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 103 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 112 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 129 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Beta strand 136 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Turn 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Beta strand 148 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 160 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 164 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 169 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 198 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Beta strand 201 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 205 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Beta strand 209 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 234 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 239 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 251 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Beta strand 269 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 277 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 290 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 306 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LFI +P15790 UniProtKB Helix 319 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Turn 325 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 328 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 334 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 348 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 354 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 361 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +P15790 UniProtKB Helix 364 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JR7 +##sequence-region P19454 1 339 +P19454 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3468112;Dbxref=PMID:3468112 +P19454 UniProtKB Chain 2 339 . . . ID=PRO_0000085896;Note=Casein kinase II subunit alpha' +P19454 UniProtKB Domain 50 334 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P19454 UniProtKB Nucleotide binding 56 64 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P19454 UniProtKB Active site 167 167 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P19454 UniProtKB Binding site 79 79 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +##sequence-region Q12748 1 733 +Q12748 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12748 UniProtKB Chain 2 733 . . . ID=PRO_0000079493;Note=Central kinetochore subunit CTF3 +Q12748 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P47977 1 285 +P47977 UniProtKB Chain 1 285 . . . ID=PRO_0000089174;Note=mRNA decay factor CTH2 +P47977 UniProtKB Zinc finger 169 197 . . . Note=C3H1-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 +P47977 UniProtKB Zinc finger 207 235 . . . Note=C3H1-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 +P47977 UniProtKB Region 37 55 . . . Note=Required for mRNA decay activity +P47977 UniProtKB Mutagenesis 190 190 . . . Note=Abolishes mRNA binding. C->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15652485;Dbxref=PMID:15652485 +P47977 UniProtKB Mutagenesis 213 213 . . . Note=Abolishes mRNA binding. C->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15652485;Dbxref=PMID:15652485 +##sequence-region Q08923 1 506 +Q08923 UniProtKB Chain 1 506 . . . ID=PRO_0000234079;Note=Histone deacetylase complex subunit CTI6 +Q08923 UniProtKB Zinc finger 72 123 . . . Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 +Q08923 UniProtKB Modified residue 174 174 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08923 UniProtKB Modified residue 175 175 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08923 UniProtKB Modified residue 177 177 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08923 UniProtKB Modified residue 216 216 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q08923 UniProtKB Modified residue 267 267 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08923 UniProtKB Mutagenesis 95 95 . . . Note=Impairs growth under iron-limiting conditions. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15133041;Dbxref=PMID:15133041 +Q08923 UniProtKB Mutagenesis 100 100 . . . Note=Impairs growth under iron-limiting conditions. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15133041;Dbxref=PMID:15133041 +Q08923 UniProtKB Sequence conflict 342 342 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12734 1 1121 +Q12734 UniProtKB Chain 1 1121 . . . ID=PRO_0000228156;Note=Transcription factor CSR2 +Q12734 UniProtKB Compositional bias 304 346 . . . Note=Asn-rich +Q12734 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12734 UniProtKB Modified residue 46 46 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12734 UniProtKB Modified residue 127 127 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12734 UniProtKB Modified residue 327 327 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12734 UniProtKB Modified residue 987 987 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12734 UniProtKB Cross-link 841 841 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region Q06032 1 482 +Q06032 UniProtKB Chain 1 482 . . . ID=PRO_0000232995;Note=Chromosome stability protein 9 +Q06032 UniProtKB Compositional bias 333 445 . . . Note=Ser-rich +##sequence-region Q02732 1 369 +Q02732 UniProtKB Chain 1 369 . . . ID=PRO_0000079492;Note=Central kinetochore subunit CTF19 +Q02732 UniProtKB Coiled coil 51 87 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P46962 1 323 +P46962 UniProtKB Chain 1 323 . . . ID=PRO_0000080507;Note=CTD kinase subunit beta +##sequence-region Q03220 1 320 +Q03220 UniProtKB Chain 1 320 . . . ID=PRO_0000210120;Note=Polynucleotide 5'-triphosphatase +##sequence-region P38818 1 585 +P38818 UniProtKB Chain 1 585 . . . ID=PRO_0000202911;Note=Cytochrome c lysine N-methyltransferase 1 +P38818 UniProtKB Domain 18 273 . . . Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 +P38818 UniProtKB Region 186 288 . . . Note=SET-like +P38818 UniProtKB Sequence conflict 256 256 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P41817 1 306 +P41817 UniProtKB Chain 1 306 . . . ID=PRO_0000048859;Note=Homeobox protein CUP9 +P41817 UniProtKB DNA binding 162 224 . . . Note=Homeobox%3B TALE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00108 +##sequence-region P53333 1 577 +P53333 UniProtKB Chain 1 577 . . . ID=PRO_0000215678;Note=Pre-mRNA-splicing factor CWC22 +P53333 UniProtKB Domain 22 204 . . . Note=MIF4G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00698 +P53333 UniProtKB Domain 290 407 . . . Note=MI;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00698 +P53333 UniProtKB Compositional bias 533 577 . . . Note=Arg-rich +P53333 UniProtKB Helix 9 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Turn 34 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 37 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Turn 49 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 53 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 73 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 88 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 111 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 132 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 148 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 167 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 188 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Turn 217 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 237 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 286 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Beta strand 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Turn 304 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 308 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Turn 319 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 324 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Beta strand 336 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 341 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 355 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 373 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 380 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 399 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Beta strand 409 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 414 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 434 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Beta strand 447 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 455 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53333 UniProtKB Helix 475 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P25603 1 130 +P25603 UniProtKB Chain 1 130 . . . ID=PRO_0000079617;Note=Putative uncharacterized protein CWH36 +##sequence-region P25618 1 953 +P25618 UniProtKB Chain 1 953 . . . ID=PRO_0000021052;Note=Protein CWH43 +P25618 UniProtKB Topological domain 1 7 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 29 64 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Transmembrane 65 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 86 91 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Transmembrane 92 112 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 113 117 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Transmembrane 118 138 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 139 149 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Transmembrane 150 170 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 171 175 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Transmembrane 176 196 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 197 278 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Transmembrane 279 299 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 300 307 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Transmembrane 308 328 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 329 330 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Transmembrane 331 351 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 352 352 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Transmembrane 353 368 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 369 380 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Transmembrane 381 401 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 402 420 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Transmembrane 421 441 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 442 450 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Transmembrane 451 471 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 472 495 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Transmembrane 496 516 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 517 517 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Transmembrane 518 538 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 539 547 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Transmembrane 548 568 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 569 585 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Transmembrane 586 606 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 607 613 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Transmembrane 614 634 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 635 642 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Transmembrane 643 663 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Topological domain 664 953 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Region 1 229 . . . Note=PGAP2-like +P25618 UniProtKB Region 230 953 . . . Note=PGAP2IP-like +P25618 UniProtKB Region 862 882 . . . Note=Required for function in lipid remodeling +P25618 UniProtKB Active site 802 802 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25618 UniProtKB Glycosylation 419 419 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Glycosylation 490 490 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Glycosylation 767 767 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Glycosylation 792 792 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Glycosylation 825 825 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25618 UniProtKB Mutagenesis 57 57 . . . Note=Causes destabilization of the protein and induces the release of cell wall proteins in the culture medium. G->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11427965,ECO:0000269|PubMed:17761529;Dbxref=PMID:11427965,PMID:17761529 +P25618 UniProtKB Mutagenesis 472 472 . . . Note=No effect on introduction of ceramides into the GPI anchor. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17761529;Dbxref=PMID:17761529 +P25618 UniProtKB Mutagenesis 693 693 . . . Note=No effect on introduction of ceramides into the GPI anchor. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17761529;Dbxref=PMID:17761529 +P25618 UniProtKB Mutagenesis 713 713 . . . Note=Impairs the introduction of ceramides into the GPI anchor. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17714445;Dbxref=PMID:17714445 +P25618 UniProtKB Mutagenesis 770 770 . . . Note=No effect on introduction of ceramides into the GPI anchor. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17761529;Dbxref=PMID:17761529 +P25618 UniProtKB Mutagenesis 771 771 . . . Note=No effect on introduction of ceramides into the GPI anchor. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17761529;Dbxref=PMID:17761529 +P25618 UniProtKB Mutagenesis 802 802 . . . Note=Abrogates the introduction of ceramides into the GPI anchor. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17714445;Dbxref=PMID:17714445 +P25618 UniProtKB Mutagenesis 807 807 . . . Note=No effect on introduction of ceramides into the GPI anchor. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17761529;Dbxref=PMID:17761529 +P25618 UniProtKB Mutagenesis 862 862 . . . Note=Impairs the introduction of ceramides into the GPI anchor. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17761529;Dbxref=PMID:17761529 +P25618 UniProtKB Mutagenesis 882 882 . . . Note=Abrogates the introduction of ceramides into the GPI anchor. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17761529;Dbxref=PMID:17761529 +##sequence-region P53271 1 262 +P53271 UniProtKB Chain 1 262 . . . ID=PRO_0000213499;Note=Conserved oligomeric Golgi complex subunit 2 +P53271 UniProtKB Helix 110 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQQ +P53271 UniProtKB Helix 133 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQQ +P53271 UniProtKB Beta strand 154 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQQ +P53271 UniProtKB Helix 158 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQQ +P53271 UniProtKB Helix 184 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQQ +P53271 UniProtKB Helix 214 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQQ +P53271 UniProtKB Turn 245 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQQ +P53271 UniProtKB Helix 249 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQQ +##sequence-region Q04632 1 607 +Q04632 UniProtKB Chain 1 607 . . . ID=PRO_0000213525;Note=Conserved oligomeric Golgi complex subunit 8 +Q04632 UniProtKB Modified residue 410 410 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P07255 1 59 +P07255 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3013877;Dbxref=PMID:3013877 +P07255 UniProtKB Chain 2 56 . . . ID=PRO_0000006076;Note=Cytochrome c oxidase subunit 7A +P07255 UniProtKB Propeptide 57 59 . . . ID=PRO_0000006077;Note=Removed in mature form +P07255 UniProtKB Transmembrane 16 34 . . . Note=Helical +##sequence-region P36064 1 111 +P36064 UniProtKB Chain 1 111 . . . ID=PRO_0000203147;Note=COX assembly mitochondrial protein +P36064 UniProtKB Domain 39 82 . . . Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +P36064 UniProtKB Motif 42 52 . . . Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +P36064 UniProtKB Motif 64 74 . . . Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +P36064 UniProtKB Disulfide bond 42 74 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +P36064 UniProtKB Disulfide bond 52 64 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +##sequence-region P38845 1 465 +P38845 UniProtKB Chain 1 465 . . . ID=PRO_0000202923;Note=Cruciform DNA-recognizing protein 1 +P38845 UniProtKB Chain 1 160 . . . ID=PRO_0000409594;Note=CRP1 short N-terminal subpeptide +P38845 UniProtKB Chain 161 465 . . . ID=PRO_0000409595;Note=CRP1 short C-terminal subpeptide +P38845 UniProtKB Region 160 161 . . . Note=X-DNA-binding +P38845 UniProtKB Modified residue 153 153 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38845 UniProtKB Modified residue 156 156 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38845 UniProtKB Modified residue 182 182 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38845 UniProtKB Modified residue 271 271 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38845 UniProtKB Modified residue 295 295 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38845 UniProtKB Modified residue 319 319 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38845 UniProtKB Modified residue 343 343 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38845 UniProtKB Modified residue 366 366 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38845 UniProtKB Modified residue 394 394 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38845 UniProtKB Modified residue 440 440 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P41902 1 69 +P41902 UniProtKB Chain 1 69 . . . ID=PRO_0000197370;Note=Metallothionein-like protein CRS5 +##sequence-region P33307 1 960 +P33307 UniProtKB Chain 1 960 . . . ID=PRO_0000117293;Note=Importin alpha re-exporter +P33307 UniProtKB Repeat 1 33 . . . Note=HEAT 1 +P33307 UniProtKB Domain 23 96 . . . Note=Importin N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00115 +P33307 UniProtKB Repeat 34 73 . . . Note=HEAT 2 +P33307 UniProtKB Repeat 74 120 . . . Note=HEAT 3 +P33307 UniProtKB Repeat 121 157 . . . Note=HEAT 4 +P33307 UniProtKB Repeat 158 220 . . . Note=HEAT 5 +P33307 UniProtKB Repeat 221 278 . . . Note=HEAT 6 +P33307 UniProtKB Repeat 279 323 . . . Note=HEAT 7 +P33307 UniProtKB Repeat 324 392 . . . Note=HEAT 8 +P33307 UniProtKB Repeat 393 445 . . . Note=HEAT 9 +P33307 UniProtKB Repeat 446 489 . . . Note=HEAT 10 +P33307 UniProtKB Repeat 490 528 . . . Note=HEAT 11 +P33307 UniProtKB Repeat 529 586 . . . Note=HEAT 12 +P33307 UniProtKB Repeat 587 630 . . . Note=HEAT 13 +P33307 UniProtKB Repeat 631 674 . . . Note=HEAT 14 +P33307 UniProtKB Repeat 675 716 . . . Note=HEAT 15 +P33307 UniProtKB Repeat 717 751 . . . Note=HEAT 16 +P33307 UniProtKB Repeat 752 794 . . . Note=HEAT 17 +P33307 UniProtKB Repeat 795 826 . . . Note=HEAT 18 +P33307 UniProtKB Repeat 827 928 . . . Note=HEAT 19%3B with insert +P33307 UniProtKB Repeat 929 960 . . . Note=HEAT 20 +P33307 UniProtKB Motif 366 381 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33307 UniProtKB Sequence conflict 515 515 . . . Note=Y->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33307 UniProtKB Helix 3 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 20 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 36 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 51 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Beta strand 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Beta strand 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 80 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 99 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Turn 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 124 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 139 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 161 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 197 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 223 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 229 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 245 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z3H +P33307 UniProtKB Beta strand 253 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z3H +P33307 UniProtKB Helix 258 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 278 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 303 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z3H +P33307 UniProtKB Helix 306 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 323 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 327 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 332 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 343 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 351 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Turn 354 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 361 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 377 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 393 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Turn 415 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z3H +P33307 UniProtKB Helix 419 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Beta strand 434 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 452 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 461 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 472 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 486 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 491 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 510 523 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Beta strand 530 532 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Beta strand 535 537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 539 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Turn 542 545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 546 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 564 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 571 584 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Turn 585 588 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 589 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 592 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 613 628 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 632 634 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 635 651 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Turn 655 657 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 658 671 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Beta strand 672 674 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z3H +P33307 UniProtKB Turn 677 679 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 680 682 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 683 686 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 689 692 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Turn 695 697 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 698 712 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 713 715 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 720 730 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Turn 733 735 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 736 749 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 752 755 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 756 758 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 759 768 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 769 771 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 776 793 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 795 803 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 809 816 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 818 821 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 822 824 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 828 843 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 846 851 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 853 855 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 856 868 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 894 896 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z3H +P33307 UniProtKB Helix 899 901 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Turn 914 916 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 917 932 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Beta strand 934 936 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z3H +P33307 UniProtKB Helix 937 941 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 942 944 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +P33307 UniProtKB Helix 947 957 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +##sequence-region P43497 1 92 +P43497 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7768807;Dbxref=PMID:7768807 +P43497 UniProtKB Chain 21 71 . . . ID=PRO_0000033252;Note=Cell wall protein CWP2 +P43497 UniProtKB Propeptide 72 92 . . . ID=PRO_0000033253;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43497 UniProtKB Repeat 24 37 . . . Note=PIR1/2/3 +P43497 UniProtKB Site 33 33 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43497 UniProtKB Lipidation 71 71 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CX12 1 379 +P0CX12 UniProtKB Chain 1 379 . . . ID=PRO_0000207514;Note=Protein COS2 +P0CX12 UniProtKB Topological domain 1 72 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX12 UniProtKB Transmembrane 73 93 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX12 UniProtKB Topological domain 94 254 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX12 UniProtKB Transmembrane 255 275 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX12 UniProtKB Topological domain 276 379 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36034 1 407 +P36034 UniProtKB Chain 1 407 . . . ID=PRO_0000207520;Note=Protein COS9 +P36034 UniProtKB Transmembrane 75 95 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36034 UniProtKB Transmembrane 98 118 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36034 UniProtKB Transmembrane 261 281 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P19516 1 300 +P19516 UniProtKB Transmembrane 85 105 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19516 UniProtKB Topological domain 106 300 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19516 UniProtKB Sequence conflict 24 31 . . . Note=WLAPHALA->MVGTSCAS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19516 UniProtKB Sequence conflict 146 146 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19516 UniProtKB Sequence conflict 146 146 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32799 1 129 +P32799 UniProtKB Transit peptide 1 9 . . . Note=Mitochondrion +P32799 UniProtKB Chain 10 129 . . . ID=PRO_0000006127;Note=Cytochrome c oxidase subunit 6A%2C mitochondrial +##sequence-region P38824 1 151 +P38824 UniProtKB Transit peptide 1 10 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38824 UniProtKB Chain 11 151 . . . ID=PRO_0000202912;Note=Cytochrome c oxidase-assembly factor COX23%2C mitochondrial +P38824 UniProtKB Domain 101 143 . . . Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +P38824 UniProtKB Motif 104 114 . . . Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +P38824 UniProtKB Motif 125 135 . . . Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +P38824 UniProtKB Disulfide bond 104 135 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +P38824 UniProtKB Disulfide bond 114 125 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +##sequence-region P53314 1 239 +P53314 UniProtKB Chain 1 239 . . . ID=PRO_0000202859;Note=2'%2C3'-cyclic-nucleotide 3'-phosphodiesterase +P53314 UniProtKB Active site 39 39 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53314 UniProtKB Active site 150 150 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53314 UniProtKB Binding site 41 41 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53314 UniProtKB Binding site 152 152 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53314 UniProtKB Binding site 155 155 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53314 UniProtKB Mutagenesis 39 39 . . . Note=Abolishes cyclic nucleotide phosphodiesterase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10734185;Dbxref=PMID:10734185 +P53314 UniProtKB Mutagenesis 41 41 . . . Note=Reduces strongly cyclic nucleotide phosphodiesterase activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10734185;Dbxref=PMID:10734185 +P53314 UniProtKB Mutagenesis 150 150 . . . Note=Abolishes cyclic nucleotide phosphodiesterase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10734185;Dbxref=PMID:10734185 +P53314 UniProtKB Mutagenesis 152 152 . . . Note=Reduces strongly cyclic nucleotide phosphodiesterase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10734185;Dbxref=PMID:10734185 +##sequence-region Q12289 1 327 +Q12289 UniProtKB Chain 1 327 . . . ID=PRO_0000090681;Note=Mitochondrial carnitine carrier +Q12289 UniProtKB Transmembrane 33 49 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12289 UniProtKB Transmembrane 107 123 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12289 UniProtKB Transmembrane 141 162 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12289 UniProtKB Transmembrane 196 212 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12289 UniProtKB Transmembrane 244 260 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12289 UniProtKB Transmembrane 293 313 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12289 UniProtKB Repeat 33 126 . . . Note=Solcar 1 +Q12289 UniProtKB Repeat 139 221 . . . Note=Solcar 2 +Q12289 UniProtKB Repeat 237 321 . . . Note=Solcar 3 +##sequence-region P38892 1 291 +P38892 UniProtKB Chain 1 291 . . . ID=PRO_0000202943;Note=Probable S-adenosylmethionine-dependent methyltransferase CRG1 +P38892 UniProtKB Sequence conflict 23 23 . . . Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53968 1 678 +P53968 UniProtKB Chain 1 678 . . . ID=PRO_0000046804;Note=Transcriptional regulator CRZ1 +P53968 UniProtKB Zinc finger 569 591 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P53968 UniProtKB Zinc finger 597 619 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P53968 UniProtKB Compositional bias 115 140 . . . Note=Poly-Gln +P53968 UniProtKB Compositional bias 367 370 . . . Note=Poly-Asn +P53968 UniProtKB Compositional bias 483 487 . . . Note=Poly-Asn +P53968 UniProtKB Modified residue 170 170 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53968 UniProtKB Modified residue 175 175 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53968 UniProtKB Modified residue 245 245 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53968 UniProtKB Modified residue 385 385 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q08054 1 341 +Q08054 UniProtKB Chain 1 341 . . . ID=PRO_0000079399;Note=Chitin synthase 3 complex protein CSI2 +Q08054 UniProtKB Compositional bias 33 112 . . . Note=Poly-Ser +##sequence-region Q12348 1 645 +Q12348 UniProtKB Chain 1 645 . . . ID=PRO_0000121024;Note=COP9 signalosome complex subunit 10 +Q12348 UniProtKB Domain 430 540 . . . Note=PCI +##sequence-region P14306 1 219 +P14306 UniProtKB Chain 1 219 . . . ID=PRO_0000204753;Note=Carboxypeptidase Y inhibitor +P14306 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12473200;Dbxref=PMID:12473200 +P14306 UniProtKB Sequence conflict 56 56 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14306 UniProtKB Sequence conflict 165 165 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14306 UniProtKB Sequence conflict 211 219 . . . Note=SNFFYAETK->VQFLLCGNEIGIYIYICICIYFLDFSAFHLTFYYFCFIYVFVTNGQMFVGTNVYVKQNT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14306 UniProtKB Helix 2 4 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +P14306 UniProtKB Helix 7 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +P14306 UniProtKB Helix 20 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +P14306 UniProtKB Beta strand 33 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +P14306 UniProtKB Beta strand 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +P14306 UniProtKB Helix 54 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +P14306 UniProtKB Beta strand 62 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +P14306 UniProtKB Beta strand 89 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +P14306 UniProtKB Beta strand 108 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +P14306 UniProtKB Beta strand 133 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +P14306 UniProtKB Beta strand 144 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +P14306 UniProtKB Beta strand 161 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +P14306 UniProtKB Helix 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +P14306 UniProtKB Helix 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +P14306 UniProtKB Beta strand 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +P14306 UniProtKB Helix 197 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +P14306 UniProtKB Turn 203 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +P14306 UniProtKB Beta strand 207 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPX +##sequence-region P53301 1 507 +P53301 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53301 UniProtKB Chain 23 482 . . . ID=PRO_0000045430;Note=Probable glycosidase CRH1 +P53301 UniProtKB Propeptide 483 507 . . . ID=PRO_0000045431;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53301 UniProtKB Domain 34 260 . . . Note=GH16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01098 +P53301 UniProtKB Compositional bias 63 66 . . . Note=Poly-Ser +P53301 UniProtKB Compositional bias 301 481 . . . Note=Ser-rich +P53301 UniProtKB Compositional bias 301 310 . . . Note=Poly-Ser +P53301 UniProtKB Compositional bias 345 357 . . . Note=Poly-Ser +P53301 UniProtKB Compositional bias 387 391 . . . Note=Poly-Ser +P53301 UniProtKB Compositional bias 467 470 . . . Note=Poly-Ser +P53301 UniProtKB Active site 134 134 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53301 UniProtKB Active site 138 138 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53301 UniProtKB Lipidation 482 482 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53301 UniProtKB Glycosylation 117 117 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53301 UniProtKB Glycosylation 177 177 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53301 UniProtKB Glycosylation 201 201 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06538 1 782 +Q06538 UniProtKB Chain 1 782 . . . ID=PRO_0000247173;Note=Calcium permeable stress-gated cation channel 1 +Q06538 UniProtKB Topological domain 1 34 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Topological domain 56 116 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Transmembrane 117 139 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Topological domain 140 181 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Transmembrane 182 202 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Topological domain 203 440 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Transmembrane 441 461 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Topological domain 462 485 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Transmembrane 486 506 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Topological domain 507 530 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Transmembrane 531 551 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Topological domain 552 578 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Transmembrane 579 599 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Topological domain 600 621 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Transmembrane 622 642 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Topological domain 643 648 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Transmembrane 649 669 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Topological domain 670 681 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Transmembrane 682 702 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Topological domain 703 709 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Transmembrane 710 730 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Topological domain 731 782 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06538 UniProtKB Glycosylation 171 171 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P35206 1 410 +P35206 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Chain 18 410 . . . ID=PRO_0000021012;Note=Mannosyl phosphorylinositol ceramide synthase regulatory protein CSG2 +P35206 UniProtKB Topological domain 18 50 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Transmembrane 51 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Topological domain 72 141 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Transmembrane 142 161 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Topological domain 162 167 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Transmembrane 168 187 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Topological domain 188 197 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Transmembrane 198 217 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Topological domain 218 245 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Transmembrane 246 265 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Topological domain 266 285 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Transmembrane 286 305 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Topological domain 306 324 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Transmembrane 325 344 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Topological domain 345 355 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Transmembrane 356 374 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Topological domain 375 385 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Transmembrane 386 404 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Topological domain 405 410 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Glycosylation 35 35 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Glycosylation 49 49 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35206 UniProtKB Sequence conflict 68 68 . . . Note=L->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25651 1 190 +P25651 UniProtKB Chain 1 190 . . . ID=PRO_0000202577;Note=Monopolin complex subunit CSM1 +P25651 UniProtKB Coiled coil 31 70 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25651 UniProtKB Helix 11 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4X +P25651 UniProtKB Helix 71 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S +P25651 UniProtKB Beta strand 83 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S +P25651 UniProtKB Beta strand 96 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S +P25651 UniProtKB Beta strand 116 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S +P25651 UniProtKB Turn 126 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S +P25651 UniProtKB Beta strand 131 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S +P25651 UniProtKB Helix 143 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S +P25651 UniProtKB Helix 155 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S +P25651 UniProtKB Beta strand 161 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S +P25651 UniProtKB Helix 165 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S +P25651 UniProtKB Helix 168 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3N4S +##sequence-region Q08955 1 156 +Q08955 UniProtKB Chain 1 156 . . . ID=PRO_0000079404;Note=Chromosome segregation in meiosis protein 4 +Q08955 UniProtKB Transmembrane 131 151 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47130 1 423 +P47130 UniProtKB Chain 1 423 . . . ID=PRO_0000121047;Note=Cop9 signalosome complex subunit 12 +P47130 UniProtKB Domain 298 415 . . . Note=PCI +##sequence-region Q12468 1 440 +Q12468 UniProtKB Chain 1 440 . . . ID=PRO_0000194859;Note=COP9 signalosome complex subunit 5 +Q12468 UniProtKB Domain 71 218 . . . Note=MPN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182 +Q12468 UniProtKB Motif 164 177 . . . Note=JAMM motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182 +Q12468 UniProtKB Metal binding 164 164 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182 +Q12468 UniProtKB Metal binding 166 166 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182 +Q12468 UniProtKB Metal binding 177 177 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182 +Q12468 UniProtKB Mutagenesis 164 164 . . . Note=Abolishes deneddylation of CDC53. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12183637;Dbxref=PMID:12183637 +Q12468 UniProtKB Mutagenesis 166 166 . . . Note=Abolishes deneddylation of CDC53. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12183637;Dbxref=PMID:12183637 +Q12468 UniProtKB Mutagenesis 177 177 . . . Note=Abolishes deneddylation of CDC53. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12183637;Dbxref=PMID:12183637 +##sequence-region P25355 1 563 +P25355 UniProtKB Chain 1 563 . . . ID=PRO_0000202572;Note=Copper transport protein 86 +P25355 UniProtKB Modified residue 433 433 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25355 UniProtKB Modified residue 559 559 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P53923 1 493 +P53923 UniProtKB Chain 1 493 . . . ID=PRO_0000203432;Note=Cytoplasmic tRNA 2-thiolation protein 2 +P53923 UniProtKB Modified residue 489 489 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P53923 UniProtKB Natural variant 7 7 . . . Note=In strain: YJM230 and YJM320. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53923 UniProtKB Natural variant 71 71 . . . Note=In strain: SK1%2C V1-09%2C YJM1129%2C YJM269%2C YJM270%2C YJM320%2C YJM326%2C YJM230%2C YJM339 and YJM627. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53923 UniProtKB Natural variant 193 193 . . . Note=In strain: SK1%2C V1-09%2C YJM230%2C YJM320 and YJM339. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53923 UniProtKB Natural variant 409 409 . . . Note=In strain: YJM627. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53923 UniProtKB Natural variant 428 428 . . . Note=In strain: YJM627. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53923 UniProtKB Natural variant 436 436 . . . Note=In strain: YJM230 and YJM320. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53923 UniProtKB Natural variant 474 474 . . . Note=In strain: YJM1129%2C YJM269%2C YJM270%2C YJM326 and YJM627. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53923 UniProtKB Sequence conflict 36 36 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53830 1 285 +P53830 UniProtKB Chain 1 285 . . . ID=PRO_0000082037;Note=Cold sensitive U2 snRNA suppressor 2 +P53830 UniProtKB Domain 45 130 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P53830 UniProtKB Domain 183 265 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P53830 UniProtKB Modified residue 163 163 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P53830 UniProtKB Sequence conflict 235 235 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P00044 1 109 +P00044 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:5771953;Dbxref=PMID:5771953 +P00044 UniProtKB Chain 2 109 . . . ID=PRO_0000108337;Note=Cytochrome c iso-1 +P00044 UniProtKB Metal binding 24 24 . . . Note=Iron (heme axial ligand) +P00044 UniProtKB Metal binding 86 86 . . . Note=Iron (heme axial ligand) +P00044 UniProtKB Binding site 20 20 . . . Note=Heme (covalent) +P00044 UniProtKB Binding site 23 23 . . . Note=Heme (covalent) +P00044 UniProtKB Modified residue 78 78 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B by CTM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10791961;Dbxref=PMID:10791961 +P00044 UniProtKB Modified residue 79 79 . . . Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10821864,ECO:0000269|PubMed:18390544;Dbxref=PMID:10821864,PMID:18390544 +P00044 UniProtKB Mutagenesis 78 78 . . . Note=Loss of methylation by CTM1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10791961;Dbxref=PMID:10791961 +P00044 UniProtKB Helix 9 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0K +P00044 UniProtKB Turn 20 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0K +P00044 UniProtKB Beta strand 27 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PCC +P00044 UniProtKB Beta strand 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MU8 +P00044 UniProtKB Helix 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q5P +P00044 UniProtKB Beta strand 44 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0K +P00044 UniProtKB Beta strand 49 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CID +P00044 UniProtKB Helix 56 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0K +P00044 UniProtKB Beta strand 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MHM +P00044 UniProtKB Helix 67 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0K +P00044 UniProtKB Helix 77 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0K +P00044 UniProtKB Beta strand 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FHB +P00044 UniProtKB Helix 84 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KKE +P00044 UniProtKB Helix 94 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0K +##sequence-region P32898 1 989 +P32898 UniProtKB Chain 1 989 . . . ID=PRO_0000178012;Note=Mitochondrial presequence protease +P32898 UniProtKB Active site 87 87 . . . Note=Proton acceptor +P32898 UniProtKB Metal binding 84 84 . . . Note=Zinc%3B catalytic +P32898 UniProtKB Metal binding 88 88 . . . Note=Zinc%3B catalytic +P32898 UniProtKB Metal binding 185 185 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32898 UniProtKB Modified residue 920 920 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P32898 UniProtKB Mutagenesis 84 84 . . . Note=Loss of function. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15772085;Dbxref=PMID:15772085 +P32898 UniProtKB Mutagenesis 87 87 . . . Note=Loss of function. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15772085;Dbxref=PMID:15772085 +P32898 UniProtKB Mutagenesis 88 88 . . . Note=Loss of function. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15772085;Dbxref=PMID:15772085 +##sequence-region P32623 1 467 +P32623 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32623 UniProtKB Chain 24 445 . . . ID=PRO_0000065745;Note=Probable glycosidase CRH2 +P32623 UniProtKB Propeptide 446 467 . . . ID=PRO_0000232722;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32623 UniProtKB Domain 63 280 . . . Note=GH16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01098 +P32623 UniProtKB Compositional bias 354 442 . . . Note=Ser-rich +P32623 UniProtKB Active site 166 166 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32623 UniProtKB Active site 170 170 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32623 UniProtKB Lipidation 445 445 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32623 UniProtKB Glycosylation 28 28 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32623 UniProtKB Glycosylation 96 96 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32623 UniProtKB Glycosylation 190 190 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32623 UniProtKB Glycosylation 196 196 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32623 UniProtKB Glycosylation 233 233 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32623 UniProtKB Glycosylation 237 237 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32623 UniProtKB Glycosylation 261 261 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32623 UniProtKB Glycosylation 297 297 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32623 UniProtKB Glycosylation 310 310 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32623 UniProtKB Sequence conflict 130 130 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32623 UniProtKB Sequence conflict 130 130 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32623 UniProtKB Sequence conflict 130 130 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32623 UniProtKB Sequence conflict 291 291 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32623 UniProtKB Sequence conflict 291 291 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32623 UniProtKB Sequence conflict 291 291 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32623 UniProtKB Sequence conflict 354 354 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32623 UniProtKB Sequence conflict 354 354 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32623 UniProtKB Sequence conflict 354 354 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q05790 1 422 +Q05790 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05790 UniProtKB Chain 21 422 . . . ID=PRO_0000228141;Note=Probable glycosidase CRR1 +Q05790 UniProtKB Domain 67 339 . . . Note=GH16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01098 +Q05790 UniProtKB Active site 217 217 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05790 UniProtKB Active site 221 221 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38308 1 924 +P38308 UniProtKB Chain 1 924 . . . ID=PRO_0000202509;Note=F-box protein COS111 +P38308 UniProtKB Domain 185 236 . . . Note=F-box +P38308 UniProtKB Compositional bias 2 162 . . . Note=Ser-rich +P38308 UniProtKB Compositional bias 354 475 . . . Note=Ser-rich +P38308 UniProtKB Sequence conflict 727 731 . . . Note=TFRQH->SWRND;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38308 UniProtKB Sequence conflict 727 731 . . . Note=TFRQH->SWRND;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38308 UniProtKB Sequence conflict 917 917 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38308 UniProtKB Sequence conflict 917 917 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38308 UniProtKB Sequence conflict 921 921 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38308 UniProtKB Sequence conflict 921 921 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04368 1 295 +Q04368 UniProtKB Chain 1 295 . . . ID=PRO_0000079398;Note=Cop9 signalosome-interactor 1 +##sequence-region P49573 1 406 +P49573 UniProtKB Chain 1 406 . . . ID=PRO_0000079496;Note=Copper transport protein CTR1 +P49573 UniProtKB Transmembrane 153 173 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P49573 UniProtKB Transmembrane 251 271 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P49573 UniProtKB Topological domain 272 406 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P49573 UniProtKB Repeat 9 27 . . . Note=1 +P49573 UniProtKB Repeat 28 46 . . . Note=2 +P49573 UniProtKB Repeat 47 65 . . . Note=3 +P49573 UniProtKB Region 9 65 . . . Note=3 X 19 AA tandem repeats of S-M-X-M-X-A-M-S-S-A-S-K-T-X-X-S-X-M-X +P49573 UniProtKB Compositional bias 1 127 . . . Note=Met/Ser-rich +P49573 UniProtKB Compositional bias 114 117 . . . Note=Poly-Ser +P49573 UniProtKB Modified residue 344 344 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P49573 UniProtKB Modified residue 349 349 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P49573 UniProtKB Modified residue 356 356 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P49573 UniProtKB Modified residue 369 369 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P49573 UniProtKB Glycosylation 113 113 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P49573 UniProtKB Glycosylation 148 148 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P49573 UniProtKB Cross-link 345 345 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P38865 1 189 +P38865 UniProtKB Chain 1 189 . . . ID=PRO_0000195046;Note=Copper transport protein CTR2 +P38865 UniProtKB Topological domain 1 81 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38865 UniProtKB Transmembrane 82 102 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38865 UniProtKB Topological domain 103 142 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38865 UniProtKB Transmembrane 143 163 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38865 UniProtKB Topological domain 164 189 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P89105 1 1077 +P89105 UniProtKB Chain 1 1077 . . . ID=PRO_0000106280;Note=RNA polymerase-associated protein CTR9 +P89105 UniProtKB Repeat 56 89 . . . Note=TPR 1 +P89105 UniProtKB Repeat 138 174 . . . Note=TPR 2 +P89105 UniProtKB Repeat 183 216 . . . Note=TPR 3 +P89105 UniProtKB Repeat 218 251 . . . Note=TPR 4 +P89105 UniProtKB Repeat 298 332 . . . Note=TPR 5 +P89105 UniProtKB Repeat 338 371 . . . Note=TPR 6 +P89105 UniProtKB Repeat 373 405 . . . Note=TPR 7 +P89105 UniProtKB Repeat 421 455 . . . Note=TPR 8 +P89105 UniProtKB Repeat 462 495 . . . Note=TPR 9 +P89105 UniProtKB Repeat 501 534 . . . Note=TPR 10 +P89105 UniProtKB Repeat 540 572 . . . Note=TPR 11 +P89105 UniProtKB Repeat 664 697 . . . Note=TPR 12 +P89105 UniProtKB Repeat 699 731 . . . Note=TPR 13 +P89105 UniProtKB Repeat 732 764 . . . Note=TPR 14 +P89105 UniProtKB Repeat 768 801 . . . Note=TPR 15 +P89105 UniProtKB Repeat 830 863 . . . Note=TPR 16 +P89105 UniProtKB Modified residue 1015 1015 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P89105 UniProtKB Modified residue 1017 1017 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P89105 UniProtKB Sequence conflict 197 197 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P89105 UniProtKB Sequence conflict 197 197 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P89105 UniProtKB Sequence conflict 461 461 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P89105 UniProtKB Sequence conflict 674 674 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P89105 UniProtKB Sequence conflict 674 674 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P89105 UniProtKB Sequence conflict 786 786 . . . Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P89105 UniProtKB Sequence conflict 786 786 . . . Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P89105 UniProtKB Sequence conflict 903 903 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P89105 UniProtKB Sequence conflict 903 903 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P89105 UniProtKB Sequence conflict 907 907 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P89105 UniProtKB Sequence conflict 907 907 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P89105 UniProtKB Sequence conflict 926 927 . . . Note=GW->ER;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P89105 UniProtKB Sequence conflict 926 927 . . . Note=GW->ER;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P89105 UniProtKB Sequence conflict 956 959 . . . Note=LIQE->IFQV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P89105 UniProtKB Sequence conflict 956 959 . . . Note=LIQE->IFQV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P89105 UniProtKB Sequence conflict 987 987 . . . Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P89105 UniProtKB Sequence conflict 987 987 . . . Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P89105 UniProtKB Sequence conflict 1045 1077 . . . Note=DSDEEEAQMSGSEQNKNDDNDENNDNDDNDGLF->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04201 1 117 +Q04201 UniProtKB Chain 1 117 . . . ID=PRO_0000203244;Note=CUE domain-containing protein CUE4 +Q04201 UniProtKB Domain 74 116 . . . Note=CUE;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00468 +Q04201 UniProtKB Modified residue 48 48 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q04201 UniProtKB Cross-link 37 37 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q08412 1 411 +Q08412 UniProtKB Chain 1 411 . . . ID=PRO_0000270974;Note=Ubiquitin-binding protein CUE5 +Q08412 UniProtKB Domain 97 140 . . . Note=CUE;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00468 +Q08412 UniProtKB Motif 373 376 . . . Note=AIM +Q08412 UniProtKB Compositional bias 77 81 . . . Note=Poly-Glu;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08412 UniProtKB Compositional bias 204 207 . . . Note=Poly-Arg;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08412 UniProtKB Modified residue 21 21 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q08412 UniProtKB Modified residue 36 36 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q08412 UniProtKB Modified residue 70 70 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q08412 UniProtKB Modified residue 91 91 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q08412 UniProtKB Modified residue 167 167 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q08412 UniProtKB Modified residue 220 220 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q08412 UniProtKB Modified residue 309 309 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q08412 UniProtKB Modified residue 318 318 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08412 UniProtKB Modified residue 346 346 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08412 UniProtKB Modified residue 348 348 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q08412 UniProtKB Modified residue 352 352 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08412 UniProtKB Modified residue 364 364 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q08412 UniProtKB Modified residue 367 367 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08412 UniProtKB Modified residue 407 407 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q08412 UniProtKB Cross-link 15 15 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q08412 UniProtKB Cross-link 59 59 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q08412 UniProtKB Cross-link 76 76 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q08412 UniProtKB Cross-link 156 156 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q08412 UniProtKB Cross-link 354 354 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q08412 UniProtKB Cross-link 396 396 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +Q08412 UniProtKB Mutagenesis 109 109 . . . Note=Impairs interaction with ubiquitin%3B when associated with A-110. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25042851;Dbxref=PMID:25042851 +Q08412 UniProtKB Mutagenesis 110 110 . . . Note=Impairs interaction with ubiquitin%3B when associated with A-109. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25042851;Dbxref=PMID:25042851 +Q08412 UniProtKB Mutagenesis 135 135 . . . Note=Impairs interaction with ubiquitin%3B when associated with A-136. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25042851;Dbxref=PMID:25042851 +Q08412 UniProtKB Mutagenesis 136 136 . . . Note=Impairs interaction with ubiquitin%3B when associated with A-135. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25042851;Dbxref=PMID:25042851 +Q08412 UniProtKB Mutagenesis 373 373 . . . Note=Impairs interaction with ATG8. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25042851;Dbxref=PMID:25042851 +Q08412 UniProtKB Mutagenesis 376 376 . . . Note=Impairs interaction with ATG8. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25042851;Dbxref=PMID:25042851 +##sequence-region P47050 1 842 +P47050 UniProtKB Chain 1 842 . . . ID=PRO_0000119807;Note=Cullin-8 +P47050 UniProtKB Region 1 50 . . . Note=Required for interaction with MMS1 +P47050 UniProtKB Cross-link 791 791 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14519104;Dbxref=PMID:14519104 +P47050 UniProtKB Mutagenesis 680 686 . . . Note=Disrupts interaction with HRT1 and prevents RUB1/NEDD8 modification. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12676951;Dbxref=PMID:12676951 +P47050 UniProtKB Mutagenesis 791 791 . . . Note=Prevents RUB1/NEDD8 modification. K->A%2CR;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12676951,ECO:0000269|PubMed:14519104;Dbxref=PMID:12676951,PMID:14519104 +##sequence-region P28320 1 278 +P28320 UniProtKB Chain 1 278 . . . ID=PRO_0000203163;Note=Protein CWC16 +P28320 UniProtKB Motif 242 258 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28320 UniProtKB Motif 260 278 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28320 UniProtKB Helix 17 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28320 UniProtKB Beta strand 31 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28320 UniProtKB Beta strand 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28320 UniProtKB Beta strand 50 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28320 UniProtKB Beta strand 64 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28320 UniProtKB Beta strand 75 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28320 UniProtKB Beta strand 82 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28320 UniProtKB Beta strand 89 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28320 UniProtKB Beta strand 94 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28320 UniProtKB Beta strand 101 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P53854 1 179 +P53854 UniProtKB Chain 1 179 . . . ID=PRO_0000079596;Note=Pre-mRNA-splicing factor CWC25 +P53854 UniProtKB Coiled coil 25 57 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53854 UniProtKB Modified residue 129 129 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53854 UniProtKB Helix 6 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53854 UniProtKB Beta strand 10 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53854 UniProtKB Helix 19 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region Q12046 1 339 +Q12046 UniProtKB Chain 1 339 . . . ID=PRO_0000081552;Note=Pre-mRNA-splicing factor CWC2 +Q12046 UniProtKB Domain 135 228 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q12046 UniProtKB Zinc finger 67 94 . . . Note=C3H1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 +Q12046 UniProtKB Modified residue 335 335 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12046 UniProtKB Modified residue 336 336 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12046 UniProtKB Mutagenesis 73 73 . . . Note=Inhibits cell growth. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19435883;Dbxref=PMID:19435883 +Q12046 UniProtKB Mutagenesis 79 79 . . . Note=No effect. Synthetic lethal when associated with CLF1 lacking a TPR domain. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12871902;Dbxref=PMID:12871902 +Q12046 UniProtKB Mutagenesis 87 87 . . . Note=Inhibits cell growth. C->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19435883;Dbxref=PMID:19435883 +Q12046 UniProtKB Mutagenesis 186 186 . . . Note=Inhibits cell growth. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19435883;Dbxref=PMID:19435883 +Q12046 UniProtKB Helix 4 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Helix 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Beta strand 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TP2 +Q12046 UniProtKB Helix 30 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Beta strand 41 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Helix 55 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Helix 63 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Helix 74 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Helix 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Beta strand 88 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Helix 96 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Beta strand 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Beta strand 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Helix 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Beta strand 125 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TP2 +Q12046 UniProtKB Helix 129 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TP2 +Q12046 UniProtKB Beta strand 136 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Helix 144 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Helix 153 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Beta strand 170 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Helix 177 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Beta strand 181 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Helix 189 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Beta strand 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12046 UniProtKB Helix 212 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Beta strand 222 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U1L +Q12046 UniProtKB Helix 232 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P53008 1 833 +P53008 UniProtKB Chain 1 833 . . . ID=PRO_0000057713;Note=Mannosyl-oligosaccharide glucosidase +P53008 UniProtKB Topological domain 1 10 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53008 UniProtKB Transmembrane 11 28 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53008 UniProtKB Topological domain 29 833 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53008 UniProtKB Active site 601 601 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23536181;Dbxref=PMID:23536181 +P53008 UniProtKB Active site 804 804 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23536181;Dbxref=PMID:23536181 +P53008 UniProtKB Binding site 42 42 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23536181;Dbxref=PMID:23536181 +P53008 UniProtKB Binding site 122 122 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23536181;Dbxref=PMID:23536181 +P53008 UniProtKB Binding site 143 143 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23536181;Dbxref=PMID:23536181 +P53008 UniProtKB Glycosylation 42 42 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53008 UniProtKB Glycosylation 122 122 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53008 UniProtKB Glycosylation 135 135 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53008 UniProtKB Glycosylation 787 787 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53008 UniProtKB Disulfide bond 669 685 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23536181;Dbxref=PMID:23536181 +P53008 UniProtKB Mutagenesis 601 601 . . . Note=Abrogates catalytic activity. D->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23536181;Dbxref=PMID:23536181 +P53008 UniProtKB Mutagenesis 804 804 . . . Note=Abrogates catalytic activity. E->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23536181;Dbxref=PMID:23536181 +P53008 UniProtKB Helix 35 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 46 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 54 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 68 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 82 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 97 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Turn 106 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 109 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Turn 117 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 121 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 136 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 152 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 164 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 171 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 183 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Turn 190 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 193 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 227 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 235 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 241 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 267 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 270 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 286 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 302 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 320 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 354 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 373 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 401 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Turn 415 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 420 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 423 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 438 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 461 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 466 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 475 477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 489 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 529 532 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 534 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 567 572 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 576 578 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 596 598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 616 635 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 639 658 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Turn 663 666 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 670 673 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Turn 675 677 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 681 684 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 689 696 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 706 715 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Turn 717 720 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 725 729 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Turn 734 737 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 742 745 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 749 762 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 764 767 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 776 798 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 804 806 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Turn 808 810 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Beta strand 813 818 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 822 825 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +P53008 UniProtKB Helix 826 831 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J5T +##sequence-region P28319 1 239 +P28319 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7768807;Dbxref=PMID:7768807 +P28319 UniProtKB Chain 21 217 . . . ID=PRO_0000033250;Note=Cell wall protein CWP1 +P28319 UniProtKB Propeptide 218 239 . . . ID=PRO_0000033251;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28319 UniProtKB Repeat 194 212 . . . Note=PIR1/2/3 +P28319 UniProtKB Compositional bias 106 198 . . . Note=Ser-rich +P28319 UniProtKB Site 204 204 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28319 UniProtKB Lipidation 217 217 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28319 UniProtKB Natural variant 19 27 . . . Note=In strain: CLIB 410. IADSEEFGL->LPIPKNSAW +P28319 UniProtKB Sequence conflict 189 189 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28319 UniProtKB Sequence conflict 189 189 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28319 UniProtKB Sequence conflict 189 189 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28319 UniProtKB Sequence conflict 189 189 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28319 UniProtKB Sequence conflict 189 189 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28319 UniProtKB Sequence conflict 189 189 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28319 UniProtKB Sequence conflict 189 189 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28319 UniProtKB Sequence conflict 189 189 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28319 UniProtKB Sequence conflict 189 189 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28319 UniProtKB Sequence conflict 189 189 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07560 1 283 +Q07560 UniProtKB Chain 1 283 . . . ID=PRO_0000056810;Note=Cardiolipin synthase (CMP-forming) +Q07560 UniProtKB Transmembrane 83 103 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07560 UniProtKB Transmembrane 155 175 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07560 UniProtKB Transmembrane 209 229 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08226 1 957 +Q08226 UniProtKB Chain 1 957 . . . ID=PRO_0000235920;Note=Protein CRT10 +Q08226 UniProtKB Modified residue 704 704 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08226 UniProtKB Sequence conflict 604 604 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53859 1 292 +P53859 UniProtKB Chain 1 292 . . . ID=PRO_0000079403;Note=Exosome complex component CSL4 +P53859 UniProtKB Modified residue 94 94 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P53859 UniProtKB Beta strand 9 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Beta strand 15 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Beta strand 32 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Beta strand 41 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Beta strand 51 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Beta strand 60 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Beta strand 106 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Helix 115 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36 +P53859 UniProtKB Turn 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36 +P53859 UniProtKB Helix 124 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36 +P53859 UniProtKB Beta strand 138 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Beta strand 148 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Beta strand 162 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Helix 183 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Turn 190 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Turn 195 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +P53859 UniProtKB Beta strand 202 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Helix 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Beta strand 212 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Helix 215 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Helix 220 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Beta strand 229 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Beta strand 240 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Beta strand 253 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Turn 259 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Beta strand 268 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Beta strand 274 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Turn 278 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53859 UniProtKB Beta strand 283 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +##sequence-region Q03981 1 162 +Q03981 UniProtKB Chain 1 162 . . . ID=PRO_0000121020;Note=COP9 signalosome complex subunit 9 +Q03981 UniProtKB Domain 6 118 . . . Note=PCI +##sequence-region P38226 1 397 +P38226 UniProtKB Chain 1 397 . . . ID=PRO_0000208207;Note=Uncharacterized acyltransferase CST26 +P38226 UniProtKB Transmembrane 13 33 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38226 UniProtKB Transmembrane 58 78 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38226 UniProtKB Transmembrane 118 138 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38226 UniProtKB Transmembrane 377 397 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38226 UniProtKB Motif 112 117 . . . Note=HXXXXD motif +##sequence-region P36075 1 443 +P36075 UniProtKB Chain 1 443 . . . ID=PRO_0000079558;Note=Ubiquitin-binding protein CUE2 +P36075 UniProtKB Domain 8 51 . . . Note=CUE 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00468 +P36075 UniProtKB Domain 55 98 . . . Note=CUE 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00468 +P36075 UniProtKB Domain 347 443 . . . Note=Smr;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00321 +P36075 UniProtKB Helix 9 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OTR +P36075 UniProtKB Beta strand 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OTR +P36075 UniProtKB Helix 25 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OTR +P36075 UniProtKB Turn 35 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OTR +P36075 UniProtKB Helix 40 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OTR +##sequence-region Q06469 1 252 +Q06469 UniProtKB Chain 1 252 . . . ID=PRO_0000257830;Note=Curing of [URE3] protein 1 +##sequence-region P21657 1 970 +P21657 UniProtKB Chain 1 970 . . . ID=PRO_0000114947;Note=Transcriptional activator protein DAL81 +P21657 UniProtKB DNA binding 150 179 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P21657 UniProtKB Compositional bias 24 50 . . . Note=Asn-rich +P21657 UniProtKB Compositional bias 73 88 . . . Note=Poly-Gln +P21657 UniProtKB Compositional bias 127 139 . . . Note=Asn-rich +P21657 UniProtKB Compositional bias 227 237 . . . Note=Poly-Gln +P21657 UniProtKB Modified residue 833 833 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P21657 UniProtKB Sequence conflict 77 82 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21657 UniProtKB Sequence conflict 465 465 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21657 UniProtKB Sequence conflict 497 497 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21657 UniProtKB Sequence conflict 507 507 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21657 UniProtKB Sequence conflict 760 760 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21657 UniProtKB Sequence conflict 785 785 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47179 1 1161 +P47179 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47179 UniProtKB Chain 20 1137 . . . ID=PRO_0000033243;Note=Cell wall protein DAN4 +P47179 UniProtKB Propeptide 1138 1161 . . . ID=PRO_0000033244;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47179 UniProtKB Repeat 373 384 . . . Note=1-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P47179 UniProtKB Repeat 385 396 . . . Note=1-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P47179 UniProtKB Repeat 397 408 . . . Note=1-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P47179 UniProtKB Repeat 409 420 . . . Note=1-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P47179 UniProtKB Repeat 421 432 . . . Note=1-5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P47179 UniProtKB Repeat 433 444 . . . Note=1-6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P47179 UniProtKB Repeat 445 456 . . . Note=1-7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P47179 UniProtKB Repeat 457 468 . . . Note=1-8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P47179 UniProtKB Repeat 469 480 . . . Note=1-9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P47179 UniProtKB Repeat 481 492 . . . Note=1-10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P47179 UniProtKB Repeat 493 504 . . . Note=1-11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P47179 UniProtKB Repeat 505 516 . . . Note=1-12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P47179 UniProtKB Repeat 517 528 . . . Note=1-13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P47179 UniProtKB Repeat 529 540 . . . Note=1-14;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P47179 UniProtKB Repeat 826 913 . . . Note=2-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P47179 UniProtKB Repeat 914 1001 . . . Note=2-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P47179 UniProtKB Repeat 1002 1040 . . . Note=2-3%3B truncated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P47179 UniProtKB Region 134 286 . . . Note=46 X 3 AA tandem repeats of T-[SP]-T +P47179 UniProtKB Region 373 540 . . . Note=14 X 12 AA approximate tandem repeats +P47179 UniProtKB Region 826 1040 . . . Note=2.5 X 88 AA approximate tandem repeats +P47179 UniProtKB Compositional bias 124 794 . . . Note=Ser/Thr-rich +P47179 UniProtKB Lipidation 1137 1137 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P22204 1 572 +P22204 UniProtKB Chain 1 572 . . . ID=PRO_0000085918;Note=Cell cycle protein kinase DBF2 +P22204 UniProtKB Domain 177 477 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P22204 UniProtKB Domain 478 555 . . . Note=AGC-kinase C-terminal +P22204 UniProtKB Nucleotide binding 183 191 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P22204 UniProtKB Active site 300 300 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P22204 UniProtKB Binding site 206 206 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P22204 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P22204 UniProtKB Modified residue 20 20 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P22204 UniProtKB Modified residue 74 74 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P22204 UniProtKB Modified residue 374 374 . . . Note=Phosphoserine%3B by CDC15;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:11404483;Dbxref=PMID:18407956,PMID:11404483 +P22204 UniProtKB Modified residue 544 544 . . . Note=Phosphothreonine%3B by CDC15;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11404483;Dbxref=PMID:11404483 +P22204 UniProtKB Sequence conflict 11 12 . . . Note=LL->YM;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22204 UniProtKB Sequence conflict 114 114 . . . Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22204 UniProtKB Sequence conflict 246 246 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36120 1 742 +P36120 UniProtKB Chain 1 742 . . . ID=PRO_0000055037;Note=ATP-dependent RNA helicase DBP7 +P36120 UniProtKB Domain 178 372 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P36120 UniProtKB Domain 405 605 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P36120 UniProtKB Nucleotide binding 191 198 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P36120 UniProtKB Motif 143 172 . . . Note=Q motif +P36120 UniProtKB Motif 307 310 . . . Note=DEGD box +##sequence-region P24309 1 405 +P24309 UniProtKB Chain 1 405 . . . ID=PRO_0000079797;Note=Lariat debranching enzyme +P24309 UniProtKB Modified residue 269 269 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P32347 1 362 +P32347 UniProtKB Chain 1 362 . . . ID=PRO_0000187577;Note=Uroporphyrinogen decarboxylase +P32347 UniProtKB Region 30 34 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32347 UniProtKB Binding site 48 48 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32347 UniProtKB Binding site 80 80 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32347 UniProtKB Binding site 81 81 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32347 UniProtKB Binding site 160 160 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32347 UniProtKB Binding site 215 215 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32347 UniProtKB Binding site 338 338 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32347 UniProtKB Site 81 81 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32347 UniProtKB Natural variant 59 59 . . . Note=In HEM12-6 and HEM12-12. S->F +P32347 UniProtKB Natural variant 62 62 . . . Note=In HEM12-14. T->I +P32347 UniProtKB Natural variant 107 107 . . . Note=In HEM12-3 and HEM12-13. L->S +P32347 UniProtKB Natural variant 215 215 . . . Note=In HEM12-2 and HEM12-11. S->N +P32347 UniProtKB Mutagenesis 33 33 . . . Note=Inactivation. G->D +P32347 UniProtKB Mutagenesis 300 300 . . . Note=Inactivation. G->D +##sequence-region P36091 1 449 +P36091 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36091 UniProtKB Chain 22 428 . . . ID=PRO_0000012125;Note=Mannan endo-1%2C6-alpha-mannosidase DCW1 +P36091 UniProtKB Propeptide 429 449 . . . ID=PRO_0000012126;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36091 UniProtKB Lipidation 428 428 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36091 UniProtKB Glycosylation 34 34 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36091 UniProtKB Glycosylation 84 84 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36091 UniProtKB Glycosylation 109 109 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36091 UniProtKB Glycosylation 133 133 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36091 UniProtKB Glycosylation 203 203 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36091 UniProtKB Glycosylation 225 225 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36091 UniProtKB Glycosylation 240 240 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36091 UniProtKB Glycosylation 265 265 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36091 UniProtKB Glycosylation 281 281 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36091 UniProtKB Glycosylation 337 337 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36091 UniProtKB Glycosylation 362 362 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36091 UniProtKB Glycosylation 420 420 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36091 UniProtKB Sequence conflict 276 276 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q99321 1 188 +Q99321 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085096;Dbxref=PMID:10085096 +Q99321 UniProtKB Chain 2 188 . . . ID=PRO_0000057067;Note=Diphosphoinositol polyphosphate phosphohydrolase DDP1 +Q99321 UniProtKB Domain 30 179 . . . Note=Nudix hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00794 +Q99321 UniProtKB Motif 65 86 . . . Note=Nudix box +Q99321 UniProtKB Metal binding 80 80 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99321 UniProtKB Metal binding 84 84 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53899 1 274 +P53899 UniProtKB Chain 1 274 . . . ID=PRO_0000203418;Note=CDC48-associated ubiquitin-like/zinc finger protein 1 +P53899 UniProtKB Zinc finger 15 58 . . . Note=AN1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00449 +P53899 UniProtKB Region 170 266 . . . Note=Ubiquitin-like;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:24121501;Dbxref=PMID:24121501 +P53899 UniProtKB Modified residue 273 273 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53899 UniProtKB Beta strand 19 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IJ4 +P53899 UniProtKB Beta strand 24 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IJ4 +P53899 UniProtKB Turn 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IJ4 +P53899 UniProtKB Helix 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IJ4 +P53899 UniProtKB Helix 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IJ4 +P53899 UniProtKB Helix 51 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IJ4 +##sequence-region P08678 1 2026 +P08678 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P08678 UniProtKB Chain 2 2026 . . . ID=PRO_0000195731;Note=Adenylate cyclase +P08678 UniProtKB Domain 676 755 . . . Note=Ras-associating;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00166 +P08678 UniProtKB Repeat 815 838 . . . Note=LRR 1 +P08678 UniProtKB Repeat 842 862 . . . Note=LRR 2 +P08678 UniProtKB Repeat 863 885 . . . Note=LRR 3 +P08678 UniProtKB Repeat 886 908 . . . Note=LRR 4 +P08678 UniProtKB Repeat 910 931 . . . Note=LRR 5 +P08678 UniProtKB Repeat 932 955 . . . Note=LRR 6 +P08678 UniProtKB Repeat 957 976 . . . Note=LRR 7 +P08678 UniProtKB Repeat 977 999 . . . Note=LRR 8 +P08678 UniProtKB Repeat 1001 1016 . . . Note=LRR 9 +P08678 UniProtKB Repeat 1017 1040 . . . Note=LRR 10 +P08678 UniProtKB Repeat 1042 1062 . . . Note=LRR 11 +P08678 UniProtKB Repeat 1063 1086 . . . Note=LRR 12 +P08678 UniProtKB Repeat 1088 1109 . . . Note=LRR 13 +P08678 UniProtKB Repeat 1110 1132 . . . Note=LRR 14 +P08678 UniProtKB Repeat 1134 1156 . . . Note=LRR 15 +P08678 UniProtKB Repeat 1188 1209 . . . Note=LRR 16 +P08678 UniProtKB Repeat 1210 1232 . . . Note=LRR 17 +P08678 UniProtKB Repeat 1233 1256 . . . Note=LRR 18 +P08678 UniProtKB Repeat 1258 1280 . . . Note=LRR 19 +P08678 UniProtKB Repeat 1285 1308 . . . Note=LRR 20 +P08678 UniProtKB Domain 1357 1624 . . . Note=PPM-type phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01082 +P08678 UniProtKB Domain 1668 1805 . . . Note=Guanylate cyclase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00099 +P08678 UniProtKB Metal binding 1673 1673 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08678 UniProtKB Metal binding 1716 1716 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08678 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P08678 UniProtKB Modified residue 376 376 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P08678 UniProtKB Modified residue 389 389 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P08678 UniProtKB Modified residue 433 433 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P08678 UniProtKB Modified residue 487 487 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P08678 UniProtKB Modified residue 497 497 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P08678 UniProtKB Modified residue 562 562 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P08678 UniProtKB Mutagenesis 1651 1651 . . . Note=Attenuation of the response to Ras proteins. T->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1991451;Dbxref=PMID:1991451 +P08678 UniProtKB Mutagenesis 1651 1651 . . . Note=Weak Ras-independent activity. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1991451;Dbxref=PMID:1991451 +P08678 UniProtKB Sequence conflict 262 262 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08678 UniProtKB Sequence conflict 548 548 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08678 UniProtKB Sequence conflict 592 592 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08678 UniProtKB Sequence conflict 709 709 . . . Note=R->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08678 UniProtKB Sequence conflict 962 962 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08678 UniProtKB Sequence conflict 1388 1388 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08678 UniProtKB Sequence conflict 1427 1427 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08678 UniProtKB Sequence conflict 1461 1461 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08678 UniProtKB Sequence conflict 1566 1566 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08678 UniProtKB Sequence conflict 1735 1735 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08678 UniProtKB Sequence conflict 1956 1956 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08678 UniProtKB Sequence conflict 1996 1996 . . . Note=C->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08678 UniProtKB Sequence conflict 2009 2026 . . . Note=NVVDELLQMVKNAKDLST->MLLTNFYKWLRTQRIYQLEFCS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P00163 1 385 +P00163 UniProtKB Chain 1 385 . . . ID=PRO_0000061769;Note=Cytochrome b +P00163 UniProtKB Transmembrane 32 52 . . . Note=Helical;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631 +P00163 UniProtKB Transmembrane 76 98 . . . Note=Helical;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631 +P00163 UniProtKB Transmembrane 113 133 . . . Note=Helical;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631 +P00163 UniProtKB Transmembrane 179 199 . . . Note=Helical;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631 +P00163 UniProtKB Transmembrane 225 245 . . . Note=Helical;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631 +P00163 UniProtKB Transmembrane 289 309 . . . Note=Helical;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631 +P00163 UniProtKB Transmembrane 321 341 . . . Note=Helical;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631 +P00163 UniProtKB Transmembrane 348 368 . . . Note=Helical;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631 +P00163 UniProtKB Metal binding 82 82 . . . Note=Iron 1 (heme b562 axial ligand);Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000244|PDB:1KB9,ECO:0000244|PDB:1KYO,ECO:0000244|PDB:1P84,ECO:0000244|PDB:2IBZ,ECO:0000244|PDB:3CX5,ECO:0000244|PDB:3CXH,ECO:0000244|PDB:4PD4,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631 +P00163 UniProtKB Metal binding 96 96 . . . Note=Iron 2 (heme b566 axial ligand);Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000244|PDB:1KB9,ECO:0000244|PDB:1KYO,ECO:0000244|PDB:1P84,ECO:0000244|PDB:2IBZ,ECO:0000244|PDB:3CX5,ECO:0000244|PDB:3CXH,ECO:0000244|PDB:4PD4,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631 +P00163 UniProtKB Metal binding 183 183 . . . Note=Iron 1 (heme b562 axial ligand);Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000244|PDB:1KB9,ECO:0000244|PDB:1KYO,ECO:0000244|PDB:1P84,ECO:0000244|PDB:2IBZ,ECO:0000244|PDB:3CX5,ECO:0000244|PDB:3CXH,ECO:0000244|PDB:4PD4,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631 +P00163 UniProtKB Metal binding 197 197 . . . Note=Iron 2 (heme b566 axial ligand);Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1EZV,ECO:0000244|PDB:1KB9,ECO:0000244|PDB:1KYO,ECO:0000244|PDB:1P84,ECO:0000244|PDB:2IBZ,ECO:0000244|PDB:3CX5,ECO:0000244|PDB:3CXH,ECO:0000244|PDB:4PD4,ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11880631;Dbxref=PMID:10873857,PMID:11880631 +P00163 UniProtKB Binding site 202 202 . . . Note=Ubiquinone;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00157 +P00163 UniProtKB Natural variant 131 131 . . . Note=In mutant W7 which is respiratory deficient. G->S +P00163 UniProtKB Sequence conflict 122 122 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00163 UniProtKB Sequence conflict 122 122 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00163 UniProtKB Sequence conflict 269 269 . . . Note=I->ID;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00163 UniProtKB Sequence conflict 269 269 . . . Note=I->ID;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00163 UniProtKB Helix 3 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 10 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Beta strand 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 28 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 32 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Turn 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 61 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 75 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Turn 103 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Turn 108 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYO +P00163 UniProtKB Helix 111 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 138 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 150 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Turn 155 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 158 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Beta strand 168 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 173 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Beta strand 217 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Turn 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 224 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Turn 248 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 254 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 273 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 276 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Beta strand 285 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 288 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 301 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 305 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Beta strand 312 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 320 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 348 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00163 UniProtKB Helix 366 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +##sequence-region P53206 1 393 +P53206 UniProtKB Chain 1 393 . . . ID=PRO_0000167130;Note=Putative cysteine synthase +P53206 UniProtKB Transmembrane 12 31 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53206 UniProtKB Region 230 234 . . . Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16703 +P53206 UniProtKB Binding site 338 338 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16703 +P53206 UniProtKB Modified residue 86 86 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16703 +##sequence-region Q00873 1 224 +Q00873 UniProtKB Chain 1 224 . . . ID=PRO_0000121719;Note=Cytochrome c1 heme lyase +##sequence-region P43550 1 591 +P43550 UniProtKB Chain 1 591 . . . ID=PRO_0000121523;Note=Dihydroxyacetone kinase 2 +P43550 UniProtKB Domain 8 344 . . . Note=DhaK;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00814 +P43550 UniProtKB Domain 384 587 . . . Note=DhaL;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00813 +P43550 UniProtKB Nucleotide binding 413 416 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43550 UniProtKB Nucleotide binding 459 460 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43550 UniProtKB Nucleotide binding 511 512 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43550 UniProtKB Nucleotide binding 572 574 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43550 UniProtKB Region 58 61 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43550 UniProtKB Active site 223 223 . . . Note=Tele-hemiaminal-histidine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00814 +P43550 UniProtKB Binding site 109 109 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43550 UniProtKB Binding site 114 114 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P47178 1 298 +P47178 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10322008;Dbxref=PMID:10322008 +P47178 UniProtKB Chain 20 275 . . . ID=PRO_0000033239;Note=Cell wall protein DAN1 +P47178 UniProtKB Propeptide 276 298 . . . ID=PRO_0000033240;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47178 UniProtKB Lipidation 275 275 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47178 UniProtKB Sequence conflict 115 115 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P18962 1 818 +P18962 UniProtKB Chain 1 818 . . . ID=PRO_0000122421;Note=Dipeptidyl aminopeptidase B +P18962 UniProtKB Topological domain 1 29 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18962 UniProtKB Transmembrane 30 45 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18962 UniProtKB Topological domain 46 818 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18962 UniProtKB Active site 679 679 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10084 +P18962 UniProtKB Active site 756 756 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10084 +P18962 UniProtKB Active site 789 789 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10084 +P18962 UniProtKB Glycosylation 63 63 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18962 UniProtKB Glycosylation 79 79 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18962 UniProtKB Glycosylation 110 110 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18962 UniProtKB Glycosylation 139 139 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18962 UniProtKB Glycosylation 372 372 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18962 UniProtKB Glycosylation 392 392 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18962 UniProtKB Glycosylation 421 421 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18962 UniProtKB Glycosylation 738 738 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18962 UniProtKB Sequence conflict 83 83 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18962 UniProtKB Sequence conflict 125 125 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18962 UniProtKB Sequence conflict 182 188 . . . Note=FEEIGNE->LRRLET;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18962 UniProtKB Sequence conflict 200 200 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18962 UniProtKB Sequence conflict 318 318 . . . Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18962 UniProtKB Sequence conflict 366 375 . . . Note=TSNVVRNESS->DFKRGKERKF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18962 UniProtKB Sequence conflict 808 818 . . . Note=AKRAFDGQFVK->QSVLSMGNLTNELTIYSSSHRDIHKTFSYLHTMYI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18962 UniProtKB Helix 34 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KL4 +P18962 UniProtKB Turn 38 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KL4 +P18962 UniProtKB Helix 42 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KL4 +##sequence-region P47005 1 663 +P47005 UniProtKB Chain 1 663 . . . ID=PRO_0000119971;Note=F-box protein DAS1 +P47005 UniProtKB Domain 46 91 . . . Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080 +P47005 UniProtKB Compositional bias 533 539 . . . Note=Poly-Asp +P47005 UniProtKB Compositional bias 647 652 . . . Note=Poly-Asn +##sequence-region Q12084 1 232 +Q12084 UniProtKB Chain 1 232 . . . ID=PRO_0000242489;Note=Putative uridine kinase DAS2 +Q12084 UniProtKB Nucleotide binding 17 24 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12517 1 231 +Q12517 UniProtKB Chain 1 231 . . . ID=PRO_0000232998;Note=mRNA-decapping enzyme subunit 1 +Q12517 UniProtKB Mutagenesis 16 20 . . . Note=In DCP1-17%3B partial loss of mRNA-decapping activity. EFYRK->AFYAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10101156;Dbxref=PMID:10101156 +Q12517 UniProtKB Mutagenesis 29 31 . . . Note=In DCP1-2%3B strong loss of mRNA decapping activity at 36 degrees Celsius. RYD->AYA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10101156,ECO:0000269|PubMed:14758354;Dbxref=PMID:10101156,PMID:14758354 +Q12517 UniProtKB Mutagenesis 32 34 . . . Note=Partial loss of mRNA-decapping activity. PKI->AKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14758354;Dbxref=PMID:14758354 +Q12517 UniProtKB Mutagenesis 37 38 . . . Note=Strong loss of mRNA-decapping activity%3B when associated with A-217 and A-221. LL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14758354;Dbxref=PMID:14758354 +Q12517 UniProtKB Mutagenesis 47 47 . . . Note=In DCP1-32%3B partial loss of mRNA decapping activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10101156;Dbxref=PMID:10101156 +Q12517 UniProtKB Mutagenesis 47 47 . . . Note=In DCP1-35%3B partial loss of mRNA decapping activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10101156;Dbxref=PMID:10101156 +Q12517 UniProtKB Mutagenesis 48 50 . . . Note=In DCP1-4%3B partial loss of mRNA decapping activity. In DCP1-43%3B strong loss of mRNA-decapping activity%3B when associated with A-187 and A-188. In DCP1-44%3B strong loss of mRNA-decapping activity%3B when associated with A-216 and A-219. KWD->AWA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10101156;Dbxref=PMID:10101156 +Q12517 UniProtKB Mutagenesis 56 56 . . . Note=In DCP1-31%3B partial loss of mRNA decapping activity. W->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10101156,ECO:0000269|PubMed:14758354,ECO:0000269|PubMed:8757137;Dbxref=PMID:10101156,PMID:14758354,PMID:8757137 +Q12517 UniProtKB Mutagenesis 70 70 . . . Note=In DCP1-33%3B strong loss of mRNA decapping activity. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10101156,ECO:0000269|PubMed:14758354;Dbxref=PMID:10101156,PMID:14758354 +Q12517 UniProtKB Mutagenesis 156 156 . . . Note=In DCP1-1%3B strong loss of mRNA decapping activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10101156;Dbxref=PMID:10101156 +Q12517 UniProtKB Mutagenesis 187 188 . . . Note=In DCP1-19%3B partial loss of mRNA decapping activity. In DCP1-43%3B strong loss of mRNA-decapping activity%3B when associated with A-48 and A-50. KD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10101156;Dbxref=PMID:10101156 +Q12517 UniProtKB Mutagenesis 204 204 . . . Note=In DCP1-33%3B partial loss of mRNA decapping activity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10101156;Dbxref=PMID:10101156 +Q12517 UniProtKB Mutagenesis 216 219 . . . Note=In DCP1-25%3B partial loss of mRNA-decapping activity. In DCP1-44%3B strong loss of mRNA-decapping activity%3B when associated with A-48 and A-50. ELIK->ALIA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10101156;Dbxref=PMID:10101156 +Q12517 UniProtKB Mutagenesis 217 217 . . . Note=Strong loss of mRNA-decapping activity%3B when associated with A-37%3B A-38 and A-221. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14758354;Dbxref=PMID:14758354 +Q12517 UniProtKB Mutagenesis 221 221 . . . Note=Strong loss of mRNA-decapping activity%3B when associated with A-37%3B A-38 and A-217. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14758354;Dbxref=PMID:14758354 +Q12517 UniProtKB Helix 24 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67 +Q12517 UniProtKB Beta strand 34 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67 +Q12517 UniProtKB Turn 51 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67 +Q12517 UniProtKB Beta strand 55 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67 +Q12517 UniProtKB Beta strand 139 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67 +Q12517 UniProtKB Beta strand 152 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67 +Q12517 UniProtKB Helix 160 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67 +Q12517 UniProtKB Helix 171 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67 +Q12517 UniProtKB Beta strand 183 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67 +Q12517 UniProtKB Beta strand 190 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67 +Q12517 UniProtKB Beta strand 200 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67 +Q12517 UniProtKB Helix 208 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q67 +##sequence-region Q12123 1 353 +Q12123 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15240832;Dbxref=PMID:15240832 +Q12123 UniProtKB Chain 2 353 . . . ID=PRO_0000109799;Note=Inactive diphosphatase DCS2 +Q12123 UniProtKB Motif 265 269 . . . Note=Histidine triad motif;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12123 UniProtKB Modified residue 341 341 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P06773 1 312 +P06773 UniProtKB Chain 1 312 . . . ID=PRO_0000171697;Note=Deoxycytidylate deaminase +P06773 UniProtKB Domain 162 291 . . . Note=CMP/dCMP-type deaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01083 +P06773 UniProtKB Active site 235 235 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06773 UniProtKB Metal binding 233 233 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06773 UniProtKB Metal binding 260 260 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06773 UniProtKB Metal binding 263 263 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06773 UniProtKB Sequence conflict 78 78 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38877 1 133 +P38877 UniProtKB Chain 1 133 . . . ID=PRO_0000079494;Note=Chromosome transmission fidelity protein 8 +P38877 UniProtKB Beta strand 3 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P38877 UniProtKB Helix 9 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P38877 UniProtKB Beta strand 22 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P38877 UniProtKB Beta strand 29 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P38877 UniProtKB Helix 45 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P38877 UniProtKB Turn 54 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P38877 UniProtKB Beta strand 59 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P38877 UniProtKB Beta strand 65 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P38877 UniProtKB Turn 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P38877 UniProtKB Beta strand 88 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P38877 UniProtKB Turn 108 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P38877 UniProtKB Beta strand 112 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +##sequence-region P46963 1 296 +P46963 UniProtKB Chain 1 296 . . . ID=PRO_0000079495;Note=CTD kinase subunit gamma +P46963 UniProtKB Modified residue 35 35 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46963 UniProtKB Mutagenesis 274 296 . . . Note=No interaction with CTK2. Still interacts with CTK1. Missing +P46963 UniProtKB Sequence conflict 101 101 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46963 UniProtKB Sequence conflict 112 112 . . . Note=M->MLM;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46963 UniProtKB Sequence conflict 163 163 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46963 UniProtKB Sequence conflict 174 174 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46963 UniProtKB Sequence conflict 295 295 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06686 1 241 +Q06686 UniProtKB Chain 1 241 . . . ID=PRO_0000195047;Note=Copper transport protein CTR3 +Q06686 UniProtKB Topological domain 1 41 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06686 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06686 UniProtKB Topological domain 63 159 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06686 UniProtKB Transmembrane 160 180 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06686 UniProtKB Topological domain 181 182 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06686 UniProtKB Transmembrane 183 203 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06686 UniProtKB Topological domain 204 241 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53088 1 359 +P53088 UniProtKB Chain 1 359 . . . ID=PRO_0000219889;Note=Cytoplasmic tRNA 2-thiolation protein 1 +P53088 UniProtKB Sequence conflict 356 359 . . . Note=KLSF->NSA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53137 1 624 +P53137 UniProtKB Chain 1 624 . . . ID=PRO_0000202749;Note=CUE domain-containing protein 3 +P53137 UniProtKB Domain 316 359 . . . Note=CUE;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00468 +P53137 UniProtKB Modified residue 377 377 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P15315 1 225 +P15315 UniProtKB Chain 1 225 . . . ID=PRO_0000194926;Note=Transcriptional activator protein CUP2 +P15315 UniProtKB DNA binding 1 40 . . . Note=Copper-fist;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055 +P15315 UniProtKB Region 1 108 . . . Note=Binds copper and DNA +P15315 UniProtKB Region 109 225 . . . Note=Required for transcriptional activation +P15315 UniProtKB Metal binding 11 11 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055 +P15315 UniProtKB Metal binding 14 14 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055 +P15315 UniProtKB Metal binding 23 23 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055 +P15315 UniProtKB Metal binding 25 25 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055 +##sequence-region Q03772 1 175 +Q03772 UniProtKB Chain 1 175 . . . ID=PRO_0000218244;Note=Pre-mRNA-splicing factor CWC15 +Q03772 UniProtKB Coiled coil 85 110 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03772 UniProtKB Helix 15 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q03772 UniProtKB Helix 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q03772 UniProtKB Beta strand 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q03772 UniProtKB Helix 164 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P46947 1 266 +P46947 UniProtKB Chain 1 266 . . . ID=PRO_0000079610;Note=Pre-mRNA-splicing factor CWC26 +P46947 UniProtKB Compositional bias 15 25 . . . Note=Poly-Lys +P46947 UniProtKB Helix 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MY2 +P46947 UniProtKB Helix 243 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MY2 +P46947 UniProtKB Beta strand 252 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UQT +##sequence-region Q02770 1 301 +Q02770 UniProtKB Chain 1 301 . . . ID=PRO_0000064189;Note=Peptidyl-prolyl isomerase CWC27 +Q02770 UniProtKB Domain 9 159 . . . Note=PPIase cyclophilin-type +##sequence-region P07143 1 309 +P07143 UniProtKB Transit peptide 1 61 . . . Note=Mitochondrion +P07143 UniProtKB Chain 62 309 . . . ID=PRO_0000006566;Note=Cytochrome c1%2C heme protein%2C mitochondrial +P07143 UniProtKB Transmembrane 273 287 . . . Note=Helical%3B Note%3DAnchors to the membrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07143 UniProtKB Domain 88 241 . . . Note=Cytochrome c;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00433 +P07143 UniProtKB Metal binding 105 105 . . . Note=Iron (heme axial ligand) +P07143 UniProtKB Metal binding 225 225 . . . Note=Iron (heme axial ligand) +P07143 UniProtKB Binding site 101 101 . . . Note=Heme (covalent) +P07143 UniProtKB Binding site 104 104 . . . Note=Heme (covalent) +P07143 UniProtKB Mutagenesis 272 272 . . . Note=Loss of RIP1 from the bc1 complex. K->A +P07143 UniProtKB Mutagenesis 288 288 . . . Note=Loss of CYT1 and COB from the bc1 complex%3B when associated with L-289 and L-296. K->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11880631;Dbxref=PMID:11880631 +P07143 UniProtKB Mutagenesis 289 289 . . . Note=Loss of CYT1 and COB from the bc1 complex%3B when associated with L-288 and L-296. K->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11880631;Dbxref=PMID:11880631 +P07143 UniProtKB Mutagenesis 296 296 . . . Note=Loss of CYT1 and COB from the bc1 complex%3B when associated with L-288 and L-289. K->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11880631;Dbxref=PMID:11880631 +P07143 UniProtKB Helix 64 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07143 UniProtKB Helix 87 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07143 UniProtKB Helix 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07143 UniProtKB Helix 112 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07143 UniProtKB Turn 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07143 UniProtKB Helix 122 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07143 UniProtKB Beta strand 132 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07143 UniProtKB Beta strand 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PD4 +P07143 UniProtKB Beta strand 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07143 UniProtKB Beta strand 158 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PD4 +P07143 UniProtKB Helix 162 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07143 UniProtKB Turn 168 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07143 UniProtKB Turn 180 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07143 UniProtKB Beta strand 183 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PD4 +P07143 UniProtKB Helix 187 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07143 UniProtKB Beta strand 216 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P84 +P07143 UniProtKB Beta strand 221 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07143 UniProtKB Helix 244 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07143 UniProtKB Helix 263 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07143 UniProtKB Beta strand 299 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +##sequence-region P38909 1 366 +P38909 UniProtKB Transit peptide 1 50 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38909 UniProtKB Chain 51 366 . . . ID=PRO_0000079749;Note=Cytochrome c mitochondrial import factor CYC2 +P38909 UniProtKB Domain 63 184 . . . Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716 +##sequence-region P15365 1 543 +P15365 UniProtKB Chain 1 543 . . . ID=PRO_0000121366;Note=Allantoate permease +P15365 UniProtKB Topological domain 1 80 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Transmembrane 81 97 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Topological domain 98 123 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Transmembrane 124 145 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Topological domain 146 154 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Transmembrane 155 171 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Topological domain 172 178 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Transmembrane 179 200 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Topological domain 201 213 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Transmembrane 214 237 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Topological domain 238 248 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Transmembrane 249 269 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Topological domain 270 317 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Transmembrane 318 342 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Topological domain 343 352 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Transmembrane 353 377 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Topological domain 378 389 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Transmembrane 390 411 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Topological domain 412 417 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Transmembrane 418 435 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Topological domain 436 453 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Transmembrane 454 472 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Topological domain 473 482 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Transmembrane 483 504 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15365 UniProtKB Topological domain 505 543 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P26343 1 269 +P26343 UniProtKB Chain 1 269 . . . ID=PRO_0000083470;Note=Nitrogen regulatory protein DAL80 +P26343 UniProtKB Zinc finger 31 55 . . . Note=GATA-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00094 +P26343 UniProtKB Compositional bias 79 100 . . . Note=Asn-rich +P26343 UniProtKB Compositional bias 101 108 . . . Note=Arg/Lys-rich (basic) +P26343 UniProtKB Sequence conflict 6 6 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P26343 UniProtKB Sequence conflict 207 207 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12091 1 152 +Q12091 UniProtKB Chain 1 152 . . . ID=PRO_0000121747;Note=Damage response protein 1 +Q12091 UniProtKB Domain 46 145 . . . Note=Cytochrome b5 heme-binding +##sequence-region P24784 1 617 +P24784 UniProtKB Chain 1 617 . . . ID=PRO_0000055016;Note=ATP-dependent RNA helicase DBP1 +P24784 UniProtKB Domain 185 374 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P24784 UniProtKB Domain 385 545 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P24784 UniProtKB Nucleotide binding 198 205 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P24784 UniProtKB Motif 154 182 . . . Note=Q motif +P24784 UniProtKB Motif 318 321 . . . Note=DEAD box +P24784 UniProtKB Sequence conflict 43 44 . . . Note=ST->RS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24784 UniProtKB Sequence conflict 48 48 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24784 UniProtKB Sequence conflict 88 88 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24784 UniProtKB Sequence conflict 115 115 . . . Note=E->QK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24784 UniProtKB Sequence conflict 496 496 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06218 1 594 +Q06218 UniProtKB Chain 1 594 . . . ID=PRO_0000055039;Note=ATP-dependent RNA helicase DBP9 +Q06218 UniProtKB Domain 49 233 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q06218 UniProtKB Domain 246 476 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q06218 UniProtKB Nucleotide binding 62 69 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q06218 UniProtKB Motif 17 45 . . . Note=Q motif +Q06218 UniProtKB Motif 179 182 . . . Note=DEAD box +Q06218 UniProtKB Mutagenesis 413 413 . . . Note=Impairs helicase activity in vitro. R->A%2CK%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15028736;Dbxref=PMID:15028736 +Q06218 UniProtKB Sequence conflict 24 24 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04895 1 635 +Q04895 UniProtKB Chain 1 635 . . . ID=PRO_0000197919;Note=Allantoin permease +Q04895 UniProtKB Topological domain 1 144 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Transmembrane 145 165 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Topological domain 166 174 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Transmembrane 175 195 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Topological domain 196 198 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Transmembrane 199 219 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Topological domain 220 243 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Transmembrane 244 264 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Topological domain 265 269 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Transmembrane 270 290 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Topological domain 291 311 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Transmembrane 312 332 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Topological domain 333 351 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Transmembrane 352 372 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Topological domain 373 401 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Transmembrane 402 422 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Topological domain 423 443 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Transmembrane 444 464 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Topological domain 465 466 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Transmembrane 467 487 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Topological domain 488 522 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Transmembrane 523 543 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Topological domain 544 560 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Transmembrane 561 581 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04895 UniProtKB Topological domain 582 635 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12389 1 995 +Q12389 UniProtKB Chain 1 995 . . . ID=PRO_0000055040;Note=ATP-dependent RNA helicase DBP10 +Q12389 UniProtKB Domain 168 340 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q12389 UniProtKB Domain 418 568 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q12389 UniProtKB Nucleotide binding 181 188 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q12389 UniProtKB Motif 137 165 . . . Note=Q motif +Q12389 UniProtKB Motif 288 291 . . . Note=DEAD box +Q12389 UniProtKB Modified residue 101 101 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12389 UniProtKB Modified residue 398 398 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12389 UniProtKB Modified residue 400 400 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12389 UniProtKB Sequence conflict 733 741 . . . Note=SHSIEDEIL->HILSKMKFW;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12389 UniProtKB Sequence conflict 733 741 . . . Note=SHSIEDEIL->HILSKMKFW;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12389 UniProtKB Sequence conflict 746 746 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12389 UniProtKB Sequence conflict 746 746 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12389 UniProtKB Sequence conflict 764 764 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12389 UniProtKB Sequence conflict 764 764 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P24783 1 546 +P24783 UniProtKB Chain 1 546 . . . ID=PRO_0000055000;Note=ATP-dependent RNA helicase DBP2 +P24783 UniProtKB Domain 144 319 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P24783 UniProtKB Domain 347 494 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P24783 UniProtKB Nucleotide binding 157 164 . . . Note=ATP +P24783 UniProtKB Region 505 530 . . . Note=RNA-binding RGG-box +P24783 UniProtKB Motif 113 141 . . . Note=Q motif +P24783 UniProtKB Motif 267 270 . . . Note=DEAD box +P24783 UniProtKB Modified residue 88 88 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P24783 UniProtKB Modified residue 90 90 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P24783 UniProtKB Cross-link 474 474 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P24783 UniProtKB Mutagenesis 163 163 . . . Note=Decreases nonsense-mediated mRNA decay. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11585918;Dbxref=PMID:11585918 +P24783 UniProtKB Mutagenesis 268 268 . . . Note=Decreases nonsense-mediated mRNA decay. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11585918;Dbxref=PMID:11585918 +P24783 UniProtKB Mutagenesis 300 300 . . . Note=Decreases nonsense-mediated mRNA decay. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11585918;Dbxref=PMID:11585918 +P24783 UniProtKB Mutagenesis 447 447 . . . Note=Decreases nonsense-mediated mRNA decay. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11585918;Dbxref=PMID:11585918 +P24783 UniProtKB Sequence conflict 425 425 . . . Note=D->GN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P20447 1 523 +P20447 UniProtKB Chain 1 523 . . . ID=PRO_0000055017;Note=ATP-dependent RNA helicase DBP3 +P20447 UniProtKB Domain 143 315 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P20447 UniProtKB Domain 344 493 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P20447 UniProtKB Nucleotide binding 156 163 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P20447 UniProtKB Motif 114 140 . . . Note=Q motif +P20447 UniProtKB Motif 262 265 . . . Note=DEAD box +P20447 UniProtKB Sequence conflict 441 441 . . . Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20447 UniProtKB Sequence conflict 444 444 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P20449 1 482 +P20449 UniProtKB Chain 1 482 . . . ID=PRO_0000055019;Note=ATP-dependent RNA helicase DBP5 +P20449 UniProtKB Domain 125 292 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P20449 UniProtKB Domain 303 480 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P20449 UniProtKB Nucleotide binding 138 145 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P20449 UniProtKB Motif 92 120 . . . Note=Q motif +P20449 UniProtKB Motif 239 242 . . . Note=DEAD box +P20449 UniProtKB Modified residue 86 86 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P20449 UniProtKB Modified residue 93 93 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P20449 UniProtKB Modified residue 162 162 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P20449 UniProtKB Mutagenesis 170 170 . . . Note=In RAT8-7%3B accumulates poly(A)+ RNA in the nucleus at 16 degrees Celsius. P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9564048;Dbxref=PMID:9564048 +P20449 UniProtKB Mutagenesis 171 171 . . . Note=In DBP5-2%3B accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius%3B when associated with L-236 and F-245. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9564047;Dbxref=PMID:9564047 +P20449 UniProtKB Mutagenesis 220 220 . . . Note=In DBP5-1%3B accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius%3B when associated with S-466. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9564047;Dbxref=PMID:9564047 +P20449 UniProtKB Mutagenesis 236 236 . . . Note=In DBP5-2%3B accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius%3B when associated with P-171 and F-245. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9564047;Dbxref=PMID:9564047 +P20449 UniProtKB Mutagenesis 267 267 . . . Note=In RAT8-2%3B accumulates poly(A)+ RNA in the nucleus at 16 and 37 degrees Celsius. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9564048;Dbxref=PMID:9564048 +P20449 UniProtKB Mutagenesis 345 345 . . . Note=In DBP5-2%3B accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius%3B when associated with P-171 and L-236. V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9564047;Dbxref=PMID:9564047 +P20449 UniProtKB Mutagenesis 385 385 . . . Note=In RAT8-3%3B accumulates poly(A)+ RNA in the nucleus at 16 and 37 degrees Celsius. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9564048;Dbxref=PMID:9564048 +P20449 UniProtKB Mutagenesis 466 466 . . . Note=In DBP5-1%3B accumulates poly(A)+ RNA in the nucleus at 37 degrees Celsius%3B when associated with P-220. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9564047;Dbxref=PMID:9564047 +P20449 UniProtKB Beta strand 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KBE +P20449 UniProtKB Helix 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KBE +P20449 UniProtKB Helix 87 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KBE +P20449 UniProtKB Helix 94 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KBE +P20449 UniProtKB Helix 101 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Beta strand 110 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KBE +P20449 UniProtKB Helix 117 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Beta strand 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RRM +P20449 UniProtKB Beta strand 134 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Helix 144 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Beta strand 165 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Helix 172 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Turn 186 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Beta strand 193 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Beta strand 210 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Helix 216 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Beta strand 235 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Helix 241 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Helix 250 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Turn 261 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KBE +P20449 UniProtKB Beta strand 266 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Helix 276 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Beta strand 290 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Helix 296 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Turn 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GFP +P20449 UniProtKB Beta strand 304 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Helix 314 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Turn 326 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Beta strand 330 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Helix 340 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Beta strand 358 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Beta strand 362 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RRM +P20449 UniProtKB Helix 366 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Turn 378 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KBF +P20449 UniProtKB Beta strand 383 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Helix 388 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Beta strand 391 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Beta strand 399 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Beta strand 413 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Helix 417 424 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Helix 425 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +P20449 UniProtKB Beta strand 434 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Helix 443 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +P20449 UniProtKB Turn 456 458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEU +P20449 UniProtKB Beta strand 462 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GFP +P20449 UniProtKB Helix 469 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEY +##sequence-region P53734 1 629 +P53734 UniProtKB Chain 1 629 . . . ID=PRO_0000055036;Note=ATP-dependent RNA helicase DBP6 +P53734 UniProtKB Domain 221 401 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P53734 UniProtKB Domain 437 603 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P53734 UniProtKB Nucleotide binding 234 241 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P53734 UniProtKB Motif 197 205 . . . Note=Q motif +P53734 UniProtKB Motif 341 344 . . . Note=DEAD box +P53734 UniProtKB Modified residue 73 73 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53734 UniProtKB Modified residue 77 77 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53734 UniProtKB Modified residue 78 78 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P21182 1 396 +P21182 UniProtKB Chain 1 87 . . . ID=PRO_0000030033;Note=S-adenosylmethionine decarboxylase beta chain +P21182 UniProtKB Chain 88 396 . . . ID=PRO_0000030034;Note=S-adenosylmethionine decarboxylase alpha chain +P21182 UniProtKB Active site 29 29 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21182 UniProtKB Active site 32 32 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21182 UniProtKB Active site 88 88 . . . Note=Schiff-base intermediate with substrate%3B via pyruvic acid;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21182 UniProtKB Active site 102 102 . . . Note=Proton donor%3B for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21182 UniProtKB Active site 287 287 . . . Note=Proton acceptor%3B for processing activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21182 UniProtKB Active site 301 301 . . . Note=Proton acceptor%3B for processing activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21182 UniProtKB Site 87 88 . . . Note=Cleavage (non-hydrolytic)%3B by autolysis +P21182 UniProtKB Modified residue 88 88 . . . Note=Pyruvic acid (Ser)%3B by autocatalysis +##sequence-region P25559 1 380 +P25559 UniProtKB Chain 1 380 . . . ID=PRO_0000079802;Note=Sister chromatid cohesion protein DCC1 +P25559 UniProtKB Beta strand 3 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P25559 UniProtKB Beta strand 15 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P25559 UniProtKB Helix 22 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P25559 UniProtKB Beta strand 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P25559 UniProtKB Beta strand 44 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P25559 UniProtKB Beta strand 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P25559 UniProtKB Beta strand 57 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P25559 UniProtKB Beta strand 96 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P25559 UniProtKB Beta strand 105 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P25559 UniProtKB Helix 131 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Helix 147 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Beta strand 154 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Helix 158 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Beta strand 170 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Beta strand 176 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Helix 182 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Helix 208 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Helix 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P25559 UniProtKB Helix 228 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Beta strand 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Beta strand 250 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Helix 254 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Beta strand 270 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Helix 277 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Helix 298 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Beta strand 304 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Beta strand 312 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Helix 318 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Helix 325 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Beta strand 337 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Helix 341 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Helix 349 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Helix 358 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Beta strand 366 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +P25559 UniProtKB Beta strand 375 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSN +##sequence-region P08432 1 466 +P08432 UniProtKB Chain 1 466 . . . ID=PRO_0000149909;Note=Ornithine decarboxylase +P08432 UniProtKB Region 318 321 . . . Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11926 +P08432 UniProtKB Region 362 363 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07805 +P08432 UniProtKB Active site 411 411 . . . Note=Proton donor%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11926 +P08432 UniProtKB Binding site 247 247 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11926 +P08432 UniProtKB Binding site 286 286 . . . Note=Pyridoxal phosphate%3B via amino nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11926 +P08432 UniProtKB Binding site 412 412 . . . Note=Substrate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07805 +P08432 UniProtKB Binding site 441 441 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11926 +P08432 UniProtKB Site 244 244 . . . Note=Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00860 +P08432 UniProtKB Modified residue 116 116 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11926 +##sequence-region Q05924 1 578 +Q05924 UniProtKB Chain 1 578 . . . ID=PRO_0000079819;Note=Phosphatase DCR2 +Q05924 UniProtKB Nucleotide binding 116 123 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05924 UniProtKB Compositional bias 520 527 . . . Note=Poly-Gly +Q05924 UniProtKB Mutagenesis 338 338 . . . Note=20%25 phosphatase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15590836;Dbxref=PMID:15590836 +##sequence-region P06634 1 604 +P06634 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P06634 UniProtKB Chain 2 604 . . . ID=PRO_0000055043;Note=ATP-dependent RNA helicase DED1 +P06634 UniProtKB Domain 173 362 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P06634 UniProtKB Domain 373 533 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P06634 UniProtKB Nucleotide binding 186 193 . . . Note=ATP +P06634 UniProtKB Motif 142 170 . . . Note=Q motif +P06634 UniProtKB Motif 306 309 . . . Note=DEAD box +P06634 UniProtKB Compositional bias 10 75 . . . Note=Asn-rich +P06634 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P06634 UniProtKB Modified residue 62 62 . . . Note=Dimethylated arginine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23865587;Dbxref=PMID:23865587 +P06634 UniProtKB Modified residue 215 215 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06634 UniProtKB Modified residue 218 218 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06634 UniProtKB Modified residue 263 263 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P06634 UniProtKB Modified residue 535 535 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P06634 UniProtKB Modified residue 539 539 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P06634 UniProtKB Modified residue 543 543 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P06634 UniProtKB Modified residue 572 572 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P06634 UniProtKB Modified residue 576 576 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P06634 UniProtKB Modified residue 598 598 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06634 UniProtKB Cross-link 158 158 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P06634 UniProtKB Mutagenesis 108 108 . . . Note=In DED1-120%3B impairs protein synthesis at 15 degrees Celsius%3B when associated with D-494. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9045610;Dbxref=PMID:9045610 +P06634 UniProtKB Mutagenesis 144 144 . . . Note=Slow growth at 18 and 30 degrees Celsius and no growth at 16 degrees Celsius. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868 +P06634 UniProtKB Mutagenesis 144 144 . . . Note=Lethal. F->D%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868 +P06634 UniProtKB Mutagenesis 162 162 . . . Note=Lethal in vivo and inhibits ATPase and helicase activities in vitro. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868 +P06634 UniProtKB Mutagenesis 162 162 . . . Note=Slow growth at 18 degrees Celsius. F->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868 +P06634 UniProtKB Mutagenesis 162 162 . . . Note=Reduces RNA-helicase activity about 5-fold in vitro. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868 +P06634 UniProtKB Mutagenesis 166 166 . . . Note=Reduces RNA-helicase activity about 2.5-fold in vitro. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868 +P06634 UniProtKB Mutagenesis 166 166 . . . Note=Slow growth at 18 and 36 degrees Celsius in vivo%2C and reduces RNA-helicase activity about 5-fold in vitro. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868 +P06634 UniProtKB Mutagenesis 169 169 . . . Note=Lethal in vivo and impairs ATPase and RNA-helicase activities in vitro. Q->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868 +P06634 UniProtKB Mutagenesis 169 169 . . . Note=Lethal. Q->C%2CD%2CF%2CG%2CH%2CK%2CL%2CM%2CN%2CS%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868 +P06634 UniProtKB Mutagenesis 192 192 . . . Note=Impairs RNA-helicase activity in vitro. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201868;Dbxref=PMID:15201868 +P06634 UniProtKB Mutagenesis 237 237 . . . Note=In DED1-18%3B impairs BMV RNA synthesis%3B when associated with D-317. L->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11069307;Dbxref=PMID:11069307 +P06634 UniProtKB Mutagenesis 307 307 . . . Note=Lethal in vivo and impairs ATPase and RNA-helicase activities in vitro. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10364207;Dbxref=PMID:10364207 +P06634 UniProtKB Mutagenesis 317 317 . . . Note=In DED1-18%3B impairs BMV RNA synthesis%3B when associated with M-237. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11069307;Dbxref=PMID:11069307 +P06634 UniProtKB Mutagenesis 368 368 . . . Note=In DED1-199%3B impairs protein synthesis at 15 degrees Celsius. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9045610;Dbxref=PMID:9045610 +P06634 UniProtKB Mutagenesis 405 405 . . . Note=Reduces strongly ATPase activity and strand displacement activity. F->Y%2CM%2CL%2CA%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18332124;Dbxref=PMID:18332124 +P06634 UniProtKB Mutagenesis 486 486 . . . Note=Reduces ATPase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18332124;Dbxref=PMID:18332124 +P06634 UniProtKB Mutagenesis 494 494 . . . Note=In DED1-120%3B impairs protein synthesis at 15 degrees Celsius%3B when associated with D-108. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9045610;Dbxref=PMID:9045610 +P06634 UniProtKB Sequence conflict 37 37 . . . Note=S->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38307 1 211 +P38307 UniProtKB Chain 1 211 . . . ID=PRO_0000219053;Note=Degradation in the endoplasmic reticulum protein 1 +P38307 UniProtKB Topological domain 1 4 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38307 UniProtKB Transmembrane 5 25 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38307 UniProtKB Topological domain 26 55 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38307 UniProtKB Transmembrane 56 76 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38307 UniProtKB Topological domain 77 93 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38307 UniProtKB Transmembrane 94 114 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38307 UniProtKB Topological domain 115 142 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38307 UniProtKB Transmembrane 143 163 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38307 UniProtKB Topological domain 164 211 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38307 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23363603;Dbxref=PMID:23363603 +P38307 UniProtKB Mutagenesis 2 2 . . . Note=Cleavage of initiator methionine%2C acetylation of Ala-2 by NatA%2C slightly reduced acetylation levels but no significant effect on endogenous stability or ability to degrade CPY*. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23363603;Dbxref=PMID:23363603 +P38307 UniProtKB Mutagenesis 2 2 . . . Note=No effect on ability to degrade CPY*. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23363603;Dbxref=PMID:23363603 +P38307 UniProtKB Mutagenesis 2 2 . . . Note=N-terminus not predicted to be acetylated. Strongly decreases endogenous stability. D->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23363603;Dbxref=PMID:23363603 +P38307 UniProtKB Mutagenesis 2 2 . . . Note=Predicted to lead to acetylation by NatC. No effect on endogenous stability or ability to degrade CPY*. D->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23363603;Dbxref=PMID:23363603 +P38307 UniProtKB Mutagenesis 59 59 . . . Note=In der1-2%3B impairs the ability to degrade misfolded proteins. S->L +P38307 UniProtKB Sequence conflict 145 145 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04930 1 467 +Q04930 UniProtKB Chain 1 467 . . . ID=PRO_0000227691;Note=Transcription factor CRF1 +##sequence-region Q04659 1 317 +Q04659 UniProtKB Chain 1 317 . . . ID=PRO_0000203277;Note=Chromosome segregation in meiosis protein 3 +##sequence-region P40512 1 444 +P40512 UniProtKB Chain 1 444 . . . ID=PRO_0000121028;Note=Cop9 signalosome complex subunit 11 +P40512 UniProtKB Domain 258 364 . . . Note=PCI +##sequence-region P49956 1 741 +P49956 UniProtKB Chain 1 741 . . . ID=PRO_0000089645;Note=Chromosome transmission fidelity protein 18 +P49956 UniProtKB Nucleotide binding 183 190 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P49956 UniProtKB Mutagenesis 189 189 . . . Note=Fails to unload PCNA. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15964801;Dbxref=PMID:15964801 +P49956 UniProtKB Beta strand 719 722 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +P49956 UniProtKB Helix 736 739 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MSM +##sequence-region Q01454 1 927 +Q01454 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1448101;Dbxref=PMID:1448101 +Q01454 UniProtKB Chain 2 927 . . . ID=PRO_0000050948;Note=DNA polymerase alpha-binding protein +Q01454 UniProtKB Repeat 10 49 . . . Note=WD 1 +Q01454 UniProtKB Repeat 134 173 . . . Note=WD 2 +Q01454 UniProtKB Repeat 227 266 . . . Note=WD 3 +Q01454 UniProtKB Repeat 273 313 . . . Note=WD 4 +Q01454 UniProtKB Repeat 699 739 . . . Note=WD 5 +Q01454 UniProtKB Modified residue 377 377 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q01454 UniProtKB Modified residue 379 379 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q01454 UniProtKB Modified residue 398 398 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q01454 UniProtKB Modified residue 401 401 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q01454 UniProtKB Modified residue 411 411 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q01454 UniProtKB Modified residue 463 463 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q01454 UniProtKB Sequence conflict 112 112 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01454 UniProtKB Sequence conflict 112 112 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01454 UniProtKB Sequence conflict 588 588 . . . Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01454 UniProtKB Sequence conflict 590 590 . . . Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01454 UniProtKB Sequence conflict 601 601 . . . Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01454 UniProtKB Sequence conflict 835 835 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01454 UniProtKB Beta strand 489 496 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 498 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 510 518 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Turn 520 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 526 532 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 536 539 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 541 547 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Turn 549 551 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 553 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 566 569 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 578 583 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 588 592 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 596 600 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 606 611 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 615 621 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 624 631 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Turn 632 634 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 635 642 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 649 656 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Helix 666 669 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Helix 674 679 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 686 689 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 695 698 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 703 709 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Turn 713 715 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 717 723 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Helix 724 731 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Turn 732 734 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HOG +Q01454 UniProtKB Beta strand 738 748 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 751 760 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 772 775 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Helix 783 795 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Helix 819 844 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Beta strand 847 849 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Helix 851 874 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Turn 875 877 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Helix 879 886 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Helix 892 904 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +Q01454 UniProtKB Helix 908 924 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C8H +##sequence-region Q03375 1 135 +Q03375 UniProtKB Chain 1 135 . . . ID=PRO_0000123505;Note=Pre-mRNA-splicing factor CWC21 +Q03375 UniProtKB Region 53 97 . . . Note=Interaction with PRP8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19854871;Dbxref=PMID:19854871 +Q03375 UniProtKB Coiled coil 65 102 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03375 UniProtKB Beta strand 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q03375 UniProtKB Beta strand 24 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P53769 1 259 +P53769 UniProtKB Chain 1 259 . . . ID=PRO_0000055895;Note=Pre-mRNA-splicing factor CWC24 +P53769 UniProtKB Zinc finger 138 166 . . . Note=C3H1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 +P53769 UniProtKB Zinc finger 199 237 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +P53769 UniProtKB Modified residue 33 33 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53769 UniProtKB Modified residue 105 105 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +##sequence-region P00045 1 113 +P00045 UniProtKB Chain 1 113 . . . ID=PRO_0000108338;Note=Cytochrome c iso-2 +P00045 UniProtKB Metal binding 28 28 . . . Note=Iron (heme axial ligand) +P00045 UniProtKB Metal binding 90 90 . . . Note=Iron (heme axial ligand) +P00045 UniProtKB Binding site 24 24 . . . Note=Heme (covalent) +P00045 UniProtKB Binding site 27 27 . . . Note=Heme (covalent) +P00045 UniProtKB Beta strand 4 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTC +P00045 UniProtKB Helix 13 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTC +P00045 UniProtKB Turn 24 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTC +P00045 UniProtKB Helix 45 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTC +P00045 UniProtKB Beta strand 48 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YEA +P00045 UniProtKB Helix 60 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTC +P00045 UniProtKB Helix 71 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTC +P00045 UniProtKB Helix 81 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTC +P00045 UniProtKB Helix 98 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTC +##sequence-region P47103 1 393 +P47103 UniProtKB Chain 1 393 . . . ID=PRO_0000064174;Note=Peptidyl-prolyl cis-trans isomerase CYP7 +P47103 UniProtKB Domain 8 196 . . . Note=PPIase cyclophilin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00156 +P47103 UniProtKB Repeat 240 273 . . . Note=TPR 1 +P47103 UniProtKB Repeat 292 325 . . . Note=TPR 2 +P47103 UniProtKB Repeat 330 363 . . . Note=TPR 3 +P47103 UniProtKB Sequence conflict 237 237 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47103 UniProtKB Beta strand 6 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Beta strand 16 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Turn 27 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Helix 31 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Beta strand 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Beta strand 61 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Turn 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Beta strand 70 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Turn 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Beta strand 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Turn 87 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Helix 100 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Beta strand 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Beta strand 125 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Beta strand 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Beta strand 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Beta strand 144 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Helix 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Turn 155 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Beta strand 160 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Helix 168 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Beta strand 185 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Beta strand 189 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Helix 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Beta strand 205 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Helix 213 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Helix 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Helix 233 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Helix 256 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Turn 277 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Helix 281 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Helix 308 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Helix 326 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Helix 346 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +P47103 UniProtKB Helix 366 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JHE +##sequence-region P35176 1 225 +P35176 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35176 UniProtKB Chain 23 225 . . . ID=PRO_0000025488;Note=Peptidyl-prolyl cis-trans isomerase D +P35176 UniProtKB Domain 37 195 . . . Note=PPIase cyclophilin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00156 +P35176 UniProtKB Motif 222 225 . . . Note=Prevents secretion from ER +P35176 UniProtKB Glycosylation 139 139 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P14832 1 162 +P14832 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:2687115;Dbxref=PMID:22814378,PMID:2687115 +P14832 UniProtKB Chain 2 162 . . . ID=PRO_0000064132;Note=Peptidyl-prolyl cis-trans isomerase +P14832 UniProtKB Domain 5 161 . . . Note=PPIase cyclophilin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00156 +P14832 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:2687115,ECO:0000269|PubMed:8431466;Dbxref=PMID:22814378,PMID:2687115,PMID:8431466 +P14832 UniProtKB Modified residue 71 71 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14832 UniProtKB Modified residue 142 142 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14832 UniProtKB Modified residue 145 145 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P14832 UniProtKB Cross-link 29 29 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P14832 UniProtKB Cross-link 42 42 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P14832 UniProtKB Cross-link 123 123 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P14832 UniProtKB Cross-link 139 139 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P14832 UniProtKB Cross-link 151 151 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P14832 UniProtKB Cross-link 158 158 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P14832 UniProtKB Beta strand 3 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN +P14832 UniProtKB Beta strand 13 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN +P14832 UniProtKB Turn 24 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN +P14832 UniProtKB Helix 28 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN +P14832 UniProtKB Turn 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN +P14832 UniProtKB Beta strand 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN +P14832 UniProtKB Turn 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN +P14832 UniProtKB Beta strand 59 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN +P14832 UniProtKB Turn 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN +P14832 UniProtKB Beta strand 68 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN +P14832 UniProtKB Beta strand 92 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN +P14832 UniProtKB Beta strand 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN +P14832 UniProtKB Beta strand 110 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN +P14832 UniProtKB Helix 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN +P14832 UniProtKB Turn 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN +P14832 UniProtKB Beta strand 126 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN +P14832 UniProtKB Helix 134 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN +P14832 UniProtKB Beta strand 154 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VDN +##sequence-region P31373 1 394 +P31373 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8511969;Dbxref=PMID:8511969 +P31373 UniProtKB Chain 2 394 . . . ID=PRO_0000114754;Note=Cystathionine gamma-lyase +P31373 UniProtKB Binding site 52 52 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P31373 UniProtKB Binding site 104 104 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P31373 UniProtKB Binding site 109 109 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P31373 UniProtKB Binding site 334 334 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P31373 UniProtKB Modified residue 204 204 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P31373 UniProtKB Modified residue 362 362 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P31373 UniProtKB Helix 9 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Beta strand 38 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Turn 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Helix 56 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Beta strand 72 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Helix 80 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Beta strand 96 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Helix 105 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Turn 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Beta strand 123 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Helix 128 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Beta strand 138 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Turn 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Helix 158 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Turn 169 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Beta strand 175 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Turn 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Helix 184 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Helix 190 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Beta strand 196 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Turn 202 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Beta strand 215 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Helix 222 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Helix 241 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Helix 254 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Turn 276 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Beta strand 279 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Helix 293 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Helix 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Beta strand 307 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Helix 317 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Beta strand 328 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Beta strand 342 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Turn 346 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Turn 356 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Beta strand 361 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Beta strand 368 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +P31373 UniProtKB Helix 378 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N8P +##sequence-region Q12248 1 94 +Q12248 UniProtKB Chain 1 94 . . . ID=PRO_0000127613;Note=DASH complex subunit DAD1 +Q12248 UniProtKB Modified residue 91 91 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P69850 1 94 +P69850 UniProtKB Chain 1 94 . . . ID=PRO_0000175951;Note=DASH complex subunit DAD3 +##sequence-region P25334 1 318 +P25334 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25334 UniProtKB Chain 21 318 . . . ID=PRO_0000025494;Note=Peptidyl-prolyl cis-trans isomerase CPR4 +P25334 UniProtKB Transmembrane 286 303 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25334 UniProtKB Domain 55 225 . . . Note=PPIase cyclophilin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00156 +P25334 UniProtKB Glycosylation 166 166 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P06106 1 444 +P06106 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7765825,ECO:0000269|PubMed:8511969;Dbxref=PMID:7765825,PMID:8511969 +P06106 UniProtKB Chain 2 444 . . . ID=PRO_0000114776;Note=Homocysteine/cysteine synthase +P06106 UniProtKB Modified residue 44 44 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P06106 UniProtKB Modified residue 209 209 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06721 +P06106 UniProtKB Cross-link 160 160 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P38719 1 431 +P38719 UniProtKB Chain 1 431 . . . ID=PRO_0000055038;Note=ATP-dependent RNA helicase DBP8 +P38719 UniProtKB Domain 33 209 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P38719 UniProtKB Domain 242 389 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P38719 UniProtKB Nucleotide binding 46 53 . . . Note=ATP +P38719 UniProtKB Motif 2 30 . . . Note=Q motif +P38719 UniProtKB Motif 155 158 . . . Note=DEAD box +P38719 UniProtKB Mutagenesis 51 52 . . . Note=In DBP8-1%3B loss of activity. GK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11222764;Dbxref=PMID:11222764 +P38719 UniProtKB Mutagenesis 52 52 . . . Note=Decreases ATPase activity in vitro. K->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16772403;Dbxref=PMID:16772403 +P38719 UniProtKB Mutagenesis 155 156 . . . Note=In DBP8-2%3B loss of activity. DE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11222764;Dbxref=PMID:11222764 +P38719 UniProtKB Mutagenesis 155 155 . . . Note=Decreases ATPase activity in vitro. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16772403;Dbxref=PMID:16772403 +P38719 UniProtKB Mutagenesis 188 190 . . . Note=In DBP8-3%3B severely affects growth. TAT->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11222764;Dbxref=PMID:11222764 +P38719 UniProtKB Mutagenesis 341 342 . . . Note=In DBP8-4%3B no effect on growth. RS->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11222764;Dbxref=PMID:11222764 +##sequence-region P32460 1 244 +P32460 UniProtKB Chain 1 244 . . . ID=PRO_0000079806;Note=Protein DCG1 +##sequence-region P0CH63 1 225 +P0CH63 UniProtKB Chain 1 225 . . . ID=PRO_0000202670;Note=Cyanamide hydratase DDI2 +P0CH63 UniProtKB Domain 52 162 . . . Note=HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01175 +##sequence-region Q99288 1 334 +Q99288 UniProtKB Chain 1 334 . . . ID=PRO_0000244436;Note=Broad-range acid phosphatase DET1 +Q99288 UniProtKB Region 44 45 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99288 UniProtKB Region 168 171 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99288 UniProtKB Region 195 205 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99288 UniProtKB Active site 32 32 . . . Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62707 +Q99288 UniProtKB Active site 126 126 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62707 +Q99288 UniProtKB Binding site 38 38 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99288 UniProtKB Binding site 108 108 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99288 UniProtKB Modified residue 248 248 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q05080 1 669 +Q05080 UniProtKB Chain 1 669 . . . ID=PRO_0000079750;Note=Cytokinesis protein 2 +Q05080 UniProtKB Domain 1 261 . . . Note=F-BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01077 +Q05080 UniProtKB Domain 599 667 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +Q05080 UniProtKB Coiled coil 134 200 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05080 UniProtKB Modified residue 337 337 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05080 UniProtKB Modified residue 366 366 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05080 UniProtKB Modified residue 421 421 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05080 UniProtKB Helix 5 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPE +Q05080 UniProtKB Helix 15 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPE +Q05080 UniProtKB Helix 31 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPE +Q05080 UniProtKB Helix 70 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPE +Q05080 UniProtKB Helix 102 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPE +Q05080 UniProtKB Helix 158 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPE +Q05080 UniProtKB Helix 164 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPE +Q05080 UniProtKB Helix 258 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPE +##sequence-region P53728 1 308 +P53728 UniProtKB Chain 1 308 . . . ID=PRO_0000064175;Note=Peptidyl-prolyl cis-trans isomerase CYP8 +P53728 UniProtKB Domain 56 215 . . . Note=PPIase cyclophilin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00156 +P53728 UniProtKB Sequence conflict 8 8 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P23285 1 205 +P23285 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23285 UniProtKB Chain 21 205 . . . ID=PRO_0000025486;Note=Peptidyl-prolyl cis-trans isomerase B +P23285 UniProtKB Domain 39 198 . . . Note=PPIase cyclophilin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00156 +##sequence-region P25719 1 182 +P25719 UniProtKB Transit peptide 1 20 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1547957;Dbxref=PMID:1547957 +P25719 UniProtKB Chain 21 182 . . . ID=PRO_0000025487;Note=Peptidyl-prolyl cis-trans isomerase C%2C mitochondrial +P25719 UniProtKB Domain 25 181 . . . Note=PPIase cyclophilin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00156 +P25719 UniProtKB Mutagenesis 73 73 . . . Note=Strongly reduces in vitro PPIase activity and in vivo protein folding activity. Reduces binding to cyclosporin A 2-fold. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10025965;Dbxref=PMID:10025965 +P25719 UniProtKB Mutagenesis 144 144 . . . Note=Strongly reduces in vitro PPIase activity and in vivo protein folding activity. Reduces binding to cyclosporin A 2-fold. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10025965;Dbxref=PMID:10025965 +##sequence-region P21705 1 255 +P21705 UniProtKB Chain 1 255 . . . ID=PRO_0000079776;Note=Protein DAL82 +P21705 UniProtKB Compositional bias 100 108 . . . Note=Poly-Ser +P21705 UniProtKB Sequence conflict 87 87 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21705 UniProtKB Sequence conflict 104 104 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P20448 1 770 +P20448 UniProtKB Chain 1 770 . . . ID=PRO_0000055018;Note=ATP-dependent RNA helicase HCA4 +P20448 UniProtKB Domain 72 246 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P20448 UniProtKB Domain 278 437 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P20448 UniProtKB Nucleotide binding 85 92 . . . Note=ATP +P20448 UniProtKB Motif 41 69 . . . Note=Q motif +P20448 UniProtKB Motif 194 197 . . . Note=DEAD box +P20448 UniProtKB Modified residue 692 692 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P20448 UniProtKB Modified residue 710 710 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P20448 UniProtKB Modified residue 714 714 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P20448 UniProtKB Modified residue 743 743 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P20448 UniProtKB Mutagenesis 91 91 . . . Note=Lethal and prevents release of U14 snoRNA from pre-ribosomes. K->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16209945;Dbxref=PMID:16209945 +P20448 UniProtKB Mutagenesis 225 225 . . . Note=Lethal and prevents release of U14 snoRNA from pre-ribosomes%3B when associated with A-227. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16209945;Dbxref=PMID:16209945 +P20448 UniProtKB Mutagenesis 227 227 . . . Note=Lethal and prevents release of U14 snoRNA from pre-ribosomes%3B when associated with A-225. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16209945;Dbxref=PMID:16209945 +P20448 UniProtKB Sequence conflict 36 36 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20448 UniProtKB Sequence conflict 381 381 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20448 UniProtKB Sequence conflict 465 465 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20448 UniProtKB Sequence conflict 512 512 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20448 UniProtKB Sequence conflict 668 673 . . . Note=KQEKKR->NKRRRG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20448 UniProtKB Sequence conflict 675 675 . . . Note=R->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08558 1 271 +Q08558 UniProtKB Chain 1 271 . . . ID=PRO_0000232996;Note=Delta(3%2C5)-Delta(2%2C4)-dienoyl-CoA isomerase +Q08558 UniProtKB Region 62 66 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05871 +Q08558 UniProtKB Motif 269 271 . . . Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08558 UniProtKB Active site 152 152 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05871 +Q08558 UniProtKB Binding site 120 120 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05871 +##sequence-region P40087 1 428 +P40087 UniProtKB Chain 1 428 . . . ID=PRO_0000210997;Note=DNA damage-inducible protein 1 +P40087 UniProtKB Domain 1 80 . . . Note=Ubiquitin-like +P40087 UniProtKB Domain 389 428 . . . Note=UBA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212 +P40087 UniProtKB Cross-link 171 171 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P40087 UniProtKB Cross-link 257 257 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14557538;Dbxref=PMID:14557538 +P40087 UniProtKB Beta strand 3 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MRP +P40087 UniProtKB Turn 8 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MRP +P40087 UniProtKB Beta strand 13 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MRP +P40087 UniProtKB Helix 25 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MRP +P40087 UniProtKB Helix 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MRP +P40087 UniProtKB Beta strand 44 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MRP +P40087 UniProtKB Beta strand 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N7E +P40087 UniProtKB Helix 60 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MRP +P40087 UniProtKB Beta strand 70 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MRP +P40087 UniProtKB Turn 76 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MRP +P40087 UniProtKB Helix 90 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KES +P40087 UniProtKB Helix 105 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KES +P40087 UniProtKB Helix 118 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KES +P40087 UniProtKB Helix 125 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KES +P40087 UniProtKB Helix 133 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KES +P40087 UniProtKB Helix 155 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KES +P40087 UniProtKB Helix 168 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KES +P40087 UniProtKB Beta strand 205 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z +P40087 UniProtKB Beta strand 213 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z +P40087 UniProtKB Beta strand 227 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z +P40087 UniProtKB Helix 230 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z +P40087 UniProtKB Helix 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z +P40087 UniProtKB Beta strand 260 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z +P40087 UniProtKB Beta strand 272 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z +P40087 UniProtKB Beta strand 286 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z +P40087 UniProtKB Helix 291 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z +P40087 UniProtKB Beta strand 300 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z +P40087 UniProtKB Turn 303 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z +P40087 UniProtKB Beta strand 307 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z +P40087 UniProtKB Beta strand 313 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z +P40087 UniProtKB Helix 320 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z2Z +P40087 UniProtKB Helix 392 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MR9 +P40087 UniProtKB Turn 400 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MR9 +P40087 UniProtKB Helix 405 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MR9 +P40087 UniProtKB Helix 419 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MR9 +##sequence-region P69851 1 72 +P69851 UniProtKB Chain 1 72 . . . ID=PRO_0000176053;Note=DASH complex subunit DAD4 +P69851 UniProtKB Coiled coil 19 47 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P69851 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P32328 1 564 +P32328 UniProtKB Chain 1 564 . . . ID=PRO_0000085917;Note=Serine/threonine-protein kinase DBF20 +P32328 UniProtKB Domain 169 469 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32328 UniProtKB Domain 470 547 . . . Note=AGC-kinase C-terminal +P32328 UniProtKB Nucleotide binding 175 183 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32328 UniProtKB Active site 292 292 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P32328 UniProtKB Binding site 198 198 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32328 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22204 +P32328 UniProtKB Modified residue 366 366 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32328 UniProtKB Modified residue 536 536 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22204 +P32328 UniProtKB Sequence conflict 81 81 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32328 UniProtKB Sequence conflict 337 337 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32328 UniProtKB Sequence conflict 350 350 . . . Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P33750 1 489 +P33750 UniProtKB Chain 1 489 . . . ID=PRO_0000051222;Note=Protein SOF1 +P33750 UniProtKB Repeat 65 105 . . . Note=WD 1 +P33750 UniProtKB Repeat 113 158 . . . Note=WD 2 +P33750 UniProtKB Repeat 177 214 . . . Note=WD 3 +P33750 UniProtKB Repeat 217 257 . . . Note=WD 4 +P33750 UniProtKB Repeat 259 299 . . . Note=WD 5 +P33750 UniProtKB Repeat 303 342 . . . Note=WD 6 +P33750 UniProtKB Repeat 346 385 . . . Note=WD 7 +##sequence-region P53550 1 970 +P53550 UniProtKB Chain 1 970 . . . ID=PRO_0000057054;Note=m7GpppN-mRNA hydrolase +P53550 UniProtKB Domain 101 228 . . . Note=Nudix hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00794 +P53550 UniProtKB Motif 134 155 . . . Note=Nudix box +P53550 UniProtKB Compositional bias 345 430 . . . Note=Pro-rich +P53550 UniProtKB Compositional bias 436 439 . . . Note=Poly-Ser +P53550 UniProtKB Metal binding 149 149 . . . Note=Manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53550 UniProtKB Metal binding 153 153 . . . Note=Manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53550 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53550 UniProtKB Modified residue 439 439 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53550 UniProtKB Modified residue 677 677 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53550 UniProtKB Modified residue 679 679 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53550 UniProtKB Modified residue 682 682 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53550 UniProtKB Modified residue 751 751 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53550 UniProtKB Modified residue 771 771 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53550 UniProtKB Modified residue 773 773 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53550 UniProtKB Modified residue 778 778 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53550 UniProtKB Natural variant 188 188 . . . Note=In strain: YJM339. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 288 288 . . . Note=In strain: V1-09%2C YJM269%2C YJM270%2C YJM326%2C YJM339%2C YJM627 and YJM1129. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 301 301 . . . Note=In strain: YJM280%2C YJM 20 and YJM339. L->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 319 319 . . . Note=In strain: YJM627. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 494 494 . . . Note=In strain: YJM339. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 505 505 . . . Note=In strain: SK1%2C V1-09%2C YJM269%2C YJM270%2C YJM280%2C YJM320%2C YJM326%2C YJM339%2C YJM627 and YJM1129. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 522 522 . . . Note=In strain: YJM269%2C YJM270%2C YJM326 and YJM1129. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 547 547 . . . Note=In strain: YJM280 and YJM320. N->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 567 567 . . . Note=In strain: YJM269%2C YJM270%2C YJM326 and YJM1129. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 574 574 . . . Note=In strain: YJM269%2C YJM270%2C YJM280%2C YJM320%2C YJM326 and YJM1129. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 577 577 . . . Note=In strain: V1-09%2C YJM269%2C YJM270%2C YJM280%2C YJM320%2C YJM326%2C YJM339 and YJM1129. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 622 622 . . . Note=In strain: V1-09 and YJM339. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 650 650 . . . Note=In strain: YJM280 and YJM320. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 740 740 . . . Note=In strain: YJM269 and YJM270. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 807 807 . . . Note=In strain: YJM 69%2C YJM270%2C YJM326 and YJM1129. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 823 823 . . . Note=In strain: YJM269%2C YJM270%2C YJM280%2C YJM320%2C YJM326 and YJM1129. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 835 835 . . . Note=In strain: YJM280 and YJM320. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 844 844 . . . Note=In strain: V1-09. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 851 851 . . . Note=In strain: YJM280%2C YJM320 and YJM627. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 854 854 . . . Note=In strain: YJM269%2C YJM270%2C YJM326 and YJM1129. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 864 864 . . . Note=In strain: YJM269 and YJM270. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 865 865 . . . Note=In strain: YJM269%2C YJM270%2C YJM326 and YJM1129. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 866 866 . . . Note=In strain: YJM627. D->A +P53550 UniProtKB Natural variant 909 909 . . . Note=In strain: YJM280 and YJM320. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 945 945 . . . Note=In strain: YJM627. I->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Natural variant 951 951 . . . Note=In strain: V1-09. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53550 UniProtKB Mutagenesis 60 60 . . . Note=In DCP2-7%3B impairs mRNA decay at 37 degrees Celsius%3B when associated with V-68 and V-142. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11139489;Dbxref=PMID:11139489 +P53550 UniProtKB Mutagenesis 68 68 . . . Note=In DCP2-7%3B impairs mRNA decay at 37 degrees Celsius%3B when associated with D-60 and V-142. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11139489;Dbxref=PMID:11139489 +P53550 UniProtKB Mutagenesis 142 142 . . . Note=In DCP2-7%3B impairs mRNA decay at 37 degrees Celsius%3B when associated with D-60 and V-68. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11139489;Dbxref=PMID:11139489 +P53550 UniProtKB Sequence conflict 425 425 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53550 UniProtKB Beta strand 105 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3 +P53550 UniProtKB Beta strand 117 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3 +P53550 UniProtKB Beta strand 132 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3 +P53550 UniProtKB Beta strand 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVB +P53550 UniProtKB Helix 142 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3 +P53550 UniProtKB Turn 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3 +P53550 UniProtKB Beta strand 167 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3 +P53550 UniProtKB Beta strand 175 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3 +P53550 UniProtKB Beta strand 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVB +P53550 UniProtKB Beta strand 194 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3 +P53550 UniProtKB Helix 207 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3 +P53550 UniProtKB Helix 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3 +P53550 UniProtKB Beta strand 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3 +P53550 UniProtKB Helix 224 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3 +P53550 UniProtKB Helix 228 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3 +P53550 UniProtKB Helix 242 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KG3 +##sequence-region P18899 1 430 +P18899 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2114092,ECO:0000269|PubMed:8444852;Dbxref=PMID:2114092,PMID:8444852 +P18899 UniProtKB Chain 2 430 . . . ID=PRO_0000079849;Note=Stress protein DDR48 +P18899 UniProtKB Repeat 74 81 . . . Note=1 +P18899 UniProtKB Repeat 82 89 . . . Note=2 +P18899 UniProtKB Repeat 90 97 . . . Note=3 +P18899 UniProtKB Repeat 98 105 . . . Note=4 +P18899 UniProtKB Repeat 106 113 . . . Note=5 +P18899 UniProtKB Repeat 114 121 . . . Note=6 +P18899 UniProtKB Repeat 124 131 . . . Note=7%3B approximate +P18899 UniProtKB Repeat 132 139 . . . Note=8 +P18899 UniProtKB Repeat 141 148 . . . Note=9 +P18899 UniProtKB Repeat 149 156 . . . Note=10 +P18899 UniProtKB Repeat 157 164 . . . Note=11 +P18899 UniProtKB Repeat 165 172 . . . Note=12 +P18899 UniProtKB Repeat 175 182 . . . Note=13%3B approximate +P18899 UniProtKB Repeat 183 190 . . . Note=14 +P18899 UniProtKB Repeat 191 198 . . . Note=15 +P18899 UniProtKB Repeat 201 208 . . . Note=16%3B approximate +P18899 UniProtKB Repeat 209 216 . . . Note=17 +P18899 UniProtKB Repeat 217 224 . . . Note=18 +P18899 UniProtKB Repeat 225 232 . . . Note=19 +P18899 UniProtKB Repeat 233 240 . . . Note=20 +P18899 UniProtKB Repeat 243 250 . . . Note=21%3B approximate +P18899 UniProtKB Repeat 251 258 . . . Note=22 +P18899 UniProtKB Repeat 260 267 . . . Note=23 +P18899 UniProtKB Repeat 268 275 . . . Note=24 +P18899 UniProtKB Repeat 278 285 . . . Note=25%3B approximate +P18899 UniProtKB Repeat 287 294 . . . Note=26 +P18899 UniProtKB Repeat 296 303 . . . Note=27 +P18899 UniProtKB Repeat 306 313 . . . Note=28%3B approximate +P18899 UniProtKB Repeat 314 321 . . . Note=29 +P18899 UniProtKB Repeat 322 329 . . . Note=30 +P18899 UniProtKB Repeat 332 339 . . . Note=31%3B approximate +P18899 UniProtKB Repeat 340 347 . . . Note=32 +P18899 UniProtKB Repeat 348 355 . . . Note=33 +P18899 UniProtKB Repeat 358 365 . . . Note=34%3B approximate +P18899 UniProtKB Repeat 366 373 . . . Note=35 +P18899 UniProtKB Repeat 375 382 . . . Note=36 +P18899 UniProtKB Repeat 393 400 . . . Note=37%3B approximate +P18899 UniProtKB Repeat 407 414 . . . Note=38 +P18899 UniProtKB Region 74 414 . . . Note=38 X 8 AA approximate tandem repeats of S-[NS]-N-[ND]-D-S-Y-G +P18899 UniProtKB Modified residue 183 183 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P18899 UniProtKB Modified residue 191 191 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P18899 UniProtKB Modified residue 314 314 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P18899 UniProtKB Modified residue 322 322 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P18899 UniProtKB Sequence conflict 9 9 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18899 UniProtKB Sequence conflict 38 38 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P31385 1 405 +P31385 UniProtKB Chain 1 405 . . . ID=PRO_0000079864;Note=Transcriptional regulatory protein DEP1 +P31385 UniProtKB Compositional bias 81 177 . . . Note=Glu-rich +P31385 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P31385 UniProtKB Modified residue 120 120 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P31385 UniProtKB Modified residue 370 370 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P36108 1 232 +P36108 UniProtKB Chain 1 232 . . . ID=PRO_0000211477;Note=DOA4-independent degradation protein 4 +P36108 UniProtKB Region 183 232 . . . Note=Interaction with VPS4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17949747;Dbxref=PMID:17949747 +P36108 UniProtKB Coiled coil 14 97 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36108 UniProtKB Motif 219 229 . . . Note=MIT-interacting motif +P36108 UniProtKB Mutagenesis 221 221 . . . Note=Abolishes interaction with VPS4. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17928861;Dbxref=PMID:17928861 +P36108 UniProtKB Mutagenesis 224 224 . . . Note=Abolishes interaction with VPS4. Impairs sorting. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17928861;Dbxref=PMID:17928861 +P36108 UniProtKB Mutagenesis 225 225 . . . Note=Abolishes interaction with VPS4. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17928861;Dbxref=PMID:17928861 +P36108 UniProtKB Mutagenesis 228 229 . . . Note=Greatly impairs sorting. LK->DD +P36108 UniProtKB Mutagenesis 228 228 . . . Note=Abolishes interaction with VPS4. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17928861;Dbxref=PMID:17928861 +P36108 UniProtKB Mutagenesis 229 229 . . . Note=Abolishes interaction with VPS4. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17928861;Dbxref=PMID:17928861 +P36108 UniProtKB Helix 188 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6X +P36108 UniProtKB Helix 197 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6X +P36108 UniProtKB Beta strand 201 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6X +P36108 UniProtKB Helix 219 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V6X +##sequence-region P52868 1 283 +P52868 UniProtKB Chain 1 283 . . . ID=PRO_0000071129;Note=Pre-mRNA-splicing factor CWC23 +P52868 UniProtKB Domain 15 87 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +##sequence-region P40312 1 120 +P40312 UniProtKB Chain 1 120 . . . ID=PRO_0000166035;Note=Cytochrome b5 +P40312 UniProtKB Transmembrane 98 118 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40312 UniProtKB Domain 2 78 . . . Note=Cytochrome b5 heme-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279 +P40312 UniProtKB Metal binding 37 37 . . . Note=Iron (heme axial ligand);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279 +P40312 UniProtKB Metal binding 61 61 . . . Note=Iron (heme axial ligand);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279 +P40312 UniProtKB Sequence conflict 17 17 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P14922 1 966 +P14922 UniProtKB Chain 1 966 . . . ID=PRO_0000106327;Note=General transcriptional corepressor CYC8 +P14922 UniProtKB Repeat 46 79 . . . Note=TPR 1 +P14922 UniProtKB Repeat 80 113 . . . Note=TPR 2 +P14922 UniProtKB Repeat 114 147 . . . Note=TPR 3 +P14922 UniProtKB Repeat 150 183 . . . Note=TPR 4 +P14922 UniProtKB Repeat 187 220 . . . Note=TPR 5 +P14922 UniProtKB Repeat 224 257 . . . Note=TPR 6 +P14922 UniProtKB Repeat 262 295 . . . Note=TPR 7 +P14922 UniProtKB Repeat 296 329 . . . Note=TPR 8 +P14922 UniProtKB Repeat 330 363 . . . Note=TPR 9 +P14922 UniProtKB Repeat 364 398 . . . Note=TPR 10 +P14922 UniProtKB Region 467 682 . . . Note=Prion domain (PrD) +P14922 UniProtKB Compositional bias 15 30 . . . Note=Poly-Gln +P14922 UniProtKB Modified residue 429 429 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P14922 UniProtKB Modified residue 475 475 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14922 UniProtKB Modified residue 710 710 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P14922 UniProtKB Modified residue 741 741 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14922 UniProtKB Modified residue 768 768 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14922 UniProtKB Modified residue 815 815 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P14922 UniProtKB Modified residue 817 817 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P14922 UniProtKB Modified residue 866 866 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14922 UniProtKB Modified residue 943 943 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P14922 UniProtKB Sequence conflict 547 547 . . . Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14922 UniProtKB Sequence conflict 547 547 . . . Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07533 1 885 +Q07533 UniProtKB Chain 1 885 . . . ID=PRO_0000079751;Note=Cytokinesis protein 3 +Q07533 UniProtKB Domain 9 70 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +Q07533 UniProtKB Modified residue 209 209 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q07533 UniProtKB Modified residue 292 292 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07533 UniProtKB Modified residue 313 313 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q07533 UniProtKB Modified residue 354 354 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q07533 UniProtKB Modified residue 391 391 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region P36162 1 133 +P36162 UniProtKB Chain 1 133 . . . ID=PRO_0000211598;Note=DASH complex subunit DAD2 +P36162 UniProtKB Coiled coil 1 51 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36162 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P53267 1 343 +P53267 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53267 UniProtKB Chain 2 343 . . . ID=PRO_0000127663;Note=DASH complex subunit DAM1 +P53267 UniProtKB Coiled coil 125 158 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53267 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53267 UniProtKB Modified residue 20 20 . . . Note=Phosphoserine%3B by IPL1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12408861;Dbxref=PMID:12408861 +P53267 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P53267 UniProtKB Modified residue 257 257 . . . Note=Phosphoserine%3B by IPL1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12408861;Dbxref=PMID:12408861 +P53267 UniProtKB Modified residue 265 265 . . . Note=Phosphoserine%3B by IPL1;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:12408861;Dbxref=PMID:19779198,PMID:12408861 +P53267 UniProtKB Modified residue 292 292 . . . Note=Phosphoserine%3B by IPL1;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:12408861;Dbxref=PMID:19779198,PMID:12408861 +P53267 UniProtKB Mutagenesis 111 111 . . . Note=In DAM1-1%3B produces abnormal spindles resulting in growth arrest at 34 degrees Celsius. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10397771;Dbxref=PMID:10397771 +##sequence-region P13483 1 248 +P13483 UniProtKB Chain 1 248 . . . ID=PRO_0000079787;Note=Oligo(A)/oligo(T)-binding protein +P13483 UniProtKB Repeat 8 12 . . . Note=1 +P13483 UniProtKB Repeat 14 18 . . . Note=2 +P13483 UniProtKB Repeat 26 30 . . . Note=3 +P13483 UniProtKB DNA binding 1 36 . . . . +P13483 UniProtKB Region 8 30 . . . Note=3 X 5 AA repeats of G-R-K-P-G +P13483 UniProtKB Compositional bias 111 127 . . . Note=Poly-Gln +P13483 UniProtKB Compositional bias 155 188 . . . Note=Asn-rich +##sequence-region P53202 1 744 +P53202 UniProtKB Chain 1 744 . . . ID=PRO_0000119806;Note=Cullin-3 +P53202 UniProtKB Cross-link 688 688 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13616 +##sequence-region Q02554 1 436 +Q02554 UniProtKB Chain 1 436 . . . ID=PRO_0000079565;Note=Cold sensitive U2 snRNA suppressor 1 +Q02554 UniProtKB Modified residue 104 104 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02554 UniProtKB Modified residue 112 112 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02554 UniProtKB Modified residue 114 114 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02554 UniProtKB Natural variant 181 181 . . . Note=In allele CUS1-54%3B cold-sensitive growth suppressor. E->K +##sequence-region P00175 1 591 +P00175 UniProtKB Transit peptide 1 80 . . . Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:165435,ECO:0000269|PubMed:6365548;Dbxref=PMID:165435,PMID:6365548 +P00175 UniProtKB Chain 81 591 . . . ID=PRO_0000006480;Note=Cytochrome b2%2C mitochondrial +P00175 UniProtKB Domain 88 165 . . . Note=Cytochrome b5 heme-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279 +P00175 UniProtKB Domain 197 563 . . . Note=FMN hydroxy acid dehydrogenase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00683 +P00175 UniProtKB Region 177 190 . . . Note=Hinge +P00175 UniProtKB Region 567 591 . . . Note=Tail (wraps around the molecular 4-fold axis) +P00175 UniProtKB Active site 453 453 . . . Note=Proton acceptor +P00175 UniProtKB Metal binding 123 123 . . . Note=Iron (heme axial ligand) +P00175 UniProtKB Metal binding 146 146 . . . Note=Iron (heme axial ligand) +P00175 UniProtKB Binding site 177 177 . . . Note=Heme b +P00175 UniProtKB Binding site 219 219 . . . Note=Heme b +P00175 UniProtKB Binding site 223 223 . . . Note=Heme b +P00175 UniProtKB Binding site 376 376 . . . Note=Heme b +P00175 UniProtKB Binding site 456 456 . . . Note=Substrate +P00175 UniProtKB Sequence conflict 165 165 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00175 UniProtKB Sequence conflict 165 165 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00175 UniProtKB Sequence conflict 466 466 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00175 UniProtKB Sequence conflict 513 513 . . . Note=R->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00175 UniProtKB Sequence conflict 570 570 . . . Note=V->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00175 UniProtKB Helix 95 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Beta strand 104 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Beta strand 112 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Turn 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 120 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 127 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Turn 132 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 139 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 150 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Beta strand 160 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Beta strand 170 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FCB +P00175 UniProtKB Helix 183 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 205 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 218 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Beta strand 228 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LDC +P00175 UniProtKB Helix 232 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 240 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Beta strand 261 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Beta strand 266 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 280 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Turn 285 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 289 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Beta strand 298 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Beta strand 305 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 315 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Beta strand 325 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FCB +P00175 UniProtKB Beta strand 329 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 339 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Beta strand 357 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 370 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 398 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Beta strand 404 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LTD +P00175 UniProtKB Helix 412 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Beta strand 426 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 434 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Beta strand 446 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Turn 453 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 464 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Turn 477 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 481 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FCB +P00175 UniProtKB Beta strand 484 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 495 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Beta strand 507 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 513 545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 550 552 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 555 557 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Turn 561 564 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +P00175 UniProtKB Helix 574 579 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KBI +##sequence-region P54838 1 584 +P54838 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P54838 UniProtKB Chain 2 584 . . . ID=PRO_0000121522;Note=Dihydroxyacetone kinase 1 +P54838 UniProtKB Domain 7 353 . . . Note=DhaK;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00814 +P54838 UniProtKB Domain 386 582 . . . Note=DhaL;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00813 +P54838 UniProtKB Nucleotide binding 415 418 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P54838 UniProtKB Nucleotide binding 459 460 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P54838 UniProtKB Nucleotide binding 514 515 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P54838 UniProtKB Nucleotide binding 567 569 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P54838 UniProtKB Region 51 54 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P54838 UniProtKB Active site 220 220 . . . Note=Tele-hemiaminal-histidine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00814 +P54838 UniProtKB Binding site 103 103 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P54838 UniProtKB Binding site 108 108 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P54838 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P54838 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P54838 UniProtKB Modified residue 5 5 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P54838 UniProtKB Modified residue 365 365 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P54838 UniProtKB Modified residue 512 512 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q12382 1 290 +Q12382 UniProtKB Chain 1 290 . . . ID=PRO_0000240382;Note=CTP-dependent diacylglycerol kinase 1 +Q12382 UniProtKB Topological domain 1 77 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12382 UniProtKB Transmembrane 78 95 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12382 UniProtKB Topological domain 96 103 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12382 UniProtKB Transmembrane 104 124 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12382 UniProtKB Topological domain 125 140 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12382 UniProtKB Transmembrane 141 161 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12382 UniProtKB Topological domain 162 163 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12382 UniProtKB Transmembrane 164 184 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12382 UniProtKB Topological domain 185 203 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12382 UniProtKB Transmembrane 204 224 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12382 UniProtKB Topological domain 225 244 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12382 UniProtKB Transmembrane 245 265 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12382 UniProtKB Topological domain 266 290 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12382 UniProtKB Modified residue 44 44 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12382 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12382 UniProtKB Modified residue 46 46 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12382 UniProtKB Glycosylation 11 11 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12382 UniProtKB Glycosylation 197 197 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12382 UniProtKB Glycosylation 270 270 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12382 UniProtKB Mutagenesis 76 76 . . . Note=Loss of kinase activity. Not temperature-sensitive for growth. Regular shaped nuclear membrane structure. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18458076;Dbxref=PMID:18458076 +Q12382 UniProtKB Mutagenesis 77 77 . . . Note=Loss of kinase activity. Not temperature-sensitive for growth. Regular shaped nuclear membrane structure. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18458076;Dbxref=PMID:18458076 +Q12382 UniProtKB Mutagenesis 177 177 . . . Note=No kinase activity. Not temperature-sensitive for growth. Does not trigger nuclear membrane expansion. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18458075,ECO:0000269|PubMed:18458076;Dbxref=PMID:18458075,PMID:18458076 +Q12382 UniProtKB Mutagenesis 184 184 . . . Note=70%25 reduction in kinase activity. Not temperature-sensitive for growth. Regular shaped nuclear membrane structure. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18458076;Dbxref=PMID:18458076 +##sequence-region Q3E808 1 48 +Q3E808 UniProtKB Transit peptide 1 28 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E808 UniProtKB Chain 29 48 . . . ID=PRO_0000247800;Note=2-deoxy-glucose resistant protein 1%2C mitochondrial +##sequence-region P21623 1 536 +P21623 UniProtKB Chain 1 536 . . . ID=PRO_0000079920;Note=Spore wall maturation protein DIT1 +P21623 UniProtKB Sequence conflict 273 273 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P54861 1 757 +P54861 UniProtKB Chain 1 757 . . . ID=PRO_0000206586;Note=Dynamin-related protein DNM1 +P54861 UniProtKB Domain 25 333 . . . Note=Dynamin-type G +P54861 UniProtKB Domain 670 757 . . . Note=GED;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00720 +P54861 UniProtKB Nucleotide binding 35 42 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54861 UniProtKB Nucleotide binding 175 179 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54861 UniProtKB Nucleotide binding 244 247 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54861 UniProtKB Modified residue 629 629 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P54861 UniProtKB Mutagenesis 705 705 . . . Note=Induces an increase of mitochondrial fission. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11553714;Dbxref=PMID:11553714 +P54861 UniProtKB Sequence conflict 124 124 . . . Note=H->ISPD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40059 1 670 +P40059 UniProtKB Chain 1 670 . . . ID=PRO_0000197108;Note=Transcriptional regulatory protein DOT6 +P40059 UniProtKB Domain 67 121 . . . Note=HTH myb-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +P40059 UniProtKB DNA binding 94 117 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +P40059 UniProtKB Modified residue 245 245 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40059 UniProtKB Modified residue 247 247 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40059 UniProtKB Modified residue 487 487 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40059 UniProtKB Modified residue 489 489 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40059 UniProtKB Modified residue 491 491 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P47027 1 764 +P47027 UniProtKB Chain 1 764 . . . ID=PRO_0000079989;Note=DNA replication regulator DPB11 +P47027 UniProtKB Domain 1 99 . . . Note=BRCT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033 +P47027 UniProtKB Domain 129 220 . . . Note=BRCT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033 +P47027 UniProtKB Domain 322 418 . . . Note=BRCT 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033 +P47027 UniProtKB Sequence conflict 72 72 . . . Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47027 UniProtKB Sequence conflict 295 296 . . . Note=QQ->HR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47027 UniProtKB Sequence conflict 515 515 . . . Note=C->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47027 UniProtKB Sequence conflict 603 603 . . . Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47027 UniProtKB Sequence conflict 656 656 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32469 1 300 +P32469 UniProtKB Chain 1 300 . . . ID=PRO_0000156147;Note=Diphthine methyl ester synthase +P32469 UniProtKB Region 113 114 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32469 UniProtKB Binding site 9 9 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32469 UniProtKB Binding site 85 85 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32469 UniProtKB Binding site 88 88 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32469 UniProtKB Binding site 164 164 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32469 UniProtKB Binding site 222 222 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32469 UniProtKB Binding site 247 247 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32469 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32469 UniProtKB Modified residue 298 298 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32469 UniProtKB Sequence conflict 287 287 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38332 1 387 +P38332 UniProtKB Chain 1 387 . . . ID=PRO_0000202523;Note=Diphthine methyltransferase +P38332 UniProtKB Repeat 62 102 . . . Note=WD 1 +P38332 UniProtKB Repeat 119 159 . . . Note=WD 2 +P38332 UniProtKB Repeat 195 237 . . . Note=WD 3 +P38332 UniProtKB Repeat 241 286 . . . Note=WD 4 +P38332 UniProtKB Repeat 357 387 . . . Note=WD 5 +##sequence-region P32892 1 752 +P32892 UniProtKB Chain 1 752 . . . ID=PRO_0000055045;Note=ATP-dependent RNA helicase DRS1 +P32892 UniProtKB Domain 262 437 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P32892 UniProtKB Domain 448 639 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P32892 UniProtKB Nucleotide binding 275 282 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P32892 UniProtKB Coiled coil 621 667 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32892 UniProtKB Motif 231 259 . . . Note=Q motif +P32892 UniProtKB Motif 385 388 . . . Note=DEAD box +P32892 UniProtKB Compositional bias 170 190 . . . Note=Poly-Glu +P32892 UniProtKB Modified residue 208 208 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32892 UniProtKB Mutagenesis 191 191 . . . Note=No growth at 13 degrees Celsius%3B when associated with Q-431 and G-472. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362 +P32892 UniProtKB Mutagenesis 260 260 . . . Note=No growth at 13 degrees Celsius%3B when associated with P-564. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362 +P32892 UniProtKB Mutagenesis 273 273 . . . Note=No growth at 13 degrees Celsius. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362 +P32892 UniProtKB Mutagenesis 288 288 . . . Note=No growth at 13 degrees Celsius. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362 +P32892 UniProtKB Mutagenesis 291 291 . . . Note=No growth at 13 degrees Celsius%3B when associated with G-637. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362 +P32892 UniProtKB Mutagenesis 305 305 . . . Note=No growth at 13 degrees Celsius%3B when associated with V-306. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362 +P32892 UniProtKB Mutagenesis 306 306 . . . Note=No growth at 13 degrees Celsius%3B when associated with D-305. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362 +P32892 UniProtKB Mutagenesis 414 414 . . . Note=No growth at 13 degrees Celsius. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362 +P32892 UniProtKB Mutagenesis 429 429 . . . Note=No growth at 13 degrees Celsius. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362 +P32892 UniProtKB Mutagenesis 431 431 . . . Note=No growth at 13 degrees Celsius%3B when associated with T-191 and G-472. L->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362 +P32892 UniProtKB Mutagenesis 472 472 . . . Note=No growth at 13 degrees Celsius%3B when associated with T-191 and Q-431. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362 +P32892 UniProtKB Mutagenesis 509 509 . . . Note=No growth at 13 degrees Celsius. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362 +P32892 UniProtKB Mutagenesis 563 563 . . . Note=No growth at 13 degrees Celsius. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362 +P32892 UniProtKB Mutagenesis 564 564 . . . Note=No growth at 13 degrees Celsius%3B when associated with V-260. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362 +P32892 UniProtKB Mutagenesis 637 637 . . . Note=No growth at 13 degrees Celsius%3B when associated with V-291. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11911362;Dbxref=PMID:11911362 +##sequence-region P23501 1 404 +P23501 UniProtKB Chain 1 404 . . . ID=PRO_0000203216;Note=Dihydrosphingosine 1-phosphate phosphatase YSR3 +P23501 UniProtKB Topological domain 1 86 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47013 +P23501 UniProtKB Transmembrane 87 107 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23501 UniProtKB Topological domain 108 113 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47013 +P23501 UniProtKB Transmembrane 114 134 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23501 UniProtKB Topological domain 135 154 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47013 +P23501 UniProtKB Transmembrane 155 176 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23501 UniProtKB Topological domain 177 182 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47013 +P23501 UniProtKB Transmembrane 183 203 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23501 UniProtKB Topological domain 204 215 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47013 +P23501 UniProtKB Transmembrane 216 236 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23501 UniProtKB Topological domain 237 241 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47013 +P23501 UniProtKB Transmembrane 242 262 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23501 UniProtKB Topological domain 263 319 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47013 +P23501 UniProtKB Transmembrane 320 340 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23501 UniProtKB Topological domain 341 379 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47013 +P23501 UniProtKB Transmembrane 380 400 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23501 UniProtKB Topological domain 401 404 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47013 +P23501 UniProtKB Region 129 137 . . . Note=Phosphatase sequence motif I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23501 UniProtKB Region 158 161 . . . Note=Phosphatase sequence motif II;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23501 UniProtKB Region 204 215 . . . Note=Phosphatase sequence motif III;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23501 UniProtKB Active site 161 161 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A924 +P23501 UniProtKB Active site 211 211 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A924 +P23501 UniProtKB Site 215 215 . . . Note=Stabilizes the active site histidine for nucleophilic attack;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A924 +P23501 UniProtKB Glycosylation 62 62 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53720 1 384 +P53720 UniProtKB Chain 1 384 . . . ID=PRO_0000162154;Note=tRNA-dihydrouridine(20) synthase [NAD(P)+] +P53720 UniProtKB Nucleotide binding 12 14 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +P53720 UniProtKB Nucleotide binding 222 224 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +P53720 UniProtKB Nucleotide binding 249 250 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +P53720 UniProtKB Active site 117 117 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +P53720 UniProtKB Binding site 88 88 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +P53720 UniProtKB Binding site 160 160 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +P53720 UniProtKB Binding site 188 188 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +##sequence-region P07262 1 454 +P07262 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P07262 UniProtKB Chain 2 454 . . . ID=PRO_0000182798;Note=NADP-specific glutamate dehydrogenase 1 +P07262 UniProtKB Nucleotide binding 174 203 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07262 UniProtKB Active site 110 110 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10011 +P07262 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P07262 UniProtKB Cross-link 325 325 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P07262 UniProtKB Cross-link 371 371 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P07262 UniProtKB Cross-link 433 433 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P07262 UniProtKB Sequence conflict 83 83 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07262 UniProtKB Sequence conflict 198 198 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07262 UniProtKB Sequence conflict 255 255 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07262 UniProtKB Sequence conflict 266 266 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07262 UniProtKB Sequence conflict 358 364 . . . Note=ATGPSEA->PLDQAT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P37298 1 181 +P37298 UniProtKB Transit peptide 1 31 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8120006;Dbxref=PMID:8120006 +P37298 UniProtKB Chain 32 181 . . . ID=PRO_0000006496;Note=Succinate dehydrogenase [ubiquinone] cytochrome b small subunit%2C mitochondrial +P37298 UniProtKB Topological domain 32 66 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37298 UniProtKB Transmembrane 67 88 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37298 UniProtKB Topological domain 89 98 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37298 UniProtKB Transmembrane 99 118 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37298 UniProtKB Topological domain 119 127 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37298 UniProtKB Transmembrane 128 148 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37298 UniProtKB Topological domain 149 181 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37298 UniProtKB Metal binding 109 109 . . . Note=Iron (heme axial ligand);Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37298 UniProtKB Binding site 120 120 . . . Note=Ubiquinone%3B shared with IP/SDHB;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P37298 UniProtKB Mutagenesis 100 100 . . . Note=Impairs respiratory growth and reduces quinone reductase activity. F->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11279023;Dbxref=PMID:11279023 +P37298 UniProtKB Mutagenesis 102 102 . . . Note=Impairs respiratory growth and reduces quinone reductase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11279023;Dbxref=PMID:11279023 +P37298 UniProtKB Mutagenesis 109 109 . . . Note=Decreases SDH cytochrome b content. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14672930;Dbxref=PMID:14672930 +P37298 UniProtKB Mutagenesis 120 120 . . . Note=Abolishes quinone reductase activity. Little effect on complex assembly. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17208193;Dbxref=PMID:17208193 +P37298 UniProtKB Mutagenesis 130 130 . . . Note=Reduces SDH FAD content. Probably impairs complex assembly. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11279023;Dbxref=PMID:11279023 +##sequence-region Q08496 1 732 +Q08496 UniProtKB Chain 1 732 . . . ID=PRO_0000233003;Note=Protein DIA2 +Q08496 UniProtKB Repeat 15 48 . . . Note=TPR 1 +Q08496 UniProtKB Repeat 78 111 . . . Note=TPR 2 +Q08496 UniProtKB Repeat 113 145 . . . Note=TPR 3 +Q08496 UniProtKB Domain 204 251 . . . Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080 +Q08496 UniProtKB Repeat 425 449 . . . Note=LRR 1 +Q08496 UniProtKB Repeat 480 505 . . . Note=LRR 2 +Q08496 UniProtKB Repeat 509 532 . . . Note=LRR 3 +Q08496 UniProtKB Repeat 550 574 . . . Note=LRR 4 +Q08496 UniProtKB Repeat 579 602 . . . Note=LRR 5 +Q08496 UniProtKB Repeat 616 637 . . . Note=LRR 6 +Q08496 UniProtKB Repeat 645 669 . . . Note=LRR 7 +Q08496 UniProtKB Modified residue 393 393 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q12086 1 430 +Q12086 UniProtKB Chain 1 430 . . . ID=PRO_0000154046;Note=DNA damage-inducible protein DIN7 +Q12086 UniProtKB Region 1 96 . . . Note=N-domain +Q12086 UniProtKB Region 114 247 . . . Note=I-domain +Q12086 UniProtKB Metal binding 30 30 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12086 UniProtKB Metal binding 78 78 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12086 UniProtKB Metal binding 150 150 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12086 UniProtKB Metal binding 152 152 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12086 UniProtKB Metal binding 171 171 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12086 UniProtKB Metal binding 173 173 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12086 UniProtKB Metal binding 227 227 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P04819 1 755 +P04819 UniProtKB Transit peptide 1 44 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04819 UniProtKB Chain 45 755 . . . ID=PRO_0000007274;Note=DNA ligase 1 +P04819 UniProtKB Region 309 318 . . . Note=Interaction with target DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04819 UniProtKB Region 493 495 . . . Note=Interaction with target DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04819 UniProtKB Active site 419 419 . . . Note=N6-AMP-lysine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10135 +P04819 UniProtKB Metal binding 472 472 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04819 UniProtKB Metal binding 571 571 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04819 UniProtKB Binding site 417 417 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04819 UniProtKB Binding site 424 424 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04819 UniProtKB Binding site 440 440 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04819 UniProtKB Binding site 576 576 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04819 UniProtKB Binding site 590 590 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04819 UniProtKB Binding site 596 596 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04819 UniProtKB Site 164 164 . . . Note=Interaction with target DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04819 UniProtKB Site 441 441 . . . Note=Interaction with target DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04819 UniProtKB Site 622 622 . . . Note=Interaction with target DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04819 UniProtKB Site 647 647 . . . Note=Interaction with target DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04819 UniProtKB Modified residue 58 58 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P04819 UniProtKB Modified residue 75 75 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +P04819 UniProtKB Modified residue 119 119 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04819 UniProtKB Modified residue 123 123 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04819 UniProtKB Alternative sequence 1 23 . . . ID=VSP_018719;Note=In isoform Nuclear. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04819 UniProtKB Sequence conflict 69 69 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04819 UniProtKB Sequence conflict 186 186 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04819 UniProtKB Sequence conflict 671 671 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04819 UniProtKB Sequence conflict 724 724 . . . Note=R->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04819 UniProtKB Helix 41 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OD8 +##sequence-region Q08387 1 944 +Q08387 UniProtKB Chain 1 944 . . . ID=PRO_0000059582;Note=DNA ligase 4 +Q08387 UniProtKB Domain 681 780 . . . Note=BRCT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033 +Q08387 UniProtKB Domain 836 941 . . . Note=BRCT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033 +Q08387 UniProtKB Active site 282 282 . . . Note=N6-AMP-lysine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10135 +Q08387 UniProtKB Metal binding 340 340 . . . Note=Magnesium 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08387 UniProtKB Metal binding 442 442 . . . Note=Magnesium 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08387 UniProtKB Binding site 280 280 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08387 UniProtKB Binding site 287 287 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08387 UniProtKB Binding site 304 304 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08387 UniProtKB Binding site 447 447 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08387 UniProtKB Binding site 458 458 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08387 UniProtKB Binding site 464 464 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38821 1 490 +P38821 UniProtKB Chain 1 490 . . . ID=PRO_0000173455;Note=Aspartyl aminopeptidase 4 +P38821 UniProtKB Metal binding 97 97 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38821 UniProtKB Metal binding 273 273 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38821 UniProtKB Metal binding 273 273 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38821 UniProtKB Metal binding 309 309 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38821 UniProtKB Metal binding 362 362 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38821 UniProtKB Metal binding 456 456 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38821 UniProtKB Binding site 173 173 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38821 UniProtKB Binding site 308 308 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38821 UniProtKB Binding site 362 362 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38821 UniProtKB Binding site 365 365 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38821 UniProtKB Binding site 390 390 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38821 UniProtKB Binding site 397 397 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38774 1 246 +P38774 UniProtKB Chain 1 246 . . . ID=PRO_0000079974;Note=2-deoxyglucose-6-phosphate phosphatase 1 +P38774 UniProtKB Active site 12 12 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38774 UniProtKB Active site 14 14 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38774 UniProtKB Metal binding 12 12 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38774 UniProtKB Metal binding 14 14 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38774 UniProtKB Metal binding 183 183 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q03921 1 1698 +Q03921 UniProtKB Chain 1 1698 . . . ID=PRO_0000190976;Note=Protein dopey +Q03921 UniProtKB Modified residue 244 244 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P46957 1 487 +P46957 UniProtKB Chain 1 487 . . . ID=PRO_0000096174;Note=DNA polymerase delta small subunit +P46957 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P46957 UniProtKB Modified residue 20 20 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P46957 UniProtKB Sequence conflict 156 156 . . . Note=L->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46957 UniProtKB Sequence conflict 465 465 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P15801 1 1254 +P15801 UniProtKB Chain 1 1254 . . . ID=PRO_0000101278;Note=DNA polymerase gamma +P15801 UniProtKB Sequence conflict 8 8 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15801 UniProtKB Sequence conflict 35 35 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15801 UniProtKB Sequence conflict 222 222 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15801 UniProtKB Sequence conflict 357 357 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15801 UniProtKB Sequence conflict 540 541 . . . Note=TH->MN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15801 UniProtKB Sequence conflict 616 616 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15801 UniProtKB Sequence conflict 661 661 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15801 UniProtKB Sequence conflict 978 978 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15801 UniProtKB Sequence conflict 986 986 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36152 1 348 +P36152 UniProtKB Chain 1 348 . . . ID=PRO_0000203219;Note=Fe-S cluster assembly protein DRE2 +P36152 UniProtKB Region 1 158 . . . Note=N-terminal domain +P36152 UniProtKB Region 159 242 . . . Note=Linker +P36152 UniProtKB Region 243 348 . . . Note=Intrinsically disordered +P36152 UniProtKB Motif 311 314 . . . Note=Cx2C motif 1 +P36152 UniProtKB Motif 322 325 . . . Note=Cx2C motif 2 +P36152 UniProtKB Metal binding 252 252 . . . Note=Iron-sulfur (2Fe-2S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03115 +P36152 UniProtKB Metal binding 263 263 . . . Note=Iron-sulfur (2Fe-2S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03115 +P36152 UniProtKB Metal binding 266 266 . . . Note=Iron-sulfur (2Fe-2S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03115 +P36152 UniProtKB Metal binding 268 268 . . . Note=Iron-sulfur (2Fe-2S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03115 +P36152 UniProtKB Modified residue 206 206 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P36152 UniProtKB Beta strand 5 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1 +P36152 UniProtKB Helix 13 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1 +P36152 UniProtKB Helix 19 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1 +P36152 UniProtKB Beta strand 34 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1 +P36152 UniProtKB Helix 42 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1 +P36152 UniProtKB Beta strand 54 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1 +P36152 UniProtKB Beta strand 59 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1 +P36152 UniProtKB Helix 75 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1 +P36152 UniProtKB Helix 96 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1 +P36152 UniProtKB Beta strand 107 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1 +P36152 UniProtKB Beta strand 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1 +P36152 UniProtKB Beta strand 116 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM1 +##sequence-region Q04792 1 585 +Q04792 UniProtKB Chain 1 585 . . . ID=PRO_0000146977;Note=Glutamate decarboxylase +Q04792 UniProtKB Modified residue 318 318 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P35732 1 738 +P35732 UniProtKB Chain 1 738 . . . ID=PRO_0000203177;Note=RNA polymerase II degradation factor 1 +P35732 UniProtKB Domain 21 63 . . . Note=CUE;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00468 +P35732 UniProtKB Compositional bias 382 718 . . . Note=Gln-rich +P35732 UniProtKB Compositional bias 574 580 . . . Note=Poly-Ala +P35732 UniProtKB Compositional bias 708 716 . . . Note=Poly-Ala +P35732 UniProtKB Modified residue 260 260 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P35732 UniProtKB Modified residue 273 273 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P35732 UniProtKB Modified residue 307 307 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35732 UniProtKB Modified residue 338 338 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P35732 UniProtKB Modified residue 646 646 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region Q99234 1 619 +Q99234 UniProtKB Chain 1 619 . . . ID=PRO_0000079873;Note=Protein DFG16 +Q99234 UniProtKB Topological domain 1 1 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99234 UniProtKB Transmembrane 2 22 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99234 UniProtKB Topological domain 23 167 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99234 UniProtKB Transmembrane 168 188 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99234 UniProtKB Topological domain 189 203 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99234 UniProtKB Transmembrane 204 224 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99234 UniProtKB Topological domain 225 291 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99234 UniProtKB Transmembrane 292 312 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99234 UniProtKB Topological domain 313 321 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99234 UniProtKB Transmembrane 322 342 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99234 UniProtKB Topological domain 343 378 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99234 UniProtKB Transmembrane 379 399 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99234 UniProtKB Topological domain 400 410 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99234 UniProtKB Transmembrane 411 431 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99234 UniProtKB Topological domain 432 619 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99234 UniProtKB Compositional bias 510 517 . . . Note=Poly-Arg +##sequence-region P32330 1 852 +P32330 UniProtKB Chain 1 852 . . . ID=PRO_0000051479;Note=2-deoxy-glucose resistant protein 2 +P32330 UniProtKB Repeat 171 210 . . . Note=WD 1 +P32330 UniProtKB Repeat 278 316 . . . Note=WD 2 +P32330 UniProtKB Repeat 318 358 . . . Note=WD 3 +P32330 UniProtKB Repeat 426 471 . . . Note=WD 4 +P32330 UniProtKB Repeat 476 515 . . . Note=WD 5 +P32330 UniProtKB Repeat 651 689 . . . Note=WD 6 +P32330 UniProtKB Modified residue 716 716 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P39708 1 457 +P39708 UniProtKB Chain 1 457 . . . ID=PRO_0000182799;Note=NADP-specific glutamate dehydrogenase 2 +P39708 UniProtKB Nucleotide binding 175 204 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39708 UniProtKB Active site 111 111 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10011 +P39708 UniProtKB Cross-link 326 326 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07262 +P39708 UniProtKB Cross-link 372 372 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07262 +P39708 UniProtKB Cross-link 436 436 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07262 +##sequence-region Q04603 1 196 +Q04603 UniProtKB Chain 1 196 . . . ID=PRO_0000191754;Note=DNA polymerase epsilon subunit D +Q04603 UniProtKB Modified residue 183 183 . . . Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q3E840 1 82 +Q3E840 UniProtKB Chain 1 82 . . . ID=PRO_0000082639;Note=Diphthamide biosynthesis protein 3 +Q3E840 UniProtKB Zinc finger 3 59 . . . Note=DPH-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00456 +Q3E840 UniProtKB Compositional bias 79 82 . . . Note=Poly-Ala +Q3E840 UniProtKB Beta strand 4 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +Q3E840 UniProtKB Helix 9 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +Q3E840 UniProtKB Beta strand 12 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +Q3E840 UniProtKB Turn 16 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +Q3E840 UniProtKB Beta strand 20 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +Q3E840 UniProtKB Beta strand 28 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +Q3E840 UniProtKB Helix 35 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +Q3E840 UniProtKB Beta strand 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +Q3E840 UniProtKB Beta strand 48 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4D4O +Q3E840 UniProtKB Beta strand 53 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4X33 +Q3E840 UniProtKB Helix 60 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AX2 +##sequence-region P39517 1 506 +P39517 UniProtKB Chain 1 506 . . . ID=PRO_0000055044;Note=ATP-dependent RNA helicase DHH1 +P39517 UniProtKB Domain 77 247 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P39517 UniProtKB Domain 257 417 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P39517 UniProtKB Nucleotide binding 90 97 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P39517 UniProtKB Motif 46 74 . . . Note=Q motif +P39517 UniProtKB Motif 195 198 . . . Note=DEAD box +P39517 UniProtKB Compositional bias 434 505 . . . Note=Gln-rich +P39517 UniProtKB Mutagenesis 89 89 . . . Note=Leads to mRNA turnover defect and no growth at 37 degrees Celsius%3B when associated with A-91. Impairs RNA binding in vitro. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15987810;Dbxref=PMID:15987810 +P39517 UniProtKB Mutagenesis 91 91 . . . Note=Leads to mRNA turnover defect and no growth at 37 degrees Celsius%3B when associated with A-89. Impairs RNA binding in vitro. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15987810;Dbxref=PMID:15987810 +P39517 UniProtKB Mutagenesis 195 195 . . . Note=Leads to mRNA turnover defect and no growth at 37 degrees Celsius. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15987810;Dbxref=PMID:15987810 +P39517 UniProtKB Mutagenesis 196 196 . . . Note=Leads to mRNA turnover defect and no growth at 37 degrees Celsius. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15987810;Dbxref=PMID:15987810 +P39517 UniProtKB Mutagenesis 345 345 . . . Note=Leads to mRNA turnover defect and no growth at 37 degrees Celsius. Impairs RNA binding in vitro. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15987810;Dbxref=PMID:15987810 +P39517 UniProtKB Mutagenesis 346 346 . . . Note=Leads to mRNA turnover defect and no growth at 37 degrees Celsius. Impairs RNA binding in vitro. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15987810;Dbxref=PMID:15987810 +P39517 UniProtKB Mutagenesis 369 369 . . . Note=Leads to mRNA turnover defect and no growth at 37 degrees Celsius. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15987810;Dbxref=PMID:15987810 +P39517 UniProtKB Mutagenesis 370 370 . . . Note=Leads to mRNA turnover defect and no growth at 37 degrees Celsius. Impairs RNA binding in vitro. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15987810;Dbxref=PMID:15987810 +P39517 UniProtKB Helix 48 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Helix 55 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Helix 71 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Beta strand 86 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Helix 96 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Beta strand 117 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Helix 124 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Turn 138 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Beta strand 145 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Beta strand 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Helix 154 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Beta strand 166 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Helix 172 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Beta strand 191 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Helix 197 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Helix 203 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Beta strand 221 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Helix 231 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Beta strand 245 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Beta strand 258 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Helix 267 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Helix 270 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Beta strand 284 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Helix 293 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Beta strand 310 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Helix 319 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Beta strand 333 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Beta strand 343 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Beta strand 352 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Helix 364 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Beta strand 373 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Beta strand 381 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Helix 389 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Helix 392 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +P39517 UniProtKB Beta strand 406 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BRW +P39517 UniProtKB Helix 415 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S2M +##sequence-region Q04217 1 1267 +Q04217 UniProtKB Chain 1 1267 . . . ID=PRO_0000055162;Note=Probable ATP-dependent RNA helicase DHR1 +Q04217 UniProtKB Domain 401 580 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q04217 UniProtKB Domain 675 858 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q04217 UniProtKB Nucleotide binding 414 421 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q04217 UniProtKB Motif 516 519 . . . Note=DEAH box +Q04217 UniProtKB Modified residue 181 181 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P35497 1 357 +P35497 UniProtKB Chain 1 357 . . . ID=PRO_0000160821;Note=Sorbitol dehydrogenase 1 +P35497 UniProtKB Metal binding 43 43 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35497 UniProtKB Metal binding 68 68 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35497 UniProtKB Metal binding 69 69 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35497 UniProtKB Binding site 49 49 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35497 UniProtKB Binding site 154 154 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35497 UniProtKB Binding site 301 301 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35497 UniProtKB Binding site 302 302 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region O13577 1 133 +O13577 UniProtKB Chain 1 133 . . . ID=PRO_0000247354;Note=Damage-regulated import facilitator 1 +O13577 UniProtKB Compositional bias 16 32 . . . Note=Poly-Gln +##sequence-region P40318 1 1319 +P40318 UniProtKB Chain 1 1319 . . . ID=PRO_0000072214;Note=ERAD-associated E3 ubiquitin-protein ligase DOA10 +P40318 UniProtKB Topological domain 1 131 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Transmembrane 132 152 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Topological domain 153 203 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Transmembrane 204 224 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Topological domain 225 468 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Transmembrane 469 489 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Topological domain 490 491 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Transmembrane 492 512 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Topological domain 513 626 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Transmembrane 627 647 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Topological domain 648 660 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Transmembrane 661 681 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Topological domain 682 739 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Transmembrane 740 760 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Topological domain 761 777 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Transmembrane 778 797 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Topological domain 798 965 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Transmembrane 966 986 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Topological domain 987 1019 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Transmembrane 1020 1040 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Topological domain 1041 1113 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Transmembrane 1114 1134 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Topological domain 1135 1168 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Transmembrane 1169 1189 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Topological domain 1190 1213 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Transmembrane 1214 1234 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Topological domain 1235 1270 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Transmembrane 1271 1291 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Topological domain 1292 1319 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40318 UniProtKB Zinc finger 31 100 . . . Note=RING-CH-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00623 +P40318 UniProtKB Compositional bias 288 291 . . . Note=Poly-Ala +P40318 UniProtKB Compositional bias 293 296 . . . Note=Poly-Asn +P40318 UniProtKB Compositional bias 332 341 . . . Note=Asp/Gln/Ser-rich (acidic) +P40318 UniProtKB Compositional bias 369 374 . . . Note=Poly-Gln +P40318 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40318 UniProtKB Sequence conflict 241 241 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40318 UniProtKB Sequence conflict 743 743 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40318 UniProtKB Sequence conflict 1085 1085 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40318 UniProtKB Sequence conflict 1186 1186 . . . Note=Y->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40318 UniProtKB Beta strand 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M6M +P40318 UniProtKB Beta strand 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M6M +P40318 UniProtKB Helix 67 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M6M +P40318 UniProtKB Beta strand 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M6M +##sequence-region P47110 1 350 +P47110 UniProtKB Chain 1 350 . . . ID=PRO_0000186050;Note=DNA polymerase delta subunit 3 +P47110 UniProtKB Modified residue 223 223 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47110 UniProtKB Modified residue 230 230 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P14284 1 1504 +P14284 UniProtKB Chain 1 1504 . . . ID=PRO_0000046470;Note=DNA polymerase zeta catalytic subunit +P14284 UniProtKB Zinc finger 1398 1417 . . . Note=CysA-type +P14284 UniProtKB Motif 1446 1473 . . . Note=CysB motif +P14284 UniProtKB Metal binding 1398 1398 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14284 UniProtKB Metal binding 1401 1401 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14284 UniProtKB Metal binding 1414 1414 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14284 UniProtKB Metal binding 1417 1417 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14284 UniProtKB Metal binding 1446 1446 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14284 UniProtKB Metal binding 1449 1449 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14284 UniProtKB Metal binding 1468 1468 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14284 UniProtKB Metal binding 1473 1473 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53255 1 507 +P53255 UniProtKB Chain 1 507 . . . ID=PRO_0000202810;Note=CWF19-like protein DRN1 +P53255 UniProtKB Modified residue 242 242 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53255 UniProtKB Mutagenesis 269 269 . . . Note=Causes accumulation of pre-mRNA splicing intermediates. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24919400;Dbxref=PMID:24919400 +P53255 UniProtKB Mutagenesis 272 272 . . . Note=Causes accumulation of pre-mRNA splicing intermediates. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24919400;Dbxref=PMID:24919400 +P53255 UniProtKB Mutagenesis 366 366 . . . Note=Causes accumulation of pre-mRNA splicing intermediates. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24919400;Dbxref=PMID:24919400 +P53255 UniProtKB Mutagenesis 459 459 . . . Note=Causes accumulation of pre-mRNA splicing intermediates. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24919400;Dbxref=PMID:24919400 +P53255 UniProtKB Mutagenesis 474 474 . . . Note=Causes accumulation of pre-mRNA splicing intermediates. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24919400;Dbxref=PMID:24919400 +##sequence-region P32325 1 704 +P32325 UniProtKB Chain 1 704 . . . ID=PRO_0000079791;Note=DDK kinase regulatory subunit DBF4 +P32325 UniProtKB Zinc finger 654 703 . . . Note=DBF4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00600 +P32325 UniProtKB Region 10 19 . . . Note=D box 1 +P32325 UniProtKB Region 62 70 . . . Note=D box 2 +P32325 UniProtKB Motif 83 88 . . . Note=POLO box domain (PBD)-binding +P32325 UniProtKB Modified residue 59 59 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32325 UniProtKB Modified residue 84 84 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32325 UniProtKB Modified residue 235 235 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32325 UniProtKB Modified residue 623 623 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32325 UniProtKB Mutagenesis 83 83 . . . Note=Defective for interaction with CDC5. R->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21036905;Dbxref=PMID:21036905 +P32325 UniProtKB Mutagenesis 84 84 . . . Note=No effect. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21036905;Dbxref=PMID:21036905 +P32325 UniProtKB Mutagenesis 85 85 . . . Note=Defective for interaction with CDC5. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21036905;Dbxref=PMID:21036905 +P32325 UniProtKB Mutagenesis 86 86 . . . Note=No effect. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21036905;Dbxref=PMID:21036905 +P32325 UniProtKB Mutagenesis 87 87 . . . Note=Defective for interaction with CDC5. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21036905;Dbxref=PMID:21036905 +P32325 UniProtKB Mutagenesis 88 88 . . . Note=Defective for interaction with CDC5. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21036905;Dbxref=PMID:21036905 +P32325 UniProtKB Mutagenesis 661 661 . . . Note=In DBF4-AAHH%3B weakens interaction with ARS1 origin DNA and MCM2%2C but not other known ligands%3B when associated with A-664. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20436286;Dbxref=PMID:20436286 +P32325 UniProtKB Mutagenesis 664 664 . . . Note=In DBF4-AAHH%3B weakens interaction with ARS1 origin DNA and MCM2%2C but not other known ligands%3B when associated with A-661. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20436286;Dbxref=PMID:20436286 +P32325 UniProtKB Mutagenesis 674 674 . . . Note=In DBF4-CCAA%3B weakens interaction with ARS1 origin DNA and MCM2%2C but not other known ligands%3B when associated with A-680. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20436286;Dbxref=PMID:20436286 +P32325 UniProtKB Mutagenesis 680 680 . . . Note=Weakens interaction with ARS1 origin DNA and MCM2%2C but not other known ligands. In DBF4-CCAA%3B weakens interaction with ARS1 origin DNA and MCM2%2C but not other known ligands%3B when associated with A-674. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20436286;Dbxref=PMID:20436286 +P32325 UniProtKB Mutagenesis 680 680 . . . Note=Weakens interaction with ARS1 origin DNA and MCM2%2C but not other known ligands. H->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20436286;Dbxref=PMID:20436286 +P32325 UniProtKB Sequence conflict 159 160 . . . Note=GA->NT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32325 UniProtKB Sequence conflict 177 177 . . . Note=R->RR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32325 UniProtKB Sequence conflict 197 197 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32325 UniProtKB Sequence conflict 256 256 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32325 UniProtKB Sequence conflict 416 425 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32325 UniProtKB Sequence conflict 439 439 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32325 UniProtKB Helix 106 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T2S +P32325 UniProtKB Beta strand 125 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4 +P32325 UniProtKB Helix 138 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4 +P32325 UniProtKB Beta strand 161 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4 +P32325 UniProtKB Beta strand 172 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4 +P32325 UniProtKB Helix 179 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4 +P32325 UniProtKB Helix 190 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4 +P32325 UniProtKB Beta strand 200 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4 +P32325 UniProtKB Helix 204 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4 +P32325 UniProtKB Helix 218 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4 +P32325 UniProtKB Helix 233 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OQ4 +##sequence-region P47089 1 198 +P47089 UniProtKB Chain 1 198 . . . ID=PRO_0000130609;Note=Translation machinery-associated protein 22 +P47089 UniProtKB Domain 99 170 . . . Note=SUI1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00200 +##sequence-region Q12743 1 341 +Q12743 UniProtKB Chain 1 341 . . . ID=PRO_0000219054;Note=DER1-like family member protein 1 +Q12743 UniProtKB Topological domain 1 41 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12743 UniProtKB Transmembrane 42 62 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12743 UniProtKB Topological domain 63 122 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12743 UniProtKB Transmembrane 123 143 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12743 UniProtKB Topological domain 144 170 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12743 UniProtKB Transmembrane 171 191 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12743 UniProtKB Topological domain 192 192 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12743 UniProtKB Transmembrane 193 213 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12743 UniProtKB Topological domain 214 341 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07786 1 357 +Q07786 UniProtKB Chain 1 357 . . . ID=PRO_0000160822;Note=Sorbitol dehydrogenase 2 +Q07786 UniProtKB Metal binding 43 43 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07786 UniProtKB Metal binding 68 68 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07786 UniProtKB Metal binding 69 69 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07786 UniProtKB Binding site 49 49 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07786 UniProtKB Binding site 154 154 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07786 UniProtKB Binding site 301 301 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07786 UniProtKB Binding site 302 302 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38791 1 387 +P38791 UniProtKB Chain 1 387 . . . ID=PRO_0000134488;Note=Deoxyhypusine synthase +P38791 UniProtKB Nucleotide binding 108 112 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38791 UniProtKB Nucleotide binding 134 136 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38791 UniProtKB Nucleotide binding 329 330 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38791 UniProtKB Nucleotide binding 363 364 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38791 UniProtKB Region 139 140 . . . Note=Spermidine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38791 UniProtKB Region 335 337 . . . Note=Spermidine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38791 UniProtKB Region 344 350 . . . Note=Spermidine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38791 UniProtKB Active site 350 350 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38791 UniProtKB Binding site 140 140 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38791 UniProtKB Binding site 257 257 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38791 UniProtKB Binding site 262 262 . . . Note=Spermidine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38791 UniProtKB Binding site 304 304 . . . Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38791 UniProtKB Binding site 309 309 . . . Note=Spermidine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q03373 1 323 +Q03373 UniProtKB Chain 1 323 . . . ID=PRO_0000079898;Note=Down-regulator of invasive growth 2 +Q03373 UniProtKB Modified residue 34 34 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q03373 UniProtKB Modified residue 225 225 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956 +Q03373 UniProtKB Modified residue 266 266 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03373 UniProtKB Modified residue 270 270 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40366 1 167 +P40366 UniProtKB Chain 1 167 . . . ID=PRO_0000203057;Note=Protein DLS1 +P40366 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q06819 1 143 +Q06819 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q06819 UniProtKB Chain 2 143 . . . ID=PRO_0000218286;Note=Spliceosomal protein DIB1 +Q06819 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P40564 1 432 +P40564 UniProtKB Chain 1 432 . . . ID=PRO_0000071141;Note=DnaJ-like protein 1 +P40564 UniProtKB Domain 4 73 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +P40564 UniProtKB Sequence conflict 325 325 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39976 1 496 +P39976 UniProtKB Chain 1 496 . . . ID=PRO_0000128176;Note=D-2-hydroxyglutarate--pyruvate transhydrogenase DLD3 +P39976 UniProtKB Domain 64 243 . . . Note=FAD-binding PCMH-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00718 +P39976 UniProtKB Cross-link 17 17 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region Q04216 1 342 +Q04216 UniProtKB Chain 1 342 . . . ID=PRO_0000203299;Note=Defect at low temperature protein 1 +Q04216 UniProtKB Topological domain 1 15 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04216 UniProtKB Transmembrane 16 36 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04216 UniProtKB Topological domain 37 47 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04216 UniProtKB Transmembrane 48 68 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04216 UniProtKB Topological domain 69 342 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03652 1 475 +Q03652 UniProtKB Chain 1 475 . . . ID=PRO_0000203331;Note=Protein DML1 +##sequence-region P31116 1 359 +P31116 UniProtKB Chain 1 359 . . . ID=PRO_0000066707;Note=Homoserine dehydrogenase +P31116 UniProtKB Nucleotide binding 11 18 . . . Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10700284;Dbxref=PMID:10700284 +P31116 UniProtKB Active site 223 223 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31116 UniProtKB Binding site 93 93 . . . Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10700284;Dbxref=PMID:10700284 +P31116 UniProtKB Binding site 117 117 . . . Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10700284;Dbxref=PMID:10700284 +P31116 UniProtKB Binding site 208 208 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10700284;Dbxref=PMID:10700284 +P31116 UniProtKB Cross-link 290 290 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P31116 UniProtKB Mutagenesis 117 117 . . . Note=Loss of activity. K->A +P31116 UniProtKB Mutagenesis 208 208 . . . Note=Increases KM for aspartate-semialdehyde 48-fold and reduces Kcat by 50%25. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10700284;Dbxref=PMID:10700284 +P31116 UniProtKB Mutagenesis 208 208 . . . Note=Loss of activity. E->L%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10700284;Dbxref=PMID:10700284 +P31116 UniProtKB Mutagenesis 219 219 . . . Note=Reduces Kcat 150-fold. D->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10700284;Dbxref=PMID:10700284 +P31116 UniProtKB Mutagenesis 223 223 . . . Note=Loss of activity. K->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10700284;Dbxref=PMID:10700284 +P31116 UniProtKB Sequence conflict 134 134 . . . Note=K->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31116 UniProtKB Sequence conflict 152 152 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31116 UniProtKB Sequence conflict 327 327 . . . Note=R->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31116 UniProtKB Sequence conflict 333 333 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31116 UniProtKB Beta strand 4 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Helix 15 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Beta strand 30 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Beta strand 41 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Turn 54 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBU +P31116 UniProtKB Helix 59 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Helix 73 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Beta strand 87 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Helix 96 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Helix 102 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Beta strand 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Helix 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Helix 124 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Beta strand 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBU +P31116 UniProtKB Helix 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Turn 146 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Beta strand 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBU +P31116 UniProtKB Helix 153 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Beta strand 166 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Helix 175 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Helix 194 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Helix 212 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Helix 218 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Helix 249 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Beta strand 255 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TVE +P31116 UniProtKB Helix 258 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Helix 265 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Helix 268 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Turn 279 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Beta strand 283 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Turn 293 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Beta strand 297 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Helix 310 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Beta strand 319 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Beta strand 332 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +P31116 UniProtKB Helix 341 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBF +##sequence-region Q06143 1 298 +Q06143 UniProtKB Chain 1 298 . . . ID=PRO_0000233005;Note=Mitochondrial dicarboxylate transporter +Q06143 UniProtKB Transmembrane 17 37 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06143 UniProtKB Transmembrane 58 76 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06143 UniProtKB Transmembrane 105 126 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06143 UniProtKB Transmembrane 170 189 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06143 UniProtKB Transmembrane 211 231 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06143 UniProtKB Transmembrane 265 283 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06143 UniProtKB Repeat 11 95 . . . Note=Solcar 1 +Q06143 UniProtKB Repeat 103 195 . . . Note=Solcar 2 +Q06143 UniProtKB Repeat 205 289 . . . Note=Solcar 3 +##sequence-region P36037 1 715 +P36037 UniProtKB Chain 1 715 . . . ID=PRO_0000050958;Note=Protein DOA1 +P36037 UniProtKB Repeat 11 40 . . . Note=WD 1 +P36037 UniProtKB Repeat 53 82 . . . Note=WD 2 +P36037 UniProtKB Repeat 97 125 . . . Note=WD 3 +P36037 UniProtKB Repeat 135 166 . . . Note=WD 4 +P36037 UniProtKB Repeat 177 206 . . . Note=WD 5 +P36037 UniProtKB Repeat 218 247 . . . Note=WD 6 +P36037 UniProtKB Repeat 259 288 . . . Note=WD 7 +P36037 UniProtKB Domain 352 449 . . . Note=PFU;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00727 +P36037 UniProtKB Domain 465 715 . . . Note=PUL;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00729 +P36037 UniProtKB Repeat 478 512 . . . Note=ARM 1 +P36037 UniProtKB Repeat 513 543 . . . Note=ARM 2 +P36037 UniProtKB Repeat 544 582 . . . Note=ARM 3 +P36037 UniProtKB Repeat 583 635 . . . Note=ARM 4 +P36037 UniProtKB Repeat 636 680 . . . Note=ARM 5 +P36037 UniProtKB Repeat 681 715 . . . Note=ARM 6 +P36037 UniProtKB Modified residue 332 332 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P36037 UniProtKB Mutagenesis 541 541 . . . Note=Depletion of cellular ubiquitin pools and reduced activity of the ubiquitin fusion degradation pathway. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19805280;Dbxref=PMID:19805280 +P36037 UniProtKB Mutagenesis 669 669 . . . Note=Depletion of cellular ubiquitin pools and reduced activity of the ubiquitin fusion degradation pathway. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19805280;Dbxref=PMID:19805280 +P36037 UniProtKB Sequence conflict 180 180 . . . Note=D->DI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36037 UniProtKB Beta strand 4 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 16 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 26 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 34 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 57 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Turn 64 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 68 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 78 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 102 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 111 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 119 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 128 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 140 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Turn 148 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 152 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 162 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 169 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 182 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 192 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 200 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Turn 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 212 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 223 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 234 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 241 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Turn 248 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 253 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 260 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 264 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 275 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 284 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Helix 291 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ODT +P36037 UniProtKB Beta strand 378 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L3F +P36037 UniProtKB Beta strand 383 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L3F +P36037 UniProtKB Beta strand 400 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L3F +P36037 UniProtKB Helix 410 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L3F +P36037 UniProtKB Helix 425 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L3F +P36037 UniProtKB Helix 428 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L3F +P36037 UniProtKB Helix 480 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Helix 499 509 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Helix 512 529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Helix 534 543 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Helix 544 546 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Helix 550 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Helix 554 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Helix 566 579 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Turn 583 585 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Helix 586 590 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Helix 593 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Helix 599 602 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Beta strand 608 610 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSP +P36037 UniProtKB Helix 612 634 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Helix 642 651 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Turn 652 656 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Helix 658 662 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Helix 664 680 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Helix 682 685 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Turn 688 690 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Helix 692 701 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +P36037 UniProtKB Helix 705 714 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GAE +##sequence-region P33309 1 386 +P33309 UniProtKB Chain 1 386 . . . ID=PRO_0000143191;Note=Protein DOM34 +P33309 UniProtKB Beta strand 2 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Beta strand 16 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Helix 25 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Beta strand 40 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Beta strand 63 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Turn 76 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Beta strand 80 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Beta strand 93 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Beta strand 104 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Beta strand 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Beta strand 115 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Helix 124 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Turn 136 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Beta strand 142 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Beta strand 151 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Beta strand 162 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Helix 186 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Turn 205 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Beta strand 209 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Helix 219 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Helix 237 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Helix 241 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Beta strand 246 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Turn 254 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGM +P33309 UniProtKB Helix 257 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Helix 266 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Helix 269 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Helix 278 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Turn 292 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Beta strand 296 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Helix 302 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Beta strand 314 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Helix 323 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Helix 329 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Beta strand 348 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Helix 357 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Turn 365 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +P33309 UniProtKB Beta strand 368 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VGN +##sequence-region Q12395 1 269 +Q12395 UniProtKB Chain 1 269 . . . ID=PRO_0000129518;Note=Defective in cullin neddylation protein 1 +Q12395 UniProtKB Domain 14 51 . . . Note=UBA-like +Q12395 UniProtKB Domain 70 266 . . . Note=DCUN1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00574 +Q12395 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12395 UniProtKB Helix 13 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3 +Q12395 UniProtKB Helix 29 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3 +Q12395 UniProtKB Turn 38 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3 +Q12395 UniProtKB Helix 43 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3 +Q12395 UniProtKB Helix 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L4F +Q12395 UniProtKB Helix 73 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3 +Q12395 UniProtKB Helix 90 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3 +Q12395 UniProtKB Helix 107 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3 +Q12395 UniProtKB Helix 127 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3 +Q12395 UniProtKB Helix 142 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3 +Q12395 UniProtKB Helix 160 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3 +Q12395 UniProtKB Beta strand 180 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3 +Q12395 UniProtKB Helix 184 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3 +Q12395 UniProtKB Beta strand 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2P +Q12395 UniProtKB Helix 205 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3 +Q12395 UniProtKB Beta strand 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3 +Q12395 UniProtKB Helix 225 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3 +Q12395 UniProtKB Helix 241 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3 +Q12395 UniProtKB Beta strand 252 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O2P +Q12395 UniProtKB Helix 256 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BQ3 +##sequence-region Q06151 1 350 +Q06151 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q06151 UniProtKB Chain 2 350 . . . ID=PRO_0000109798;Note=m7GpppX diphosphatase +Q06151 UniProtKB Region 259 270 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06151 UniProtKB Motif 266 270 . . . Note=Histidine triad motif;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06151 UniProtKB Active site 268 268 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96C86 +Q06151 UniProtKB Binding site 171 171 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96C86 +Q06151 UniProtKB Binding site 196 196 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96C86 +Q06151 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q06151 UniProtKB Modified residue 60 60 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q06151 UniProtKB Modified residue 66 66 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:15240832;Dbxref=PMID:19779198,PMID:15240832 +Q06151 UniProtKB Modified residue 66 66 . . . Note=Phosphothreonine%3B by YAK1;Ontology_term=ECO:0000244,ECO:0000305;evidence=ECO:0000244|PubMed:19779198,ECO:0000305|PubMed:15240832;Dbxref=PMID:19779198,PMID:15240832 +Q06151 UniProtKB Modified residue 70 70 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06151 UniProtKB Modified residue 120 120 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06151 UniProtKB Mutagenesis 66 66 . . . Note=Stronly reduces phosphorylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15240832;Dbxref=PMID:15240832 +Q06151 UniProtKB Mutagenesis 268 268 . . . Note=Loss of function. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12198172;Dbxref=PMID:12198172 +Q06151 UniProtKB Sequence conflict 66 66 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06151 UniProtKB Helix 8 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Beta strand 16 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Turn 25 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Beta strand 29 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Beta strand 39 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Turn 78 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Beta strand 82 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Beta strand 94 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Turn 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Beta strand 110 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Helix 121 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Beta strand 132 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Helix 139 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Helix 160 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Helix 172 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Beta strand 177 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Beta strand 189 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Helix 202 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Beta strand 206 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Helix 219 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Helix 224 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Helix 227 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Turn 245 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Helix 251 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Beta strand 254 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Beta strand 263 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Beta strand 268 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Turn 280 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Turn 285 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Beta strand 288 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Helix 291 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Turn 298 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Helix 305 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Beta strand 311 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Helix 320 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +Q06151 UniProtKB Helix 326 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BV3 +##sequence-region P0CH64 1 225 +P0CH64 UniProtKB Chain 1 225 . . . ID=PRO_0000397875;Note=Cyanamide hydratase DDI3 +P0CH64 UniProtKB Domain 52 162 . . . Note=HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01175 +##sequence-region P89113 1 61 +P89113 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P89113 UniProtKB Chain 23 61 . . . ID=PRO_0000021096;Note=Protein DDR2 +P89113 UniProtKB Glycosylation 24 24 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P89113 UniProtKB Glycosylation 27 27 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P54005 1 336 +P54005 UniProtKB Chain 1 336 . . . ID=PRO_0000203358;Note=Protein DIA1 +##sequence-region P69771 1 204 +P69771 UniProtKB Chain 1 204 . . . ID=PRO_0000211461;Note=Vacuolar protein-sorting-associated protein 46 +P69771 UniProtKB Region 1 103 . . . Note=Interaction with VSP24 +P69771 UniProtKB Region 104 204 . . . Note=Interaction with VSP4 +P69771 UniProtKB Region 176 204 . . . Note=Interaction with VTA1 +P69771 UniProtKB Coiled coil 9 56 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P69771 UniProtKB Coiled coil 109 129 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P69771 UniProtKB Modified residue 5 5 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P69771 UniProtKB Mutagenesis 198 198 . . . Note=Impairs sorting. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17928861;Dbxref=PMID:17928861 +P69771 UniProtKB Mutagenesis 199 199 . . . Note=Impairs sorting%3B when associated with D-202. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17928861;Dbxref=PMID:17928861 +P69771 UniProtKB Mutagenesis 202 202 . . . Note=Impairs sorting%3B when associated with D-199. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17928861;Dbxref=PMID:17928861 +P69771 UniProtKB Helix 186 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H7P +##sequence-region P32891 1 587 +P32891 UniProtKB Domain 146 327 . . . Note=FAD-binding PCMH-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00718 +P32891 UniProtKB Sequence conflict 439 439 . . . Note=A->RR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32891 UniProtKB Sequence conflict 572 587 . . . Note=DKIFKTDPNEPANDYR->GQNL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P09624 1 499 +P09624 UniProtKB Transit peptide 1 21 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3279419;Dbxref=PMID:3279419 +P09624 UniProtKB Chain 22 499 . . . ID=PRO_0000030301;Note=Dihydrolipoyl dehydrogenase%2C mitochondrial +P09624 UniProtKB Nucleotide binding 56 65 . . . Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9538259,ECO:0000269|Ref.9;Dbxref=PMID:9538259 +P09624 UniProtKB Nucleotide binding 174 176 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09624 UniProtKB Nucleotide binding 211 218 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09624 UniProtKB Nucleotide binding 352 355 . . . Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9538259,ECO:0000269|Ref.9;Dbxref=PMID:9538259 +P09624 UniProtKB Active site 478 478 . . . Note=Proton acceptor +P09624 UniProtKB Binding site 74 74 . . . Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9538259,ECO:0000269|Ref.9;Dbxref=PMID:9538259 +P09624 UniProtKB Binding site 139 139 . . . Note=FAD%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9538259,ECO:0000269|Ref.9;Dbxref=PMID:9538259 +P09624 UniProtKB Binding site 234 234 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09624 UniProtKB Binding site 268 268 . . . Note=NAD%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09624 UniProtKB Binding site 305 305 . . . Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09624 UniProtKB Binding site 346 346 . . . Note=FAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9538259,ECO:0000269|Ref.9;Dbxref=PMID:9538259 +P09624 UniProtKB Disulfide bond 65 70 . . . Note=Redox-active;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9538259;Dbxref=PMID:9538259 +P09624 UniProtKB Beta strand 23 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Helix 36 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 52 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Helix 63 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Helix 70 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Helix 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Helix 105 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 133 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 153 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JEH +P09624 UniProtKB Beta strand 163 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 188 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Helix 194 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 205 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Helix 214 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 229 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 235 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Helix 245 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 261 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 265 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Turn 275 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 279 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Turn 287 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 291 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 306 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Turn 311 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JEH +P09624 UniProtKB Turn 315 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 341 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Helix 345 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 348 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Helix 354 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Helix 377 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JEH +P09624 UniProtKB Beta strand 382 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 386 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Helix 397 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 407 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Helix 414 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Helix 418 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 429 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Turn 436 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Beta strand 440 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Helix 451 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Helix 468 472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +P09624 UniProtKB Helix 483 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1V59 +##sequence-region Q07505 1 273 +Q07505 UniProtKB Chain 1 273 . . . ID=PRO_0000161585;Note=Putative carboxymethylenebutenolidase +Q07505 UniProtKB Active site 130 130 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07505 UniProtKB Active site 191 191 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07505 UniProtKB Active site 223 223 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38823 1 416 +P38823 UniProtKB Chain 1 416 . . . ID=PRO_0000056338;Note=E3 ubiquitin-protein ligase DMA1 +P38823 UniProtKB Domain 189 252 . . . Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 +P38823 UniProtKB Zinc finger 327 371 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +P38823 UniProtKB Cross-link 150 150 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P38823 UniProtKB Cross-link 204 204 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P38823 UniProtKB Cross-link 217 217 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P38823 UniProtKB Cross-link 237 237 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P38823 UniProtKB Cross-link 240 240 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P38823 UniProtKB Cross-link 260 260 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P38823 UniProtKB Cross-link 300 300 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P38823 UniProtKB Cross-link 306 306 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P38823 UniProtKB Cross-link 313 313 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P38823 UniProtKB Cross-link 317 317 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P38823 UniProtKB Mutagenesis 192 192 . . . Note=Decreases the interaction with CDC123. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15319434;Dbxref=PMID:15319434 +P38823 UniProtKB Mutagenesis 220 220 . . . Note=Decreases the interaction with CDC123%2C when associated with L-223. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15319434;Dbxref=PMID:15319434 +P38823 UniProtKB Mutagenesis 223 223 . . . Note=Decreases the interaction with CDC123%2C when associated with A-220. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15319434;Dbxref=PMID:15319434 +P38823 UniProtKB Mutagenesis 345 345 . . . Note=Decreases the interaction with CDC123%2C when associated with A-350. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15319434;Dbxref=PMID:15319434 +P38823 UniProtKB Mutagenesis 350 350 . . . Note=Decreases the interaction with CDC123%2C when associated with S-345. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15319434;Dbxref=PMID:15319434 +##sequence-region P25453 1 334 +P25453 UniProtKB Chain 1 334 . . . ID=PRO_0000122915;Note=Meiotic recombination protein DMC1 +P25453 UniProtKB Nucleotide binding 121 128 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25453 UniProtKB Binding site 223 223 . . . Note=ssDNA or dsDNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25453 UniProtKB Binding site 226 226 . . . Note=ssDNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25453 UniProtKB Binding site 229 229 . . . Note=ssDNA or dsDNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25453 UniProtKB Binding site 235 235 . . . Note=ssDNA or dsDNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25453 UniProtKB Binding site 305 305 . . . Note=ssDNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25453 UniProtKB Mutagenesis 69 69 . . . Note=Recessive mutant%3B phenotypically null. Eliminates the ability for self-association. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9335591;Dbxref=PMID:9335591 +P25453 UniProtKB Mutagenesis 126 126 . . . Note=Dominant mutant%3B phenotypically null. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9335591;Dbxref=PMID:9335591 +##sequence-region P43595 1 202 +P43595 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43595 UniProtKB Chain 19 202 . . . ID=PRO_0000014319;Note=Protein DCV1 +P43595 UniProtKB Transmembrane 91 107 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43595 UniProtKB Transmembrane 137 155 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43595 UniProtKB Transmembrane 168 189 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08949 1 612 +Q08949 UniProtKB Chain 1 612 . . . ID=PRO_0000239638;Note=DNA damage checkpoint protein 1 +Q08949 UniProtKB Modified residue 436 436 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region P40526 1 253 +P40526 UniProtKB Chain 1 253 . . . ID=PRO_0000213682;Note=Polyprenol reductase +P40526 UniProtKB Transmembrane 18 38 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40526 UniProtKB Transmembrane 78 98 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40526 UniProtKB Transmembrane 123 143 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40526 UniProtKB Transmembrane 200 220 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q05031 1 458 +Q05031 UniProtKB Signal peptide 1 26 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05031 UniProtKB Chain 27 437 . . . ID=PRO_0000012127;Note=Mannan endo-1%2C6-alpha-mannosidase DFG5 +Q05031 UniProtKB Propeptide 438 458 . . . ID=PRO_0000012128;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05031 UniProtKB Lipidation 437 437 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05031 UniProtKB Glycosylation 89 89 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05031 UniProtKB Glycosylation 114 114 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05031 UniProtKB Glycosylation 138 138 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05031 UniProtKB Glycosylation 208 208 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05031 UniProtKB Glycosylation 231 231 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05031 UniProtKB Glycosylation 245 245 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05031 UniProtKB Glycosylation 270 270 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05031 UniProtKB Glycosylation 273 273 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05031 UniProtKB Glycosylation 417 417 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08650 1 418 +Q08650 UniProtKB Chain 1 418 . . . ID=PRO_0000233001;Note=Diacylglycerol O-acyltransferase 1 +Q08650 UniProtKB Topological domain 1 71 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08650 UniProtKB Transmembrane 72 92 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08650 UniProtKB Topological domain 93 186 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08650 UniProtKB Transmembrane 187 207 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08650 UniProtKB Topological domain 208 215 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08650 UniProtKB Transmembrane 216 236 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08650 UniProtKB Topological domain 237 289 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08650 UniProtKB Transmembrane 290 310 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08650 UniProtKB Topological domain 311 418 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08650 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q08650 UniProtKB Mutagenesis 71 71 . . . Note=Retains more than 40%25 of the wild-type enzyme activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21321129;Dbxref=PMID:21321129 +Q08650 UniProtKB Mutagenesis 73 73 . . . Note=Retains more than 40%25 of the wild-type enzyme activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21321129;Dbxref=PMID:21321129 +Q08650 UniProtKB Mutagenesis 129 131 . . . Note=Almost complete loss of enzyme activity. YFP->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21321129;Dbxref=PMID:21321129 +Q08650 UniProtKB Mutagenesis 193 196 . . . Note=Complete loss of enzyme activity. HPHG->EPHS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21321129;Dbxref=PMID:21321129 +Q08650 UniProtKB Mutagenesis 193 193 . . . Note=Almost complete loss of enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21321129;Dbxref=PMID:21321129 +Q08650 UniProtKB Mutagenesis 195 195 . . . Note=Complete loss of enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21321129;Dbxref=PMID:21321129 +##sequence-region P13663 1 365 +P13663 UniProtKB Chain 1 365 . . . ID=PRO_0000141400;Note=Aspartate-semialdehyde dehydrogenase +P13663 UniProtKB Nucleotide binding 13 16 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13663 UniProtKB Nucleotide binding 40 41 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13663 UniProtKB Nucleotide binding 187 188 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13663 UniProtKB Nucleotide binding 343 344 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13663 UniProtKB Active site 156 156 . . . Note=Acyl-thioester intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13663 UniProtKB Active site 256 256 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13663 UniProtKB Binding site 112 112 . . . Note=Phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13663 UniProtKB Binding site 184 184 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13663 UniProtKB Binding site 211 211 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13663 UniProtKB Binding site 214 214 . . . Note=Phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13663 UniProtKB Binding site 249 249 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13663 UniProtKB Modified residue 13 13 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P13663 UniProtKB Modified residue 318 318 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P13663 UniProtKB Modified residue 323 323 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P33327 1 1092 +P33327 UniProtKB Chain 1 1092 . . . ID=PRO_0000182733;Note=NAD-specific glutamate dehydrogenase +P33327 UniProtKB Active site 626 626 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10011 +##sequence-region P36009 1 735 +P36009 UniProtKB Chain 1 735 . . . ID=PRO_0000055163;Note=Probable ATP-dependent RNA helicase DHR2 +P36009 UniProtKB Domain 91 257 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P36009 UniProtKB Domain 262 456 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P36009 UniProtKB Nucleotide binding 104 111 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P36009 UniProtKB Motif 203 206 . . . Note=DEAH box +P36009 UniProtKB Sequence conflict 28 28 . . . Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36009 UniProtKB Sequence conflict 80 98 . . . Note=TLPVYQHKREIMSYIESNP->HFRLPTQARNNVIYSKQS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36009 UniProtKB Sequence conflict 277 288 . . . Note=DAVIRCCIQINQ->ALSSGVYTNKP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36009 UniProtKB Sequence conflict 339 339 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03063 1 452 +Q03063 UniProtKB Chain 1 452 . . . ID=PRO_0000079897;Note=Down-regulator of invasive growth 1 +Q03063 UniProtKB Region 212 452 . . . Note=Interaction with FUS3 and KSS1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8918885;Dbxref=PMID:8918885 +Q03063 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03063 UniProtKB Modified residue 126 126 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03063 UniProtKB Modified residue 142 142 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03063 UniProtKB Modified residue 272 272 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q03063 UniProtKB Modified residue 275 275 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q03063 UniProtKB Modified residue 330 330 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03063 UniProtKB Modified residue 379 379 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03063 UniProtKB Modified residue 395 395 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q03063 UniProtKB Modified residue 428 428 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P41819 1 318 +P41819 UniProtKB Chain 1 318 . . . ID=PRO_0000101464;Note=Dimethyladenosine transferase +P41819 UniProtKB Compositional bias 3 16 . . . Note=Lys-rich +P41819 UniProtKB Binding site 37 37 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026 +P41819 UniProtKB Binding site 39 39 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026 +P41819 UniProtKB Binding site 64 64 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026 +P41819 UniProtKB Binding site 85 85 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026 +P41819 UniProtKB Binding site 113 113 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026 +P41819 UniProtKB Binding site 128 128 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026 +##sequence-region P53388 1 608 +P53388 UniProtKB Chain 1 608 . . . ID=PRO_0000054150;Note=Dicarboxylic amino acid permease +P53388 UniProtKB Topological domain 1 90 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Transmembrane 91 111 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Topological domain 112 119 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Transmembrane 120 142 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Topological domain 143 156 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Transmembrane 157 177 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Topological domain 178 201 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Transmembrane 202 222 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Topological domain 223 231 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Transmembrane 232 252 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Topological domain 253 285 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Transmembrane 286 306 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Topological domain 307 322 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Transmembrane 323 343 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Topological domain 344 372 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Transmembrane 373 393 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Topological domain 394 423 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Transmembrane 424 444 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Topological domain 445 454 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Transmembrane 455 475 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Topological domain 476 501 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Transmembrane 502 522 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Topological domain 523 530 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Transmembrane 531 551 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Topological domain 552 608 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53388 UniProtKB Compositional bias 574 577 . . . Note=Poly-Glu +P53388 UniProtKB Modified residue 22 22 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53388 UniProtKB Cross-link 76 76 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P46681 1 530 +P46681 UniProtKB Domain 98 277 . . . Note=FAD-binding PCMH-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00718 +P46681 UniProtKB Sequence conflict 239 239 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53924 1 522 +P53924 UniProtKB Chain 1 522 . . . ID=PRO_0000056342;Note=E3 ubiquitin-protein ligase DMA2 +P53924 UniProtKB Domain 295 358 . . . Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 +P53924 UniProtKB Zinc finger 433 477 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +P53924 UniProtKB Modified residue 206 206 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53924 UniProtKB Cross-link 211 211 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P53924 UniProtKB Cross-link 256 256 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P53924 UniProtKB Cross-link 258 258 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P53924 UniProtKB Cross-link 288 288 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P53924 UniProtKB Cross-link 310 310 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P53924 UniProtKB Cross-link 333 333 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P53924 UniProtKB Cross-link 343 343 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P53924 UniProtKB Cross-link 346 346 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P53924 UniProtKB Cross-link 366 366 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P53924 UniProtKB Cross-link 406 406 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P53924 UniProtKB Cross-link 412 412 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P53924 UniProtKB Cross-link 423 423 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18202552;Dbxref=PMID:18202552 +P53924 UniProtKB Natural variant 13 13 . . . Note=In strain: YJM 269%2C YJM 270%2C YJM 326 and YJM 1129. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53924 UniProtKB Natural variant 111 111 . . . Note=In strain: YJM 269%2C YJM 270%2C YJM 326 and YJM 1129. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53924 UniProtKB Natural variant 149 149 . . . Note=In strain: YJM 269%2C YJM 270%2C YJM 326 and YJM 1129. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53924 UniProtKB Natural variant 165 165 . . . Note=In strain: YJM 267. S->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53924 UniProtKB Natural variant 202 202 . . . Note=In strain: YJM 269%2C YJM 270%2C YJM 326 and YJM 1129. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53924 UniProtKB Natural variant 239 239 . . . Note=In strain: YJM 267. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53924 UniProtKB Natural variant 428 428 . . . Note=In strain: SK1%2C V1-09%2C YJM 267%2C YJM 269%2C YJM 270%2C YJM 280%2C YJM 320%2CYJM 326%2C YJM 339 and YJM 1129. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53924 UniProtKB Natural variant 511 522 . . . Note=In strain: SK1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +##sequence-region P38859 1 1522 +P38859 UniProtKB Chain 1 1522 . . . ID=PRO_0000080711;Note=DNA replication ATP-dependent helicase/nuclease DNA2 +P38859 UniProtKB Nucleotide binding 1074 1081 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38859 UniProtKB Region 450 900 . . . Note=Nuclease activity +P38859 UniProtKB Region 901 1522 . . . Note=Helicase activity +P38859 UniProtKB Metal binding 519 519 . . . Note=Iron-sulfur (4Fe-4S) +P38859 UniProtKB Metal binding 768 768 . . . Note=Iron-sulfur (4Fe-4S) +P38859 UniProtKB Metal binding 771 771 . . . Note=Iron-sulfur (4Fe-4S) +P38859 UniProtKB Metal binding 777 777 . . . Note=Iron-sulfur (4Fe-4S) +P38859 UniProtKB Modified residue 4 4 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787 +P38859 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine%3B by CDK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787 +P38859 UniProtKB Modified residue 237 237 . . . Note=Phosphoserine%3B by CDK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787 +P38859 UniProtKB Modified residue 962 962 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38859 UniProtKB Mutagenesis 4 4 . . . Note=Abolishes phosphorylation by CDK1%2C leading to a poor recruitment at double-strand. break (DSB) sites following DNA damage%3B when associated with A-17 and A-237. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787 +P38859 UniProtKB Mutagenesis 17 17 . . . Note=Abolishes phosphorylation by CDK1%2C leading to a poor recruitment at double-strand. break (DSB) sites following DNA damage%3B when associated with A-4 and A-237. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787 +P38859 UniProtKB Mutagenesis 17 17 . . . Note=Mimics phosphorylation%3B restores nuclear localization and recruitment at double-strand. break (DSB) sites following DNA damage%3B when associated with D-237. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787 +P38859 UniProtKB Mutagenesis 237 237 . . . Note=Abolishes phosphorylation by CDK1%2C leading to a poor recruitment at double-strand. break (DSB) sites following DNA damage%3B when associated with A-4 and A-17. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787 +P38859 UniProtKB Mutagenesis 237 237 . . . Note=Mimics phosphorylation%3B restores nuclear localization and recruitment at double-strand. break (DSB) sites following DNA damage%3B when associated with D-17. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787 +P38859 UniProtKB Mutagenesis 504 504 . . . Note=In dna2-1%3B temperature-sensitive mutant unable to grow at 37 degrees Celsius%2C probably due to abolition of iron-sulfur-binding. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22684504;Dbxref=PMID:22684504 +P38859 UniProtKB Mutagenesis 519 519 . . . Note=Abolishes iron-sulfur-binding%3B when associated with A-768%3B A-771 and A-777. Impaired nuclease and ATPase activities%3B when associated with A-768. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22684504;Dbxref=PMID:22684504 +P38859 UniProtKB Mutagenesis 675 675 . . . Note=Nuclease dead mutant. No helicase activity when the 5'-end of the substrate is blocked. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20929864;Dbxref=PMID:20929864 +P38859 UniProtKB Mutagenesis 677 677 . . . Note=Nuclease dead mutant. No helicase activity when the 5'-end of the substrate is blocked. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20929864;Dbxref=PMID:20929864 +P38859 UniProtKB Mutagenesis 768 768 . . . Note=Abolishes iron-sulfur-binding%3B when associated with A-519%3B A-771 and A-777. Impaired nuclease and ATPase activities%3B when associated with A-519. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22684504;Dbxref=PMID:22684504 +P38859 UniProtKB Mutagenesis 771 771 . . . Note=Abolishes iron-sulfur-binding%3B when associated with A-519%3B A-768 and A-777. Impaired nuclease and ATPase activities%3B when associated with A-777. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22684504;Dbxref=PMID:22684504 +P38859 UniProtKB Mutagenesis 777 777 . . . Note=Abolishes iron-sulfur-binding%3B when associated with A-519%3B A-768 and A-771. Impaired nuclease and ATPase activities%3B when associated with A-771. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22684504;Dbxref=PMID:22684504 +P38859 UniProtKB Helix 212 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HOG +##sequence-region P53871 1 357 +P53871 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53871 UniProtKB Chain 2 357 . . . ID=PRO_0000203401;Note=Probable glutamine amidotransferase DUG3 +P53871 UniProtKB Domain 2 260 . . . Note=Glutamine amidotransferase type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609 +P53871 UniProtKB Active site 2 2 . . . Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q04110 1 302 +Q04110 UniProtKB Chain 1 302 . . . ID=PRO_0000086912;Note=Protein ECM11 +##sequence-region Q06011 1 112 +Q06011 UniProtKB Chain 1 112 . . . ID=PRO_0000086915;Note=Protein ECM19 +Q06011 UniProtKB Transmembrane 35 57 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03214 1 1411 +Q03214 UniProtKB Chain 1 1411 . . . ID=PRO_0000200597;Note=Protein ECM5 +Q03214 UniProtKB Domain 118 159 . . . Note=JmjN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00537 +Q03214 UniProtKB Domain 185 279 . . . Note=ARID;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00355 +Q03214 UniProtKB Domain 476 695 . . . Note=JmjC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00538 +Q03214 UniProtKB Zinc finger 1238 1290 . . . Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 +##sequence-region P33412 1 323 +P33412 UniProtKB Chain 1 323 . . . ID=PRO_0000208465;Note=Ethanolamine-phosphate cytidylyltransferase +P33412 UniProtKB Sequence conflict 252 252 . . . Note=S->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40023 1 145 +P40023 UniProtKB Chain 1 145 . . . ID=PRO_0000202626;Note=Enhancer of mRNA-decapping protein 2 +##sequence-region P02994 1 458 +P02994 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26545399;Dbxref=PMID:26545399 +P02994 UniProtKB Chain 2 458 . . . ID=PRO_0000090973;Note=Elongation factor 1-alpha +P02994 UniProtKB Domain 5 240 . . . Note=tr-type G +P02994 UniProtKB Nucleotide binding 14 21 . . . Note=GTP +P02994 UniProtKB Nucleotide binding 91 95 . . . Note=GTP +P02994 UniProtKB Nucleotide binding 153 156 . . . Note=GTP +P02994 UniProtKB Region 14 21 . . . Note=G1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P02994 UniProtKB Region 70 74 . . . Note=G2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P02994 UniProtKB Region 91 94 . . . Note=G3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P02994 UniProtKB Region 153 156 . . . Note=G4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P02994 UniProtKB Region 192 194 . . . Note=G5;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P02994 UniProtKB Site 298 298 . . . Note=Not modified +P02994 UniProtKB Site 372 372 . . . Note=Not modified +P02994 UniProtKB Modified residue 2 2 . . . Note=N%2CN%2CN-trimethylglycine%3B by EFM7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26545399;Dbxref=PMID:26545399 +P02994 UniProtKB Modified residue 3 3 . . . Note=N6%2CN6-dimethyllysine%3B by EFM7%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26545399;Dbxref=PMID:26545399 +P02994 UniProtKB Modified residue 3 3 . . . Note=N6-methyllysine%3B by EFM7%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26545399;Dbxref=PMID:26545399 +P02994 UniProtKB Modified residue 18 18 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P02994 UniProtKB Modified residue 30 30 . . . Note=N6-methyllysine%3B by EFM1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22522802,ECO:0000269|PubMed:24517342,ECO:0000269|PubMed:8476932;Dbxref=PMID:22522802,PMID:24517342,PMID:8476932 +P02994 UniProtKB Modified residue 72 72 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P02994 UniProtKB Modified residue 79 79 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B by EFM5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22522802,ECO:0000269|PubMed:24517342,ECO:0000269|PubMed:25446118,ECO:0000269|PubMed:8476932;Dbxref=PMID:22522802,PMID:24517342,PMID:25446118,PMID:8476932 +P02994 UniProtKB Modified residue 82 82 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P02994 UniProtKB Modified residue 163 163 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P02994 UniProtKB Modified residue 259 259 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P02994 UniProtKB Modified residue 289 289 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P02994 UniProtKB Modified residue 316 316 . . . Note=N6%2CN6-dimethyllysine%3B by EFM4%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22522802,ECO:0000269|PubMed:24517342,ECO:0000269|PubMed:8476932;Dbxref=PMID:22522802,PMID:24517342,PMID:8476932 +P02994 UniProtKB Modified residue 316 316 . . . Note=N6-methyllysine%3B by EFM4%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24517342;Dbxref=PMID:24517342 +P02994 UniProtKB Modified residue 390 390 . . . Note=N6-methyllysine%3B by EFM6;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22522802,ECO:0000269|PubMed:24517342,ECO:0000269|PubMed:26115316,ECO:0000269|PubMed:8476932;Dbxref=PMID:22522802,PMID:24517342,PMID:26115316,PMID:8476932 +P02994 UniProtKB Modified residue 414 414 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P02994 UniProtKB Modified residue 430 430 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P02994 UniProtKB Modified residue 458 458 . . . Note=Lysine methyl ester;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10973948;Dbxref=PMID:10973948 +P02994 UniProtKB Cross-link 224 224 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P02994 UniProtKB Cross-link 242 242 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P02994 UniProtKB Cross-link 253 253 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P02994 UniProtKB Cross-link 271 271 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P02994 UniProtKB Cross-link 393 393 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P02994 UniProtKB Cross-link 437 437 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P02994 UniProtKB Mutagenesis 122 122 . . . Note=Reduces interaction with YEF3. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9990316;Dbxref=PMID:9990316 +P02994 UniProtKB Mutagenesis 153 153 . . . Note=Increases KM for GTP to 2.7 mM. N->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10514524,ECO:0000269|PubMed:9786872;Dbxref=PMID:10514524,PMID:9786872 +P02994 UniProtKB Mutagenesis 153 153 . . . Note=Increases KM for GTP to 6.0 mM and reduces translation fidelity. Increases Km for GTP to 10.3 mM and reduces translation fidelity%3B when associated with E-156. N->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10514524,ECO:0000269|PubMed:9786872;Dbxref=PMID:10514524,PMID:9786872 +P02994 UniProtKB Mutagenesis 156 156 . . . Note=Increases KM for GTP to 10.3 mM and reduces translation fidelity%3B when associated with T-152. D->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10514524,ECO:0000269|PubMed:15601860,ECO:0000269|PubMed:9786872;Dbxref=PMID:10514524,PMID:15601860,PMID:9786872 +P02994 UniProtKB Mutagenesis 156 156 . . . Note=Increases KM for GTP to 13.1 mM and reduces translation fidelity. Confers hyperresistance to canavanine. D->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10514524,ECO:0000269|PubMed:15601860,ECO:0000269|PubMed:9786872;Dbxref=PMID:10514524,PMID:15601860,PMID:9786872 +P02994 UniProtKB Mutagenesis 156 156 . . . Note=Increases KM for GTP to 4.2 mM. Preferres XTP over GTP as substrate. D->W;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10514524,ECO:0000269|PubMed:15601860,ECO:0000269|PubMed:9786872;Dbxref=PMID:10514524,PMID:15601860,PMID:9786872 +P02994 UniProtKB Mutagenesis 286 286 . . . Note=In TEF2-1%3B strongly reduces translation fidelity by increasing the frequency of frameshifting and amino acid misincorporation. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3066688;Dbxref=PMID:3066688 +P02994 UniProtKB Mutagenesis 317 317 . . . Note=In TEF2-2%3B strongly reduces translation fidelity by increasing the frequency of frameshifting and amino acid misincorporation. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3066688;Dbxref=PMID:3066688 +P02994 UniProtKB Sequence conflict 86 86 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02994 UniProtKB Beta strand 6 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Helix 20 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Helix 36 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Helix 46 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Helix 56 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 78 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 83 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Helix 98 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 110 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Helix 120 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Helix 132 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 147 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Helix 155 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Helix 162 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Helix 183 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Turn 193 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Turn 197 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 212 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 217 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Helix 226 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 239 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7C +P02994 UniProtKB Beta strand 245 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Turn 255 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 258 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 275 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Turn 280 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 283 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 295 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7C +P02994 UniProtKB Beta strand 305 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Turn 315 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 323 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 336 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 358 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 364 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Turn 379 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 384 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 397 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Turn 413 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Helix 417 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 420 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P02994 UniProtKB Beta strand 429 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +##sequence-region P25039 1 761 +P25039 UniProtKB Transit peptide 1 42 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03061 +P25039 UniProtKB Chain 43 761 . . . ID=PRO_0000007449;Note=Elongation factor G%2C mitochondrial +P25039 UniProtKB Domain 68 349 . . . Note=tr-type G +P25039 UniProtKB Nucleotide binding 77 84 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03061 +P25039 UniProtKB Nucleotide binding 148 152 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03061 +P25039 UniProtKB Nucleotide binding 202 205 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03061 +P25039 UniProtKB Sequence conflict 2 2 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25039 UniProtKB Sequence conflict 66 66 . . . Note=R->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25039 UniProtKB Sequence conflict 233 233 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25039 UniProtKB Sequence conflict 478 478 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25039 UniProtKB Sequence conflict 629 629 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38347 1 419 +P38347 UniProtKB Chain 1 419 . . . ID=PRO_0000202531;Note=Protein-lysine N-methyltransferase EFM2 +P38347 UniProtKB Region 261 263 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867 +P38347 UniProtKB Binding site 222 222 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867 +P38347 UniProtKB Binding site 290 290 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867 +P38347 UniProtKB Binding site 318 318 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867 +P38347 UniProtKB Binding site 340 340 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867 +##sequence-region P40516 1 257 +P40516 UniProtKB Chain 1 257 . . . ID=PRO_0000202983;Note=Protein-lysine N-methyltransferase EFM4 +P40516 UniProtKB Sequence conflict 104 104 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53970 1 246 +P53970 UniProtKB Chain 1 246 . . . ID=PRO_0000203460;Note=Protein-lysine N-methyltransferase EFM6 +P53970 UniProtKB Region 87 89 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9H867,ECO:0000255|HAMAP-Rule:MF_03198 +P53970 UniProtKB Binding site 51 51 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9H867,ECO:0000255|HAMAP-Rule:MF_03198 +P53970 UniProtKB Binding site 115 115 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9H867,ECO:0000255|HAMAP-Rule:MF_03198 +P53970 UniProtKB Binding site 143 143 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9H867,ECO:0000255|HAMAP-Rule:MF_03198 +P53970 UniProtKB Binding site 169 169 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q9H867,ECO:0000255|HAMAP-Rule:MF_03198 +##sequence-region Q03653 1 782 +Q03653 UniProtKB Chain 1 782 . . . ID=PRO_0000203332;Note=Protein EFR3 +Q03653 UniProtKB Modified residue 227 227 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q03653 UniProtKB Modified residue 231 231 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q03653 UniProtKB Modified residue 564 564 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03653 UniProtKB Modified residue 625 625 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03653 UniProtKB Modified residue 632 632 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03653 UniProtKB Modified residue 643 643 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q03653 UniProtKB Modified residue 675 675 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q03653 UniProtKB Modified residue 687 687 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q03653 UniProtKB Modified residue 690 690 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q03653 UniProtKB Modified residue 735 735 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q03653 UniProtKB Modified residue 771 771 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q03653 UniProtKB Modified residue 774 774 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03653 UniProtKB Helix 12 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 33 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 47 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 70 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 88 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 95 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Turn 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 115 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 134 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 141 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Turn 159 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 165 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Turn 185 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 188 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Turn 201 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 207 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Beta strand 236 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 246 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 260 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 280 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 292 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 296 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Beta strand 311 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 315 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 337 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 355 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 377 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 396 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 420 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 431 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 434 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 448 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 464 477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 479 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 499 512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 515 526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 533 537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Turn 543 545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +Q03653 UniProtKB Helix 549 557 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N5A +##sequence-region P09032 1 578 +P09032 UniProtKB Chain 1 578 . . . ID=PRO_0000156083;Note=Translation initiation factor eIF-2B subunit gamma +P09032 UniProtKB Modified residue 296 296 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P09032 UniProtKB Modified residue 300 300 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P09032 UniProtKB Modified residue 306 306 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P09032 UniProtKB Sequence conflict 217 240 . . . Note=QKQQQFFTVYSENEDSERQPILLD->AKNNSNFSLFIQKTKTQRGSQYFWN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09032 UniProtKB Sequence conflict 491 492 . . . Note=IG->SV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q05610 1 365 +Q05610 UniProtKB Chain 1 365 . . . ID=PRO_0000079977;Note=Donuts protein 1 +Q05610 UniProtKB Domain 82 125 . . . Note=CUE;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00468 +Q05610 UniProtKB Compositional bias 286 292 . . . Note=Poly-Glu +Q05610 UniProtKB Sequence conflict 327 327 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32461 1 534 +P32461 UniProtKB Chain 1 534 . . . ID=PRO_0000083394;Note=2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 +##sequence-region P38121 1 705 +P38121 UniProtKB Chain 1 705 . . . ID=PRO_0000194041;Note=DNA polymerase alpha subunit B +P38121 UniProtKB Compositional bias 80 83 . . . Note=Poly-Ser +P38121 UniProtKB Modified residue 126 126 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38121 UniProtKB Helix 254 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Helix 280 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 294 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 315 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Helix 322 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 329 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 340 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 347 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 355 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 360 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 375 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Helix 378 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 393 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Helix 411 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 427 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 435 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Helix 441 445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Helix 461 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Helix 470 473 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 480 485 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 497 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Turn 505 509 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Turn 512 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 515 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 520 526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 529 533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Helix 538 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 545 547 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Helix 549 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Helix 556 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Helix 614 620 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Helix 623 625 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 629 632 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 640 644 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 647 651 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 664 670 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 675 678 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 680 683 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 685 687 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 689 691 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Helix 694 697 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P38121 UniProtKB Beta strand 698 704 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +##sequence-region P13382 1 1468 +P13382 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P13382 UniProtKB Chain 2 1468 . . . ID=PRO_0000046440;Note=DNA polymerase alpha catalytic subunit A +P13382 UniProtKB Zinc finger 1287 1317 . . . Note=CysA-type +P13382 UniProtKB Region 1246 1381 . . . Note=DNA-binding region;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13382 UniProtKB Motif 1348 1372 . . . Note=CysB motif +P13382 UniProtKB Metal binding 1287 1287 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13382 UniProtKB Metal binding 1290 1290 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13382 UniProtKB Metal binding 1314 1314 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13382 UniProtKB Metal binding 1317 1317 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13382 UniProtKB Metal binding 1348 1348 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13382 UniProtKB Metal binding 1353 1353 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13382 UniProtKB Metal binding 1367 1367 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13382 UniProtKB Metal binding 1372 1372 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13382 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P13382 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P13382 UniProtKB Modified residue 82 82 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13382 UniProtKB Modified residue 83 83 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13382 UniProtKB Modified residue 84 84 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13382 UniProtKB Modified residue 169 169 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13382 UniProtKB Modified residue 170 170 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P13382 UniProtKB Modified residue 172 172 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13382 UniProtKB Modified residue 240 240 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P13382 UniProtKB Modified residue 274 274 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P13382 UniProtKB Modified residue 309 309 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13382 UniProtKB Modified residue 313 313 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P13382 UniProtKB Natural variant 493 493 . . . Note=In temperature sensitive mutant. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3287376;Dbxref=PMID:3287376 +P13382 UniProtKB Mutagenesis 236 236 . . . Note=Increase in length of X' and Y' telomeres. No effect on telomere position effect. Reduced interaction with CDC13. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792 +P13382 UniProtKB Mutagenesis 238 238 . . . Note=Increase in length of X' and Y' telomeres. Reduced interaction with CDC13. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792 +P13382 UniProtKB Mutagenesis 241 241 . . . Note=Increase in length of X' and Y' telomeres. Reduced interaction with CDC13. P->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10898792;Dbxref=PMID:10898792 +P13382 UniProtKB Sequence conflict 759 760 . . . Note=MI->IV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13382 UniProtKB Helix 141 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C93 +P13382 UniProtKB Helix 217 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIQ +P13382 UniProtKB Beta strand 351 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 365 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 379 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 390 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 403 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 425 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 441 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 469 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 481 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 496 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 503 506 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 511 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 522 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 525 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 536 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Turn 549 552 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 553 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 569 571 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B08 +P13382 UniProtKB Beta strand 580 586 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 589 593 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 598 605 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 606 612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 616 630 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 633 639 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Turn 640 643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 644 654 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 660 663 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 664 666 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Turn 673 676 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FXD +P13382 UniProtKB Helix 682 691 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 694 698 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 702 706 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 716 724 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 739 742 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 744 767 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 770 781 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 785 790 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 794 807 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 854 856 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 860 864 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 868 875 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Turn 880 882 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 905 926 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 930 947 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 948 950 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 951 955 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 964 987 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 991 995 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 997 1003 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 1009 1026 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 1033 1045 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 1048 1054 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 1064 1071 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 1072 1074 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FXD +P13382 UniProtKB Helix 1080 1093 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 1094 1097 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 1101 1118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 1124 1127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 1129 1132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 1137 1139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 1143 1145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 1147 1158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 1167 1173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Turn 1189 1192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Beta strand 1193 1195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 1196 1200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 1202 1204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 1210 1215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Turn 1216 1218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Helix 1219 1225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FVM +P13382 UniProtKB Turn 1226 1228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FXD +P13382 UniProtKB Helix 1234 1239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FXD +P13382 UniProtKB Turn 1274 1279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P13382 UniProtKB Beta strand 1283 1286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P13382 UniProtKB Turn 1288 1290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P13382 UniProtKB Beta strand 1293 1296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P13382 UniProtKB Beta strand 1298 1300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P13382 UniProtKB Beta strand 1303 1308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P13382 UniProtKB Beta strand 1311 1314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P13382 UniProtKB Turn 1315 1317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P13382 UniProtKB Helix 1323 1343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P13382 UniProtKB Beta strand 1346 1349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P13382 UniProtKB Turn 1351 1353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P13382 UniProtKB Beta strand 1356 1358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P13382 UniProtKB Beta strand 1375 1380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P13382 UniProtKB Helix 1382 1395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P13382 UniProtKB Helix 1398 1402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P13382 UniProtKB Helix 1424 1433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +P13382 UniProtKB Helix 1435 1449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FLO +##sequence-region Q05521 1 289 +Q05521 UniProtKB Chain 1 289 . . . ID=PRO_0000220918;Note=Diacylglycerol pyrophosphate phosphatase 1 +Q05521 UniProtKB Topological domain 1 21 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05521 UniProtKB Transmembrane 22 42 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05521 UniProtKB Topological domain 43 65 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05521 UniProtKB Transmembrane 66 86 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05521 UniProtKB Topological domain 87 92 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05521 UniProtKB Transmembrane 93 113 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05521 UniProtKB Topological domain 114 172 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05521 UniProtKB Transmembrane 173 193 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05521 UniProtKB Transmembrane 194 214 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05521 UniProtKB Topological domain 215 222 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05521 UniProtKB Transmembrane 223 243 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05521 UniProtKB Topological domain 244 289 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05521 UniProtKB Region 118 126 . . . Note=Phosphatase sequence motif I +Q05521 UniProtKB Region 166 169 . . . Note=Phosphatase sequence motif II +Q05521 UniProtKB Region 216 227 . . . Note=Phosphatase sequence motif III +Q05521 UniProtKB Modified residue 285 285 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +Q05521 UniProtKB Mutagenesis 125 125 . . . Note=Complete loss of DGPP phosphatase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10545184;Dbxref=PMID:10545184 +Q05521 UniProtKB Mutagenesis 169 169 . . . Note=91%25 decrease of DGPP phosphatase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10545184;Dbxref=PMID:10545184 +Q05521 UniProtKB Mutagenesis 223 223 . . . Note=Complete loss of DGPP phosphatase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10545184;Dbxref=PMID:10545184 +##sequence-region Q08729 1 430 +Q08729 UniProtKB Chain 1 430 . . . ID=PRO_0000233007;Note=Protein DSE3 +Q08729 UniProtKB Modified residue 395 395 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P48510 1 373 +P48510 UniProtKB Chain 1 373 . . . ID=PRO_0000114900;Note=Ubiquitin domain-containing protein DSK2 +P48510 UniProtKB Domain 1 76 . . . Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 +P48510 UniProtKB Domain 327 371 . . . Note=UBA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212 +P48510 UniProtKB Cross-link 13 13 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P48510 UniProtKB Cross-link 76 76 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P48510 UniProtKB Sequence conflict 109 109 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P48510 UniProtKB Sequence conflict 296 296 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P48510 UniProtKB Beta strand 1 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BWF +P48510 UniProtKB Beta strand 12 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BWF +P48510 UniProtKB Helix 24 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BWF +P48510 UniProtKB Helix 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BWF +P48510 UniProtKB Beta strand 42 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BWF +P48510 UniProtKB Helix 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BWF +P48510 UniProtKB Beta strand 67 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BWF +P48510 UniProtKB Helix 328 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UN2 +P48510 UniProtKB Helix 333 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UN2 +P48510 UniProtKB Helix 347 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UN2 +P48510 UniProtKB Helix 361 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UN2 +##sequence-region P40568 1 576 +P40568 UniProtKB Chain 1 576 . . . ID=PRO_0000080024;Note=Kinetochore-associated protein DSN1 +P40568 UniProtKB Modified residue 250 250 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40568 UniProtKB Helix 561 570 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J +##sequence-region P33413 1 735 +P33413 UniProtKB Chain 1 735 . . . ID=PRO_0000105397;Note=Urea active transporter +P33413 UniProtKB Topological domain 1 14 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Transmembrane 15 35 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Topological domain 36 85 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Transmembrane 86 106 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Topological domain 107 130 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Transmembrane 131 151 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Topological domain 152 166 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Transmembrane 167 187 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Topological domain 188 189 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Transmembrane 190 210 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Topological domain 211 253 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Transmembrane 254 274 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Topological domain 275 295 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Transmembrane 296 316 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Topological domain 317 343 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Transmembrane 344 364 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Topological domain 365 403 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Transmembrane 404 424 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Topological domain 425 425 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Transmembrane 426 446 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Topological domain 447 454 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Transmembrane 455 475 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Topological domain 476 496 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Transmembrane 497 517 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Topological domain 518 618 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Transmembrane 619 639 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Topological domain 640 650 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Transmembrane 651 671 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Topological domain 672 735 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33413 UniProtKB Sequence conflict 58 63 . . . Note=GLVAAA->RLSGCS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06063 1 367 +Q06063 UniProtKB Chain 1 367 . . . ID=PRO_0000162156;Note=tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+] +Q06063 UniProtKB Nucleotide binding 45 47 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +Q06063 UniProtKB Nucleotide binding 231 233 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +Q06063 UniProtKB Nucleotide binding 255 256 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +Q06063 UniProtKB Active site 128 128 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +Q06063 UniProtKB Binding site 99 99 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +Q06063 UniProtKB Binding site 169 169 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +Q06063 UniProtKB Binding site 197 197 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +##sequence-region P47128 1 113 +P47128 UniProtKB Chain 1 113 . . . ID=PRO_0000086901;Note=Chromatin modification-related protein EAF6 +P47128 UniProtKB Coiled coil 1 43 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47128 UniProtKB Helix 2 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P47128 UniProtKB Helix 8 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P47128 UniProtKB Turn 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P47128 UniProtKB Helix 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P47128 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P47128 UniProtKB Helix 100 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +##sequence-region P36049 1 427 +P36049 UniProtKB Chain 1 427 . . . ID=PRO_0000120000;Note=rRNA-processing protein EBP2 +P36049 UniProtKB Coiled coil 45 174 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36049 UniProtKB Coiled coil 234 265 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36049 UniProtKB Coiled coil 291 348 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36049 UniProtKB Modified residue 104 104 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P36049 UniProtKB Modified residue 177 177 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P36049 UniProtKB Modified residue 183 183 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P36049 UniProtKB Mutagenesis 36 37 . . . Note=Reduces sumoylation and impairs interaction with SIZ2%2C WSS1 and ULS1%2C when associated with R-61 and R-62. KK->RR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18603780;Dbxref=PMID:18603780 +P36049 UniProtKB Mutagenesis 61 62 . . . Note=Reduces sumoylation and impairs interaction with SIZ2%2C WSS1 and ULS1%2C when associated with R-36 and R-37. KK->RR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18603780;Dbxref=PMID:18603780 +##sequence-region P48235 1 211 +P48235 UniProtKB Chain 1 211 . . . ID=PRO_0000202828;Note=Extender of the chronological lifespan protein 1 +##sequence-region Q04623 1 453 +Q04623 UniProtKB Chain 1 453 . . . ID=PRO_0000086914;Note=Protein ECM18 +Q04623 UniProtKB Domain 130 435 . . . Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04623 UniProtKB Motif 428 433 . . . Note=HXXXXD motif;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P32525 1 599 +P32525 UniProtKB Chain 1 599 . . . ID=PRO_0000086918;Note=Protein ECM25 +P32525 UniProtKB Domain 181 359 . . . Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172 +P32525 UniProtKB Compositional bias 363 493 . . . Note=Ser-rich +##sequence-region Q99252 1 613 +Q99252 UniProtKB Chain 1 613 . . . ID=PRO_0000086921;Note=Protein ECM3 +Q99252 UniProtKB Transmembrane 10 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99252 UniProtKB Transmembrane 74 94 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99252 UniProtKB Transmembrane 106 126 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99252 UniProtKB Transmembrane 143 163 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99252 UniProtKB Transmembrane 432 452 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99252 UniProtKB Transmembrane 471 491 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99252 UniProtKB Transmembrane 546 566 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99252 UniProtKB Transmembrane 587 607 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99252 UniProtKB Compositional bias 199 203 . . . Note=Poly-Ser +Q99252 UniProtKB Modified residue 291 291 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q99252 UniProtKB Modified residue 338 338 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q3E705 1 233 +Q3E705 UniProtKB Chain 1 233 . . . ID=PRO_0000245390;Note=rRNA-processing protein EFG1 +Q3E705 UniProtKB Coiled coil 26 109 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E705 UniProtKB Sequence conflict 152 152 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53168 1 247 +P53168 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53168 UniProtKB Chain 2 247 . . . ID=PRO_0000215595;Note=DASH complex subunit DUO1 +P53168 UniProtKB Coiled coil 152 180 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53168 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53168 UniProtKB Mutagenesis 67 67 . . . Note=In DUO1-1%3B produces abnormal spindles resulting in growth arrest at 37 degrees Celsius%3B when associated with V-157. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9817759;Dbxref=PMID:9817759 +P53168 UniProtKB Mutagenesis 117 117 . . . Note=In DUO1-2%3B produces abnormal spindles resulting in growth arrest at 37 degrees Celsius%3B when associated with I-124. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9817759;Dbxref=PMID:9817759 +P53168 UniProtKB Mutagenesis 124 124 . . . Note=In DUO1-2%3B produces abnormal spindles resulting in growth arrest at 37 degrees Celsius%3B when associated with T-117. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9817759;Dbxref=PMID:9817759 +P53168 UniProtKB Mutagenesis 157 157 . . . Note=In DUO1-1%3B produces abnormal spindles resulting in growth arrest at 37 degrees Celsius%3B when associated with K-67. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9817759;Dbxref=PMID:9817759 +##sequence-region Q06053 1 668 +Q06053 UniProtKB Chain 1 668 . . . ID=PRO_0000162155;Note=tRNA-dihydrouridine(47) synthase [NAD(P)(+)] +Q06053 UniProtKB Zinc finger 92 122 . . . Note=C3H1-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 +Q06053 UniProtKB Zinc finger 134 164 . . . Note=C3H1-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 +Q06053 UniProtKB Nucleotide binding 299 301 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +Q06053 UniProtKB Nucleotide binding 509 511 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +Q06053 UniProtKB Nucleotide binding 534 535 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +Q06053 UniProtKB Active site 386 386 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +Q06053 UniProtKB Binding site 354 354 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +Q06053 UniProtKB Binding site 426 426 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +Q06053 UniProtKB Binding site 457 457 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +##sequence-region P36041 1 632 +P36041 UniProtKB Chain 1 632 . . . ID=PRO_0000203133;Note=Protein EAP1 +P36041 UniProtKB Nucleotide binding 440 447 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36041 UniProtKB Modified residue 30 30 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36041 UniProtKB Modified residue 281 281 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36041 UniProtKB Modified residue 282 282 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P36041 UniProtKB Modified residue 327 327 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P36041 UniProtKB Modified residue 344 344 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36041 UniProtKB Modified residue 387 387 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36041 UniProtKB Mutagenesis 109 109 . . . Note=Abolishes interaction with eIF4E%3B when associated with A-114. Y->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10848587,ECO:0000269|PubMed:15848184;Dbxref=PMID:10848587,PMID:15848184 +P36041 UniProtKB Mutagenesis 114 114 . . . Note=Abolishes interaction with eIF4E%3B when associated with A-109. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15848184;Dbxref=PMID:15848184 +##sequence-region P38195 1 257 +P38195 UniProtKB Chain 1 257 . . . ID=PRO_0000086913;Note=Protein ECM13 +P38195 UniProtKB Compositional bias 107 147 . . . Note=Asp-rich +##sequence-region P35195 1 104 +P35195 UniProtKB Chain 1 104 . . . ID=PRO_0000147621;Note=UPF0045 protein ECM15 +P35195 UniProtKB Beta strand 5 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LXJ +P35195 UniProtKB Helix 23 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LXJ +P35195 UniProtKB Beta strand 36 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LXJ +P35195 UniProtKB Beta strand 46 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LXJ +P35195 UniProtKB Helix 53 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LXJ +P35195 UniProtKB Beta strand 74 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LXJ +P35195 UniProtKB Helix 91 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LXJ +##sequence-region P47144 1 725 +P47144 UniProtKB Chain 1 725 . . . ID=PRO_0000209503;Note=Protein ECM27 +P47144 UniProtKB Transmembrane 21 41 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47144 UniProtKB Transmembrane 119 139 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47144 UniProtKB Transmembrane 157 177 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47144 UniProtKB Transmembrane 178 198 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47144 UniProtKB Transmembrane 397 417 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47144 UniProtKB Transmembrane 439 459 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47144 UniProtKB Transmembrane 470 490 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47144 UniProtKB Transmembrane 526 546 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47144 UniProtKB Transmembrane 559 579 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47144 UniProtKB Transmembrane 621 641 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47144 UniProtKB Transmembrane 668 688 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47144 UniProtKB Transmembrane 704 724 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47144 UniProtKB Sequence conflict 219 219 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02202 1 377 +Q02202 UniProtKB Chain 1 377 . . . ID=PRO_0000086925;Note=Protein ECM9 +##sequence-region P38073 1 919 +P38073 UniProtKB Chain 1 919 . . . ID=PRO_0000114991;Note=Transcriptional regulatory protein EDS1 +P38073 UniProtKB DNA binding 56 85 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +##sequence-region P42835 1 1041 +P42835 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Chain 21 1020 . . . ID=PRO_0000021159;Note=Protein EGT2 +P42835 UniProtKB Propeptide 1021 1041 . . . ID=PRO_0000372451;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Repeat 457 492 . . . Note=1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P42835 UniProtKB Repeat 577 606 . . . Note=2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P42835 UniProtKB Repeat 613 647 . . . Note=3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P42835 UniProtKB Repeat 716 745 . . . Note=4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P42835 UniProtKB Repeat 773 802 . . . Note=5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P42835 UniProtKB Repeat 811 840 . . . Note=6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P42835 UniProtKB Repeat 849 886 . . . Note=7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P42835 UniProtKB Repeat 887 924 . . . Note=8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P42835 UniProtKB Repeat 925 962 . . . Note=9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P42835 UniProtKB Region 457 962 . . . Note=9 X approximate repeats +P42835 UniProtKB Compositional bias 301 764 . . . Note=Ser-rich +P42835 UniProtKB Compositional bias 403 1003 . . . Note=Thr-rich +P42835 UniProtKB Lipidation 1020 1020 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 65 65 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 103 103 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 161 161 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 175 175 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 249 249 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 332 332 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 401 401 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 435 435 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 465 465 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 485 485 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 506 506 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 526 526 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 544 544 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 556 556 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 635 635 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 636 636 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 657 657 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 709 709 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Glycosylation 756 756 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42835 UniProtKB Sequence conflict 577 577 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P42835 UniProtKB Sequence conflict 577 577 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P42835 UniProtKB Sequence conflict 577 577 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47120 1 325 +P47120 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03101,ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P47120 UniProtKB Chain 2 325 . . . ID=PRO_0000203100;Note=Deoxyhypusine hydroxylase +P47120 UniProtKB Repeat 77 103 . . . Note=HEAT-like PBS-type 1 +P47120 UniProtKB Repeat 110 136 . . . Note=HEAT-like PBS-type 2 +P47120 UniProtKB Repeat 202 231 . . . Note=HEAT-like PBS-type 3 +P47120 UniProtKB Repeat 235 261 . . . Note=HEAT-like PBS-type 4 +P47120 UniProtKB Repeat 268 294 . . . Note=HEAT-like PBS-type 5 +P47120 UniProtKB Metal binding 79 79 . . . Note=Iron 1 +P47120 UniProtKB Metal binding 80 80 . . . Note=Iron 1 +P47120 UniProtKB Metal binding 112 112 . . . Note=Iron 1 +P47120 UniProtKB Metal binding 113 113 . . . Note=Iron 1 +P47120 UniProtKB Metal binding 237 237 . . . Note=Iron 2 +P47120 UniProtKB Metal binding 238 238 . . . Note=Iron 2 +P47120 UniProtKB Metal binding 270 270 . . . Note=Iron 2 +P47120 UniProtKB Metal binding 271 271 . . . Note=Iron 2 +P47120 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03101,ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P47120 UniProtKB Modified residue 126 126 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47120 UniProtKB Modified residue 187 187 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47120 UniProtKB Modified residue 281 281 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P47120 UniProtKB Mutagenesis 79 79 . . . Note=Abolishes both iron-binding and enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996 +P47120 UniProtKB Mutagenesis 80 80 . . . Note=Abolishes enzyme activity and impairs iron-binding. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996 +P47120 UniProtKB Mutagenesis 112 112 . . . Note=Abolishes both iron-binding and enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996 +P47120 UniProtKB Mutagenesis 113 113 . . . Note=Abolishes iron-binding%2C substrate-binding%2C and enzyme activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996 +P47120 UniProtKB Mutagenesis 116 116 . . . Note=Abolishes substrate-binding and enzyme activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996 +P47120 UniProtKB Mutagenesis 116 116 . . . Note=Reduces enzyme activity by 97%25. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996 +P47120 UniProtKB Mutagenesis 237 237 . . . Note=Abolishes both iron-binding and enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996 +P47120 UniProtKB Mutagenesis 238 238 . . . Note=Abolishes substrate-binding%2C enzyme activity%2C and impairs iron-binding. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996 +P47120 UniProtKB Mutagenesis 270 270 . . . Note=Abolishes iron-binding%2C substrate-binding%2C and enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996 +P47120 UniProtKB Mutagenesis 271 271 . . . Note=Abolishes iron-binding%2C substrate-binding%2C and enzyme activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996 +P47120 UniProtKB Mutagenesis 274 274 . . . Note=Abolishes substrate-binding. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19956996;Dbxref=PMID:19956996 +##sequence-region P27344 1 201 +P27344 UniProtKB Chain 1 201 . . . ID=PRO_0000208350;Note=DNA polymerase epsilon subunit C +P27344 UniProtKB Compositional bias 120 154 . . . Note=Asp/Glu-rich (acidic) +P27344 UniProtKB Modified residue 186 186 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P27344 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P27344 UniProtKB Modified residue 189 189 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P27344 UniProtKB Sequence conflict 196 196 . . . Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40487 1 425 +P40487 UniProtKB Chain 1 425 . . . ID=PRO_0000083381;Note=2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 +P40487 UniProtKB Modified residue 44 44 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region Q12429 1 685 +Q12429 UniProtKB Chain 1 685 . . . ID=PRO_0000262869;Note=Diphthine--ammonia ligase +Q12429 UniProtKB Mutagenesis 216 216 . . . Note=Completely inactivates the enzyme. G->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23468660;Dbxref=PMID:23468660 +Q12429 UniProtKB Mutagenesis 220 220 . . . Note=Completely inactivates the enzyme. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23468660;Dbxref=PMID:23468660 +##sequence-region Q08225 1 711 +Q08225 UniProtKB Chain 1 711 . . . ID=PRO_0000078243;Note=Probable dipeptidyl peptidase 3 +Q08225 UniProtKB Active site 461 461 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O55096 +Q08225 UniProtKB Metal binding 460 460 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NY33 +Q08225 UniProtKB Metal binding 465 465 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NY33 +Q08225 UniProtKB Metal binding 517 517 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NY33 +Q08225 UniProtKB Beta strand 12 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Turn 18 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 27 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 44 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 55 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Turn 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 78 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 99 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Turn 103 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 115 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 133 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 154 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Turn 160 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Turn 167 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 171 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 175 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 184 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 191 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 202 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 212 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 221 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Turn 236 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 242 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 252 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 261 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 281 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 299 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 316 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 327 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 336 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 346 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 359 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 366 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 370 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 384 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 397 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 405 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 414 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 419 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Turn 439 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 442 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 472 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 477 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 482 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 491 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 504 508 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 509 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 512 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 531 536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 542 562 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 563 566 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Turn 569 571 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 577 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 592 595 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 598 603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 610 614 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 616 618 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Turn 619 621 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 622 639 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 643 653 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 658 661 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 664 669 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 676 678 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 681 684 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Beta strand 690 693 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +Q08225 UniProtKB Helix 699 710 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CSK +##sequence-region P47013 1 409 +P47013 UniProtKB Chain 1 409 . . . ID=PRO_0000203037;Note=Dihydrosphingosine 1-phosphate phosphatase LCB3 +P47013 UniProtKB Topological domain 1 86 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P47013 UniProtKB Transmembrane 87 107 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47013 UniProtKB Topological domain 108 112 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P47013 UniProtKB Transmembrane 113 133 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47013 UniProtKB Topological domain 134 182 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P47013 UniProtKB Transmembrane 183 203 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47013 UniProtKB Topological domain 204 207 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P47013 UniProtKB Transmembrane 208 228 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47013 UniProtKB Topological domain 229 245 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P47013 UniProtKB Transmembrane 246 266 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47013 UniProtKB Topological domain 267 276 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P47013 UniProtKB Transmembrane 277 297 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47013 UniProtKB Topological domain 298 315 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P47013 UniProtKB Transmembrane 316 336 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47013 UniProtKB Topological domain 337 384 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P47013 UniProtKB Transmembrane 385 405 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47013 UniProtKB Topological domain 406 409 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +P47013 UniProtKB Region 128 136 . . . Note=Phosphatase sequence motif I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47013 UniProtKB Region 157 160 . . . Note=Phosphatase sequence motif II;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47013 UniProtKB Region 203 214 . . . Note=Phosphatase sequence motif III;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47013 UniProtKB Active site 160 160 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A924 +P47013 UniProtKB Active site 210 210 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A924 +P47013 UniProtKB Site 214 214 . . . Note=Stabilizes the active site histidine for nucleophilic attack;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A924 +P47013 UniProtKB Modified residue 16 16 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P47013 UniProtKB Modified residue 18 18 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P47013 UniProtKB Mutagenesis 128 128 . . . Note=Impairs dihydrosphingosine 1-phosphate phosphatase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12786943;Dbxref=PMID:12786943 +P47013 UniProtKB Mutagenesis 160 160 . . . Note=Impairs dihydrosphingosine 1-phosphate phosphatase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12786943;Dbxref=PMID:12786943 +P47013 UniProtKB Mutagenesis 210 210 . . . Note=Impairs dihydrosphingosine 1-phosphate phosphatase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12786943;Dbxref=PMID:12786943 +##sequence-region P38844 1 325 +P38844 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38844 UniProtKB Chain 22 308 . . . ID=PRO_0000014328;Note=Protein DSE2 +P38844 UniProtKB Propeptide 309 325 . . . ID=PRO_0000285355;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38844 UniProtKB Compositional bias 72 281 . . . Note=Ser-rich +P38844 UniProtKB Lipidation 308 308 . . . Note=GPI-anchor amidated aspartate;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39112 1 969 +P39112 UniProtKB Transit peptide 1 41 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12426313;Dbxref=PMID:12426313 +P39112 UniProtKB Chain 42 969 . . . ID=PRO_0000030820;Note=Exoribonuclease II%2C mitochondrial +P39112 UniProtKB Sequence conflict 222 222 . . . Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39112 UniProtKB Sequence conflict 870 870 . . . Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38125 1 572 +P38125 UniProtKB Chain 1 572 . . . ID=PRO_0000173438;Note=Dityrosine transporter 1 +P38125 UniProtKB Topological domain 1 110 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Transmembrane 111 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Topological domain 132 149 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Transmembrane 150 170 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Topological domain 171 184 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Transmembrane 185 205 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Topological domain 206 207 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Transmembrane 208 228 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Topological domain 229 240 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Transmembrane 241 261 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Topological domain 262 267 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Transmembrane 268 288 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Topological domain 289 366 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Transmembrane 367 387 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Topological domain 388 398 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Transmembrane 399 419 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Topological domain 420 446 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Transmembrane 447 469 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Topological domain 470 472 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Transmembrane 473 493 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Topological domain 494 520 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Transmembrane 521 541 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Topological domain 542 542 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Transmembrane 543 563 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Topological domain 564 572 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38125 UniProtKB Region 548 572 . . . Note=Required for the localization to the prospore membrane +##sequence-region P43616 1 481 +P43616 UniProtKB Chain 1 481 . . . ID=PRO_0000185275;Note=Cys-Gly metallodipeptidase DUG1 +P43616 UniProtKB Active site 104 104 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43616 UniProtKB Active site 171 171 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43616 UniProtKB Metal binding 102 102 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43616 UniProtKB Metal binding 137 137 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43616 UniProtKB Metal binding 137 137 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43616 UniProtKB Metal binding 172 172 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43616 UniProtKB Metal binding 200 200 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43616 UniProtKB Metal binding 450 450 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43616 UniProtKB Modified residue 451 451 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P43616 UniProtKB Helix 5 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Helix 16 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Helix 36 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Helix 39 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 59 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 83 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 96 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Helix 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Turn 125 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 129 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Turn 133 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Helix 139 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 161 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Helix 171 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Turn 174 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Helix 178 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Turn 186 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 195 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 204 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 210 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 217 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 228 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Turn 234 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Turn 238 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Helix 244 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Helix 267 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Helix 276 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Turn 282 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Helix 289 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Helix 306 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 318 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 330 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 339 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Helix 355 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 376 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Helix 397 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 415 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Helix 426 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 437 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 451 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Beta strand 455 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +P43616 UniProtKB Helix 458 477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G1P +##sequence-region P32528 1 1835 +P32528 UniProtKB Chain 1 1835 . . . ID=PRO_0000146832;Note=Urea amidolyase +P32528 UniProtKB Domain 632 1075 . . . Note=Biotin carboxylation +P32528 UniProtKB Domain 751 948 . . . Note=ATP-grasp;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 +P32528 UniProtKB Domain 1754 1832 . . . Note=Biotinyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066 +P32528 UniProtKB Nucleotide binding 122 129 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 +P32528 UniProtKB Binding site 747 747 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32528 UniProtKB Binding site 830 830 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32528 UniProtKB Binding site 865 865 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32528 UniProtKB Modified residue 803 803 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32528 UniProtKB Modified residue 1798 1798 . . . Note=N6-biotinyllysine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250,ECO:0000255|PROSITE-ProRule:PRU01066 +P32528 UniProtKB Sequence conflict 96 96 . . . Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32528 UniProtKB Sequence conflict 256 258 . . . Note=LKK->KKN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32528 UniProtKB Sequence conflict 459 459 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32528 UniProtKB Sequence conflict 830 830 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32528 UniProtKB Sequence conflict 1395 1395 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P33317 1 147 +P33317 UniProtKB Chain 1 147 . . . ID=PRO_0000182937;Note=Deoxyuridine 5'-triphosphate nucleotidohydrolase +P33317 UniProtKB Region 68 70 . . . Note=Substrate binding +P33317 UniProtKB Region 82 85 . . . Note=Substrate binding +P33317 UniProtKB Region 142 143 . . . Note=Substrate binding +P33317 UniProtKB Binding site 93 93 . . . Note=Substrate%3B via amide nitrogen and carbonyl oxygen +P33317 UniProtKB Binding site 137 137 . . . Note=Substrate +P33317 UniProtKB Sequence conflict 10 10 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33317 UniProtKB Beta strand 8 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48 +P33317 UniProtKB Beta strand 22 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48 +P33317 UniProtKB Beta strand 29 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48 +P33317 UniProtKB Beta strand 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48 +P33317 UniProtKB Beta strand 45 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48 +P33317 UniProtKB Beta strand 53 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48 +P33317 UniProtKB Beta strand 61 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48 +P33317 UniProtKB Helix 69 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48 +P33317 UniProtKB Beta strand 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48 +P33317 UniProtKB Beta strand 93 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48 +P33317 UniProtKB Beta strand 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48 +P33317 UniProtKB Beta strand 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48 +P33317 UniProtKB Beta strand 111 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48 +P33317 UniProtKB Beta strand 125 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P48 +P33317 UniProtKB Beta strand 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F4F +##sequence-region P36022 1 4092 +P36022 UniProtKB Chain 1 4092 . . . ID=PRO_0000114643;Note=Dynein heavy chain%2C cytoplasmic +P36022 UniProtKB Nucleotide binding 1796 1803 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36022 UniProtKB Nucleotide binding 2074 2081 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36022 UniProtKB Nucleotide binding 2418 2425 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36022 UniProtKB Nucleotide binding 2760 2767 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36022 UniProtKB Region 1 1757 . . . Note=Stem;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36022 UniProtKB Region 1758 1979 . . . Note=AAA 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36022 UniProtKB Region 2036 2273 . . . Note=AAA 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36022 UniProtKB Region 2379 2628 . . . Note=AAA 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36022 UniProtKB Region 2722 2984 . . . Note=AAA 4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36022 UniProtKB Region 2993 3300 . . . Note=Stalk;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36022 UniProtKB Region 3370 3599 . . . Note=AAA 5;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36022 UniProtKB Region 3760 3970 . . . Note=AAA 6;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36022 UniProtKB Coiled coil 154 175 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36022 UniProtKB Coiled coil 486 508 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36022 UniProtKB Coiled coil 542 566 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36022 UniProtKB Coiled coil 932 959 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36022 UniProtKB Coiled coil 1042 1063 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36022 UniProtKB Coiled coil 1681 1705 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36022 UniProtKB Coiled coil 2993 3092 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36022 UniProtKB Coiled coil 3242 3300 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36022 UniProtKB Coiled coil 3532 3608 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36022 UniProtKB Sequence conflict 589 589 . . . Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36022 UniProtKB Sequence conflict 601 601 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36022 UniProtKB Sequence conflict 1364 1364 . . . Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36022 UniProtKB Sequence conflict 2118 2119 . . . Note=ML->IV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36022 UniProtKB Helix 1366 1378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 1384 1387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 1389 1391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 1393 1396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1399 1414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 1420 1424 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1425 1458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1464 1468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1470 1491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1497 1501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1505 1533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1537 1540 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1542 1550 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 1551 1554 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1556 1558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1559 1565 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 1567 1574 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 1576 1584 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 1589 1597 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1604 1631 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1636 1640 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1645 1666 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1669 1688 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1692 1717 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1721 1730 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 1733 1736 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1743 1745 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 1747 1751 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 1754 1757 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1773 1787 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 1791 1795 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1802 1811 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 1812 1814 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 1818 1821 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1828 1841 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 1844 1849 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1855 1874 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 1877 1880 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 1882 1887 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 1893 1898 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 1902 1905 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1910 1913 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 1916 1920 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1926 1938 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1942 1959 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1970 1986 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 1991 2001 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2003 2005 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2008 2021 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2029 2032 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2033 2045 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2051 2066 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2068 2073 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2080 2094 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2098 2104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 2106 2108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2111 2114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 2120 2122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2130 2138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2146 2154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2160 2164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2167 2170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2175 2177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2179 2181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2183 2185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2188 2197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2204 2209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2210 2214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2222 2238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2243 2256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2259 2270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2280 2297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2300 2302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2303 2305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AI6 +P36022 UniProtKB Helix 2307 2327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2333 2345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2348 2350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2363 2365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2383 2385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2395 2410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2413 2417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2424 2433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2439 2444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2451 2461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2465 2467 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 2468 2470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2471 2480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2482 2487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 2488 2490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2496 2498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2501 2511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2513 2516 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 2518 2520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2523 2535 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2548 2551 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2554 2558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 2563 2565 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2566 2578 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2583 2588 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2589 2606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 2609 2611 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2619 2634 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2641 2656 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 2657 2659 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2664 2680 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 2691 2693 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2696 2703 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2709 2726 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2736 2750 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2751 2759 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 2761 2763 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2766 2776 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2780 2782 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2792 2808 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2813 2818 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 2819 2821 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2825 2836 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2837 2839 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 2841 2843 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2847 2863 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2870 2884 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2886 2892 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2897 2904 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2906 2911 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2912 2916 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2922 2932 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2961 2979 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 2983 2985 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 2991 3027 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3300 3304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 3305 3307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3308 3333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 3334 3336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AI6 +P36022 UniProtKB Helix 3339 3355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3366 3370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3373 3382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3388 3399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 3402 3408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3414 3422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3423 3425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 3426 3429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3436 3445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 3449 3453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 3455 3457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3463 3466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 3477 3480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 3482 3487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 3493 3498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3507 3512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 3513 3517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3523 3537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3539 3572 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 3573 3576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3580 3638 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3646 3655 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3670 3686 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3692 3710 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3713 3726 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 3727 3729 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 3738 3740 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3743 3752 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3756 3765 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3774 3780 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 3784 3790 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3797 3805 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 3806 3808 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 3813 3815 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3819 3835 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 3839 3842 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3844 3847 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3848 3853 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3855 3861 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 3865 3867 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 3868 3870 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AI6 +P36022 UniProtKB Beta strand 3873 3876 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 3879 3881 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3886 3891 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 3892 3897 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3903 3913 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3914 3917 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3923 3944 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 3946 3949 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 3950 3952 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3958 3974 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3980 3982 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 3983 3991 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Turn 3995 3997 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 4001 4014 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 4018 4020 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 4023 4026 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 4038 4051 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 4058 4061 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Beta strand 4063 4065 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +P36022 UniProtKB Helix 4067 4090 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AKG +##sequence-region P53759 1 423 +P53759 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53759 UniProtKB Chain 2 423 . . . ID=PRO_0000162153;Note=tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)] +P53759 UniProtKB Nucleotide binding 35 37 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +P53759 UniProtKB Nucleotide binding 223 225 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +P53759 UniProtKB Nucleotide binding 247 248 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +P53759 UniProtKB Active site 121 121 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +P53759 UniProtKB Binding site 92 92 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +P53759 UniProtKB Binding site 160 160 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +P53759 UniProtKB Binding site 188 188 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SMC7 +P53759 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region Q06349 1 442 +Q06349 UniProtKB Chain 1 442 . . . ID=PRO_0000253847;Note=Decapping and exoribonuclease protein 1 +Q06349 UniProtKB Compositional bias 41 46 . . . Note=Poly-Ser +Q06349 UniProtKB Metal binding 255 255 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06349 UniProtKB Metal binding 295 295 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06349 UniProtKB Metal binding 306 306 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53063 1 387 +P53063 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10805743;Dbxref=PMID:10805743 +P53063 UniProtKB Chain 2 387 . . . ID=PRO_0000202708;Note=Decapping nuclease RAI1 +P53063 UniProtKB Region 273 387 . . . Note=Interaction with RAT1 +P53063 UniProtKB Metal binding 172 172 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53063 UniProtKB Metal binding 223 223 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53063 UniProtKB Metal binding 241 241 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53063 UniProtKB Metal binding 242 242 . . . Note=Divalent metal cation%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53063 UniProtKB Binding site 105 105 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53063 UniProtKB Binding site 221 221 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53063 UniProtKB Binding site 267 267 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53063 UniProtKB Modified residue 198 198 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53063 UniProtKB Mutagenesis 221 221 . . . Note=Abolishes the decapping activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20802481;Dbxref=PMID:20802481 +P53063 UniProtKB Mutagenesis 223 223 . . . Note=Abolishes the decapping activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20802481;Dbxref=PMID:20802481 +P53063 UniProtKB Sequence conflict 8 8 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06337 1 982 +Q06337 UniProtKB Chain 1 982 . . . ID=PRO_0000065825;Note=Chromatin modification-related protein EAF1 +Q06337 UniProtKB Domain 346 425 . . . Note=HSA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00549 +Q06337 UniProtKB Domain 642 704 . . . Note=Myb-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00133 +Q06337 UniProtKB Compositional bias 825 942 . . . Note=Gln-rich +Q06337 UniProtKB Modified residue 841 841 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06337 UniProtKB Modified residue 971 971 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P39995 1 279 +P39995 UniProtKB Chain 1 279 . . . ID=PRO_0000086892;Note=Chromatin modification-related protein EAF5 +##sequence-region P53911 1 425 +P53911 UniProtKB Chain 1 425 . . . ID=PRO_0000215882;Note=Chromatin modification-related protein EAF7 +P53911 UniProtKB Coiled coil 209 310 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53911 UniProtKB Modified residue 200 200 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53911 UniProtKB Modified residue 225 225 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region Q03212 1 550 +Q03212 UniProtKB Chain 1 550 . . . ID=PRO_0000203316;Note=Protein EAR1 +Q03212 UniProtKB Topological domain 1 45 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03212 UniProtKB Transmembrane 46 66 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03212 UniProtKB Topological domain 67 550 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03212 UniProtKB Domain 172 375 . . . Note=B30.2/SPRY;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00548 +Q03212 UniProtKB Modified residue 519 519 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03212 UniProtKB Modified residue 538 538 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03212 UniProtKB Glycosylation 110 110 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03212 UniProtKB Glycosylation 203 203 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03212 UniProtKB Glycosylation 210 210 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03212 UniProtKB Glycosylation 256 256 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03212 UniProtKB Glycosylation 295 295 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q05871 1 280 +Q05871 UniProtKB Chain 1 280 . . . ID=PRO_0000109263;Note=3%2C2-trans-enoyl-CoA isomerase +Q05871 UniProtKB Region 68 72 . . . Note=Substrate binding;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4ZDB,ECO:0000244|PDB:4ZDC,ECO:0000269|PubMed:26527136;Dbxref=PMID:26527136 +Q05871 UniProtKB Motif 278 280 . . . Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05871 UniProtKB Active site 158 158 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26527136;Dbxref=PMID:26527136 +Q05871 UniProtKB Binding site 126 126 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4ZDC,ECO:0000269|PubMed:26527136;Dbxref=PMID:26527136 +Q05871 UniProtKB Mutagenesis 158 158 . . . Note=Loss of activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11399063;Dbxref=PMID:11399063 +Q05871 UniProtKB Beta strand 11 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Beta strand 19 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Helix 27 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Helix 35 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Beta strand 56 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Beta strand 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Helix 73 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Turn 77 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K39 +Q05871 UniProtKB Beta strand 82 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDB +Q05871 UniProtKB Helix 89 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Helix 98 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Beta strand 113 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Helix 125 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Beta strand 134 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Beta strand 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Helix 150 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Helix 161 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Helix 171 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Helix 186 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Beta strand 196 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Helix 206 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Turn 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Helix 226 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Turn 238 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Helix 241 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +Q05871 UniProtKB Turn 263 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZDF +##sequence-region P38167 1 1117 +P38167 UniProtKB Chain 1 1117 . . . ID=PRO_0000086917;Note=Protein ECM21 +P38167 UniProtKB Compositional bias 490 511 . . . Note=Ser-rich +P38167 UniProtKB Modified residue 18 18 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38167 UniProtKB Modified residue 115 115 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38167 UniProtKB Modified residue 140 140 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P38167 UniProtKB Modified residue 286 286 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38167 UniProtKB Modified residue 527 527 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38167 UniProtKB Modified residue 550 550 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38167 UniProtKB Modified residue 775 775 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38167 UniProtKB Modified residue 1035 1035 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38167 UniProtKB Cross-link 191 191 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38167 UniProtKB Cross-link 577 577 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12872131,ECO:0000269|PubMed:14557538;Dbxref=PMID:12872131,PMID:14557538 +P38167 UniProtKB Cross-link 651 651 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P38167 UniProtKB Cross-link 712 712 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P38167 UniProtKB Cross-link 794 794 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38167 UniProtKB Cross-link 807 807 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P38167 UniProtKB Cross-link 1024 1024 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P38167 UniProtKB Sequence conflict 964 967 . . . Note=PSGY->HPDT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38167 UniProtKB Sequence conflict 964 967 . . . Note=PSGY->HPDT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38737 1 1868 +P38737 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38737 UniProtKB Chain 2 1868 . . . ID=PRO_0000212558;Note=Proteasome component ECM29 +P38737 UniProtKB Repeat 32 69 . . . Note=HEAT 1 +P38737 UniProtKB Repeat 116 153 . . . Note=HEAT 2 +P38737 UniProtKB Repeat 256 292 . . . Note=HEAT 3 +P38737 UniProtKB Repeat 313 351 . . . Note=HEAT 4 +P38737 UniProtKB Repeat 384 422 . . . Note=HEAT 5 +P38737 UniProtKB Repeat 439 476 . . . Note=HEAT 6 +P38737 UniProtKB Repeat 590 627 . . . Note=HEAT 7 +P38737 UniProtKB Repeat 707 745 . . . Note=HEAT 8 +P38737 UniProtKB Repeat 748 780 . . . Note=HEAT 9 +P38737 UniProtKB Repeat 781 818 . . . Note=HEAT 10 +P38737 UniProtKB Repeat 846 885 . . . Note=HEAT 11 +P38737 UniProtKB Repeat 945 982 . . . Note=HEAT 12 +P38737 UniProtKB Repeat 988 1025 . . . Note=HEAT 13 +P38737 UniProtKB Repeat 1030 1067 . . . Note=HEAT 14 +P38737 UniProtKB Repeat 1137 1174 . . . Note=HEAT 15 +P38737 UniProtKB Repeat 1178 1215 . . . Note=HEAT 16 +P38737 UniProtKB Repeat 1272 1311 . . . Note=HEAT 17 +P38737 UniProtKB Repeat 1361 1398 . . . Note=HEAT 18 +P38737 UniProtKB Repeat 1422 1459 . . . Note=HEAT 19 +P38737 UniProtKB Repeat 1503 1540 . . . Note=HEAT 20 +P38737 UniProtKB Repeat 1544 1581 . . . Note=HEAT 21 +P38737 UniProtKB Repeat 1649 1687 . . . Note=HEAT 22 +P38737 UniProtKB Repeat 1746 1785 . . . Note=HEAT 23 +P38737 UniProtKB Repeat 1830 1867 . . . Note=HEAT 24 +P38737 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38737 UniProtKB Modified residue 1692 1692 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P38246 1 354 +P38246 UniProtKB Chain 1 354 . . . ID=PRO_0000086924;Note=Protein ECM8 +##sequence-region P38732 1 585 +P38732 UniProtKB Chain 1 585 . . . ID=PRO_0000202879;Note=Protein-lysine N-methyltransferase EFM1 +P38732 UniProtKB Domain 23 281 . . . Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 +P38732 UniProtKB Binding site 280 280 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 +##sequence-region P53235 1 642 +P53235 UniProtKB Chain 1 642 . . . ID=PRO_0000202800;Note=Eukaryotic translation initiation factor 2A +P53235 UniProtKB Repeat 69 115 . . . Note=WD 1 +P53235 UniProtKB Repeat 186 224 . . . Note=WD 2 +P53235 UniProtKB Repeat 289 331 . . . Note=WD 3 +P53235 UniProtKB Repeat 374 419 . . . Note=WD 4 +P53235 UniProtKB Modified residue 564 564 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53235 UniProtKB Modified residue 567 567 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53235 UniProtKB Modified residue 572 572 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53235 UniProtKB Natural variant 145 145 . . . Note=In strain: SK1. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P53235 UniProtKB Natural variant 165 165 . . . Note=In strain: SK1. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P53235 UniProtKB Natural variant 569 569 . . . Note=In strain: SK1. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +##sequence-region P32497 1 812 +P32497 UniProtKB Chain 1 812 . . . ID=PRO_0000123530;Note=Eukaryotic translation initiation factor 3 subunit C +P32497 UniProtKB Domain 650 780 . . . Note=PCI;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03002 +P32497 UniProtKB Compositional bias 15 147 . . . Note=Asp/Glu-rich (acidic) +P32497 UniProtKB Compositional bias 15 36 . . . Note=Ser-rich +P32497 UniProtKB Modified residue 98 98 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32497 UniProtKB Modified residue 99 99 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32497 UniProtKB Modified residue 103 103 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32497 UniProtKB Sequence conflict 111 111 . . . Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32497 UniProtKB Sequence conflict 583 583 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32497 UniProtKB Sequence conflict 641 641 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32497 UniProtKB Sequence conflict 643 643 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32497 UniProtKB Helix 252 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Beta strand 267 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 272 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 289 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Turn 307 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Beta strand 310 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 315 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 338 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Turn 342 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Turn 350 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Turn 363 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 368 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 392 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 422 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Turn 439 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 445 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 469 472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 478 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Turn 490 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 496 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 516 526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 530 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 538 556 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 560 571 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 576 579 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 585 592 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 595 602 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 608 610 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 614 637 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 652 660 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 671 684 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 687 695 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 698 702 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 706 729 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Turn 730 732 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Beta strand 733 737 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 738 745 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 749 763 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Beta strand 768 770 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Turn 771 774 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Beta strand 775 777 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +P32497 UniProtKB Helix 784 793 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1C +##sequence-region Q12050 1 791 +Q12050 UniProtKB Chain 1 791 . . . ID=PRO_0000086954;Note=Telomere length regulation protein ELG1 +Q12050 UniProtKB Compositional bias 86 91 . . . Note=Poly-Asp +Q12050 UniProtKB Modified residue 6 6 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P25574 1 760 +P25574 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25574 UniProtKB Chain 25 760 . . . ID=PRO_0000202547;Note=ER membrane protein complex subunit 1 +P25574 UniProtKB Topological domain 25 723 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25574 UniProtKB Transmembrane 724 744 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25574 UniProtKB Topological domain 745 760 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25574 UniProtKB Glycosylation 73 73 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25574 UniProtKB Glycosylation 106 106 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25574 UniProtKB Glycosylation 192 192 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25574 UniProtKB Glycosylation 202 202 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25574 UniProtKB Glycosylation 420 420 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25574 UniProtKB Glycosylation 443 443 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25574 UniProtKB Glycosylation 574 574 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25574 UniProtKB Glycosylation 578 578 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47133 1 292 +P47133 UniProtKB Chain 1 292 . . . ID=PRO_0000203107;Note=ER membrane protein complex subunit 2 +P47133 UniProtKB Repeat 163 196 . . . Note=TPR +P47133 UniProtKB Sequence conflict 20 20 . . . Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53095 1 428 +P53095 UniProtKB Chain 1 428 . . . ID=PRO_0000202722;Note=D-serine dehydratase +P53095 UniProtKB Sequence conflict 125 125 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53095 UniProtKB Sequence conflict 125 125 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40077 1 573 +P40077 UniProtKB Chain 1 573 . . . ID=PRO_0000202647;Note=Protein DSE1 +P40077 UniProtKB Repeat 144 185 . . . Note=WD 1 +P40077 UniProtKB Repeat 315 351 . . . Note=WD 2 +P40077 UniProtKB Repeat 356 395 . . . Note=WD 3 +P40077 UniProtKB Repeat 397 448 . . . Note=WD 4 +P40077 UniProtKB Cross-link 553 553 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P0CX08 1 502 +P0CX08 UniProtKB Chain 1 502 . . . ID=PRO_0000170751;Note=Mannitol dehydrogenase DSF1 +##sequence-region Q04949 1 312 +Q04949 UniProtKB Chain 1 312 . . . ID=PRO_0000203353;Note=Cytoplasmic dynein intermediate light chain DYN3 +##sequence-region Q12432 1 401 +Q12432 UniProtKB Chain 1 401 . . . ID=PRO_0000088783;Note=Chromatin modification-related protein EAF3 +Q12432 UniProtKB Domain 216 399 . . . Note=MRG;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00972 +Q12432 UniProtKB Compositional bias 148 205 . . . Note=Ser-rich +Q12432 UniProtKB Modified residue 201 201 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12432 UniProtKB Helix 3 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K3Y +Q12432 UniProtKB Beta strand 13 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F +Q12432 UniProtKB Beta strand 21 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F +Q12432 UniProtKB Turn 33 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F +Q12432 UniProtKB Beta strand 37 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F +Q12432 UniProtKB Beta strand 47 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K3X +Q12432 UniProtKB Beta strand 54 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K3Y +Q12432 UniProtKB Turn 69 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F +Q12432 UniProtKB Beta strand 76 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F +Q12432 UniProtKB Helix 86 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F +Q12432 UniProtKB Beta strand 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F +Q12432 UniProtKB Turn 94 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F +Q12432 UniProtKB Beta strand 97 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K3X +Q12432 UniProtKB Helix 102 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9F +##sequence-region Q03466 1 884 +Q03466 UniProtKB Chain 1 884 . . . ID=PRO_0000086907;Note=Protein EBS1 +##sequence-region P32471 1 206 +P32471 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P32471 UniProtKB Chain 2 206 . . . ID=PRO_0000155042;Note=Elongation factor 1-beta +P32471 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P32471 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32471 UniProtKB Modified residue 86 86 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P32471 UniProtKB Cross-link 13 13 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32471 UniProtKB Mutagenesis 120 122 . . . Note=In TEF5-7%3B reduces translation efficiency and enhances translation fidelity. KSI->R +P32471 UniProtKB Mutagenesis 121 121 . . . Note=Reduces translation efficiency and enhances translation fidelity. S->I%2CL%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10409717;Dbxref=PMID:10409717 +P32471 UniProtKB Mutagenesis 163 163 . . . Note=Temperature-sensitive. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11106763;Dbxref=PMID:11106763 +P32471 UniProtKB Mutagenesis 205 205 . . . Note=Loss of catalytic activity%2C but still binds to eEF1A. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11373622;Dbxref=PMID:11373622 +P32471 UniProtKB Sequence conflict 49 49 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32471 UniProtKB Sequence conflict 57 57 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32471 UniProtKB Sequence conflict 98 98 . . . Note=L->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32471 UniProtKB Sequence conflict 168 168 . . . Note=L->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32471 UniProtKB Beta strand 120 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P32471 UniProtKB Helix 136 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P32471 UniProtKB Beta strand 151 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P32471 UniProtKB Beta strand 165 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P32471 UniProtKB Turn 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P32471 UniProtKB Helix 181 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P32471 UniProtKB Turn 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +P32471 UniProtKB Beta strand 195 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F60 +##sequence-region P29547 1 415 +P29547 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P29547 UniProtKB Chain 2 415 . . . ID=PRO_0000208831;Note=Elongation factor 1-gamma 1 +P29547 UniProtKB Domain 2 78 . . . Note=GST N-terminal +P29547 UniProtKB Domain 89 215 . . . Note=GST C-terminal +P29547 UniProtKB Domain 254 415 . . . Note=EF-1-gamma C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00519 +P29547 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P29547 UniProtKB Modified residue 32 32 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P29547 UniProtKB Sequence conflict 191 191 . . . Note=W->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29547 UniProtKB Beta strand 5 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Helix 12 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Beta strand 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Helix 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Helix 37 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Beta strand 49 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Helix 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Beta strand 59 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Helix 63 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Helix 77 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Helix 90 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Turn 105 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Helix 109 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Helix 115 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Helix 126 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Beta strand 151 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Helix 160 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Helix 179 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Helix 186 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Turn 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +P29547 UniProtKB Helix 202 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NHY +##sequence-region P32324 1 842 +P32324 UniProtKB Chain 1 842 . . . ID=PRO_0000091024;Note=Elongation factor 2 +P32324 UniProtKB Domain 17 346 . . . Note=tr-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P32324 UniProtKB Nucleotide binding 26 33 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32324 UniProtKB Nucleotide binding 104 108 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32324 UniProtKB Nucleotide binding 158 161 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32324 UniProtKB Modified residue 509 509 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B by EFM3%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24517342,ECO:0000269|PubMed:25086354;Dbxref=PMID:24517342,PMID:25086354 +P32324 UniProtKB Modified residue 509 509 . . . Note=N6%2CN6-dimethyllysine%3B by EFM3%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22522802,ECO:0000269|PubMed:24517342,ECO:0000269|PubMed:25086354;Dbxref=PMID:22522802,PMID:24517342,PMID:25086354 +P32324 UniProtKB Modified residue 509 509 . . . Note=N6-methyllysine%3B by EFM3%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24517342,ECO:0000269|PubMed:25086354;Dbxref=PMID:24517342,PMID:25086354 +P32324 UniProtKB Modified residue 579 579 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32324 UniProtKB Modified residue 613 613 . . . Note=N6%2CN6-dimethyllysine%3B by EFM2%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24517342,ECO:0000269|PubMed:25086354;Dbxref=PMID:24517342,PMID:25086354 +P32324 UniProtKB Modified residue 613 613 . . . Note=N6-methyllysine%3B by EFM2%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24517342,ECO:0000269|PubMed:25086354;Dbxref=PMID:24517342,PMID:25086354 +P32324 UniProtKB Modified residue 699 699 . . . Note=Diphthamide;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:721806;Dbxref=PMID:721806 +P32324 UniProtKB Modified residue 713 713 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32324 UniProtKB Modified residue 763 763 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32324 UniProtKB Cross-link 841 841 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32324 UniProtKB Mutagenesis 180 180 . . . Note=Causes resistance to fusidic acid and reduces sensitivity to sordarin. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424 +P32324 UniProtKB Mutagenesis 187 187 . . . Note=Causes resistance to fusidic acid and reduces sensitivity to sordarin. V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424 +P32324 UniProtKB Mutagenesis 490 490 . . . Note=Reduces sensitivity to sordarin. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424 +P32324 UniProtKB Mutagenesis 521 521 . . . Note=Reduces sensitivity to fusidic acid and sordarin. Y->D%2CN%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424 +P32324 UniProtKB Mutagenesis 523 523 . . . Note=Causes resistance to fusidic acid and sordarin. S->F%2CP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424 +P32324 UniProtKB Mutagenesis 529 529 . . . Note=Reduces sensitivity to sordarin. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424 +P32324 UniProtKB Mutagenesis 559 559 . . . Note=Causes resistance to fusidic acid and sordarin. P->L%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424 +P32324 UniProtKB Mutagenesis 562 562 . . . Note=Reduces sensitivity to fusidic acid and causes resistance to sordarin. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424 +P32324 UniProtKB Mutagenesis 580 580 . . . Note=Causes impaired ribosomal translocation with an increased rate of -1 programmed ribosomal frameshift read-through during translation. P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23001565;Dbxref=PMID:23001565 +P32324 UniProtKB Mutagenesis 699 699 . . . Note=Prevents post-translational modification of this residue to diphthamide. Results in a functional protein that is resistant to diphtheria toxin. H->D%2CE%2CL%2CM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8473309;Dbxref=PMID:8473309 +P32324 UniProtKB Mutagenesis 701 701 . . . Note=Prevents ADP-ribosylation of the diphthamide by diphtheria toxin. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8466491;Dbxref=PMID:8466491 +P32324 UniProtKB Mutagenesis 727 727 . . . Note=Causes resistance to sordarin. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424 +P32324 UniProtKB Mutagenesis 774 774 . . . Note=Causes resistance to sordarin. V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424 +P32324 UniProtKB Mutagenesis 790 790 . . . Note=Causes resistance to fusidic acid and sordarin. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9452424;Dbxref=PMID:9452424 +P32324 UniProtKB Beta strand 2 4 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E1R +P32324 UniProtKB Helix 6 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 16 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 19 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 28 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 32 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 44 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E1R +P32324 UniProtKB Beta strand 74 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 83 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 95 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZM9 +P32324 UniProtKB Helix 113 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 123 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Turn 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 137 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 152 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 160 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 171 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 204 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 209 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Turn 214 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 218 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 222 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Turn 231 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 237 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 245 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 249 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Turn 252 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 256 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 261 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0V +P32324 UniProtKB Turn 264 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0V +P32324 UniProtKB Helix 272 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 278 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 295 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 309 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 316 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 330 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 345 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 357 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 364 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 374 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B82 +P32324 UniProtKB Beta strand 379 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 394 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 410 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 420 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 426 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 433 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 441 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 453 458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Turn 460 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 465 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 489 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 498 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 501 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 519 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 528 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 535 547 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 554 557 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 564 569 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 575 578 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 580 582 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZM9 +P32324 UniProtKB Beta strand 585 592 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 595 602 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 604 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0V +P32324 UniProtKB Beta strand 608 610 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0V +P32324 UniProtKB Helix 612 621 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 627 631 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 633 638 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Turn 639 641 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 642 648 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 656 672 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Turn 675 677 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 683 692 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 697 699 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 702 719 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 722 735 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 737 739 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 740 748 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Turn 749 751 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 753 758 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 766 773 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 774 776 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 780 787 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Turn 788 790 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 793 803 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Beta strand 811 813 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZIT +P32324 UniProtKB Helix 814 825 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +P32324 UniProtKB Helix 835 838 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N0U +##sequence-region P47163 1 339 +P47163 UniProtKB Chain 1 339 . . . ID=PRO_0000203120;Note=Protein-lysine N-methyltransferase EFM3 +P47163 UniProtKB Region 174 176 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867 +P47163 UniProtKB Binding site 137 137 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867 +P47163 UniProtKB Binding site 199 199 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867 +P47163 UniProtKB Binding site 233 233 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867 +P47163 UniProtKB Binding site 248 248 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867 +P47163 UniProtKB Modified residue 177 177 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47163 UniProtKB Sequence conflict 118 118 . . . Note=K->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53200 1 248 +P53200 UniProtKB Chain 1 248 . . . ID=PRO_0000202778;Note=Protein-lysine N-methyltransferase EFM5 +P53200 UniProtKB Compositional bias 49 52 . . . Note=Poly-Lys +##sequence-region Q05874 1 261 +Q05874 UniProtKB Chain 1 261 . . . ID=PRO_0000096901;Note=Protein N-terminal and lysine N-methyltransferase EFM7 +Q05874 UniProtKB Region 90 92 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q5VZV1,ECO:0000255|HAMAP-Rule:MF_03223 +Q05874 UniProtKB Binding site 64 64 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q5VZV1,ECO:0000255|HAMAP-Rule:MF_03223 +Q05874 UniProtKB Binding site 112 112 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q5VZV1,ECO:0000255|HAMAP-Rule:MF_03223 +Q05874 UniProtKB Binding site 144 144 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q5VZV1,ECO:0000255|HAMAP-Rule:MF_03223 +Q05874 UniProtKB Binding site 171 171 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q5VZV1,ECO:0000255|HAMAP-Rule:MF_03223 +##sequence-region P54858 1 310 +P54858 UniProtKB Chain 1 310 . . . ID=PRO_0000079981;Note=Protein DOS2 +P54858 UniProtKB Domain 176 228 . . . Note=BSD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00036 +P54858 UniProtKB Compositional bias 255 259 . . . Note=Poly-Glu +P54858 UniProtKB Compositional bias 302 308 . . . Note=Poly-Asp +##sequence-region P40553 1 215 +P40553 UniProtKB Chain 1 215 . . . ID=PRO_0000135152;Note=Peroxiredoxin DOT5 +P40553 UniProtKB Domain 63 211 . . . Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +P40553 UniProtKB Active site 107 107 . . . Note=Cysteine sulfenic acid (-SOH) intermediate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12730197;Dbxref=PMID:12730197 +P40553 UniProtKB Disulfide bond 107 112 . . . Note=Redox-active;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12730197;Dbxref=PMID:12730197 +P40553 UniProtKB Mutagenesis 107 107 . . . Note=No TPx activity%2C no effect on DOT activity. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10681558,ECO:0000269|PubMed:12730197,ECO:0000269|PubMed:12925864;Dbxref=PMID:10681558,PMID:12730197,PMID:12925864 +P40553 UniProtKB Mutagenesis 112 112 . . . Note=No TPx activity%2C no effect on DOT activity. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12730197,ECO:0000269|PubMed:12925864;Dbxref=PMID:12730197,PMID:12925864 +P40553 UniProtKB Beta strand 73 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V +P40553 UniProtKB Beta strand 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V +P40553 UniProtKB Helix 84 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V +P40553 UniProtKB Beta strand 92 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V +P40553 UniProtKB Beta strand 100 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V +P40553 UniProtKB Helix 105 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V +P40553 UniProtKB Turn 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V +P40553 UniProtKB Beta strand 126 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V +P40553 UniProtKB Helix 135 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V +P40553 UniProtKB Beta strand 148 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V +P40553 UniProtKB Helix 158 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V +P40553 UniProtKB Beta strand 166 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V +P40553 UniProtKB Beta strand 176 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V +P40553 UniProtKB Beta strand 184 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V +P40553 UniProtKB Helix 194 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A4V +##sequence-region P24482 1 689 +P24482 UniProtKB Chain 1 689 . . . ID=PRO_0000071573;Note=DNA polymerase epsilon subunit B +P24482 UniProtKB Modified residue 122 122 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P24482 UniProtKB Modified residue 141 141 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14747467;Dbxref=PMID:14747467 +P24482 UniProtKB Modified residue 613 613 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14747467;Dbxref=PMID:14747467 +P24482 UniProtKB Sequence conflict 458 458 . . . Note=F->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24482 UniProtKB Sequence conflict 521 521 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24482 UniProtKB Sequence conflict 565 565 . . . Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24482 UniProtKB Sequence conflict 584 584 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24482 UniProtKB Sequence conflict 644 644 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25615 1 582 +P25615 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8265341;Dbxref=PMID:8265341 +P25615 UniProtKB Chain 2 582 . . . ID=PRO_0000218789;Note=DNA polymerase IV +P25615 UniProtKB Region 360 369 . . . Note=Involved in ssDNA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25615 UniProtKB Compositional bias 472 478 . . . Note=Poly-Glu +P25615 UniProtKB Metal binding 367 367 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25615 UniProtKB Metal binding 369 369 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25615 UniProtKB Metal binding 502 502 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25615 UniProtKB Mutagenesis 247 247 . . . Note=Weakened DNA-binding. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10438542;Dbxref=PMID:10438542 +P25615 UniProtKB Mutagenesis 248 248 . . . Note=Weakened DNA-binding. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10438542;Dbxref=PMID:10438542 +P25615 UniProtKB Mutagenesis 367 367 . . . Note=Loss of nucleotidyl transfer. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10438542;Dbxref=PMID:10438542 +##sequence-region P39985 1 1022 +P39985 UniProtKB Chain 1 1022 . . . ID=PRO_0000046472;Note=DNA polymerase V +P39985 UniProtKB Modified residue 789 789 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39985 UniProtKB Natural variant 625 625 . . . Note=Lethal. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12093911;Dbxref=PMID:12093911 +##sequence-region P21951 1 2222 +P21951 UniProtKB Chain 1 2222 . . . ID=PRO_0000046467;Note=DNA polymerase epsilon catalytic subunit A +P21951 UniProtKB Zinc finger 2108 2133 . . . Note=CysA-type +P21951 UniProtKB Motif 2164 2181 . . . Note=CysB motif +P21951 UniProtKB Metal binding 2108 2108 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21951 UniProtKB Metal binding 2111 2111 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21951 UniProtKB Metal binding 2130 2130 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21951 UniProtKB Metal binding 2133 2133 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21951 UniProtKB Metal binding 2164 2164 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21951 UniProtKB Metal binding 2167 2167 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21951 UniProtKB Metal binding 2179 2179 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21951 UniProtKB Metal binding 2181 2181 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21951 UniProtKB Mutagenesis 644 644 . . . Note=In POL2-9%3B temperature-sensitive mutant. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1537345;Dbxref=PMID:1537345 +P21951 UniProtKB Mutagenesis 710 710 . . . Note=In POL2-18%3B temperature-sensitive mutant. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1537345;Dbxref=PMID:1537345 +P21951 UniProtKB Helix 33 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Turn 67 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 72 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 114 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 128 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 138 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 149 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Turn 160 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 166 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 180 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 186 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 196 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Turn 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 235 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 239 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 249 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 263 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 271 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 286 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Turn 303 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 308 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 318 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Turn 325 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 328 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PTF +P21951 UniProtKB Beta strand 346 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 355 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 372 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Turn 379 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 383 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 398 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 415 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 422 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 434 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 439 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 456 458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 459 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 467 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 489 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 500 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 504 509 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 512 526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 546 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 558 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 564 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 572 575 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 578 597 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 604 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 607 609 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 610 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 629 632 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 634 641 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 644 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 656 658 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 659 662 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 664 666 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 678 689 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 694 705 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 708 710 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 720 722 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 723 725 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 728 747 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 752 766 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 769 797 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Turn 798 800 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 801 803 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 808 832 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 833 835 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 844 868 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 869 875 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 878 884 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 890 895 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 900 904 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 905 918 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 920 928 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Turn 929 932 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 933 939 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 944 955 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 969 972 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 978 984 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Turn 985 987 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 988 992 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 993 1002 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 1003 1007 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 1009 1011 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PTF +P21951 UniProtKB Helix 1012 1031 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Turn 1032 1036 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 1039 1046 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 1048 1051 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 1056 1059 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 1065 1077 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 1079 1082 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 1083 1086 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 1088 1095 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 1097 1099 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PTF +P21951 UniProtKB Helix 1102 1104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Beta strand 1106 1108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 1109 1113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 1116 1127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 1137 1140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 1143 1157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 1159 1164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +P21951 UniProtKB Helix 1178 1183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8O +##sequence-region P38213 1 736 +P38213 UniProtKB Chain 1 736 . . . ID=PRO_0000202467;Note=Protein DSF2 +P38213 UniProtKB Sequence conflict 205 205 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38213 UniProtKB Sequence conflict 327 327 . . . Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53847 1 754 +P53847 UniProtKB Chain 1 754 . . . ID=PRO_0000203383;Note=Protein transport protein DSL1 +P53847 UniProtKB Region 1 200 . . . Note=Interaction with TIP20;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11739780;Dbxref=PMID:11739780 +P53847 UniProtKB Region 406 459 . . . Note=Interaction with RET2 +P53847 UniProtKB Region 406 440 . . . Note=Interaction with RET1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14504276;Dbxref=PMID:14504276 +P53847 UniProtKB Mutagenesis 413 413 . . . Note=Viable and reduced interaction with RET2%2C strong Golgi-ER retrograde transport defect. Loss of interaction with RET2%3B when associated with A-455. Lethal and loss of interactions with RET1 and RET2%3B when associated with A-425. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14504276;Dbxref=PMID:14504276 +P53847 UniProtKB Mutagenesis 425 425 . . . Note=Loss of interaction with RET1%3B when associated with A-413. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14504276;Dbxref=PMID:14504276 +P53847 UniProtKB Mutagenesis 455 455 . . . Note=Viable and no effect. Lethal and loss of interaction with RET2 and reduced interaction with RET1%3B when associated with A-413. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14504276;Dbxref=PMID:14504276 +P53847 UniProtKB Mutagenesis 725 754 . . . Note=In dsl1-22%3B strong Golgi-ER retrograde transport defect. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11493604;Dbxref=PMID:11493604 +P53847 UniProtKB Helix 45 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Helix 77 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Helix 95 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Helix 102 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Beta strand 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Beta strand 136 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Beta strand 143 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Turn 148 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Beta strand 152 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Helix 156 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Helix 169 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Helix 178 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Helix 186 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Helix 207 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Beta strand 222 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Turn 228 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Beta strand 232 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Helix 246 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Helix 266 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Helix 292 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Beta strand 297 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Helix 302 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Helix 331 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETV +P53847 UniProtKB Helix 340 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ETU +##sequence-region Q02647 1 92 +Q02647 UniProtKB Chain 1 92 . . . ID=PRO_0000195149;Note=Dynein light chain 1%2C cytoplasmic +Q02647 UniProtKB Beta strand 10 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DS1 +Q02647 UniProtKB Helix 18 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DS1 +Q02647 UniProtKB Helix 38 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DS1 +Q02647 UniProtKB Beta strand 57 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DS1 +Q02647 UniProtKB Beta strand 75 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DS1 +Q02647 UniProtKB Beta strand 84 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DS1 +##sequence-region P07807 1 211 +P07807 UniProtKB Chain 1 211 . . . ID=PRO_0000186378;Note=Dihydrofolate reductase +P07807 UniProtKB Domain 7 210 . . . Note=DHFR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00660 +P07807 UniProtKB Nucleotide binding 20 26 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07807 UniProtKB Nucleotide binding 58 60 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07807 UniProtKB Nucleotide binding 80 82 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07807 UniProtKB Nucleotide binding 123 130 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07807 UniProtKB Region 34 39 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07807 UniProtKB Binding site 13 13 . . . Note=NADP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07807 UniProtKB Binding site 74 74 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07807 UniProtKB Sequence conflict 27 27 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06673 1 1274 +Q06673 UniProtKB Chain 1 1274 . . . ID=PRO_0000086919;Note=Protein ECM30 +Q06673 UniProtKB Compositional bias 247 253 . . . Note=Poly-Leu +Q06673 UniProtKB Compositional bias 416 419 . . . Note=Poly-Ser +Q06673 UniProtKB Compositional bias 425 428 . . . Note=Poly-Ser +Q06673 UniProtKB Compositional bias 491 498 . . . Note=Poly-Ser +Q06673 UniProtKB Compositional bias 1103 1109 . . . Note=Poly-Ser +Q06673 UniProtKB Compositional bias 1136 1166 . . . Note=Asn-rich +Q06673 UniProtKB Modified residue 635 635 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06673 UniProtKB Modified residue 1065 1065 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P38728 1 170 +P38728 UniProtKB Chain 1 170 . . . ID=PRO_0000207532;Note=Protein ECM34 +P38728 UniProtKB Transmembrane 51 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38728 UniProtKB Transmembrane 98 118 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38728 UniProtKB Glycosylation 45 45 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q05902 1 660 +Q05902 UniProtKB Chain 1 469 . . . ID=PRO_0000011078;Note=Glutathione hydrolase heavy chain;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05902 UniProtKB Chain 470 660 . . . ID=PRO_0000011079;Note=Glutathione hydrolase light chain;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05902 UniProtKB Topological domain 1 13 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05902 UniProtKB Transmembrane 14 34 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05902 UniProtKB Topological domain 35 660 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05902 UniProtKB Region 540 541 . . . Note=Glutamate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05902 UniProtKB Region 562 563 . . . Note=Glutamate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05902 UniProtKB Active site 470 470 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05902 UniProtKB Binding site 177 177 . . . Note=Glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05902 UniProtKB Binding site 488 488 . . . Note=Glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05902 UniProtKB Binding site 490 490 . . . Note=Glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05902 UniProtKB Binding site 509 509 . . . Note=Glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05902 UniProtKB Binding site 512 512 . . . Note=Glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05902 UniProtKB Glycosylation 119 119 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05902 UniProtKB Glycosylation 191 191 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05902 UniProtKB Glycosylation 270 270 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05902 UniProtKB Glycosylation 298 298 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05902 UniProtKB Glycosylation 454 454 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05902 UniProtKB Glycosylation 517 517 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05902 UniProtKB Natural variant 171 171 . . . Note=In strain: YPH499. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12868055;Dbxref=PMID:12868055 +Q05902 UniProtKB Natural variant 494 494 . . . Note=In strain: YPH499%3B lack of gamma-glutamyl transferase activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12868055;Dbxref=PMID:12868055 +##sequence-region P38773 1 246 +P38773 UniProtKB Chain 1 246 . . . ID=PRO_0000079975;Note=2-deoxyglucose-6-phosphate phosphatase 2 +P38773 UniProtKB Active site 12 12 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38773 UniProtKB Active site 14 14 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38773 UniProtKB Metal binding 12 12 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38773 UniProtKB Metal binding 14 14 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38773 UniProtKB Metal binding 183 183 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q04089 1 582 +Q04089 UniProtKB Chain 1 582 . . . ID=PRO_0000186091;Note=Histone-lysine N-methyltransferase%2C H3 lysine-79 specific +Q04089 UniProtKB Domain 254 568 . . . Note=DOT1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00902 +Q04089 UniProtKB Region 158 172 . . . Note=Required for interaction with nucleosomes and DNA +Q04089 UniProtKB Region 372 375 . . . Note=S-adenosyl-L-methionine binding +Q04089 UniProtKB Region 395 404 . . . Note=S-adenosyl-L-methionine binding +Q04089 UniProtKB Region 459 460 . . . Note=S-adenosyl-L-methionine binding +Q04089 UniProtKB Compositional bias 106 169 . . . Note=Lys-rich +Q04089 UniProtKB Binding site 422 422 . . . Note=S-adenosyl-L-methionine +Q04089 UniProtKB Mutagenesis 301 301 . . . Note=Abolishes methyltransferase activity. D->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292170;Dbxref=PMID:15292170 +Q04089 UniProtKB Mutagenesis 350 350 . . . Note=Reduces methyltransferase activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292170;Dbxref=PMID:15292170 +Q04089 UniProtKB Mutagenesis 372 372 . . . Note=Reduces methyltransferase activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292170;Dbxref=PMID:15292170 +Q04089 UniProtKB Mutagenesis 374 374 . . . Note=Abolishes methyltransferase activity. E->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292170;Dbxref=PMID:15292170 +Q04089 UniProtKB Mutagenesis 399 399 . . . Note=Abolishes methyltransferase activity. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12080090;Dbxref=PMID:12080090 +Q04089 UniProtKB Mutagenesis 401 403 . . . Note=Abolishes methyltransferase activity. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12080090;Dbxref=PMID:12080090 +Q04089 UniProtKB Mutagenesis 401 401 . . . Note=Abolishes silencing function. G->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12086673;Dbxref=PMID:12086673 +Q04089 UniProtKB Mutagenesis 422 422 . . . Note=Abolishes S-adenosyl-L-methionine binding and methyltransferase activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292170;Dbxref=PMID:15292170 +Q04089 UniProtKB Mutagenesis 422 422 . . . Note=No effect. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292170;Dbxref=PMID:15292170 +Q04089 UniProtKB Mutagenesis 543 543 . . . Note=Abolishes methyltransferase activity%2C but not S-adenosyl-L-methionine binding. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292170;Dbxref=PMID:15292170 +Q04089 UniProtKB Mutagenesis 550 550 . . . Note=Abolishes methyltransferase activity%2C but not S-adenosyl-L-methionine binding. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292170;Dbxref=PMID:15292170 +Q04089 UniProtKB Mutagenesis 550 550 . . . Note=No effect. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292170;Dbxref=PMID:15292170 +Q04089 UniProtKB Beta strand 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Beta strand 186 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Helix 196 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Helix 212 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Beta strand 236 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Beta strand 248 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Beta strand 255 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Beta strand 260 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Helix 264 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Helix 284 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Helix 293 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Helix 305 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Helix 324 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Beta strand 336 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Helix 340 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Helix 355 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Helix 368 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Helix 377 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Beta strand 394 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Helix 404 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Beta strand 416 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Helix 425 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Beta strand 452 458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Helix 464 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Helix 470 472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Beta strand 474 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Helix 485 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Beta strand 503 508 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Beta strand 519 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Helix 525 528 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Beta strand 529 535 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Beta strand 544 546 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Beta strand 549 555 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +Q04089 UniProtKB Helix 561 563 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1U2Z +##sequence-region P47138 1 172 +P47138 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P47138 UniProtKB Chain 2 172 . . . ID=PRO_0000071154;Note=Diphthamide biosynthesis protein 4 +P47138 UniProtKB Domain 6 77 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +P47138 UniProtKB Zinc finger 91 164 . . . Note=DPH-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00456 +P47138 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P14020 1 267 +P14020 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4 +P14020 UniProtKB Chain 2 267 . . . ID=PRO_0000059175;Note=Dolichol-phosphate mannosyltransferase +P14020 UniProtKB Topological domain 2 238 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14020 UniProtKB Transmembrane 239 259 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14020 UniProtKB Topological domain 260 267 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14020 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4 +P14020 UniProtKB Modified residue 141 141 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15548536;Dbxref=PMID:15548536 +P14020 UniProtKB Mutagenesis 141 141 . . . Note=Reduces specific activity 2-fold. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15548536;Dbxref=PMID:15548536 +##sequence-region P15436 1 1097 +P15436 UniProtKB Chain 1 1097 . . . ID=PRO_0000046454;Note=DNA polymerase delta catalytic subunit +P15436 UniProtKB Zinc finger 1009 1027 . . . Note=CysA-type +P15436 UniProtKB Motif 1056 1074 . . . Note=CysB motif +P15436 UniProtKB Metal binding 1009 1009 . . . Note=Zinc +P15436 UniProtKB Metal binding 1012 1012 . . . Note=Zinc +P15436 UniProtKB Metal binding 1024 1024 . . . Note=Zinc +P15436 UniProtKB Metal binding 1027 1027 . . . Note=Zinc +P15436 UniProtKB Metal binding 1056 1056 . . . Note=Iron-sulfur (4Fe-4S) +P15436 UniProtKB Metal binding 1059 1059 . . . Note=Iron-sulfur (4Fe-4S) +P15436 UniProtKB Metal binding 1069 1069 . . . Note=Iron-sulfur (4Fe-4S) +P15436 UniProtKB Metal binding 1074 1074 . . . Note=Iron-sulfur (4Fe-4S) +P15436 UniProtKB Modified residue 30 30 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P15436 UniProtKB Modified residue 37 37 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P15436 UniProtKB Mutagenesis 1009 1009 . . . Note=Impairs iron-sulfur-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22119860;Dbxref=PMID:22119860 +P15436 UniProtKB Mutagenesis 1012 1012 . . . Note=Impairs iron-sulfur-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22119860;Dbxref=PMID:22119860 +P15436 UniProtKB Mutagenesis 1024 1024 . . . Note=Impairs iron-sulfur-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22119860;Dbxref=PMID:22119860 +P15436 UniProtKB Mutagenesis 1027 1027 . . . Note=Impairs iron-sulfur-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22119860;Dbxref=PMID:22119860 +P15436 UniProtKB Mutagenesis 1056 1056 . . . Note=Abolishes iron-sulfur-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22119860;Dbxref=PMID:22119860 +P15436 UniProtKB Mutagenesis 1059 1059 . . . Note=Abolishes iron-sulfur-binding. C->A +P15436 UniProtKB Mutagenesis 1069 1069 . . . Note=Abolishes iron-sulfur-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22119860;Dbxref=PMID:22119860 +P15436 UniProtKB Mutagenesis 1074 1074 . . . Note=Abolishes iron-sulfur-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22119860;Dbxref=PMID:22119860 +P15436 UniProtKB Mutagenesis 1074 1074 . . . Note=In pol3-13%3B synthetically lethal with mutations of NBP35%2C DRE2 and TAH18. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22119860;Dbxref=PMID:22119860 +P15436 UniProtKB Sequence conflict 78 79 . . . Note=EL->DV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15436 UniProtKB Sequence conflict 78 79 . . . Note=EL->DV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15436 UniProtKB Sequence conflict 78 79 . . . Note=EL->DV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15436 UniProtKB Sequence conflict 189 189 . . . Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15436 UniProtKB Sequence conflict 204 204 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15436 UniProtKB Sequence conflict 347 363 . . . Note=SIAGAKKPFIRNVFTLN->YLALRNHSFVMCYSD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15436 UniProtKB Sequence conflict 647 649 . . . Note=TPN->HY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15436 UniProtKB Sequence conflict 870 870 . . . Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15436 UniProtKB Sequence conflict 974 974 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15436 UniProtKB Turn 108 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 113 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 126 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 135 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 148 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 159 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 168 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 173 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Turn 185 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 191 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 211 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 223 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 238 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 254 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 269 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 282 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 290 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Turn 297 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 307 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 316 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Turn 334 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 339 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 355 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 371 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 379 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 396 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Turn 403 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 407 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 427 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 439 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Turn 444 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 447 451 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 460 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 464 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 479 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 499 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 507 530 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 533 544 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 550 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 556 570 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 598 600 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 604 609 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 612 619 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 624 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 630 635 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Turn 641 643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 644 646 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 652 654 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Turn 656 658 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 662 682 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 687 711 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 714 717 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 721 745 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 748 750 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 757 760 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 762 769 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 775 790 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 799 812 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 815 826 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 829 835 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 836 838 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 844 858 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 863 878 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 884 887 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 889 892 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 902 914 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 922 929 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Beta strand 931 933 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 935 937 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 942 947 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 954 960 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 963 974 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +P15436 UniProtKB Helix 976 982 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAY +##sequence-region P32601 1 143 +P32601 UniProtKB Chain 1 143 . . . ID=PRO_0000174180;Note=Protein DSS4 +P32601 UniProtKB Domain 1 131 . . . Note=MSS4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01132 +P32601 UniProtKB Metal binding 6 6 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01132 +P32601 UniProtKB Metal binding 11 11 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01132 +P32601 UniProtKB Metal binding 104 104 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01132 +P32601 UniProtKB Metal binding 107 107 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01132 +P32601 UniProtKB Natural variant 108 108 . . . Note=In DSS4-1%3B a dominant suppressor of SEC4-8. D->G +P32601 UniProtKB Sequence conflict 136 136 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32601 UniProtKB Sequence conflict 136 136 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07648 1 150 +Q07648 UniProtKB Chain 1 150 . . . ID=PRO_0000164634;Note=D-aminoacyl-tRNA deacylase +Q07648 UniProtKB Motif 140 141 . . . Note=Gly-cisPro motif%2C important for rejection of L-amino acids;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8IIS0 +##sequence-region P38149 1 878 +P38149 UniProtKB Chain 1 878 . . . ID=PRO_0000051469;Note=Probable di- and tripeptidase DUG2 +P38149 UniProtKB Repeat 18 57 . . . Note=WD 1 +P38149 UniProtKB Repeat 68 107 . . . Note=WD 2 +P38149 UniProtKB Repeat 235 274 . . . Note=WD 3 +P38149 UniProtKB Repeat 282 322 . . . Note=WD 4 +P38149 UniProtKB Repeat 362 405 . . . Note=WD 5 +P38149 UniProtKB Repeat 608 651 . . . Note=WD 6 +P38149 UniProtKB Active site 522 522 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38149 UniProtKB Active site 586 586 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38149 UniProtKB Metal binding 520 520 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38149 UniProtKB Metal binding 553 553 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38149 UniProtKB Metal binding 553 553 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38149 UniProtKB Metal binding 587 587 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38149 UniProtKB Metal binding 853 853 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P39009 1 513 +P39009 UniProtKB Chain 1 513 . . . ID=PRO_0000085930;Note=DNA damage response protein kinase DUN1 +P39009 UniProtKB Domain 56 112 . . . Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 +P39009 UniProtKB Domain 200 480 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P39009 UniProtKB Nucleotide binding 206 214 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P39009 UniProtKB Active site 328 328 . . . Note=Proton acceptor +P39009 UniProtKB Binding site 229 229 . . . Note=ATP +P39009 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39009 UniProtKB Modified residue 139 139 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39009 UniProtKB Modified residue 380 380 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39009 UniProtKB Mutagenesis 229 229 . . . Note=Loss of kinase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8261511;Dbxref=PMID:8261511 +P39009 UniProtKB Mutagenesis 328 328 . . . Note=Loss of kinase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8261511;Dbxref=PMID:8261511 +P39009 UniProtKB Beta strand 28 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ +P39009 UniProtKB Beta strand 33 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ +P39009 UniProtKB Beta strand 44 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ +P39009 UniProtKB Beta strand 56 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ +P39009 UniProtKB Beta strand 64 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ +P39009 UniProtKB Beta strand 77 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ +P39009 UniProtKB Beta strand 90 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ +P39009 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQL +P39009 UniProtKB Beta strand 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ +P39009 UniProtKB Beta strand 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ +P39009 UniProtKB Beta strand 121 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ +P39009 UniProtKB Turn 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ +P39009 UniProtKB Beta strand 131 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ +P39009 UniProtKB Beta strand 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQL +P39009 UniProtKB Beta strand 154 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JQJ +##sequence-region Q04067 1 274 +Q04067 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q04067 UniProtKB Chain 2 274 . . . ID=PRO_0000123514;Note=Eukaryotic translation initiation factor 3 subunit G +Q04067 UniProtKB Domain 191 270 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03006 +Q04067 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q04067 UniProtKB Modified residue 131 131 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04067 UniProtKB Beta strand 13 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1E +Q04067 UniProtKB Beta strand 17 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1E +Q04067 UniProtKB Beta strand 28 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1E +Q04067 UniProtKB Helix 47 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1E +Q04067 UniProtKB Helix 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1E +Q04067 UniProtKB Helix 87 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1E +##sequence-region Q03764 1 534 +Q03764 UniProtKB Chain 1 534 . . . ID=PRO_0000206230;Note=Ethanolamine kinase +Q03764 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q02884 1 456 +Q02884 UniProtKB Chain 1 456 . . . ID=PRO_0000235812;Note=Elongator complex protein 4 +Q02884 UniProtKB Modified residue 222 222 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q02884 UniProtKB Beta strand 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Turn 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Beta strand 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Helix 91 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Beta strand 99 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Beta strand 107 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Helix 119 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Beta strand 149 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Helix 158 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Beta strand 165 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EJS +Q02884 UniProtKB Beta strand 241 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EJS +Q02884 UniProtKB Turn 253 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Beta strand 256 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Beta strand 261 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EJS +Q02884 UniProtKB Helix 265 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Turn 279 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Beta strand 282 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Turn 289 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Turn 294 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Helix 299 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Helix 304 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Turn 321 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Beta strand 325 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Helix 333 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EJS +Q02884 UniProtKB Helix 338 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Beta strand 349 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Helix 359 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Turn 369 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Helix 373 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Beta strand 379 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Helix 389 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Beta strand 398 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q02884 UniProtKB Beta strand 411 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +##sequence-region Q04409 1 500 +Q04409 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17709 +Q04409 UniProtKB Chain 2 500 . . . ID=PRO_0000197604;Note=Putative glucokinase-2 +Q04409 UniProtKB Domain 12 498 . . . Note=Hexokinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084 +Q04409 UniProtKB Nucleotide binding 487 492 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04409 UniProtKB Region 74 217 . . . Note=Hexokinase small subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084 +Q04409 UniProtKB Region 159 185 . . . Note=Glucose-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04409 UniProtKB Region 218 487 . . . Note=Hexokinase large subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084 +Q04409 UniProtKB Binding site 110 110 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04409 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17709 +Q04409 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17709 +Q04409 UniProtKB Modified residue 470 470 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17709 +##sequence-region P38333 1 483 +P38333 UniProtKB Chain 1 483 . . . ID=PRO_0000186118;Note=Essential nuclear protein 1 +P38333 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38333 UniProtKB Modified residue 190 190 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38333 UniProtKB Modified residue 404 404 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P43572 1 832 +P43572 UniProtKB Chain 1 832 . . . ID=PRO_0000214167;Note=Enhancer of polycomb-like protein 1 +P43572 UniProtKB Compositional bias 419 428 . . . Note=Poly-Ala +P43572 UniProtKB Compositional bias 447 451 . . . Note=Poly-Gln +P43572 UniProtKB Compositional bias 454 461 . . . Note=Poly-Gln +P43572 UniProtKB Compositional bias 476 481 . . . Note=Poly-Ser +P43572 UniProtKB Compositional bias 777 795 . . . Note=Poly-Gln +P43572 UniProtKB Beta strand 65 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9U +P43572 UniProtKB Beta strand 71 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9U +P43572 UniProtKB Beta strand 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9U +P43572 UniProtKB Helix 133 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P43572 UniProtKB Helix 155 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P43572 UniProtKB Helix 166 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P43572 UniProtKB Beta strand 177 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P43572 UniProtKB Helix 186 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P43572 UniProtKB Helix 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P43572 UniProtKB Helix 211 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P43572 UniProtKB Helix 217 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P43572 UniProtKB Helix 229 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P43572 UniProtKB Helix 232 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P43572 UniProtKB Helix 256 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P43572 UniProtKB Helix 264 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P43572 UniProtKB Turn 286 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P43572 UniProtKB Beta strand 300 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9W +P43572 UniProtKB Beta strand 310 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9U +P43572 UniProtKB Helix 324 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +P43572 UniProtKB Helix 388 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9W +##sequence-region P41912 1 237 +P41912 UniProtKB Chain 1 237 . . . ID=PRO_0000213988;Note=Ras modification protein ERF4 +P41912 UniProtKB Mutagenesis 128 128 . . . Note=In ERF4-1%3B loss of function. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12379641;Dbxref=PMID:12379641 +P41912 UniProtKB Mutagenesis 148 148 . . . Note=In ERF4-2%3B loss of function. V->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12379641;Dbxref=PMID:12379641 +P41912 UniProtKB Mutagenesis 204 204 . . . Note=In ERF4-3%3B loss of function. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12379641;Dbxref=PMID:12379641 +##sequence-region P32352 1 222 +P32352 UniProtKB Chain 1 222 . . . ID=PRO_0000087021;Note=C-8 sterol isomerase +P32352 UniProtKB Transmembrane 3 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P54781 1 538 +P54781 UniProtKB Chain 1 538 . . . ID=PRO_0000052050;Note=Cytochrome P450 61 +P54781 UniProtKB Metal binding 476 476 . . . Note=Iron (heme axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04798 +P54781 UniProtKB Cross-link 164 164 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P54781 UniProtKB Cross-link 198 198 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P54781 UniProtKB Sequence conflict 286 286 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P62651 1 68 +P62651 UniProtKB Chain 1 68 . . . ID=PRO_0000087028;Note=Phosphatidylinositol N-acetylglucosaminyltransferase ERI1 subunit +P62651 UniProtKB Transmembrane 8 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P62651 UniProtKB Transmembrane 34 54 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43613 1 295 +P43613 UniProtKB Signal peptide 1 20 . . . . +P43613 UniProtKB Chain 21 295 . . . ID=PRO_0000007272;Note=ER-localized J domain-containing protein 5 +P43613 UniProtKB Topological domain 21 130 . . . Note=Lumenal +P43613 UniProtKB Transmembrane 131 151 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43613 UniProtKB Topological domain 152 295 . . . Note=Cytoplasmic +P43613 UniProtKB Domain 42 110 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +##sequence-region P53080 1 175 +P53080 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53080 UniProtKB Chain 2 175 . . . ID=PRO_0000202715;Note=Enhancer of mRNA-decapping protein 1 +P53080 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53080 UniProtKB Modified residue 82 82 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P39998 1 551 +P39998 UniProtKB Chain 1 551 . . . ID=PRO_0000202613;Note=Enhancer of mRNA-decapping protein 3 +P39998 UniProtKB Domain 93 129 . . . Note=DFDF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00845 +P39998 UniProtKB Domain 288 527 . . . Note=YjeF N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00719 +P39998 UniProtKB Modified residue 257 257 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198 +P39998 UniProtKB Modified residue 261 261 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39998 UniProtKB Mutagenesis 360 361 . . . Note=Abolishes homodimerization. RH->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18678652;Dbxref=PMID:18678652 +P39998 UniProtKB Helix 91 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BRU +P39998 UniProtKB Turn 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BRU +P39998 UniProtKB Helix 107 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BRU +##sequence-region P14741 1 305 +P14741 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P14741 UniProtKB Chain 2 305 . . . ID=PRO_0000156060;Note=Translation initiation factor eIF-2B subunit alpha +P14741 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P14741 UniProtKB Modified residue 291 291 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P32501 1 712 +P32501 UniProtKB Chain 1 712 . . . ID=PRO_0000156078;Note=Translation initiation factor eIF-2B subunit epsilon +P32501 UniProtKB Domain 539 710 . . . Note=W2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00695 +P32501 UniProtKB Modified residue 478 478 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32501 UniProtKB Modified residue 481 481 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32501 UniProtKB Modified residue 507 507 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P32501 UniProtKB Modified residue 525 525 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32501 UniProtKB Modified residue 538 538 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32501 UniProtKB Modified residue 707 707 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32501 UniProtKB Mutagenesis 552 552 . . . Note=Reduced exchange activity. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10805739;Dbxref=PMID:10805739 +P32501 UniProtKB Mutagenesis 569 569 . . . Note=Lethal. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14681227;Dbxref=PMID:14681227 +P32501 UniProtKB Mutagenesis 576 576 . . . Note=Reduced exchange activity. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10805739;Dbxref=PMID:10805739 +P32501 UniProtKB Mutagenesis 655 677 . . . Note=Abolishes binding to SUI3. LFSALVSLYDNDIIEEDVIYKWW->AFSAAVSAADNDAAEAAVAAKWA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10075937;Dbxref=PMID:10075937 +P32501 UniProtKB Mutagenesis 696 706 . . . Note=Abolishes binding to SUI3%3B probably impairs the conversion of eIF-2-GDP to eIF-2-GTP. WVEWLQNADEE->AAEAAQNAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10075937;Dbxref=PMID:10075937 +P32501 UniProtKB Helix 545 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ +P32501 UniProtKB Helix 563 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ +P32501 UniProtKB Helix 581 601 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ +P32501 UniProtKB Helix 607 618 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ +P32501 UniProtKB Helix 619 624 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ +P32501 UniProtKB Helix 629 646 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ +P32501 UniProtKB Helix 651 664 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ +P32501 UniProtKB Helix 670 678 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ +P32501 UniProtKB Helix 684 686 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ +P32501 UniProtKB Helix 687 702 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PAQ +##sequence-region Q05775 1 265 +Q05775 UniProtKB Chain 1 265 . . . ID=PRO_0000123509;Note=Eukaryotic translation initiation factor 3 subunit J +Q05775 UniProtKB Modified residue 75 75 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q05775 UniProtKB Modified residue 92 92 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05775 UniProtKB Mutagenesis 215 215 . . . Note=Increased association of the eIF-3 complex and 40S ribosomes. R->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16581774;Dbxref=PMID:16581774 +##sequence-region P36053 1 145 +P36053 UniProtKB Chain 1 145 . . . ID=PRO_0000120950;Note=Transcription elongation factor 1 +P36053 UniProtKB Metal binding 25 25 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P60003 +P36053 UniProtKB Metal binding 28 28 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P60003 +P36053 UniProtKB Metal binding 49 49 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P60003 +P36053 UniProtKB Metal binding 52 52 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P60003 +P36053 UniProtKB Modified residue 55 55 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36053 UniProtKB Modified residue 117 117 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P36053 UniProtKB Modified residue 124 124 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P36053 UniProtKB Modified residue 142 142 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P25358 1 347 +P25358 UniProtKB Chain 1 347 . . . ID=PRO_0000207549;Note=Elongation of fatty acids protein 2 +P25358 UniProtKB Topological domain 1 62 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P25358 UniProtKB Transmembrane 63 83 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25358 UniProtKB Topological domain 84 96 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P25358 UniProtKB Transmembrane 97 119 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25358 UniProtKB Topological domain 120 122 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P25358 UniProtKB Transmembrane 123 142 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25358 UniProtKB Topological domain 143 146 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P25358 UniProtKB Transmembrane 147 169 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25358 UniProtKB Topological domain 170 200 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P25358 UniProtKB Transmembrane 201 221 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25358 UniProtKB Topological domain 222 231 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P25358 UniProtKB Transmembrane 232 254 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25358 UniProtKB Topological domain 255 275 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P25358 UniProtKB Transmembrane 276 296 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25358 UniProtKB Topological domain 297 347 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +P25358 UniProtKB Motif 344 347 . . . Note=Di-lysine-like motif;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9832547;Dbxref=PMID:9832547 +P25358 UniProtKB Modified residue 334 334 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198 +P25358 UniProtKB Modified residue 336 336 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P25358 UniProtKB Modified residue 338 338 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198 +P25358 UniProtKB Glycosylation 32 32 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +##sequence-region P39013 1 349 +P39013 UniProtKB Chain 1 349 . . . ID=PRO_0000073648;Note=Actin cytoskeleton-regulatory complex protein END3 +P39013 UniProtKB Domain 8 98 . . . Note=EH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00077 +P39013 UniProtKB Domain 130 222 . . . Note=EH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00077 +P39013 UniProtKB Repeat 276 295 . . . Note=1 +P39013 UniProtKB Repeat 315 334 . . . Note=2 +P39013 UniProtKB Region 96 105 . . . Note=Polyphosphoinositide (PIP2)-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39013 UniProtKB Region 276 334 . . . Note=2 X 20 AA approximate repeats +P39013 UniProtKB Coiled coil 307 349 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39013 UniProtKB Compositional bias 53 64 . . . Note=Asp/Glu-rich (acidic) +P39013 UniProtKB Modified residue 276 276 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39013 UniProtKB Natural variant 245 245 . . . Note=In strain: YJM 421. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11907579;Dbxref=PMID:11907579 +P39013 UniProtKB Natural variant 258 258 . . . Note=In strain: YJM 280%2C YJM 320%2C YJM 326%2C YJM 627%2C YJM 789 and YJM 1129. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11907579;Dbxref=PMID:11907579 +P39013 UniProtKB Natural variant 268 268 . . . Note=In strain: SK1%2C YJM 269%2C YJM 270%2C YJM 280%2C YJM 320%2C YJM 326%2C YJM 339%2C YJM 421%2C YJM 627%2C YJM 789 and YJM 1129. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11907579,ECO:0000269|PubMed:16273108;Dbxref=PMID:11907579,PMID:16273108 +##sequence-region P32626 1 227 +P32626 UniProtKB Chain 1 227 . . . ID=PRO_0000065746;Note=Enolase-phosphatase E1 +P32626 UniProtKB Region 118 119 . . . Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03117 +P32626 UniProtKB Metal binding 11 11 . . . Note=Magnesium;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03117,ECO:0000269|Ref.7 +P32626 UniProtKB Metal binding 13 13 . . . Note=Magnesium%3B via carbonyl oxygen;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03117,ECO:0000269|Ref.7 +P32626 UniProtKB Metal binding 186 186 . . . Note=Magnesium;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03117,ECO:0000269|Ref.7 +P32626 UniProtKB Binding site 161 161 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03117 +P32626 UniProtKB Sequence conflict 56 57 . . . Note=ID->MH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32626 UniProtKB Sequence conflict 56 57 . . . Note=ID->MH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32626 UniProtKB Sequence conflict 56 57 . . . Note=ID->MH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32626 UniProtKB Sequence conflict 179 179 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32626 UniProtKB Sequence conflict 179 179 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32626 UniProtKB Sequence conflict 179 179 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32626 UniProtKB Beta strand 6 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Turn 14 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Helix 21 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Helix 26 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Helix 46 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Helix 59 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Helix 77 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Helix 102 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Beta strand 114 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Helix 122 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Helix 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Beta strand 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Helix 155 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Helix 164 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Helix 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Beta strand 181 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Helix 188 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Turn 196 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Beta strand 200 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +P32626 UniProtKB Beta strand 220 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G80 +##sequence-region Q05785 1 613 +Q05785 UniProtKB Chain 1 613 . . . ID=PRO_0000074525;Note=Epsin-2 +Q05785 UniProtKB Domain 11 143 . . . Note=ENTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243 +Q05785 UniProtKB Domain 175 194 . . . Note=UIM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213 +Q05785 UniProtKB Domain 206 225 . . . Note=UIM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213 +Q05785 UniProtKB Compositional bias 138 166 . . . Note=Arg-rich +Q05785 UniProtKB Compositional bias 192 606 . . . Note=Gln-rich +Q05785 UniProtKB Modified residue 165 165 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q05785 UniProtKB Modified residue 167 167 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q05785 UniProtKB Modified residue 430 430 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q05785 UniProtKB Modified residue 434 434 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q05785 UniProtKB Modified residue 450 450 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q05785 UniProtKB Modified residue 468 468 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q05785 UniProtKB Modified residue 470 470 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05785 UniProtKB Cross-link 426 426 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q05785 UniProtKB Helix 18 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC +Q05785 UniProtKB Beta strand 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC +Q05785 UniProtKB Helix 36 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC +Q05785 UniProtKB Helix 49 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC +Q05785 UniProtKB Helix 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC +Q05785 UniProtKB Helix 70 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC +Q05785 UniProtKB Helix 89 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC +Q05785 UniProtKB Helix 99 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC +Q05785 UniProtKB Helix 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC +Q05785 UniProtKB Helix 120 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC +Q05785 UniProtKB Helix 136 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GZC +##sequence-region P53246 1 860 +P53246 UniProtKB Chain 1 860 . . . ID=PRO_0000202806;Note=Late endosome and vacuole interface protein 11 +P53246 UniProtKB Zinc finger 84 138 . . . Note=BED-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00027 +##sequence-region Q12003 1 364 +Q12003 UniProtKB Chain 1 364 . . . ID=PRO_0000255977;Note=Serine/threonine-protein kinase ENV7 +Q12003 UniProtKB Domain 30 364 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12003 UniProtKB Nucleotide binding 36 44 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12003 UniProtKB Active site 215 215 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12003 UniProtKB Binding site 69 69 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12003 UniProtKB Lipidation 13 13 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107 +Q12003 UniProtKB Lipidation 14 14 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107 +Q12003 UniProtKB Lipidation 15 15 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107 +##sequence-region O13529 1 151 +O13529 UniProtKB Chain 1 151 . . . ID=PRO_0000239641;Note=Protein ECM12 +O13529 UniProtKB Transmembrane 17 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13529 UniProtKB Transmembrane 51 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13529 UniProtKB Glycosylation 2 2 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13529 UniProtKB Glycosylation 132 132 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13529 UniProtKB Glycosylation 137 137 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39715 1 212 +P39715 UniProtKB Chain 1 212 . . . ID=PRO_0000086916;Note=Shuttling pre-60S factor ECM1 +P39715 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39715 UniProtKB Sequence conflict 102 102 . . . Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02710 1 187 +Q02710 UniProtKB Chain 1 187 . . . ID=PRO_0000083483;Note=Protein ECM23 +Q02710 UniProtKB Zinc finger 126 180 . . . Note=GATA-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00094 +##sequence-region P34216 1 1381 +P34216 UniProtKB Chain 1 1381 . . . ID=PRO_0000202457;Note=EH domain-containing and endocytosis protein 1 +P34216 UniProtKB Domain 14 113 . . . Note=EH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00077 +P34216 UniProtKB Domain 135 227 . . . Note=EH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00077 +P34216 UniProtKB Domain 277 366 . . . Note=EH 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00077 +P34216 UniProtKB Domain 1338 1380 . . . Note=UBA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212 +P34216 UniProtKB Region 1217 1381 . . . Note=Able to bind biological membranes +P34216 UniProtKB Coiled coil 593 882 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34216 UniProtKB Compositional bias 550 575 . . . Note=Ala-rich +P34216 UniProtKB Modified residue 238 238 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P34216 UniProtKB Modified residue 241 241 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +P34216 UniProtKB Modified residue 244 244 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P34216 UniProtKB Modified residue 245 245 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P34216 UniProtKB Modified residue 248 248 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P34216 UniProtKB Modified residue 249 249 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P34216 UniProtKB Modified residue 251 251 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34216 UniProtKB Modified residue 265 265 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P34216 UniProtKB Modified residue 419 419 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P34216 UniProtKB Modified residue 450 450 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34216 UniProtKB Modified residue 477 477 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34216 UniProtKB Modified residue 487 487 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P34216 UniProtKB Modified residue 495 495 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P34216 UniProtKB Modified residue 848 848 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P34216 UniProtKB Modified residue 931 931 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P34216 UniProtKB Modified residue 950 950 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P34216 UniProtKB Modified residue 964 964 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34216 UniProtKB Modified residue 1008 1008 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34216 UniProtKB Modified residue 1012 1012 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34216 UniProtKB Modified residue 1020 1020 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34216 UniProtKB Modified residue 1046 1046 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34216 UniProtKB Modified residue 1069 1069 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P34216 UniProtKB Modified residue 1087 1087 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P34216 UniProtKB Modified residue 1093 1093 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P34216 UniProtKB Modified residue 1095 1095 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34216 UniProtKB Modified residue 1096 1096 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P34216 UniProtKB Modified residue 1100 1100 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P34216 UniProtKB Modified residue 1111 1111 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P34216 UniProtKB Modified residue 1181 1181 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34216 UniProtKB Modified residue 1187 1187 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34216 UniProtKB Modified residue 1307 1307 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P34216 UniProtKB Modified residue 1343 1343 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34216 UniProtKB Cross-link 674 674 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P34216 UniProtKB Cross-link 1329 1329 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P34216 UniProtKB Mutagenesis 56 56 . . . Note=Abnormal spatiotemporal behavior. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18448668;Dbxref=PMID:18448668 +P34216 UniProtKB Mutagenesis 176 176 . . . Note=Abnormal spatiotemporal behavior. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18448668;Dbxref=PMID:18448668 +P34216 UniProtKB Mutagenesis 319 319 . . . Note=Abnormal spatiotemporal behavior. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18448668;Dbxref=PMID:18448668 +P34216 UniProtKB Mutagenesis 1352 1352 . . . Note=Reduced ubiquitin-binding. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16563434;Dbxref=PMID:16563434 +P34216 UniProtKB Mutagenesis 1370 1370 . . . Note=Reduced ubiquitin-binding. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16563434;Dbxref=PMID:16563434 +P34216 UniProtKB Mutagenesis 1374 1374 . . . Note=Enhanced ubiquitin-binding. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16563434;Dbxref=PMID:16563434 +P34216 UniProtKB Mutagenesis 1378 1378 . . . Note=Reduced ubiquitin-binding. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16563434;Dbxref=PMID:16563434 +P34216 UniProtKB Helix 1341 1350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G3Q +P34216 UniProtKB Turn 1351 1353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G3Q +P34216 UniProtKB Helix 1356 1365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G3Q +P34216 UniProtKB Helix 1370 1378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2G3Q +##sequence-region P36008 1 412 +P36008 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P36008 UniProtKB Chain 2 412 . . . ID=PRO_0000208832;Note=Elongation factor 1-gamma 2 +P36008 UniProtKB Domain 2 77 . . . Note=GST N-terminal +P36008 UniProtKB Domain 86 217 . . . Note=GST C-terminal +P36008 UniProtKB Domain 251 412 . . . Note=EF-1-gamma C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00519 +P36008 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P36008 UniProtKB Sequence conflict 8 8 . . . Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36008 UniProtKB Sequence conflict 347 347 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53978 1 1044 +P53978 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16521 +P53978 UniProtKB Chain 2 1044 . . . ID=PRO_0000093459;Note=Elongation factor 3B +P53978 UniProtKB Repeat 5 42 . . . Note=HEAT 1 +P53978 UniProtKB Repeat 86 123 . . . Note=HEAT 2 +P53978 UniProtKB Repeat 124 162 . . . Note=HEAT 3 +P53978 UniProtKB Repeat 166 203 . . . Note=HEAT 4 +P53978 UniProtKB Repeat 205 241 . . . Note=HEAT 5 +P53978 UniProtKB Repeat 242 279 . . . Note=HEAT 6 +P53978 UniProtKB Repeat 285 323 . . . Note=HEAT 7 +P53978 UniProtKB Domain 426 641 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P53978 UniProtKB Domain 667 993 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P53978 UniProtKB Nucleotide binding 463 470 . . . Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P53978 UniProtKB Nucleotide binding 701 708 . . . Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P53978 UniProtKB Compositional bias 1009 1031 . . . Note=Lys-rich (basic) +P53978 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16521 +P53978 UniProtKB Modified residue 187 187 . . . Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16521 +P53978 UniProtKB Modified residue 196 196 . . . Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16521 +P53978 UniProtKB Modified residue 789 789 . . . Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16521 +P53978 UniProtKB Modified residue 972 972 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16521 +P53978 UniProtKB Modified residue 974 974 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16521 +P53978 UniProtKB Modified residue 1039 1039 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16521 +P53978 UniProtKB Modified residue 1040 1040 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16521 +##sequence-region P12754 1 651 +P12754 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P12754 UniProtKB Chain 2 651 . . . ID=PRO_0000156072;Note=Translation initiation factor eIF-2B subunit delta +P12754 UniProtKB Compositional bias 6 106 . . . Note=Arg/Lys-rich (basic) +P12754 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P12754 UniProtKB Modified residue 106 106 . . . Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12754 UniProtKB Modified residue 121 121 . . . Note=Phosphothreonine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32801 1 640 +P32801 UniProtKB Chain 1 640 . . . ID=PRO_0000085951;Note=Serine/threonine-protein kinase ELM1 +P32801 UniProtKB Domain 88 420 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32801 UniProtKB Nucleotide binding 94 102 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32801 UniProtKB Active site 259 259 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P32801 UniProtKB Binding site 117 117 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32801 UniProtKB Modified residue 152 152 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32801 UniProtKB Modified residue 516 516 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32801 UniProtKB Modified residue 519 519 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32801 UniProtKB Mutagenesis 200 200 . . . Note=Allows selective inhibition in vivo. T->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12917352;Dbxref=PMID:12917352 +P32801 UniProtKB Sequence conflict 390 390 . . . Note=E->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32801 UniProtKB Sequence conflict 484 485 . . . Note=TV->SD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P42935 1 788 +P42935 UniProtKB Chain 1 788 . . . ID=PRO_0000051474;Note=Elongator complex protein 2 +P42935 UniProtKB Repeat 57 87 . . . Note=WD 1 +P42935 UniProtKB Repeat 101 130 . . . Note=WD 2 +P42935 UniProtKB Repeat 141 181 . . . Note=WD 3 +P42935 UniProtKB Repeat 200 234 . . . Note=WD 4 +P42935 UniProtKB Repeat 279 309 . . . Note=WD 5 +P42935 UniProtKB Repeat 383 413 . . . Note=WD 6 +P42935 UniProtKB Repeat 438 466 . . . Note=WD 7 +P42935 UniProtKB Repeat 604 634 . . . Note=WD 8 +P42935 UniProtKB Repeat 651 683 . . . Note=WD 9 +P42935 UniProtKB Sequence conflict 579 579 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P42935 UniProtKB Beta strand 4 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 20 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Turn 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 30 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 37 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 51 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 62 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 69 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 83 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 94 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 107 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 116 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 124 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 133 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 138 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 153 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 165 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 188 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 205 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 214 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XFV +P42935 UniProtKB Beta strand 218 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 228 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 259 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 267 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 280 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 291 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 296 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 303 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Turn 312 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 317 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 344 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 352 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 364 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 376 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 384 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XFV +P42935 UniProtKB Beta strand 388 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 398 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Turn 405 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 408 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 429 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 442 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 460 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Helix 469 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Helix 539 544 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 550 555 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 561 566 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 572 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 581 583 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 586 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Turn 592 594 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 597 603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 609 614 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 618 625 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 626 628 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XFV +P42935 UniProtKB Beta strand 630 636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Turn 637 640 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 641 651 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 656 661 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Helix 664 666 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 668 674 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 677 685 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 687 699 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 704 709 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 717 724 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 729 735 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 738 744 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Turn 747 749 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 755 760 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 768 775 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +P42935 UniProtKB Beta strand 780 786 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M2N +##sequence-region P40540 1 141 +P40540 UniProtKB Chain 1 141 . . . ID=PRO_0000202998;Note=ER membrane protein complex subunit 5 +P40540 UniProtKB Topological domain 1 6 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40540 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40540 UniProtKB Topological domain 28 48 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40540 UniProtKB Transmembrane 49 69 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40540 UniProtKB Topological domain 70 141 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12431 1 108 +Q12431 UniProtKB Chain 1 108 . . . ID=PRO_0000247112;Note=ER membrane protein complex subunit 6 +Q12431 UniProtKB Transmembrane 24 44 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12431 UniProtKB Transmembrane 49 69 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12431 UniProtKB Transmembrane 88 108 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P42842 1 904 +P42842 UniProtKB Chain 1 904 . . . ID=PRO_0000203365;Note=Essential for maintenance of the cell wall protein 1 +P42842 UniProtKB Repeat 510 544 . . . Note=TPR 1 +P42842 UniProtKB Repeat 563 596 . . . Note=TPR 2 +P42842 UniProtKB Repeat 603 636 . . . Note=TPR 3 +P42842 UniProtKB Repeat 637 670 . . . Note=TPR 4 +P42842 UniProtKB Repeat 671 704 . . . Note=TPR 5 +P42842 UniProtKB Repeat 706 739 . . . Note=TPR 6 +P42842 UniProtKB Compositional bias 149 158 . . . Note=Poly-Leu +##sequence-region P18414 1 219 +P18414 UniProtKB Chain 1 219 . . . ID=PRO_0000194171;Note=ER lumen protein-retaining receptor +P18414 UniProtKB Topological domain 1 2 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18414 UniProtKB Transmembrane 3 21 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18414 UniProtKB Topological domain 22 35 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18414 UniProtKB Transmembrane 36 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18414 UniProtKB Topological domain 54 62 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18414 UniProtKB Transmembrane 63 82 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18414 UniProtKB Topological domain 83 102 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18414 UniProtKB Transmembrane 103 116 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18414 UniProtKB Topological domain 117 123 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18414 UniProtKB Transmembrane 124 143 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18414 UniProtKB Topological domain 144 155 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18414 UniProtKB Transmembrane 156 174 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18414 UniProtKB Topological domain 175 185 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18414 UniProtKB Transmembrane 186 206 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18414 UniProtKB Topological domain 207 219 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06551 1 359 +Q06551 UniProtKB Chain 1 359 . . . ID=PRO_0000212948;Note=Palmitoyltransferase ERF2 +Q06551 UniProtKB Topological domain 1 75 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06551 UniProtKB Transmembrane 76 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06551 UniProtKB Topological domain 97 104 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06551 UniProtKB Transmembrane 105 125 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06551 UniProtKB Topological domain 126 217 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06551 UniProtKB Transmembrane 218 238 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06551 UniProtKB Topological domain 239 250 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06551 UniProtKB Transmembrane 251 271 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06551 UniProtKB Topological domain 272 359 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06551 UniProtKB Domain 173 223 . . . Note=DHHC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00067 +Q06551 UniProtKB Mutagenesis 173 173 . . . Note=In ERF2-1%3B loss of function. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10490616;Dbxref=PMID:10490616 +Q06551 UniProtKB Mutagenesis 182 182 . . . Note=In ERF2-7%3B loss of function. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10490616;Dbxref=PMID:10490616 +Q06551 UniProtKB Mutagenesis 189 189 . . . Note=Abolishes palmitoyltransferase activity and interaction with SHR5. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10490616,ECO:0000269|PubMed:12193598;Dbxref=PMID:10490616,PMID:12193598 +Q06551 UniProtKB Mutagenesis 200 200 . . . Note=Loss of function. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10490616;Dbxref=PMID:10490616 +Q06551 UniProtKB Mutagenesis 201 201 . . . Note=Abolishes palmitoyltransferase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12193598;Dbxref=PMID:12193598 +Q06551 UniProtKB Mutagenesis 203 203 . . . Note=Abolishes palmitoyltransferase activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12193598;Dbxref=PMID:12193598 +Q06551 UniProtKB Mutagenesis 218 218 . . . Note=In ERF2-2%3B loss of function. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10490616;Dbxref=PMID:10490616 +Q06551 UniProtKB Sequence conflict 68 68 . . . Note=R->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32476 1 496 +P32476 UniProtKB Chain 1 496 . . . ID=PRO_0000209851;Note=Squalene monooxygenase +P32476 UniProtKB Topological domain 1 16 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32476 UniProtKB Transmembrane 17 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32476 UniProtKB Topological domain 38 474 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32476 UniProtKB Transmembrane 475 495 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32476 UniProtKB Topological domain 496 496 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32476 UniProtKB Nucleotide binding 21 48 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32476 UniProtKB Cross-link 284 284 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14557538;Dbxref=PMID:14557538 +P32476 UniProtKB Cross-link 289 289 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32476 UniProtKB Cross-link 311 311 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32476 UniProtKB Natural variant 251 251 . . . Note=In strain: A2-M8%3B confers resistance to the allylamine antifungal terbinafine. L->F +##sequence-region P53199 1 349 +P53199 UniProtKB Chain 1 349 . . . ID=PRO_0000087798;Note=Sterol-4-alpha-carboxylate 3-dehydrogenase%2C decarboxylating +P53199 UniProtKB Active site 151 151 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53199 UniProtKB Binding site 155 155 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P0CX10 1 437 +P0CX10 UniProtKB Chain 1 437 . . . ID=PRO_0000134064;Note=Enolase-related protein 1 +P0CX10 UniProtKB Region 373 376 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX10 UniProtKB Active site 212 212 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX10 UniProtKB Active site 346 346 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX10 UniProtKB Metal binding 247 247 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX10 UniProtKB Metal binding 296 296 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX10 UniProtKB Metal binding 321 321 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX10 UniProtKB Binding site 160 160 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX10 UniProtKB Binding site 169 169 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX10 UniProtKB Binding site 296 296 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX10 UniProtKB Binding site 321 321 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX10 UniProtKB Binding site 397 397 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX10 UniProtKB Sequence conflict 231 231 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53337 1 310 +P53337 UniProtKB Chain 1 310 . . . ID=PRO_0000127671;Note=ER-derived vesicles protein ERV29 +P53337 UniProtKB Topological domain 1 108 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53337 UniProtKB Transmembrane 109 129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53337 UniProtKB Topological domain 130 137 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53337 UniProtKB Transmembrane 138 158 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53337 UniProtKB Topological domain 159 160 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53337 UniProtKB Transmembrane 161 181 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53337 UniProtKB Topological domain 182 209 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53337 UniProtKB Transmembrane 210 230 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53337 UniProtKB Topological domain 231 245 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53337 UniProtKB Transmembrane 246 266 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53337 UniProtKB Topological domain 267 282 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53337 UniProtKB Transmembrane 283 303 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53337 UniProtKB Topological domain 304 310 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53337 UniProtKB Motif 307 310 . . . Note=Di-lysine motif +P53337 UniProtKB Sequence conflict 64 64 . . . Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12168 1 779 +Q12168 UniProtKB Chain 1 779 . . . ID=PRO_0000215819;Note=Endo-1%2C3(4)-beta-glucanase 2 +##sequence-region Q99382 1 181 +Q99382 UniProtKB Chain 1 181 . . . ID=PRO_0000247246;Note=SRP-independent targeting protein 2 +Q99382 UniProtKB Topological domain 1 15 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q99382 UniProtKB Transmembrane 16 36 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99382 UniProtKB Topological domain 37 45 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q99382 UniProtKB Transmembrane 46 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99382 UniProtKB Topological domain 67 89 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q99382 UniProtKB Transmembrane 90 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99382 UniProtKB Topological domain 111 112 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q99382 UniProtKB Transmembrane 113 133 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99382 UniProtKB Topological domain 134 181 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +##sequence-region P22140 1 391 +P22140 UniProtKB Chain 1 391 . . . ID=PRO_0000056809;Note=Choline/ethanolaminephosphotransferase 1 +P22140 UniProtKB Topological domain 1 49 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22140 UniProtKB Transmembrane 50 69 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22140 UniProtKB Topological domain 70 172 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22140 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22140 UniProtKB Topological domain 194 211 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22140 UniProtKB Transmembrane 212 232 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22140 UniProtKB Topological domain 233 264 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22140 UniProtKB Transmembrane 265 282 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22140 UniProtKB Topological domain 283 285 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22140 UniProtKB Transmembrane 286 308 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22140 UniProtKB Topological domain 309 321 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22140 UniProtKB Transmembrane 322 342 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22140 UniProtKB Topological domain 343 346 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22140 UniProtKB Transmembrane 347 367 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22140 UniProtKB Topological domain 368 391 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22140 UniProtKB Sequence conflict 96 96 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22140 UniProtKB Sequence conflict 98 98 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38819 1 212 +P38819 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38819 UniProtKB Chain 21 212 . . . ID=PRO_0000010412;Note=Protein ERP5 +P38819 UniProtKB Topological domain 21 178 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38819 UniProtKB Transmembrane 179 199 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38819 UniProtKB Topological domain 200 212 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38819 UniProtKB Domain 31 124 . . . Note=GOLD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00096 +P38819 UniProtKB Glycosylation 171 171 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38312 1 142 +P38312 UniProtKB Chain 1 142 . . . ID=PRO_0000122237;Note=ER-derived vesicles protein ERV15 +P38312 UniProtKB Topological domain 1 7 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38312 UniProtKB Transmembrane 8 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38312 UniProtKB Topological domain 29 55 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38312 UniProtKB Transmembrane 56 76 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38312 UniProtKB Topological domain 77 114 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38312 UniProtKB Transmembrane 115 135 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38312 UniProtKB Topological domain 136 142 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08649 1 445 +Q08649 UniProtKB Chain 1 445 . . . ID=PRO_0000051562;Note=Histone acetyltransferase ESA1 +Q08649 UniProtKB Domain 33 86 . . . Note=Chromo +Q08649 UniProtKB Domain 162 433 . . . Note=MYST-type HAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063 +Q08649 UniProtKB Zinc finger 195 220 . . . Note=C2HC MYST-type%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063 +Q08649 UniProtKB Region 303 307 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11106757,ECO:0000269|PubMed:12368900,ECO:0000269|PubMed:22020126;Dbxref=PMID:11106757,PMID:12368900,PMID:22020126 +Q08649 UniProtKB Region 312 318 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11106757,ECO:0000269|PubMed:12368900,ECO:0000269|PubMed:22020126;Dbxref=PMID:11106757,PMID:12368900,PMID:22020126 +Q08649 UniProtKB Motif 245 266 . . . Note=ESA1-RPD3 motif +Q08649 UniProtKB Active site 338 338 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000305;evidence=ECO:0000303|PubMed:12368900,ECO:0000303|PubMed:17223684,ECO:0000303|PubMed:18245364,ECO:0000303|PubMed:22020126,ECO:0000305;Dbxref=PMID:12368900,PMID:17223684,PMID:18245364,PMID:22020126 +Q08649 UniProtKB Binding site 342 342 . . . Note=Acetyl-CoA;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11106757,ECO:0000269|PubMed:12368900,ECO:0000269|PubMed:22020126;Dbxref=PMID:11106757,PMID:12368900,PMID:22020126 +Q08649 UniProtKB Site 304 304 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08649 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q08649 UniProtKB Modified residue 262 262 . . . Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22020126;Dbxref=PMID:22020126 +Q08649 UniProtKB Mutagenesis 247 247 . . . Note=Strongly reduces HAT activity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +Q08649 UniProtKB Mutagenesis 250 250 . . . Note=Strongly reduces HAT activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +Q08649 UniProtKB Mutagenesis 251 251 . . . Note=Strongly reduces HAT activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +Q08649 UniProtKB Mutagenesis 252 252 . . . Note=Strongly reduces HAT activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +Q08649 UniProtKB Mutagenesis 253 253 . . . Note=Strongly reduces HAT activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +Q08649 UniProtKB Mutagenesis 254 254 . . . Note=Strongly reduces HAT activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +Q08649 UniProtKB Mutagenesis 256 256 . . . Note=Strongly reduces HAT activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +Q08649 UniProtKB Mutagenesis 259 259 . . . Note=Strongly reduces HAT activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +Q08649 UniProtKB Mutagenesis 260 260 . . . Note=Strongly reduces HAT activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +Q08649 UniProtKB Mutagenesis 262 262 . . . Note=Strongly reduces HAT activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +Q08649 UniProtKB Mutagenesis 262 262 . . . Note=Strongly reduces HAT activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22020126;Dbxref=PMID:22020126 +Q08649 UniProtKB Mutagenesis 304 304 . . . Note=Reduces HAT activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17223684;Dbxref=PMID:17223684 +Q08649 UniProtKB Mutagenesis 304 304 . . . Note=Strongly reduces HAT activity%2C but is not lethal (in vivo). Lethal%2C when associated with Q-338. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12368900,ECO:0000269|PubMed:17223684,ECO:0000269|PubMed:18245364;Dbxref=PMID:12368900,PMID:17223684,PMID:18245364 +Q08649 UniProtKB Mutagenesis 315 315 . . . Note=Loss of function. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9520405;Dbxref=PMID:9520405 +Q08649 UniProtKB Mutagenesis 338 338 . . . Note=Strongly reduces HAT activity at pH 9.2. Nearly abolishes HAT activity at pH 8.0%2C but is not lethal (in vivo). Lethal%3B when associated with S-334. E->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12368900,ECO:0000269|PubMed:17223684,ECO:0000269|PubMed:18245364;Dbxref=PMID:12368900,PMID:17223684,PMID:18245364 +Q08649 UniProtKB Beta strand 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RO0 +Q08649 UniProtKB Helix 18 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNZ +Q08649 UniProtKB Beta strand 25 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNZ +Q08649 UniProtKB Beta strand 35 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNZ +Q08649 UniProtKB Beta strand 46 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNZ +Q08649 UniProtKB Beta strand 51 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNZ +Q08649 UniProtKB Beta strand 65 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNZ +Q08649 UniProtKB Turn 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNZ +Q08649 UniProtKB Beta strand 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNZ +Q08649 UniProtKB Beta strand 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RO0 +Q08649 UniProtKB Helix 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +Q08649 UniProtKB Beta strand 169 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Beta strand 175 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Helix 187 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9T +Q08649 UniProtKB Beta strand 194 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Turn 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Beta strand 204 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Helix 208 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Beta strand 224 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Beta strand 232 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Helix 241 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Helix 245 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Beta strand 271 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Beta strand 283 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Beta strand 300 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Beta strand 305 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Helix 309 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Beta strand 313 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FY7 +Q08649 UniProtKB Helix 316 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Beta strand 335 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Helix 343 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Beta strand 366 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Helix 370 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Helix 381 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Beta strand 394 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Beta strand 400 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Helix 407 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Helix 426 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TO7 +Q08649 UniProtKB Turn 438 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J9U +##sequence-region Q06340 1 456 +Q06340 UniProtKB Chain 1 456 . . . ID=PRO_0000227693;Note=Protein ESC2 +Q06340 UniProtKB Repeat 169 287 . . . Note=SUMO-like region 1 +Q06340 UniProtKB Repeat 380 456 . . . Note=SUMO-like region 2 +Q06340 UniProtKB Coiled coil 301 360 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06340 UniProtKB Modified residue 90 90 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06340 UniProtKB Modified residue 125 125 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06340 UniProtKB Modified residue 126 126 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q06344 1 628 +Q06344 UniProtKB Chain 1 628 . . . ID=PRO_0000228158;Note=Pre-rRNA-processing protein ESF1 +Q06344 UniProtKB Coiled coil 426 495 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06344 UniProtKB Modified residue 86 86 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06344 UniProtKB Modified residue 220 220 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q06344 UniProtKB Modified residue 223 223 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06344 UniProtKB Modified residue 225 225 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +Q06344 UniProtKB Modified residue 367 367 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q06344 UniProtKB Modified residue 369 369 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06344 UniProtKB Modified residue 372 372 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06344 UniProtKB Modified residue 542 542 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P22696 1 170 +P22696 UniProtKB Chain 1 170 . . . ID=PRO_0000193433;Note=Peptidyl-prolyl cis-trans isomerase ESS1 +P22696 UniProtKB Domain 9 43 . . . Note=WW;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00224 +P22696 UniProtKB Domain 57 170 . . . Note=PpiC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00278 +P22696 UniProtKB Modified residue 161 161 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P22696 UniProtKB Mutagenesis 120 120 . . . Note=Abolishes PPIase activity. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15728580;Dbxref=PMID:15728580 +P22696 UniProtKB Mutagenesis 122 122 . . . Note=Abolishes PPIase activity. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15728580;Dbxref=PMID:15728580 +P22696 UniProtKB Mutagenesis 127 127 . . . Note=In PTF1-2%3B decreases the catalytic efficiency 20-fold. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9867817;Dbxref=PMID:9867817 +P22696 UniProtKB Mutagenesis 162 162 . . . Note=In PTF1-5%3B decreases the catalytic efficiency 12-fold. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9867817;Dbxref=PMID:9867817 +P22696 UniProtKB Mutagenesis 164 164 . . . Note=Abolishes PPIase activity. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15728580;Dbxref=PMID:15728580 +P22696 UniProtKB Sequence conflict 8 8 . . . Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22696 UniProtKB Sequence conflict 17 17 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22696 UniProtKB Sequence conflict 128 128 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32474 1 517 +P32474 UniProtKB Signal peptide 1 29 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32474 UniProtKB Chain 30 517 . . . ID=PRO_0000034219;Note=Protein disulfide-isomerase EUG1 +P32474 UniProtKB Domain 30 141 . . . Note=Thioredoxin 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +P32474 UniProtKB Domain 355 487 . . . Note=Thioredoxin 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +P32474 UniProtKB Motif 514 517 . . . Note=Prevents secretion from ER +P32474 UniProtKB Glycosylation 159 159 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32474 UniProtKB Glycosylation 174 174 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32474 UniProtKB Glycosylation 207 207 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32474 UniProtKB Glycosylation 293 293 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32474 UniProtKB Glycosylation 462 462 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32474 UniProtKB Mutagenesis 65 65 . . . Note=Increases PDI activity. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11485577;Dbxref=PMID:11485577 +P32474 UniProtKB Mutagenesis 408 408 . . . Note=Increases PDI activity. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11485577;Dbxref=PMID:11485577 +P32474 UniProtKB Sequence conflict 364 364 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P02992 1 437 +P02992 UniProtKB Transit peptide 1 38 . . . Note=Mitochondrion;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02992 UniProtKB Chain 39 437 . . . ID=PRO_0000007465;Note=Elongation factor Tu%2C mitochondrial +P02992 UniProtKB Domain 46 242 . . . Note=tr-type G +P02992 UniProtKB Nucleotide binding 55 62 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P02992 UniProtKB Nucleotide binding 117 121 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P02992 UniProtKB Nucleotide binding 172 175 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P02992 UniProtKB Region 55 62 . . . Note=G1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P02992 UniProtKB Region 96 100 . . . Note=G2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P02992 UniProtKB Region 117 120 . . . Note=G3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P02992 UniProtKB Region 172 175 . . . Note=G4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P02992 UniProtKB Region 210 212 . . . Note=G5;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q06706 1 1349 +Q06706 UniProtKB Chain 1 1349 . . . ID=PRO_0000084179;Note=Elongator complex protein 1 +Q06706 UniProtKB Helix 923 930 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 934 943 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 948 950 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 952 959 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 963 974 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 977 984 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 995 1004 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 1007 1013 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 1014 1016 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 1018 1032 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Turn 1033 1036 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 1038 1047 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 1051 1060 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 1064 1073 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Turn 1076 1078 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 1079 1092 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 1096 1107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 1110 1119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 1123 1132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 1138 1141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 1143 1170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 1253 1282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 1286 1308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +Q06706 UniProtKB Helix 1345 1347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CQS +##sequence-region Q02908 1 557 +Q02908 UniProtKB Chain 1 557 . . . ID=PRO_0000235811;Note=Elongator complex protein 3 +Q02908 UniProtKB Domain 405 557 . . . Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532 +Q02908 UniProtKB Metal binding 108 108 . . . Note=Iron-sulfur (4Fe-4S-S-AdoMet);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16420352;Dbxref=PMID:16420352 +Q02908 UniProtKB Metal binding 118 118 . . . Note=Iron-sulfur (4Fe-4S-S-AdoMet);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16420352;Dbxref=PMID:16420352 +Q02908 UniProtKB Metal binding 121 121 . . . Note=Iron-sulfur (4Fe-4S-S-AdoMet);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16420352;Dbxref=PMID:16420352 +Q02908 UniProtKB Cross-link 453 453 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +Q02908 UniProtKB Mutagenesis 108 108 . . . Note=Eliminates iron contents%3B when associated with S-118 and S-121. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16420352;Dbxref=PMID:16420352 +Q02908 UniProtKB Mutagenesis 118 118 . . . Note=Eliminates iron contents%3B when associated with S-108 and S-121. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16420352;Dbxref=PMID:16420352 +Q02908 UniProtKB Mutagenesis 121 121 . . . Note=Eliminates iron contents%3B when associated with S-108 and S-118. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16420352;Dbxref=PMID:16420352 +##sequence-region P00925 1 437 +P00925 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8935650,ECO:0000269|Ref.4;Dbxref=PMID:8935650 +P00925 UniProtKB Chain 2 437 . . . ID=PRO_0000134063;Note=Enolase 2 +P00925 UniProtKB Active site 160 160 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00925 UniProtKB Metal binding 247 247 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00925 UniProtKB Metal binding 296 296 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00925 UniProtKB Metal binding 321 321 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00925 UniProtKB Modified residue 138 138 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00925 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P00925 UniProtKB Modified residue 313 313 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00925 UniProtKB Modified residue 324 324 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P00925 UniProtKB Cross-link 60 60 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00925 UniProtKB Cross-link 243 243 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00925 UniProtKB Cross-link 358 358 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q12518 1 454 +Q12518 UniProtKB Chain 1 454 . . . ID=PRO_0000074524;Note=Epsin-1 +Q12518 UniProtKB Domain 11 143 . . . Note=ENTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243 +Q12518 UniProtKB Domain 165 184 . . . Note=UIM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213 +Q12518 UniProtKB Domain 189 208 . . . Note=UIM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213 +Q12518 UniProtKB Region 447 454 . . . Note=Clathrin-binding +Q12518 UniProtKB Compositional bias 211 349 . . . Note=Gln-rich +Q12518 UniProtKB Modified residue 160 160 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12518 UniProtKB Modified residue 163 163 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12518 UniProtKB Modified residue 180 180 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12518 UniProtKB Modified residue 328 328 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12518 UniProtKB Modified residue 364 364 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12518 UniProtKB Modified residue 366 366 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12518 UniProtKB Modified residue 384 384 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12518 UniProtKB Modified residue 386 386 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12518 UniProtKB Modified residue 388 388 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12518 UniProtKB Modified residue 395 395 . . . Note=Phosphothreonine%3B by PRK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11694597;Dbxref=PMID:11694597 +Q12518 UniProtKB Modified residue 415 415 . . . Note=Phosphothreonine%3B by PRK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11694597;Dbxref=PMID:11694597 +Q12518 UniProtKB Cross-link 357 357 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q12518 UniProtKB Mutagenesis 395 395 . . . Note=No phosphorylation. T->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11694597;Dbxref=PMID:11694597 +Q12518 UniProtKB Mutagenesis 415 415 . . . Note=No phosphorylation. T->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11694597;Dbxref=PMID:11694597 +Q12518 UniProtKB Helix 18 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ +Q12518 UniProtKB Helix 36 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ +Q12518 UniProtKB Helix 49 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ +Q12518 UniProtKB Helix 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ +Q12518 UniProtKB Helix 70 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ +Q12518 UniProtKB Helix 89 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ +Q12518 UniProtKB Helix 99 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ +Q12518 UniProtKB Helix 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ +Q12518 UniProtKB Helix 119 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ +Q12518 UniProtKB Helix 136 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LOZ +##sequence-region P47160 1 408 +P47160 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P47160 UniProtKB Chain 2 408 . . . ID=PRO_0000074526;Note=Epsin-3 +P47160 UniProtKB Domain 24 157 . . . Note=ENTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243 +P47160 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P47160 UniProtKB Modified residue 196 196 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47160 UniProtKB Modified residue 198 198 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47160 UniProtKB Modified residue 203 203 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P47160 UniProtKB Modified residue 212 212 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47160 UniProtKB Modified residue 223 223 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47160 UniProtKB Mutagenesis 272 272 . . . Note=Reduced binding to GGA2. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12483220;Dbxref=PMID:12483220 +P47160 UniProtKB Mutagenesis 275 275 . . . Note=Reduced binding to GGA2. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12483220;Dbxref=PMID:12483220 +P47160 UniProtKB Helix 31 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONK +P47160 UniProtKB Helix 49 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONK +P47160 UniProtKB Helix 62 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONK +P47160 UniProtKB Helix 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONL +P47160 UniProtKB Helix 84 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONK +P47160 UniProtKB Helix 103 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONK +P47160 UniProtKB Helix 113 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONK +P47160 UniProtKB Helix 118 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONK +P47160 UniProtKB Helix 133 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONK +P47160 UniProtKB Helix 150 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONK +##sequence-region Q03769 1 411 +Q03769 UniProtKB Chain 1 411 . . . ID=PRO_0000074528;Note=Epsin-5 +Q03769 UniProtKB Domain 25 184 . . . Note=ENTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243 +Q03769 UniProtKB Compositional bias 304 323 . . . Note=Asn-rich +Q03769 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q03769 UniProtKB Modified residue 322 322 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03769 UniProtKB Modified residue 324 324 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03769 UniProtKB Modified residue 363 363 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03769 UniProtKB Modified residue 368 368 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03769 UniProtKB Modified residue 394 394 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q03769 UniProtKB Modified residue 401 401 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03769 UniProtKB Mutagenesis 331 331 . . . Note=Reduced binding to GGA2. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12483220;Dbxref=PMID:12483220 +Q03769 UniProtKB Mutagenesis 334 334 . . . Note=Reduced binding to GGA2. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12483220;Dbxref=PMID:12483220 +Q03769 UniProtKB Helix 32 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08 +Q03769 UniProtKB Beta strand 43 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08 +Q03769 UniProtKB Helix 50 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08 +Q03769 UniProtKB Helix 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08 +Q03769 UniProtKB Helix 65 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08 +Q03769 UniProtKB Helix 87 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08 +Q03769 UniProtKB Turn 96 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08 +Q03769 UniProtKB Helix 101 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08 +Q03769 UniProtKB Helix 123 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08 +Q03769 UniProtKB Helix 137 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08 +Q03769 UniProtKB Turn 141 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08 +Q03769 UniProtKB Helix 156 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08 +Q03769 UniProtKB Helix 177 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08 +Q03769 UniProtKB Turn 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J08 +##sequence-region Q08651 1 330 +Q08651 UniProtKB Chain 1 330 . . . ID=PRO_0000245256;Note=Probable oxidoreductase ENV9 +Q08651 UniProtKB Transmembrane 27 47 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08651 UniProtKB Transmembrane 245 265 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08651 UniProtKB Nucleotide binding 47 53 . . . Note=NAD or NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08651 UniProtKB Active site 202 202 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08651 UniProtKB Binding site 173 173 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08651 UniProtKB Glycosylation 282 282 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P25340 1 473 +P25340 UniProtKB Chain 1 473 . . . ID=PRO_0000207491;Note=Delta(24(24(1)))-sterol reductase +P25340 UniProtKB Topological domain 1 39 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25340 UniProtKB Transmembrane 40 64 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25340 UniProtKB Topological domain 65 101 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25340 UniProtKB Transmembrane 102 123 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25340 UniProtKB Topological domain 124 138 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25340 UniProtKB Transmembrane 139 157 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25340 UniProtKB Topological domain 158 174 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25340 UniProtKB Transmembrane 175 197 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25340 UniProtKB Topological domain 198 232 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25340 UniProtKB Transmembrane 233 249 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25340 UniProtKB Topological domain 250 326 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25340 UniProtKB Transmembrane 327 346 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25340 UniProtKB Topological domain 347 414 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25340 UniProtKB Transmembrane 415 439 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25340 UniProtKB Topological domain 440 473 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25340 UniProtKB Sequence conflict 33 33 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25340 UniProtKB Sequence conflict 366 366 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25340 UniProtKB Sequence conflict 366 366 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25087 1 383 +P25087 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P25087 UniProtKB Chain 2 383 . . . ID=PRO_0000124799;Note=Sterol 24-C-methyltransferase +P25087 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P25087 UniProtKB Modified residue 99 99 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25087 UniProtKB Sequence conflict 380 380 . . . Note=E->EE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P24521 1 451 +P24521 UniProtKB Chain 1 451 . . . ID=PRO_0000156671;Note=Phosphomevalonate kinase +P24521 UniProtKB Nucleotide binding 150 160 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P24521 UniProtKB Sequence conflict 213 213 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24521 UniProtKB Sequence conflict 418 423 . . . Note=TANDKR->PLMTKD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12450 1 207 +Q12450 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12450 UniProtKB Chain 22 207 . . . ID=PRO_0000010411;Note=Protein ERP4 +Q12450 UniProtKB Topological domain 22 174 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12450 UniProtKB Transmembrane 175 195 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12450 UniProtKB Topological domain 196 207 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12450 UniProtKB Domain 36 118 . . . Note=GOLD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00096 +##sequence-region P40456 1 1118 +P40456 UniProtKB Chain 1 1118 . . . ID=PRO_0000202957;Note=EST/SMG-like protein 1 +P40456 UniProtKB Domain 947 1087 . . . Note=PINc;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40456 UniProtKB Modified residue 170 170 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40456 UniProtKB Modified residue 190 190 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q03018 1 1630 +Q03018 UniProtKB Chain 1 1630 . . . ID=PRO_0000205904;Note=Separin +Q03018 UniProtKB Domain 1443 1542 . . . Note=Peptidase C50 +Q03018 UniProtKB Active site 1531 1531 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03018 UniProtKB Mutagenesis 1568 1570 . . . Note=Reduces function. Loss of function. DKD->AKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11149918;Dbxref=PMID:11149918 +Q03018 UniProtKB Sequence conflict 136 136 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03018 UniProtKB Sequence conflict 250 253 . . . Note=TVEC->IRRV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03018 UniProtKB Sequence conflict 540 540 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03018 UniProtKB Sequence conflict 636 636 . . . Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03018 UniProtKB Sequence conflict 782 782 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03018 UniProtKB Sequence conflict 800 800 . . . Note=A->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03018 UniProtKB Sequence conflict 1146 1146 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03018 UniProtKB Sequence conflict 1295 1295 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03018 UniProtKB Sequence conflict 1333 1336 . . . Note=QEID->ARKSI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03018 UniProtKB Sequence conflict 1443 1443 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03018 UniProtKB Helix 54 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1S +Q03018 UniProtKB Helix 75 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1S +Q03018 UniProtKB Helix 82 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 103 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 125 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 147 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Turn 157 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 163 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 180 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 194 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Turn 198 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 206 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 224 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 242 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 251 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Turn 261 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 267 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 273 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 286 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1S +Q03018 UniProtKB Helix 292 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 298 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 320 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 324 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1S +Q03018 UniProtKB Helix 332 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 353 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 376 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 399 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 422 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 442 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Turn 462 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 465 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 482 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 495 498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 504 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 519 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 535 543 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 552 554 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 557 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 574 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 586 590 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 591 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 612 622 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 624 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 627 630 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 636 651 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 655 667 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 669 672 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Turn 673 675 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 676 689 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 693 706 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 709 712 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 714 723 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 727 729 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 730 732 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 734 742 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 744 748 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 750 753 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 763 786 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 790 809 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 810 812 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1S +Q03018 UniProtKB Helix 816 839 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 843 859 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 863 879 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 883 897 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Turn 902 904 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 906 915 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 919 925 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 927 930 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 931 933 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 939 946 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 953 955 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 958 960 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 961 980 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 984 989 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 994 997 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1046 1062 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1065 1067 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1070 1088 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1096 1106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1109 1122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1126 1130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1145 1161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 1165 1173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Turn 1175 1177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 1180 1186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Turn 1187 1190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 1191 1197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1214 1232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1234 1237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1243 1271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Turn 1272 1275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1276 1279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1286 1303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1305 1309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1313 1315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1S +Q03018 UniProtKB Helix 1321 1328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1337 1354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1361 1363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1366 1381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 1390 1396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1398 1400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1405 1407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Turn 1409 1413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 1416 1420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1422 1431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Turn 1432 1434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 1436 1441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 1446 1450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1457 1470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 1478 1483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1487 1495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 1498 1505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Turn 1509 1511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1514 1517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 1526 1528 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Turn 1531 1534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 1537 1539 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1S +Q03018 UniProtKB Beta strand 1542 1545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1S +Q03018 UniProtKB Helix 1547 1553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 1557 1564 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1568 1582 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1598 1605 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Helix 1606 1608 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 1609 1611 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Turn 1612 1617 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 1619 1623 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +Q03018 UniProtKB Beta strand 1626 1629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +##sequence-region Q07872 1 247 +Q07872 UniProtKB Chain 1 247 . . . ID=PRO_0000074527;Note=Epsin-4 +Q07872 UniProtKB Domain 7 146 . . . Note=ENTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243 +Q07872 UniProtKB Modified residue 195 195 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40557 1 701 +P40557 UniProtKB Signal peptide 1 27 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40557 UniProtKB Chain 28 701 . . . ID=PRO_0000034221;Note=ER-retained PMA1-suppressing protein 1 +P40557 UniProtKB Transmembrane 646 666 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40557 UniProtKB Domain 28 142 . . . Note=Thioredoxin 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +P40557 UniProtKB Domain 408 446 . . . Note=Thioredoxin 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +P40557 UniProtKB Glycosylation 85 85 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40557 UniProtKB Glycosylation 264 264 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40557 UniProtKB Glycosylation 299 299 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40557 UniProtKB Glycosylation 370 370 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40557 UniProtKB Disulfide bond 60 63 . . . Note=Redox-active;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +P40557 UniProtKB Disulfide bond 200 203 . . . Note=Redox-active;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +##sequence-region P38767 1 581 +P38767 UniProtKB Chain 1 581 . . . ID=PRO_0000164256;Note=Ethionine resistance-conferring protein 1 +P38767 UniProtKB Topological domain 1 172 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38767 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38767 UniProtKB Topological domain 194 248 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38767 UniProtKB Transmembrane 249 269 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38767 UniProtKB Topological domain 270 281 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38767 UniProtKB Transmembrane 282 302 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38767 UniProtKB Topological domain 303 345 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38767 UniProtKB Transmembrane 346 366 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38767 UniProtKB Topological domain 367 471 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38767 UniProtKB Transmembrane 472 492 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38767 UniProtKB Topological domain 493 581 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32462 1 438 +P32462 UniProtKB Chain 1 438 . . . ID=PRO_0000207494;Note=Delta(14)-sterol reductase +P32462 UniProtKB Topological domain 1 13 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32462 UniProtKB Transmembrane 14 34 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32462 UniProtKB Topological domain 35 71 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32462 UniProtKB Transmembrane 72 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32462 UniProtKB Topological domain 91 109 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32462 UniProtKB Transmembrane 110 127 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32462 UniProtKB Topological domain 128 147 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32462 UniProtKB Transmembrane 148 172 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32462 UniProtKB Topological domain 173 242 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32462 UniProtKB Transmembrane 243 263 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32462 UniProtKB Topological domain 264 308 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32462 UniProtKB Transmembrane 309 328 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32462 UniProtKB Topological domain 329 368 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32462 UniProtKB Transmembrane 369 387 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32462 UniProtKB Topological domain 388 438 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32462 UniProtKB Nucleotide binding 370 371 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G4SW86 +P32462 UniProtKB Nucleotide binding 414 418 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G4SW86 +P32462 UniProtKB Binding site 335 335 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G4SW86 +P32462 UniProtKB Binding site 339 339 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G4SW86 +P32462 UniProtKB Binding site 358 358 . . . Note=NADP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G4SW86 +P32462 UniProtKB Binding site 363 363 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G4SW86 +P32462 UniProtKB Binding site 410 410 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G4SW86 +P32462 UniProtKB Binding site 425 425 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G4SW86 +P32462 UniProtKB Sequence conflict 253 253 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38604 1 731 +P38604 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8134375,ECO:0000269|Ref.7;Dbxref=PMID:8134375 +P38604 UniProtKB Chain 2 731 . . . ID=PRO_0000072657;Note=Lanosterol synthase +P38604 UniProtKB Repeat 125 167 . . . Note=PFTB 1 +P38604 UniProtKB Repeat 566 603 . . . Note=PFTB 2 +P38604 UniProtKB Repeat 615 661 . . . Note=PFTB 3 +P38604 UniProtKB Active site 234 234 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38604 UniProtKB Active site 456 456 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38604 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7 +P38604 UniProtKB Natural variant 359 731 . . . Note=In strain: SGL9%3B loss of activity. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3 +P38604 UniProtKB Mutagenesis 457 457 . . . Note=Reduces thermal stability and enzyme activity%3B when associated with A-526 or C-526. No effect%3B when associated with D-526 or Q-526. C->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16235265;Dbxref=PMID:16235265 +P38604 UniProtKB Mutagenesis 526 526 . . . Note=Reduces thermal stability and enzyme activity%3B when associated with D-457. E->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16235265;Dbxref=PMID:16235265 +P38604 UniProtKB Mutagenesis 526 526 . . . Note=No effect%3B when associated with D-457. E->D%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16235265;Dbxref=PMID:16235265 +P38604 UniProtKB Sequence conflict 61 61 . . . Note=H->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38604 UniProtKB Sequence conflict 530 530 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38604 UniProtKB Sequence conflict 530 530 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53198 1 216 +P53198 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53198 UniProtKB Chain 20 216 . . . ID=PRO_0000010413;Note=Protein ERP6 +P53198 UniProtKB Topological domain 20 183 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53198 UniProtKB Transmembrane 184 204 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53198 UniProtKB Topological domain 205 216 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53198 UniProtKB Domain 29 130 . . . Note=GOLD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00096 +P53198 UniProtKB Sequence conflict 106 106 . . . Note=C->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CX11 1 437 +P0CX11 UniProtKB Chain 1 437 . . . ID=PRO_0000409749;Note=Enolase-related protein 2 +P0CX11 UniProtKB Region 373 376 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX11 UniProtKB Active site 212 212 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX11 UniProtKB Active site 346 346 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX11 UniProtKB Metal binding 247 247 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX11 UniProtKB Metal binding 296 296 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX11 UniProtKB Metal binding 321 321 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX11 UniProtKB Binding site 160 160 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX11 UniProtKB Binding site 169 169 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX11 UniProtKB Binding site 296 296 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX11 UniProtKB Binding site 321 321 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX11 UniProtKB Binding site 397 397 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q04651 1 352 +Q04651 UniProtKB Chain 1 352 . . . ID=PRO_0000203251;Note=ER-derived vesicles protein ERV41 +Q04651 UniProtKB Topological domain 1 23 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04651 UniProtKB Transmembrane 24 44 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04651 UniProtKB Topological domain 45 311 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04651 UniProtKB Transmembrane 312 332 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04651 UniProtKB Topological domain 333 352 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04651 UniProtKB Motif 349 350 . . . Note=Isoleucine-leucine motif +Q04651 UniProtKB Beta strand 52 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Beta strand 63 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Helix 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Beta strand 80 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Beta strand 98 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Helix 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Helix 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Beta strand 162 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Beta strand 184 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Helix 194 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Beta strand 201 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Turn 218 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Beta strand 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Beta strand 233 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Turn 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Beta strand 250 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Beta strand 254 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Helix 266 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Beta strand 278 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +Q04651 UniProtKB Beta strand 287 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZLC +##sequence-region P36168 1 1195 +P36168 UniProtKB Chain 1 1195 . . . ID=PRO_0000203229;Note=EST/SMG-like protein 2 +P36168 UniProtKB Domain 1025 1164 . . . Note=PINc;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36168 UniProtKB Compositional bias 210 250 . . . Note=Asn-rich +##sequence-region Q03096 1 181 +Q03096 UniProtKB Chain 1 181 . . . ID=PRO_0000021206;Note=Telomere replication protein EST3 +Q03096 UniProtKB Alternative sequence 93 93 . . . ID=VSP_035813;Note=In isoform 2. V->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03096 UniProtKB Alternative sequence 94 181 . . . ID=VSP_035814;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03096 UniProtKB Mutagenesis 3 3 . . . Note=Causes telomere shortening. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16418502;Dbxref=PMID:16418502 +Q03096 UniProtKB Mutagenesis 21 21 . . . Note=Causes telomere shortening. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19172754;Dbxref=PMID:19172754 +Q03096 UniProtKB Mutagenesis 49 49 . . . Note=Reduces ability to dimerize and causes telomere shortening. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16418502;Dbxref=PMID:16418502 +Q03096 UniProtKB Mutagenesis 68 68 . . . Note=Reduces ability to dimerize and causes telomere shortening. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16418502,ECO:0000269|PubMed:19172754;Dbxref=PMID:16418502,PMID:19172754 +Q03096 UniProtKB Mutagenesis 68 68 . . . Note=Causes telomere shortening. K->E%2CS%2CY;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16418502,ECO:0000269|PubMed:19172754;Dbxref=PMID:16418502,PMID:19172754 +Q03096 UniProtKB Mutagenesis 71 71 . . . Note=Causes telomere shortening%2C but does not impair interaction with the telomerase RNP. K->A%2CE;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16418502,ECO:0000269|PubMed:19172754;Dbxref=PMID:16418502,PMID:19172754 +Q03096 UniProtKB Mutagenesis 72 72 . . . Note=Causes telomere shortening. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16418502;Dbxref=PMID:16418502 +Q03096 UniProtKB Mutagenesis 82 82 . . . Note=Causes telomere shortening. A->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16418502;Dbxref=PMID:16418502 +Q03096 UniProtKB Mutagenesis 86 86 . . . Note=Causes progressive telomere shortening and cell senescence. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16418502;Dbxref=PMID:16418502 +Q03096 UniProtKB Mutagenesis 87 87 . . . Note=Causes telomere shortening. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16418502;Dbxref=PMID:16418502 +Q03096 UniProtKB Mutagenesis 95 95 . . . Note=Causes telomere shortening. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16418502;Dbxref=PMID:16418502 +Q03096 UniProtKB Mutagenesis 103 103 . . . Note=Causes telomere shortening. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16418502;Dbxref=PMID:16418502 +Q03096 UniProtKB Mutagenesis 104 104 . . . Note=Reduces binding to DNA and RNA%2C and causes progressive telomere shortening and cell senescence. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16884717,ECO:0000269|PubMed:19172754;Dbxref=PMID:16884717,PMID:19172754 +Q03096 UniProtKB Mutagenesis 104 104 . . . Note=Impairs interaction with the telomerase RNP and causes progressive telomere shortening and cell senescence. E->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16884717,ECO:0000269|PubMed:19172754;Dbxref=PMID:16884717,PMID:19172754 +Q03096 UniProtKB Mutagenesis 110 110 . . . Note=Causes progressive telomere shortening and cell senescence%2C but does not impair interaction with the telomerase RNP. R->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19172754;Dbxref=PMID:19172754 +Q03096 UniProtKB Mutagenesis 114 114 . . . Note=Impairs interaction with the telomerase RNP and causes telomere shortening. E->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19172754;Dbxref=PMID:19172754 +Q03096 UniProtKB Mutagenesis 115 115 . . . Note=Impairs interaction with the telomerase RNP and causes telomere shortening. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16418502,ECO:0000269|PubMed:19172754;Dbxref=PMID:16418502,PMID:19172754 +Q03096 UniProtKB Mutagenesis 117 117 . . . Note=Impairs interaction with the telomerase RNP and causes telomere shortening. N->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19172754;Dbxref=PMID:19172754 +Q03096 UniProtKB Mutagenesis 164 164 . . . Note=Causes telomere shortening%2C but does not impair interaction with the telomerase RNP. D->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19172754;Dbxref=PMID:19172754 +Q03096 UniProtKB Mutagenesis 166 166 . . . Note=Reduces ability to dimerize and causes telomere shortening. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16418502,ECO:0000269|PubMed:19172754;Dbxref=PMID:16418502,PMID:19172754 +Q03096 UniProtKB Mutagenesis 166 166 . . . Note=Impairs interaction with the telomerase RNP and causes telomere shortening. D->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16418502,ECO:0000269|PubMed:19172754;Dbxref=PMID:16418502,PMID:19172754 +Q03096 UniProtKB Mutagenesis 168 168 . . . Note=Causes telomere shortening. V->A%2CD%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19172754;Dbxref=PMID:19172754 +Q03096 UniProtKB Helix 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V +Q03096 UniProtKB Helix 22 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V +Q03096 UniProtKB Turn 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V +Q03096 UniProtKB Helix 47 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V +Q03096 UniProtKB Helix 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V +Q03096 UniProtKB Helix 57 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V +Q03096 UniProtKB Helix 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V +Q03096 UniProtKB Beta strand 66 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V +Q03096 UniProtKB Beta strand 79 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V +Q03096 UniProtKB Beta strand 90 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V +Q03096 UniProtKB Helix 97 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V +Q03096 UniProtKB Beta strand 118 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V +Q03096 UniProtKB Beta strand 126 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V +Q03096 UniProtKB Helix 132 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V +Q03096 UniProtKB Helix 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V +Q03096 UniProtKB Beta strand 148 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V +Q03096 UniProtKB Turn 177 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M9V +##sequence-region P38836 1 430 +P38836 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38836 UniProtKB Chain 25 430 . . . ID=PRO_0000004417;Note=Putative metallocarboxypeptidase ECM14 +P38836 UniProtKB Region 182 185 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38836 UniProtKB Region 257 258 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38836 UniProtKB Region 311 312 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38836 UniProtKB Metal binding 182 182 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38836 UniProtKB Metal binding 185 185 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38836 UniProtKB Metal binding 310 310 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38836 UniProtKB Binding site 240 240 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38836 UniProtKB Glycosylation 41 41 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38836 UniProtKB Glycosylation 295 295 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38836 UniProtKB Disulfide bond 251 272 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q05958 1 814 +Q05958 UniProtKB Chain 1 814 . . . ID=PRO_0000114948;Note=Sterol regulatory element-binding protein ECM22 +Q05958 UniProtKB DNA binding 43 73 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +Q05958 UniProtKB Modified residue 431 431 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q05958 UniProtKB Modified residue 445 445 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q05958 UniProtKB Modified residue 464 464 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q05958 UniProtKB Mutagenesis 790 790 . . . Note=Increases aerobic sterol uptake. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11208779;Dbxref=PMID:11208779 +##sequence-region P32644 1 1121 +P32644 UniProtKB Chain 1 1121 . . . ID=PRO_0000080725;Note=Putative ATP-dependent RNA helicase ECM32 +P32644 UniProtKB Nucleotide binding 670 677 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32644 UniProtKB Modified residue 227 227 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32644 UniProtKB Modified residue 392 392 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P32644 UniProtKB Modified residue 465 465 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P38248 1 429 +P38248 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38248 UniProtKB Chain 20 406 . . . ID=PRO_0000033191;Note=Cell wall protein ECM33 +P38248 UniProtKB Propeptide 407 429 . . . ID=PRO_0000033192;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38248 UniProtKB Compositional bias 311 404 . . . Note=Ser-rich +P38248 UniProtKB Modified residue 339 339 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P38248 UniProtKB Lipidation 406 406 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38248 UniProtKB Glycosylation 21 21 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38248 UniProtKB Glycosylation 56 56 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38248 UniProtKB Glycosylation 82 82 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38248 UniProtKB Glycosylation 196 196 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38248 UniProtKB Glycosylation 209 209 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38248 UniProtKB Glycosylation 227 227 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38248 UniProtKB Glycosylation 234 234 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38248 UniProtKB Glycosylation 241 241 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38248 UniProtKB Glycosylation 267 267 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38248 UniProtKB Glycosylation 279 279 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38248 UniProtKB Glycosylation 304 304 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38248 UniProtKB Glycosylation 328 328 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38248 UniProtKB Glycosylation 389 389 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06200 1 448 +Q06200 UniProtKB Chain 1 448 . . . ID=PRO_0000086923;Note=Protein ECM7 +Q06200 UniProtKB Topological domain 1 28 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06200 UniProtKB Transmembrane 29 49 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06200 UniProtKB Topological domain 50 204 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06200 UniProtKB Transmembrane 205 225 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06200 UniProtKB Topological domain 226 246 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06200 UniProtKB Transmembrane 247 267 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06200 UniProtKB Topological domain 268 287 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06200 UniProtKB Transmembrane 288 308 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06200 UniProtKB Topological domain 309 448 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43605 1 281 +P43605 UniProtKB Chain 1 281 . . . ID=PRO_0000074550;Note=N-acetyltransferase ECO1 +P43605 UniProtKB Zinc finger 33 57 . . . Note=CCHH-type +P43605 UniProtKB Modified residue 223 223 . . . Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574 +P43605 UniProtKB Mutagenesis 35 35 . . . Note=In ctf7-109%3B loss of function. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15668154;Dbxref=PMID:15668154 +P43605 UniProtKB Mutagenesis 53 53 . . . Note=In ctf7-108%3B loss of function. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15668154;Dbxref=PMID:15668154 +P43605 UniProtKB Mutagenesis 211 211 . . . Note=Abolishes acetyltransferase activity%3B but not chromatid cohesion activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574 +P43605 UniProtKB Mutagenesis 222 223 . . . Note=Abolishes acetyltransferase activity%3B but not chromatid cohesion activity. RK->GG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574 +P43605 UniProtKB Mutagenesis 225 225 . . . Note=Abolishes acetyltransferase activity%3B but not chromatid cohesion activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574 +P43605 UniProtKB Mutagenesis 232 232 . . . Note=Abolishes acetyltransferase activity%3B but not chromatid cohesion activity. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574 +##sequence-region P38249 1 964 +P38249 UniProtKB Chain 1 964 . . . ID=PRO_0000123544;Note=Eukaryotic translation initiation factor 3 subunit A +P38249 UniProtKB Domain 382 493 . . . Note=PCI;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03000 +P38249 UniProtKB Coiled coil 625 668 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03000 +P38249 UniProtKB Coiled coil 702 734 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03000 +P38249 UniProtKB Coiled coil 796 869 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03000 +P38249 UniProtKB Compositional bias 506 542 . . . Note=Glu-rich +P38249 UniProtKB Modified residue 508 508 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38249 UniProtKB Modified residue 691 691 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38249 UniProtKB Modified residue 935 935 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38249 UniProtKB Mutagenesis 692 701 . . . Note=Reduces interaction of eIF-3 with the 40S ribosome. LDLDTIKQVI->AAAAAAAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18765792;Dbxref=PMID:18765792 +P38249 UniProtKB Helix 8 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D +P38249 UniProtKB Helix 24 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D +P38249 UniProtKB Helix 38 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D +P38249 UniProtKB Helix 45 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D +P38249 UniProtKB Helix 49 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D +P38249 UniProtKB Helix 65 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D +P38249 UniProtKB Helix 83 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D +P38249 UniProtKB Helix 112 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D +P38249 UniProtKB Helix 152 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D +P38249 UniProtKB Helix 176 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D +P38249 UniProtKB Helix 196 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D +P38249 UniProtKB Helix 217 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D +P38249 UniProtKB Helix 230 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D +P38249 UniProtKB Helix 253 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D +P38249 UniProtKB Helix 279 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51 +P38249 UniProtKB Helix 296 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51 +P38249 UniProtKB Helix 318 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51 +P38249 UniProtKB Helix 349 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51 +P38249 UniProtKB Helix 363 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51 +P38249 UniProtKB Helix 374 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51 +P38249 UniProtKB Helix 382 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51 +P38249 UniProtKB Turn 397 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51 +P38249 UniProtKB Helix 400 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51 +P38249 UniProtKB Beta strand 415 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51 +P38249 UniProtKB Helix 418 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51 +P38249 UniProtKB Helix 421 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51 +P38249 UniProtKB Beta strand 441 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51 +P38249 UniProtKB Helix 445 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51 +P38249 UniProtKB Helix 456 458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51 +P38249 UniProtKB Helix 462 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51 +P38249 UniProtKB Beta strand 481 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1D +P38249 UniProtKB Beta strand 487 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K51 +##sequence-region P40217 1 347 +P40217 UniProtKB Chain 1 347 . . . ID=PRO_0000051041;Note=Eukaryotic translation initiation factor 3 subunit I +P40217 UniProtKB Repeat 8 47 . . . Note=WD 1 +P40217 UniProtKB Repeat 50 89 . . . Note=WD 2 +P40217 UniProtKB Repeat 149 190 . . . Note=WD 3 +P40217 UniProtKB Repeat 194 233 . . . Note=WD 4 +P40217 UniProtKB Repeat 291 330 . . . Note=WD 5 +P40217 UniProtKB Modified residue 302 302 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40217 UniProtKB Beta strand 1 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 13 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 24 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 34 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Turn 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 44 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 55 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 64 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 74 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Turn 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 86 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 96 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 105 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 121 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Turn 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 136 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 144 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 156 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Helix 163 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 167 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 175 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Turn 182 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 187 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 199 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 208 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 218 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Turn 225 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 230 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 240 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 247 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 267 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 274 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Turn 280 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 285 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 296 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 305 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Beta strand 315 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Helix 324 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +P40217 UniProtKB Helix 332 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZWL +##sequence-region Q05050 1 843 +Q05050 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +Q05050 UniProtKB Chain 2 843 . . . ID=PRO_0000203273;Note=Eisosome protein 1 +Q05050 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +Q05050 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q05050 UniProtKB Modified residue 88 88 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05050 UniProtKB Modified residue 130 130 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17761666;Dbxref=PMID:17287358,PMID:17761666 +Q05050 UniProtKB Modified residue 182 182 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05050 UniProtKB Modified residue 401 401 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q05050 UniProtKB Modified residue 584 584 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:19779198 +Q05050 UniProtKB Modified residue 710 710 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q05050 UniProtKB Modified residue 720 720 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q05050 UniProtKB Modified residue 763 763 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05050 UniProtKB Modified residue 775 775 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05050 UniProtKB Modified residue 816 816 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q05050 UniProtKB Modified residue 828 828 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05050 UniProtKB Modified residue 829 829 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05050 UniProtKB Modified residue 838 838 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P40319 1 345 +P40319 UniProtKB Chain 1 345 . . . ID=PRO_0000207550;Note=Elongation of fatty acids protein 3 +P40319 UniProtKB Topological domain 1 73 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P40319 UniProtKB Transmembrane 74 94 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40319 UniProtKB Topological domain 95 105 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P40319 UniProtKB Transmembrane 106 126 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40319 UniProtKB Topological domain 127 155 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P40319 UniProtKB Transmembrane 156 176 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40319 UniProtKB Topological domain 177 180 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P40319 UniProtKB Transmembrane 181 201 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40319 UniProtKB Topological domain 202 207 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P40319 UniProtKB Transmembrane 208 228 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40319 UniProtKB Topological domain 229 242 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P40319 UniProtKB Transmembrane 243 263 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40319 UniProtKB Topological domain 264 283 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P40319 UniProtKB Transmembrane 284 304 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40319 UniProtKB Topological domain 305 345 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +P40319 UniProtKB Motif 308 311 . . . Note=Di-lysine motif 1;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9832547;Dbxref=PMID:9832547 +P40319 UniProtKB Motif 312 315 . . . Note=Di-lysine motif 2;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9832547;Dbxref=PMID:9832547 +P40319 UniProtKB Motif 316 319 . . . Note=Di-lysine motif 3;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9832547;Dbxref=PMID:9832547 +P40319 UniProtKB Glycosylation 2 2 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P40319 UniProtKB Glycosylation 20 20 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P40319 UniProtKB Glycosylation 66 66 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P40319 UniProtKB Sequence conflict 35 35 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40319 UniProtKB Sequence conflict 208 208 . . . Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40319 UniProtKB Sequence conflict 330 331 . . . Note=ST->FY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53861 1 379 +P53861 UniProtKB Chain 1 379 . . . ID=PRO_0000203386;Note=Elongin-A +P53861 UniProtKB Domain 19 63 . . . Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080 +P53861 UniProtKB Region 1 143 . . . Note=ELC1-binding +P53861 UniProtKB Modified residue 235 235 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53861 UniProtKB Modified residue 278 278 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +##sequence-region P43555 1 445 +P43555 UniProtKB Signal peptide 1 28 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8314797;Dbxref=PMID:8314797 +P43555 UniProtKB Chain 29 445 . . . ID=PRO_0000021173;Note=Protein EMP47 +P43555 UniProtKB Topological domain 29 412 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43555 UniProtKB Transmembrane 413 433 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43555 UniProtKB Topological domain 434 445 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43555 UniProtKB Domain 36 254 . . . Note=L-type lectin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00658 +P43555 UniProtKB Region 430 433 . . . Note=Mediates the interactions with COPI and COPII coat complexes;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43555 UniProtKB Motif 441 445 . . . Note=Di-lysine motif +P43555 UniProtKB Disulfide bond 179 213 . . . . +P43555 UniProtKB Sequence conflict 52 52 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43555 UniProtKB Sequence conflict 77 77 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43555 UniProtKB Sequence conflict 125 125 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43555 UniProtKB Helix 37 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Helix 42 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Beta strand 59 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Beta strand 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Beta strand 71 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Beta strand 81 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Beta strand 90 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Y +P43555 UniProtKB Beta strand 96 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Beta strand 114 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Beta strand 123 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Beta strand 139 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Beta strand 152 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Helix 168 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Helix 171 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Beta strand 176 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Beta strand 186 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Helix 198 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Beta strand 201 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Beta strand 211 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Beta strand 223 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Helix 237 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +P43555 UniProtKB Beta strand 243 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6Z +##sequence-region P53753 1 1117 +P53753 UniProtKB Signal peptide 1 16 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53753 UniProtKB Chain 17 1117 . . . ID=PRO_0000012133;Note=Endo-1%2C3(4)-beta-glucanase 1 +P53753 UniProtKB Compositional bias 342 345 . . . Note=Poly-Ser +P53753 UniProtKB Compositional bias 365 370 . . . Note=Poly-Ser +P53753 UniProtKB Compositional bias 376 383 . . . Note=Poly-Ser +P53753 UniProtKB Glycosylation 138 138 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53753 UniProtKB Glycosylation 186 186 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53753 UniProtKB Glycosylation 223 223 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53753 UniProtKB Glycosylation 259 259 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53753 UniProtKB Glycosylation 280 280 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53753 UniProtKB Glycosylation 303 303 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53753 UniProtKB Glycosylation 307 307 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53753 UniProtKB Glycosylation 393 393 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53753 UniProtKB Glycosylation 533 533 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53753 UniProtKB Glycosylation 886 886 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P06103 1 763 +P06103 UniProtKB Chain 1 763 . . . ID=PRO_0000123535;Note=Eukaryotic translation initiation factor 3 subunit B +P06103 UniProtKB Domain 77 162 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03001 +P06103 UniProtKB Repeat 228 266 . . . Note=WD 1 +P06103 UniProtKB Repeat 277 325 . . . Note=WD 2 +P06103 UniProtKB Repeat 373 416 . . . Note=WD 3 +P06103 UniProtKB Repeat 484 524 . . . Note=WD 4 +P06103 UniProtKB Repeat 544 589 . . . Note=WD 5 +P06103 UniProtKB Repeat 605 650 . . . Note=WD 6 +P06103 UniProtKB Region 1 136 . . . Note=Sufficient for interaction with HCR1 and TIF32;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16581774;Dbxref=PMID:16581774 +P06103 UniProtKB Region 28 261 . . . Note=Sufficient for interaction with PIC8 +P06103 UniProtKB Modified residue 61 61 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P06103 UniProtKB Modified residue 67 67 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06103 UniProtKB Modified residue 669 669 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P06103 UniProtKB Mutagenesis 124 130 . . . Note=Impairs interaction with HCR1 and TIF32%2C impairs interaction of the eIF-3 complex with eIF-1%2C eIF-2 and the 40S ribosome%2C and impairs initiation of translation. KGFLFVE->AAAAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16581774;Dbxref=PMID:16581774 +P06103 UniProtKB Beta strand 78 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6 +P06103 UniProtKB Helix 89 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6 +P06103 UniProtKB Helix 92 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6 +P06103 UniProtKB Beta strand 109 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6 +P06103 UniProtKB Turn 118 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6 +P06103 UniProtKB Beta strand 125 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6 +P06103 UniProtKB Helix 134 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6 +P06103 UniProtKB Beta strand 148 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6 +P06103 UniProtKB Beta strand 156 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6 +P06103 UniProtKB Helix 161 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NS6 +P06103 UniProtKB Helix 186 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Helix 191 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 201 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 207 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 224 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 236 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 245 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 250 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Turn 258 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 262 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 272 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 283 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Helix 305 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 312 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Turn 317 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 322 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 338 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 345 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 355 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Helix 361 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Helix 371 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 380 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 395 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 400 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 411 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 416 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 427 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 435 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 447 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 464 472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 480 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 486 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 501 506 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 519 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 538 547 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 551 554 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 558 565 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 571 573 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 575 580 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 593 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 600 603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 611 615 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 622 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Turn 628 630 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 636 641 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 646 651 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Beta strand 657 660 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1F +P06103 UniProtKB Helix 694 728 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U1E +##sequence-region P39540 1 310 +P39540 UniProtKB Chain 1 310 . . . ID=PRO_0000207548;Note=Elongation of fatty acids protein 1 +P39540 UniProtKB Topological domain 1 63 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P39540 UniProtKB Transmembrane 64 84 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39540 UniProtKB Topological domain 85 100 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P39540 UniProtKB Transmembrane 101 121 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39540 UniProtKB Topological domain 122 141 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P39540 UniProtKB Transmembrane 142 163 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39540 UniProtKB Topological domain 164 174 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P39540 UniProtKB Transmembrane 175 196 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39540 UniProtKB Topological domain 197 201 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P39540 UniProtKB Transmembrane 202 223 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39540 UniProtKB Topological domain 224 234 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P39540 UniProtKB Transmembrane 235 255 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39540 UniProtKB Topological domain 256 271 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P39540 UniProtKB Transmembrane 272 292 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39540 UniProtKB Topological domain 293 310 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +P39540 UniProtKB Motif 304 307 . . . Note=Di-lysine motif;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:8702485;Dbxref=PMID:8702485 +##sequence-region P38874 1 309 +P38874 UniProtKB Chain 1 309 . . . ID=PRO_0000084178;Note=Elongator complex protein 5 +P38874 UniProtKB Helix 8 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +P38874 UniProtKB Beta strand 23 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +P38874 UniProtKB Helix 36 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +P38874 UniProtKB Beta strand 55 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +P38874 UniProtKB Beta strand 70 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +P38874 UniProtKB Helix 80 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +P38874 UniProtKB Beta strand 102 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +P38874 UniProtKB Helix 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +P38874 UniProtKB Helix 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +P38874 UniProtKB Helix 117 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +P38874 UniProtKB Beta strand 129 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +P38874 UniProtKB Turn 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EJS +P38874 UniProtKB Helix 157 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +P38874 UniProtKB Beta strand 166 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +P38874 UniProtKB Helix 181 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +P38874 UniProtKB Beta strand 200 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +P38874 UniProtKB Beta strand 215 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +P38874 UniProtKB Turn 224 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +P38874 UniProtKB Beta strand 228 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +##sequence-region P53073 1 190 +P53073 UniProtKB Chain 1 190 . . . ID=PRO_0000202711;Note=ER membrane protein complex subunit 4 +P53073 UniProtKB Transmembrane 98 118 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53073 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12396 1 444 +Q12396 UniProtKB Signal peptide 1 46 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12134087;Dbxref=PMID:12134087 +Q12396 UniProtKB Chain 47 444 . . . ID=PRO_0000239645;Note=Protein EMP46 +Q12396 UniProtKB Topological domain 47 408 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12396 UniProtKB Transmembrane 409 429 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12396 UniProtKB Topological domain 430 444 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12396 UniProtKB Domain 52 269 . . . Note=L-type lectin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00658 +Q12396 UniProtKB Region 429 432 . . . Note=Mediates the interactions with COPI and COPII coat complexes +Q12396 UniProtKB Motif 440 444 . . . Note=Di-lysine motif +Q12396 UniProtKB Metal binding 177 177 . . . Note=Potassium +Q12396 UniProtKB Disulfide bond 196 230 . . . . +Q12396 UniProtKB Mutagenesis 177 177 . . . Note=Impairs potassium-binding. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16439369;Dbxref=PMID:16439369 +Q12396 UniProtKB Mutagenesis 429 429 . . . Note=Impairs interaction with COP1%2C SEC21 and SEC23 and loss of reticulum endoplasmic exit. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12134087;Dbxref=PMID:12134087 +Q12396 UniProtKB Mutagenesis 432 432 . . . Note=Impairs interaction with COP1%2C SEC21 and SEC23 and loss of reticulum endoplasmic exit. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12134087;Dbxref=PMID:12134087 +Q12396 UniProtKB Mutagenesis 440 444 . . . Note=Loss of endoplasmic reticulum exit. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12134087;Dbxref=PMID:12134087 +Q12396 UniProtKB Mutagenesis 440 442 . . . Note=Impairs interaction with COP1 and SEC21 and mislocalizes to the vacuole. KVK->SVS%2CRVR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12134087;Dbxref=PMID:12134087 +Q12396 UniProtKB Mutagenesis 443 444 . . . Note=Loss of endoplasmic reticulum exit. LL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12134087;Dbxref=PMID:12134087 +Q12396 UniProtKB Helix 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Turn 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Helix 71 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Turn 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Beta strand 78 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Beta strand 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Beta strand 90 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Beta strand 100 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Beta strand 115 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Beta strand 133 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Turn 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Beta strand 158 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Turn 168 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Beta strand 171 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Turn 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Beta strand 193 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Beta strand 207 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Helix 215 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Beta strand 219 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Beta strand 228 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Helix 238 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Beta strand 244 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +Q12396 UniProtKB Beta strand 258 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A6V +##sequence-region P00924 1 437 +P00924 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7005235,ECO:0000269|Ref.6;Dbxref=PMID:7005235 +P00924 UniProtKB Chain 2 437 . . . ID=PRO_0000134062;Note=Enolase 1 +P00924 UniProtKB Region 373 376 . . . Note=Substrate binding +P00924 UniProtKB Active site 212 212 . . . Note=Proton donor;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00924 UniProtKB Active site 346 346 . . . Note=Proton acceptor +P00924 UniProtKB Metal binding 247 247 . . . Note=Magnesium;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8605183;Dbxref=PMID:8605183 +P00924 UniProtKB Metal binding 296 296 . . . Note=Magnesium;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8605183;Dbxref=PMID:8605183 +P00924 UniProtKB Metal binding 321 321 . . . Note=Magnesium;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8605183;Dbxref=PMID:8605183 +P00924 UniProtKB Binding site 160 160 . . . Note=Substrate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8605183,ECO:0000269|PubMed:9376357;Dbxref=PMID:8605183,PMID:9376357 +P00924 UniProtKB Binding site 169 169 . . . Note=Substrate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8605183,ECO:0000269|PubMed:9376357;Dbxref=PMID:8605183,PMID:9376357 +P00924 UniProtKB Binding site 296 296 . . . Note=Substrate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8605183,ECO:0000269|PubMed:9376357;Dbxref=PMID:8605183,PMID:9376357 +P00924 UniProtKB Binding site 321 321 . . . Note=Substrate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8605183,ECO:0000269|PubMed:9376357;Dbxref=PMID:8605183,PMID:9376357 +P00924 UniProtKB Binding site 397 397 . . . Note=Substrate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8605183,ECO:0000269|PubMed:9376357;Dbxref=PMID:8605183,PMID:9376357 +P00924 UniProtKB Modified residue 119 119 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P00924 UniProtKB Modified residue 138 138 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00925 +P00924 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00925 +P00924 UniProtKB Modified residue 313 313 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00925 +P00924 UniProtKB Modified residue 324 324 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00925 +P00924 UniProtKB Cross-link 60 60 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00925 +P00924 UniProtKB Cross-link 243 243 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00925 +P00924 UniProtKB Cross-link 358 358 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00924 UniProtKB Mutagenesis 40 40 . . . Note=Reduces activity by 99.9%25. S->A +P00924 UniProtKB Mutagenesis 160 160 . . . Note=Reduces activity by 99%25. H->A%2CF%2CN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11027610,ECO:0000269|PubMed:13678299;Dbxref=PMID:11027610,PMID:13678299 +P00924 UniProtKB Mutagenesis 169 169 . . . Note=Reduces Kcat over 100000-fold. E->Q +P00924 UniProtKB Mutagenesis 208 208 . . . Note=Reduces activity by 44%25. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:13678299;Dbxref=PMID:13678299 +P00924 UniProtKB Mutagenesis 212 212 . . . Note=Reduces Kcat over 100000-fold. E->Q +P00924 UniProtKB Mutagenesis 346 346 . . . Note=Reduces Kcat over 100000-fold. Abolishes of the proton exchange reaction that initiates the enzymatic reaction. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8634301;Dbxref=PMID:8634301 +P00924 UniProtKB Sequence conflict 242 242 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00924 UniProtKB Beta strand 5 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Beta strand 18 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Beta strand 29 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Beta strand 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBH +P00924 UniProtKB Helix 57 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 63 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 73 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 87 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Beta strand 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EBH +P00924 UniProtKB Turn 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 108 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 130 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Beta strand 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Beta strand 152 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 158 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Beta strand 161 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Beta strand 169 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 180 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 204 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Beta strand 213 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P48 +P00924 UniProtKB Helix 222 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Turn 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Beta strand 243 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 250 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Turn 261 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 270 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 276 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Beta strand 292 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 304 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Turn 312 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL2 +P00924 UniProtKB Beta strand 316 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Turn 322 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 328 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Beta strand 341 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 347 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 353 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Beta strand 369 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 383 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Beta strand 394 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 404 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 421 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Beta strand 424 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 428 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +P00924 UniProtKB Helix 434 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AL1 +##sequence-region P32353 1 365 +P32353 UniProtKB Chain 1 365 . . . ID=PRO_0000117027;Note=Delta(7)-sterol 5(6)-desaturase +P32353 UniProtKB Topological domain 1 92 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32353 UniProtKB Transmembrane 93 113 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32353 UniProtKB Topological domain 114 140 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32353 UniProtKB Transmembrane 141 161 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32353 UniProtKB Topological domain 162 242 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32353 UniProtKB Transmembrane 243 263 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32353 UniProtKB Topological domain 264 365 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32353 UniProtKB Motif 200 204 . . . Note=Histidine box-1 +P32353 UniProtKB Motif 213 217 . . . Note=Histidine box-2 +P32353 UniProtKB Motif 288 292 . . . Note=Histidine box-3 +P32353 UniProtKB Cross-link 324 324 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P32353 UniProtKB Cross-link 344 344 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region Q12403 1 225 +Q12403 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12403 UniProtKB Chain 24 225 . . . ID=PRO_0000010410;Note=Protein ERP3 +Q12403 UniProtKB Topological domain 24 195 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12403 UniProtKB Transmembrane 196 216 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12403 UniProtKB Topological domain 217 225 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12403 UniProtKB Domain 33 172 . . . Note=GOLD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00096 +##sequence-region Q12284 1 196 +Q12284 UniProtKB Chain 1 196 . . . ID=PRO_0000001188;Note=FAD-linked sulfhydryl oxidase ERV2 +Q12284 UniProtKB Topological domain 1 12 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12284 UniProtKB Transmembrane 13 35 . . . Note=Helical%3B Signal-anchor;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12284 UniProtKB Topological domain 36 196 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12284 UniProtKB Domain 72 174 . . . Note=ERV/ALR sulfhydryl oxidase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00654 +Q12284 UniProtKB Region 78 86 . . . Note=FAD-binding +Q12284 UniProtKB Region 153 174 . . . Note=FAD-binding +Q12284 UniProtKB Disulfide bond 121 124 . . . Note=Redox-active;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00654 +Q12284 UniProtKB Disulfide bond 150 167 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00654,ECO:0000269|PubMed:11740506;Dbxref=PMID:11740506 +Q12284 UniProtKB Disulfide bond 176 178 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00654,ECO:0000269|PubMed:11740506;Dbxref=PMID:11740506 +Q12284 UniProtKB Mutagenesis 121 121 . . . Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11584268;Dbxref=PMID:11584268 +Q12284 UniProtKB Mutagenesis 124 124 . . . Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11584268;Dbxref=PMID:11584268 +Q12284 UniProtKB Helix 75 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JR8 +Q12284 UniProtKB Helix 102 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JR8 +Q12284 UniProtKB Helix 122 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JR8 +Q12284 UniProtKB Helix 142 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JR8 +Q12284 UniProtKB Helix 170 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JR8 +##sequence-region Q12480 1 344 +Q12480 UniProtKB Nucleotide binding 284 312 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03071 1 99 +Q03071 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +Q03071 UniProtKB Chain 2 99 . . . ID=PRO_0000239644;Note=Elongin-C +Q03071 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +Q03071 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q03071 UniProtKB Sequence conflict 64 64 . . . Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03071 UniProtKB Beta strand 4 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HV2 +Q03071 UniProtKB Turn 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HV2 +Q03071 UniProtKB Beta strand 14 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HV2 +Q03071 UniProtKB Helix 20 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HV2 +Q03071 UniProtKB Helix 27 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HV2 +Q03071 UniProtKB Turn 37 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HV2 +Q03071 UniProtKB Beta strand 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HV2 +Q03071 UniProtKB Helix 51 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HV2 +Q03071 UniProtKB Helix 84 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HV2 +##sequence-region Q04868 1 273 +Q04868 UniProtKB Chain 1 273 . . . ID=PRO_0000203355;Note=Elongator complex protein 6 +Q04868 UniProtKB Helix 20 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Beta strand 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Beta strand 30 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Helix 43 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Helix 59 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Beta strand 76 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Helix 86 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Helix 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Beta strand 103 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Helix 112 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Turn 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Helix 122 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Beta strand 143 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Helix 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Helix 154 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Helix 163 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Helix 171 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Beta strand 179 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Helix 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Helix 197 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Helix 202 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Beta strand 216 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Beta strand 234 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Beta strand 257 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +Q04868 UniProtKB Beta strand 267 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A8J +##sequence-region P36039 1 253 +P36039 UniProtKB Chain 1 253 . . . ID=PRO_0000211411;Note=ER membrane protein complex subunit 3 +P36039 UniProtKB Transmembrane 10 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36039 UniProtKB Transmembrane 126 146 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36039 UniProtKB Transmembrane 176 196 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04406 1 187 +Q04406 UniProtKB Chain 1 187 . . . ID=PRO_0000223039;Note=Early meiotic induction protein 1 +##sequence-region P32803 1 203 +P32803 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10713261,ECO:0000269|PubMed:8314797;Dbxref=PMID:10713261,PMID:8314797 +P32803 UniProtKB Chain 21 203 . . . ID=PRO_0000010407;Note=Endosomal protein P24B +P32803 UniProtKB Topological domain 21 172 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32803 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32803 UniProtKB Topological domain 194 203 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32803 UniProtKB Domain 30 118 . . . Note=GOLD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00096 +P32803 UniProtKB Mutagenesis 202 203 . . . Note=No change in COPII-binding. LV->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11560939;Dbxref=PMID:11560939 +P32803 UniProtKB Sequence conflict 32 32 . . . Note=C->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08299 1 606 +Q08299 UniProtKB Chain 1 606 . . . ID=PRO_0000084865;Note=Siderophore iron transporter ENB1 +Q08299 UniProtKB Topological domain 1 140 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Transmembrane 141 161 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Topological domain 162 187 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Transmembrane 188 208 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Topological domain 209 224 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Transmembrane 225 245 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Topological domain 246 279 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Transmembrane 280 300 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Topological domain 301 310 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Transmembrane 311 331 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Topological domain 332 337 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Transmembrane 338 358 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Topological domain 359 360 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Transmembrane 361 381 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Topological domain 382 390 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Transmembrane 391 410 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Topological domain 411 414 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Transmembrane 415 432 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Topological domain 433 435 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Transmembrane 436 456 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Topological domain 457 480 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Transmembrane 481 501 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Topological domain 502 550 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Transmembrane 551 571 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08299 UniProtKB Topological domain 572 606 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53938 1 366 +P53938 UniProtKB Chain 1 366 . . . ID=PRO_0000203446;Note=N-glycosylation protein EOS1 +P53938 UniProtKB Topological domain 1 136 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53938 UniProtKB Transmembrane 137 157 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53938 UniProtKB Topological domain 158 167 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53938 UniProtKB Transmembrane 168 188 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53938 UniProtKB Topological domain 189 195 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53938 UniProtKB Transmembrane 196 216 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53938 UniProtKB Topological domain 217 321 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53938 UniProtKB Transmembrane 322 342 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53938 UniProtKB Topological domain 343 366 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53938 UniProtKB Glycosylation 103 103 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53938 UniProtKB Glycosylation 104 104 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P16151 1 362 +P16151 UniProtKB Chain 1 362 . . . ID=PRO_0000087009;Note=Protein ERD1 +P16151 UniProtKB Topological domain 1 24 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16151 UniProtKB Transmembrane 25 45 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16151 UniProtKB Topological domain 46 84 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16151 UniProtKB Transmembrane 85 105 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16151 UniProtKB Topological domain 106 109 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16151 UniProtKB Transmembrane 110 130 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16151 UniProtKB Topological domain 131 362 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16151 UniProtKB Domain 181 362 . . . Note=EXS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00712 +P16151 UniProtKB Sequence conflict 168 168 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12452 1 347 +Q12452 UniProtKB Chain 1 347 . . . ID=PRO_0000054595;Note=3-keto-steroid reductase +Q12452 UniProtKB Active site 202 202 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12452 UniProtKB Modified residue 345 345 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region Q05359 1 219 +Q05359 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10713261;Dbxref=PMID:10713261 +Q05359 UniProtKB Chain 23 219 . . . ID=PRO_0000010408;Note=Protein ERP1 +Q05359 UniProtKB Topological domain 23 186 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05359 UniProtKB Transmembrane 187 207 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05359 UniProtKB Topological domain 208 219 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05359 UniProtKB Domain 32 131 . . . Note=GOLD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00096 +Q05359 UniProtKB Sequence conflict 152 152 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38748 1 585 +P38748 UniProtKB Chain 1 585 . . . ID=PRO_0000056337;Note=RING finger protein ETP1 +P38748 UniProtKB Zinc finger 240 280 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +P38748 UniProtKB Zinc finger 299 360 . . . Note=UBP-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502 +P38748 UniProtKB Modified residue 376 376 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38748 UniProtKB Cross-link 369 369 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38748 UniProtKB Cross-link 410 410 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12872131,ECO:0000269|PubMed:14557538;Dbxref=PMID:12872131,PMID:14557538 +P38748 UniProtKB Cross-link 450 450 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38748 UniProtKB Sequence conflict 558 558 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38071 1 380 +P38071 UniProtKB Transit peptide 1 9 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8195160;Dbxref=PMID:8195160 +P38071 UniProtKB Chain 10 380 . . . ID=PRO_0000160924;Note=Enoyl-[acyl-carrier-protein] reductase%2C mitochondrial +P38071 UniProtKB Nucleotide binding 185 188 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3 +P38071 UniProtKB Nucleotide binding 208 210 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3 +P38071 UniProtKB Nucleotide binding 283 286 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3 +P38071 UniProtKB Nucleotide binding 308 310 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3 +P38071 UniProtKB Active site 73 73 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3 +P38071 UniProtKB Binding site 157 157 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3 +P38071 UniProtKB Binding site 373 373 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WZM3 +P38071 UniProtKB Modified residue 339 339 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38071 UniProtKB Mutagenesis 73 73 . . . Note=0.1%25 of catalytic activity. No specific ARS1 binding. Y->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12614607;Dbxref=PMID:12614607 +P38071 UniProtKB Sequence conflict 24 24 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P23776 1 448 +P23776 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23776 UniProtKB Propeptide 20 40 . . . ID=PRO_0000007892;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1900250,ECO:0000269|PubMed:2125957,ECO:0000269|PubMed:8488724,ECO:0000269|PubMed:9748433;Dbxref=PMID:1900250,PMID:2125957,PMID:8488724,PMID:9748433 +P23776 UniProtKB Chain 41 448 . . . ID=PRO_0000007893;Note=Glucan 1%2C3-beta-glucosidase I/II +P23776 UniProtKB Active site 232 232 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23776 UniProtKB Active site 334 334 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23776 UniProtKB Glycosylation 165 165 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14730348;Dbxref=PMID:14730348 +P23776 UniProtKB Glycosylation 325 325 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14730348;Dbxref=PMID:14730348 +P23776 UniProtKB Sequence conflict 41 41 . . . Note=Y->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23776 UniProtKB Sequence conflict 46 46 . . . Note=H->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23776 UniProtKB Sequence conflict 77 77 . . . Note=R->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23776 UniProtKB Beta strand 53 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Beta strand 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Turn 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 70 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 90 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 99 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 116 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Beta strand 129 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 152 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Beta strand 169 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 185 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 198 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 218 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Beta strand 224 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 235 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 240 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 248 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Beta strand 265 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 276 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 283 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Beta strand 289 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 302 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 309 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Beta strand 327 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Beta strand 339 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Turn 344 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Turn 373 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 378 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 383 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Turn 401 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Beta strand 405 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 421 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +P23776 UniProtKB Helix 442 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H4P +##sequence-region P52911 1 562 +P52911 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52911 UniProtKB Chain 23 562 . . . ID=PRO_0000007894;Note=Glucan 1%2C3-beta-glucosidase 2 +P52911 UniProtKB Active site 254 254 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52911 UniProtKB Active site 334 334 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52911 UniProtKB Glycosylation 50 50 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52911 UniProtKB Glycosylation 77 77 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52911 UniProtKB Glycosylation 86 86 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52911 UniProtKB Glycosylation 90 90 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52911 UniProtKB Glycosylation 106 106 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52911 UniProtKB Glycosylation 157 157 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52911 UniProtKB Glycosylation 220 220 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52911 UniProtKB Glycosylation 281 281 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52911 UniProtKB Glycosylation 285 285 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52911 UniProtKB Glycosylation 310 310 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52911 UniProtKB Glycosylation 317 317 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52911 UniProtKB Glycosylation 322 322 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52911 UniProtKB Glycosylation 401 401 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52911 UniProtKB Glycosylation 480 480 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52911 UniProtKB Glycosylation 539 539 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04660 1 807 +Q04660 UniProtKB Chain 1 807 . . . ID=PRO_0000050968;Note=Ribosome biogenesis protein ERB1 +Q04660 UniProtKB Repeat 435 474 . . . Note=WD 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03027 +Q04660 UniProtKB Repeat 483 523 . . . Note=WD 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03027 +Q04660 UniProtKB Repeat 592 634 . . . Note=WD 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03027 +Q04660 UniProtKB Repeat 637 675 . . . Note=WD 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03027 +Q04660 UniProtKB Repeat 678 717 . . . Note=WD 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03027 +Q04660 UniProtKB Repeat 721 760 . . . Note=WD 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03027 +Q04660 UniProtKB Repeat 776 807 . . . Note=WD 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03027 +Q04660 UniProtKB Region 265 383 . . . Note=Required for interaction with NOP7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18448671;Dbxref=PMID:18448671 +Q04660 UniProtKB Region 383 419 . . . Note=Required for interaction with YTM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18448671;Dbxref=PMID:18448671 +Q04660 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956 +Q04660 UniProtKB Modified residue 72 72 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q04660 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q04660 UniProtKB Modified residue 146 146 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04660 UniProtKB Modified residue 149 149 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04660 UniProtKB Modified residue 418 418 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +Q04660 UniProtKB Cross-link 127 127 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q04660 UniProtKB Mutagenesis 465 465 . . . Note=Disrupts the interaction with YTM1 and cannot sustain growth. E->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26476442,ECO:0000269|PubMed:26657628;Dbxref=PMID:26476442,PMID:26657628 +Q04660 UniProtKB Mutagenesis 470 470 . . . Note=Weakens the interaction with YTM1%2C impairs pre-rRNA processing and leads to a deficiency in 60S ribosomal subunits. Disrupts the interaction with YTM1 and cannot sustain growth%3B when associated with R-790. R->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26476442,ECO:0000269|PubMed:26657628;Dbxref=PMID:26476442,PMID:26657628 +Q04660 UniProtKB Mutagenesis 790 790 . . . Note=Disrupts the interaction with YTM1 and cannot sustain growth%3B when associated with E-470. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26657628;Dbxref=PMID:26657628 +Q04660 UniProtKB Helix 419 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 428 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 440 445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 451 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 459 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Turn 466 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 471 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 488 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 502 506 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 509 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Helix 520 532 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 573 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Helix 580 583 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Turn 584 586 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 587 595 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 599 602 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 606 612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Helix 617 619 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 620 625 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Helix 626 628 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 630 632 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 642 647 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 649 660 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 662 666 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Turn 667 670 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 671 676 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 683 688 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 692 699 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 704 708 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Turn 709 711 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 716 719 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 726 731 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 733 742 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 747 753 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 756 759 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 763 770 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 781 786 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 788 791 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 793 797 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +Q04660 UniProtKB Beta strand 802 806 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U7A +##sequence-region P05453 1 685 +P05453 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P05453 UniProtKB Chain 2 685 . . . ID=PRO_0000091482;Note=Eukaryotic peptide chain release factor GTP-binding subunit +P05453 UniProtKB Domain 258 484 . . . Note=tr-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P05453 UniProtKB Nucleotide binding 267 274 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05453 UniProtKB Nucleotide binding 344 348 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05453 UniProtKB Nucleotide binding 406 409 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05453 UniProtKB Region 2 239 . . . Note=Interaction with PAB1 +P05453 UniProtKB Region 5 135 . . . Note=Prion domain (PrD) +P05453 UniProtKB Region 139 249 . . . Note=Charged +P05453 UniProtKB Region 267 274 . . . Note=G1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P05453 UniProtKB Region 323 327 . . . Note=G2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P05453 UniProtKB Region 344 347 . . . Note=G3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P05453 UniProtKB Region 406 409 . . . Note=G4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P05453 UniProtKB Region 448 450 . . . Note=G5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P05453 UniProtKB Site 273 273 . . . Note=Interacts with GTP/GDP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05453 UniProtKB Site 407 407 . . . Note=Interacts with GTP/GDP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05453 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P05453 UniProtKB Modified residue 571 571 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P05453 UniProtKB Sequence conflict 53 53 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P42222 1 437 +P42222 UniProtKB Chain 1 437 . . . ID=PRO_0000134065;Note=Enolase-related protein 3 +P42222 UniProtKB Region 373 376 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42222 UniProtKB Active site 212 212 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42222 UniProtKB Active site 346 346 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42222 UniProtKB Metal binding 247 247 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42222 UniProtKB Metal binding 296 296 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42222 UniProtKB Metal binding 321 321 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42222 UniProtKB Binding site 160 160 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42222 UniProtKB Binding site 169 169 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42222 UniProtKB Binding site 296 296 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42222 UniProtKB Binding site 321 321 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42222 UniProtKB Binding site 397 397 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38140 1 529 +P38140 UniProtKB Chain 1 529 . . . ID=PRO_0000114993;Note=Transcription activator of gluconeogenesis ERT1 +P38140 UniProtKB Domain 408 480 . . . Note=PAS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00140 +P38140 UniProtKB DNA binding 40 68 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +##sequence-region P27882 1 189 +P27882 UniProtKB Chain 1 189 . . . ID=PRO_0000001187;Note=Mitochondrial FAD-linked sulfhydryl oxidase ERV1 +P27882 UniProtKB Domain 83 183 . . . Note=ERV/ALR sulfhydryl oxidase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00654 +P27882 UniProtKB Region 166 183 . . . Note=FAD-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P27882 UniProtKB Disulfide bond 130 133 . . . Note=Redox-active;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00654 +P27882 UniProtKB Disulfide bond 159 176 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00654 +P27882 UniProtKB Mutagenesis 30 30 . . . Note=Reduces catalytic activity 3-fold. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654008;Dbxref=PMID:12654008 +P27882 UniProtKB Mutagenesis 33 33 . . . Note=Reduces catalytic activity 2-fold. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654008;Dbxref=PMID:12654008 +P27882 UniProtKB Mutagenesis 130 130 . . . Note=Loss of function. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654008;Dbxref=PMID:12654008 +P27882 UniProtKB Mutagenesis 133 133 . . . Note=Loss of function. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654008;Dbxref=PMID:12654008 +P27882 UniProtKB Mutagenesis 159 159 . . . Note=Reduces catalytic activity 3.3-fold. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654008;Dbxref=PMID:12654008 +P27882 UniProtKB Mutagenesis 176 176 . . . Note=Reduces catalytic activity 2.6-fold. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654008;Dbxref=PMID:12654008 +P27882 UniProtKB Beta strand 16 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E0I +P27882 UniProtKB Beta strand 26 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E0I +P27882 UniProtKB Helix 36 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E0I +P27882 UniProtKB Turn 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E0I +P27882 UniProtKB Helix 87 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W4Y +P27882 UniProtKB Helix 111 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W4Y +P27882 UniProtKB Helix 131 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W4Y +P27882 UniProtKB Helix 151 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W4Y +P27882 UniProtKB Helix 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W4Y +P27882 UniProtKB Helix 179 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W4Y +##sequence-region P39727 1 415 +P39727 UniProtKB Chain 1 415 . . . ID=PRO_0000202419;Note=ER-derived vesicles protein ERV46 +P39727 UniProtKB Topological domain 1 24 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39727 UniProtKB Transmembrane 25 45 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39727 UniProtKB Topological domain 46 376 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39727 UniProtKB Transmembrane 377 397 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39727 UniProtKB Topological domain 398 415 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39727 UniProtKB Motif 402 403 . . . Note=Phenylalanine-tyrosine motif +##sequence-region P19097 1 1887 +P19097 UniProtKB Chain 1 1887 . . . ID=PRO_0000180287;Note=Fatty acid synthase subunit alpha +P19097 UniProtKB Domain 145 220 . . . Note=Carrier;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00258 +P19097 UniProtKB Region 675 874 . . . Note=Beta-ketoacyl reductase +P19097 UniProtKB Region 1149 1363 . . . Note=Beta-ketoacyl synthase +P19097 UniProtKB Region 1772 1774 . . . Note=Acetyl-CoA binding +P19097 UniProtKB Region 1817 1833 . . . Note=Acetyl-CoA binding +P19097 UniProtKB Region 1841 1844 . . . Note=Acetyl-CoA binding +P19097 UniProtKB Region 1871 1873 . . . Note=Acetyl-CoA binding +P19097 UniProtKB Active site 1305 1305 . . . Note=For beta-ketoacyl synthase activity +P19097 UniProtKB Metal binding 1772 1772 . . . Note=Magnesium +P19097 UniProtKB Metal binding 1773 1773 . . . Note=Magnesium%3B via carbonyl oxygen +P19097 UniProtKB Metal binding 1774 1774 . . . Note=Magnesium +P19097 UniProtKB Metal binding 1872 1872 . . . Note=Magnesium +P19097 UniProtKB Metal binding 1873 1873 . . . Note=Magnesium%3B via carbonyl oxygen +P19097 UniProtKB Binding site 1798 1798 . . . Note=Acetyl-CoA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086 +P19097 UniProtKB Binding site 1808 1808 . . . Note=Acetyl-CoA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086 +P19097 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P19097 UniProtKB Modified residue 180 180 . . . Note=O-(pantetheine 4'-phosphoryl)serine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00258,ECO:0000269|PubMed:17431182;Dbxref=PMID:17431182 +P19097 UniProtKB Modified residue 523 523 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P19097 UniProtKB Modified residue 958 958 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P19097 UniProtKB Modified residue 1440 1440 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P19097 UniProtKB Cross-link 37 37 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P19097 UniProtKB Mutagenesis 1250 1250 . . . Note=Cerulenin-resistance. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8041367;Dbxref=PMID:8041367 +P19097 UniProtKB Mutagenesis 1769 1769 . . . Note=Does not affect oligomerization%3B when associated with S-1771 and L-1773 or S-1771%3B L-1773%3B S-1879 and E-1881. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086 +P19097 UniProtKB Mutagenesis 1770 1770 . . . Note=Loss of transferase activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086 +P19097 UniProtKB Mutagenesis 1771 1771 . . . Note=Does not affect oligomerization but lacks transferase activity%3B when associated with D-1769 and L-1773 or D-1769%3B L-1773%3B S-1879 and E-1881. V->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086 +P19097 UniProtKB Mutagenesis 1772 1772 . . . Note=Loss of transferase activity%3B when associated with S-1774. D->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086 +P19097 UniProtKB Mutagenesis 1773 1773 . . . Note=Does not affect oligomerization but lacks transferase activity%3B when associated with D-1769 and S-1771 or D-1769%3B S-1771%3B S-1879 and E-1881. V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086 +P19097 UniProtKB Mutagenesis 1774 1774 . . . Note=Loss of transferase activity%3B when associated with S-1772. E->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086 +P19097 UniProtKB Mutagenesis 1841 1841 . . . Note=Loss off transferase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086 +P19097 UniProtKB Mutagenesis 1879 1879 . . . Note=Does not affect oligomerization but lacks transferase activity%3B when associated with D-1769%3B S-1771%3B L-1773 and E-1881. V->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086 +P19097 UniProtKB Mutagenesis 1881 1881 . . . Note=Does not affect oligomerization but lacks transferase activity%3B when associated with D-1769%3B S-1771%3B L-1773 and S-1879. V->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19679086;Dbxref=PMID:19679086 +P19097 UniProtKB Sequence conflict 310 310 . . . Note=G->GTTGTGG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19097 UniProtKB Sequence conflict 594 594 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19097 UniProtKB Sequence conflict 941 1019 . . . Note=AKLRKELVETSEVRKAVSIETALEHKVVNGNSADAAYAQVEIQPRANIQLDFPELKPYKQVKQIAPAELEGLLDLERVI->CLNCVKSWLKLLKLERQFPSKLLWSIRLSMAIALMLHMLKSKFNQELTFNWTSQNRNHTNRLNKLLPLSLRVCWIWKELF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19097 UniProtKB Sequence conflict 1036 1041 . . . Note=RWEMEA->KMGNGS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19097 UniProtKB Sequence conflict 1408 1408 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19097 UniProtKB Sequence conflict 1671 1671 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19097 UniProtKB Helix 3 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 28 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 42 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 52 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 66 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 77 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 85 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 147 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 158 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 163 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 172 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 180 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 201 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 206 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 223 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 243 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 258 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 261 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 274 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ML8 +P19097 UniProtKB Helix 280 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 329 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 356 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 384 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 396 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 400 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 405 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 430 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 445 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 460 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 464 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 497 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 509 515 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 522 531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 605 607 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 609 615 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 626 629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 637 643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 649 651 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 653 668 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 677 682 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 685 687 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 688 698 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 702 709 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 712 725 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 731 736 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 742 753 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 756 759 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 766 770 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 781 783 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 786 795 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 797 811 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 812 814 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 820 826 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 839 845 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 846 848 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 849 855 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 859 861 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 862 869 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 885 889 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 898 906 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 907 909 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 911 919 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 922 927 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 930 932 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 933 935 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 936 968 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 971 976 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 998 1004 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1007 1009 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 1010 1012 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1015 1017 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1019 1028 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1033 1042 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1047 1056 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1059 1067 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1070 1077 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 1078 1080 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1086 1088 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1089 1099 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1101 1105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1108 1111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1118 1126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1134 1136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1138 1148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1149 1151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1152 1156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 1158 1160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1163 1167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1172 1179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1185 1187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 1195 1199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1202 1207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1210 1225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1231 1233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1234 1237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1240 1242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1243 1245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1248 1251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1254 1261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 1262 1267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1274 1278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1282 1290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1304 1306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1307 1320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1325 1333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1337 1345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1352 1357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1362 1364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1381 1389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1390 1396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1402 1410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1424 1429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1441 1443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1445 1474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1483 1508 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 1512 1515 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1517 1519 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1521 1527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 1528 1530 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1533 1535 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1536 1540 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1547 1564 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1572 1575 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1578 1581 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1585 1587 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1588 1600 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1612 1614 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1616 1620 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1638 1645 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 1646 1648 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1649 1656 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1659 1662 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1667 1693 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1708 1710 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1711 1716 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1726 1728 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1730 1732 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Turn 1735 1739 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Helix 1742 1745 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P19097 UniProtKB Beta strand 1769 1775 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS +P19097 UniProtKB Helix 1776 1778 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS +P19097 UniProtKB Helix 1784 1790 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS +P19097 UniProtKB Helix 1793 1800 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS +P19097 UniProtKB Beta strand 1802 1804 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS +P19097 UniProtKB Helix 1805 1823 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS +P19097 UniProtKB Beta strand 1837 1842 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS +P19097 UniProtKB Beta strand 1845 1851 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS +P19097 UniProtKB Helix 1853 1860 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS +P19097 UniProtKB Turn 1861 1863 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS +P19097 UniProtKB Beta strand 1866 1873 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS +P19097 UniProtKB Beta strand 1875 1885 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WAS +##sequence-region Q12283 1 360 +Q12283 UniProtKB Transit peptide 1 24 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12283 UniProtKB Chain 25 360 . . . ID=PRO_0000257811;Note=Malonyl CoA-acyl carrier protein transacylase%2C mitochondrial +Q12283 UniProtKB Active site 105 105 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12283 UniProtKB Active site 235 235 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53917 1 953 +P53917 UniProtKB Chain 1 953 . . . ID=PRO_0000087190;Note=Factor arrest protein 11 +P53917 UniProtKB Modified residue 18 18 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P53917 UniProtKB Modified residue 81 81 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53917 UniProtKB Modified residue 524 524 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P53917 UniProtKB Modified residue 527 527 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53917 UniProtKB Modified residue 528 528 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P21268 1 830 +P21268 UniProtKB Chain 1 830 . . . ID=PRO_0000055910;Note=Cyclin-dependent kinase inhibitor FAR1 +P21268 UniProtKB Zinc finger 202 252 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +P21268 UniProtKB Modified residue 87 87 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21268 UniProtKB Modified residue 110 110 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P21268 UniProtKB Modified residue 114 114 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P21268 UniProtKB Modified residue 306 306 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P21268 UniProtKB Natural variant 87 87 . . . Note=In FAR1-22P%3B induces cell cycle arrest in the absence of alpha-factor. S->P +P21268 UniProtKB Mutagenesis 87 87 . . . Note=Prevents cell cycle-dependent degradation of FAR1. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9632750;Dbxref=PMID:9632750 +P21268 UniProtKB Mutagenesis 306 306 . . . Note=Abolishes G1 arrest function. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9632750;Dbxref=PMID:9632750 +P21268 UniProtKB Sequence conflict 20 20 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21268 UniProtKB Sequence conflict 568 568 . . . Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P43592 1 221 +P43592 UniProtKB Chain 1 221 . . . ID=PRO_0000087192;Note=Factor arrest protein 7 +P43592 UniProtKB Compositional bias 11 22 . . . Note=Poly-Gln +##sequence-region P15646 1 327 +P15646 UniProtKB Chain 1 327 . . . ID=PRO_0000148527;Note=rRNA 2'-O-methyltransferase fibrillarin +P15646 UniProtKB Region 8 83 . . . Note=RGG-box +P15646 UniProtKB Region 22 42 . . . Note=RNA-binding RGG-box;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15646 UniProtKB Region 58 75 . . . Note=RNA-binding RGG-box;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15646 UniProtKB Region 179 180 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15646 UniProtKB Region 198 199 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15646 UniProtKB Region 223 224 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15646 UniProtKB Region 243 246 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15646 UniProtKB Region 281 313 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15646 UniProtKB Compositional bias 6 83 . . . Note=DMA/Gly-rich +P15646 UniProtKB Modified residue 16 16 . . . Note=Asymmetric dimethylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332 +P15646 UniProtKB Modified residue 16 16 . . . Note=Omega-N-methylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332 +P15646 UniProtKB Modified residue 22 22 . . . Note=Omega-N-methylarginine%3B by HMT1;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332 +P15646 UniProtKB Modified residue 30 30 . . . Note=Asymmetric dimethylarginine%3B by HMT1;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332 +P15646 UniProtKB Modified residue 34 34 . . . Note=Asymmetric dimethylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332 +P15646 UniProtKB Modified residue 34 34 . . . Note=Omega-N-methylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332 +P15646 UniProtKB Modified residue 40 40 . . . Note=Omega-N-methylarginine%3B by HMT1;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332 +P15646 UniProtKB Modified residue 48 48 . . . Note=Asymmetric dimethylarginine%3B by HMT1;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332 +P15646 UniProtKB Modified residue 52 52 . . . Note=Asymmetric dimethylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332 +P15646 UniProtKB Modified residue 52 52 . . . Note=Omega-N-methylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332 +P15646 UniProtKB Modified residue 58 58 . . . Note=Omega-N-methylarginine%3B by HMT1;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332 +P15646 UniProtKB Modified residue 70 70 . . . Note=Asymmetric dimethylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332 +P15646 UniProtKB Modified residue 70 70 . . . Note=Omega-N-methylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332 +P15646 UniProtKB Modified residue 73 73 . . . Note=Asymmetric dimethylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332 +P15646 UniProtKB Modified residue 73 73 . . . Note=Omega-N-methylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332 +P15646 UniProtKB Modified residue 81 81 . . . Note=Asymmetric dimethylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332 +P15646 UniProtKB Modified residue 81 81 . . . Note=Omega-N-methylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:23865587,ECO:0000305|PubMed:12756332;Dbxref=PMID:23865587,PMID:12756332 +P15646 UniProtKB Cross-link 150 150 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P15646 UniProtKB Mutagenesis 87 87 . . . Note=In nop1.3%3B thermosensitive allele showing a decrease in histone-glutamine N-methyltransferase activity upon shift to restrictive temperature%3B when associated with G-103%3B V-175 and S-219. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24352239;Dbxref=PMID:24352239 +P15646 UniProtKB Mutagenesis 103 103 . . . Note=In nop1.3%3B thermosensitive allele showing a decrease in histone-glutamine N-methyltransferase activity upon shift to restrictive temperature%3B when associated with D-87%3B V-175 and S-219. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24352239;Dbxref=PMID:24352239 +P15646 UniProtKB Mutagenesis 175 175 . . . Note=In nop1.3%3B thermosensitive allele showing a decrease in histone-glutamine N-methyltransferase activity upon shift to restrictive temperature%3B when associated with D-87%3B G-103 and S-219. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24352239;Dbxref=PMID:24352239 +P15646 UniProtKB Mutagenesis 219 219 . . . Note=In nop1.3%3B thermosensitive allele showing a decrease in histone-glutamine N-methyltransferase activity upon shift to restrictive temperature%3B when associated with D-87%3B G-103 and V-175. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24352239;Dbxref=PMID:24352239 +##sequence-region Q03034 1 503 +Q03034 UniProtKB Chain 1 503 . . . ID=PRO_0000157387;Note=Ferulic acid decarboxylase 1 +Q03034 UniProtKB Region 170 175 . . . Note=prenyl-FMN binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03196,ECO:0000269|PubMed:26083754;Dbxref=PMID:26083754 +Q03034 UniProtKB Region 192 193 . . . Note=prenyl-FMN binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03196,ECO:0000269|PubMed:26083754;Dbxref=PMID:26083754 +Q03034 UniProtKB Active site 285 285 . . . Note=Proton donor;Ontology_term=ECO:0000250,ECO:0000255,ECO:0000305;evidence=ECO:0000250|UniProtKB:A2QHE5,ECO:0000255|HAMAP-Rule:MF_03196,ECO:0000305|PubMed:25862228;Dbxref=PMID:25862228 +Q03034 UniProtKB Metal binding 170 170 . . . Note=Manganese;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03196,ECO:0000269|PubMed:26083754;Dbxref=PMID:26083754 +Q03034 UniProtKB Metal binding 193 193 . . . Note=Manganese;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03196,ECO:0000269|PubMed:26083754;Dbxref=PMID:26083754 +Q03034 UniProtKB Metal binding 236 236 . . . Note=Manganese;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03196,ECO:0000269|PubMed:26083754;Dbxref=PMID:26083754 +Q03034 UniProtKB Binding site 236 236 . . . Note=prenyl-FMN;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03196,ECO:0000269|PubMed:26083754;Dbxref=PMID:26083754 +Q03034 UniProtKB Binding site 394 394 . . . Note=prenyl-FMN;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03196,ECO:0000269|PubMed:26083754;Dbxref=PMID:26083754 +Q03034 UniProtKB Mutagenesis 285 285 . . . Note=Abolishes catalytic activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25862228;Dbxref=PMID:25862228 +Q03034 UniProtKB Turn 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 10 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 23 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 35 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 50 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 61 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 82 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 96 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 119 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 123 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 126 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 152 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 158 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 169 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 180 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 193 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Turn 203 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 210 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 220 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 236 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 249 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 254 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 259 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 265 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 288 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 296 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 312 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 321 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 325 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 330 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 349 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 356 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 362 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 369 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 379 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Turn 395 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 401 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 414 424 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Turn 427 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 431 434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 436 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 444 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 451 454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Beta strand 459 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 467 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 481 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +Q03034 UniProtKB Helix 487 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZAC +##sequence-region P29704 1 444 +P29704 UniProtKB Chain 1 444 . . . ID=PRO_0000067454;Note=Squalene synthase +P29704 UniProtKB Transmembrane 291 311 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P29704 UniProtKB Transmembrane 421 441 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P29704 UniProtKB Sequence conflict 48 48 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29704 UniProtKB Sequence conflict 286 286 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29704 UniProtKB Sequence conflict 320 320 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29704 UniProtKB Sequence conflict 330 330 . . . Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29704 UniProtKB Sequence conflict 429 429 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P26793 1 382 +P26793 UniProtKB Chain 1 382 . . . ID=PRO_0000154038;Note=Flap endonuclease 1 +P26793 UniProtKB Region 1 105 . . . Note=N-domain +P26793 UniProtKB Region 120 251 . . . Note=I-domain +P26793 UniProtKB Region 339 347 . . . Note=Interaction with PCNA;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140 +P26793 UniProtKB Metal binding 34 34 . . . Note=Magnesium 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140 +P26793 UniProtKB Metal binding 87 87 . . . Note=Magnesium 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140 +P26793 UniProtKB Metal binding 156 156 . . . Note=Magnesium 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140 +P26793 UniProtKB Metal binding 158 158 . . . Note=Magnesium 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140 +P26793 UniProtKB Metal binding 177 177 . . . Note=Magnesium 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140 +P26793 UniProtKB Metal binding 179 179 . . . Note=Magnesium 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140 +P26793 UniProtKB Metal binding 231 231 . . . Note=Magnesium 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140 +P26793 UniProtKB Binding site 47 47 . . . Note=DNA substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140 +P26793 UniProtKB Binding site 71 71 . . . Note=DNA substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140 +P26793 UniProtKB Binding site 156 156 . . . Note=DNA substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140 +P26793 UniProtKB Binding site 229 229 . . . Note=DNA substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140 +P26793 UniProtKB Binding site 231 231 . . . Note=DNA substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03140 +P26793 UniProtKB Mutagenesis 67 67 . . . Note=Deficient in double and single flap endonuclease cleavage and exonucleolytic cleavage. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16837458;Dbxref=PMID:16837458 +P26793 UniProtKB Mutagenesis 176 176 . . . Note=Deficient in exonuclease and gap endonuclease activities%2C but retains almost all of its flap endonuclease activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17138563;Dbxref=PMID:17138563 +P26793 UniProtKB Mutagenesis 240 240 . . . Note=Can only cleave double-flap structures with a 3' 1-nucleotide tail. Has no exonuclease activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11825897;Dbxref=PMID:11825897 +P26793 UniProtKB Mutagenesis 346 347 . . . Note=Reduces interaction with POL30 more than 100 fold. FF->GA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10899134;Dbxref=PMID:10899134 +##sequence-region P40988 1 552 +P40988 UniProtKB Chain 1 552 . . . ID=PRO_0000087233;Note=Low-affinity Fe(2+) transport protein +P40988 UniProtKB Topological domain 1 97 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40988 UniProtKB Transmembrane 98 118 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40988 UniProtKB Topological domain 119 225 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40988 UniProtKB Transmembrane 226 246 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40988 UniProtKB Topological domain 247 271 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40988 UniProtKB Transmembrane 272 292 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40988 UniProtKB Topological domain 293 354 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40988 UniProtKB Transmembrane 355 375 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40988 UniProtKB Topological domain 376 383 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40988 UniProtKB Transmembrane 384 404 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40988 UniProtKB Topological domain 405 465 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40988 UniProtKB Transmembrane 466 486 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40988 UniProtKB Topological domain 487 493 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40988 UniProtKB Transmembrane 494 514 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40988 UniProtKB Topological domain 515 552 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40988 UniProtKB Modified residue 48 48 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40988 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40988 UniProtKB Cross-link 39 39 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P40988 UniProtKB Sequence conflict 283 283 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40988 UniProtKB Sequence conflict 441 441 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40988 UniProtKB Sequence conflict 450 450 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53918 1 673 +P53918 UniProtKB Chain 1 673 . . . ID=PRO_0000211405;Note=Uncharacterized transporter ESBP6 +P53918 UniProtKB Topological domain 1 208 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Transmembrane 209 229 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Topological domain 230 255 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Transmembrane 256 276 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Topological domain 277 277 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Transmembrane 278 298 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Topological domain 299 315 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Transmembrane 316 336 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Topological domain 337 339 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Transmembrane 340 360 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Topological domain 361 372 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Transmembrane 373 393 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Topological domain 394 426 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Transmembrane 427 447 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Topological domain 448 504 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Transmembrane 505 525 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Topological domain 526 549 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Transmembrane 550 570 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Topological domain 571 584 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Transmembrane 585 605 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Topological domain 606 673 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Modified residue 57 57 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53918 UniProtKB Modified residue 112 112 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53918 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53918 UniProtKB Modified residue 637 637 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53918 UniProtKB Glycosylation 230 230 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Glycosylation 471 471 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53918 UniProtKB Glycosylation 492 492 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08119 1 714 +Q08119 UniProtKB Chain 1 714 . . . ID=PRO_0000227694;Note=Protein ESC8 +##sequence-region P17214 1 699 +P17214 UniProtKB Chain 1 699 . . . ID=PRO_0000087072;Note=Telomere elongation protein EST1 +P17214 UniProtKB Sequence conflict 49 49 . . . Note=R->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17214 UniProtKB Sequence conflict 85 85 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17214 UniProtKB Sequence conflict 287 287 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17214 UniProtKB Sequence conflict 351 351 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17214 UniProtKB Sequence conflict 535 535 . . . Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17214 UniProtKB Sequence conflict 571 571 . . . Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17214 UniProtKB Sequence conflict 579 579 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17214 UniProtKB Sequence conflict 582 582 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17214 UniProtKB Sequence conflict 665 665 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08822 1 631 +Q08822 UniProtKB Domain 591 620 . . . Note=4Fe-4S ferredoxin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00711 +Q08822 UniProtKB Nucleotide binding 65 79 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08822 UniProtKB Metal binding 574 574 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08822 UniProtKB Metal binding 600 600 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08822 UniProtKB Metal binding 603 603 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08822 UniProtKB Metal binding 606 606 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P35731 1 278 +P35731 UniProtKB Chain 1 278 . . . ID=PRO_0000054872;Note=3-oxoacyl-[acyl-carrier-protein] reductase +P35731 UniProtKB Nucleotide binding 8 32 . . . Note=NAD or NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35731 UniProtKB Active site 198 198 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001 +P35731 UniProtKB Binding site 183 183 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35731 UniProtKB Beta strand 2 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Helix 15 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Beta strand 30 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Helix 38 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Helix 49 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Beta strand 60 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Helix 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Helix 72 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Beta strand 79 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Beta strand 86 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Beta strand 91 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Helix 100 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Beta strand 108 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Helix 129 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Helix 134 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Helix 146 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Helix 167 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Beta strand 172 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FD3 +P35731 UniProtKB Beta strand 177 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Helix 184 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Beta strand 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Helix 196 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Helix 217 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Beta strand 222 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +P35731 UniProtKB Helix 246 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HBG +P35731 UniProtKB Helix 260 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FDA +##sequence-region P38913 1 306 +P38913 UniProtKB Chain 1 306 . . . ID=PRO_0000100691;Note=FAD synthase +P38913 UniProtKB Helix 3 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Helix 25 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Turn 44 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Beta strand 51 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Helix 64 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Beta strand 102 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Helix 114 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Beta strand 129 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Helix 144 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Beta strand 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Beta strand 169 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Beta strand 177 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Beta strand 189 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Turn 193 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Helix 199 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Helix 215 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Turn 227 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Helix 234 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Helix 238 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Helix 248 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Turn 255 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Helix 274 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Turn 280 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Helix 290 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Helix 296 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +P38913 UniProtKB Turn 299 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WSI +##sequence-region P38224 1 298 +P38224 UniProtKB Chain 1 298 . . . ID=PRO_0000087242;Note=Factor-induced gene 1 protein +P38224 UniProtKB Transmembrane 17 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38224 UniProtKB Transmembrane 163 183 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38224 UniProtKB Transmembrane 195 215 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38224 UniProtKB Transmembrane 243 263 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38224 UniProtKB Modified residue 288 288 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38224 UniProtKB Modified residue 293 293 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38224 UniProtKB Modified residue 296 296 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38224 UniProtKB Natural variant 1 5 . . . Note=In strain: CLIB 556 haplotype Ha1 and CLIB 630. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38224 UniProtKB Natural variant 153 153 . . . Note=In strain: CLIB 413 haplotype Ha1. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38224 UniProtKB Natural variant 203 203 . . . Note=In strain: CLIB 630. I->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38224 UniProtKB Natural variant 204 204 . . . Note=In strain: K1. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38224 UniProtKB Natural variant 220 220 . . . Note=In strain: CLIB 413 haplotype Ha2. A->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38224 UniProtKB Natural variant 223 223 . . . Note=In strain: CLIB 630. R->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38224 UniProtKB Natural variant 236 236 . . . Note=In strain: CLIB 219. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P38224 UniProtKB Natural variant 241 241 . . . Note=In strain: CLIB 388 haplotype Ha2. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +##sequence-region P40020 1 876 +P40020 UniProtKB Chain 1 876 . . . ID=PRO_0000058446;Note=Factor interacting with REF2 +P40020 UniProtKB Compositional bias 655 683 . . . Note=Ser-rich +P40020 UniProtKB Modified residue 81 81 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40020 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40020 UniProtKB Modified residue 225 225 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40020 UniProtKB Natural variant 614 614 . . . Note=In strain: ATCC 200060 / W303. P->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9236779;Dbxref=PMID:9236779 +##sequence-region Q08906 1 153 +Q08906 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08906 UniProtKB Chain 19 130 . . . ID=PRO_0000021267;Note=Facilitator of iron transport 2 +Q08906 UniProtKB Propeptide 131 153 . . . ID=PRO_0000021268;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08906 UniProtKB Compositional bias 5 106 . . . Note=Thr-rich +Q08906 UniProtKB Compositional bias 111 129 . . . Note=Poly-Ser +Q08906 UniProtKB Lipidation 130 130 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08906 UniProtKB Glycosylation 92 92 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P12385 1 437 +P12385 UniProtKB Chain 1 437 . . . ID=PRO_0000143167;Note=Eukaryotic peptide chain release factor subunit 1 +P12385 UniProtKB Modified residue 182 182 . . . Note=N5-methylglutamine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15509572,ECO:0000269|PubMed:16321977;Dbxref=PMID:15509572,PMID:16321977 +P12385 UniProtKB Modified residue 421 421 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P12385 UniProtKB Cross-link 331 331 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P12385 UniProtKB Sequence conflict 41 41 . . . Note=Q->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12385 UniProtKB Sequence conflict 41 41 . . . Note=Q->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40030 1 148 +P40030 UniProtKB Chain 1 148 . . . ID=PRO_0000193908;Note=Ergosterol biosynthetic protein 28 +P40030 UniProtKB Topological domain 1 25 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40030 UniProtKB Transmembrane 26 46 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40030 UniProtKB Topological domain 47 92 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40030 UniProtKB Transmembrane 93 113 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40030 UniProtKB Topological domain 114 120 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40030 UniProtKB Transmembrane 121 136 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40030 UniProtKB Topological domain 137 148 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03103 1 563 +Q03103 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03103 UniProtKB Chain 19 563 . . . ID=PRO_0000008429;Note=Endoplasmic oxidoreductin-1 +Q03103 UniProtKB Active site 352 352 . . . Note=Nucleophile;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408 +Q03103 UniProtKB Active site 355 355 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408 +Q03103 UniProtKB Binding site 187 187 . . . Note=FAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408 +Q03103 UniProtKB Binding site 189 189 . . . Note=FAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408 +Q03103 UniProtKB Binding site 200 200 . . . Note=FAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408 +Q03103 UniProtKB Binding site 228 228 . . . Note=FAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408 +Q03103 UniProtKB Binding site 231 231 . . . Note=FAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408 +Q03103 UniProtKB Binding site 260 260 . . . Note=FAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408 +Q03103 UniProtKB Glycosylation 21 21 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03103 UniProtKB Glycosylation 35 35 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03103 UniProtKB Glycosylation 53 53 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03103 UniProtKB Glycosylation 130 130 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03103 UniProtKB Glycosylation 342 342 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03103 UniProtKB Glycosylation 425 425 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03103 UniProtKB Glycosylation 458 458 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03103 UniProtKB Glycosylation 468 468 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03103 UniProtKB Glycosylation 491 491 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03103 UniProtKB Disulfide bond 90 349 . . . Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1RP4,ECO:0000244|PDB:1RQ1,ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408 +Q03103 UniProtKB Disulfide bond 100 105 . . . Note=Redox-active;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1RP4,ECO:0000244|PDB:1RQ1,ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408 +Q03103 UniProtKB Disulfide bond 143 166 . . . Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1RP4,ECO:0000244|PDB:1RQ1,ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408 +Q03103 UniProtKB Disulfide bond 150 295 . . . Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1RP4,ECO:0000244|PDB:1RQ1,ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408 +Q03103 UniProtKB Disulfide bond 352 355 . . . Note=Redox-active;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1RP4,ECO:0000244|PDB:1RQ1,ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408 +Q03103 UniProtKB Mutagenesis 90 90 . . . Note=No effect. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10982384,ECO:0000269|PubMed:17448992;Dbxref=PMID:10982384,PMID:17448992 +Q03103 UniProtKB Mutagenesis 100 100 . . . Note=Impairs the capture of mixed-disulfide with PDI1 thereby blocking its function. Loss of activity%3B when associated with A-105. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10982384,ECO:0000269|PubMed:17448992;Dbxref=PMID:10982384,PMID:17448992 +Q03103 UniProtKB Mutagenesis 105 105 . . . Note=Loss of activity. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10982384,ECO:0000269|PubMed:17448992;Dbxref=PMID:10982384,PMID:17448992 +Q03103 UniProtKB Mutagenesis 143 143 . . . Note=No effect%3B when associated with A-166. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17448992;Dbxref=PMID:17448992 +Q03103 UniProtKB Mutagenesis 150 150 . . . Note=Loss of regulatory disulfide bond and strongly increased activity towards PDI%3B when associated with A-295. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17448992;Dbxref=PMID:17448992 +Q03103 UniProtKB Mutagenesis 166 166 . . . Note=No effect%3B when associated with A-143. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17448992;Dbxref=PMID:17448992 +Q03103 UniProtKB Mutagenesis 208 208 . . . Note=No effect. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10982384;Dbxref=PMID:10982384 +Q03103 UniProtKB Mutagenesis 229 229 . . . Note=In ERO1-1%3B induces defective folding of disulfide proteins. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15163408;Dbxref=PMID:15163408 +Q03103 UniProtKB Mutagenesis 231 231 . . . Note=In ERO1-2%3B induces defective folding of disulfide proteins. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9659914;Dbxref=PMID:9659914 +Q03103 UniProtKB Mutagenesis 295 295 . . . Note=Loss of regulatory disulfide bond and strongly increased activity towards PDI%3B when associated with A-150. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17448992;Dbxref=PMID:17448992 +Q03103 UniProtKB Mutagenesis 349 349 . . . Note=Does not affect activity but increases by twofold the amount of protein found in mixed disulfide with PDI1 or MPD2. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10982384;Dbxref=PMID:10982384 +Q03103 UniProtKB Mutagenesis 352 352 . . . Note=Loss of activity. Prevents its reoxidation thereby blocking its function. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10982384,ECO:0000269|PubMed:17448992;Dbxref=PMID:10982384,PMID:17448992 +Q03103 UniProtKB Mutagenesis 355 355 . . . Note=Loss of activity. Prevents its reoxidation thereby blocking its function. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10982384,ECO:0000269|PubMed:17448992;Dbxref=PMID:10982384,PMID:17448992 +Q03103 UniProtKB Sequence conflict 555 555 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03103 UniProtKB Helix 56 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Turn 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Beta strand 80 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Beta strand 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Beta strand 95 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RP4 +Q03103 UniProtKB Turn 102 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Beta strand 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NVJ +Q03103 UniProtKB Helix 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RP4 +Q03103 UniProtKB Helix 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Helix 122 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Turn 130 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Beta strand 133 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RQ1 +Q03103 UniProtKB Beta strand 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RQ1 +Q03103 UniProtKB Helix 141 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Helix 146 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Turn 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RP4 +Q03103 UniProtKB Beta strand 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RP4 +Q03103 UniProtKB Helix 165 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Beta strand 176 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Turn 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Helix 193 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Helix 216 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Beta strand 241 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Turn 245 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Helix 254 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Turn 261 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Helix 265 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Helix 286 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Helix 297 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Helix 316 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Turn 325 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Helix 330 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Helix 347 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Helix 353 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Helix 381 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +Q03103 UniProtKB Helix 393 424 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M31 +##sequence-region P39704 1 215 +P39704 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39704 UniProtKB Chain 26 215 . . . ID=PRO_0000010409;Note=Protein ERP2 +P39704 UniProtKB Topological domain 26 182 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39704 UniProtKB Transmembrane 183 203 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39704 UniProtKB Topological domain 204 215 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39704 UniProtKB Domain 41 123 . . . Note=GOLD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00096 +##sequence-region P17261 1 260 +P17261 UniProtKB Chain 1 260 . . . ID=PRO_0000205519;Note=Cystine transporter +P17261 UniProtKB Transmembrane 7 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17261 UniProtKB Transmembrane 40 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17261 UniProtKB Transmembrane 81 102 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17261 UniProtKB Transmembrane 118 138 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17261 UniProtKB Transmembrane 151 175 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17261 UniProtKB Transmembrane 185 205 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17261 UniProtKB Transmembrane 227 247 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17261 UniProtKB Domain 1 67 . . . Note=PQ-loop 1 +P17261 UniProtKB Domain 162 212 . . . Note=PQ-loop 2 +P17261 UniProtKB Glycosylation 177 177 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53173 1 138 +P53173 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9732282;Dbxref=PMID:9732282 +P53173 UniProtKB Chain 2 138 . . . ID=PRO_0000122236;Note=ER-derived vesicles protein ERV14 +P53173 UniProtKB Topological domain 2 6 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53173 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53173 UniProtKB Topological domain 28 52 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53173 UniProtKB Transmembrane 53 73 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53173 UniProtKB Topological domain 74 111 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53173 UniProtKB Transmembrane 112 132 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53173 UniProtKB Topological domain 133 138 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03661 1 1658 +Q03661 UniProtKB Chain 1 1658 . . . ID=PRO_0000203333;Note=Silent chromatin protein ESC1 +Q03661 UniProtKB Modified residue 500 500 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03661 UniProtKB Modified residue 532 532 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q03661 UniProtKB Modified residue 579 579 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03661 UniProtKB Modified residue 583 583 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03661 UniProtKB Modified residue 608 608 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03661 UniProtKB Modified residue 662 662 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03661 UniProtKB Modified residue 865 865 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03661 UniProtKB Modified residue 866 866 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03661 UniProtKB Modified residue 888 888 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03661 UniProtKB Modified residue 911 911 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q03661 UniProtKB Modified residue 937 937 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03661 UniProtKB Modified residue 1092 1092 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03661 UniProtKB Modified residue 1096 1096 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03661 UniProtKB Modified residue 1098 1098 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03661 UniProtKB Modified residue 1166 1166 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03661 UniProtKB Modified residue 1176 1176 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03661 UniProtKB Modified residue 1178 1178 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03661 UniProtKB Modified residue 1214 1214 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03661 UniProtKB Modified residue 1254 1254 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03661 UniProtKB Modified residue 1290 1290 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03661 UniProtKB Modified residue 1326 1326 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q03661 UniProtKB Modified residue 1332 1332 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03661 UniProtKB Modified residue 1403 1403 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03661 UniProtKB Modified residue 1409 1409 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03661 UniProtKB Modified residue 1450 1450 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03661 UniProtKB Modified residue 1454 1454 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03661 UniProtKB Modified residue 1539 1539 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03661 UniProtKB Modified residue 1590 1590 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03661 UniProtKB Modified residue 1591 1591 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P53743 1 316 +P53743 UniProtKB Chain 1 316 . . . ID=PRO_0000203480;Note=Pre-rRNA-processing protein ESF2 +P53743 UniProtKB Domain 114 204 . . . Note=RRM +P53743 UniProtKB Modified residue 7 7 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53743 UniProtKB Modified residue 13 13 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53743 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P42940 1 261 +P42940 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P42940 UniProtKB Chain 2 261 . . . ID=PRO_0000167874;Note=Probable electron transfer flavoprotein subunit beta +P42940 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region Q08421 1 412 +Q08421 UniProtKB Chain 1 412 . . . ID=PRO_0000245279;Note=Enhancer of translation termination 1 +Q08421 UniProtKB Modified residue 30 30 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q08421 UniProtKB Sequence conflict 338 338 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39875 1 702 +P39875 UniProtKB Chain 1 702 . . . ID=PRO_0000154045;Note=Exodeoxyribonuclease 1 +P39875 UniProtKB Region 1 96 . . . Note=N-domain +P39875 UniProtKB Region 114 247 . . . Note=I-domain +P39875 UniProtKB Compositional bias 501 520 . . . Note=Asp/Glu-rich (acidic) +P39875 UniProtKB Compositional bias 537 553 . . . Note=Asp/Glu-rich (acidic) +P39875 UniProtKB Compositional bias 618 625 . . . Note=Asp-rich (acidic) +P39875 UniProtKB Metal binding 30 30 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39875 UniProtKB Metal binding 78 78 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39875 UniProtKB Metal binding 150 150 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39875 UniProtKB Metal binding 152 152 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39875 UniProtKB Metal binding 171 171 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39875 UniProtKB Metal binding 173 173 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39875 UniProtKB Metal binding 227 227 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39875 UniProtKB Modified residue 372 372 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P38289 1 585 +P38289 UniProtKB Transit peptide 1 26 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38289 UniProtKB Chain 27 585 . . . ID=PRO_0000202501;Note=Exonuclease V%2C mitochondrial +P38289 UniProtKB Metal binding 141 141 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38289 UniProtKB Metal binding 549 549 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38289 UniProtKB Metal binding 552 552 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38289 UniProtKB Metal binding 558 558 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38289 UniProtKB Mutagenesis 270 270 . . . Note=Impairs exonuclease activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20086101;Dbxref=PMID:20086101 +P38289 UniProtKB Mutagenesis 320 320 . . . Note=Impairs exonuclease activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20086101;Dbxref=PMID:20086101 +##sequence-region P38261 1 753 +P38261 UniProtKB Chain 1 753 . . . ID=PRO_0000118987;Note=Exocyst complex component EXO84 +P38261 UniProtKB Coiled coil 227 279 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38261 UniProtKB Coiled coil 531 585 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38261 UniProtKB Modified residue 58 58 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38261 UniProtKB Modified residue 139 139 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38261 UniProtKB Modified residue 482 482 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38261 UniProtKB Cross-link 219 219 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P38261 UniProtKB Helix 528 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S +P38261 UniProtKB Helix 552 568 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S +P38261 UniProtKB Helix 579 604 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S +P38261 UniProtKB Helix 609 621 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S +P38261 UniProtKB Helix 625 645 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S +P38261 UniProtKB Helix 653 678 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S +P38261 UniProtKB Helix 684 708 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S +P38261 UniProtKB Helix 717 728 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S +P38261 UniProtKB Helix 729 733 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S +P38261 UniProtKB Helix 738 746 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S +P38261 UniProtKB Helix 747 751 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2D2S +##sequence-region P09201 1 348 +P09201 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3008716;Dbxref=PMID:3008716 +P09201 UniProtKB Chain 2 348 . . . ID=PRO_0000200511;Note=Fructose-1%2C6-bisphosphatase +P09201 UniProtKB Nucleotide binding 38 42 . . . Note=AMP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09201 UniProtKB Nucleotide binding 122 123 . . . Note=AMP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09201 UniProtKB Region 131 134 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09201 UniProtKB Metal binding 79 79 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09201 UniProtKB Metal binding 108 108 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09201 UniProtKB Metal binding 108 108 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09201 UniProtKB Metal binding 128 128 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09201 UniProtKB Metal binding 128 128 . . . Note=Magnesium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09201 UniProtKB Metal binding 130 130 . . . Note=Magnesium 2%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09201 UniProtKB Metal binding 131 131 . . . Note=Magnesium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09201 UniProtKB Metal binding 292 292 . . . Note=Magnesium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09201 UniProtKB Binding site 222 222 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09201 UniProtKB Binding site 256 256 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09201 UniProtKB Binding site 276 276 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09201 UniProtKB Binding site 286 286 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09201 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P09201 UniProtKB Sequence conflict 278 278 . . . Note=C->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P34756 1 2278 +P34756 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P34756 UniProtKB Chain 2 2278 . . . ID=PRO_0000185451;Note=1-phosphatidylinositol 3-phosphate 5-kinase FAB1 +P34756 UniProtKB Domain 1932 2266 . . . Note=PIPK;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00781 +P34756 UniProtKB Zinc finger 240 299 . . . Note=FYVE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091 +P34756 UniProtKB Region 2 676 . . . Note=Required for localization to the vacuole membrane +P34756 UniProtKB Region 800 1500 . . . Note=Mediates interaction with VAC14 and FIG4 +P34756 UniProtKB Compositional bias 393 397 . . . Note=Poly-Pro +P34756 UniProtKB Compositional bias 571 590 . . . Note=Poly-Asn +P34756 UniProtKB Compositional bias 1808 1811 . . . Note=Poly-Thr +P34756 UniProtKB Compositional bias 1891 1897 . . . Note=Poly-Gln +P34756 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P34756 UniProtKB Modified residue 186 186 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34756 UniProtKB Modified residue 1627 1627 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34756 UniProtKB Modified residue 1630 1630 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34756 UniProtKB Modified residue 1938 1938 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34756 UniProtKB Modified residue 1953 1953 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P34756 UniProtKB Mutagenesis 262 262 . . . Note=Cells show growth at 38 degrees Celsius. Failure to localize to the vacuole membrane. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18653468;Dbxref=PMID:18653468 +P34756 UniProtKB Mutagenesis 864 864 . . . Note=Loss of interaction with VAC14. Failure to localize to the vacuole membrane. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19037259;Dbxref=PMID:19037259 +P34756 UniProtKB Mutagenesis 1017 1017 . . . Note=Cells are defective for growth at 38 degrees Celsius. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18653468;Dbxref=PMID:18653468 +P34756 UniProtKB Mutagenesis 1243 1243 . . . Note=Cells are defective for growth at 38 degrees Celsius and show single-lobed%2C enlarged vacuoles. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18653468;Dbxref=PMID:18653468 +P34756 UniProtKB Mutagenesis 2134 2134 . . . Note=Cells are defective for growth at 38 degrees Celsius. PtdIns(3%2C5)P2 levels are severely reduced. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18653468;Dbxref=PMID:18653468 +P34756 UniProtKB Sequence conflict 2275 2275 . . . Note=R->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32771 1 386 +P32771 UniProtKB Chain 1 386 . . . ID=PRO_0000160785;Note=S-(hydroxymethyl)glutathione dehydrogenase +P32771 UniProtKB Metal binding 49 49 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32771 UniProtKB Metal binding 71 71 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32771 UniProtKB Metal binding 101 101 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32771 UniProtKB Metal binding 104 104 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32771 UniProtKB Metal binding 107 107 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32771 UniProtKB Metal binding 115 115 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32771 UniProtKB Metal binding 179 179 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P32604 1 452 +P32604 UniProtKB Chain 1 452 . . . ID=PRO_0000179975;Note=Fructose-2%2C6-bisphosphatase +P32604 UniProtKB Nucleotide binding 20 28 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Nucleotide binding 143 148 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Nucleotide binding 324 327 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07953 +P32604 UniProtKB Nucleotide binding 368 372 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07953 +P32604 UniProtKB Region 1 223 . . . Note=6-phosphofructo-2-kinase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32604 UniProtKB Region 224 452 . . . Note=Fructose-2%2C6-bisphosphatase +P32604 UniProtKB Active site 104 104 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32604 UniProtKB Active site 232 232 . . . Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Active site 302 302 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Binding site 53 53 . . . Note=Fructose 6-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Binding site 78 78 . . . Note=Fructose 6-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Binding site 106 106 . . . Note=Fructose 6-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Binding site 112 112 . . . Note=Fructose 6-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Binding site 169 169 . . . Note=Fructose 6-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Binding site 173 173 . . . Note=Fructose 6-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Binding site 231 231 . . . Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Binding site 238 238 . . . Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Binding site 244 244 . . . Note=Fructose 2%2C6-bisphosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Binding site 313 313 . . . Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Binding site 327 327 . . . Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Binding site 331 331 . . . Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Binding site 342 342 . . . Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Binding site 368 368 . . . Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Binding site 372 372 . . . Note=Fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07953 +P32604 UniProtKB Binding site 404 404 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Site 231 231 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Site 238 238 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Site 367 367 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16875 +P32604 UniProtKB Modified residue 435 435 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32604 UniProtKB Modified residue 446 446 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P32604 UniProtKB Sequence conflict 199 199 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32604 UniProtKB Sequence conflict 362 362 . . . Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32604 UniProtKB Sequence conflict 448 449 . . . Note=LE->FQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12099 1 399 +Q12099 UniProtKB Chain 1 399 . . . ID=PRO_0000054975;Note=ATP-dependent RNA helicase FAL1 +Q12099 UniProtKB Domain 54 227 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q12099 UniProtKB Domain 238 399 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q12099 UniProtKB Nucleotide binding 67 74 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q12099 UniProtKB Motif 23 51 . . . Note=Q motif +Q12099 UniProtKB Motif 173 176 . . . Note=DEAD box +Q12099 UniProtKB Mutagenesis 85 85 . . . Note=Decreases the amount of 40S ribosomal subunit%3B when associated with R-144%3B A-244 and A-246. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372960;Dbxref=PMID:9372960 +Q12099 UniProtKB Mutagenesis 144 144 . . . Note=Decreases the amount of 40S ribosomal subunit%3B when associated with T-85%3B A-244 and A-246. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372960;Dbxref=PMID:9372960 +Q12099 UniProtKB Mutagenesis 244 244 . . . Note=Decreases the amount of 40S ribosomal subunit%3B when associated with T-85%3B R-144 and A-246. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372960;Dbxref=PMID:9372960 +Q12099 UniProtKB Mutagenesis 246 246 . . . Note=Decreases the amount of 40S ribosomal subunit%3B when associated with T-85%3B R-144 and A-244. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372960;Dbxref=PMID:9372960 +##sequence-region Q04952 1 1785 +Q04952 UniProtKB Chain 1 1785 . . . ID=PRO_0000121727;Note=1%2C3-beta-glucan synthase component FKS3 +Q04952 UniProtKB Transmembrane 337 357 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Transmembrane 375 395 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Transmembrane 415 435 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Transmembrane 444 464 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Transmembrane 508 528 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Transmembrane 547 567 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Transmembrane 572 592 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Transmembrane 712 732 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Transmembrane 1215 1235 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Transmembrane 1268 1288 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Transmembrane 1303 1323 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Transmembrane 1370 1390 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Transmembrane 1394 1414 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Transmembrane 1475 1495 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Transmembrane 1514 1534 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Transmembrane 1549 1569 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Transmembrane 1585 1605 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Transmembrane 1655 1675 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Transmembrane 1713 1733 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Glycosylation 844 844 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Glycosylation 874 874 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Glycosylation 955 955 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Glycosylation 1002 1002 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Glycosylation 1170 1170 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Glycosylation 1360 1360 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Glycosylation 1579 1579 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04952 UniProtKB Glycosylation 1761 1761 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36170 1 1169 +P36170 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36170 UniProtKB Chain 25 1146 . . . ID=PRO_0000014336;Note=Flocculation protein FLO10 +P36170 UniProtKB Propeptide 1147 1169 . . . ID=PRO_0000372449;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36170 UniProtKB Domain 111 271 . . . Note=PA14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01164 +P36170 UniProtKB Repeat 303 326 . . . Note=1-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P36170 UniProtKB Repeat 330 356 . . . Note=1-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P36170 UniProtKB Repeat 357 383 . . . Note=1-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P36170 UniProtKB Repeat 384 419 . . . Note=2-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P36170 UniProtKB Repeat 420 446 . . . Note=1-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P36170 UniProtKB Repeat 447 482 . . . Note=2-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P36170 UniProtKB Repeat 483 509 . . . Note=1-5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P36170 UniProtKB Repeat 510 545 . . . Note=2-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P36170 UniProtKB Repeat 546 572 . . . Note=1-6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P36170 UniProtKB Repeat 573 608 . . . Note=2-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P36170 UniProtKB Region 303 572 . . . Note=6 X 27 AA approximate repeats%2C Ser/Thr-rich +P36170 UniProtKB Region 384 608 . . . Note=4 X 36 AA approximate repeats%2C Ser/Thr-rich +P36170 UniProtKB Compositional bias 299 1143 . . . Note=Ser/Thr-rich +P36170 UniProtKB Lipidation 1146 1146 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36170 UniProtKB Glycosylation 122 122 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36170 UniProtKB Glycosylation 157 157 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36170 UniProtKB Glycosylation 279 279 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36170 UniProtKB Glycosylation 389 389 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36170 UniProtKB Glycosylation 452 452 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36170 UniProtKB Glycosylation 515 515 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36170 UniProtKB Glycosylation 578 578 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36170 UniProtKB Glycosylation 656 656 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36170 UniProtKB Glycosylation 686 686 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36170 UniProtKB Glycosylation 879 879 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36170 UniProtKB Glycosylation 1092 1092 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36170 UniProtKB Glycosylation 1099 1099 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P08640 1 1367 +P08640 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08640 UniProtKB Chain 22 1346 . . . ID=PRO_0000019586;Note=Flocculation protein FLO11 +P08640 UniProtKB Propeptide 1347 1367 . . . ID=PRO_0000019587;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08640 UniProtKB Domain 31 207 . . . Note=Flo11;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01168 +P08640 UniProtKB Repeat 210 219 . . . Note=1-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 220 229 . . . Note=1-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 230 239 . . . Note=1-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 240 249 . . . Note=1-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 262 274 . . . Note=2-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 275 287 . . . Note=2-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 313 327 . . . Note=3-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 328 342 . . . Note=3-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 343 354 . . . Note=4-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 355 369 . . . Note=3-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 370 381 . . . Note=4-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 382 393 . . . Note=4-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 394 408 . . . Note=3-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 409 420 . . . Note=4-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 421 432 . . . Note=4-5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 433 444 . . . Note=4-6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 445 456 . . . Note=4-7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 457 471 . . . Note=3-5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 472 483 . . . Note=4-8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 484 498 . . . Note=3-6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 499 510 . . . Note=4-9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 511 525 . . . Note=3-7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 526 540 . . . Note=3-8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 541 552 . . . Note=4-10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 568 579 . . . Note=4-11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 580 594 . . . Note=3-9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 595 609 . . . Note=3-10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 610 625 . . . Note=3-11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 625 636 . . . Note=4-12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 637 651 . . . Note=3-12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 652 666 . . . Note=3-13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 667 681 . . . Note=3-14;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 682 693 . . . Note=4-13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 694 705 . . . Note=4-14;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 706 720 . . . Note=3-15;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 721 735 . . . Note=3-16;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 736 750 . . . Note=3-17;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 751 762 . . . Note=4-15;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 763 777 . . . Note=3-18;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 778 792 . . . Note=3-19;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 808 822 . . . Note=3-21;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 838 852 . . . Note=3-20;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 865 879 . . . Note=3-22;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 937 968 . . . Note=5-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 981 1012 . . . Note=5-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Repeat 1088 1119 . . . Note=5-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P08640 UniProtKB Region 22 209 . . . Note=Involved in homotypic binding;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08640 UniProtKB Region 210 249 . . . Note=4 X 10 AA repeats%2C Ser/Thr-rich +P08640 UniProtKB Region 262 287 . . . Note=2 X 13 AA repeats%2C Thr-rich +P08640 UniProtKB Region 313 852 . . . Note=22 X 15 AA approximate repeats%2C Ser-rich +P08640 UniProtKB Region 343 762 . . . Note=15 X 12 AA repeats%2C Ser/Thr-rich +P08640 UniProtKB Region 937 1119 . . . Note=3 X 32 AA tandem repeats%2C Thr-rich +P08640 UniProtKB Lipidation 1346 1346 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08640 UniProtKB Glycosylation 817 817 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08640 UniProtKB Glycosylation 874 874 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08640 UniProtKB Mutagenesis 1340 1367 . . . Note=Increased shedding%2C associated with loss of GPI-anchor site. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20619652;Dbxref=PMID:20619652 +P08640 UniProtKB Beta strand 31 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Beta strand 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Helix 50 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Turn 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Beta strand 61 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Beta strand 75 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Helix 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Beta strand 93 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Beta strand 102 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Beta strand 108 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Turn 113 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Beta strand 125 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Beta strand 136 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Beta strand 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Beta strand 149 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Helix 157 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Beta strand 171 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Beta strand 186 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Beta strand 195 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +P08640 UniProtKB Helix 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UYR +##sequence-region P32768 1 1537 +P32768 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32768 UniProtKB Chain 25 1514 . . . ID=PRO_0000021273;Note=Flocculation protein FLO1 +P32768 UniProtKB Propeptide 1515 1537 . . . ID=PRO_0000021274;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32768 UniProtKB Domain 74 249 . . . Note=PA14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01164 +P32768 UniProtKB Repeat 278 322 . . . Note=1-1 +P32768 UniProtKB Repeat 323 367 . . . Note=1-2 +P32768 UniProtKB Repeat 368 412 . . . Note=1-3 +P32768 UniProtKB Repeat 413 457 . . . Note=1-4 +P32768 UniProtKB Repeat 458 502 . . . Note=1-5 +P32768 UniProtKB Repeat 503 547 . . . Note=1-6 +P32768 UniProtKB Repeat 548 592 . . . Note=1-7 +P32768 UniProtKB Repeat 593 637 . . . Note=1-8 +P32768 UniProtKB Repeat 638 682 . . . Note=1-9 +P32768 UniProtKB Repeat 683 727 . . . Note=1-10 +P32768 UniProtKB Repeat 728 772 . . . Note=1-11 +P32768 UniProtKB Repeat 773 817 . . . Note=1-12 +P32768 UniProtKB Repeat 818 862 . . . Note=1-13 +P32768 UniProtKB Repeat 863 907 . . . Note=1-14 +P32768 UniProtKB Repeat 908 952 . . . Note=1-15 +P32768 UniProtKB Repeat 953 997 . . . Note=1-16 +P32768 UniProtKB Repeat 998 1042 . . . Note=1-17 +P32768 UniProtKB Repeat 1043 1087 . . . Note=1-18 +P32768 UniProtKB Repeat 1118 1137 . . . Note=2-1 +P32768 UniProtKB Repeat 1138 1157 . . . Note=2-2 +P32768 UniProtKB Repeat 1226 1276 . . . Note=3-1 +P32768 UniProtKB Repeat 1291 1341 . . . Note=3-2 +P32768 UniProtKB Repeat 1342 1392 . . . Note=3-3 +P32768 UniProtKB Repeat 1408 1416 . . . Note=4-1 +P32768 UniProtKB Repeat 1417 1425 . . . Note=4-2 +P32768 UniProtKB Repeat 1426 1434 . . . Note=4-3 +P32768 UniProtKB Region 197 240 . . . Note=Sugar recognition +P32768 UniProtKB Region 278 1087 . . . Note=18 X 45 AA approximate tandem repeats%2C Thr-rich +P32768 UniProtKB Region 1118 1157 . . . Note=2 X 20 AA approximate tandem repeats%2C Ser/Thr-rich +P32768 UniProtKB Region 1226 1392 . . . Note=3 X 51 AA approximate repeats%2C Ser/Thr-rich +P32768 UniProtKB Region 1408 1434 . . . Note=3 X 9 AA approximate tandem repeats%2C Thr-rich +P32768 UniProtKB Lipidation 1514 1514 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32768 UniProtKB Glycosylation 135 135 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32768 UniProtKB Glycosylation 187 187 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32768 UniProtKB Glycosylation 262 262 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32768 UniProtKB Glycosylation 329 329 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32768 UniProtKB Glycosylation 374 374 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32768 UniProtKB Glycosylation 419 419 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32768 UniProtKB Glycosylation 464 464 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32768 UniProtKB Glycosylation 509 509 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32768 UniProtKB Glycosylation 554 554 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32768 UniProtKB Glycosylation 599 599 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32768 UniProtKB Glycosylation 644 644 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32768 UniProtKB Glycosylation 689 689 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32768 UniProtKB Glycosylation 734 734 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32768 UniProtKB Glycosylation 1114 1114 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32768 UniProtKB Natural variant 303 797 . . . Note=In strain: S288c / KV295. Missing +P32768 UniProtKB Natural variant 317 946 . . . Note=In strain: S288c / KV333. Missing +P32768 UniProtKB Natural variant 317 901 . . . Note=In strain: S288c / KV291. Missing +P32768 UniProtKB Sequence conflict 330 330 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 349 349 . . . Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 375 375 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 384 384 . . . Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 416 422 . . . Note=QPWNDTF->HHGTTLL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 429 429 . . . Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 429 429 . . . Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 436 436 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 464 464 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 469 469 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 474 474 . . . Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 519 519 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 550 550 . . . Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 609 609 . . . Note=M->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 637 637 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 699 699 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 706 706 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 926 926 . . . Note=H->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 926 926 . . . Note=H->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 926 926 . . . Note=H->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Sequence conflict 926 926 . . . Note=H->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32768 UniProtKB Beta strand 35 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Helix 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Helix 57 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Helix 63 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Beta strand 69 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Beta strand 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Beta strand 86 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Beta strand 92 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Helix 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Turn 103 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Turn 108 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Turn 125 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Beta strand 135 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Beta strand 147 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Beta strand 160 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Turn 169 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Beta strand 189 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Beta strand 204 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Beta strand 215 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Beta strand 229 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Beta strand 233 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Beta strand 242 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Turn 248 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Beta strand 251 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Beta strand 264 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +P32768 UniProtKB Helix 268 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LHL +##sequence-region Q08023 1 583 +Q08023 UniProtKB Transit peptide 1 25 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08023 UniProtKB Chain 26 583 . . . ID=PRO_0000247338;Note=Protein FMP25%2C mitochondrial +Q08023 UniProtKB Transmembrane 83 105 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08023 UniProtKB Repeat 332 389 . . . Note=RCC1 1 +Q08023 UniProtKB Repeat 390 452 . . . Note=RCC1 2 +Q08023 UniProtKB Repeat 459 510 . . . Note=RCC1 3 +Q08023 UniProtKB Repeat 512 569 . . . Note=RCC1 4 +Q08023 UniProtKB Sequence conflict 160 160 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P43557 1 207 +P43557 UniProtKB Transmembrane 184 206 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43557 UniProtKB Coiled coil 100 136 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53233 1 369 +P53233 UniProtKB Chain 1 369 . . . ID=PRO_0000086113;Note=Probable serine/threonine-protein kinase FMP48 +P53233 UniProtKB Domain 2 369 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53233 UniProtKB Nucleotide binding 8 16 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53233 UniProtKB Active site 133 133 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P53233 UniProtKB Binding site 31 31 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +##sequence-region P50264 1 508 +P50264 UniProtKB Chain 1 508 . . . ID=PRO_0000087317;Note=Polyamine oxidase FMS1 +P50264 UniProtKB Beta strand 7 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 18 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Beta strand 34 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Beta strand 40 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Beta strand 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 54 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Beta strand 58 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Turn 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 73 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Beta strand 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ECH +P50264 UniProtKB Beta strand 98 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Turn 102 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Turn 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 115 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Turn 131 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BNM +P50264 UniProtKB Helix 141 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 158 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 169 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 172 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Turn 179 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 184 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Beta strand 196 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 201 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Beta strand 217 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BNU +P50264 UniProtKB Beta strand 223 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Beta strand 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GDP +P50264 UniProtKB Beta strand 234 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Beta strand 243 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 255 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 260 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Beta strand 263 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CNT +P50264 UniProtKB Beta strand 268 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CND +P50264 UniProtKB Beta strand 273 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 280 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 286 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GDP +P50264 UniProtKB Beta strand 290 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BI4 +P50264 UniProtKB Beta strand 295 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Beta strand 311 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 321 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 333 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 353 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ECH +P50264 UniProtKB Beta strand 358 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 363 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Beta strand 370 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 380 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Turn 387 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 391 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 420 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GDP +P50264 UniProtKB Helix 424 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Beta strand 427 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CN8 +P50264 UniProtKB Beta strand 431 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Turn 440 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Turn 444 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 461 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Beta strand 470 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +P50264 UniProtKB Helix 479 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BI4 +P50264 UniProtKB Turn 484 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GDP +P50264 UniProtKB Helix 489 508 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RSG +##sequence-region P40546 1 346 +P40546 UniProtKB Chain 1 346 . . . ID=PRO_0000087172;Note=Protein FAF1 +P40546 UniProtKB Helix 146 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +##sequence-region P46671 1 204 +P46671 UniProtKB Chain 1 204 . . . ID=PRO_0000087191;Note=Factor arrest protein 3 +P46671 UniProtKB Sequence conflict 6 6 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46671 UniProtKB Sequence conflict 131 131 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q05040 1 523 +Q05040 UniProtKB Chain 1 523 . . . ID=PRO_0000087193;Note=Factor arrest protein 8 +Q05040 UniProtKB Coiled coil 26 76 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05040 UniProtKB Modified residue 115 115 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q05040 UniProtKB Modified residue 132 132 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P38137 1 543 +P38137 UniProtKB Chain 1 543 . . . ID=PRO_0000193182;Note=Peroxisomal-coenzyme A synthetase +P38137 UniProtKB Nucleotide binding 190 207 . . . Note=AMP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38137 UniProtKB Motif 541 543 . . . Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12178 1 158 +Q12178 UniProtKB Chain 1 158 . . . ID=PRO_0000171702;Note=Cytosine deaminase +Q12178 UniProtKB Domain 9 129 . . . Note=CMP/dCMP-type deaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01083 +Q12178 UniProtKB Compositional bias 129 132 . . . Note=Poly-Val +Q12178 UniProtKB Active site 64 64 . . . Note=Proton donor +Q12178 UniProtKB Metal binding 62 62 . . . Note=Zinc%3B catalytic +Q12178 UniProtKB Metal binding 91 91 . . . Note=Zinc%3B catalytic +Q12178 UniProtKB Metal binding 94 94 . . . Note=Zinc%3B catalytic +Q12178 UniProtKB Binding site 51 51 . . . Note=Substrate +Q12178 UniProtKB Binding site 155 155 . . . Note=Substrate +Q12178 UniProtKB Helix 11 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O +Q12178 UniProtKB Beta strand 34 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O +Q12178 UniProtKB Turn 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O +Q12178 UniProtKB Beta strand 45 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O +Q12178 UniProtKB Helix 53 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O +Q12178 UniProtKB Helix 63 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O +Q12178 UniProtKB Helix 76 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O +Q12178 UniProtKB Beta strand 82 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O +Q12178 UniProtKB Helix 92 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O +Q12178 UniProtKB Beta strand 105 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O +Q12178 UniProtKB Helix 118 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O +Q12178 UniProtKB Beta strand 128 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O +Q12178 UniProtKB Helix 135 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O +Q12178 UniProtKB Helix 149 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P6O +##sequence-region P25621 1 512 +P25621 UniProtKB Chain 1 512 . . . ID=PRO_0000121367;Note=Pantothenate transporter FEN2 +P25621 UniProtKB Topological domain 1 27 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Transmembrane 28 48 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Topological domain 49 79 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Transmembrane 80 100 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Topological domain 101 102 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Transmembrane 103 123 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Topological domain 124 132 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Transmembrane 133 153 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Topological domain 154 164 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Transmembrane 165 185 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Topological domain 186 198 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Transmembrane 199 219 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Topological domain 220 271 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Transmembrane 272 292 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Topological domain 293 312 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Transmembrane 313 333 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Topological domain 334 342 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Transmembrane 343 363 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Topological domain 364 372 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Transmembrane 373 393 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Topological domain 394 401 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Transmembrane 402 422 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Topological domain 423 434 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Transmembrane 435 455 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25621 UniProtKB Topological domain 456 512 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08907 1 204 +Q08907 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08907 UniProtKB Chain 19 182 . . . ID=PRO_0000021269;Note=Facilitator of iron transport 3 +Q08907 UniProtKB Propeptide 183 204 . . . ID=PRO_0000372453;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08907 UniProtKB Compositional bias 22 191 . . . Note=Ser/Thr-rich +Q08907 UniProtKB Lipidation 182 182 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P19658 1 623 +P19658 UniProtKB Chain 1 623 . . . ID=PRO_0000118975;Note=Exocyst complex component EXO70 +P19658 UniProtKB Sequence conflict 497 497 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19658 UniProtKB Helix 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 74 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 92 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 97 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Beta strand 116 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PFV +P19658 UniProtKB Turn 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7M +P19658 UniProtKB Helix 125 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 161 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 176 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 195 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Turn 215 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 218 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PFV +P19658 UniProtKB Helix 239 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 268 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 298 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PFV +P19658 UniProtKB Helix 304 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Turn 319 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 327 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 370 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 383 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 386 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Turn 393 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 398 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 408 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 423 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 469 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 492 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Turn 496 498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 499 532 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Beta strand 535 537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 542 563 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 571 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 597 599 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Beta strand 600 602 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 603 605 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +P19658 UniProtKB Helix 611 622 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B1E +##sequence-region P53971 1 965 +P53971 UniProtKB Chain 1 965 . . . ID=PRO_0000056343;Note=FKBP12-associated protein 1 +P53971 UniProtKB Domain 733 796 . . . Note=R3H;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00382 +P53971 UniProtKB Zinc finger 68 118 . . . Note=RING-type%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +P53971 UniProtKB Zinc finger 159 177 . . . Note=NF-X1-type 1 +P53971 UniProtKB Zinc finger 216 235 . . . Note=NF-X1-type 2 +P53971 UniProtKB Zinc finger 362 382 . . . Note=NF-X1-type 3 +P53971 UniProtKB Zinc finger 468 487 . . . Note=NF-X1-type 4 +P53971 UniProtKB Zinc finger 586 606 . . . Note=NF-X1-type 5 +P53971 UniProtKB Modified residue 951 951 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53971 UniProtKB Modified residue 958 958 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q05498 1 189 +Q05498 UniProtKB Chain 1 189 . . . ID=PRO_0000253818;Note=rRNA-processing protein FCF1 +Q05498 UniProtKB Domain 63 162 . . . Note=PINc +##sequence-region Q03254 1 732 +Q03254 UniProtKB Chain 1 732 . . . ID=PRO_0000212568;Note=RNA polymerase II subunit A C-terminal domain phosphatase +Q03254 UniProtKB Domain 170 363 . . . Note=FCP1 homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00336 +Q03254 UniProtKB Domain 499 593 . . . Note=BRCT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033 +Q03254 UniProtKB Modified residue 701 701 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03254 UniProtKB Modified residue 718 718 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03254 UniProtKB Modified residue 720 720 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03254 UniProtKB Cross-link 74 74 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q12119 1 530 +Q12119 UniProtKB Chain 1 530 . . . ID=PRO_0000197922;Note=Purine-cytosine permease FCY22 +Q12119 UniProtKB Transmembrane 96 116 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12119 UniProtKB Transmembrane 119 139 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12119 UniProtKB Transmembrane 162 182 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12119 UniProtKB Transmembrane 197 217 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12119 UniProtKB Transmembrane 220 240 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12119 UniProtKB Transmembrane 263 283 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12119 UniProtKB Transmembrane 298 318 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12119 UniProtKB Transmembrane 345 365 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12119 UniProtKB Transmembrane 372 392 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12119 UniProtKB Transmembrane 396 416 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12119 UniProtKB Transmembrane 418 438 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12119 UniProtKB Transmembrane 463 483 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12119 UniProtKB Modified residue 46 46 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P40039 +##sequence-region Q06001 1 478 +Q06001 UniProtKB Chain 1 478 . . . ID=PRO_0000087189;Note=Factor arrest protein 10 +Q06001 UniProtKB Topological domain 1 454 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06001 UniProtKB Transmembrane 455 475 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06001 UniProtKB Topological domain 476 478 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06001 UniProtKB Domain 116 176 . . . Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 +Q06001 UniProtKB Coiled coil 342 426 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06001 UniProtKB Compositional bias 108 115 . . . Note=Poly-Ser +##sequence-region P17064 1 533 +P17064 UniProtKB Chain 1 533 . . . ID=PRO_0000197920;Note=Purine-cytosine permease FCY2 +P17064 UniProtKB Topological domain 1 98 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17064 UniProtKB Transmembrane 99 119 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17064 UniProtKB Topological domain 120 121 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17064 UniProtKB Transmembrane 122 141 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17064 UniProtKB Topological domain 142 198 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17064 UniProtKB Transmembrane 199 218 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17064 UniProtKB Topological domain 219 256 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17064 UniProtKB Transmembrane 257 276 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17064 UniProtKB Topological domain 277 300 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17064 UniProtKB Transmembrane 301 320 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17064 UniProtKB Topological domain 321 347 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17064 UniProtKB Transmembrane 348 367 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17064 UniProtKB Topological domain 368 398 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17064 UniProtKB Transmembrane 399 418 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17064 UniProtKB Topological domain 419 465 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17064 UniProtKB Transmembrane 466 485 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17064 UniProtKB Topological domain 486 533 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17064 UniProtKB Region 165 184 . . . Note=Surface seeking;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17064 UniProtKB Modified residue 18 18 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P17064 UniProtKB Cross-link 16 16 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P17064 UniProtKB Sequence conflict 192 192 . . . Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17064 UniProtKB Sequence conflict 261 261 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17064 UniProtKB Sequence conflict 459 459 . . . Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CF35 1 236 +P0CF35 UniProtKB Chain 1 236 . . . ID=PRO_0000223648;Note=Truncated formate dehydrogenase 2 +P0CF35 UniProtKB Nucleotide binding 36 37 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160 +P0CF35 UniProtKB Nucleotide binding 104 108 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160 +P0CF35 UniProtKB Nucleotide binding 185 188 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160 +P0CF35 UniProtKB Binding site 57 57 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160 +P0CF35 UniProtKB Binding site 130 130 . . . Note=NAD%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160 +P0CF35 UniProtKB Binding site 156 156 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160 +P0CF35 UniProtKB Site 132 132 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160 +P0CF35 UniProtKB Site 185 185 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33160 +##sequence-region P39676 1 399 +P39676 UniProtKB Chain 1 399 . . . ID=PRO_0000052458;Note=Flavohemoprotein +P39676 UniProtKB Domain 147 264 . . . Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716 +P39676 UniProtKB Nucleotide binding 207 210 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39676 UniProtKB Nucleotide binding 281 286 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39676 UniProtKB Nucleotide binding 389 392 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39676 UniProtKB Region 1 138 . . . Note=Globin +P39676 UniProtKB Region 146 399 . . . Note=Reductase +P39676 UniProtKB Region 272 399 . . . Note=NAD or NADP-binding +P39676 UniProtKB Active site 95 95 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39676 UniProtKB Active site 137 137 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39676 UniProtKB Metal binding 85 85 . . . Note=Iron (heme proximal ligand);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00238 +P39676 UniProtKB Binding site 189 189 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39676 UniProtKB Site 29 29 . . . Note=Involved in heme-bound ligand stabilization and O-O bond activation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39676 UniProtKB Site 84 84 . . . Note=Influences the redox potential of the prosthetic heme and FAD groups;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39676 UniProtKB Site 388 388 . . . Note=Influences the redox potential of the prosthetic heme and FAD groups;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39676 UniProtKB Modified residue 22 22 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39676 UniProtKB Natural variant 153 153 . . . Note=In strain: JM43. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1594608;Dbxref=PMID:1594608 +P39676 UniProtKB Natural variant 345 345 . . . Note=In strain: JM43. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1594608;Dbxref=PMID:1594608 +P39676 UniProtKB Natural variant 365 365 . . . Note=In strain: JM43. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1594608;Dbxref=PMID:1594608 +##sequence-region P07149 1 2051 +P07149 UniProtKB Chain 1 2051 . . . ID=PRO_0000180282;Note=Fatty acid synthase subunit beta +P07149 UniProtKB Domain 1523 1648 . . . Note=MaoC-like +P07149 UniProtKB Region 1 468 . . . Note=Acetyltransferase +P07149 UniProtKB Region 480 868 . . . Note=Enoyl reductase +P07149 UniProtKB Region 1144 1626 . . . Note=Dehydratase +P07149 UniProtKB Region 1627 1845 . . . Note=Malonyl/palmitoyl transferase +P07149 UniProtKB Active site 274 274 . . . Note=For acetyltransferase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07149 UniProtKB Active site 1808 1808 . . . Note=For malonyltransferase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07149 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P07149 UniProtKB Modified residue 733 733 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07149 UniProtKB Modified residue 1121 1121 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P07149 UniProtKB Cross-link 1364 1364 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P07149 UniProtKB Sequence conflict 191 191 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 191 191 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 212 212 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 403 403 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1039 1039 . . . Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1039 1039 . . . Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1149 1149 . . . Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1184 1184 . . . Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1184 1184 . . . Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1290 1292 . . . Note=FEI->SET;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1331 1333 . . . Note=WRA->LRG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1331 1333 . . . Note=WRA->LRG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1407 1411 . . . Note=TSSFF->IFLFL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1559 1559 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1559 1559 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1576 1576 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1587 1587 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1631 1631 . . . Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1647 1647 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1661 1661 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1661 1661 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1876 1876 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Sequence conflict 1980 1980 . . . Note=Y->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07149 UniProtKB Beta strand 10 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 16 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Turn 24 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 27 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Turn 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 50 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 57 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 81 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 101 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 116 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 144 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 156 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 169 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 181 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 202 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 205 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 215 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 228 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 234 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 260 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 267 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 274 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 277 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 289 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 321 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 337 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 346 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 362 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 367 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 373 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 377 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 383 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 404 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 409 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 417 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Turn 430 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 433 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 445 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Turn 452 454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Turn 462 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 466 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 475 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 490 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 499 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 505 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 508 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 512 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 526 529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 540 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Turn 544 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 552 554 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 561 564 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 568 571 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 577 580 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 582 587 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 591 594 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 598 601 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 604 612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 616 620 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 621 623 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 627 640 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 647 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 658 671 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 675 684 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 688 697 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 703 705 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 710 722 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 728 732 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 738 740 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 748 757 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 766 770 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 774 777 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 778 780 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Turn 781 783 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 785 787 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Turn 788 790 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 803 805 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 815 822 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 829 836 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 841 847 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 853 857 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 860 870 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Turn 871 874 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Turn 877 879 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 880 885 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 888 898 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 914 916 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 919 930 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Turn 933 936 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 937 939 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 941 958 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 970 974 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 976 986 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 988 991 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 997 1006 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1010 1012 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1016 1018 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1025 1030 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1035 1038 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1040 1042 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1048 1050 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Turn 1057 1062 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1070 1090 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1094 1096 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1125 1128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1135 1143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1149 1155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1158 1161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1164 1167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1169 1174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1181 1186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1190 1192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1194 1201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1204 1214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Turn 1215 1217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1218 1225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1229 1232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1234 1241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1258 1270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1294 1304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1323 1325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1326 1335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1336 1338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1341 1343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1347 1349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1350 1359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1367 1369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1375 1383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1385 1398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1401 1414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1419 1421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1423 1434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1438 1446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1450 1454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1463 1474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1476 1478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1480 1492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1498 1510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1515 1522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1524 1527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1529 1545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1551 1557 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1562 1564 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1567 1572 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1576 1578 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1582 1597 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1602 1604 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1605 1612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1621 1632 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1635 1643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1649 1658 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1662 1666 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Turn 1674 1677 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1678 1683 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1685 1702 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1706 1711 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1715 1720 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1724 1734 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1749 1754 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1761 1765 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1770 1772 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1774 1794 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1803 1806 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1810 1819 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1824 1840 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1850 1857 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1859 1862 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1868 1882 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1886 1893 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Turn 1894 1896 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1897 1903 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1904 1919 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1924 1930 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1933 1952 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 1964 1968 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1979 1981 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1988 1993 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 1998 2000 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 2003 2006 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Turn 2007 2009 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Beta strand 2013 2015 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 2023 2033 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Helix 2036 2043 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +P07149 UniProtKB Turn 2044 2048 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2UV8 +##sequence-region P40039 1 528 +P40039 UniProtKB Chain 1 528 . . . ID=PRO_0000197921;Note=Purine-cytosine permease FCY21 +P40039 UniProtKB Topological domain 1 90 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Transmembrane 91 111 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Topological domain 112 118 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Transmembrane 119 139 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Topological domain 140 161 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Transmembrane 162 182 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Topological domain 183 198 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Transmembrane 199 219 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Topological domain 220 221 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Transmembrane 222 242 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Topological domain 243 260 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Transmembrane 261 281 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Topological domain 282 295 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Transmembrane 296 316 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Topological domain 317 340 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Transmembrane 341 361 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Topological domain 362 393 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Transmembrane 394 414 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Topological domain 415 416 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Transmembrane 417 437 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Topological domain 438 460 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Transmembrane 461 481 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Topological domain 482 493 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Transmembrane 494 514 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Topological domain 515 528 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40039 UniProtKB Modified residue 43 43 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40039 UniProtKB Modified residue 46 46 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q08991 1 375 +Q08991 UniProtKB Chain 1 375 . . . ID=PRO_0000255979;Note=Fluoride export protein 2 +Q08991 UniProtKB Topological domain 1 11 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08913 +Q08991 UniProtKB Transmembrane 12 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08991 UniProtKB Topological domain 33 34 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08913 +Q08991 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08991 UniProtKB Topological domain 56 79 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:Q08913,ECO:0000305 +Q08991 UniProtKB Transmembrane 80 100 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08991 UniProtKB Topological domain 101 127 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08913 +Q08991 UniProtKB Transmembrane 128 148 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08991 UniProtKB Topological domain 149 213 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08913 +Q08991 UniProtKB Transmembrane 214 234 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08991 UniProtKB Topological domain 235 241 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08913 +Q08991 UniProtKB Transmembrane 242 262 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08991 UniProtKB Topological domain 263 268 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08913 +Q08991 UniProtKB Transmembrane 269 289 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08991 UniProtKB Topological domain 290 310 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08913 +Q08991 UniProtKB Transmembrane 311 331 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08991 UniProtKB Topological domain 332 338 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08913 +Q08991 UniProtKB Transmembrane 339 359 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08991 UniProtKB Topological domain 360 375 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08913 +Q08991 UniProtKB Glycosylation 109 109 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +Q08991 UniProtKB Glycosylation 117 117 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +Q08991 UniProtKB Glycosylation 235 235 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +##sequence-region P25653 1 1609 +P25653 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25653 UniProtKB Chain 23 1588 . . . ID=PRO_0000021264;Note=Factor-induced gene 2 protein +P25653 UniProtKB Propeptide 1589 1609 . . . ID=PRO_0000372452;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25653 UniProtKB Compositional bias 30 1366 . . . Note=Ser-rich +P25653 UniProtKB Compositional bias 529 1554 . . . Note=Thr-rich +P25653 UniProtKB Lipidation 1588 1588 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25653 UniProtKB Glycosylation 29 29 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25653 UniProtKB Glycosylation 231 231 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25653 UniProtKB Glycosylation 298 298 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25653 UniProtKB Glycosylation 347 347 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25653 UniProtKB Glycosylation 386 386 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25653 UniProtKB Glycosylation 426 426 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25653 UniProtKB Glycosylation 495 495 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25653 UniProtKB Glycosylation 535 535 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25653 UniProtKB Glycosylation 661 661 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25653 UniProtKB Glycosylation 674 674 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25653 UniProtKB Glycosylation 713 713 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25653 UniProtKB Glycosylation 889 889 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25653 UniProtKB Glycosylation 907 907 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25653 UniProtKB Glycosylation 1079 1079 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25653 UniProtKB Glycosylation 1400 1400 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P42837 1 879 +P42837 UniProtKB Chain 1 879 . . . ID=PRO_0000209742;Note=Polyphosphoinositide phosphatase +P42837 UniProtKB Domain 166 528 . . . Note=SAC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00183 +P42837 UniProtKB Region 761 879 . . . Note=Required for vacuolar localization +P42837 UniProtKB Modified residue 829 829 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P42837 UniProtKB Mutagenesis 59 59 . . . Note=Defective activation of FAB1. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17572665;Dbxref=PMID:17572665 +P42837 UniProtKB Mutagenesis 469 469 . . . Note=Partially defective in both hyperosmotic shock-induced PtdIns(3%2C5)P2 elevation and turnover. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492811;Dbxref=PMID:16492811 +P42837 UniProtKB Mutagenesis 519 519 . . . Note=In FIG4-1%3B loss of catalytic activity in vitro. Almost 3-fold increase in PtdIns(3%2C5)P2 level in vivo. Partially defective in both hyperosmotic shock-induced PtdIns(3%2C5)P2 elevation and turnover. G->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11950935,ECO:0000269|PubMed:14528018,ECO:0000269|PubMed:16492811;Dbxref=PMID:11950935,PMID:14528018,PMID:16492811 +##sequence-region P38911 1 411 +P38911 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38911 UniProtKB Chain 2 411 . . . ID=PRO_0000075313;Note=FK506-binding nuclear protein +P38911 UniProtKB Domain 324 411 . . . Note=PPIase FKBP-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00277 +P38911 UniProtKB Motif 256 271 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38911 UniProtKB Compositional bias 60 87 . . . Note=Asp/Glu-rich (highly acidic) +P38911 UniProtKB Compositional bias 88 99 . . . Note=Lys-rich (highly basic) +P38911 UniProtKB Compositional bias 101 119 . . . Note=Asp/Glu-rich (highly acidic) +P38911 UniProtKB Compositional bias 173 248 . . . Note=Asp/Glu-rich (highly acidic) +P38911 UniProtKB Compositional bias 250 298 . . . Note=Lys-rich (highly basic) +P38911 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38911 UniProtKB Modified residue 80 80 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38911 UniProtKB Modified residue 81 81 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38911 UniProtKB Modified residue 89 89 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38911 UniProtKB Modified residue 184 184 . . . Note=Phosphotyrosine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9148902;Dbxref=PMID:9148902 +P38911 UniProtKB Modified residue 186 186 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9148902;Dbxref=PMID:9148902 +P38911 UniProtKB Sequence conflict 122 122 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38911 UniProtKB Sequence conflict 240 240 . . . Note=E->EEE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38911 UniProtKB Sequence conflict 335 335 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P20081 1 114 +P20081 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P20081 UniProtKB Chain 2 114 . . . ID=PRO_0000075305;Note=FK506-binding protein 1 +P20081 UniProtKB Domain 26 114 . . . Note=PPIase FKBP-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00277 +P20081 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P20081 UniProtKB Modified residue 51 51 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P20081 UniProtKB Mutagenesis 43 43 . . . Note=Reduces interaction with FAP1. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10998178;Dbxref=PMID:10998178 +P20081 UniProtKB Mutagenesis 44 44 . . . Note=Abrogates interaction with FAP1. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10998178;Dbxref=PMID:10998178 +P20081 UniProtKB Mutagenesis 48 48 . . . Note=Abrogates interaction with FAP1. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10998178;Dbxref=PMID:10998178 +P20081 UniProtKB Mutagenesis 49 49 . . . Note=Abrogates interaction with FAP1. R->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10998178;Dbxref=PMID:10998178 +P20081 UniProtKB Mutagenesis 94 94 . . . Note=Abrogates interaction with FAP1. F->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10998178;Dbxref=PMID:10998178 +P20081 UniProtKB Mutagenesis 106 106 . . . Note=Reduces interaction with FAP1. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10998178;Dbxref=PMID:10998178 +P20081 UniProtKB Helix 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT +P20081 UniProtKB Beta strand 10 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT +P20081 UniProtKB Beta strand 28 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT +P20081 UniProtKB Beta strand 42 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT +P20081 UniProtKB Turn 47 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT +P20081 UniProtKB Beta strand 53 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT +P20081 UniProtKB Beta strand 59 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT +P20081 UniProtKB Helix 64 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT +P20081 UniProtKB Helix 70 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT +P20081 UniProtKB Beta strand 78 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT +P20081 UniProtKB Helix 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT +P20081 UniProtKB Turn 88 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT +P20081 UniProtKB Turn 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT +P20081 UniProtKB Beta strand 104 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YAT +##sequence-region P38631 1 1876 +P38631 UniProtKB Chain 1 1876 . . . ID=PRO_0000121725;Note=1%2C3-beta-glucan synthase component FKS1 +P38631 UniProtKB Topological domain 1 454 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Transmembrane 455 475 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Topological domain 476 492 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Transmembrane 493 513 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Topological domain 514 531 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Transmembrane 532 552 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Topological domain 553 563 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Transmembrane 564 584 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Topological domain 585 621 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Transmembrane 622 642 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Topological domain 643 678 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Transmembrane 679 699 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Topological domain 700 1358 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Transmembrane 1359 1379 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Topological domain 1380 1444 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Transmembrane 1445 1465 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Topological domain 1466 1469 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Transmembrane 1470 1490 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Topological domain 1491 1560 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Transmembrane 1561 1581 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Topological domain 1582 1601 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Transmembrane 1602 1622 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Topological domain 1623 1643 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Transmembrane 1644 1664 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Topological domain 1665 1672 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Transmembrane 1673 1695 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Topological domain 1696 1802 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Transmembrane 1803 1823 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Topological domain 1824 1876 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38631 UniProtKB Modified residue 269 269 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38631 UniProtKB Modified residue 272 272 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38631 UniProtKB Cross-link 259 259 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38631 UniProtKB Cross-link 275 275 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38631 UniProtKB Cross-link 386 386 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38631 UniProtKB Cross-link 910 910 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38631 UniProtKB Cross-link 915 915 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38631 UniProtKB Cross-link 1539 1539 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38631 UniProtKB Cross-link 1547 1547 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38631 UniProtKB Mutagenesis 146 146 . . . Note=In 1132%3B temperature-sensitive mutant%3B no gross alteration in beta-glucan content of cells%3B when associated with N-329%3B N-335 and DEL-GSC2. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 302 302 . . . Note=In 1082%3B temperature-sensitive mutant%3B no gross alteration in beta-glucan content of cells%3B when associated with DEL-GSC2. V->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 329 329 . . . Note=In 1132%3B temperature-sensitive mutant%3B no gross alteration in beta-glucan content of cells%3B when associated with V-146%3B N-335 and DEL-GSC2. Y->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 335 335 . . . Note=In 1132%3B temperature-sensitive mutant%3B no gross alteration in beta-glucan content of cells%3B when associated with V-146%3B N-329 and DEL-GSC2. Y->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 470 470 . . . Note=In ACR79-5%3B selectively resistant to antibiotic arborcandin C. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14693557;Dbxref=PMID:14693557 +P38631 UniProtKB Mutagenesis 605 605 . . . Note=In 1093%3B temperature-sensitive mutant%3B higher beta-glucan content of cells%3B when associated with T-761 and DEL-GSC2. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 642 642 . . . Note=In ACR1A3%3B selectively resistant to antibiotic arborcandin C. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14693557;Dbxref=PMID:14693557 +P38631 UniProtKB Mutagenesis 713 713 . . . Note=In 1163%3B temperature-sensitive mutant%3B no gross alteration in beta-glucan content of cells%3B when associated with V-722 and DEL-GSC2. I->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 722 722 . . . Note=In 1163%3B temperature-sensitive mutant%3B no gross alteration in beta-glucan content of cells%3B when associated with L-713 and DEL-GSC2. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 761 761 . . . Note=In 1093%3B temperature-sensitive mutant%3B higher beta-glucan content of cells%3B when associated with I-605 and DEL-GSC2. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 823 823 . . . Note=In 1104%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with E-920 and DEL-GSC2. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 828 828 . . . Note=In 1014%3B temperature-sensitive mutant%3B no gross alteration in beta-glucan content of cells%3B partially K1 killer toxin-sensitive%3B when associated with DEL-GSC2. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 853 853 . . . Note=In 1114%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with G-932%3B D-934%3B Y-1020%3B N-1047 and DEL-GSC2. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 855 855 . . . Note=In A6%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with DEL-GSC2. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 872 872 . . . Note=In 1144%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with K-907%3B S-982 and DEL-GSC2. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 877 877 . . . Note=In 1154%3B temperature-sensitive mutant which is able to grow at 25 degrees Celsius but fails to grow at temperatures above 35 degrees Celsius%3B defective in 1%2C3-beta-glucan synthesis and thus has lower beta-glucan content%3B hypersensitive to echinocandin B and to a chitin-binding reagent%2C Calcofluor white%3B fails to grow in a low glucose medium%3B when associated with S-899%3B P-977 and DEL-GSC2. K->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12185837,ECO:0000269|PubMed:12399379;Dbxref=PMID:12185837,PMID:12399379 +P38631 UniProtKB Mutagenesis 899 899 . . . Note=In 1154%3B temperature-sensitive mutant which is able to grow at 25 degrees Celsius but fails to grow at temperatures above 35 degrees Celsius%3B defective in 1%2C3-beta-glucan synthesis and thus has lower beta-glucan content%3B hypersensitive to echinocandin B and to a chitin-binding reagent%2C Calcofluor white%3B fails to grow in a low glucose medium%3B when associated with N-877%3B P-977 and DEL-GSC2. A->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12185837,ECO:0000269|PubMed:12399379;Dbxref=PMID:12185837,PMID:12399379 +P38631 UniProtKB Mutagenesis 907 907 . . . Note=In 1144%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with F-872%3B S-982 and DEL-GSC2. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 920 920 . . . Note=In 1104%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with V-823 and DEL-GSC2. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 932 932 . . . Note=In 1114%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with T-853%3B D-934%3B Y-1020%3B N-1047 and DEL-GSC2. A->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 934 934 . . . Note=In 1114%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with T-853%3B G-932%3B Y-1020%3B N-1047 and DEL-GSC2. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 977 977 . . . Note=In 1154%3B temperature-sensitive mutant which is able to grow at 25 degrees Celsius but fails to grow at temperatures above 35 degrees Celsius%3B defective in 1%2C3-beta-glucan synthesis and thus has lower beta-glucan content%3B hypersensitive to echinocandin B and to a chitin-binding reagent%2C Calcofluor white%3B fails to grow in a low glucose medium%3B when associated with N-877%3B S-899 and DEL-GSC2. Q->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12185837,ECO:0000269|PubMed:12399379;Dbxref=PMID:12185837,PMID:12399379 +P38631 UniProtKB Mutagenesis 982 982 . . . Note=In 1144%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with F-872%3B K-907 and DEL-GSC2. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 1020 1020 . . . Note=In 1114%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with T-853%3B G-932%3B D-934%3B N-1047 and DEL-GSC2. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 1047 1047 . . . Note=In 1114%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with T-853%3B G-932%3B D-934%3B Y-1020 and DEL-GSC2. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 1111 1111 . . . Note=In F4%3B temperature-sensitive mutant%3B lower beta-glucan content of cells%3B when associated with DEL-GSC2. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 1258 1258 . . . Note=In 1125%3B temperature-sensitive mutant%3B lower beta-glucan content of cells and partially K1 killer toxin-resistant%3B when associated with D-1520 and DEL-GSC2. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Mutagenesis 1520 1520 . . . Note=In 1125%3B temperature-sensitive mutant%3B lower beta-glucan content of cells and partial K1 killer toxin-resistant phenotype%3B when associated with Y-1258 and DEL-GSC2. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12185837;Dbxref=PMID:12185837 +P38631 UniProtKB Sequence conflict 19 19 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 19 19 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 19 19 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 19 19 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 19 19 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 113 113 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 113 113 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 113 113 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 113 113 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 113 113 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 236 236 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 236 236 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 236 236 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 236 236 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 236 236 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 373 373 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 373 373 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 373 373 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 373 373 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 373 373 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 437 437 . . . Note=K->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 470 470 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 492 492 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 492 492 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 492 492 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 492 492 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 492 492 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 642 642 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1341 1341 . . . Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1341 1341 . . . Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1341 1341 . . . Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1341 1341 . . . Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1341 1341 . . . Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1457 1457 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1457 1457 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1457 1457 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1457 1457 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1457 1457 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1790 1790 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1790 1790 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1790 1790 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1790 1790 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1790 1790 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1827 1828 . . . Note=KH->DQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1827 1828 . . . Note=KH->DQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1827 1828 . . . Note=KH->DQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1827 1828 . . . Note=KH->DQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1827 1828 . . . Note=KH->DQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1834 1834 . . . Note=D->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1834 1834 . . . Note=D->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1834 1834 . . . Note=D->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1834 1834 . . . Note=D->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1834 1834 . . . Note=D->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1844 1844 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1844 1844 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1844 1844 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1844 1844 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1844 1844 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1853 1853 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1853 1853 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1853 1853 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1853 1853 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38631 UniProtKB Sequence conflict 1853 1853 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40068 1 799 +P40068 UniProtKB Chain 1 799 . . . ID=PRO_0000087303;Note=Transcriptional activator FLO8 +P40068 UniProtKB Domain 73 105 . . . Note=LisH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00126 +P40068 UniProtKB Compositional bias 41 55 . . . Note=Poly-Gln +P40068 UniProtKB Natural variant 54 54 . . . Note=In strain: Diastaticus / ATCC 60715 / YIY2-11A. Q->QQQ +P40068 UniProtKB Natural variant 112 112 . . . Note=In strain: Diastaticus / ATCC 60715 / YIY2-11A. V->I +P40068 UniProtKB Natural variant 115 115 . . . Note=In strain: Diastaticus / ATCC 60715 / YIY2-11A. P->S +P40068 UniProtKB Natural variant 383 383 . . . Note=In strain: Diastaticus / ATCC 60715 / YIY2-11A. C->G +P40068 UniProtKB Natural variant 441 441 . . . Note=In strain: Diastaticus / ATCC 60715 / YIY2-11A. A->T +P40068 UniProtKB Natural variant 447 447 . . . Note=In strain: Diastaticus / ATCC 60715 / YIY2-11A. A->V +P40068 UniProtKB Natural variant 598 598 . . . Note=In strain: Diastaticus / ATCC 60715 / YIY2-11A. R->P +##sequence-region P53279 1 174 +P53279 UniProtKB Chain 1 174 . . . ID=PRO_0000202823;Note=Non-classical export protein 2 homolog 1 +P53279 UniProtKB Topological domain 1 7 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53279 UniProtKB Transmembrane 8 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53279 UniProtKB Topological domain 29 41 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53279 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53279 UniProtKB Topological domain 63 69 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53279 UniProtKB Transmembrane 70 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53279 UniProtKB Topological domain 91 122 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53279 UniProtKB Transmembrane 123 143 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53279 UniProtKB Topological domain 144 174 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08645 1 548 +Q08645 UniProtKB Chain 1 548 . . . ID=PRO_0000168312;Note=Folylpolyglutamate synthase +Q08645 UniProtKB Nucleotide binding 130 133 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192 +Q08645 UniProtKB Metal binding 157 157 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192 +Q08645 UniProtKB Metal binding 234 234 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192 +Q08645 UniProtKB Metal binding 262 262 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192 +Q08645 UniProtKB Binding site 382 382 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192 +Q08645 UniProtKB Binding site 396 396 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192 +##sequence-region P08524 1 352 +P08524 UniProtKB Chain 1 352 . . . ID=PRO_0000123952;Note=Farnesyl pyrophosphate synthase +P08524 UniProtKB Metal binding 100 100 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08524 UniProtKB Metal binding 100 100 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08524 UniProtKB Metal binding 104 104 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08524 UniProtKB Metal binding 104 104 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08524 UniProtKB Metal binding 240 240 . . . Note=Magnesium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08524 UniProtKB Binding site 52 52 . . . Note=Isopentenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08524 UniProtKB Binding site 55 55 . . . Note=Isopentenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08524 UniProtKB Binding site 93 93 . . . Note=Isopentenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08524 UniProtKB Binding site 109 109 . . . Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08524 UniProtKB Binding site 110 110 . . . Note=Isopentenyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08524 UniProtKB Binding site 197 197 . . . Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08524 UniProtKB Binding site 198 198 . . . Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08524 UniProtKB Binding site 237 237 . . . Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08524 UniProtKB Binding site 254 254 . . . Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08524 UniProtKB Binding site 263 263 . . . Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08524 UniProtKB Mutagenesis 197 197 . . . Note=In ERG20-2%3B 14-fold decrease in FPPS activity. K->E +##sequence-region Q07825 1 749 +Q07825 UniProtKB Chain 1 749 . . . ID=PRO_0000185086;Note=Putative Xaa-Pro aminopeptidase FRA1 +Q07825 UniProtKB Metal binding 551 551 . . . Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07825 UniProtKB Metal binding 562 562 . . . Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07825 UniProtKB Metal binding 562 562 . . . Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07825 UniProtKB Metal binding 660 660 . . . Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07825 UniProtKB Metal binding 674 674 . . . Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07825 UniProtKB Metal binding 674 674 . . . Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07825 UniProtKB Modified residue 69 69 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07825 UniProtKB Modified residue 92 92 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07825 UniProtKB Modified residue 95 95 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P32791 1 686 +P32791 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Chain 23 686 . . . ID=PRO_0000010137;Note=Ferric/cupric reductase transmembrane component 1 +P32791 UniProtKB Topological domain 23 148 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Transmembrane 149 169 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Topological domain 170 215 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Transmembrane 216 236 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Topological domain 237 259 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Transmembrane 260 280 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Topological domain 281 296 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Transmembrane 297 317 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Topological domain 318 328 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Transmembrane 329 349 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Topological domain 350 358 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Transmembrane 359 378 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Topological domain 379 383 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Transmembrane 384 401 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Topological domain 402 686 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Domain 258 398 . . . Note=Ferric oxidoreductase;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Domain 399 522 . . . Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716 +P32791 UniProtKB Nucleotide binding 462 468 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Nucleotide binding 514 517 . . . Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Nucleotide binding 652 653 . . . Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Metal binding 294 294 . . . Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8940093;Dbxref=PMID:8940093 +P32791 UniProtKB Metal binding 308 308 . . . Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8940093;Dbxref=PMID:8940093 +P32791 UniProtKB Metal binding 364 364 . . . Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8940093;Dbxref=PMID:8940093 +P32791 UniProtKB Metal binding 378 378 . . . Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8940093;Dbxref=PMID:8940093 +P32791 UniProtKB Glycosylation 69 69 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Glycosylation 100 100 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Glycosylation 124 124 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32791 UniProtKB Mutagenesis 294 294 . . . Note=Impairs heme binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8940093;Dbxref=PMID:8940093 +P32791 UniProtKB Mutagenesis 308 308 . . . Note=Impairs heme binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8940093;Dbxref=PMID:8940093 +P32791 UniProtKB Mutagenesis 364 364 . . . Note=Impairs heme binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8940093;Dbxref=PMID:8940093 +P32791 UniProtKB Mutagenesis 378 378 . . . Note=Impairs heme binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8940093;Dbxref=PMID:8940093 +##sequence-region P53746 1 719 +P53746 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53746 UniProtKB Chain 19 719 . . . ID=PRO_0000010140;Note=Ferric reductase transmembrane component 4 +P53746 UniProtKB Topological domain 19 156 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53746 UniProtKB Transmembrane 157 177 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53746 UniProtKB Topological domain 178 228 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53746 UniProtKB Transmembrane 229 249 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53746 UniProtKB Topological domain 250 267 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53746 UniProtKB Transmembrane 268 288 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53746 UniProtKB Topological domain 289 304 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53746 UniProtKB Transmembrane 305 325 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53746 UniProtKB Topological domain 326 346 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53746 UniProtKB Transmembrane 347 367 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53746 UniProtKB Topological domain 368 373 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53746 UniProtKB Transmembrane 374 394 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53746 UniProtKB Topological domain 395 395 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53746 UniProtKB Transmembrane 396 416 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53746 UniProtKB Topological domain 417 719 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53746 UniProtKB Domain 273 407 . . . Note=Ferric oxidoreductase +P53746 UniProtKB Domain 408 527 . . . Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716 +P53746 UniProtKB Nucleotide binding 472 478 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53746 UniProtKB Nucleotide binding 519 522 . . . Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53746 UniProtKB Nucleotide binding 685 686 . . . Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53746 UniProtKB Metal binding 309 309 . . . Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53746 UniProtKB Metal binding 323 323 . . . Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53746 UniProtKB Metal binding 379 379 . . . Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53746 UniProtKB Metal binding 393 393 . . . Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53746 UniProtKB Glycosylation 51 51 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53746 UniProtKB Glycosylation 80 80 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53746 UniProtKB Glycosylation 101 101 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53746 UniProtKB Glycosylation 113 113 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53746 UniProtKB Glycosylation 127 127 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53746 UniProtKB Glycosylation 135 135 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P08417 1 488 +P08417 UniProtKB Region 164 166 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08417 UniProtKB Binding site 126 126 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08417 UniProtKB Modified residue 428 428 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P08417 UniProtKB Sequence conflict 173 173 . . . Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08417 UniProtKB Sequence conflict 289 289 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08417 UniProtKB Sequence conflict 392 392 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08417 UniProtKB Beta strand 28 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Beta strand 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Beta strand 38 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 48 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 61 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 68 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 93 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Beta strand 118 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 126 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 155 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Turn 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 165 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 185 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Turn 203 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Beta strand 207 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Beta strand 215 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 222 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Turn 255 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 267 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 289 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 297 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Beta strand 327 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 353 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 387 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 413 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 420 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 432 434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Turn 435 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 438 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 443 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 460 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 472 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +P08417 UniProtKB Helix 481 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YFM +##sequence-region P28003 1 413 +P28003 UniProtKB Chain 1 413 . . . ID=PRO_0000202417;Note=SWIRM domain-containing protein FUN19 +P28003 UniProtKB Domain 316 413 . . . Note=SWIRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00247 +P28003 UniProtKB Compositional bias 31 76 . . . Note=Asn-rich +P28003 UniProtKB Modified residue 194 194 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P28003 UniProtKB Modified residue 207 207 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P28003 UniProtKB Modified residue 211 211 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P28003 UniProtKB Sequence conflict 255 255 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28003 UniProtKB Sequence conflict 369 369 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P11412 1 505 +P11412 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2040308,ECO:0000269|PubMed:2387402;Dbxref=PMID:2040308,PMID:2387402 +P11412 UniProtKB Chain 2 505 . . . ID=PRO_0000068107;Note=Glucose-6-phosphate 1-dehydrogenase +P11412 UniProtKB Nucleotide binding 18 25 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11412 UniProtKB Region 187 191 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11412 UniProtKB Active site 249 249 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11412 UniProtKB Binding site 52 52 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11412 UniProtKB Binding site 157 157 . . . Note=NADP%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11412 UniProtKB Binding site 157 157 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11412 UniProtKB Binding site 225 225 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11412 UniProtKB Binding site 244 244 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11412 UniProtKB Binding site 343 343 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11412 UniProtKB Binding site 377 377 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11412 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2040308,ECO:0000269|PubMed:2387402;Dbxref=PMID:2040308,PMID:2387402 +P11412 UniProtKB Modified residue 142 142 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P11412 UniProtKB Modified residue 145 145 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P11412 UniProtKB Sequence conflict 59 59 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11412 UniProtKB Sequence conflict 80 80 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11412 UniProtKB Sequence conflict 175 175 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P04385 1 528 +P04385 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:200486;Dbxref=PMID:200486 +P04385 UniProtKB Chain 2 528 . . . ID=PRO_0000184657;Note=Galactokinase +P04385 UniProtKB Nucleotide binding 163 173 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04385 UniProtKB Active site 217 217 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04385 UniProtKB Site 53 53 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04385 UniProtKB Modified residue 381 381 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04385 UniProtKB Sequence conflict 6 6 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04385 UniProtKB Sequence conflict 162 162 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04385 UniProtKB Sequence conflict 206 239 . . . Note=EHYVGVNNGGMDQAASVCGEEDHALYVEFKPQLK->DIMLVLTMAVWIRLPLFAVRKIMLYTLSSNAVE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04385 UniProtKB Sequence conflict 297 297 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04385 UniProtKB Sequence conflict 428 428 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04385 UniProtKB Sequence conflict 483 483 . . . Note=N->NN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04385 UniProtKB Helix 23 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Beta strand 45 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Beta strand 68 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Beta strand 90 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Beta strand 103 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 123 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 143 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Beta strand 147 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Beta strand 153 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Beta strand 166 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 170 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 195 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 203 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 216 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Beta strand 229 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Beta strand 235 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Beta strand 239 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Beta strand 252 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Turn 266 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 274 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 310 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 332 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 351 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 359 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 370 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Beta strand 379 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 390 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 419 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 446 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Beta strand 461 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Beta strand 470 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 486 496 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 498 501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Helix 507 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Beta strand 514 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +P04385 UniProtKB Beta strand 523 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AJ4 +##sequence-region P04386 1 881 +P04386 UniProtKB Chain 1 881 . . . ID=PRO_0000114951;Note=Regulatory protein GAL4 +P04386 UniProtKB DNA binding 11 38 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P04386 UniProtKB Motif 862 870 . . . Note=9aaTAD +P04386 UniProtKB Metal binding 11 11 . . . Note=Zinc 1 +P04386 UniProtKB Metal binding 11 11 . . . Note=Zinc 2 +P04386 UniProtKB Metal binding 14 14 . . . Note=Zinc 1 +P04386 UniProtKB Metal binding 21 21 . . . Note=Zinc 1 +P04386 UniProtKB Metal binding 28 28 . . . Note=Zinc 1 +P04386 UniProtKB Metal binding 28 28 . . . Note=Zinc 2 +P04386 UniProtKB Metal binding 31 31 . . . Note=Zinc 2 +P04386 UniProtKB Metal binding 38 38 . . . Note=Zinc 2 +P04386 UniProtKB Modified residue 694 694 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04386 UniProtKB Modified residue 696 696 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04386 UniProtKB Modified residue 699 699 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04386 UniProtKB Modified residue 703 703 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04386 UniProtKB Modified residue 712 712 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P04386 UniProtKB Mutagenesis 26 26 . . . Note=Loss of DNA-binding. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3299106;Dbxref=PMID:3299106 +P04386 UniProtKB Helix 12 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3COQ +P04386 UniProtKB Beta strand 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3COQ +P04386 UniProtKB Helix 29 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3COQ +P04386 UniProtKB Helix 51 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3COQ +P04386 UniProtKB Beta strand 73 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3COQ +P04386 UniProtKB Helix 77 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3COQ +P04386 UniProtKB Helix 86 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3COQ +##sequence-region Q04739 1 417 +Q04739 UniProtKB Chain 1 417 . . . ID=PRO_0000204373;Note=SNF1 protein kinase subunit beta-3 +Q04739 UniProtKB Region 152 342 . . . Note=Kinase-interacting sequence (KIS)%3B required for interaction with SNF1 +Q04739 UniProtKB Region 343 417 . . . Note=Association with SNF1 kinase complex (ASC) domain%3B required for interaction with SNF4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9121458;Dbxref=PMID:9121458 +Q04739 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q04739 UniProtKB Modified residue 21 21 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04739 UniProtKB Modified residue 44 44 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04739 UniProtKB Modified residue 135 135 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04739 UniProtKB Modified residue 276 276 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q04739 UniProtKB Modified residue 279 279 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region P39719 1 783 +P39719 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Chain 23 783 . . . ID=PRO_0000202424;Note=Flavin carrier protein 2 +P39719 UniProtKB Topological domain 23 182 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Transmembrane 183 203 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Topological domain 204 211 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Transmembrane 212 232 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Topological domain 233 347 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Transmembrane 348 368 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Topological domain 369 402 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Transmembrane 403 423 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Topological domain 424 430 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Transmembrane 431 451 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Topological domain 452 492 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Transmembrane 493 513 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Topological domain 514 521 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Transmembrane 522 542 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Topological domain 543 547 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Transmembrane 548 568 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Topological domain 569 581 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Transmembrane 582 602 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Topological domain 603 783 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Glycosylation 28 28 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Glycosylation 65 65 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Glycosylation 81 81 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Glycosylation 156 156 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Glycosylation 323 323 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39719 UniProtKB Sequence conflict 111 111 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39719 UniProtKB Sequence conflict 312 312 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39719 UniProtKB Sequence conflict 641 643 . . . Note=NDS->IDP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32785 1 401 +P32785 UniProtKB Transit peptide 1 26 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32785 UniProtKB Chain 27 401 . . . ID=PRO_0000010096;Note=Methionyl-tRNA formyltransferase%2C mitochondrial +P32785 UniProtKB Region 159 162 . . . Note=Tetrahydrofolate (THF) binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q02207 1 900 +Q02207 UniProtKB Chain 1 900 . . . ID=PRO_0000054700;Note=Peroxisomal hydratase-dehydrogenase-epimerase +Q02207 UniProtKB Domain 775 887 . . . Note=MaoC-like +Q02207 UniProtKB Nucleotide binding 13 37 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02207 UniProtKB Nucleotide binding 75 76 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02207 UniProtKB Nucleotide binding 165 169 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02207 UniProtKB Nucleotide binding 197 200 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02207 UniProtKB Nucleotide binding 326 350 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02207 UniProtKB Region 6 230 . . . Note=Short-chain dehydrogenase like 1 +Q02207 UniProtKB Region 319 535 . . . Note=Short-chain dehydrogenase like 2 +Q02207 UniProtKB Region 689 690 . . . Note=(3R)-3-hydroxydecanoyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02207 UniProtKB Region 803 808 . . . Note=(3R)-3-hydroxydecanoyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02207 UniProtKB Motif 898 900 . . . Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02207 UniProtKB Active site 165 165 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001 +Q02207 UniProtKB Active site 469 469 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001 +Q02207 UniProtKB Binding site 21 21 . . . Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02207 UniProtKB Binding site 40 40 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02207 UniProtKB Binding site 100 100 . . . Note=NAD%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02207 UniProtKB Binding site 152 152 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02207 UniProtKB Binding site 456 456 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02207 UniProtKB Binding site 719 719 . . . Note=(3R)-3-hydroxydecanoyl-CoA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02207 UniProtKB Binding site 826 826 . . . Note=(3R)-3-hydroxydecanoyl-CoA%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02207 UniProtKB Binding site 851 851 . . . Note=(3R)-3-hydroxydecanoyl-CoA%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P36033 1 711 +P36033 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Chain 24 711 . . . ID=PRO_0000010138;Note=Ferric/cupric reductase transmembrane component 2 +P36033 UniProtKB Topological domain 24 164 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Transmembrane 165 185 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Topological domain 186 235 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Transmembrane 236 256 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Topological domain 257 280 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Transmembrane 281 301 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Topological domain 302 317 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Transmembrane 318 340 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Topological domain 341 353 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Transmembrane 354 374 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Topological domain 375 377 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Transmembrane 378 398 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Topological domain 399 400 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Transmembrane 401 423 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Topological domain 424 711 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Domain 280 414 . . . Note=Ferric oxidoreductase +P36033 UniProtKB Domain 415 534 . . . Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716 +P36033 UniProtKB Nucleotide binding 479 485 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Nucleotide binding 526 529 . . . Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Nucleotide binding 677 678 . . . Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Metal binding 316 316 . . . Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36033 UniProtKB Metal binding 330 330 . . . Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36033 UniProtKB Metal binding 386 386 . . . Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36033 UniProtKB Metal binding 400 400 . . . Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36033 UniProtKB Glycosylation 85 85 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Glycosylation 108 108 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Glycosylation 120 120 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Glycosylation 134 134 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36033 UniProtKB Glycosylation 341 341 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12473 1 712 +Q12473 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Chain 18 712 . . . ID=PRO_0000010142;Note=Ferric reductase transmembrane component 6 +Q12473 UniProtKB Topological domain 18 167 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Transmembrane 168 188 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Topological domain 189 244 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Transmembrane 245 265 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Topological domain 266 287 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Transmembrane 288 308 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Topological domain 309 328 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Transmembrane 329 349 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Topological domain 350 360 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Transmembrane 361 381 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Topological domain 382 387 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Transmembrane 388 408 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Topological domain 409 416 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Transmembrane 417 437 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Topological domain 438 712 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Domain 287 411 . . . Note=Ferric oxidoreductase +Q12473 UniProtKB Domain 412 546 . . . Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716 +Q12473 UniProtKB Nucleotide binding 493 499 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Nucleotide binding 538 541 . . . Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Nucleotide binding 678 679 . . . Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Compositional bias 553 556 . . . Note=Poly-Leu +Q12473 UniProtKB Metal binding 323 323 . . . Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12473 UniProtKB Metal binding 337 337 . . . Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12473 UniProtKB Metal binding 393 393 . . . Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12473 UniProtKB Metal binding 407 407 . . . Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12473 UniProtKB Glycosylation 89 89 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Glycosylation 112 112 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Glycosylation 124 124 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12473 UniProtKB Mutagenesis 493 496 . . . Note=Loss of function. HPFT->AAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17553781;Dbxref=PMID:17553781 +##sequence-region Q12333 1 620 +Q12333 UniProtKB Chain 1 620 . . . ID=PRO_0000210150;Note=Ferric/cupric reductase transmembrane component 7 +Q12333 UniProtKB Topological domain 1 45 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12333 UniProtKB Transmembrane 46 66 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12333 UniProtKB Topological domain 67 107 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12333 UniProtKB Transmembrane 108 128 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12333 UniProtKB Topological domain 129 167 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12333 UniProtKB Transmembrane 168 188 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12333 UniProtKB Topological domain 189 194 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12333 UniProtKB Transmembrane 195 215 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12333 UniProtKB Topological domain 216 237 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12333 UniProtKB Transmembrane 238 258 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12333 UniProtKB Topological domain 259 265 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12333 UniProtKB Transmembrane 266 286 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12333 UniProtKB Topological domain 287 292 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12333 UniProtKB Transmembrane 293 313 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12333 UniProtKB Topological domain 314 620 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12333 UniProtKB Domain 161 320 . . . Note=Ferric oxidoreductase +Q12333 UniProtKB Domain 321 419 . . . Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716 +Q12333 UniProtKB Nucleotide binding 369 375 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12333 UniProtKB Nucleotide binding 411 414 . . . Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12333 UniProtKB Nucleotide binding 578 579 . . . Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12333 UniProtKB Metal binding 197 197 . . . Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12333 UniProtKB Metal binding 211 211 . . . Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12333 UniProtKB Metal binding 271 271 . . . Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12333 UniProtKB Metal binding 285 285 . . . Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P12709 1 554 +P12709 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P12709 UniProtKB Chain 2 554 . . . ID=PRO_0000180578;Note=Glucose-6-phosphate isomerase +P12709 UniProtKB Active site 367 367 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12709 UniProtKB Active site 398 398 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12709 UniProtKB Active site 520 520 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12709 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P12709 UniProtKB Modified residue 53 53 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P12709 UniProtKB Modified residue 220 220 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P17649 1 471 +P17649 UniProtKB Chain 1 471 . . . ID=PRO_0000120382;Note=4-aminobutyrate aminotransferase +P17649 UniProtKB Region 135 136 . . . Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80147 +P17649 UniProtKB Binding site 192 192 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80147 +P17649 UniProtKB Binding site 351 351 . . . Note=Pyridoxal phosphate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80147 +P17649 UniProtKB Modified residue 326 326 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80147 +P17649 UniProtKB Sequence conflict 240 240 . . . Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17649 UniProtKB Sequence conflict 240 240 . . . Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38225 1 669 +P38225 UniProtKB Chain 1 669 . . . ID=PRO_0000193181;Note=Very long-chain fatty acid transport protein +P38225 UniProtKB Transmembrane 6 26 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38225 UniProtKB Transmembrane 54 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38225 UniProtKB Transmembrane 149 169 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38225 UniProtKB Transmembrane 293 313 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38225 UniProtKB Glycosylation 184 184 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38225 UniProtKB Glycosylation 289 289 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38225 UniProtKB Glycosylation 534 534 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38225 UniProtKB Glycosylation 591 591 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38993 1 636 +P38993 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38993 UniProtKB Chain 22 636 . . . ID=PRO_0000002959;Note=Iron transport multicopper oxidase FET3 +P38993 UniProtKB Topological domain 22 559 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38993 UniProtKB Transmembrane 560 584 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38993 UniProtKB Topological domain 585 636 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38993 UniProtKB Domain 73 144 . . . Note=Plastocyanin-like 1 +P38993 UniProtKB Domain 190 300 . . . Note=Plastocyanin-like 2 +P38993 UniProtKB Domain 382 500 . . . Note=Plastocyanin-like 3 +P38993 UniProtKB Metal binding 81 81 . . . Note=Copper 1%3B type 2 +P38993 UniProtKB Metal binding 83 83 . . . Note=Copper 2%3B type 3 +P38993 UniProtKB Metal binding 126 126 . . . Note=Copper 2%3B type 3 +P38993 UniProtKB Metal binding 128 128 . . . Note=Copper 3%3B type 3 +P38993 UniProtKB Metal binding 413 413 . . . Note=Copper 4%3B type 1 +P38993 UniProtKB Metal binding 416 416 . . . Note=Copper 1%3B type 2 +P38993 UniProtKB Metal binding 418 418 . . . Note=Copper 3%3B type 3 +P38993 UniProtKB Metal binding 483 483 . . . Note=Copper 3%3B type 3 +P38993 UniProtKB Metal binding 484 484 . . . Note=Copper 4%3B type 1 +P38993 UniProtKB Metal binding 485 485 . . . Note=Copper 2%3B type 3 +P38993 UniProtKB Metal binding 489 489 . . . Note=Copper 4%3B type 1 +P38993 UniProtKB Glycosylation 27 27 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618 +P38993 UniProtKB Glycosylation 74 74 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38993 UniProtKB Glycosylation 77 77 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618 +P38993 UniProtKB Glycosylation 88 88 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618 +P38993 UniProtKB Glycosylation 113 113 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618 +P38993 UniProtKB Glycosylation 194 194 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618 +P38993 UniProtKB Glycosylation 198 198 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618 +P38993 UniProtKB Glycosylation 244 244 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618 +P38993 UniProtKB Glycosylation 265 265 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38993 UniProtKB Glycosylation 292 292 . . . Note=N-linked (GlcNAc...) asparagine +P38993 UniProtKB Glycosylation 300 300 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618 +P38993 UniProtKB Glycosylation 359 359 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618 +P38993 UniProtKB Glycosylation 381 381 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16230618;Dbxref=PMID:16230618 +P38993 UniProtKB Beta strand 23 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 37 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 43 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 57 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 64 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Helix 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Turn 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 109 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 121 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 129 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Helix 132 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 138 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 153 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Helix 168 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 189 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 196 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 200 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 208 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 222 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 231 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 239 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 249 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 256 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 271 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Helix 279 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 282 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 292 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Helix 320 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 325 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 336 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 353 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Helix 369 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Helix 377 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Helix 383 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 388 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 392 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 400 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 409 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 413 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 422 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Helix 433 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 455 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 467 473 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 478 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Helix 487 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 495 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Helix 502 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Helix 509 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Helix 515 523 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 529 533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +P38993 UniProtKB Beta strand 535 537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZPU +##sequence-region Q08913 1 375 +Q08913 UniProtKB Chain 1 375 . . . ID=PRO_0000241699;Note=Fluoride export protein 1 +Q08913 UniProtKB Topological domain 1 11 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26055717;Dbxref=PMID:26055717 +Q08913 UniProtKB Transmembrane 12 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08913 UniProtKB Topological domain 33 34 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26055717;Dbxref=PMID:26055717 +Q08913 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08913 UniProtKB Topological domain 56 79 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26055717;Dbxref=PMID:26055717 +Q08913 UniProtKB Transmembrane 80 100 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08913 UniProtKB Topological domain 101 127 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26055717;Dbxref=PMID:26055717 +Q08913 UniProtKB Transmembrane 128 148 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08913 UniProtKB Topological domain 149 213 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26055717;Dbxref=PMID:26055717 +Q08913 UniProtKB Transmembrane 214 234 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08913 UniProtKB Topological domain 235 241 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26055717;Dbxref=PMID:26055717 +Q08913 UniProtKB Transmembrane 242 262 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08913 UniProtKB Topological domain 263 268 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26055717;Dbxref=PMID:26055717 +Q08913 UniProtKB Transmembrane 269 289 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08913 UniProtKB Topological domain 290 310 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26055717;Dbxref=PMID:26055717 +Q08913 UniProtKB Transmembrane 311 331 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08913 UniProtKB Topological domain 332 338 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26055717;Dbxref=PMID:26055717 +Q08913 UniProtKB Transmembrane 339 359 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08913 UniProtKB Topological domain 360 375 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26055717;Dbxref=PMID:26055717 +Q08913 UniProtKB Glycosylation 109 109 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +Q08913 UniProtKB Glycosylation 117 117 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +Q08913 UniProtKB Glycosylation 235 235 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +##sequence-region P39521 1 936 +P39521 UniProtKB Chain 1 936 . . . ID=PRO_0000091901;Note=Pre-rRNA-processing protein FHL1 +P39521 UniProtKB Domain 300 357 . . . Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 +P39521 UniProtKB DNA binding 460 552 . . . Note=Fork-head;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00089 +P39521 UniProtKB Compositional bias 816 862 . . . Note=Ser-rich +P39521 UniProtKB Modified residue 44 44 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950;Dbxref=PMID:15665377,PMID:17330950 +P39521 UniProtKB Modified residue 228 228 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39521 UniProtKB Modified residue 230 230 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39521 UniProtKB Modified residue 247 247 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39521 UniProtKB Modified residue 264 264 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P32472 1 135 +P32472 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32472 UniProtKB Chain 18 135 . . . ID=PRO_0000025512;Note=Peptidyl-prolyl cis-trans isomerase FPR2 +P32472 UniProtKB Domain 43 132 . . . Note=PPIase FKBP-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00277 +##sequence-region P53121 1 802 +P53121 UniProtKB Signal peptide 1 28 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Chain 29 802 . . . ID=PRO_0000202738;Note=Putative flavin carrier protein 3 +P53121 UniProtKB Topological domain 29 169 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Transmembrane 170 190 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Topological domain 191 200 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Transmembrane 201 221 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Topological domain 222 229 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Transmembrane 230 250 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Topological domain 251 255 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Transmembrane 256 278 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Topological domain 279 323 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Transmembrane 324 344 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Topological domain 345 377 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Transmembrane 378 398 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Topological domain 399 405 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Transmembrane 406 426 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Topological domain 427 467 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Transmembrane 468 488 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Topological domain 489 495 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Transmembrane 496 516 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Topological domain 517 525 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Transmembrane 526 546 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Topological domain 547 557 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Transmembrane 558 578 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Topological domain 579 802 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Modified residue 616 616 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53121 UniProtKB Modified residue 635 635 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53121 UniProtKB Modified residue 779 779 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53121 UniProtKB Modified residue 782 782 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53121 UniProtKB Glycosylation 149 149 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Glycosylation 321 321 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53121 UniProtKB Glycosylation 547 547 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40491 1 155 +##sequence-region Q12497 1 93 +Q12497 UniProtKB Transit peptide 1 25 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12497 UniProtKB Chain 26 93 . . . ID=PRO_0000244462;Note=Protein FMP16%2C mitochondrial +##sequence-region P40008 1 231 +P40008 UniProtKB Transit peptide 1 44 . . . Note=Mitochondrion +P40008 UniProtKB Chain 45 231 . . . ID=PRO_0000202620;Note=Protein FMP52%2C mitochondrial +##sequence-region P22007 1 431 +P22007 UniProtKB Chain 1 431 . . . ID=PRO_0000119768;Note=Protein farnesyltransferase subunit beta +P22007 UniProtKB Repeat 130 171 . . . Note=PFTB 1 +P22007 UniProtKB Repeat 182 224 . . . Note=PFTB 2 +P22007 UniProtKB Repeat 231 273 . . . Note=PFTB 3 +P22007 UniProtKB Repeat 280 322 . . . Note=PFTB 4 +P22007 UniProtKB Repeat 332 375 . . . Note=PFTB 5 +P22007 UniProtKB Region 258 261 . . . Note=Farnesyl diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22007 UniProtKB Region 301 304 . . . Note=Farnesyl diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22007 UniProtKB Region 310 313 . . . Note=Farnesyl diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22007 UniProtKB Metal binding 307 307 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22007 UniProtKB Metal binding 309 309 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22007 UniProtKB Metal binding 363 363 . . . Note=Zinc%3B via tele nitrogen%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22007 UniProtKB Site 108 108 . . . Note=Important for selectivity against geranylgeranyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22007 UniProtKB Sequence conflict 47 47 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region O13329 1 566 +O13329 UniProtKB Chain 1 566 . . . ID=PRO_0000087323;Note=DNA replication fork-blocking protein FOB1 +O13329 UniProtKB Zinc finger 159 196 . . . Note=C2H2-type;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:14645529;Dbxref=PMID:14645529 +O13329 UniProtKB Mutagenesis 159 159 . . . Note=Abolishes RFB-binding%2C replication fork blocking activity and reduces recombination rate. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14645529;Dbxref=PMID:14645529 +O13329 UniProtKB Mutagenesis 164 164 . . . Note=Abolishes RFB-binding%2C replication fork blocking activity and reduces recombination rate. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14645529;Dbxref=PMID:14645529 +O13329 UniProtKB Mutagenesis 193 193 . . . Note=Abolishes RFB-binding%2C replication fork blocking activity and reduces recombination rate. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14645529;Dbxref=PMID:14645529 +O13329 UniProtKB Mutagenesis 196 196 . . . Note=Abolishes RFB-binding%2C replication fork blocking activity and reduces recombination rate. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14645529;Dbxref=PMID:14645529 +O13329 UniProtKB Mutagenesis 291 291 . . . Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14645529;Dbxref=PMID:14645529 +O13329 UniProtKB Sequence conflict 103 103 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08911 1 376 +Q08911 UniProtKB Chain 1 376 . . . ID=PRO_0000223647;Note=Formate dehydrogenase 1 +Q08911 UniProtKB Nucleotide binding 176 177 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 +Q08911 UniProtKB Nucleotide binding 244 248 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 +Q08911 UniProtKB Nucleotide binding 325 328 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 +Q08911 UniProtKB Region 5 121 . . . Note=Catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 +Q08911 UniProtKB Region 122 326 . . . Note=Coenzyme-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 +Q08911 UniProtKB Region 327 372 . . . Note=Catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 +Q08911 UniProtKB Binding site 97 97 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 +Q08911 UniProtKB Binding site 121 121 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 +Q08911 UniProtKB Binding site 197 197 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 +Q08911 UniProtKB Binding site 270 270 . . . Note=NAD%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 +Q08911 UniProtKB Binding site 296 296 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 +Q08911 UniProtKB Site 272 272 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 +Q08911 UniProtKB Site 325 325 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 +Q08911 UniProtKB Mutagenesis 197 198 . . . Note=Shifts the coenzyme preference of the enzyme from NAD(+) to NADP(+). DY->AR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12144528;Dbxref=PMID:12144528 +##sequence-region P40466 1 484 +P40466 UniProtKB Chain 1 484 . . . ID=PRO_0000091903;Note=Fork head protein homolog 1 +P40466 UniProtKB Domain 76 142 . . . Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 +P40466 UniProtKB DNA binding 302 393 . . . Note=Fork-head;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00089 +##sequence-region Q08967 1 793 +Q08967 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Chain 22 793 . . . ID=PRO_0000252267;Note=Flavin carrier protein 1 +Q08967 UniProtKB Topological domain 22 163 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Transmembrane 164 184 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Topological domain 185 194 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Transmembrane 195 215 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Topological domain 216 223 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Transmembrane 224 244 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Topological domain 245 249 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Transmembrane 250 272 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Topological domain 273 317 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Transmembrane 318 338 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Topological domain 339 372 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Transmembrane 373 393 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Topological domain 394 397 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Transmembrane 398 418 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Topological domain 419 461 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Transmembrane 462 482 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Topological domain 483 484 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Transmembrane 485 505 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Topological domain 506 516 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Transmembrane 517 537 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Topological domain 538 551 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Transmembrane 552 572 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Topological domain 573 793 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Modified residue 610 610 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53121 +Q08967 UniProtKB Modified residue 626 626 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08967 UniProtKB Modified residue 771 771 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198 +Q08967 UniProtKB Modified residue 774 774 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08967 UniProtKB Glycosylation 143 143 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08967 UniProtKB Glycosylation 281 281 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53739 1 893 +P53739 UniProtKB Chain 1 893 . . . ID=PRO_0000086154;Note=Flippase kinase 1 +P53739 UniProtKB Domain 496 777 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53739 UniProtKB Domain 778 861 . . . Note=AGC-kinase C-terminal +P53739 UniProtKB Nucleotide binding 502 510 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53739 UniProtKB Active site 621 621 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P53739 UniProtKB Binding site 525 525 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53739 UniProtKB Modified residue 140 140 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53739 UniProtKB Modified residue 144 144 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53739 UniProtKB Modified residue 171 171 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53739 UniProtKB Modified residue 175 175 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53739 UniProtKB Modified residue 185 185 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53739 UniProtKB Modified residue 300 300 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53739 UniProtKB Modified residue 414 414 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53739 UniProtKB Modified residue 462 462 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P23900 1 669 +P23900 UniProtKB Chain 1 669 . . . ID=PRO_0000064098;Note=Glycerol uptake/efflux facilitator protein +P23900 UniProtKB Topological domain 1 254 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23900 UniProtKB Transmembrane 255 275 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23900 UniProtKB Topological domain 276 325 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23900 UniProtKB Transmembrane 326 346 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23900 UniProtKB Topological domain 347 369 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23900 UniProtKB Transmembrane 370 390 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23900 UniProtKB Topological domain 391 446 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23900 UniProtKB Transmembrane 447 467 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23900 UniProtKB Topological domain 468 506 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23900 UniProtKB Transmembrane 507 527 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23900 UniProtKB Topological domain 528 669 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23900 UniProtKB Motif 352 354 . . . Note=NPA 1 +P23900 UniProtKB Motif 480 482 . . . Note=NPA 2 +P23900 UniProtKB Compositional bias 50 69 . . . Note=Asn-rich +P23900 UniProtKB Modified residue 150 150 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P23900 UniProtKB Modified residue 168 168 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P23900 UniProtKB Modified residue 209 209 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P23900 UniProtKB Modified residue 212 212 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P23900 UniProtKB Sequence conflict 640 640 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q05015 1 223 +Q05015 UniProtKB Chain 1 223 . . . ID=PRO_0000212581;Note=Family of serine hydrolases 2 +Q05015 UniProtKB Active site 110 110 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05015 UniProtKB Active site 174 174 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05015 UniProtKB Active site 203 203 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q99369 1 266 +Q99369 UniProtKB Chain 1 266 . . . ID=PRO_0000212582;Note=Family of serine hydrolases 3 +Q99369 UniProtKB Active site 117 117 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99369 UniProtKB Active site 180 180 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99369 UniProtKB Active site 209 209 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38310 1 465 +P38310 UniProtKB Chain 1 465 . . . ID=PRO_0000159650;Note=Iron transporter FTH1 +P38310 UniProtKB Topological domain 1 11 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38310 UniProtKB Transmembrane 12 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38310 UniProtKB Topological domain 33 135 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38310 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38310 UniProtKB Topological domain 157 170 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38310 UniProtKB Transmembrane 171 191 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38310 UniProtKB Topological domain 192 289 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38310 UniProtKB Transmembrane 290 310 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38310 UniProtKB Topological domain 311 358 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38310 UniProtKB Transmembrane 359 379 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38310 UniProtKB Topological domain 380 465 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38310 UniProtKB Modified residue 449 449 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +P38310 UniProtKB Modified residue 453 453 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38310 UniProtKB Sequence conflict 18 18 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38310 UniProtKB Sequence conflict 18 18 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38310 UniProtKB Sequence conflict 36 36 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38310 UniProtKB Sequence conflict 36 36 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38310 UniProtKB Sequence conflict 228 228 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38310 UniProtKB Sequence conflict 228 228 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38310 UniProtKB Sequence conflict 249 250 . . . Note=VF->YS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38310 UniProtKB Sequence conflict 249 250 . . . Note=VF->YS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38310 UniProtKB Sequence conflict 334 334 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38310 UniProtKB Sequence conflict 334 334 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38310 UniProtKB Sequence conflict 389 390 . . . Note=IC->KY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38310 UniProtKB Sequence conflict 389 390 . . . Note=IC->KY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38310 UniProtKB Sequence conflict 399 401 . . . Note=EKY->GKC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38310 UniProtKB Sequence conflict 399 401 . . . Note=EKY->GKC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12247 1 151 +Q12247 UniProtKB Chain 1 151 . . . ID=PRO_0000087404;Note=rRNA-processing protein FYV7 +Q12247 UniProtKB Coiled coil 70 113 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32805 1 299 +P32805 UniProtKB Chain 1 299 . . . ID=PRO_0000046805;Note=Zinc finger protein FZF1 +P32805 UniProtKB Zinc finger 12 36 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P32805 UniProtKB Zinc finger 42 66 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P32805 UniProtKB Zinc finger 72 94 . . . Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P32805 UniProtKB Zinc finger 155 179 . . . Note=C2H2-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P32805 UniProtKB Zinc finger 246 271 . . . Note=C2H2-type 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P32805 UniProtKB Motif 96 107 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32805 UniProtKB Natural variant 110 110 . . . Note=In strain: Sgu52E and Sgu52F. G->E +P32805 UniProtKB Natural variant 120 120 . . . Note=In strain: MMW1-15h2%2C MMW1-2h2%2C Sgu52E and Sgu52F. N->D +P32805 UniProtKB Natural variant 228 228 . . . Note=In strain: MMW1-15h2%2C MMW1-2h2%2C Sgu52E and Sgu52F. V->I +P32805 UniProtKB Natural variant 238 238 . . . Note=In strain: MMW1-15h2 and MMW1-2h2. D->N +P32805 UniProtKB Sequence conflict 180 180 . . . Note=H->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32805 UniProtKB Sequence conflict 235 235 . . . Note=T->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32805 UniProtKB Sequence conflict 246 246 . . . Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P00358 1 332 +P00358 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6 +P00358 UniProtKB Chain 2 332 . . . ID=PRO_0000145590;Note=Glyceraldehyde-3-phosphate dehydrogenase 2 +P00358 UniProtKB Nucleotide binding 11 12 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00358 UniProtKB Region 149 151 . . . Note=Glyceraldehyde 3-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00358 UniProtKB Region 209 210 . . . Note=Glyceraldehyde 3-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00358 UniProtKB Active site 150 150 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10009 +P00358 UniProtKB Binding site 33 33 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00358 UniProtKB Binding site 78 78 . . . Note=NAD%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00358 UniProtKB Binding site 180 180 . . . Note=Glyceraldehyde 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00358 UniProtKB Binding site 232 232 . . . Note=Glyceraldehyde 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00358 UniProtKB Binding site 314 314 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00358 UniProtKB Site 177 177 . . . Note=Activates thiol group during catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00358 UniProtKB Modified residue 302 302 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00359 +P00358 UniProtKB Cross-link 46 46 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00359 +P00358 UniProtKB Cross-link 63 63 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00358 UniProtKB Sequence conflict 77 77 . . . Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P00359 1 332 +P00359 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11946592;Dbxref=PMID:11946592 +P00359 UniProtKB Chain 2 332 . . . ID=PRO_0000145591;Note=Glyceraldehyde-3-phosphate dehydrogenase 3 +P00359 UniProtKB Nucleotide binding 11 12 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00359 UniProtKB Region 149 151 . . . Note=Glyceraldehyde 3-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00359 UniProtKB Region 209 210 . . . Note=Glyceraldehyde 3-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00359 UniProtKB Active site 150 150 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10009 +P00359 UniProtKB Binding site 33 33 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00359 UniProtKB Binding site 78 78 . . . Note=NAD%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00359 UniProtKB Binding site 180 180 . . . Note=Glyceraldehyde 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00359 UniProtKB Binding site 232 232 . . . Note=Glyceraldehyde 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00359 UniProtKB Binding site 314 314 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00359 UniProtKB Site 177 177 . . . Note=Activates thiol group during catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00359 UniProtKB Modified residue 302 302 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P00359 UniProtKB Cross-link 46 46 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00359 UniProtKB Cross-link 63 63 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00359 UniProtKB Sequence conflict 136 136 . . . Note=E->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00359 UniProtKB Sequence conflict 136 136 . . . Note=E->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00359 UniProtKB Sequence conflict 248 248 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00359 UniProtKB Sequence conflict 248 248 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00359 UniProtKB Sequence conflict 287 287 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00359 UniProtKB Sequence conflict 329 329 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00359 UniProtKB Sequence conflict 329 329 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00359 UniProtKB Beta strand 3 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Helix 11 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Beta strand 27 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Helix 38 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Turn 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Beta strand 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Beta strand 62 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Beta strand 70 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Helix 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Turn 85 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Beta strand 91 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Beta strand 97 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Helix 103 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Beta strand 115 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Beta strand 124 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Turn 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Helix 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Beta strand 144 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Helix 150 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Beta strand 168 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Beta strand 183 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Helix 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Helix 200 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Beta strand 205 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Helix 211 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Helix 220 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Beta strand 225 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Beta strand 239 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Helix 253 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Turn 266 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Beta strand 272 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Helix 281 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Beta strand 290 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Helix 295 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Beta strand 299 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Beta strand 305 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +P00359 UniProtKB Helix 316 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PYM +##sequence-region P40569 1 121 +P40569 UniProtKB Chain 1 121 . . . ID=PRO_0000083487;Note=Protein GAT4 +P40569 UniProtKB Zinc finger 53 79 . . . Note=GATA-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00094 +##sequence-region P38260 1 290 +P38260 UniProtKB Chain 1 290 . . . ID=PRO_0000202485;Note=Hsp70 nucleotide exchange factor FES1 +P38260 UniProtKB Repeat 13 57 . . . Note=ARM 1 +P38260 UniProtKB Repeat 76 116 . . . Note=ARM 2 +P38260 UniProtKB Repeat 120 161 . . . Note=ARM 3 +P38260 UniProtKB Repeat 164 205 . . . Note=ARM 4 +P38260 UniProtKB Repeat 211 251 . . . Note=ARM 5 +P38260 UniProtKB Repeat 253 290 . . . Note=ARM 6 +P38260 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P43561 1 622 +P43561 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43561 UniProtKB Chain 19 622 . . . ID=PRO_0000002960;Note=Iron transport multicopper oxidase FET5 +P43561 UniProtKB Topological domain 19 573 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43561 UniProtKB Transmembrane 574 594 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43561 UniProtKB Topological domain 595 622 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43561 UniProtKB Domain 43 146 . . . Note=Plastocyanin-like 1 +P43561 UniProtKB Domain 192 301 . . . Note=Plastocyanin-like 2 +P43561 UniProtKB Domain 392 514 . . . Note=Plastocyanin-like 3 +P43561 UniProtKB Metal binding 79 79 . . . Note=Copper 1%3B type 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43561 UniProtKB Metal binding 81 81 . . . Note=Copper 2%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43561 UniProtKB Metal binding 128 128 . . . Note=Copper 2%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43561 UniProtKB Metal binding 130 130 . . . Note=Copper 3%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43561 UniProtKB Metal binding 418 418 . . . Note=Copper 4%3B type 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43561 UniProtKB Metal binding 421 421 . . . Note=Copper 1%3B type 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43561 UniProtKB Metal binding 423 423 . . . Note=Copper 3%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43561 UniProtKB Metal binding 496 496 . . . Note=Copper 3%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43561 UniProtKB Metal binding 497 497 . . . Note=Copper 4%3B type 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43561 UniProtKB Metal binding 498 498 . . . Note=Copper 2%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43561 UniProtKB Metal binding 502 502 . . . Note=Copper 4%3B type 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43561 UniProtKB Glycosylation 24 24 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43561 UniProtKB Glycosylation 86 86 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43561 UniProtKB Glycosylation 115 115 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43561 UniProtKB Glycosylation 196 196 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43561 UniProtKB Glycosylation 200 200 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43561 UniProtKB Glycosylation 246 246 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43561 UniProtKB Glycosylation 295 295 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43561 UniProtKB Glycosylation 364 364 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43561 UniProtKB Glycosylation 455 455 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P41813 1 862 +P41813 UniProtKB Chain 1 862 . . . ID=PRO_0000091904;Note=Fork head protein homolog 2 +P41813 UniProtKB Domain 83 152 . . . Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 +P41813 UniProtKB DNA binding 339 430 . . . Note=Fork-head;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00089 +P41813 UniProtKB Modified residue 708 708 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P41813 UniProtKB Modified residue 832 832 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P41813 UniProtKB Modified residue 833 833 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P40989 1 1895 +P40989 UniProtKB Chain 1 1895 . . . ID=PRO_0000121726;Note=1%2C3-beta-glucan synthase component GSC2 +P40989 UniProtKB Topological domain 1 473 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40989 UniProtKB Transmembrane 474 494 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40989 UniProtKB Topological domain 495 511 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40989 UniProtKB Transmembrane 512 532 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40989 UniProtKB Topological domain 533 550 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40989 UniProtKB Transmembrane 551 571 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40989 UniProtKB Topological domain 572 582 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40989 UniProtKB Transmembrane 583 603 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40989 UniProtKB Topological domain 604 1579 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40989 UniProtKB Transmembrane 1580 1600 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40989 UniProtKB Topological domain 1601 1620 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40989 UniProtKB Transmembrane 1621 1641 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40989 UniProtKB Topological domain 1642 1758 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40989 UniProtKB Transmembrane 1759 1779 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40989 UniProtKB Topological domain 1780 1821 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40989 UniProtKB Transmembrane 1822 1842 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40989 UniProtKB Topological domain 1843 1895 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40989 UniProtKB Modified residue 288 288 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38631 +P40989 UniProtKB Modified residue 291 291 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38631 +P40989 UniProtKB Cross-link 278 278 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38631 +P40989 UniProtKB Cross-link 405 405 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38631 +P40989 UniProtKB Cross-link 929 929 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38631 +P40989 UniProtKB Cross-link 934 934 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38631 +P40989 UniProtKB Cross-link 1558 1558 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38631 +P40989 UniProtKB Cross-link 1566 1566 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38631 +P40989 UniProtKB Natural variant 1059 1059 . . . Note=In strain: SK1. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P40989 UniProtKB Natural variant 1853 1854 . . . Note=In strain: SK1. TG->KD +P40989 UniProtKB Sequence conflict 137 137 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40989 UniProtKB Sequence conflict 261 261 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40989 UniProtKB Sequence conflict 275 275 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12676 1 427 +Q12676 UniProtKB Chain 1 427 . . . ID=PRO_0000168308;Note=Dihydrofolate synthetase +Q12676 UniProtKB Nucleotide binding 34 37 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192 +Q12676 UniProtKB Metal binding 123 123 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192 +Q12676 UniProtKB Metal binding 153 153 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192 +Q12676 UniProtKB Binding site 275 275 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192 +Q12676 UniProtKB Binding site 296 296 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192 +##sequence-region Q08905 1 711 +Q08905 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Chain 21 711 . . . ID=PRO_0000010139;Note=Ferric reductase transmembrane component 3 +Q08905 UniProtKB Topological domain 21 166 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Transmembrane 167 187 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Topological domain 188 237 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Transmembrane 238 258 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Topological domain 259 280 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Transmembrane 281 301 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Topological domain 302 321 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Transmembrane 322 341 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Topological domain 342 353 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Transmembrane 354 374 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Topological domain 375 376 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Transmembrane 377 397 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Topological domain 398 398 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Transmembrane 399 419 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Topological domain 420 711 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Domain 280 414 . . . Note=Ferric oxidoreductase +Q08905 UniProtKB Domain 415 534 . . . Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716 +Q08905 UniProtKB Nucleotide binding 479 485 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Nucleotide binding 526 529 . . . Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Nucleotide binding 677 678 . . . Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Metal binding 316 316 . . . Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08905 UniProtKB Metal binding 330 330 . . . Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08905 UniProtKB Metal binding 386 386 . . . Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08905 UniProtKB Metal binding 400 400 . . . Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08905 UniProtKB Glycosylation 85 85 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Glycosylation 108 108 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Glycosylation 120 120 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08905 UniProtKB Glycosylation 134 134 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08908 1 694 +Q08908 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08908 UniProtKB Chain 20 694 . . . ID=PRO_0000010141;Note=Ferric reductase transmembrane component 5 +Q08908 UniProtKB Topological domain 20 163 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08908 UniProtKB Transmembrane 164 184 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08908 UniProtKB Topological domain 185 222 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08908 UniProtKB Transmembrane 223 243 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08908 UniProtKB Topological domain 244 267 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08908 UniProtKB Transmembrane 268 288 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08908 UniProtKB Topological domain 289 311 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08908 UniProtKB Transmembrane 312 334 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08908 UniProtKB Topological domain 335 347 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08908 UniProtKB Transmembrane 348 368 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08908 UniProtKB Topological domain 369 371 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08908 UniProtKB Transmembrane 372 392 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08908 UniProtKB Topological domain 393 403 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08908 UniProtKB Transmembrane 404 424 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08908 UniProtKB Topological domain 425 694 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08908 UniProtKB Domain 274 408 . . . Note=Ferric oxidoreductase +Q08908 UniProtKB Domain 409 528 . . . Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716 +Q08908 UniProtKB Nucleotide binding 473 479 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08908 UniProtKB Nucleotide binding 520 523 . . . Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08908 UniProtKB Nucleotide binding 660 661 . . . Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08908 UniProtKB Compositional bias 362 368 . . . Note=Poly-Phe +Q08908 UniProtKB Metal binding 310 310 . . . Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08908 UniProtKB Metal binding 324 324 . . . Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08908 UniProtKB Metal binding 380 380 . . . Note=Iron (heme 1 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08908 UniProtKB Metal binding 394 394 . . . Note=Iron (heme 2 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08908 UniProtKB Glycosylation 117 117 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12209 1 686 +Q12209 UniProtKB Chain 1 686 . . . ID=PRO_0000239647;Note=Probable ferric reductase transmembrane component 8 +Q12209 UniProtKB Topological domain 1 35 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Transmembrane 36 56 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Topological domain 57 89 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Transmembrane 90 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Topological domain 111 128 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Transmembrane 129 149 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Topological domain 150 157 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Transmembrane 158 178 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Topological domain 179 186 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Transmembrane 187 207 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Topological domain 208 216 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Transmembrane 217 237 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Topological domain 238 267 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Transmembrane 268 288 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Topological domain 289 402 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Transmembrane 403 423 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Topological domain 424 686 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Domain 119 666 . . . Note=Ferric oxidoreductase +Q12209 UniProtKB Nucleotide binding 320 326 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Nucleotide binding 442 450 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Glycosylation 371 371 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Glycosylation 383 383 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12209 UniProtKB Glycosylation 384 384 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03002 1 865 +Q03002 UniProtKB Chain 1 865 . . . ID=PRO_0000234367;Note=Fatty acyl-CoA synthetase and RNA processing-associated kinase 1 +Q03002 UniProtKB Domain 41 313 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03002 UniProtKB Nucleotide binding 47 55 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03002 UniProtKB Active site 175 175 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q03002 UniProtKB Binding site 80 80 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03002 UniProtKB Modified residue 441 441 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P37261 1 193 +P37261 UniProtKB Chain 1 193 . . . ID=PRO_0000087340;Note=Fatty acid repression mutant protein 2 +P37261 UniProtKB Helix 7 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP +P37261 UniProtKB Helix 31 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP +P37261 UniProtKB Helix 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP +P37261 UniProtKB Beta strand 55 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP +P37261 UniProtKB Helix 60 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP +P37261 UniProtKB Turn 81 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP +P37261 UniProtKB Beta strand 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP +P37261 UniProtKB Beta strand 91 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP +P37261 UniProtKB Helix 100 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP +P37261 UniProtKB Helix 117 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP +P37261 UniProtKB Beta strand 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP +P37261 UniProtKB Helix 149 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP +P37261 UniProtKB Beta strand 158 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP +P37261 UniProtKB Beta strand 164 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP +P37261 UniProtKB Beta strand 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4URP +##sequence-region P32599 1 642 +P32599 UniProtKB Chain 1 642 . . . ID=PRO_0000073757;Note=Fimbrin +P32599 UniProtKB Domain 16 50 . . . Note=EF-hand 1 +P32599 UniProtKB Domain 51 86 . . . Note=EF-hand 2 +P32599 UniProtKB Domain 139 259 . . . Note=Calponin-homology (CH) 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00044 +P32599 UniProtKB Domain 287 390 . . . Note=Calponin-homology (CH) 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00044 +P32599 UniProtKB Domain 411 521 . . . Note=Calponin-homology (CH) 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00044 +P32599 UniProtKB Domain 534 642 . . . Note=Calponin-homology (CH) 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00044 +P32599 UniProtKB Calcium binding 29 40 . . . Note=1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32599 UniProtKB Calcium binding 64 75 . . . Note=2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32599 UniProtKB Region 125 394 . . . Note=Actin-binding 1 +P32599 UniProtKB Region 395 642 . . . Note=Actin-binding 2 +##sequence-region Q03898 1 291 +Q03898 UniProtKB Chain 1 291 . . . ID=PRO_0000087257;Note=Filament protein FIN1 +Q03898 UniProtKB Coiled coil 254 284 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03898 UniProtKB Compositional bias 153 158 . . . Note=Poly-Gln +Q03898 UniProtKB Modified residue 54 54 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q03898 UniProtKB Modified residue 68 68 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q03898 UniProtKB Modified residue 74 74 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +Q03898 UniProtKB Modified residue 88 88 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region Q04433 1 528 +Q04433 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04433 UniProtKB Chain 19 506 . . . ID=PRO_0000021265;Note=Facilitator of iron transport 1 +Q04433 UniProtKB Propeptide 507 528 . . . ID=PRO_0000021266;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04433 UniProtKB Repeat 20 98 . . . Note=1-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q04433 UniProtKB Repeat 99 168 . . . Note=1-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q04433 UniProtKB Repeat 169 233 . . . Note=1-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q04433 UniProtKB Repeat 234 274 . . . Note=1-4%3B truncated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q04433 UniProtKB Repeat 289 294 . . . Note=2-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q04433 UniProtKB Repeat 295 300 . . . Note=2-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q04433 UniProtKB Repeat 301 306 . . . Note=2-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q04433 UniProtKB Repeat 307 312 . . . Note=2-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q04433 UniProtKB Repeat 313 318 . . . Note=2-5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q04433 UniProtKB Repeat 319 324 . . . Note=2-6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q04433 UniProtKB Repeat 325 330 . . . Note=2-7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q04433 UniProtKB Repeat 331 336 . . . Note=2-8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q04433 UniProtKB Repeat 337 342 . . . Note=2-9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q04433 UniProtKB Repeat 343 348 . . . Note=2-10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q04433 UniProtKB Repeat 349 353 . . . Note=2-11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q04433 UniProtKB Repeat 354 359 . . . Note=2-12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q04433 UniProtKB Nucleotide binding 488 495 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04433 UniProtKB Region 20 274 . . . Note=4 X approximate tandem repeats +Q04433 UniProtKB Region 289 359 . . . Note=12 X 6 AA approximate tandem repeats%2C Ser/Thr-rich +Q04433 UniProtKB Compositional bias 22 498 . . . Note=Thr-rich +Q04433 UniProtKB Compositional bias 275 478 . . . Note=Ser-rich +Q04433 UniProtKB Lipidation 506 506 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04433 UniProtKB Glycosylation 412 412 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04433 UniProtKB Glycosylation 464 464 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04433 UniProtKB Glycosylation 503 503 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39712 1 1322 +P39712 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39712 UniProtKB Chain 25 1299 . . . ID=PRO_0000021277;Note=Flocculation protein FLO9 +P39712 UniProtKB Propeptide 1300 1322 . . . ID=PRO_0000372454;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39712 UniProtKB Domain 74 249 . . . Note=PA14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01164 +P39712 UniProtKB Repeat 278 322 . . . Note=1-1 +P39712 UniProtKB Repeat 323 367 . . . Note=1-2 +P39712 UniProtKB Repeat 368 412 . . . Note=1-3 +P39712 UniProtKB Repeat 413 457 . . . Note=1-4 +P39712 UniProtKB Repeat 458 502 . . . Note=1-5 +P39712 UniProtKB Repeat 503 547 . . . Note=1-6 +P39712 UniProtKB Repeat 548 592 . . . Note=1-7 +P39712 UniProtKB Repeat 593 637 . . . Note=1-8 +P39712 UniProtKB Repeat 638 682 . . . Note=1-9 +P39712 UniProtKB Repeat 683 727 . . . Note=1-10 +P39712 UniProtKB Repeat 728 772 . . . Note=1-11 +P39712 UniProtKB Repeat 773 817 . . . Note=1-12 +P39712 UniProtKB Repeat 818 862 . . . Note=1-13 +P39712 UniProtKB Repeat 892 906 . . . Note=2-1 +P39712 UniProtKB Repeat 907 921 . . . Note=2-2 +P39712 UniProtKB Repeat 922 936 . . . Note=2-3 +P39712 UniProtKB Repeat 1013 1063 . . . Note=3-1 +P39712 UniProtKB Repeat 1085 1135 . . . Note=3-2 +P39712 UniProtKB Repeat 1136 1186 . . . Note=3-3 +P39712 UniProtKB Region 197 240 . . . Note=Sugar recognition;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39712 UniProtKB Region 278 862 . . . Note=13 X 45 AA approximate tandem repeats%2C Thr-rich +P39712 UniProtKB Region 892 936 . . . Note=3 X 15 AA approximate repeats%2C Ser-rich +P39712 UniProtKB Region 1013 1186 . . . Note=3 X 51 AA approximate repeats%2C Thr-rich +P39712 UniProtKB Lipidation 1299 1299 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39712 UniProtKB Glycosylation 135 135 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39712 UniProtKB Glycosylation 187 187 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39712 UniProtKB Glycosylation 203 203 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39712 UniProtKB Glycosylation 257 257 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39712 UniProtKB Glycosylation 262 262 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39712 UniProtKB Glycosylation 270 270 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39712 UniProtKB Glycosylation 329 329 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39712 UniProtKB Glycosylation 419 419 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39712 UniProtKB Glycosylation 464 464 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39712 UniProtKB Glycosylation 509 509 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39712 UniProtKB Glycosylation 554 554 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39712 UniProtKB Glycosylation 599 599 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39712 UniProtKB Glycosylation 644 644 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39712 UniProtKB Glycosylation 689 689 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39712 UniProtKB Glycosylation 734 734 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39712 UniProtKB Glycosylation 888 888 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P03870 1 423 +P03870 UniProtKB Chain 1 423 . . . ID=PRO_0000197567;Note=Site-specific recombinase Flp +P03870 UniProtKB Active site 343 343 . . . Note=O-(3'-phospho-DNA)-tyrosine intermediate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2211714;Dbxref=PMID:2211714 +P03870 UniProtKB Mutagenesis 305 305 . . . Note=Inactive and weakened DNA binding. H->L%2CP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2974924;Dbxref=PMID:2974924 +P03870 UniProtKB Mutagenesis 305 305 . . . Note=Reduced activity. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2974924;Dbxref=PMID:2974924 +P03870 UniProtKB Mutagenesis 308 308 . . . Note=Inactive and weakened DNA binding. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2974924;Dbxref=PMID:2974924 +P03870 UniProtKB Mutagenesis 343 343 . . . Note=No strand cleavage or recombination. Y->F%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3104911;Dbxref=PMID:3104911 +P03870 UniProtKB Sequence conflict 5 5 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03870 UniProtKB Sequence conflict 5 5 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03870 UniProtKB Helix 3 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 12 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 28 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 35 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Turn 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 54 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Beta strand 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Turn 72 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Beta strand 76 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 86 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Beta strand 101 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 116 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 138 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Beta strand 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M6X +P03870 UniProtKB Helix 154 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Turn 164 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 172 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 192 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Beta strand 199 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Turn 209 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Beta strand 214 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Beta strand 228 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Beta strand 236 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 241 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Beta strand 267 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P4E +P03870 UniProtKB Beta strand 272 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 279 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 294 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 306 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 324 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 337 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Turn 341 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P4E +P03870 UniProtKB Helix 352 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Beta strand 361 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Turn 366 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Beta strand 370 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 380 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 395 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Helix 401 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +P03870 UniProtKB Turn 404 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P4E +P03870 UniProtKB Helix 409 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FLO +##sequence-region P38124 1 548 +P38124 UniProtKB Chain 1 548 . . . ID=PRO_0000173435;Note=Fluconazole resistance protein 1 +P38124 UniProtKB Transmembrane 104 124 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38124 UniProtKB Transmembrane 139 159 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38124 UniProtKB Transmembrane 179 199 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38124 UniProtKB Transmembrane 203 223 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38124 UniProtKB Transmembrane 230 250 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38124 UniProtKB Transmembrane 261 281 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38124 UniProtKB Transmembrane 347 367 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38124 UniProtKB Transmembrane 376 396 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38124 UniProtKB Transmembrane 416 436 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38124 UniProtKB Transmembrane 440 460 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38124 UniProtKB Transmembrane 476 496 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38124 UniProtKB Transmembrane 511 531 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06179 1 2628 +##sequence-region P46998 1 180 +P46998 UniProtKB Chain 1 180 . . . ID=PRO_0000203028;Note=Mitochondrial membrane protein FMP33 +P46998 UniProtKB Transmembrane 34 54 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46998 UniProtKB Transmembrane 121 141 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46998 UniProtKB Transmembrane 145 165 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53889 1 259 +P53889 UniProtKB Chain 1 259 . . . ID=PRO_0000156843;Note=Uncharacterized mitochondrial hydrolase FMP41 +P53889 UniProtKB Metal binding 87 87 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53889 UniProtKB Metal binding 89 89 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53889 UniProtKB Metal binding 121 121 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53889 UniProtKB Helix 4 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Beta strand 12 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Helix 23 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Beta strand 36 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Helix 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Beta strand 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Beta strand 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Beta strand 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Beta strand 88 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Helix 106 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Helix 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Beta strand 113 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Helix 125 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Helix 139 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Beta strand 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Helix 156 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Turn 167 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Beta strand 170 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Beta strand 179 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Helix 186 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Beta strand 189 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Helix 193 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Beta strand 211 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Beta strand 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Beta strand 228 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +P53889 UniProtKB Beta strand 238 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NKQ +##sequence-region Q07651 1 309 +Q07651 UniProtKB Chain 1 309 . . . ID=PRO_0000202591;Note=SUR7 family protein FMP45 +Q07651 UniProtKB Topological domain 1 5 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07651 UniProtKB Transmembrane 6 26 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07651 UniProtKB Topological domain 27 116 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07651 UniProtKB Transmembrane 117 137 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07651 UniProtKB Topological domain 138 140 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07651 UniProtKB Transmembrane 141 161 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07651 UniProtKB Topological domain 162 188 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07651 UniProtKB Transmembrane 189 209 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07651 UniProtKB Topological domain 210 309 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07651 UniProtKB Modified residue 230 230 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07651 UniProtKB Modified residue 232 232 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07651 UniProtKB Modified residue 235 235 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07651 UniProtKB Glycosylation 73 73 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P31380 1 1131 +P31380 UniProtKB Chain 1 1131 . . . ID=PRO_0000074384;Note=ATP-dependent helicase FUN30 +P31380 UniProtKB Domain 584 752 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P31380 UniProtKB Domain 953 1108 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P31380 UniProtKB Nucleotide binding 597 604 . . . Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31380 UniProtKB Region 76 111 . . . Note=CUE-like region +P31380 UniProtKB Motif 703 706 . . . Note=DEGH box +P31380 UniProtKB Modified residue 232 232 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P31380 UniProtKB Modified residue 369 369 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P31380 UniProtKB Modified residue 451 451 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P31380 UniProtKB Mutagenesis 603 603 . . . Note=Abolishes both the silencing function and the ability to promote DNA end resection of double-strand breaks (DSBs). K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22960744;Dbxref=PMID:22960744 +P31380 UniProtKB Beta strand 813 820 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 824 846 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 853 858 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 859 861 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 864 874 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 878 880 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Beta strand 883 885 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 887 897 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 901 904 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 909 917 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 921 930 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 932 935 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 936 938 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 944 946 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 949 962 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Beta strand 969 974 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 976 988 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Beta strand 993 996 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Turn 1002 1004 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 1005 1014 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Beta strand 1020 1024 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 1025 1029 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Beta strand 1039 1044 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 1049 1056 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Turn 1057 1059 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Beta strand 1068 1075 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 1079 1086 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 1094 1096 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +P31380 UniProtKB Helix 1109 1122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GN1 +##sequence-region Q12035 1 217 +Q12035 UniProtKB Chain 1 217 . . . ID=PRO_0000253819;Note=rRNA-processing protein FCF2 +Q12035 UniProtKB Compositional bias 75 79 . . . Note=Poly-Lys +Q12035 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region Q06205 1 392 +Q06205 UniProtKB Chain 1 392 . . . ID=PRO_0000075314;Note=FK506-binding protein 4 +Q06205 UniProtKB Domain 306 392 . . . Note=PPIase FKBP-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00277 +Q06205 UniProtKB Compositional bias 191 199 . . . Note=Poly-Glu +Q06205 UniProtKB Modified residue 80 80 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06205 UniProtKB Modified residue 82 82 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06205 UniProtKB Beta strand 282 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8 +Q06205 UniProtKB Beta strand 291 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8 +Q06205 UniProtKB Beta strand 308 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8 +Q06205 UniProtKB Beta strand 322 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8 +Q06205 UniProtKB Beta strand 332 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8 +Q06205 UniProtKB Beta strand 339 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8 +Q06205 UniProtKB Helix 343 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8 +Q06205 UniProtKB Beta strand 357 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8 +Q06205 UniProtKB Helix 364 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8 +Q06205 UniProtKB Turn 367 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8 +Q06205 UniProtKB Beta strand 382 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BF8 +##sequence-region P38866 1 432 +P38866 UniProtKB Chain 1 432 . . . ID=PRO_0000147670;Note=Thiol-specific monooxygenase +##sequence-region Q08968 1 688 +Q08968 UniProtKB Chain 1 688 . . . ID=PRO_0000121401;Note=UPF0061 protein FMP40 +##sequence-region Q04991 1 504 +Q04991 UniProtKB Chain 1 504 . . . ID=PRO_0000218642;Note=Protein FMP42 +Q04991 UniProtKB Topological domain 1 11 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Transmembrane 12 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Topological domain 33 64 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Transmembrane 65 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Topological domain 86 91 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Transmembrane 92 112 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Topological domain 113 119 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Transmembrane 120 140 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Topological domain 141 150 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Transmembrane 151 171 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Topological domain 172 186 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Transmembrane 187 207 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Topological domain 208 302 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Transmembrane 303 323 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Topological domain 324 344 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Transmembrane 345 365 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Topological domain 366 385 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Transmembrane 386 406 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Topological domain 407 421 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Transmembrane 422 442 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Topological domain 443 462 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Transmembrane 463 483 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Topological domain 484 504 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04991 UniProtKB Modified residue 238 238 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q04991 UniProtKB Modified residue 249 249 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q04991 UniProtKB Modified residue 269 269 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P29703 1 316 +P29703 UniProtKB Chain 1 316 . . . ID=PRO_0000119754;Note=Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha +P29703 UniProtKB Repeat 47 81 . . . Note=PFTA 1 +P29703 UniProtKB Repeat 89 123 . . . Note=PFTA 2 +P29703 UniProtKB Repeat 125 159 . . . Note=PFTA 3 +P29703 UniProtKB Repeat 160 193 . . . Note=PFTA 4 +P29703 UniProtKB Repeat 199 233 . . . Note=PFTA 5 +##sequence-region P53848 1 824 +P53848 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53848 UniProtKB Chain 2 824 . . . ID=PRO_0000168243;Note=Folic acid synthesis protein FOL1 +P53848 UniProtKB Domain 504 814 . . . Note=Pterin-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00334 +P53848 UniProtKB Region 22 144 . . . Note=DHNA 1 +P53848 UniProtKB Region 147 284 . . . Note=DHNA 2 +P53848 UniProtKB Region 295 466 . . . Note=HPPK +P53848 UniProtKB Region 506 824 . . . Note=DHPS +P53848 UniProtKB Region 802 804 . . . Note=6-hydroxymethyl-7%2C8-dihydropterin diphosphate binding;Ontology_term=ECO:0000244,ECO:0000305;evidence=ECO:0000244|PDB:2BMB,ECO:0000305|PubMed:15826662;Dbxref=PMID:15826662 +P53848 UniProtKB Metal binding 511 511 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WND1 +P53848 UniProtKB Binding site 558 558 . . . Note=6-hydroxymethyl-7%2C8-dihydropterin diphosphate;Ontology_term=ECO:0000244,ECO:0000305;evidence=ECO:0000244|PDB:2BMB,ECO:0000305|PubMed:15826662;Dbxref=PMID:15826662 +P53848 UniProtKB Binding site 596 596 . . . Note=6-hydroxymethyl-7%2C8-dihydropterin diphosphate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15826662;Dbxref=PMID:15826662 +P53848 UniProtKB Binding site 615 615 . . . Note=6-hydroxymethyl-7%2C8-dihydropterin diphosphate;Ontology_term=ECO:0000244,ECO:0000305;evidence=ECO:0000244|PDB:2BMB,ECO:0000305|PubMed:15826662;Dbxref=PMID:15826662 +P53848 UniProtKB Binding site 715 715 . . . Note=6-hydroxymethyl-7%2C8-dihydropterin diphosphate;Ontology_term=ECO:0000244,ECO:0000305;evidence=ECO:0000244|PDB:2BMB,ECO:0000305|PubMed:15826662;Dbxref=PMID:15826662 +P53848 UniProtKB Binding site 767 767 . . . Note=6-hydroxymethyl-7%2C8-dihydropterin diphosphate;Ontology_term=ECO:0000244,ECO:0000305;evidence=ECO:0000244|PDB:2BMB,ECO:0000305|PubMed:15826662;Dbxref=PMID:15826662 +P53848 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53848 UniProtKB Modified residue 286 286 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53848 UniProtKB Beta strand 298 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 308 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 311 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 328 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 336 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 350 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 363 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 392 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 414 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 420 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 424 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Turn 431 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Turn 441 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 447 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 460 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 464 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 479 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 498 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 505 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Turn 517 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 527 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 548 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 566 582 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 584 586 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 588 590 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 591 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 600 608 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 613 616 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Turn 617 620 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 626 631 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 636 641 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Turn 647 649 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 650 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Turn 660 664 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 665 670 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 675 677 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 681 684 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 686 704 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 709 711 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 712 715 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 724 732 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 734 737 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 740 746 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 749 754 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 760 762 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 768 774 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 779 782 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 783 795 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Beta strand 799 804 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +P53848 UniProtKB Helix 806 821 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BMB +##sequence-region P38894 1 1075 +P38894 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38894 UniProtKB Chain 25 1052 . . . ID=PRO_0000021275;Note=Flocculation protein FLO5 +P38894 UniProtKB Propeptide 1053 1075 . . . ID=PRO_0000021276;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38894 UniProtKB Domain 74 249 . . . Note=PA14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01164 +P38894 UniProtKB Repeat 278 322 . . . Note=1-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P38894 UniProtKB Repeat 323 367 . . . Note=1-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P38894 UniProtKB Repeat 368 412 . . . Note=1-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P38894 UniProtKB Repeat 413 457 . . . Note=1-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P38894 UniProtKB Repeat 458 502 . . . Note=1-5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P38894 UniProtKB Repeat 503 547 . . . Note=1-6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P38894 UniProtKB Repeat 548 592 . . . Note=1-7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P38894 UniProtKB Repeat 593 637 . . . Note=1-8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P38894 UniProtKB Repeat 667 686 . . . Note=2-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P38894 UniProtKB Repeat 687 706 . . . Note=2-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P38894 UniProtKB Repeat 775 825 . . . Note=3-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P38894 UniProtKB Repeat 847 897 . . . Note=3-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P38894 UniProtKB Repeat 898 948 . . . Note=3-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P38894 UniProtKB Region 197 240 . . . Note=Sugar recognition;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38894 UniProtKB Region 278 637 . . . Note=8 X 45 AA approximate tandem repeats%2C Thr-rich +P38894 UniProtKB Region 667 706 . . . Note=2 X 20 AA approximate tandem repeats%2C Ser-rich +P38894 UniProtKB Region 775 948 . . . Note=3 X 51 AA approximate repeats%2C Ser/Thr-rich +P38894 UniProtKB Lipidation 1052 1052 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38894 UniProtKB Glycosylation 135 135 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38894 UniProtKB Glycosylation 187 187 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38894 UniProtKB Glycosylation 203 203 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38894 UniProtKB Glycosylation 262 262 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38894 UniProtKB Glycosylation 663 663 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38894 UniProtKB Glycosylation 749 749 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38894 UniProtKB Beta strand 36 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Helix 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Helix 57 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Helix 63 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Beta strand 69 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Beta strand 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Beta strand 86 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Beta strand 92 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Helix 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Turn 103 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Turn 108 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Turn 125 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Beta strand 135 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Beta strand 147 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Beta strand 160 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Turn 169 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Beta strand 189 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Beta strand 196 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4AHW +P38894 UniProtKB Beta strand 205 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Beta strand 215 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Beta strand 229 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Beta strand 233 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Beta strand 242 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Turn 248 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Beta strand 251 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Beta strand 264 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +P38894 UniProtKB Turn 268 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XJP +##sequence-region P40464 1 311 +P40464 UniProtKB Chain 1 311 . . . ID=PRO_0000090682;Note=Mitochondrial FAD carrier protein FLX1 +P40464 UniProtKB Transmembrane 13 33 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40464 UniProtKB Transmembrane 77 97 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40464 UniProtKB Transmembrane 129 149 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40464 UniProtKB Transmembrane 183 203 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40464 UniProtKB Transmembrane 230 250 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40464 UniProtKB Transmembrane 266 286 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40464 UniProtKB Repeat 7 101 . . . Note=Solcar 1 +P40464 UniProtKB Repeat 123 210 . . . Note=Solcar 2 +P40464 UniProtKB Repeat 224 310 . . . Note=Solcar 3 +##sequence-region P38231 1 175 +P38231 UniProtKB Transit peptide 1 38 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38231 UniProtKB Chain 39 175 . . . ID=PRO_0000202474;Note=Protein FMP23%2C mitochondrial +##sequence-region Q02883 1 468 +Q02883 UniProtKB Transit peptide 1 39 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02883 UniProtKB Chain 40 468 . . . ID=PRO_0000238633;Note=N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D%2C mitochondrial +Q02883 UniProtKB Transmembrane 54 76 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02883 UniProtKB Metal binding 265 265 . . . Note=Zinc 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02883 UniProtKB Metal binding 267 267 . . . Note=Zinc 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02883 UniProtKB Metal binding 269 269 . . . Note=Zinc 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02883 UniProtKB Metal binding 270 270 . . . Note=Zinc 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02883 UniProtKB Metal binding 332 332 . . . Note=Zinc 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02883 UniProtKB Metal binding 425 425 . . . Note=Zinc 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PZB3 1 126 +A0A023PZB3 UniProtKB Chain 1 126 . . . ID=PRO_0000430968;Note=Protein FMP49%2C mitochondrial +##sequence-region Q12029 1 327 +Q12029 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12029 UniProtKB Chain 2 327 . . . ID=PRO_0000237642;Note=Probable mitochondrial transport protein FSF1 +Q12029 UniProtKB Transmembrane 98 118 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12029 UniProtKB Transmembrane 143 163 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12029 UniProtKB Transmembrane 179 199 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12029 UniProtKB Transmembrane 272 292 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12029 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P25659 1 250 +P25659 UniProtKB Chain 1 250 . . . ID=PRO_0000202574;Note=Silencing boundary-establishment protein FUB1 +P25659 UniProtKB Compositional bias 228 248 . . . Note=Gly/Ser-rich +##sequence-region P16892 1 353 +P16892 UniProtKB Chain 1 353 . . . ID=PRO_0000186326;Note=Mitogen-activated protein kinase FUS3 +P16892 UniProtKB Domain 13 309 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P16892 UniProtKB Nucleotide binding 19 27 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P16892 UniProtKB Motif 180 182 . . . Note=TXY +P16892 UniProtKB Active site 137 137 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P16892 UniProtKB Binding site 42 42 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P16892 UniProtKB Modified residue 180 180 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1628831;Dbxref=PMID:1628831 +P16892 UniProtKB Modified residue 182 182 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1628831;Dbxref=PMID:1628831 +P16892 UniProtKB Cross-link 345 345 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P16892 UniProtKB Sequence conflict 334 334 . . . Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16892 UniProtKB Beta strand 4 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F49 +P16892 UniProtKB Beta strand 13 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Beta strand 23 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Turn 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Beta strand 38 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Helix 50 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Beta strand 74 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Turn 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9F +P16892 UniProtKB Beta strand 89 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Beta strand 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Helix 100 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Helix 111 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Helix 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Beta strand 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Beta strand 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Helix 156 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9F +P16892 UniProtKB Beta strand 182 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F49 +P16892 UniProtKB Helix 186 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Helix 191 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Helix 202 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Helix 228 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Turn 245 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Helix 254 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Helix 271 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Helix 280 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Helix 294 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Helix 300 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Helix 307 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Turn 310 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Helix 326 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +P16892 UniProtKB Helix 340 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B9H +##sequence-region P38783 1 130 +P38783 UniProtKB Transit peptide 1 27 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38783 UniProtKB Chain 28 130 . . . ID=PRO_0000202897;Note=Protein FYV4%2C mitochondrial +##sequence-region P53913 1 173 +P53913 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53913 UniProtKB Chain 2 173 . . . ID=PRO_0000203427;Note=Protein FYV6 +P53913 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P45976 1 327 +P45976 UniProtKB Chain 1 327 . . . ID=PRO_0000215042;Note=Pre-mRNA polyadenylation factor FIP1 +P45976 UniProtKB Compositional bias 61 80 . . . Note=Asp-rich (acidic) +P45976 UniProtKB Compositional bias 258 266 . . . Note=Poly-Asn +P45976 UniProtKB Compositional bias 284 318 . . . Note=Pro-rich +P45976 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P45976 UniProtKB Beta strand 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C66 +P45976 UniProtKB Beta strand 87 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C66 +P45976 UniProtKB Beta strand 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C66 +P45976 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C66 +P45976 UniProtKB Helix 99 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C66 +##sequence-region P40515 1 155 +P40515 UniProtKB Chain 1 155 . . . ID=PRO_0000202982;Note=Mitochondrial fission 1 protein +P40515 UniProtKB Topological domain 1 131 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40515 UniProtKB Transmembrane 132 149 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40515 UniProtKB Topological domain 150 155 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40515 UniProtKB Mutagenesis 80 80 . . . Note=In fis1-L80P%3B no interaction with MDV1%3B mitochondrial fission is blocked%3B DNM1 assembly at punctate structures normal as in wild-type. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12163467;Dbxref=PMID:12163467 +P40515 UniProtKB Helix 12 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O48 +P40515 UniProtKB Helix 19 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O48 +P40515 UniProtKB Helix 34 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O48 +P40515 UniProtKB Helix 39 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O48 +P40515 UniProtKB Beta strand 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y8M +P40515 UniProtKB Helix 55 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O48 +P40515 UniProtKB Helix 73 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O48 +P40515 UniProtKB Helix 76 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O48 +P40515 UniProtKB Helix 93 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O48 +P40515 UniProtKB Helix 111 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O48 +##sequence-region P40098 1 244 +P40098 UniProtKB Chain 1 244 . . . ID=PRO_0000202660;Note=Uncharacterized mitochondrial membrane protein FMP10 +P40098 UniProtKB Transmembrane 29 49 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40098 UniProtKB Transmembrane 139 159 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36141 1 133 +P36141 UniProtKB Transit peptide 1 21 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36141 UniProtKB Chain 22 133 . . . ID=PRO_0000203215;Note=Putative redox protein FMP46%2C mitochondrial +P36141 UniProtKB Active site 97 97 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36141 UniProtKB Beta strand 13 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI +P36141 UniProtKB Beta strand 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI +P36141 UniProtKB Helix 27 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI +P36141 UniProtKB Turn 32 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI +P36141 UniProtKB Beta strand 41 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI +P36141 UniProtKB Helix 53 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI +P36141 UniProtKB Beta strand 62 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI +P36141 UniProtKB Helix 66 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI +P36141 UniProtKB Beta strand 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI +P36141 UniProtKB Helix 77 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI +P36141 UniProtKB Turn 81 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI +P36141 UniProtKB Helix 86 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI +P36141 UniProtKB Helix 95 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI +P36141 UniProtKB Beta strand 109 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI +P36141 UniProtKB Beta strand 118 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI +P36141 UniProtKB Helix 123 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WPI +##sequence-region P36001 1 430 +P36001 UniProtKB Chain 1 430 . . . ID=PRO_0000168307;Note=Probable folylpolyglutamate synthase +P36001 UniProtKB Nucleotide binding 37 40 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192 +P36001 UniProtKB Metal binding 132 132 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192 +P36001 UniProtKB Binding site 300 300 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08192 +##sequence-region P40099 1 211 +P40099 UniProtKB Chain 1 211 . . . ID=PRO_0000200280;Note=5-formyltetrahydrofolate cyclo-ligase +P40099 UniProtKB Nucleotide binding 4 8 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40099 UniProtKB Nucleotide binding 151 158 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40099 UniProtKB Region 152 156 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40099 UniProtKB Binding site 56 56 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40099 UniProtKB Binding site 194 194 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P04397 1 699 +P04397 UniProtKB Chain 1 699 . . . ID=PRO_0000197442;Note=Bifunctional protein GAL10 +P04397 UniProtKB Nucleotide binding 13 44 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04397 UniProtKB Region 1 357 . . . Note=Galactowaldenase +P04397 UniProtKB Region 358 699 . . . Note=Mutarotase +P04397 UniProtKB Active site 537 537 . . . Note=For mutarotase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04397 UniProtKB Modified residue 562 562 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04397 UniProtKB Sequence conflict 302 306 . . . Note=DLPYK->WSSVR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04397 UniProtKB Sequence conflict 464 464 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04397 UniProtKB Sequence conflict 479 480 . . . Note=KD->NY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04397 UniProtKB Sequence conflict 498 498 . . . Note=P->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04397 UniProtKB Sequence conflict 518 518 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04397 UniProtKB Sequence conflict 667 667 . . . Note=G->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04397 UniProtKB Sequence conflict 694 695 . . . Note=IV->TL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04397 UniProtKB Beta strand 13 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Turn 18 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 22 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 37 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 50 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 73 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 87 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 97 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 104 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 129 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 136 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 162 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 186 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 194 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 209 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 215 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 226 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 248 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 251 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 274 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 288 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 323 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 337 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 360 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 373 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 382 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 395 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 412 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 432 434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 435 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 438 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 444 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 455 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 460 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 464 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 470 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 481 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 492 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 495 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Turn 511 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 515 531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Turn 542 545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 548 550 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 553 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 561 565 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 571 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 585 587 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 589 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 599 604 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 621 627 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Turn 629 631 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 634 647 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 662 668 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 672 674 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Turn 676 678 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Helix 679 682 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 683 685 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +P04397 UniProtKB Beta strand 689 699 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z45 +##sequence-region P13181 1 574 +P13181 UniProtKB Chain 1 574 . . . ID=PRO_0000050416;Note=Galactose transporter +P13181 UniProtKB Topological domain 1 70 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Transmembrane 71 91 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Topological domain 92 121 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Transmembrane 122 142 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Topological domain 143 149 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Transmembrane 150 170 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Topological domain 171 175 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Transmembrane 176 196 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Topological domain 197 207 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Transmembrane 208 228 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Topological domain 229 242 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Transmembrane 243 263 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Topological domain 264 342 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Transmembrane 343 362 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Topological domain 363 366 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Transmembrane 367 387 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Topological domain 388 394 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Transmembrane 395 415 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Topological domain 416 435 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Transmembrane 436 456 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Topological domain 457 472 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Transmembrane 473 493 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Topological domain 494 499 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Transmembrane 500 520 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Topological domain 521 574 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13181 UniProtKB Modified residue 32 32 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13181 UniProtKB Modified residue 35 35 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13181 UniProtKB Modified residue 39 39 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13181 UniProtKB Modified residue 48 48 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13181 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13181 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13181 UniProtKB Modified residue 55 55 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13181 UniProtKB Sequence conflict 50 50 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13181 UniProtKB Sequence conflict 50 50 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13181 UniProtKB Sequence conflict 79 79 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13181 UniProtKB Sequence conflict 90 90 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13181 UniProtKB Sequence conflict 90 90 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13181 UniProtKB Sequence conflict 392 392 . . . Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13181 UniProtKB Sequence conflict 392 392 . . . Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P13045 1 520 +P13045 UniProtKB Chain 1 520 . . . ID=PRO_0000184658;Note=Protein GAL3 +P13045 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P13045 UniProtKB Sequence conflict 37 45 . . . Note=KPDFIARSP->NLILSLGLL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13045 UniProtKB Sequence conflict 170 171 . . . Note=AA->GR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13045 UniProtKB Sequence conflict 192 211 . . . Note=RITAVAEHYVGVNNGGMDQA->ASQRLRSTMLESIMVVWIKQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13045 UniProtKB Sequence conflict 227 241 . . . Note=RPKLKATPFKFPQLK->MAKTKWPHFQVSSIE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13045 UniProtKB Sequence conflict 251 294 . . . Note=NTLVKSNKFETAPTNYNLRVIEVTVAANALATRYSVALPSHKDN->ILCTRSNNRTLLHISLSCSLLTLLYISTFAREPCGPDTLGLTISQGQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13045 UniProtKB Sequence conflict 303 338 . . . Note=RDFMDAYYARYENQAQPWNGDIGTGIERLLKMLQLV->EIYGCLLRPDTKTKPNHGMEISELVLNVYSRCYNWY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13045 UniProtKB Sequence conflict 407 425 . . . Note=TFHTDEDFFTDFGRLMNES->IFTRTRFLYRFWPTNE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13045 UniProtKB Beta strand 7 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V2U +P13045 UniProtKB Helix 20 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Beta strand 39 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Beta strand 62 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Beta strand 84 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Beta strand 97 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Beta strand 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 119 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 137 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Beta strand 141 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Beta strand 148 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 162 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 187 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 198 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 208 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Beta strand 220 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Beta strand 227 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Beta strand 231 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Beta strand 244 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 258 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V2U +P13045 UniProtKB Turn 263 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 266 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Beta strand 296 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 302 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 324 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 343 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 351 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 362 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Beta strand 370 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Beta strand 378 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 382 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 411 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 438 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Beta strand 453 473 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 478 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 490 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Helix 499 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Beta strand 506 509 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +P13045 UniProtKB Beta strand 515 519 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V5R +##sequence-region P43574 1 510 +P43574 UniProtKB Chain 1 510 . . . ID=PRO_0000083484;Note=Transcriptional regulatory protein GAT1 +P43574 UniProtKB Zinc finger 310 334 . . . Note=GATA-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00094 +P43574 UniProtKB Compositional bias 151 158 . . . Note=Poly-Asp +P43574 UniProtKB Modified residue 167 167 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P43574 UniProtKB Modified residue 262 262 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P43574 UniProtKB Modified residue 270 270 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P43574 UniProtKB Modified residue 369 369 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43574 UniProtKB Modified residue 399 399 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P43574 UniProtKB Modified residue 418 418 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +##sequence-region P39012 1 614 +P39012 UniProtKB Chain 1 614 . . . ID=PRO_0000087417;Note=GPI transamidase component GAA1 +P39012 UniProtKB Topological domain 1 19 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39012 UniProtKB Transmembrane 20 40 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39012 UniProtKB Topological domain 41 356 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39012 UniProtKB Transmembrane 357 377 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39012 UniProtKB Topological domain 378 394 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39012 UniProtKB Transmembrane 395 415 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39012 UniProtKB Topological domain 416 464 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39012 UniProtKB Transmembrane 465 485 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39012 UniProtKB Topological domain 486 535 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39012 UniProtKB Transmembrane 536 556 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39012 UniProtKB Topological domain 557 577 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39012 UniProtKB Transmembrane 578 598 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39012 UniProtKB Topological domain 599 614 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39012 UniProtKB Motif 610 614 . . . Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39012 UniProtKB Glycosylation 87 87 . . . Note=N-linked (GlcNAc...) asparagine +P39012 UniProtKB Mutagenesis 87 87 . . . Note=Loss of N-glycosylation. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7730400;Dbxref=PMID:7730400 +##sequence-region P28006 1 793 +P28006 UniProtKB Chain 1 793 . . . ID=PRO_0000071518;Note=Serine/threonine-protein phosphatase 1 regulatory subunit GAC1 +P28006 UniProtKB Domain 235 360 . . . Note=CBM21;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00491 +P28006 UniProtKB Compositional bias 500 523 . . . Note=Ser-rich +P28006 UniProtKB Modified residue 415 415 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P28006 UniProtKB Modified residue 424 424 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P28006 UniProtKB Sequence conflict 228 228 . . . Note=S->SS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P41913 1 522 +P41913 UniProtKB Chain 1 522 . . . ID=PRO_0000087453;Note=Protein GDS1 +##sequence-region Q08622 1 556 +Q08622 UniProtKB Transit peptide 1 21 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08622 UniProtKB Chain 22 556 . . . ID=PRO_0000237640;Note=Genetic interactor of prohibitins 3%2C mitochondrial +Q08622 UniProtKB Domain 113 305 . . . Note=CP-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01058 +##sequence-region P40056 1 285 +P40056 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40056 UniProtKB Chain 2 285 . . . ID=PRO_0000097362;Note=Golgi to ER traffic protein 2 +P40056 UniProtKB Topological domain 2 148 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03114 +P40056 UniProtKB Transmembrane 149 169 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03114 +P40056 UniProtKB Topological domain 170 196 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03114 +P40056 UniProtKB Transmembrane 197 216 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03114 +P40056 UniProtKB Topological domain 217 263 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03114 +P40056 UniProtKB Transmembrane 264 284 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03114 +P40056 UniProtKB Topological domain 285 285 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03114 +P40056 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40056 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40056 UniProtKB Glycosylation 173 173 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03114 +P40056 UniProtKB Glycosylation 196 196 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03114 +P40056 UniProtKB Helix 6 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZS9 +P40056 UniProtKB Turn 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZS9 +P40056 UniProtKB Helix 25 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZS9 +##sequence-region P14742 1 717 +P14742 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15699032;Dbxref=PMID:15699032 +P14742 UniProtKB Chain 2 717 . . . ID=PRO_0000135289;Note=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] +P14742 UniProtKB Domain 2 318 . . . Note=Glutamine amidotransferase type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609 +P14742 UniProtKB Domain 390 529 . . . Note=SIS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00797 +P14742 UniProtKB Domain 562 707 . . . Note=SIS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00797 +P14742 UniProtKB Active site 2 2 . . . Note=For GATase activity;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15699032;Dbxref=PMID:15699032 +P14742 UniProtKB Modified residue 253 253 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P14742 UniProtKB Modified residue 334 334 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14742 UniProtKB Modified residue 336 336 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14742 UniProtKB Sequence conflict 453 454 . . . Note=QS->HC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14742 UniProtKB Sequence conflict 534 534 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40036 1 548 +P40036 UniProtKB Chain 1 548 . . . ID=PRO_0000071521;Note=GLC7-interacting protein 2 +P40036 UniProtKB Domain 419 534 . . . Note=CBM21;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00491 +P40036 UniProtKB Modified residue 51 51 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40036 UniProtKB Modified residue 52 52 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40036 UniProtKB Modified residue 155 155 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40036 UniProtKB Modified residue 221 221 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P40036 UniProtKB Modified residue 238 238 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P39732 1 760 +P39732 UniProtKB Chain 1 760 . . . ID=PRO_0000202416;Note=GLC7-interacting protein 4 +P39732 UniProtKB Modified residue 497 497 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P39732 UniProtKB Modified residue 501 501 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P39732 UniProtKB Modified residue 609 609 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P53849 1 153 +P53849 UniProtKB Chain 1 153 . . . ID=PRO_0000087496;Note=Zinc finger protein GIS2 +P53849 UniProtKB Zinc finger 4 21 . . . Note=CCHC-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +P53849 UniProtKB Zinc finger 23 40 . . . Note=CCHC-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +P53849 UniProtKB Zinc finger 47 64 . . . Note=CCHC-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +P53849 UniProtKB Zinc finger 65 82 . . . Note=CCHC-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +P53849 UniProtKB Zinc finger 92 109 . . . Note=CCHC-type 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +P53849 UniProtKB Zinc finger 116 133 . . . Note=CCHC-type 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +P53849 UniProtKB Zinc finger 135 152 . . . Note=CCHC-type 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +##sequence-region P25346 1 518 +P25346 UniProtKB Chain 1 518 . . . ID=PRO_0000050459;Note=Glycerophosphoinositol transporter 1 +P25346 UniProtKB Topological domain 1 44 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Transmembrane 45 65 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Topological domain 66 91 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Transmembrane 92 112 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Topological domain 113 114 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Transmembrane 115 136 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Topological domain 137 138 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Transmembrane 139 159 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Topological domain 160 184 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Transmembrane 185 205 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Topological domain 206 216 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Transmembrane 217 237 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Topological domain 238 268 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Transmembrane 269 289 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Topological domain 290 306 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Transmembrane 307 327 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Topological domain 328 335 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Transmembrane 336 356 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Topological domain 357 360 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Transmembrane 361 381 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Topological domain 382 399 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Transmembrane 400 420 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Topological domain 421 430 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Transmembrane 431 451 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Topological domain 452 518 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25346 UniProtKB Glycosylation 80 80 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12315 1 538 +Q12315 UniProtKB Chain 1 538 . . . ID=PRO_0000204820;Note=Nucleoporin GLE1 +Q12315 UniProtKB Region 257 538 . . . Note=Interactions with NUP42%2C DBP5 and GFD1 +Q12315 UniProtKB Coiled coil 131 244 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12315 UniProtKB Motif 154 170 . . . Note=Bipartite nuclear localization signal 1 +Q12315 UniProtKB Motif 272 288 . . . Note=Bipartite nuclear localization signal 2 +Q12315 UniProtKB Compositional bias 157 229 . . . Note=Glu-rich +Q12315 UniProtKB Compositional bias 161 273 . . . Note=Lys-rich +Q12315 UniProtKB Compositional bias 164 167 . . . Note=Poly-Glu +Q12315 UniProtKB Mutagenesis 351 351 . . . Note=Partial loss of activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8848052;Dbxref=PMID:8848052 +Q12315 UniProtKB Mutagenesis 353 353 . . . Note=Partial loss of activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8848052;Dbxref=PMID:8848052 +Q12315 UniProtKB Mutagenesis 356 356 . . . Note=Temperature-sensitive. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8848052;Dbxref=PMID:8848052 +Q12315 UniProtKB Mutagenesis 358 358 . . . Note=Partial loss of activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8848052;Dbxref=PMID:8848052 +Q12315 UniProtKB Helix 245 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Helix 268 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Helix 276 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Helix 292 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Helix 300 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Turn 316 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Helix 321 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Helix 347 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Helix 350 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Helix 367 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Helix 380 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Helix 392 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Helix 411 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Turn 435 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Helix 448 458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Helix 462 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Helix 467 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Helix 490 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Helix 502 506 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Helix 508 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +Q12315 UniProtKB Helix 513 526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PEV +##sequence-region P36143 1 616 +P36143 UniProtKB Chain 1 616 . . . ID=PRO_0000215181;Note=Glycogenin-1 +P36143 UniProtKB Glycosylation 230 230 . . . Note=O-linked (Glc...) tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36143 UniProtKB Glycosylation 598 598 . . . Note=O-linked (Glc...) tyrosine;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36143 UniProtKB Mutagenesis 230 230 . . . Note=Eliminates glycogen accumulation%3B when associated with F-598. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8900126;Dbxref=PMID:8900126 +P36143 UniProtKB Mutagenesis 598 598 . . . Note=Eliminates glycogen accumulation%3B when associated with F-230. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8900126;Dbxref=PMID:8900126 +##sequence-region P38777 1 243 +P38777 UniProtKB Chain 1 243 . . . ID=PRO_0000212580;Note=Family of serine hydrolases 1 +P38777 UniProtKB Active site 110 110 . . . Note=Charge relay system;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15802654;Dbxref=PMID:15802654 +P38777 UniProtKB Active site 183 183 . . . Note=Charge relay system;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15802654;Dbxref=PMID:15802654 +P38777 UniProtKB Active site 218 218 . . . Note=Charge relay system;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15802654;Dbxref=PMID:15802654 +P38777 UniProtKB Beta strand 7 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Helix 18 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Helix 26 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Beta strand 38 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Beta strand 45 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Helix 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Helix 59 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Beta strand 72 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Helix 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Helix 87 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Beta strand 104 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Helix 111 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Beta strand 134 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Beta strand 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Beta strand 155 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Helix 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Turn 162 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Beta strand 174 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Beta strand 184 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Helix 188 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Turn 202 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Turn 206 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Beta strand 209 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +P38777 UniProtKB Helix 224 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YCD +##sequence-region P05316 1 633 +P05316 UniProtKB Chain 1 633 . . . ID=PRO_0000197925;Note=Uracil permease +P05316 UniProtKB Transmembrane 143 163 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05316 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05316 UniProtKB Transmembrane 197 217 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05316 UniProtKB Transmembrane 242 262 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05316 UniProtKB Transmembrane 268 288 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05316 UniProtKB Transmembrane 310 330 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05316 UniProtKB Transmembrane 350 370 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05316 UniProtKB Transmembrane 400 420 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05316 UniProtKB Transmembrane 442 462 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05316 UniProtKB Transmembrane 465 485 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05316 UniProtKB Transmembrane 521 541 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05316 UniProtKB Transmembrane 559 579 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05316 UniProtKB Sequence conflict 217 217 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05316 UniProtKB Sequence conflict 229 229 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05316 UniProtKB Sequence conflict 320 320 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q05670 1 677 +Q05670 UniProtKB Chain 1 677 . . . ID=PRO_0000080954;Note=Nuclear fusion protein FUS2 +Q05670 UniProtKB Domain 112 326 . . . Note=DH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00062 +Q05670 UniProtKB Modified residue 20 20 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q05670 UniProtKB Modified residue 67 67 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q05670 UniProtKB Modified residue 72 72 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q05670 UniProtKB Modified residue 84 84 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q05670 UniProtKB Modified residue 88 88 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q05670 UniProtKB Modified residue 100 100 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q05670 UniProtKB Modified residue 106 106 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q05670 UniProtKB Sequence conflict 185 185 . . . Note=L->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q05670 UniProtKB Sequence conflict 203 203 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q05670 UniProtKB Sequence conflict 543 546 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q05670 UniProtKB Sequence conflict 589 677 . . . Note=HDTIECILLNYIKVFLKYLEIIAGGKKYLQKDLENMSLNDSIATGQIKNLDILQCYSKSRYMTKRMVRKDWPFPGDPSGSRVVRKLFEL->PRYYRMYLVELYQSLLKIFGNHCWWKKIPAKRS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08559 1 129 +Q08559 UniProtKB Chain 1 129 . . . ID=PRO_0000239648;Note=Protein FYV12 +Q08559 UniProtKB Transmembrane 109 128 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08559 UniProtKB Glycosylation 91 91 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P25585 1 152 +P25585 UniProtKB Chain 1 152 . . . ID=PRO_0000202552;Note=Protein FYV5 +P25585 UniProtKB Transmembrane 26 46 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25585 UniProtKB Transmembrane 56 76 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25585 UniProtKB Transmembrane 82 102 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25585 UniProtKB Transmembrane 106 126 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25585 UniProtKB Transmembrane 127 147 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P46949 1 817 +P46949 UniProtKB Chain 1 817 . . . ID=PRO_0000202842;Note=Protein FYV8 +P46949 UniProtKB Modified residue 92 92 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P46949 UniProtKB Modified residue 100 100 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P46949 UniProtKB Modified residue 134 134 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P46949 UniProtKB Modified residue 163 163 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P46949 UniProtKB Modified residue 180 180 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P46949 UniProtKB Modified residue 182 182 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P46949 UniProtKB Modified residue 237 237 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P46949 UniProtKB Modified residue 238 238 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P46949 UniProtKB Modified residue 532 532 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P00360 1 332 +P00360 UniProtKB Chain 1 332 . . . ID=PRO_0000145589;Note=Glyceraldehyde-3-phosphate dehydrogenase 1 +P00360 UniProtKB Nucleotide binding 11 12 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00360 UniProtKB Region 149 151 . . . Note=Glyceraldehyde 3-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00360 UniProtKB Region 209 210 . . . Note=Glyceraldehyde 3-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00360 UniProtKB Active site 150 150 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10009 +P00360 UniProtKB Binding site 33 33 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00360 UniProtKB Binding site 78 78 . . . Note=NAD%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00360 UniProtKB Binding site 180 180 . . . Note=Glyceraldehyde 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00360 UniProtKB Binding site 232 232 . . . Note=Glyceraldehyde 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00360 UniProtKB Binding site 314 314 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00360 UniProtKB Site 177 177 . . . Note=Activates thiol group during catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00360 UniProtKB Sequence conflict 248 248 . . . Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P08431 1 366 +P08431 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6324089;Dbxref=PMID:6324089 +P08431 UniProtKB Chain 2 366 . . . ID=PRO_0000169893;Note=Galactose-1-phosphate uridylyltransferase +P08431 UniProtKB Region 79 80 . . . Note=UDP-alpha-D-glucose binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07902 +P08431 UniProtKB Region 329 332 . . . Note=UDP-alpha-D-glucose binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07902 +P08431 UniProtKB Region 334 335 . . . Note=UDP-alpha-D-glucose binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07902 +P08431 UniProtKB Active site 182 182 . . . Note=Tele-UMP-histidine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10033 +P08431 UniProtKB Metal binding 54 54 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10033 +P08431 UniProtKB Metal binding 57 57 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10033 +P08431 UniProtKB Metal binding 124 124 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10033 +P08431 UniProtKB Metal binding 180 180 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10033 +P08431 UniProtKB Metal binding 198 198 . . . Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09148 +P08431 UniProtKB Metal binding 297 297 . . . Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09148 +P08431 UniProtKB Metal binding 314 314 . . . Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09148 +P08431 UniProtKB Metal binding 316 316 . . . Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09148 +P08431 UniProtKB Binding site 63 63 . . . Note=UDP-alpha-D-glucose%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07902 +P08431 UniProtKB Binding site 169 169 . . . Note=UDP-alpha-D-glucose%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07902 +P08431 UniProtKB Binding site 184 184 . . . Note=UDP-alpha-D-glucose;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07902 +P08431 UniProtKB Modified residue 27 27 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P08431 UniProtKB Sequence conflict 11 11 . . . Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08431 UniProtKB Sequence conflict 58 58 . . . Note=P->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08431 UniProtKB Sequence conflict 85 86 . . . Note=RL->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08431 UniProtKB Sequence conflict 267 267 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08431 UniProtKB Sequence conflict 345 345 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P04387 1 435 +P04387 UniProtKB Chain 1 435 . . . ID=PRO_0000087427;Note=Galactose/lactose metabolism regulatory protein GAL80 +P04387 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1985957;Dbxref=PMID:1985957 +P04387 UniProtKB Sequence conflict 101 101 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04387 UniProtKB Beta strand 18 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Beta strand 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Turn 32 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Helix 36 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Turn 43 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Beta strand 47 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Helix 57 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Beta strand 73 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V2U +P04387 UniProtKB Helix 78 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Beta strand 88 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Helix 99 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Helix 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Beta strand 118 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Helix 129 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Beta strand 145 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Helix 151 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Helix 156 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Turn 167 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Beta strand 172 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Beta strand 183 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Helix 195 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Turn 206 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Helix 210 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Beta strand 226 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Beta strand 238 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Beta strand 245 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTS +P04387 UniProtKB Beta strand 249 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Beta strand 260 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Turn 269 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Beta strand 273 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Beta strand 287 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V2U +P04387 UniProtKB Beta strand 291 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Beta strand 302 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Helix 312 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V2U +P04387 UniProtKB Beta strand 316 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Beta strand 348 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Helix 360 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Turn 377 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Beta strand 396 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Helix 402 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +P04387 UniProtKB Turn 428 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BTV +##sequence-region P25555 1 427 +P25555 UniProtKB Chain 1 427 . . . ID=PRO_0000081596;Note=Single-strand telomeric DNA-binding protein GBP2 +P25555 UniProtKB Domain 122 198 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P25555 UniProtKB Domain 219 296 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P25555 UniProtKB Domain 349 426 . . . Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P25555 UniProtKB Modified residue 130 130 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25555 UniProtKB Helix 332 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ +P25555 UniProtKB Turn 337 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ +P25555 UniProtKB Beta strand 349 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ +P25555 UniProtKB Helix 362 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ +P25555 UniProtKB Helix 365 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ +P25555 UniProtKB Turn 370 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ +P25555 UniProtKB Beta strand 375 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ +P25555 UniProtKB Beta strand 390 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ +P25555 UniProtKB Helix 399 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ +P25555 UniProtKB Beta strand 420 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZQ +##sequence-region P51601 1 243 +P51601 UniProtKB Chain 1 243 . . . ID=PRO_0000119489;Note=GTP cyclohydrolase 1 +P51601 UniProtKB Metal binding 132 132 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P51601 UniProtKB Metal binding 135 135 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P51601 UniProtKB Metal binding 203 203 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P51601 UniProtKB Modified residue 15 15 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P51601 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P51601 UniProtKB Sequence conflict 159 160 . . . Note=LA->QG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P51601 UniProtKB Sequence conflict 206 206 . . . Note=S->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P51601 UniProtKB Sequence conflict 217 217 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07928 1 141 +Q07928 UniProtKB Chain 1 141 . . . ID=PRO_0000083486;Note=Protein GAT3 +Q07928 UniProtKB Zinc finger 72 98 . . . Note=GATA-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00094 +##sequence-region P33893 1 541 +P33893 UniProtKB Chain 1 541 . . . ID=PRO_0000010712;Note=Glutamyl-tRNA(Gln) amidotransferase subunit B%2C mitochondrial +P33893 UniProtKB Sequence conflict 415 415 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33893 UniProtKB Sequence conflict 415 415 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33893 UniProtKB Beta strand 29 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Beta strand 45 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Turn 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Turn 66 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Helix 80 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Beta strand 99 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Beta strand 104 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Beta strand 116 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Beta strand 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Beta strand 126 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Beta strand 131 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Helix 136 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Beta strand 142 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Beta strand 161 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Beta strand 172 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Beta strand 183 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Helix 196 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Turn 220 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Beta strand 224 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Beta strand 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Helix 247 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Beta strand 277 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Beta strand 304 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P33893 UniProtKB Beta strand 309 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0I +P33893 UniProtKB Helix 313 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +##sequence-region P43535 1 752 +P43535 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P43535 UniProtKB Chain 2 752 . . . ID=PRO_0000093461;Note=Protein GCN20 +P43535 UniProtKB Domain 199 464 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P43535 UniProtKB Domain 532 748 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P43535 UniProtKB Nucleotide binding 232 239 . . . Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P43535 UniProtKB Nucleotide binding 565 572 . . . Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P43535 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P53171 1 287 +P53171 UniProtKB Transit peptide 1 24 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53171 UniProtKB Chain 25 287 . . . ID=PRO_0000202766;Note=Genetic interactor of prohibitin 7%2C mitochondrial +P53171 UniProtKB Transmembrane 250 266 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53192 1 235 +P53192 UniProtKB Chain 1 235 . . . ID=PRO_0000414847;Note=Golgi to ER traffic protein 1 +P53192 UniProtKB Topological domain 1 1 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03113 +P53192 UniProtKB Transmembrane 2 21 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03113 +P53192 UniProtKB Topological domain 22 104 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03113 +P53192 UniProtKB Transmembrane 105 125 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03113 +P53192 UniProtKB Topological domain 126 181 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03113 +P53192 UniProtKB Transmembrane 182 198 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03113 +P53192 UniProtKB Topological domain 199 235 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03113 +P53192 UniProtKB Coiled coil 68 104 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03113 +P53192 UniProtKB Helix 40 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E +P53192 UniProtKB Turn 61 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E +P53192 UniProtKB Helix 65 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E +P53192 UniProtKB Turn 79 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E +P53192 UniProtKB Helix 85 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E +P53192 UniProtKB Turn 89 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E +P53192 UniProtKB Turn 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E +P53192 UniProtKB Helix 100 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SJB +##sequence-region Q12154 1 354 +Q12154 UniProtKB Chain 1 354 . . . ID=PRO_0000152256;Note=ATPase GET3 +Q12154 UniProtKB Nucleotide binding 26 33 . . . Note=ATP +Q12154 UniProtKB Nucleotide binding 315 322 . . . Note=ATP +Q12154 UniProtKB Active site 57 57 . . . . +Q12154 UniProtKB Metal binding 285 285 . . . Note=Zinc%3B shared with dimeric partner;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03112,ECO:0000269|PubMed:19675567;Dbxref=PMID:19675567 +Q12154 UniProtKB Metal binding 288 288 . . . Note=Zinc%3B shared with dimeric partner;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03112,ECO:0000269|PubMed:19675567;Dbxref=PMID:19675567 +Q12154 UniProtKB Binding site 245 245 . . . Note=ATP +Q12154 UniProtKB Binding site 272 272 . . . Note=ATP +Q12154 UniProtKB Mutagenesis 30 30 . . . Note=Abolishes ATPase activity%2C leading to secretion of resident ER proteins. G->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12680698,ECO:0000269|PubMed:19706470;Dbxref=PMID:12680698,PMID:19706470 +Q12154 UniProtKB Mutagenesis 57 57 . . . Note=Abolishes ATP hydrolysis. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19675567;Dbxref=PMID:19675567 +Q12154 UniProtKB Mutagenesis 285 285 . . . Note=Prevents dimerization%3B when associated with S-288. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19675567;Dbxref=PMID:19675567 +Q12154 UniProtKB Mutagenesis 288 288 . . . Note=Prevents dimerization%3B when associated with S-285. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19675567;Dbxref=PMID:19675567 +Q12154 UniProtKB Sequence conflict 43 43 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12154 UniProtKB Beta strand 7 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XWO +Q12154 UniProtKB Helix 10 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Beta strand 20 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Beta strand 27 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H84 +Q12154 UniProtKB Helix 31 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Beta strand 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E +Q12154 UniProtKB Beta strand 51 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Beta strand 57 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XVU +Q12154 UniProtKB Helix 62 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Beta strand 81 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Helix 90 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Turn 102 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E +Q12154 UniProtKB Beta strand 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H84 +Q12154 UniProtKB Helix 117 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H84 +Q12154 UniProtKB Helix 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H84 +Q12154 UniProtKB Helix 125 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Helix 136 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Beta strand 155 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H84 +Q12154 UniProtKB Beta strand 161 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Helix 170 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Helix 179 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Helix 191 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H84 +Q12154 UniProtKB Beta strand 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B2E +Q12154 UniProtKB Helix 200 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H84 +Q12154 UniProtKB Turn 206 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H84 +Q12154 UniProtKB Helix 213 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Turn 233 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Beta strand 236 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Helix 246 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Beta strand 268 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Turn 277 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H84 +Q12154 UniProtKB Helix 286 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Turn 306 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Beta strand 309 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Helix 323 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Helix 340 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +Q12154 UniProtKB Helix 344 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WOJ +##sequence-region Q04839 1 188 +Q04839 UniProtKB Chain 1 188 . . . ID=PRO_0000087477;Note=mRNA transport factor GFD1 +Q04839 UniProtKB Coiled coil 119 164 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04839 UniProtKB Compositional bias 17 136 . . . Note=Lys-rich +Q04839 UniProtKB Compositional bias 152 155 . . . Note=Poly-Gln +Q04839 UniProtKB Modified residue 87 87 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956 +Q04839 UniProtKB Modified residue 106 106 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +Q04839 UniProtKB Modified residue 111 111 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q04839 UniProtKB Helix 127 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LCN +##sequence-region P22146 1 559 +P22146 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1824714;Dbxref=PMID:1824714 +P22146 UniProtKB Chain 23 528 . . . ID=PRO_0000010473;Note=1%2C3-beta-glucanosyltransferase GAS1 +P22146 UniProtKB Propeptide 529 559 . . . ID=PRO_0000010474;Note=Removed in mature form +P22146 UniProtKB Region 119 127 . . . Note=Donor substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22146 UniProtKB Compositional bias 438 525 . . . Note=Ser-rich +P22146 UniProtKB Active site 161 161 . . . Note=Proton donor +P22146 UniProtKB Active site 262 262 . . . Note=Nucleophile +P22146 UniProtKB Binding site 92 92 . . . Note=Donor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22146 UniProtKB Binding site 160 160 . . . Note=Donor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22146 UniProtKB Binding site 161 161 . . . Note=Acceptor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22146 UniProtKB Binding site 202 202 . . . Note=Acceptor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22146 UniProtKB Binding site 207 207 . . . Note=Acceptor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22146 UniProtKB Binding site 294 294 . . . Note=Donor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22146 UniProtKB Lipidation 528 528 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1824714;Dbxref=PMID:1824714 +P22146 UniProtKB Glycosylation 40 40 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22146 UniProtKB Glycosylation 57 57 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22146 UniProtKB Glycosylation 95 95 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22146 UniProtKB Glycosylation 149 149 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22146 UniProtKB Glycosylation 165 165 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22146 UniProtKB Glycosylation 253 253 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22146 UniProtKB Glycosylation 283 283 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22146 UniProtKB Glycosylation 321 321 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22146 UniProtKB Glycosylation 409 409 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22146 UniProtKB Glycosylation 495 495 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22146 UniProtKB Disulfide bond 74 103 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22146 UniProtKB Disulfide bond 216 348 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22146 UniProtKB Disulfide bond 234 265 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22146 UniProtKB Disulfide bond 370 421 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22146 UniProtKB Disulfide bond 372 462 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22146 UniProtKB Disulfide bond 379 445 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22146 UniProtKB Disulfide bond 398 403 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22146 UniProtKB Mutagenesis 74 74 . . . Note=Impairs the folding and stability of the protein. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15355340;Dbxref=PMID:15355340 +P22146 UniProtKB Mutagenesis 103 103 . . . Note=Partially impairs the folding and stability of the protein. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15355340;Dbxref=PMID:15355340 +P22146 UniProtKB Mutagenesis 161 161 . . . Note=Loss of function. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15355340;Dbxref=PMID:15355340 +P22146 UniProtKB Mutagenesis 262 262 . . . Note=Loss of function. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15355340;Dbxref=PMID:15355340 +P22146 UniProtKB Mutagenesis 265 265 . . . Note=Partially impairs the folding and stability of the protein. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15355340;Dbxref=PMID:15355340 +P22146 UniProtKB Mutagenesis 348 348 . . . Note=Impairs the folding and stability of the protein. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18468997;Dbxref=PMID:18468997 +P22146 UniProtKB Sequence conflict 211 211 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06135 1 555 +Q06135 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06135 UniProtKB Chain 25 531 . . . ID=PRO_0000010475;Note=1%2C3-beta-glucanosyltransferase GAS2 +Q06135 UniProtKB Propeptide 532 555 . . . ID=PRO_0000010476;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06135 UniProtKB Region 134 142 . . . Note=Donor substrate binding;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19097997;Dbxref=PMID:19097997 +Q06135 UniProtKB Active site 176 176 . . . Note=Proton donor +Q06135 UniProtKB Active site 275 275 . . . Note=Nucleophile +Q06135 UniProtKB Binding site 107 107 . . . Note=Donor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19097997;Dbxref=PMID:19097997 +Q06135 UniProtKB Binding site 175 175 . . . Note=Donor substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19097997;Dbxref=PMID:19097997 +Q06135 UniProtKB Binding site 176 176 . . . Note=Acceptor substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19097997;Dbxref=PMID:19097997 +Q06135 UniProtKB Binding site 217 217 . . . Note=Acceptor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19097997;Dbxref=PMID:19097997 +Q06135 UniProtKB Binding site 222 222 . . . Note=Acceptor substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19097997;Dbxref=PMID:19097997 +Q06135 UniProtKB Binding site 307 307 . . . Note=Donor substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19097997;Dbxref=PMID:19097997 +Q06135 UniProtKB Lipidation 531 531 . . . Note=GPI-anchor amidated aspartate;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06135 UniProtKB Glycosylation 498 498 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06135 UniProtKB Disulfide bond 89 118 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18468997,ECO:0000269|PubMed:19097997;Dbxref=PMID:18468997,PMID:19097997 +Q06135 UniProtKB Disulfide bond 231 367 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18468997,ECO:0000269|PubMed:19097997;Dbxref=PMID:18468997,PMID:19097997 +Q06135 UniProtKB Disulfide bond 247 278 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18468997,ECO:0000269|PubMed:19097997;Dbxref=PMID:18468997,PMID:19097997 +Q06135 UniProtKB Disulfide bond 390 442 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18468997,ECO:0000269|PubMed:19097997;Dbxref=PMID:18468997,PMID:19097997 +Q06135 UniProtKB Disulfide bond 392 489 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18468997,ECO:0000269|PubMed:19097997;Dbxref=PMID:18468997,PMID:19097997 +Q06135 UniProtKB Disulfide bond 399 466 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18468997,ECO:0000269|PubMed:19097997;Dbxref=PMID:18468997,PMID:19097997 +Q06135 UniProtKB Disulfide bond 419 424 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18468997,ECO:0000269|PubMed:19097997;Dbxref=PMID:18468997,PMID:19097997 +Q06135 UniProtKB Mutagenesis 62 62 . . . Note=Slightly reduces catalytic activity. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997 +Q06135 UniProtKB Mutagenesis 107 107 . . . Note=Slightly reduces catalytic activity. Y->F%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997 +Q06135 UniProtKB Mutagenesis 132 132 . . . Note=Slightly reduces catalytic activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997 +Q06135 UniProtKB Mutagenesis 175 175 . . . Note=Abolishes catalytic activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997 +Q06135 UniProtKB Mutagenesis 176 176 . . . Note=Abolishes catalytic activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997 +Q06135 UniProtKB Mutagenesis 244 244 . . . Note=Moderately reduces hydrolysis%2C and causes a 10-fold reduction in transglycosylation activity. Y->F%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997 +Q06135 UniProtKB Mutagenesis 275 275 . . . Note=Abolishes catalytic activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997 +Q06135 UniProtKB Mutagenesis 307 307 . . . Note=Moderately reduces catalytic activity. Y->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997 +Q06135 UniProtKB Mutagenesis 404 404 . . . Note=Slightly reduces catalytic activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997 +Q06135 UniProtKB Mutagenesis 474 474 . . . Note=No effect. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19097997;Dbxref=PMID:19097997 +Q06135 UniProtKB Beta strand 36 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Beta strand 42 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Turn 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Beta strand 54 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Turn 72 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 86 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Beta strand 102 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 116 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Beta strand 128 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Beta strand 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FIH +Q06135 UniProtKB Helix 149 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Beta strand 168 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 184 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 187 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Beta strand 204 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Beta strand 211 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Turn 219 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 222 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Beta strand 239 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 252 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 257 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Beta strand 271 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Beta strand 280 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 288 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 295 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Beta strand 303 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Beta strand 313 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W62 +Q06135 UniProtKB Beta strand 318 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Beta strand 327 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 331 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 350 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Turn 372 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 387 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Beta strand 398 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 408 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 411 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Turn 419 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 424 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Turn 431 434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Turn 438 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 444 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Beta strand 473 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 477 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +Q06135 UniProtKB Helix 490 501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2W61 +##sequence-region P18851 1 423 +P18851 UniProtKB Chain 1 423 . . . ID=PRO_0000127720;Note=Guanine nucleotide-binding protein subunit beta +P18851 UniProtKB Repeat 90 120 . . . Note=WD 1 +P18851 UniProtKB Repeat 132 162 . . . Note=WD 2 +P18851 UniProtKB Repeat 179 208 . . . Note=WD 3 +P18851 UniProtKB Repeat 220 256 . . . Note=WD 4 +P18851 UniProtKB Repeat 268 298 . . . Note=WD 5 +P18851 UniProtKB Repeat 348 377 . . . Note=WD 6 +P18851 UniProtKB Repeat 389 419 . . . Note=WD 7 +P18851 UniProtKB Sequence conflict 33 33 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18851 UniProtKB Sequence conflict 236 236 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39993 1 1459 +P39993 UniProtKB Chain 1 1459 . . . ID=PRO_0000120213;Note=ARF guanine-nucleotide exchange factor 2 +P39993 UniProtKB Domain 570 714 . . . Note=SEC7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00189 +P39993 UniProtKB Modified residue 46 46 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39993 UniProtKB Modified residue 284 284 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P39993 UniProtKB Helix 558 572 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1 +P39993 UniProtKB Helix 574 583 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1 +P39993 UniProtKB Beta strand 586 588 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1 +P39993 UniProtKB Helix 592 601 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1 +P39993 UniProtKB Turn 602 605 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1 +P39993 UniProtKB Helix 608 615 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1 +P39993 UniProtKB Helix 618 620 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1 +P39993 UniProtKB Helix 621 629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1 +P39993 UniProtKB Helix 638 645 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1 +P39993 UniProtKB Turn 646 648 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1 +P39993 UniProtKB Helix 655 671 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1 +P39993 UniProtKB Helix 677 679 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1 +P39993 UniProtKB Helix 688 690 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1 +P39993 UniProtKB Helix 695 712 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1 +P39993 UniProtKB Helix 723 729 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1 +P39993 UniProtKB Turn 730 732 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1 +P39993 UniProtKB Helix 741 753 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KU1 +##sequence-region P25370 1 566 +P25370 UniProtKB Chain 1 566 . . . ID=PRO_0000202543;Note=Good for full DBP5 activity protein 2 +##sequence-region Q12051 1 335 +Q12051 UniProtKB Chain 1 335 . . . ID=PRO_0000228139;Note=Geranylgeranyl pyrophosphate synthase +Q12051 UniProtKB Metal binding 75 75 . . . Note=Magnesium 1;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16554305,ECO:0000269|PubMed:17535895;Dbxref=PMID:16554305,PMID:17535895 +Q12051 UniProtKB Metal binding 75 75 . . . Note=Magnesium 2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16554305,ECO:0000269|PubMed:17535895;Dbxref=PMID:16554305,PMID:17535895 +Q12051 UniProtKB Metal binding 79 79 . . . Note=Magnesium 1;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16554305,ECO:0000269|PubMed:17535895;Dbxref=PMID:16554305,PMID:17535895 +Q12051 UniProtKB Metal binding 79 79 . . . Note=Magnesium 2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16554305,ECO:0000269|PubMed:17535895;Dbxref=PMID:16554305,PMID:17535895 +Q12051 UniProtKB Metal binding 209 209 . . . Note=Magnesium 3;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16554305,ECO:0000269|PubMed:17535895;Dbxref=PMID:16554305,PMID:17535895 +Q12051 UniProtKB Binding site 36 36 . . . Note=Isopentenyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895 +Q12051 UniProtKB Binding site 39 39 . . . Note=Isopentenyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895 +Q12051 UniProtKB Binding site 68 68 . . . Note=Isopentenyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895 +Q12051 UniProtKB Binding site 84 84 . . . Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895 +Q12051 UniProtKB Binding site 85 85 . . . Note=Isopentenyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895 +Q12051 UniProtKB Binding site 169 169 . . . Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895 +Q12051 UniProtKB Binding site 170 170 . . . Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895 +Q12051 UniProtKB Binding site 206 206 . . . Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895 +Q12051 UniProtKB Binding site 213 213 . . . Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895 +Q12051 UniProtKB Binding site 223 223 . . . Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12051 UniProtKB Binding site 233 233 . . . Note=Dimethylallyl diphosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17535895;Dbxref=PMID:17535895 +Q12051 UniProtKB Site 107 107 . . . Note=Important for determining product chain length +Q12051 UniProtKB Mutagenesis 7 7 . . . Note=No effect. Monomer%3B when associated with G-8. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19245203;Dbxref=PMID:19245203 +Q12051 UniProtKB Mutagenesis 8 8 . . . Note=Monomer and homodimer. Monomer%3B when associated with G-7. L->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19245203;Dbxref=PMID:19245203 +Q12051 UniProtKB Mutagenesis 9 9 . . . Note=Mostly monomer. Exclusively monomer%3B when associated with G-8. Reduces enzyme activity 1000-fold. I->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19245203;Dbxref=PMID:19245203 +Q12051 UniProtKB Mutagenesis 107 107 . . . Note=Reduced affinity for isopentenyl diphosphate (IPP). Y->A +Q12051 UniProtKB Mutagenesis 108 108 . . . Note=Reduced affinity for isopentenyl diphosphate (IPP). F->A +Q12051 UniProtKB Mutagenesis 139 139 . . . Note=Reduced affinity for isopentenyl diphosphate (IPP). H->A +Q12051 UniProtKB Helix 1 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V +Q12051 UniProtKB Helix 17 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V +Q12051 UniProtKB Beta strand 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8X +Q12051 UniProtKB Helix 38 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V +Q12051 UniProtKB Helix 54 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V +Q12051 UniProtKB Beta strand 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V +Q12051 UniProtKB Helix 90 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V +Q12051 UniProtKB Helix 96 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V +Q12051 UniProtKB Helix 114 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V +Q12051 UniProtKB Helix 121 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V +Q12051 UniProtKB Turn 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4V +Q12051 UniProtKB Helix 159 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V +Q12051 UniProtKB Helix 171 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V +Q12051 UniProtKB Helix 195 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V +Q12051 UniProtKB Turn 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DH4 +Q12051 UniProtKB Helix 227 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V +Q12051 UniProtKB Helix 236 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V +Q12051 UniProtKB Helix 251 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V +Q12051 UniProtKB Helix 268 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V +Q12051 UniProtKB Helix 284 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E8V +Q12051 UniProtKB Helix 325 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4V +Q12051 UniProtKB Turn 331 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4V +##sequence-region Q06648 1 383 +Q06648 UniProtKB Chain 1 383 . . . ID=PRO_0000212660;Note=GTPase-interacting component 2 +Q06648 UniProtKB Domain 134 147 . . . Note=CRIB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00057 +Q06648 UniProtKB Compositional bias 74 102 . . . Note=Ser-rich +Q06648 UniProtKB Modified residue 254 254 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q06648 UniProtKB Modified residue 258 258 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q06648 UniProtKB Modified residue 337 337 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06648 UniProtKB Modified residue 345 345 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +Q06648 UniProtKB Modified residue 367 367 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region Q03833 1 894 +Q03833 UniProtKB Chain 1 894 . . . ID=PRO_0000046806;Note=Transcriptional activator/repressor GIS1 +Q03833 UniProtKB Domain 12 53 . . . Note=JmjN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00537 +Q03833 UniProtKB Domain 170 324 . . . Note=JmjC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00538 +Q03833 UniProtKB Zinc finger 828 851 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q03833 UniProtKB Zinc finger 857 882 . . . Note=C2H2-type 2%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q03833 UniProtKB Coiled coil 90 110 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03833 UniProtKB Coiled coil 361 385 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03833 UniProtKB Motif 316 332 . . . Note=Bipartite nuclear localization signal +Q03833 UniProtKB Compositional bias 462 806 . . . Note=Asn-rich +Q03833 UniProtKB Modified residue 70 70 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03833 UniProtKB Modified residue 343 343 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03833 UniProtKB Modified residue 690 690 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03833 UniProtKB Modified residue 694 694 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03833 UniProtKB Modified residue 696 696 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03833 UniProtKB Modified residue 734 734 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03833 UniProtKB Modified residue 747 747 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P38196 1 639 +P38196 UniProtKB Chain 1 639 . . . ID=PRO_0000197923;Note=Uridine permease +P38196 UniProtKB Topological domain 1 162 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Transmembrane 163 180 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Topological domain 181 200 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Transmembrane 201 225 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Topological domain 226 259 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Transmembrane 260 276 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Topological domain 277 283 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Transmembrane 284 305 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Topological domain 306 367 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Transmembrane 368 392 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Topological domain 393 416 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Transmembrane 417 435 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Topological domain 436 460 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Transmembrane 461 477 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Topological domain 478 483 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Transmembrane 484 507 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Topological domain 508 537 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Transmembrane 538 562 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Topological domain 563 572 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Transmembrane 573 590 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Topological domain 591 639 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38196 UniProtKB Modified residue 54 54 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38196 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38196 UniProtKB Cross-link 635 635 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P11710 1 512 +P11710 UniProtKB Chain 1 512 . . . ID=PRO_0000087384;Note=Nuclear fusion protein FUS1 +P11710 UniProtKB Transmembrane 72 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P11710 UniProtKB Domain 436 512 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P11710 UniProtKB Region 97 512 . . . Note=Hydrophilic +P11710 UniProtKB Compositional bias 1 71 . . . Note=Ser/Thr-rich +P11710 UniProtKB Modified residue 178 178 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P11710 UniProtKB Modified residue 190 190 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P11710 UniProtKB Modified residue 256 256 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P11710 UniProtKB Modified residue 281 281 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P11710 UniProtKB Modified residue 424 424 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region P40492 1 516 +P40492 UniProtKB Chain 1 516 . . . ID=PRO_0000202970;Note=Protein FYV10 +P40492 UniProtKB Domain 187 245 . . . Note=CTLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00058 +##sequence-region Q99341 1 161 +Q99341 UniProtKB Chain 1 161 . . . ID=PRO_0000299774;Note=Putative uncharacterized protein FYV1 +##sequence-region P38297 1 855 +P38297 UniProtKB Chain 1 855 . . . ID=PRO_0000127682;Note=Mitofusin FZO1 +P38297 UniProtKB Topological domain 1 705 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11266460;Dbxref=PMID:11266460 +P38297 UniProtKB Transmembrane 706 726 . . . Note=Helical%3B Name%3D1 +P38297 UniProtKB Topological domain 727 736 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11266460;Dbxref=PMID:11266460 +P38297 UniProtKB Transmembrane 737 757 . . . Note=Helical%3B Name%3D2 +P38297 UniProtKB Topological domain 758 855 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11266460;Dbxref=PMID:11266460 +P38297 UniProtKB Domain 184 467 . . . Note=Dynamin-type G +P38297 UniProtKB Nucleotide binding 197 202 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8IWA4 +P38297 UniProtKB Nucleotide binding 370 373 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8IWA4 +P38297 UniProtKB Region 91 190 . . . Note=HRN +P38297 UniProtKB Region 484 547 . . . Note=HR1 +P38297 UniProtKB Region 630 843 . . . Note=Required for interaction with UGO1 +P38297 UniProtKB Region 769 831 . . . Note=HR2 +P38297 UniProtKB Coiled coil 798 825 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38297 UniProtKB Binding site 408 408 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8IWA4 +P38297 UniProtKB Cross-link 398 398 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23317502;Dbxref=PMID:23317502 +P38297 UniProtKB Cross-link 464 464 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23317502;Dbxref=PMID:23317502 +P38297 UniProtKB Mutagenesis 172 172 . . . Note=Abolishes fusion function. V->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624808;Dbxref=PMID:16624808 +P38297 UniProtKB Mutagenesis 195 195 . . . Note=Abolishes fusion function. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21385840;Dbxref=PMID:21385840 +P38297 UniProtKB Mutagenesis 196 196 . . . Note=Leads to an unusual intermediate mitochondrial morphology described as disorganized tubules in which mitochondria are tubular%2C distorted%2C less branched%2C and poorly distributed throughout the cell. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19812251;Dbxref=PMID:19812251 +P38297 UniProtKB Mutagenesis 197 197 . . . Note=Abolishes fusion function. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21385840;Dbxref=PMID:21385840 +P38297 UniProtKB Mutagenesis 200 200 . . . Note=Abolishes fusion function%2C MDM30-binding and MDM30-dependent ubiquitination. No effect on localization or interaction with UGO1. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16624808,ECO:0000269|PubMed:21385840,ECO:0000269|PubMed:21502136,ECO:0000269|PubMed:9786948;Dbxref=PMID:16624808,PMID:21385840,PMID:21502136,PMID:9786948 +P38297 UniProtKB Mutagenesis 201 201 . . . Note=Abolishes fusion function%2C MDM30-binding and MDM30-dependent ubiquitination%2C but not localization to mitochondrial outer membrane. S->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16624808,ECO:0000269|PubMed:21385840,ECO:0000269|PubMed:21502136,ECO:0000269|PubMed:9786948;Dbxref=PMID:16624808,PMID:21385840,PMID:21502136,PMID:9786948 +P38297 UniProtKB Mutagenesis 221 221 . . . Note=Abolishes fusion function%2C MDM30-binding and MDM30-dependent ubiquitination%2C but not localization to mitochondrial outer membrane. T->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16624808,ECO:0000269|PubMed:21385840,ECO:0000269|PubMed:21502136,ECO:0000269|PubMed:9786948;Dbxref=PMID:16624808,PMID:21385840,PMID:21502136,PMID:9786948 +P38297 UniProtKB Mutagenesis 320 320 . . . Note=Loss of mitochondrial fusion. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21385840;Dbxref=PMID:21385840 +P38297 UniProtKB Mutagenesis 327 327 . . . Note=Impairs GTP Hydrolysis and abolishes fusion function. V->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19812251;Dbxref=PMID:19812251 +P38297 UniProtKB Mutagenesis 371 371 . . . Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9786948;Dbxref=PMID:9786948 +P38297 UniProtKB Mutagenesis 398 398 . . . Note=Leads to accelerated proteolysis. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23317502;Dbxref=PMID:23317502 +P38297 UniProtKB Mutagenesis 464 464 . . . Note=Abolishes fusion function. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23317502;Dbxref=PMID:23317502 +P38297 UniProtKB Mutagenesis 490 490 . . . Note=Abolishes fusion function. Y->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624808;Dbxref=PMID:16624808 +P38297 UniProtKB Mutagenesis 501 501 . . . Note=Abolishes fusion function%3B when associated with Ala-504. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624808;Dbxref=PMID:16624808 +P38297 UniProtKB Mutagenesis 504 504 . . . Note=Abolishes fusion function%3B when associated with Ala-501. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624808;Dbxref=PMID:16624808 +P38297 UniProtKB Mutagenesis 518 518 . . . Note=Abolishes fusion function. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624808;Dbxref=PMID:16624808 +P38297 UniProtKB Mutagenesis 538 538 . . . Note=Abolishes fusion function. K->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624808;Dbxref=PMID:16624808 +P38297 UniProtKB Mutagenesis 769 769 . . . Note=Abolishes fusion function. Y->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624808;Dbxref=PMID:16624808 +P38297 UniProtKB Mutagenesis 773 773 . . . Note=Abolishes fusion function. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624808;Dbxref=PMID:16624808 +P38297 UniProtKB Mutagenesis 819 819 . . . Note=Abolishes fusion function. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624808;Dbxref=PMID:16624808 +##sequence-region P53260 1 183 +P53260 UniProtKB Chain 1 183 . . . ID=PRO_0000202811;Note=Glutamyl-tRNA(Gln) amidotransferase subunit F%2C mitochondrial +P53260 UniProtKB Sequence conflict 9 9 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53260 UniProtKB Helix 39 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P53260 UniProtKB Helix 53 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P53260 UniProtKB Helix 71 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P53260 UniProtKB Helix 90 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P53260 UniProtKB Helix 105 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P53260 UniProtKB Helix 135 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P53260 UniProtKB Helix 149 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P53260 UniProtKB Turn 160 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +P53260 UniProtKB Beta strand 171 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +##sequence-region P18852 1 110 +P18852 UniProtKB Chain 1 107 . . . ID=PRO_0000194812;Note=Guanine nucleotide-binding protein subunit gamma +P18852 UniProtKB Propeptide 108 110 . . . ID=PRO_0000396775;Note=Removed in mature form +P18852 UniProtKB Compositional bias 11 22 . . . Note=Gln-rich +P18852 UniProtKB Compositional bias 96 104 . . . Note=Asn/Ser-rich +P18852 UniProtKB Modified residue 107 107 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523659;Dbxref=PMID:10523659 +P18852 UniProtKB Lipidation 106 106 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10523659,ECO:0000269|PubMed:10712512;Dbxref=PMID:10523659,PMID:10712512 +P18852 UniProtKB Lipidation 107 107 . . . Note=S-farnesyl cysteine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10523659,ECO:0000269|PubMed:10712512;Dbxref=PMID:10523659,PMID:10712512 +P18852 UniProtKB Mutagenesis 106 106 . . . Note=Partial loss of function. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523659;Dbxref=PMID:10523659 +P18852 UniProtKB Mutagenesis 107 107 . . . Note=Loss of function. C->X;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7982577;Dbxref=PMID:7982577 +##sequence-region P38301 1 280 +P38301 UniProtKB Chain 1 280 . . . ID=PRO_0000212467;Note=GCR1-dependent translation factor 1 +P38301 UniProtKB Topological domain 1 3 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38301 UniProtKB Transmembrane 4 24 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38301 UniProtKB Topological domain 25 45 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38301 UniProtKB Transmembrane 46 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38301 UniProtKB Topological domain 67 71 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38301 UniProtKB Transmembrane 72 92 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38301 UniProtKB Topological domain 93 104 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38301 UniProtKB Transmembrane 105 125 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38301 UniProtKB Topological domain 126 183 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38301 UniProtKB Transmembrane 184 204 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38301 UniProtKB Topological domain 205 222 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38301 UniProtKB Transmembrane 223 243 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38301 UniProtKB Topological domain 244 255 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38301 UniProtKB Transmembrane 256 276 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38301 UniProtKB Topological domain 277 280 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38301 UniProtKB Mutagenesis 71 71 . . . Note=Loss of function in calcium homeostasis. R->C%2CH;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23575229;Dbxref=PMID:23575229 +P38301 UniProtKB Sequence conflict 158 158 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47102 1 1408 +P47102 UniProtKB Chain 1 1408 . . . ID=PRO_0000120212;Note=ARF guanine-nucleotide exchange factor 1 +P47102 UniProtKB Domain 552 706 . . . Note=SEC7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00189 +P47102 UniProtKB Modified residue 49 49 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P39993 +P47102 UniProtKB Mutagenesis 862 862 . . . Note=Abolishes interaction with GMH1. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12808035;Dbxref=PMID:12808035 +P47102 UniProtKB Helix 540 554 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0 +P47102 UniProtKB Helix 556 565 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0 +P47102 UniProtKB Beta strand 568 570 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0 +P47102 UniProtKB Helix 574 584 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0 +P47102 UniProtKB Helix 585 587 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0 +P47102 UniProtKB Helix 590 597 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0 +P47102 UniProtKB Helix 600 602 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0 +P47102 UniProtKB Helix 603 610 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0 +P47102 UniProtKB Helix 620 627 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0 +P47102 UniProtKB Helix 637 653 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0 +P47102 UniProtKB Helix 687 705 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0 +P47102 UniProtKB Helix 715 721 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0 +P47102 UniProtKB Turn 722 725 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0 +P47102 UniProtKB Helix 733 745 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0 +P47102 UniProtKB Helix 751 753 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RE0 +##sequence-region P38988 1 300 +P38988 UniProtKB Chain 1 300 . . . ID=PRO_0000090687;Note=Mitochondrial GTP/GDP carrier protein 1 +P38988 UniProtKB Transmembrane 14 34 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38988 UniProtKB Transmembrane 85 101 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38988 UniProtKB Transmembrane 122 142 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38988 UniProtKB Transmembrane 173 189 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38988 UniProtKB Transmembrane 214 234 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38988 UniProtKB Transmembrane 268 285 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38988 UniProtKB Repeat 8 108 . . . Note=Solcar 1 +P38988 UniProtKB Repeat 117 198 . . . Note=Solcar 2 +P38988 UniProtKB Repeat 208 293 . . . Note=Solcar 3 +##sequence-region Q04233 1 774 +Q04233 UniProtKB Chain 1 774 . . . ID=PRO_0000087498;Note=Protein GIS4 +Q04233 UniProtKB Compositional bias 147 152 . . . Note=Poly-Asn +Q04233 UniProtKB Compositional bias 183 203 . . . Note=Thr-rich +Q04233 UniProtKB Compositional bias 329 358 . . . Note=Ser-rich +Q04233 UniProtKB Compositional bias 340 349 . . . Note=Poly-Ser +Q04233 UniProtKB Compositional bias 353 358 . . . Note=Poly-Ser +Q04233 UniProtKB Compositional bias 576 589 . . . Note=Asp-rich +Q04233 UniProtKB Modified residue 165 165 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04233 UniProtKB Modified residue 304 304 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04233 UniProtKB Modified residue 616 616 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04233 UniProtKB Modified residue 622 622 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q04233 UniProtKB Modified residue 707 707 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q04233 UniProtKB Modified residue 720 720 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region Q07540 1 174 +Q07540 UniProtKB Transit peptide 1 21 . . . Note=Mitochondrion;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q07540 UniProtKB Chain 22 174 . . . ID=PRO_0000010135;Note=Frataxin homolog intermediate form +Q07540 UniProtKB Chain 52 174 . . . ID=PRO_0000010136;Note=Frataxin homolog%2C mitochondrial +Q07540 UniProtKB Mutagenesis 79 79 . . . Note=Nearly abolishes ferroxidase activity%2C slows down oligomerization%2C impairs resistance to iron-catalyzed oxidative stress%2C no effect on Fe(2+) delivery and cell growth%3B when associated with A-82. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16371422;Dbxref=PMID:16371422 +Q07540 UniProtKB Mutagenesis 82 82 . . . Note=Nearly abolishes ferroxidase activity%2C slows down oligomerization%2C impairs resistance to iron-catalyzed oxidative stress%2C no effect on Fe(2+) delivery and cell growth%3B when associated with A-79. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16371422;Dbxref=PMID:16371422 +Q07540 UniProtKB Mutagenesis 93 93 . . . Note=Impairs oligomerization and iron mineralization. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16371422;Dbxref=PMID:16371422 +Q07540 UniProtKB Mutagenesis 93 93 . . . Note=Impairs resistance to iron-catalyzed oxidative stress%2C no effect on Fe(2+) delivery and cell growth%3B when associated with A-97 and A-103. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16371422;Dbxref=PMID:16371422 +Q07540 UniProtKB Mutagenesis 97 97 . . . Note=Impairs resistance to iron-catalyzed oxidative stress%2C no effect on Fe(2+) delivery and cell growth%3B when associated with A-93 and A-103. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16371422;Dbxref=PMID:16371422 +Q07540 UniProtKB Mutagenesis 103 103 . . . Note=Impairs resistance to iron-catalyzed oxidative stress%2C no effect on Fe(2+) delivery and cell growth%3B when associated with A-93 and A-97. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16371422;Dbxref=PMID:16371422 +Q07540 UniProtKB Mutagenesis 122 124 . . . Note=Impairs cell growth%2C lowers activity of motochondrial iron-sulfur cluster-containing enzymes%2C no effect on iron binding and oligomerization. NKQ->ATA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18319250;Dbxref=PMID:18319250 +Q07540 UniProtKB Mutagenesis 129 129 . . . Note=Impairs cell growth and lowers aconitase activity. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19884169;Dbxref=PMID:19884169 +Q07540 UniProtKB Mutagenesis 130 130 . . . Note=Impairs cell growth and lowers aconitase activity. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19884169;Dbxref=PMID:19884169 +Q07540 UniProtKB Mutagenesis 131 131 . . . Note=Impairs cell growth%2C lowers aconitase activity and strongly decreases interaction with ISU1. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19884169;Dbxref=PMID:19884169 +Q07540 UniProtKB Mutagenesis 131 131 . . . Note=Lowers aconitase activity and no effexct on interaction with ISU1. W->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19884169;Dbxref=PMID:19884169 +Q07540 UniProtKB Mutagenesis 141 141 . . . Note=Impairs cell growth and lowers aconitase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19884169;Dbxref=PMID:19884169 +Q07540 UniProtKB Turn 64 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ +Q07540 UniProtKB Helix 76 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ +Q07540 UniProtKB Turn 89 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ +Q07540 UniProtKB Beta strand 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ +Q07540 UniProtKB Beta strand 96 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FQL +Q07540 UniProtKB Beta strand 101 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ +Q07540 UniProtKB Beta strand 106 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ +Q07540 UniProtKB Turn 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ +Q07540 UniProtKB Beta strand 119 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ +Q07540 UniProtKB Beta strand 126 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ +Q07540 UniProtKB Beta strand 131 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ +Q07540 UniProtKB Turn 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ +Q07540 UniProtKB Beta strand 138 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ +Q07540 UniProtKB Turn 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ +Q07540 UniProtKB Helix 158 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OEQ +##sequence-region P32614 1 470 +P32614 UniProtKB Chain 1 470 . . . ID=PRO_0000158669;Note=Fumarate reductase 1 +P32614 UniProtKB Nucleotide binding 6 20 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32614 UniProtKB Active site 249 249 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32614 UniProtKB Active site 272 272 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32614 UniProtKB Modified residue 66 66 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P32614 UniProtKB Sequence conflict 285 285 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32614 UniProtKB Sequence conflict 440 440 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36088 1 180 +P36088 UniProtKB Chain 1 180 . . . ID=PRO_0000171552;Note=Free methionine-R-sulfoxide reductase +P36088 UniProtKB Domain 99 177 . . . Note=GAF +P36088 UniProtKB Mutagenesis 91 91 . . . Note=Dramatic reduction in enzyme activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19049972;Dbxref=PMID:19049972 +P36088 UniProtKB Mutagenesis 101 101 . . . Note=Dramatic reduction in enzyme activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19049972;Dbxref=PMID:19049972 +P36088 UniProtKB Mutagenesis 125 125 . . . Note=Dramatic reduction in enzyme activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19049972;Dbxref=PMID:19049972 +P36088 UniProtKB Helix 9 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M +P36088 UniProtKB Helix 21 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M +P36088 UniProtKB Helix 42 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M +P36088 UniProtKB Beta strand 64 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M +P36088 UniProtKB Beta strand 74 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M +P36088 UniProtKB Beta strand 79 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M +P36088 UniProtKB Beta strand 92 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M +P36088 UniProtKB Helix 99 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M +P36088 UniProtKB Beta strand 111 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M +P36088 UniProtKB Helix 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M +P36088 UniProtKB Beta strand 131 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M +P36088 UniProtKB Beta strand 144 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M +P36088 UniProtKB Helix 160 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F5M +##sequence-region P40088 1 404 +P40088 UniProtKB Chain 1 404 . . . ID=PRO_0000159649;Note=Plasma membrane iron permease +P40088 UniProtKB Transmembrane 8 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40088 UniProtKB Transmembrane 51 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40088 UniProtKB Transmembrane 87 107 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40088 UniProtKB Transmembrane 147 167 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40088 UniProtKB Transmembrane 183 203 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40088 UniProtKB Transmembrane 207 227 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40088 UniProtKB Transmembrane 294 314 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P18411 1 198 +P18411 UniProtKB Chain 1 198 . . . ID=PRO_0000202412;Note=Protein FUN14 +P18411 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18411 UniProtKB Transmembrane 112 132 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18411 UniProtKB Transmembrane 172 192 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P31381 1 517 +P31381 UniProtKB Chain 1 517 . . . ID=PRO_0000209346;Note=Nucleoside transporter FUN26 +P31381 UniProtKB Transmembrane 76 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31381 UniProtKB Transmembrane 116 136 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31381 UniProtKB Transmembrane 151 171 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31381 UniProtKB Transmembrane 174 194 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31381 UniProtKB Transmembrane 214 234 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31381 UniProtKB Transmembrane 243 263 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31381 UniProtKB Transmembrane 344 364 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31381 UniProtKB Transmembrane 367 387 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31381 UniProtKB Transmembrane 411 431 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31381 UniProtKB Transmembrane 446 466 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31381 UniProtKB Transmembrane 492 512 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31381 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P31381 UniProtKB Modified residue 58 58 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P19145 1 602 +P19145 UniProtKB Chain 1 602 . . . ID=PRO_0000054151;Note=General amino-acid permease GAP1 +P19145 UniProtKB Topological domain 1 95 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Transmembrane 96 116 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Topological domain 117 121 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Transmembrane 122 142 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Topological domain 143 165 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Transmembrane 166 185 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Topological domain 186 204 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Transmembrane 205 224 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Topological domain 225 237 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Transmembrane 238 256 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Topological domain 257 280 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Transmembrane 281 298 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Topological domain 299 321 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Transmembrane 322 342 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Topological domain 343 376 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Transmembrane 377 396 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Topological domain 397 421 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Transmembrane 422 442 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Topological domain 443 451 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Transmembrane 452 472 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Topological domain 473 491 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Transmembrane 492 510 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Topological domain 511 529 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Transmembrane 530 548 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Topological domain 549 602 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19145 UniProtKB Cross-link 76 76 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12872131,ECO:0000269|PubMed:14557538;Dbxref=PMID:12872131,PMID:14557538 +P19145 UniProtKB Mutagenesis 297 297 . . . Note=Impairs basic amino-acids transport and regulation by these amino-acids. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21471002;Dbxref=PMID:21471002 +P19145 UniProtKB Sequence conflict 122 122 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19145 UniProtKB Sequence conflict 189 189 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19145 UniProtKB Sequence conflict 338 338 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19145 UniProtKB Sequence conflict 518 518 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P28007 1 205 +P28007 UniProtKB Chain 1 205 . . . ID=PRO_0000208566;Note=H/ACA ribonucleoprotein complex subunit 1 +P28007 UniProtKB Region 4 21 . . . Note=RGG-box 1 +P28007 UniProtKB Region 147 205 . . . Note=RGG-box 2 +P28007 UniProtKB Modified residue 4 4 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P28007 UniProtKB Modified residue 8 8 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P28007 UniProtKB Modified residue 11 11 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P28007 UniProtKB Modified residue 15 15 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P28007 UniProtKB Modified residue 19 19 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P28007 UniProtKB Modified residue 147 147 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P28007 UniProtKB Modified residue 154 154 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P28007 UniProtKB Modified residue 158 158 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P28007 UniProtKB Modified residue 162 162 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P28007 UniProtKB Modified residue 165 165 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P28007 UniProtKB Modified residue 171 171 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P28007 UniProtKB Modified residue 174 174 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P28007 UniProtKB Modified residue 180 180 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P28007 UniProtKB Modified residue 184 184 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P28007 UniProtKB Modified residue 189 189 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P28007 UniProtKB Modified residue 193 193 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P28007 UniProtKB Modified residue 197 197 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P28007 UniProtKB Modified residue 201 201 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P28007 UniProtKB Cross-link 77 77 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P28007 UniProtKB Beta strand 37 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P28007 UniProtKB Beta strand 50 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P28007 UniProtKB Beta strand 57 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P28007 UniProtKB Beta strand 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P28007 UniProtKB Beta strand 74 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P28007 UniProtKB Beta strand 89 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P28007 UniProtKB Helix 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P28007 UniProtKB Beta strand 108 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P28007 UniProtKB Helix 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +P28007 UniProtKB Helix 119 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +##sequence-region Q03655 1 524 +Q03655 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03655 UniProtKB Chain 22 498 . . . ID=PRO_0000010477;Note=Probable 1%2C3-beta-glucanosyltransferase GAS3 +Q03655 UniProtKB Propeptide 499 524 . . . ID=PRO_0000010478;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03655 UniProtKB Compositional bias 458 496 . . . Note=Ser-rich +Q03655 UniProtKB Active site 169 169 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03655 UniProtKB Active site 283 283 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03655 UniProtKB Binding site 96 96 . . . Note=Donor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q03655 UniProtKB Binding site 168 168 . . . Note=Donor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q03655 UniProtKB Binding site 169 169 . . . Note=Acceptor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q03655 UniProtKB Binding site 212 212 . . . Note=Acceptor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q03655 UniProtKB Binding site 217 217 . . . Note=Acceptor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q03655 UniProtKB Binding site 315 315 . . . Note=Donor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q03655 UniProtKB Lipidation 498 498 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03655 UniProtKB Glycosylation 201 201 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03655 UniProtKB Glycosylation 269 269 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03655 UniProtKB Glycosylation 350 350 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03655 UniProtKB Glycosylation 385 385 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03655 UniProtKB Glycosylation 404 404 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03655 UniProtKB Glycosylation 422 422 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03655 UniProtKB Disulfide bond 78 107 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q03655 UniProtKB Disulfide bond 226 369 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q03655 UniProtKB Disulfide bond 254 286 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +##sequence-region P40209 1 560 +P40209 UniProtKB Chain 1 560 . . . ID=PRO_0000083485;Note=Protein GAT2 +P40209 UniProtKB Zinc finger 472 497 . . . Note=GATA-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00094 +##sequence-region P39726 1 170 +P39726 UniProtKB Transit peptide 1 47 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39726 UniProtKB Chain 48 170 . . . ID=PRO_0000010739;Note=Glycine cleavage system H protein%2C mitochondrial +P39726 UniProtKB Domain 61 143 . . . Note=Lipoyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066 +P39726 UniProtKB Modified residue 102 102 . . . Note=N6-lipoyllysine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250,ECO:0000255|PROSITE-ProRule:PRU01066 +P39726 UniProtKB Sequence conflict 14 14 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39726 UniProtKB Sequence conflict 73 73 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39726 UniProtKB Sequence conflict 90 90 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08271 1 471 +Q08271 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08271 UniProtKB Chain 22 447 . . . ID=PRO_0000010479;Note=1%2C3-beta-glucanosyltransferase GAS4 +Q08271 UniProtKB Propeptide 448 471 . . . ID=PRO_0000010480;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08271 UniProtKB Active site 161 161 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08271 UniProtKB Active site 266 266 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08271 UniProtKB Binding site 88 88 . . . Note=Donor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q08271 UniProtKB Binding site 160 160 . . . Note=Donor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q08271 UniProtKB Binding site 161 161 . . . Note=Acceptor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q08271 UniProtKB Binding site 203 203 . . . Note=Acceptor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q08271 UniProtKB Binding site 208 208 . . . Note=Acceptor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q08271 UniProtKB Binding site 298 298 . . . Note=Donor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q08271 UniProtKB Lipidation 447 447 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08271 UniProtKB Glycosylation 151 151 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08271 UniProtKB Glycosylation 398 398 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08271 UniProtKB Disulfide bond 70 99 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q08271 UniProtKB Disulfide bond 217 354 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q08271 UniProtKB Disulfide bond 238 269 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +##sequence-region Q08193 1 484 +Q08193 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08193 UniProtKB Chain 20 462 . . . ID=PRO_0000010481;Note=1%2C3-beta-glucanosyltransferase GAS5 +Q08193 UniProtKB Propeptide 463 484 . . . ID=PRO_0000010482;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08193 UniProtKB Compositional bias 395 403 . . . Note=Asp/Glu-rich (highly acidic) +Q08193 UniProtKB Compositional bias 405 460 . . . Note=Ser-rich +Q08193 UniProtKB Compositional bias 405 427 . . . Note=Poly-Ser +Q08193 UniProtKB Compositional bias 432 439 . . . Note=Poly-Ser +Q08193 UniProtKB Active site 160 160 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08193 UniProtKB Active site 262 262 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08193 UniProtKB Binding site 89 89 . . . Note=Donor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q08193 UniProtKB Binding site 159 159 . . . Note=Donor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q08193 UniProtKB Binding site 160 160 . . . Note=Acceptor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q08193 UniProtKB Binding site 201 201 . . . Note=Acceptor substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q08193 UniProtKB Binding site 206 206 . . . Note=Acceptor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q08193 UniProtKB Binding site 295 295 . . . Note=Donor substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q08193 UniProtKB Lipidation 462 462 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08193 UniProtKB Glycosylation 24 24 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08193 UniProtKB Glycosylation 60 60 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08193 UniProtKB Glycosylation 166 166 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08193 UniProtKB Glycosylation 299 299 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08193 UniProtKB Glycosylation 344 344 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08193 UniProtKB Glycosylation 359 359 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08193 UniProtKB Disulfide bond 71 100 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q08193 UniProtKB Disulfide bond 215 348 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +Q08193 UniProtKB Disulfide bond 234 265 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06135 +##sequence-region Q03557 1 464 +Q03557 UniProtKB Chain 1 464 . . . ID=PRO_0000001205;Note=Glutamyl-tRNA(Gln) amidotransferase subunit A%2C mitochondrial +Q03557 UniProtKB Active site 52 52 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03150 +Q03557 UniProtKB Active site 130 130 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03150 +Q03557 UniProtKB Active site 154 154 . . . Note=Acyl-ester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03150 +Q03557 UniProtKB Helix 7 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Beta strand 24 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Turn 43 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Beta strand 48 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Beta strand 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 79 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Beta strand 90 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 99 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Beta strand 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Beta strand 129 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 132 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Beta strand 142 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 156 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Beta strand 164 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Turn 184 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Beta strand 188 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 196 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 219 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Beta strand 236 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 241 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 252 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Beta strand 269 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 276 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 281 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Turn 297 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Beta strand 301 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Beta strand 313 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 321 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 329 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 344 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Beta strand 369 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Turn 374 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Beta strand 384 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 400 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 411 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0I +Q03557 UniProtKB Turn 417 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 422 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Beta strand 431 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Beta strand 443 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +Q03557 UniProtKB Helix 453 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0H +##sequence-region P38011 1 319 +P38011 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.3;Dbxref=PMID:22814378 +P38011 UniProtKB Chain 2 319 . . . ID=PRO_0000127758;Note=Guanine nucleotide-binding protein subunit beta-like protein +P38011 UniProtKB Repeat 15 55 . . . Note=WD 1 +P38011 UniProtKB Repeat 63 102 . . . Note=WD 2 +P38011 UniProtKB Repeat 105 145 . . . Note=WD 3 +P38011 UniProtKB Repeat 147 191 . . . Note=WD 4 +P38011 UniProtKB Repeat 194 233 . . . Note=WD 5 +P38011 UniProtKB Repeat 235 275 . . . Note=WD 6 +P38011 UniProtKB Repeat 284 319 . . . Note=WD 7 +P38011 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.3;Dbxref=PMID:22814378 +P38011 UniProtKB Modified residue 96 96 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38011 UniProtKB Modified residue 168 168 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38011 UniProtKB Cross-link 46 46 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38011 UniProtKB Cross-link 53 53 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38011 UniProtKB Cross-link 107 107 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38011 UniProtKB Cross-link 137 137 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38011 UniProtKB Cross-link 161 161 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38011 UniProtKB Beta strand 5 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 20 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 32 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 40 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 53 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 68 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 77 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 87 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Turn 94 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 98 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 110 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 121 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 131 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 140 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 151 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 168 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 178 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Turn 183 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 187 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 199 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 208 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Helix 216 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RFH +P38011 UniProtKB Beta strand 219 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Turn 225 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 229 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 240 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 247 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 259 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Turn 265 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 269 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Helix 283 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 289 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 298 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +P38011 UniProtKB Beta strand 310 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FRX +##sequence-region P07261 1 785 +P07261 UniProtKB Chain 1 785 . . . ID=PRO_0000087445;Note=Glycolytic genes transcriptional activator GCR1 +P07261 UniProtKB Region 267 299 . . . Note=Leucine-zipper +P07261 UniProtKB Region 632 785 . . . Note=DNA-binding +P07261 UniProtKB Compositional bias 412 618 . . . Note=Pro/Ser-rich +P07261 UniProtKB Modified residue 447 447 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07261 UniProtKB Modified residue 449 449 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P07261 UniProtKB Modified residue 482 482 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07261 UniProtKB Modified residue 489 489 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07261 UniProtKB Modified residue 538 538 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07261 UniProtKB Sequence conflict 399 399 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P14065 1 312 +P14065 UniProtKB Chain 1 312 . . . ID=PRO_0000124611;Note=Glycerol 2-dehydrogenase (NADP(+)) +P14065 UniProtKB Nucleotide binding 220 274 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14065 UniProtKB Active site 56 56 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14065 UniProtKB Binding site 112 112 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14065 UniProtKB Site 81 81 . . . Note=Lowers pKa of active site Tyr;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14065 UniProtKB Modified residue 306 306 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14065 UniProtKB Mutagenesis 29 29 . . . Note=Decreases catalytic activity. Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23770562;Dbxref=PMID:23770562 +P14065 UniProtKB Mutagenesis 56 56 . . . Note=Loss of catalytic activity. Y->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17140678;Dbxref=PMID:17140678 +P14065 UniProtKB Mutagenesis 264 264 . . . Note=Decreases catalytic activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23770562;Dbxref=PMID:23770562 +P14065 UniProtKB Mutagenesis 267 267 . . . Note=Decreases catalytic activity. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23770562;Dbxref=PMID:23770562 +P14065 UniProtKB Mutagenesis 270 270 . . . Note=Decreases catalytic activity. R->H%2CY%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23770562;Dbxref=PMID:23770562 +##sequence-region P32775 1 704 +P32775 UniProtKB Chain 1 704 . . . ID=PRO_0000188786;Note=1%2C4-alpha-glucan-branching enzyme +P32775 UniProtKB Active site 356 356 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32775 UniProtKB Active site 417 417 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32775 UniProtKB Modified residue 190 190 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32775 UniProtKB Sequence conflict 564 564 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P17695 1 143 +P17695 UniProtKB Transit peptide 1 35 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2189409;Dbxref=PMID:2189409 +P17695 UniProtKB Chain 36 143 . . . ID=PRO_0000141612;Note=Glutaredoxin-2%2C mitochondrial +P17695 UniProtKB Domain 41 143 . . . Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686 +P17695 UniProtKB Region 58 63 . . . Note=Glutathione binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18992757;Dbxref=PMID:18992757 +P17695 UniProtKB Region 122 123 . . . Note=Glutathione binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18992757;Dbxref=PMID:18992757 +P17695 UniProtKB Binding site 109 109 . . . Note=Glutathione%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18992757;Dbxref=PMID:18992757 +P17695 UniProtKB Modified residue 37 37 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P17695 UniProtKB Modified residue 61 61 . . . Note=S-glutathionyl cysteine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18992757;Dbxref=PMID:18992757 +P17695 UniProtKB Modified residue 91 91 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P17695 UniProtKB Disulfide bond 61 64 . . . Note=Redox-active%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20417731;Dbxref=PMID:20417731 +P17695 UniProtKB Mutagenesis 64 64 . . . Note=Leads to 30 percent decreased oxidoreductase activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18992757;Dbxref=PMID:18992757 +P17695 UniProtKB Mutagenesis 123 123 . . . Note=Leads to decreased oxidoreductase activity. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20417731;Dbxref=PMID:20417731 +P17695 UniProtKB Helix 38 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG +P17695 UniProtKB Beta strand 51 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG +P17695 UniProtKB Helix 62 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG +P17695 UniProtKB Helix 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG +P17695 UniProtKB Beta strand 82 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG +P17695 UniProtKB Helix 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG +P17695 UniProtKB Helix 93 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG +P17695 UniProtKB Beta strand 111 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG +P17695 UniProtKB Beta strand 117 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG +P17695 UniProtKB Helix 122 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG +P17695 UniProtKB Helix 133 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG +P17695 UniProtKB Turn 138 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CTG +##sequence-region P37303 1 387 +P37303 UniProtKB Chain 1 387 . . . ID=PRO_0000121572;Note=Low specificity L-threonine aldolase +P37303 UniProtKB Modified residue 213 213 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P37303 UniProtKB Modified residue 367 367 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P37303 UniProtKB Modified residue 369 369 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P37303 UniProtKB Modified residue 370 370 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P37303 UniProtKB Cross-link 228 228 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P37303 UniProtKB Sequence conflict 253 253 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32191 1 649 +P32191 UniProtKB Nucleotide binding 69 97 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32191 UniProtKB Sequence conflict 1 51 . . . Note=MFSVTRRRAAGAAAAMATATGTLYWMTSQGDRPLVHNDPSYMVQFPTAAPP->MTRATWCNSPPPLHR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32191 UniProtKB Sequence conflict 63 63 . . . Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32191 UniProtKB Sequence conflict 182 182 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32191 UniProtKB Sequence conflict 234 234 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32191 UniProtKB Sequence conflict 243 243 . . . Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32191 UniProtKB Sequence conflict 249 249 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32191 UniProtKB Sequence conflict 320 320 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32191 UniProtKB Sequence conflict 342 342 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32191 UniProtKB Sequence conflict 645 646 . . . Note=KT->QGR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38875 1 610 +P38875 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38875 UniProtKB Chain 20 610 . . . ID=PRO_0000024110;Note=GPI transamidase component GPI16 +P38875 UniProtKB Topological domain 20 551 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38875 UniProtKB Transmembrane 552 572 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38875 UniProtKB Topological domain 573 610 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38875 UniProtKB Glycosylation 184 184 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11598210;Dbxref=PMID:11598210 +P38875 UniProtKB Disulfide bond 202 202 . . . Note=Interchain (with C-85 in GPI8);Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P46961 1 280 +P46961 UniProtKB Chain 1 280 . . . ID=PRO_0000087558;Note=Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit +P46961 UniProtKB Topological domain 1 53 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46961 UniProtKB Transmembrane 54 74 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46961 UniProtKB Topological domain 75 75 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46961 UniProtKB Transmembrane 76 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46961 UniProtKB Topological domain 97 108 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46961 UniProtKB Transmembrane 109 129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46961 UniProtKB Topological domain 130 135 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46961 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46961 UniProtKB Topological domain 157 189 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46961 UniProtKB Transmembrane 190 210 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46961 UniProtKB Topological domain 211 220 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46961 UniProtKB Transmembrane 221 241 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46961 UniProtKB Topological domain 242 280 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46961 UniProtKB Sequence conflict 48 48 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46961 UniProtKB Sequence conflict 239 280 . . . Note=IFFASVFYITVLPKWFIYWKINYHKRDNDLLSTWDARTPILD->FSLLQYFILQFYLSGSSTGKSIIINGITIY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40106 1 250 +P40106 UniProtKB Chain 1 250 . . . ID=PRO_0000087561;Note=Glycerol-1-phosphate phosphohydrolase 2 +P40106 UniProtKB Active site 18 18 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40106 UniProtKB Active site 20 20 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40106 UniProtKB Metal binding 18 18 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40106 UniProtKB Metal binding 20 20 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40106 UniProtKB Metal binding 179 179 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40106 UniProtKB Modified residue 90 90 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41277 +P40106 UniProtKB Cross-link 64 64 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41277 +P40106 UniProtKB Cross-link 144 144 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41277 +##sequence-region P35197 1 352 +P35197 UniProtKB Chain 1 352 . . . ID=PRO_0000074224;Note=ADP-ribosylation factor GTPase-activating protein GCS1 +P35197 UniProtKB Domain 11 127 . . . Note=Arf-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288 +P35197 UniProtKB Zinc finger 26 49 . . . Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288 +P35197 UniProtKB Modified residue 151 151 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35197 UniProtKB Modified residue 157 157 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P35197 UniProtKB Modified residue 161 161 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P35197 UniProtKB Modified residue 168 168 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35197 UniProtKB Modified residue 170 170 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35197 UniProtKB Modified residue 260 260 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P35197 UniProtKB Natural variant 27 27 . . . Note=M->I +P35197 UniProtKB Mutagenesis 29 29 . . . Note=In GCS1-1%3B severely affect the function. C->Y +##sequence-region Q12393 1 293 +Q12393 UniProtKB Chain 1 293 . . . ID=PRO_0000247349;Note=Genetic interactor of prohibitin 5%2C mitochondrial +##sequence-region P25596 1 615 +P25596 UniProtKB Chain 1 615 . . . ID=PRO_0000202557;Note=Glutathione exchanger 1 +P25596 UniProtKB Topological domain 1 58 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Transmembrane 59 79 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Topological domain 80 120 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Transmembrane 121 141 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Topological domain 142 152 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Transmembrane 153 173 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Topological domain 174 186 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Transmembrane 187 207 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Topological domain 208 216 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Transmembrane 217 237 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Topological domain 238 275 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Transmembrane 276 296 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Topological domain 297 306 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Transmembrane 307 327 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Topological domain 328 343 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Transmembrane 344 364 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Topological domain 365 383 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Transmembrane 384 404 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Topological domain 405 407 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Transmembrane 408 428 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Topological domain 429 440 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Transmembrane 441 461 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Topological domain 462 547 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Transmembrane 548 568 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25596 UniProtKB Topological domain 569 615 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03016 1 1276 +Q03016 UniProtKB Chain 1 1276 . . . ID=PRO_0000238623;Note=GLC7-interacting protein 3 +Q03016 UniProtKB Compositional bias 28 214 . . . Note=Ser-rich +Q03016 UniProtKB Modified residue 68 68 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q03016 UniProtKB Modified residue 99 99 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03016 UniProtKB Modified residue 103 103 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03016 UniProtKB Modified residue 143 143 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q03016 UniProtKB Modified residue 260 260 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q03016 UniProtKB Modified residue 264 264 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q03016 UniProtKB Modified residue 269 269 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region Q05926 1 109 +Q05926 UniProtKB Chain 1 109 . . . ID=PRO_0000268192;Note=Glutaredoxin-8 +Q05926 UniProtKB Domain 5 109 . . . Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686 +Q05926 UniProtKB Disulfide bond 25 28 . . . Note=Redox-active;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q05926 UniProtKB Mutagenesis 25 25 . . . Note=Impairs activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19166312;Dbxref=PMID:19166312 +Q05926 UniProtKB Mutagenesis 28 28 . . . Note=Impairs activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19166312;Dbxref=PMID:19166312 +Q05926 UniProtKB Helix 5 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80 +Q05926 UniProtKB Beta strand 17 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80 +Q05926 UniProtKB Helix 28 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80 +Q05926 UniProtKB Turn 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80 +Q05926 UniProtKB Beta strand 44 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80 +Q05926 UniProtKB Helix 54 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80 +Q05926 UniProtKB Beta strand 72 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80 +Q05926 UniProtKB Beta strand 81 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80 +Q05926 UniProtKB Helix 86 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80 +Q05926 UniProtKB Helix 98 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M80 +##sequence-region P03069 1 281 +P03069 UniProtKB Chain 1 281 . . . ID=PRO_0000076490;Note=General control protein GCN4 +P03069 UniProtKB Domain 225 281 . . . Note=bZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P03069 UniProtKB Region 89 100 . . . Note=Required for transcriptional activation +P03069 UniProtKB Region 106 125 . . . Note=Required for transcriptional activation +P03069 UniProtKB Region 231 251 . . . Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P03069 UniProtKB Region 253 274 . . . Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P03069 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P03069 UniProtKB Modified residue 165 165 . . . Note=Phosphothreonine%3B by PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12101234;Dbxref=PMID:12101234 +P03069 UniProtKB Modified residue 218 218 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P03069 UniProtKB Natural variant 24 24 . . . Note=In strain: CLIB 219. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P03069 UniProtKB Natural variant 62 62 . . . Note=In strain: CLIB 630 haplotype Ha2. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P03069 UniProtKB Natural variant 82 82 . . . Note=In strain: CLIB 556 haplotype Ha1. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P03069 UniProtKB Natural variant 91 91 . . . Note=In strain: CLIB 95%2C CLIB 219%2C CLIB 382%2C CLIB 388%2C CLIB 410%2C CLIB 413%2C CLIB 556%2C CLIB 630%2C K1%2C R12%2C R13 haplotype Ha2%2C Sigma 1278B haplotype Ha1%2C YIIc12 and YIIc17. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P03069 UniProtKB Natural variant 125 125 . . . Note=In strain: CLIB 556 haplotype Ha1. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P03069 UniProtKB Natural variant 196 196 . . . Note=In strain: CLIB 388%2C CLIB 410%2C CLIB 413%2C CLIB 630 haplotype Ha1%2C K1%2C YIIc12 haplotype Ha2 and YIIc17 haplotype Ha1. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P03069 UniProtKB Mutagenesis 97 98 . . . Note=Reduces transcriptional activation activity%3B when associated with A-107%3B A-110%3B A-113%3B A-120%3B A-123 and A-124. FF->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7862116;Dbxref=PMID:7862116 +P03069 UniProtKB Mutagenesis 107 107 . . . Note=Reduces transcriptional activation activity%3B when associated with A-97%3B A-98%3B A-110%3B A-113%3B A-120%3B A-123 and A-124. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7862116;Dbxref=PMID:7862116 +P03069 UniProtKB Mutagenesis 110 110 . . . Note=Reduces transcriptional activation activity%3B when associated with A-97%3B A-98%3B A-107%3B A-113%3B A-120%3B A-123 and A-124. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7862116;Dbxref=PMID:7862116 +P03069 UniProtKB Mutagenesis 113 113 . . . Note=Reduces transcriptional activation activity%3B when associated with A-97%3B A-98%3B A-107%3B A-110%3B A-120%3B A-123 and A-124. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7862116;Dbxref=PMID:7862116 +P03069 UniProtKB Mutagenesis 120 124 . . . Note=Reduces transcriptional activation activity%3B when associated with A-97%3B A-98%3B A-107%3B A-110 and A-113. WTSLF->ATSAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7862116;Dbxref=PMID:7862116 +P03069 UniProtKB Sequence conflict 239 281 . . . Note=ARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVGER->PGVLVRESCKE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03069 UniProtKB Helix 118 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LPB +P03069 UniProtKB Helix 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LPB +P03069 UniProtKB Helix 250 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TL1 +P03069 UniProtKB Turn 264 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AZD +P03069 UniProtKB Helix 268 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AZD +P03069 UniProtKB Turn 276 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AZD +##sequence-region Q03330 1 439 +Q03330 UniProtKB Chain 1 439 . . . ID=PRO_0000211201;Note=Histone acetyltransferase GCN5 +Q03330 UniProtKB Domain 100 255 . . . Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532 +Q03330 UniProtKB Domain 344 414 . . . Note=Bromo;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 +Q03330 UniProtKB Region 177 179 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92830 +Q03330 UniProtKB Region 184 190 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92830 +Q03330 UniProtKB Region 216 219 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92830 +Q03330 UniProtKB Active site 173 173 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92830 +Q03330 UniProtKB Site 173 173 . . . Note=Important for catalytic activity +Q03330 UniProtKB Sequence conflict 187 187 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03330 UniProtKB Beta strand 100 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH +Q03330 UniProtKB Helix 111 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH +Q03330 UniProtKB Helix 133 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH +Q03330 UniProtKB Beta strand 146 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH +Q03330 UniProtKB Turn 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH +Q03330 UniProtKB Beta strand 156 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH +Q03330 UniProtKB Helix 167 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH +Q03330 UniProtKB Beta strand 171 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH +Q03330 UniProtKB Helix 188 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH +Q03330 UniProtKB Beta strand 208 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH +Q03330 UniProtKB Helix 215 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH +Q03330 UniProtKB Helix 218 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH +Q03330 UniProtKB Beta strand 227 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH +Q03330 UniProtKB Helix 234 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH +Q03330 UniProtKB Beta strand 248 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGH +Q03330 UniProtKB Helix 333 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E6I +Q03330 UniProtKB Helix 350 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E6I +Q03330 UniProtKB Turn 358 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E6I +Q03330 UniProtKB Helix 364 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E6I +Q03330 UniProtKB Helix 374 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E6I +Q03330 UniProtKB Helix 389 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E6I +Q03330 UniProtKB Helix 412 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E6I +Q03330 UniProtKB Helix 432 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E6I +##sequence-region Q01722 1 534 +Q01722 UniProtKB Chain 1 534 . . . ID=PRO_0000087446;Note=Glycolytic genes transcriptional activator GCR2 +Q01722 UniProtKB Region 497 534 . . . Note=Leucine-zipper +Q01722 UniProtKB Motif 281 288 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01722 UniProtKB Compositional bias 255 283 . . . Note=Asn-rich +Q01722 UniProtKB Modified residue 151 151 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q01722 UniProtKB Modified residue 406 406 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q01722 UniProtKB Modified residue 409 409 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P32621 1 518 +P32621 UniProtKB Chain 1 518 . . . ID=PRO_0000209919;Note=Guanosine-diphosphatase +P32621 UniProtKB Topological domain 1 9 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32621 UniProtKB Transmembrane 10 24 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32621 UniProtKB Topological domain 25 518 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32621 UniProtKB Active site 216 216 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32621 UniProtKB Glycosylation 41 41 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32621 UniProtKB Glycosylation 280 280 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32621 UniProtKB Glycosylation 335 335 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q02979 1 1223 +Q02979 UniProtKB Chain 1 1223 . . . ID=PRO_0000233009;Note=Glycerophosphocholine phosphodiesterase GDE1 +Q02979 UniProtKB Domain 1 213 . . . Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714 +Q02979 UniProtKB Repeat 427 456 . . . Note=ANK 1 +Q02979 UniProtKB Repeat 472 502 . . . Note=ANK 2 +Q02979 UniProtKB Repeat 504 533 . . . Note=ANK 3 +Q02979 UniProtKB Repeat 538 567 . . . Note=ANK 4 +Q02979 UniProtKB Repeat 572 601 . . . Note=ANK 5 +Q02979 UniProtKB Repeat 605 634 . . . Note=ANK 6 +Q02979 UniProtKB Domain 872 1217 . . . Note=GP-PDE +Q02979 UniProtKB Modified residue 653 653 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q02979 UniProtKB Modified residue 983 983 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q99339 1 116 +Q99339 UniProtKB Chain 1 116 . . . ID=PRO_0000211376;Note=Putative UPF0320 protein YLL065W +##sequence-region P38229 1 639 +P38229 UniProtKB Chain 1 639 . . . ID=PRO_0000071520;Note=GLC7-interacting protein 1 +##sequence-region Q03768 1 265 +Q03768 UniProtKB Chain 1 265 . . . ID=PRO_0000087495;Note=Protein GIR2 +Q03768 UniProtKB Domain 9 159 . . . Note=RWD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00179 +##sequence-region P38068 1 203 +P38068 UniProtKB Signal peptide 1 32 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38068 UniProtKB Chain 33 203 . . . ID=PRO_0000042989;Note=Monothiol glutaredoxin-7 +P38068 UniProtKB Domain 88 191 . . . Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686 +P38068 UniProtKB Metal binding 108 108 . . . Note=Iron-sulfur (2Fe-2S)%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P37291 1 469 +P37291 UniProtKB Chain 1 469 . . . ID=PRO_0000113516;Note=Serine hydroxymethyltransferase%2C cytosolic +P37291 UniProtKB Modified residue 20 20 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P37291 UniProtKB Modified residue 26 26 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P37291 UniProtKB Modified residue 248 248 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P37291 UniProtKB Modified residue 429 429 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P37291 UniProtKB Cross-link 456 456 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P37291 UniProtKB Sequence conflict 429 429 . . . Note=S->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40107 1 337 +P40107 UniProtKB Chain 1 337 . . . ID=PRO_0000213398;Note=GDP-mannose transporter 1 +P40107 UniProtKB Topological domain 1 16 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Transmembrane 17 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Topological domain 38 51 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Transmembrane 52 72 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Topological domain 73 92 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Transmembrane 93 113 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Topological domain 114 119 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Transmembrane 120 140 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Topological domain 141 144 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Transmembrane 145 165 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Topological domain 166 180 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Transmembrane 181 201 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Topological domain 202 215 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Transmembrane 216 236 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Topological domain 237 252 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Transmembrane 253 273 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Topological domain 274 279 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Transmembrane 280 300 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Topological domain 301 304 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Transmembrane 305 325 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Topological domain 326 337 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Region 279 291 . . . Note=GDP-mannose-binding +P40107 UniProtKB Region 326 337 . . . Note=RET2-binding +P40107 UniProtKB Glycosylation 119 119 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Glycosylation 242 242 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Glycosylation 246 246 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Glycosylation 249 249 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40107 UniProtKB Mutagenesis 278 278 . . . Note=In VIG4-2%3B increases drug sensitivity and decreases protein glycolysis. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10570930;Dbxref=PMID:10570930 +P40107 UniProtKB Mutagenesis 280 280 . . . Note=Decreases transport activity and GDP-mannose-binding. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11067855;Dbxref=PMID:11067855 +P40107 UniProtKB Mutagenesis 282 282 . . . Note=Decreases transport activity and GDP-mannose-binding. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11067855;Dbxref=PMID:11067855 +P40107 UniProtKB Mutagenesis 285 285 . . . Note=Decreases transport activity and GDP-mannose-binding. G->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11067855;Dbxref=PMID:11067855 +P40107 UniProtKB Mutagenesis 286 286 . . . Note=In VIG4-1%3B increases drug sensitivity and decreases protein glycolysis. A->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10570930,ECO:0000269|PubMed:11067855;Dbxref=PMID:10570930,PMID:11067855 +P40107 UniProtKB Mutagenesis 287 287 . . . Note=Decreases transport activity and GDP-mannose-binding. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11067855;Dbxref=PMID:11067855 +P40107 UniProtKB Mutagenesis 288 288 . . . Note=Decreases transport activity and GDP-mannose-binding. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11067855;Dbxref=PMID:11067855 +P40107 UniProtKB Mutagenesis 289 289 . . . Note=Decreases transport activity and GDP-mannose-binding. K->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11067855;Dbxref=PMID:11067855 +P40107 UniProtKB Mutagenesis 291 291 . . . Note=Decreases transport activity and GDP-mannose-binding. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11067855;Dbxref=PMID:11067855 +##sequence-region P0CE11 1 249 +P0CE11 UniProtKB Chain 1 249 . . . ID=PRO_0000202628;Note=Probable GDP-mannose transporter 2 +P0CE11 UniProtKB Topological domain 1 15 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE11 UniProtKB Transmembrane 16 36 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE11 UniProtKB Topological domain 37 47 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE11 UniProtKB Transmembrane 48 68 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE11 UniProtKB Topological domain 69 84 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE11 UniProtKB Transmembrane 85 105 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE11 UniProtKB Topological domain 106 122 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE11 UniProtKB Transmembrane 123 143 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE11 UniProtKB Topological domain 144 159 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE11 UniProtKB Transmembrane 160 180 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE11 UniProtKB Topological domain 181 186 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE11 UniProtKB Transmembrane 187 207 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE11 UniProtKB Topological domain 208 211 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE11 UniProtKB Transmembrane 212 232 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE11 UniProtKB Topological domain 233 249 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE11 UniProtKB Glycosylation 149 149 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE11 UniProtKB Glycosylation 153 153 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43577 1 159 +P43577 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P43577 UniProtKB Chain 2 159 . . . ID=PRO_0000074552;Note=Glucosamine 6-phosphate N-acetyltransferase +P43577 UniProtKB Domain 28 159 . . . Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532 +P43577 UniProtKB Region 86 89 . . . Note=Substrate binding;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11278591;Dbxref=PMID:11278591 +P43577 UniProtKB Region 98 100 . . . Note=Substrate binding;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11278591;Dbxref=PMID:11278591 +P43577 UniProtKB Region 100 102 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1I12,ECO:0000269|PubMed:11278591;Dbxref=PMID:11278591 +P43577 UniProtKB Region 108 113 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1I12,ECO:0000269|PubMed:11278591;Dbxref=PMID:11278591 +P43577 UniProtKB Region 129 130 . . . Note=Substrate binding;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11278591;Dbxref=PMID:11278591 +P43577 UniProtKB Region 143 145 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1I12,ECO:0000269|PubMed:11278591;Dbxref=PMID:11278591 +P43577 UniProtKB Binding site 28 28 . . . Note=Substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11278591;Dbxref=PMID:11278591 +P43577 UniProtKB Binding site 134 134 . . . Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11278591;Dbxref=PMID:11278591 +P43577 UniProtKB Binding site 158 158 . . . Note=Substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11278591;Dbxref=PMID:11278591 +P43577 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P43577 UniProtKB Sequence conflict 112 159 . . . Note=GKLLIDQLVTIGFDYGCYKIILDCDEKNVKFYEKCGFSNAGVEMQIRK->ASS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43577 UniProtKB Turn 4 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I21 +P43577 UniProtKB Beta strand 7 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12 +P43577 UniProtKB Helix 14 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12 +P43577 UniProtKB Helix 17 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12 +P43577 UniProtKB Turn 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12 +P43577 UniProtKB Helix 35 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12 +P43577 UniProtKB Beta strand 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12 +P43577 UniProtKB Beta strand 65 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12 +P43577 UniProtKB Turn 70 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12 +P43577 UniProtKB Beta strand 74 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12 +P43577 UniProtKB Helix 88 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12 +P43577 UniProtKB Beta strand 93 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12 +P43577 UniProtKB Helix 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12 +P43577 UniProtKB Helix 111 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12 +P43577 UniProtKB Beta strand 129 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12 +P43577 UniProtKB Helix 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12 +P43577 UniProtKB Helix 140 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12 +P43577 UniProtKB Beta strand 149 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I12 +##sequence-region Q03554 1 138 +Q03554 UniProtKB Chain 1 138 . . . ID=PRO_0000218586;Note=Protein transport protein GOT1 +Q03554 UniProtKB Topological domain 1 8 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03554 UniProtKB Transmembrane 9 29 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03554 UniProtKB Topological domain 30 31 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03554 UniProtKB Transmembrane 32 52 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03554 UniProtKB Topological domain 53 67 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03554 UniProtKB Transmembrane 68 88 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03554 UniProtKB Topological domain 89 112 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03554 UniProtKB Transmembrane 113 133 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03554 UniProtKB Topological domain 134 138 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03554 UniProtKB Mutagenesis 73 73 . . . Note=In got1-1%3B loss of function. ER-Golgi transport defect when associated with lack of SFT2. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10406798;Dbxref=PMID:10406798 +##sequence-region P10823 1 449 +P10823 UniProtKB Initiator methionine 1 1 . . . Note=Removed +P10823 UniProtKB Chain 2 449 . . . ID=PRO_0000203617;Note=Guanine nucleotide-binding protein alpha-2 subunit +P10823 UniProtKB Nucleotide binding 130 137 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P10823 UniProtKB Nucleotide binding 270 276 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P10823 UniProtKB Nucleotide binding 296 300 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P10823 UniProtKB Nucleotide binding 365 368 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P10823 UniProtKB Metal binding 137 137 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P10823 UniProtKB Metal binding 276 276 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P10823 UniProtKB Binding site 420 420 . . . Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P10823 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16030250;Dbxref=PMID:16030250 +P10823 UniProtKB Lipidation 4 4 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16030250;Dbxref=PMID:16030250 +P10823 UniProtKB Mutagenesis 2 2 . . . Note=Abolishes both palmitoylation and N-myristoylation. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16030250;Dbxref=PMID:16030250 +P10823 UniProtKB Mutagenesis 4 4 . . . Note=Abolishes palmitoylation but not N-myristoylation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16030250;Dbxref=PMID:16030250 +P10823 UniProtKB Mutagenesis 6 6 . . . Note=Abolishes both palmitoylation and N-myristoylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16030250;Dbxref=PMID:16030250 +P10823 UniProtKB Mutagenesis 132 132 . . . Note=Locks GPA2 in its activated GTP-bound form and abrogates the negative control by RGS2. G->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10523302,ECO:0000269|PubMed:12150916;Dbxref=PMID:10523302,PMID:12150916 +P10823 UniProtKB Mutagenesis 299 299 . . . Note=Dominant negativ allele unable to undergo the GTP-induced conformational change. G->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12150916,ECO:0000269|PubMed:16030250;Dbxref=PMID:12150916,PMID:16030250 +P10823 UniProtKB Mutagenesis 300 300 . . . Note=Dominant active allele that abolishes intrinsic GTPase activity. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12150916;Dbxref=PMID:12150916 +P10823 UniProtKB Sequence conflict 375 375 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08886 1 897 +Q08886 UniProtKB Chain 1 897 . . . ID=PRO_0000239649;Note=Guanine nucleotide-binding protein subunit beta 1 +Q08886 UniProtKB Repeat 304 352 . . . Note=Kelch 1 +Q08886 UniProtKB Repeat 390 438 . . . Note=Kelch 2 +Q08886 UniProtKB Repeat 543 589 . . . Note=Kelch 3 +Q08886 UniProtKB Repeat 715 761 . . . Note=Kelch 4 +Q08886 UniProtKB Modified residue 91 91 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08886 UniProtKB Modified residue 161 161 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P40066 1 365 +P40066 UniProtKB Chain 1 365 . . . ID=PRO_0000051007;Note=Nucleoporin GLE2 +P40066 UniProtKB Repeat 34 74 . . . Note=WD 1 +P40066 UniProtKB Repeat 78 117 . . . Note=WD 2 +P40066 UniProtKB Repeat 119 162 . . . Note=WD 3 +P40066 UniProtKB Repeat 267 306 . . . Note=WD 4 +##sequence-region Q05584 1 274 +Q05584 UniProtKB Chain 1 274 . . . ID=PRO_0000192346;Note=Hydroxyacylglutathione hydrolase%2C cytoplasmic isozyme +Q05584 UniProtKB Region 188 190 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775 +Q05584 UniProtKB Region 268 271 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775 +Q05584 UniProtKB Metal binding 59 59 . . . Note=Zinc 1%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775 +Q05584 UniProtKB Metal binding 61 61 . . . Note=Zinc 1%3B via pros nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775 +Q05584 UniProtKB Metal binding 63 63 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775 +Q05584 UniProtKB Metal binding 64 64 . . . Note=Zinc 2%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775 +Q05584 UniProtKB Metal binding 121 121 . . . Note=Zinc 1%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775 +Q05584 UniProtKB Metal binding 144 144 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775 +Q05584 UniProtKB Metal binding 144 144 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775 +Q05584 UniProtKB Metal binding 188 188 . . . Note=Zinc 2%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775 +Q05584 UniProtKB Binding site 153 153 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05584 UniProtKB Modified residue 257 257 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q05584 UniProtKB Sequence conflict 222 222 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38682 1 493 +P38682 UniProtKB Chain 1 493 . . . ID=PRO_0000074225;Note=ADP-ribosylation factor GTPase-activating protein GLO3 +P38682 UniProtKB Domain 16 137 . . . Note=Arf-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288 +P38682 UniProtKB Zinc finger 31 54 . . . Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288 +P38682 UniProtKB Modified residue 170 170 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38682 UniProtKB Modified residue 306 306 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38682 UniProtKB Modified residue 389 389 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38682 UniProtKB Modified residue 398 398 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38682 UniProtKB Sequence conflict 222 222 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38682 UniProtKB Sequence conflict 406 493 . . . Note=EAHDKLKTFDNATSISSSSYFGEDKEVDEFGNPINSSGSGAGNFDGRNSNNGFIDFNASADDELQMLRDVVEQGAEKLGSYLRDYLRK->GSA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32190 1 709 +P32190 UniProtKB Chain 1 709 . . . ID=PRO_0000059542;Note=Glycerol kinase +P32190 UniProtKB Nucleotide binding 584 588 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32190 UniProtKB Binding site 56 56 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32190 UniProtKB Binding site 60 60 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32190 UniProtKB Binding site 201 201 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32190 UniProtKB Binding site 258 258 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32190 UniProtKB Binding site 386 386 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32190 UniProtKB Binding site 408 408 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32190 UniProtKB Binding site 463 463 . . . Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q12438 1 231 +Q12438 UniProtKB Signal peptide 1 29 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12438 UniProtKB Chain 30 231 . . . ID=PRO_0000042988;Note=Monothiol glutaredoxin-6 +Q12438 UniProtKB Domain 116 219 . . . Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686 +Q12438 UniProtKB Metal binding 136 136 . . . Note=Iron-sulfur (2Fe-2S)%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12438 UniProtKB Helix 115 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N +Q12438 UniProtKB Beta strand 127 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N +Q12438 UniProtKB Helix 137 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N +Q12438 UniProtKB Beta strand 150 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N +Q12438 UniProtKB Beta strand 157 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N +Q12438 UniProtKB Helix 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N +Q12438 UniProtKB Helix 167 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N +Q12438 UniProtKB Beta strand 185 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N +Q12438 UniProtKB Helix 196 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N +Q12438 UniProtKB Helix 208 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N +Q12438 UniProtKB Beta strand 221 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3L4N +##sequence-region P48813 1 663 +P48813 UniProtKB Chain 1 663 . . . ID=PRO_0000054152;Note=High-affinity glutamine permease +P48813 UniProtKB Topological domain 1 154 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Transmembrane 155 175 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Topological domain 176 177 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Transmembrane 178 198 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Topological domain 199 219 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Transmembrane 220 240 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Topological domain 241 264 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Transmembrane 265 285 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Topological domain 286 289 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Transmembrane 290 310 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Topological domain 311 342 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Transmembrane 343 363 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Topological domain 364 381 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Transmembrane 382 402 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Topological domain 403 432 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Transmembrane 433 453 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Topological domain 454 481 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Transmembrane 482 502 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Topological domain 503 506 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Transmembrane 507 527 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Topological domain 528 560 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Transmembrane 561 581 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Topological domain 582 590 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Transmembrane 591 611 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Topological domain 612 663 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48813 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48813 UniProtKB Modified residue 113 113 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48813 UniProtKB Modified residue 124 124 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P48813 UniProtKB Modified residue 127 127 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P48813 UniProtKB Cross-link 34 34 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P48813 UniProtKB Cross-link 39 39 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P48813 UniProtKB Cross-link 41 41 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P48813 UniProtKB Cross-link 61 61 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P48813 UniProtKB Cross-link 132 132 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P48813 UniProtKB Sequence conflict 319 319 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53839 1 350 +P53839 UniProtKB Chain 1 350 . . . ID=PRO_0000076040;Note=Glyoxylate reductase 1 +P53839 UniProtKB Nucleotide binding 173 174 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53839 UniProtKB Nucleotide binding 252 254 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53839 UniProtKB Nucleotide binding 301 304 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53839 UniProtKB Active site 254 254 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53839 UniProtKB Active site 283 283 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53839 UniProtKB Active site 301 301 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53839 UniProtKB Binding site 278 278 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53839 UniProtKB Modified residue 31 31 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q00055 1 391 +Q00055 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.9 +Q00055 UniProtKB Chain 2 391 . . . ID=PRO_0000138100;Note=Glycerol-3-phosphate dehydrogenase [NAD(+)] 1 +Q00055 UniProtKB Nucleotide binding 41 46 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00055 UniProtKB Region 310 311 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00055 UniProtKB Active site 245 245 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00055 UniProtKB Binding site 129 129 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00055 UniProtKB Binding site 152 152 . . . Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00055 UniProtKB Binding site 152 152 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00055 UniProtKB Binding site 185 185 . . . Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00055 UniProtKB Binding site 310 310 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00055 UniProtKB Binding site 339 339 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00055 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.9 +Q00055 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q00055 UniProtKB Modified residue 27 27 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198 +Q00055 UniProtKB Natural variant 16 16 . . . Note=In strain: WFB. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4 +Q00055 UniProtKB Natural variant 143 143 . . . Note=In strain: WFB. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4 +Q00055 UniProtKB Natural variant 164 164 . . . Note=In strain: WFB. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4 +Q00055 UniProtKB Natural variant 183 183 . . . Note=In strain: WFB. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4 +Q00055 UniProtKB Natural variant 225 225 . . . Note=In strain: WFB. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4 +Q00055 UniProtKB Natural variant 256 256 . . . Note=In strain: WFB. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4 +Q00055 UniProtKB Sequence conflict 103 107 . . . Note=DNLVA->TIWLL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00055 UniProtKB Beta strand 35 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Helix 44 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Turn 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Beta strand 64 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Beta strand 76 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Helix 82 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Turn 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Turn 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Beta strand 103 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Helix 111 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Beta strand 119 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Helix 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Helix 130 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Turn 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Beta strand 146 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Beta strand 155 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Beta strand 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Helix 164 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Beta strand 175 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Helix 185 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Beta strand 194 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Beta strand 209 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Helix 215 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Beta strand 227 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Helix 235 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Helix 261 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Helix 289 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Turn 296 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Helix 299 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Helix 310 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Helix 325 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Helix 340 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Helix 361 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +Q00055 UniProtKB Helix 379 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FGW +##sequence-region Q06636 1 219 +Q06636 UniProtKB Chain 1 219 . . . ID=PRO_0000191771;Note=Glycosylphosphatidylinositol anchor biosynthesis protein 11 +Q06636 UniProtKB Topological domain 1 45 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06636 UniProtKB Transmembrane 46 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06636 UniProtKB Topological domain 67 67 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06636 UniProtKB Transmembrane 68 88 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06636 UniProtKB Topological domain 89 108 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06636 UniProtKB Transmembrane 109 129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06636 UniProtKB Topological domain 130 135 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06636 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06636 UniProtKB Topological domain 157 170 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06636 UniProtKB Transmembrane 171 191 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06636 UniProtKB Topological domain 192 198 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06636 UniProtKB Transmembrane 199 217 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06636 UniProtKB Topological domain 218 219 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06636 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P47088 1 403 +P47088 UniProtKB Chain 1 403 . . . ID=PRO_0000203084;Note=GPI mannosyltransferase 1 +P47088 UniProtKB Topological domain 1 4 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Transmembrane 5 25 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Topological domain 26 78 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Transmembrane 79 99 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Topological domain 100 110 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Transmembrane 111 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Topological domain 132 132 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Transmembrane 133 149 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Topological domain 150 160 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Transmembrane 161 181 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Topological domain 182 193 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Transmembrane 194 214 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Topological domain 215 266 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Transmembrane 267 287 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Topological domain 288 310 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Transmembrane 311 331 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Topological domain 332 334 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Transmembrane 335 355 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Topological domain 356 361 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Transmembrane 362 382 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47088 UniProtKB Topological domain 383 403 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04082 1 140 +Q04082 UniProtKB Chain 1 140 . . . ID=PRO_0000240380;Note=Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI19 +Q04082 UniProtKB Topological domain 1 12 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16278447;Dbxref=PMID:16278447 +Q04082 UniProtKB Transmembrane 13 33 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04082 UniProtKB Topological domain 34 52 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16278447;Dbxref=PMID:16278447 +Q04082 UniProtKB Transmembrane 53 73 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04082 UniProtKB Topological domain 74 140 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16278447;Dbxref=PMID:16278447 +##sequence-region P32363 1 452 +P32363 UniProtKB Chain 1 452 . . . ID=PRO_0000080325;Note=Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit +P32363 UniProtKB Transmembrane 407 427 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32363 UniProtKB Mutagenesis 289 289 . . . Note=Severe growth defect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14622279;Dbxref=PMID:14622279 +P32363 UniProtKB Mutagenesis 289 289 . . . Note=Reduces the transferase reaction 12-fold. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14622279;Dbxref=PMID:14622279 +P32363 UniProtKB Mutagenesis 289 289 . . . Note=Lethal. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14622279;Dbxref=PMID:14622279 +P32363 UniProtKB Mutagenesis 297 297 . . . Note=Lethal. E->A%2CG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14622279;Dbxref=PMID:14622279 +P32363 UniProtKB Mutagenesis 297 297 . . . Note=No transferase activity. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14622279;Dbxref=PMID:14622279 +P32363 UniProtKB Mutagenesis 301 301 . . . Note=Reduces the transferase reaction 5-fold. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14622279;Dbxref=PMID:14622279 +##sequence-region Q08726 1 347 +Q08726 UniProtKB Chain 1 347 . . . ID=PRO_0000245255;Note=GPN-loop GTPase 2 +Q08726 UniProtKB Nucleotide binding 12 17 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9 +Q08726 UniProtKB Nucleotide binding 175 178 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9 +Q08726 UniProtKB Motif 69 71 . . . Note=Gly-Pro-Asn (GPN)-loop%3B involved in dimer interface;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9 +Q08726 UniProtKB Site 71 71 . . . Note=Stabilizes the phosphate intermediate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9 +Q08726 UniProtKB Mutagenesis 112 112 . . . Note=Impairs heterodimer formation with NPA3/GPN1. E->K%2CA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23324351;Dbxref=PMID:23324351 +##sequence-region P40581 1 163 +P40581 UniProtKB Chain 1 163 . . . ID=PRO_0000066643;Note=Glutathione peroxidase-like peroxiredoxin HYR1 +P40581 UniProtKB Active site 36 36 . . . Note=Cysteine sulfenic acid (-SOH) intermediate;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:17720812,ECO:0000305|PubMed:18767166;Dbxref=PMID:17720812,PMID:18767166 +P40581 UniProtKB Disulfide bond 36 82 . . . Note=Redox-active;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:18767166;Dbxref=PMID:18767166 +P40581 UniProtKB Disulfide bond 36 36 . . . Note=Interchain (with C-598 in YAP1)%3B transient;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12437921,ECO:0000269|PubMed:17720812;Dbxref=PMID:12437921,PMID:17720812 +P40581 UniProtKB Mutagenesis 82 82 . . . Note=Loss of enzyme activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18767166;Dbxref=PMID:18767166 +P40581 UniProtKB Helix 3 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI +P40581 UniProtKB Helix 19 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI +P40581 UniProtKB Beta strand 26 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI +P40581 UniProtKB Helix 39 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI +P40581 UniProtKB Helix 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI +P40581 UniProtKB Beta strand 57 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI +P40581 UniProtKB Beta strand 97 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI +P40581 UniProtKB Helix 105 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI +P40581 UniProtKB Beta strand 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI +P40581 UniProtKB Beta strand 129 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI +P40581 UniProtKB Beta strand 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI +P40581 UniProtKB Beta strand 138 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI +P40581 UniProtKB Helix 148 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI +P40581 UniProtKB Helix 152 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CMI +##sequence-region P33892 1 2672 +P33892 UniProtKB Chain 1 2672 . . . ID=PRO_0000087444;Note=eIF-2-alpha kinase activator GCN1 +P33892 UniProtKB Repeat 5 42 . . . Note=HEAT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 79 117 . . . Note=HEAT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 174 211 . . . Note=HEAT 3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 227 267 . . . Note=HEAT 4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 329 366 . . . Note=HEAT 5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 372 410 . . . Note=HEAT 6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 509 549 . . . Note=HEAT 7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 611 648 . . . Note=HEAT 8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 706 745 . . . Note=HEAT 9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 902 932 . . . Note=HEAT 10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 933 970 . . . Note=HEAT 11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 975 994 . . . Note=HEAT 12%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 995 1030 . . . Note=HEAT 13%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1031 1067 . . . Note=HEAT 14;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1099 1138 . . . Note=HEAT 15;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1185 1224 . . . Note=HEAT 16;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1243 1281 . . . Note=HEAT 17;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1284 1321 . . . Note=HEAT 18;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1363 1401 . . . Note=HEAT 19;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1405 1442 . . . Note=HEAT 20;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1444 1480 . . . Note=HEAT 21;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1484 1521 . . . Note=HEAT 22;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1523 1559 . . . Note=HEAT 23;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1561 1598 . . . Note=HEAT 24;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1603 1640 . . . Note=HEAT 25;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1641 1679 . . . Note=HEAT 26;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1681 1717 . . . Note=HEAT 27;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1721 1758 . . . Note=HEAT 28;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1760 1796 . . . Note=HEAT 29;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1825 1862 . . . Note=HEAT 30;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1863 1903 . . . Note=HEAT 31;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1905 1942 . . . Note=HEAT 32;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1947 1984 . . . Note=HEAT 33;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 1985 2024 . . . Note=HEAT 34;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 2026 2055 . . . Note=HEAT 35;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 2057 2095 . . . Note=HEAT 36;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 2097 2134 . . . Note=HEAT 37;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 2138 2175 . . . Note=HEAT 38;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 2206 2243 . . . Note=HEAT 39;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 2250 2286 . . . Note=HEAT 40;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 2290 2328 . . . Note=HEAT 41;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 2347 2384 . . . Note=HEAT 42;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 2392 2429 . . . Note=HEAT 43;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 2450 2487 . . . Note=HEAT 44;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Repeat 2506 2546 . . . Note=HEAT 45;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33892 UniProtKB Region 1330 1641 . . . Note=EF3-like region;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9234705;Dbxref=PMID:9234705 +P33892 UniProtKB Mutagenesis 757 758 . . . Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20%2C weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner%3B when associated with A-762%3B A-765%3B A-775%3B 777-A-A-778%3B 782-A-A-783%3B 786-A-A-787 and A-790. KK->AA%2CDD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15722345,ECO:0000269|PubMed:22888004;Dbxref=PMID:15722345,PMID:22888004 +P33892 UniProtKB Mutagenesis 762 762 . . . Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20%2C weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner%3B when associated with A-757-758-A%3B A-765%3B A-775%3B 777-A-A-778%3B 782-A-A-783%3B 786-A-A-787 and A-790. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15722345,ECO:0000269|PubMed:22888004;Dbxref=PMID:15722345,PMID:22888004 +P33892 UniProtKB Mutagenesis 765 765 . . . Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20%2C weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner%3B when associated with A-757-758-A%3B A-762%3B A-775%3B 777-A-A-778%3B 782-A-A-783%3B 786-A-A-787 and A-790. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15722345,ECO:0000269|PubMed:22888004;Dbxref=PMID:15722345,PMID:22888004 +P33892 UniProtKB Mutagenesis 775 775 . . . Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20%2C weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner%3B when associated with A-757-758-A%3B A-762%3B A-765%3B 777-A-A-778%3B 782-A-A-783%3B 786-A-A-787 and A-790. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15722345,ECO:0000269|PubMed:22888004;Dbxref=PMID:15722345,PMID:22888004 +P33892 UniProtKB Mutagenesis 777 778 . . . Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20%2C weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner%3B when associated with A-757-758-A%3B A-762%3B A-765%3B A-775%3B 782-A-A-783%3B 786-A-A-787 and A-790. RK->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15722345,ECO:0000269|PubMed:22888004;Dbxref=PMID:15722345,PMID:22888004 +P33892 UniProtKB Mutagenesis 782 783 . . . Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20%2C weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner%3B when associated with A-757-758-A%3B A-762%3B A-765%3B A-775%3B 777-A-A-778%3B 786-A-A-787 and A-790. KK->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15722345,ECO:0000269|PubMed:22888004;Dbxref=PMID:15722345,PMID:22888004 +P33892 UniProtKB Mutagenesis 786 787 . . . Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20%2C weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner%3B when associated with A-757-758-A%3B A-762%3B A-765%3B A-775%3B 777-A-A-778%3B 782-A-A-783 and A-790. KK->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15722345,ECO:0000269|PubMed:22888004;Dbxref=PMID:15722345,PMID:22888004 +P33892 UniProtKB Mutagenesis 790 790 . . . Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20%2C weakly impairs eIF-2-alpha phosphorylation but strongly impairs eIF-2-alpha phosphorylation in a YEF3-dependent manner%3B when associated with A-757-758-A%3B A-762%3B A-765%3B A-775%3B 777-A-A-778%3B 782-A-A-783 and 786-A-A-787. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15722345,ECO:0000269|PubMed:22888004;Dbxref=PMID:15722345,PMID:22888004 +P33892 UniProtKB Mutagenesis 1444 1444 . . . Note=Decreases interaction with GCN20 and polysomal association. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234705;Dbxref=PMID:9234705 +P33892 UniProtKB Mutagenesis 1458 1458 . . . Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20 and strongly impairs eIF-2-alpha phosphorylation%3B when associated with 1461-A--A-1465. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15722345;Dbxref=PMID:15722345 +P33892 UniProtKB Mutagenesis 1461 1465 . . . Note=Does not inhibit interaction with GCN20%2C reduces ribosome binding%2C ribosome binding by GCN20 and strongly impairs eIF-2-alpha phosphorylation%3B when associated with A-1458. WRTKR->AAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15722345;Dbxref=PMID:15722345 +P33892 UniProtKB Mutagenesis 2259 2259 . . . Note=Decreases interaction with GCN2 and YIH1 but not with GCN20 and ribosomes. R->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11101534,ECO:0000269|PubMed:15126500,ECO:0000269|PubMed:21239490;Dbxref=PMID:11101534,PMID:15126500,PMID:21239490 +P33892 UniProtKB Mutagenesis 2291 2291 . . . Note=Does not interact with GCN2%2C impairs eIF-2-alpha phosphorylation and fails to derepress GCN4 translation in amino acid-starved cells. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350982;Dbxref=PMID:11350982 +P33892 UniProtKB Mutagenesis 2304 2304 . . . Note=Does not interact with GCN2. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350982;Dbxref=PMID:11350982 +P33892 UniProtKB Mutagenesis 2353 2353 . . . Note=Does not interact with GCN2. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350982;Dbxref=PMID:11350982 +##sequence-region P49095 1 1034 +P49095 UniProtKB Modified residue 773 773 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P37020 1 779 +P37020 UniProtKB Chain 1 779 . . . ID=PRO_0000094472;Note=Anion/proton exchange transporter GEF1 +P37020 UniProtKB Chain 1 136 . . . ID=PRO_0000419270;Note=GEF1 N-terminal +P37020 UniProtKB Chain 137 779 . . . ID=PRO_0000419271;Note=GEF1 C-terminal +P37020 UniProtKB Topological domain 1 75 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Transmembrane 76 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Topological domain 97 154 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Transmembrane 155 175 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Topological domain 176 177 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Transmembrane 178 198 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Topological domain 199 203 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Transmembrane 204 224 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Topological domain 225 264 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Transmembrane 265 285 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Topological domain 286 296 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Transmembrane 297 319 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Topological domain 320 336 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Transmembrane 337 357 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Topological domain 358 369 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Transmembrane 370 390 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Topological domain 391 436 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Transmembrane 437 457 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Topological domain 458 465 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Transmembrane 466 486 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Topological domain 487 500 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Transmembrane 501 523 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Topological domain 524 529 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Transmembrane 530 552 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Topological domain 553 779 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37020 UniProtKB Domain 591 659 . . . Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +P37020 UniProtKB Domain 688 744 . . . Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +P37020 UniProtKB Site 136 137 . . . Note=Cleavage%3B by KEX2 +P37020 UniProtKB Site 230 230 . . . Note=Mediates proton transfer from the outer aqueous phase to the interior of the protein%3B involved in linking H(+) and Cl(-) transport;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P37020 UniProtKB Site 287 287 . . . Note=Mediates proton transfer from the protein to the inner aqueous phase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P37020 UniProtKB Sequence conflict 13 13 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37020 UniProtKB Sequence conflict 207 207 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37020 UniProtKB Sequence conflict 257 257 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37020 UniProtKB Sequence conflict 262 262 . . . Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37020 UniProtKB Sequence conflict 497 497 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38812 1 185 +P38812 UniProtKB Chain 1 185 . . . ID=PRO_0000202908;Note=Phosphatidylglycerophosphatase GEP4%2C mitochondrial +P38812 UniProtKB Motif 45 49 . . . Note=Phosphoryl acceptor +P38812 UniProtKB Mutagenesis 45 45 . . . Note=Abolishes phosphatase activity and impairs cardiolipin biosynthesis. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20485265;Dbxref=PMID:20485265 +P38812 UniProtKB Mutagenesis 47 47 . . . Note=Abolishes phosphatase activity and impairs cardiolipin biosynthesis. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20485265;Dbxref=PMID:20485265 +##sequence-region Q12125 1 312 +Q12125 UniProtKB Chain 1 312 . . . ID=PRO_0000228107;Note=Golgi to ER traffic protein 4 +Q12125 UniProtKB Helix 13 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +Q12125 UniProtKB Helix 29 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +Q12125 UniProtKB Helix 49 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +Q12125 UniProtKB Helix 69 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +Q12125 UniProtKB Helix 92 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +Q12125 UniProtKB Helix 112 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +Q12125 UniProtKB Helix 134 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +Q12125 UniProtKB Helix 150 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +Q12125 UniProtKB Helix 162 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +Q12125 UniProtKB Helix 184 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +Q12125 UniProtKB Helix 204 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +Q12125 UniProtKB Beta strand 226 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +Q12125 UniProtKB Beta strand 234 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +Q12125 UniProtKB Helix 243 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +Q12125 UniProtKB Helix 260 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +Q12125 UniProtKB Helix 271 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +Q12125 UniProtKB Helix 278 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +##sequence-region P36173 1 615 +P36173 UniProtKB Chain 1 615 . . . ID=PRO_0000203231;Note=Glutathione exchanger 2 +P36173 UniProtKB Topological domain 1 58 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Transmembrane 59 79 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Topological domain 80 120 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Transmembrane 121 141 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Topological domain 142 152 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Transmembrane 153 173 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Topological domain 174 216 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Transmembrane 217 237 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Topological domain 238 275 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Transmembrane 276 296 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Topological domain 297 307 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Transmembrane 308 328 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Topological domain 329 343 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Transmembrane 344 364 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Topological domain 365 383 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Transmembrane 384 404 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Topological domain 405 407 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Transmembrane 408 428 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Topological domain 429 440 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Transmembrane 441 461 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Topological domain 462 471 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Transmembrane 472 492 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Topological domain 493 548 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Transmembrane 549 569 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36173 UniProtKB Topological domain 570 615 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06336 1 557 +Q06336 UniProtKB Chain 1 557 . . . ID=PRO_0000212686;Note=ADP-ribosylation factor-binding protein GGA1 +Q06336 UniProtKB Domain 29 165 . . . Note=VHS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00218 +Q06336 UniProtKB Domain 192 317 . . . Note=GAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00373 +Q06336 UniProtKB Domain 440 556 . . . Note=GAE;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00093 +Q06336 UniProtKB Modified residue 348 348 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q06336 UniProtKB Modified residue 353 353 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06336 UniProtKB Modified residue 357 357 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q06336 UniProtKB Modified residue 378 378 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06336 UniProtKB Modified residue 394 394 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06336 UniProtKB Beta strand 445 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2 +Q06336 UniProtKB Beta strand 451 461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2 +Q06336 UniProtKB Beta strand 463 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2 +Q06336 UniProtKB Beta strand 477 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2 +Q06336 UniProtKB Beta strand 481 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2 +Q06336 UniProtKB Beta strand 495 498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2 +Q06336 UniProtKB Beta strand 510 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2 +Q06336 UniProtKB Helix 523 526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2 +Q06336 UniProtKB Beta strand 531 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2 +Q06336 UniProtKB Beta strand 544 554 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CN2 +##sequence-region P38817 1 585 +P38817 UniProtKB Chain 1 585 . . . ID=PRO_0000212687;Note=ADP-ribosylation factor-binding protein GGA2 +P38817 UniProtKB Domain 33 169 . . . Note=VHS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00218 +P38817 UniProtKB Domain 196 321 . . . Note=GAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00373 +P38817 UniProtKB Domain 466 581 . . . Note=GAE;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00093 +P38817 UniProtKB Cross-link 180 180 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38817 UniProtKB Cross-link 287 287 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38817 UniProtKB Mutagenesis 560 560 . . . Note=Reduced binding to ENT3. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12483220;Dbxref=PMID:12483220 +P38817 UniProtKB Mutagenesis 563 563 . . . Note=Reduced binding to ENT3 and ENT5. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12483220;Dbxref=PMID:12483220 +P38817 UniProtKB Mutagenesis 564 564 . . . Note=Reduced binding to ENT3 and ENT5. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12483220;Dbxref=PMID:12483220 +P38817 UniProtKB Beta strand 472 477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM +P38817 UniProtKB Beta strand 479 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM +P38817 UniProtKB Beta strand 491 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM +P38817 UniProtKB Beta strand 495 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM +P38817 UniProtKB Beta strand 505 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM +P38817 UniProtKB Beta strand 509 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM +P38817 UniProtKB Beta strand 522 526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM +P38817 UniProtKB Beta strand 542 550 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM +P38817 UniProtKB Beta strand 560 569 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM +P38817 UniProtKB Beta strand 572 581 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MNM +##sequence-region P25569 1 745 +P25569 UniProtKB Chain 1 745 . . . ID=PRO_0000051006;Note=Glucose-induced degradation protein 7 +P25569 UniProtKB Repeat 167 209 . . . Note=WD 1 +P25569 UniProtKB Repeat 322 365 . . . Note=WD 2 +P25569 UniProtKB Repeat 369 408 . . . Note=WD 3 +P25569 UniProtKB Repeat 540 579 . . . Note=WD 4 +P25569 UniProtKB Repeat 613 652 . . . Note=WD 5 +P25569 UniProtKB Repeat 657 696 . . . Note=WD 6 +P25569 UniProtKB Repeat 710 745 . . . Note=WD 7 +##sequence-region P32642 1 244 +P32642 UniProtKB Chain 1 244 . . . ID=PRO_0000102250;Note=Monothiol glutaredoxin-4 +P32642 UniProtKB Domain 3 110 . . . Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +P32642 UniProtKB Domain 146 244 . . . Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686 +P32642 UniProtKB Region 225 226 . . . Note=Glutathione binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32642 UniProtKB Metal binding 171 171 . . . Note=Iron-sulfur (2Fe-2S)%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32642 UniProtKB Binding site 163 163 . . . Note=Glutathione;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32642 UniProtKB Binding site 200 200 . . . Note=Glutathione;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32642 UniProtKB Binding site 212 212 . . . Note=Glutathione%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38138 1 954 +P38138 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38138 UniProtKB Chain 23 954 . . . ID=PRO_0000185370;Note=Glucosidase 2 subunit alpha +P38138 UniProtKB Active site 537 537 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10066 +P38138 UniProtKB Active site 540 540 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38138 UniProtKB Active site 614 614 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38138 UniProtKB Glycosylation 114 114 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38138 UniProtKB Glycosylation 126 126 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38138 UniProtKB Glycosylation 142 142 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38138 UniProtKB Glycosylation 173 173 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38138 UniProtKB Glycosylation 345 345 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38138 UniProtKB Glycosylation 783 783 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38138 UniProtKB Glycosylation 791 791 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38138 UniProtKB Glycosylation 867 867 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38138 UniProtKB Glycosylation 880 880 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38138 UniProtKB Glycosylation 907 907 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38138 UniProtKB Glycosylation 941 941 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04924 1 702 +Q04924 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04924 UniProtKB Chain 21 702 . . . ID=PRO_0000245572;Note=Glucosidase 2 subunit beta +Q04924 UniProtKB Coiled coil 163 228 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04924 UniProtKB Coiled coil 478 517 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04924 UniProtKB Glycosylation 145 145 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04924 UniProtKB Glycosylation 240 240 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04924 UniProtKB Glycosylation 358 358 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04924 UniProtKB Glycosylation 520 520 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04924 UniProtKB Glycosylation 525 525 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04924 UniProtKB Glycosylation 688 688 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04924 UniProtKB Glycosylation 699 699 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P48015 1 400 +P48015 UniProtKB Binding site 221 221 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P48015 UniProtKB Binding site 250 250 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P48015 UniProtKB Binding site 397 397 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P48015 UniProtKB Sequence conflict 122 122 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06625 1 1536 +Q06625 UniProtKB Chain 1 1536 . . . ID=PRO_0000087452;Note=Glycogen debranching enzyme +Q06625 UniProtKB Active site 535 535 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06625 UniProtKB Active site 538 538 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06625 UniProtKB Active site 670 670 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06625 UniProtKB Sequence conflict 368 368 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06625 UniProtKB Sequence conflict 536 536 . . . Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06625 UniProtKB Sequence conflict 774 774 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06625 UniProtKB Sequence conflict 1180 1180 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06625 UniProtKB Sequence conflict 1289 1289 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06625 UniProtKB Sequence conflict 1489 1489 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39958 1 451 +P39958 UniProtKB Chain 1 451 . . . ID=PRO_0000056684;Note=Rab GDP-dissociation inhibitor +P39958 UniProtKB Region 106 112 . . . Note=Interaction with YPT1 +P39958 UniProtKB Region 234 259 . . . Note=Interaction with YPT1 +P39958 UniProtKB Beta strand 11 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 19 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 35 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 40 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 53 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 67 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 82 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 94 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 116 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 123 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 131 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPJ +P39958 UniProtKB Helix 142 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 163 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Turn 171 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 176 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 187 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 201 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 204 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 211 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 231 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 241 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 256 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 265 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Turn 270 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 275 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 283 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 290 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 294 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 298 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 301 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 322 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPI +P39958 UniProtKB Beta strand 326 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 334 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 343 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 350 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 360 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 373 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 378 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 382 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 388 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Turn 405 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 408 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Beta strand 419 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +P39958 UniProtKB Helix 422 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BCG +##sequence-region Q12434 1 202 +Q12434 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12434 UniProtKB Chain 2 202 . . . ID=PRO_0000219022;Note=Rho GDP-dissociation inhibitor +Q12434 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12434 UniProtKB Modified residue 27 27 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +Q12434 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P39722 1 662 +P39722 UniProtKB Chain 1 662 . . . ID=PRO_0000202422;Note=Mitochondrial Rho GTPase 1 +P39722 UniProtKB Topological domain 1 634 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39722 UniProtKB Transmembrane 635 655 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39722 UniProtKB Topological domain 656 662 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39722 UniProtKB Domain 1 140 . . . Note=Miro 1 +P39722 UniProtKB Domain 201 236 . . . Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P39722 UniProtKB Domain 330 365 . . . Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P39722 UniProtKB Domain 442 662 . . . Note=Miro 2 +P39722 UniProtKB Nucleotide binding 12 19 . . . Note=GTP 1;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39722 UniProtKB Nucleotide binding 62 64 . . . Note=GTP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39722 UniProtKB Nucleotide binding 116 119 . . . Note=GTP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39722 UniProtKB Calcium binding 214 225 . . . Note=1;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39722 UniProtKB Calcium binding 343 354 . . . Note=2;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39722 UniProtKB Nucleotide binding 455 462 . . . Note=GTP 2;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39722 UniProtKB Nucleotide binding 491 495 . . . Note=GTP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39722 UniProtKB Nucleotide binding 560 563 . . . Note=GTP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39722 UniProtKB Mutagenesis 18 18 . . . Note=Loss of function. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15479738;Dbxref=PMID:15479738 +P39722 UniProtKB Mutagenesis 19 19 . . . Note=Loss of function. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15479738;Dbxref=PMID:15479738 +P39722 UniProtKB Mutagenesis 33 33 . . . Note=No effect. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15479738;Dbxref=PMID:15479738 +P39722 UniProtKB Mutagenesis 225 225 . . . Note=Induces collapsed%2C globular or grape-like mitochondria%3B when associated with A-354. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15479738;Dbxref=PMID:15479738 +P39722 UniProtKB Mutagenesis 354 354 . . . Note=Induces collapsed%2C globular or grape-like mitochondria%3B when associated with A-225. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15479738;Dbxref=PMID:15479738 +P39722 UniProtKB Mutagenesis 461 461 . . . Note=Induces collapsed%2C globular or grape-like mitochondria. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15479738;Dbxref=PMID:15479738 +P39722 UniProtKB Mutagenesis 462 462 . . . Note=Induces collapsed%2C globular or grape-like mitochondria. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15479738;Dbxref=PMID:15479738 +P39722 UniProtKB Mutagenesis 480 480 . . . Note=Induces collapsed%2C globular or grape-like mitochondria. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15479738;Dbxref=PMID:15479738 +##sequence-region P38785 1 314 +P38785 UniProtKB Chain 1 314 . . . ID=PRO_0000212659;Note=GTPase-interacting component 1 +P38785 UniProtKB Domain 126 139 . . . Note=CRIB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00057 +##sequence-region Q12418 1 502 +Q12418 UniProtKB Chain 1 502 . . . ID=PRO_0000087497;Note=Protein GIS3 +##sequence-region P41818 1 229 +P41818 UniProtKB Chain 1 229 . . . ID=PRO_0000071517;Note=Protein GLC8 +P41818 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198 +P41818 UniProtKB Modified residue 118 118 . . . Note=Phosphothreonine%3B by PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12407105;Dbxref=PMID:12407105 +P41818 UniProtKB Modified residue 158 158 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P41818 UniProtKB Modified residue 184 184 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P47011 1 380 +P47011 UniProtKB Chain 1 380 . . . ID=PRO_0000215182;Note=Glycogenin-2 +P47011 UniProtKB Glycosylation 230 230 . . . Note=O-linked (Glc...) tyrosine +P47011 UniProtKB Glycosylation 232 232 . . . Note=O-linked (Glc...) tyrosine +P47011 UniProtKB Glycosylation 367 367 . . . Note=O-linked (Glc...) tyrosine;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47011 UniProtKB Mutagenesis 230 230 . . . Note=Eliminates glycogen accumulation%3B when associated with F-232 and F-367. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8900126;Dbxref=PMID:8900126 +P47011 UniProtKB Mutagenesis 232 232 . . . Note=Eliminates glycogen accumulation%3B when associated with F-230 and F-367. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8900126;Dbxref=PMID:8900126 +P47011 UniProtKB Mutagenesis 367 367 . . . Note=Eliminates glycogen accumulation%3B when associated with F-230 and F-232. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8900126;Dbxref=PMID:8900126 +P47011 UniProtKB Sequence conflict 241 241 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38263 1 362 +P38263 UniProtKB Chain 1 362 . . . ID=PRO_0000065826;Note=Vacuolar import and degradation protein 24 +P38263 UniProtKB Modified residue 27 27 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38263 UniProtKB Cross-link 20 20 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P40208 1 455 +P40208 UniProtKB Chain 1 455 . . . ID=PRO_0000087486;Note=Glucose-induced degradation protein 8 +P40208 UniProtKB Domain 85 116 . . . Note=LisH +P40208 UniProtKB Domain 130 213 . . . Note=CTLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00058 +P40208 UniProtKB Compositional bias 179 186 . . . Note=Poly-Gln +##sequence-region Q12263 1 1142 +Q12263 UniProtKB Chain 1 1142 . . . ID=PRO_0000085964;Note=Serine/threonine-protein kinase GIN4 +Q12263 UniProtKB Domain 19 289 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12263 UniProtKB Nucleotide binding 25 33 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12263 UniProtKB Active site 156 156 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q12263 UniProtKB Binding site 48 48 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12263 UniProtKB Modified residue 406 406 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12263 UniProtKB Modified residue 465 465 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12263 UniProtKB Modified residue 471 471 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12263 UniProtKB Modified residue 617 617 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12263 UniProtKB Modified residue 689 689 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +Q12263 UniProtKB Modified residue 719 719 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12263 UniProtKB Modified residue 805 805 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q12263 UniProtKB Modified residue 807 807 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q12263 UniProtKB Modified residue 883 883 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12263 UniProtKB Modified residue 884 884 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12263 UniProtKB Modified residue 930 930 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region P32288 1 370 +P32288 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:2891705,ECO:0000269|PubMed:9298649;Dbxref=PMID:15665377,PMID:22814378,PMID:2891705,PMID:9298649 +P32288 UniProtKB Chain 2 370 . . . ID=PRO_0000153166;Note=Glutamine synthetase +P32288 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:9298649;Dbxref=PMID:15665377,PMID:22814378,PMID:9298649 +P32288 UniProtKB Modified residue 5 5 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P32288 UniProtKB Cross-link 283 283 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32288 UniProtKB Cross-link 324 324 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32288 UniProtKB Cross-link 363 363 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32288 UniProtKB Sequence conflict 165 165 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32288 UniProtKB Sequence conflict 172 172 . . . Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32288 UniProtKB Sequence conflict 251 251 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32288 UniProtKB Sequence conflict 251 251 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32288 UniProtKB Sequence conflict 264 264 . . . Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32288 UniProtKB Sequence conflict 264 264 . . . Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32288 UniProtKB Beta strand 24 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Beta strand 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Beta strand 37 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Helix 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Beta strand 57 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Turn 61 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Beta strand 74 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Turn 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Beta strand 92 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Beta strand 103 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Helix 111 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Helix 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Beta strand 127 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Beta strand 141 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Beta strand 155 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Turn 164 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Helix 170 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Beta strand 187 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Beta strand 198 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Helix 209 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Turn 228 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Beta strand 232 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Beta strand 239 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Beta strand 248 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Helix 256 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Beta strand 260 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Helix 264 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Helix 278 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Helix 289 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Beta strand 307 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Beta strand 314 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Helix 320 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Beta strand 330 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Helix 341 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +P32288 UniProtKB Turn 361 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FKY +##sequence-region Q12320 1 285 +Q12320 UniProtKB Metal binding 69 69 . . . Note=Zinc 1%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775 +Q12320 UniProtKB Metal binding 71 71 . . . Note=Zinc 1%3B via pros nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775 +Q12320 UniProtKB Metal binding 73 73 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775 +Q12320 UniProtKB Metal binding 74 74 . . . Note=Zinc 2%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775 +Q12320 UniProtKB Metal binding 131 131 . . . Note=Zinc 1%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775 +Q12320 UniProtKB Metal binding 154 154 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775 +Q12320 UniProtKB Metal binding 154 154 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775 +Q12320 UniProtKB Metal binding 198 198 . . . Note=Zinc 2%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16775 +##sequence-region P25373 1 110 +P25373 UniProtKB Chain 1 110 . . . ID=PRO_0000141613;Note=Glutaredoxin-1 +P25373 UniProtKB Domain 7 110 . . . Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686 +P25373 UniProtKB Region 24 29 . . . Note=Glutathione binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17327665,ECO:0000269|PubMed:18473363;Dbxref=PMID:17327665,PMID:18473363 +P25373 UniProtKB Region 88 89 . . . Note=Glutathione binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17327665,ECO:0000269|PubMed:18473363;Dbxref=PMID:17327665,PMID:18473363 +P25373 UniProtKB Binding site 63 63 . . . Note=Glutathione;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17327665,ECO:0000269|PubMed:18473363;Dbxref=PMID:17327665,PMID:18473363 +P25373 UniProtKB Binding site 75 75 . . . Note=Glutathione%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17327665,ECO:0000269|PubMed:18473363;Dbxref=PMID:17327665,PMID:18473363 +P25373 UniProtKB Modified residue 27 27 . . . Note=S-glutathionyl cysteine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17327665,ECO:0000269|PubMed:18473363;Dbxref=PMID:17327665,PMID:18473363 +P25373 UniProtKB Disulfide bond 27 30 . . . Note=Redox-active%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18473363;Dbxref=PMID:18473363 +P25373 UniProtKB Cross-link 11 11 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25373 UniProtKB Mutagenesis 30 30 . . . Note=Leads to increased oxidoreductase activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18992757;Dbxref=PMID:18992757 +P25373 UniProtKB Mutagenesis 89 89 . . . Note=Leads to increased oxidoreductase activity. D->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20417731;Dbxref=PMID:20417731 +P25373 UniProtKB Helix 4 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R +P25373 UniProtKB Beta strand 17 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R +P25373 UniProtKB Helix 28 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R +P25373 UniProtKB Turn 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JAD +P25373 UniProtKB Helix 45 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R +P25373 UniProtKB Beta strand 48 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R +P25373 UniProtKB Helix 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R +P25373 UniProtKB Helix 59 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R +P25373 UniProtKB Beta strand 77 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R +P25373 UniProtKB Beta strand 83 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R +P25373 UniProtKB Helix 88 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R +P25373 UniProtKB Helix 99 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C1R +##sequence-region Q12680 1 2145 +Q12680 UniProtKB Propeptide 1 53 . . . ID=PRO_0000011612;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7836314;Dbxref=PMID:7836314 +Q12680 UniProtKB Chain 54 2145 . . . ID=PRO_0000011613;Note=Glutamate synthase [NADH] +Q12680 UniProtKB Domain 54 455 . . . Note=Glutamine amidotransferase type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609 +Q12680 UniProtKB Nucleotide binding 1132 1189 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12680 UniProtKB Nucleotide binding 1928 1942 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12680 UniProtKB Coiled coil 1551 1600 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12680 UniProtKB Active site 54 54 . . . Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12680 UniProtKB Metal binding 1185 1185 . . . Note=Iron-sulfur (3Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12680 UniProtKB Metal binding 1191 1191 . . . Note=Iron-sulfur (3Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12680 UniProtKB Metal binding 1196 1196 . . . Note=Iron-sulfur (3Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12680 UniProtKB Modified residue 2070 2070 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12680 UniProtKB Sequence conflict 166 173 . . . Note=NVPVDSTI->TSRRFYY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12680 UniProtKB Sequence conflict 450 452 . . . Note=FLV->IPS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12680 UniProtKB Sequence conflict 1753 1753 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P37292 1 490 +P37292 UniProtKB Transit peptide 1 20 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37292 UniProtKB Chain 21 490 . . . ID=PRO_0000032568;Note=Serine hydroxymethyltransferase%2C mitochondrial +P37292 UniProtKB Modified residue 265 265 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P37292 UniProtKB Sequence conflict 72 72 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03786 1 193 +Q03786 UniProtKB Chain 1 193 . . . ID=PRO_0000253810;Note=Probable gluconokinase +Q03786 UniProtKB Nucleotide binding 18 25 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P30777 1 616 +P30777 UniProtKB Chain 1 616 . . . ID=PRO_0000202736;Note=GPI mannosyltransferase 3 +P30777 UniProtKB Topological domain 1 16 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Transmembrane 17 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Topological domain 38 86 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Transmembrane 87 107 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Topological domain 108 136 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Transmembrane 137 157 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Topological domain 158 188 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Transmembrane 189 209 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Topological domain 210 240 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Transmembrane 241 261 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Topological domain 262 278 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Transmembrane 279 299 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Topological domain 300 338 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Transmembrane 339 359 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Topological domain 360 392 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Transmembrane 393 413 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Topological domain 414 423 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Transmembrane 424 444 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Topological domain 445 616 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30777 UniProtKB Mutagenesis 48 48 . . . Note=In gpi10-1%3B accumulate M2%2C an abnormal GPI-anchor intermediate due to the absence of third mannose. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9639537;Dbxref=PMID:9639537 +P30777 UniProtKB Sequence conflict 339 339 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07830 1 1017 +Q07830 UniProtKB Chain 1 1017 . . . ID=PRO_0000240363;Note=GPI ethanolamine phosphate transferase 3 +Q07830 UniProtKB Transmembrane 34 54 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Transmembrane 347 367 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Transmembrane 457 477 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Transmembrane 484 504 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Transmembrane 515 535 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Transmembrane 558 578 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Transmembrane 582 602 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Transmembrane 644 664 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Transmembrane 685 705 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Transmembrane 715 735 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Transmembrane 765 785 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Transmembrane 806 826 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Transmembrane 829 849 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Transmembrane 903 923 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Transmembrane 947 967 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Transmembrane 981 1001 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Glycosylation 66 66 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Glycosylation 71 71 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Glycosylation 100 100 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Glycosylation 182 182 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Glycosylation 203 203 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Glycosylation 411 411 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Glycosylation 681 681 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Glycosylation 682 682 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Glycosylation 707 707 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Glycosylation 742 742 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07830 UniProtKB Mutagenesis 198 198 . . . Note=In MCP1-5%3B impairs growth at 36 degrees Celsius%3B when associated with S-231 and T-411. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12441642;Dbxref=PMID:12441642 +Q07830 UniProtKB Mutagenesis 231 231 . . . Note=In MCP1-5%3B impairs growth at 36 degrees Celsius%3B when associated with R-198 and T-411. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12441642;Dbxref=PMID:12441642 +Q07830 UniProtKB Mutagenesis 367 367 . . . Note=In MCP1-4%3B impairs growth at 36 degrees Celsius%3B when associated with P-556%3B G-887 and A-901. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12441642;Dbxref=PMID:12441642 +Q07830 UniProtKB Mutagenesis 411 411 . . . Note=In MCP1-5%3B impairs growth at 36 degrees Celsius%3B when associated with R-198 and S-231. N->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12441642;Dbxref=PMID:12441642 +Q07830 UniProtKB Mutagenesis 556 556 . . . Note=In MCP1-4%3B impairs growth at 36 degrees Celsius%3B when associated with T-367%3B G-887 and A-901. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12441642;Dbxref=PMID:12441642 +Q07830 UniProtKB Mutagenesis 887 887 . . . Note=In MCP1-4%3B impairs growth at 36 degrees Celsius%3B when associated with T-367%3B P-556 and A-901. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12441642;Dbxref=PMID:12441642 +Q07830 UniProtKB Mutagenesis 901 901 . . . Note=In MCP1-4%3B impairs growth at 36 degrees Celsius%3B when associated with T-367%3B P-556 and G-887. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12441642;Dbxref=PMID:12441642 +##sequence-region P53306 1 609 +P53306 UniProtKB Chain 1 609 . . . ID=PRO_0000215666;Note=Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI1 +P53306 UniProtKB Topological domain 1 186 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53306 UniProtKB Transmembrane 187 207 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53306 UniProtKB Topological domain 208 280 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53306 UniProtKB Transmembrane 281 301 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53306 UniProtKB Topological domain 302 380 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53306 UniProtKB Transmembrane 381 401 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53306 UniProtKB Topological domain 402 451 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53306 UniProtKB Transmembrane 452 472 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53306 UniProtKB Topological domain 473 485 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53306 UniProtKB Transmembrane 486 506 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53306 UniProtKB Topological domain 507 609 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06543 1 272 +Q06543 UniProtKB Chain 1 272 . . . ID=PRO_0000255597;Note=GPN-loop GTPase 3 +Q06543 UniProtKB Nucleotide binding 13 18 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9 +Q06543 UniProtKB Nucleotide binding 173 176 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9 +Q06543 UniProtKB Motif 70 72 . . . Note=Gly-Pro-Asn (GPN)-loop%3B involved in dimer interface;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9 +Q06543 UniProtKB Site 72 72 . . . Note=Stabilizes the phosphate intermediate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9 +Q06543 UniProtKB Mutagenesis 110 110 . . . Note=Impairs heterodimer formation with NPA3/GPN1. E->K%2CA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23324351;Dbxref=PMID:23324351 +##sequence-region P41277 1 250 +P41277 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9038161;Dbxref=PMID:9038161 +P41277 UniProtKB Chain 2 250 . . . ID=PRO_0000087560;Note=Glycerol-1-phosphate phosphohydrolase 1 +P41277 UniProtKB Active site 18 18 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41277 UniProtKB Active site 20 20 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41277 UniProtKB Metal binding 18 18 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41277 UniProtKB Metal binding 20 20 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41277 UniProtKB Metal binding 179 179 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41277 UniProtKB Modified residue 90 90 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P41277 UniProtKB Cross-link 64 64 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15166219;Dbxref=PMID:15166219 +P41277 UniProtKB Cross-link 64 64 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P41277 UniProtKB Cross-link 144 144 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P41277 UniProtKB Sequence conflict 91 91 . . . Note=I->IK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41277 UniProtKB Beta strand 6 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Turn 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Helix 27 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Helix 46 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Helix 58 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Helix 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Helix 72 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Helix 82 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Helix 96 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Helix 108 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Beta strand 111 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Helix 119 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Beta strand 135 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Helix 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Helix 151 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Helix 169 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Beta strand 174 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Helix 181 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Beta strand 193 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Helix 203 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Beta strand 212 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Helix 218 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Beta strand 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Turn 228 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Beta strand 232 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Beta strand 241 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +P41277 UniProtKB Turn 245 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLT +##sequence-region P18494 1 730 +P18494 UniProtKB Chain 1 730 . . . ID=PRO_0000083477;Note=Nitrogen regulatory protein GLN3 +P18494 UniProtKB Zinc finger 306 330 . . . Note=GATA-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00094 +P18494 UniProtKB Motif 129 137 . . . Note=9aaTAD +P18494 UniProtKB Compositional bias 351 361 . . . Note=Arg/Lys-rich (basic) +P18494 UniProtKB Modified residue 251 251 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P18494 UniProtKB Modified residue 267 267 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P18494 UniProtKB Modified residue 285 285 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P18494 UniProtKB Modified residue 469 469 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P18494 UniProtKB Modified residue 552 552 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P18494 UniProtKB Modified residue 562 562 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P18494 UniProtKB Sequence conflict 474 474 . . . Note=P->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03835 1 250 +Q03835 UniProtKB Chain 1 250 . . . ID=PRO_0000102249;Note=Monothiol glutaredoxin-3 +Q03835 UniProtKB Domain 1 110 . . . Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +Q03835 UniProtKB Domain 151 250 . . . Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686 +Q03835 UniProtKB Metal binding 176 176 . . . Note=Iron-sulfur (2Fe-2S)%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03835 UniProtKB Beta strand 3 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I +Q03835 UniProtKB Helix 9 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I +Q03835 UniProtKB Turn 17 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I +Q03835 UniProtKB Beta strand 25 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I +Q03835 UniProtKB Helix 37 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I +Q03835 UniProtKB Helix 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I +Q03835 UniProtKB Beta strand 56 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I +Q03835 UniProtKB Turn 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I +Q03835 UniProtKB Helix 67 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I +Q03835 UniProtKB Beta strand 77 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I +Q03835 UniProtKB Beta strand 88 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I +Q03835 UniProtKB Helix 98 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D6I +##sequence-region Q02784 1 150 +Q02784 UniProtKB Transit peptide 1 29 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11950925;Dbxref=PMID:11950925 +Q02784 UniProtKB Chain 30 150 . . . ID=PRO_0000011632;Note=Monothiol glutaredoxin-5%2C mitochondrial +Q02784 UniProtKB Domain 35 140 . . . Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686 +Q02784 UniProtKB Region 92 96 . . . Note=Glutathione binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02784 UniProtKB Region 117 118 . . . Note=Glutathione binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02784 UniProtKB Metal binding 60 60 . . . Note=Iron-sulfur (2Fe-2S)%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02784 UniProtKB Binding site 52 52 . . . Note=Glutathione;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02784 UniProtKB Binding site 104 104 . . . Note=Glutathione%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02784 UniProtKB Helix 32 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8 +Q02784 UniProtKB Beta strand 46 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8 +Q02784 UniProtKB Beta strand 55 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8 +Q02784 UniProtKB Helix 62 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8 +Q02784 UniProtKB Helix 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8 +Q02784 UniProtKB Beta strand 80 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8 +Q02784 UniProtKB Helix 89 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8 +Q02784 UniProtKB Beta strand 106 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8 +Q02784 UniProtKB Beta strand 112 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8 +Q02784 UniProtKB Helix 117 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8 +Q02784 UniProtKB Helix 128 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GX8 +##sequence-region P32784 1 759 +P32784 UniProtKB Chain 1 759 . . . ID=PRO_0000195257;Note=Glycerol-3-phosphate O-acyltransferase 1 +P32784 UniProtKB Transmembrane 49 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32784 UniProtKB Transmembrane 123 139 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32784 UniProtKB Transmembrane 260 276 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32784 UniProtKB Transmembrane 440 463 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32784 UniProtKB Transmembrane 494 516 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32784 UniProtKB Transmembrane 524 545 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32784 UniProtKB Motif 414 419 . . . Note=HXXXXD motif +P32784 UniProtKB Compositional bias 736 753 . . . Note=Poly-Glu +P32784 UniProtKB Sequence conflict 10 10 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32784 UniProtKB Sequence conflict 10 10 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32784 UniProtKB Sequence conflict 30 38 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32784 UniProtKB Sequence conflict 88 88 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32784 UniProtKB Sequence conflict 125 125 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32784 UniProtKB Sequence conflict 278 278 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32784 UniProtKB Sequence conflict 324 324 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32784 UniProtKB Sequence conflict 574 574 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32784 UniProtKB Sequence conflict 730 730 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P07286 1 448 +P07286 UniProtKB Chain 1 448 . . . ID=PRO_0000108765;Note=UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase +P07286 UniProtKB Transmembrane 24 44 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07286 UniProtKB Transmembrane 72 92 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07286 UniProtKB Transmembrane 129 149 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07286 UniProtKB Transmembrane 157 177 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07286 UniProtKB Transmembrane 202 222 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07286 UniProtKB Transmembrane 231 251 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07286 UniProtKB Transmembrane 256 276 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07286 UniProtKB Transmembrane 283 303 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07286 UniProtKB Transmembrane 309 329 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07286 UniProtKB Transmembrane 387 407 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07286 UniProtKB Transmembrane 419 439 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07286 UniProtKB Motif 81 93 . . . Note=Dolichol recognition +P07286 UniProtKB Motif 257 269 . . . Note=Dolichol recognition +##sequence-region P36148 1 743 +P36148 UniProtKB Chain 1 743 . . . ID=PRO_0000195258;Note=Glycerol-3-phosphate O-acyltransferase 2 +P36148 UniProtKB Topological domain 1 30 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36148 UniProtKB Transmembrane 31 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36148 UniProtKB Topological domain 56 68 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36148 UniProtKB Transmembrane 69 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36148 UniProtKB Topological domain 86 501 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36148 UniProtKB Transmembrane 502 524 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36148 UniProtKB Topological domain 525 538 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36148 UniProtKB Transmembrane 539 555 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36148 UniProtKB Topological domain 556 743 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36148 UniProtKB Modified residue 632 632 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36148 UniProtKB Modified residue 637 637 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36148 UniProtKB Modified residue 647 647 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36148 UniProtKB Modified residue 651 651 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36148 UniProtKB Modified residue 654 654 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P36148 UniProtKB Modified residue 657 657 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36148 UniProtKB Modified residue 664 664 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36148 UniProtKB Modified residue 668 668 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P36148 UniProtKB Modified residue 671 671 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P36148 UniProtKB Modified residue 673 673 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36148 UniProtKB Modified residue 688 688 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36148 UniProtKB Modified residue 692 692 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36148 UniProtKB Modified residue 693 693 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q04410 1 372 +Q04410 UniProtKB Chain 1 372 . . . ID=PRO_0000270975;Note=GRASP65 homolog protein 1 +Q04410 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17261844;Dbxref=PMID:17261844 +Q04410 UniProtKB Modified residue 155 155 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q04410 UniProtKB Mutagenesis 2 2 . . . Note=Abolishes acetylation and association with cis-Golgi. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17261844;Dbxref=PMID:17261844 +##sequence-region Q08929 1 609 +Q08929 UniProtKB Chain 1 609 . . . ID=PRO_0000213133;Note=Glycerol uptake protein 2 +Q08929 UniProtKB Transmembrane 76 95 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08929 UniProtKB Transmembrane 129 151 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08929 UniProtKB Transmembrane 164 186 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08929 UniProtKB Transmembrane 201 218 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08929 UniProtKB Transmembrane 323 345 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08929 UniProtKB Transmembrane 365 387 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08929 UniProtKB Transmembrane 408 427 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08929 UniProtKB Transmembrane 501 523 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08929 UniProtKB Transmembrane 535 557 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08929 UniProtKB Transmembrane 577 594 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08929 UniProtKB Active site 496 496 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04322 1 720 +Q04322 UniProtKB Chain 1 720 . . . ID=PRO_0000208062;Note=Probable GTPase-activating protein GYL1 +Q04322 UniProtKB Domain 297 477 . . . Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163 +Q04322 UniProtKB Coiled coil 572 696 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04322 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q04322 UniProtKB Modified residue 17 17 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +Q04322 UniProtKB Modified residue 37 37 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +Q04322 UniProtKB Modified residue 73 73 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04322 UniProtKB Modified residue 139 139 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04322 UniProtKB Cross-link 498 498 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15542864;Dbxref=PMID:15542864 +##sequence-region P48365 1 746 +P48365 UniProtKB Chain 1 746 . . . ID=PRO_0000208017;Note=GTPase-activating protein GYP7 +P48365 UniProtKB Domain 385 633 . . . Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163 +P48365 UniProtKB Modified residue 265 265 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48365 UniProtKB Modified residue 339 339 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P23337 1 708 +P23337 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2123485;Dbxref=PMID:2123485 +P23337 UniProtKB Chain 2 708 . . . ID=PRO_0000194773;Note=Glycogen [starch] synthase isoform 1 +P23337 UniProtKB Binding site 20 20 . . . Note=UDP-glucose;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23337 UniProtKB Modified residue 159 159 . . . Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23337 UniProtKB Modified residue 363 363 . . . Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23337 UniProtKB Modified residue 560 560 . . . Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23337 UniProtKB Modified residue 651 651 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P23337 UniProtKB Modified residue 655 655 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P23337 UniProtKB Modified residue 660 660 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23337 UniProtKB Modified residue 662 662 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23337 UniProtKB Modified residue 667 667 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27472 +##sequence-region P04911 1 132 +P04911 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12915400;Dbxref=PMID:12915400 +P04911 UniProtKB Chain 2 132 . . . ID=PRO_0000055326;Note=Histone H2A.1 +P04911 UniProtKB Motif 129 130 . . . Note=[ST]-Q motif +P04911 UniProtKB Site 120 120 . . . Note=Not ubiquitinated;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10642555,ECO:0000269|PubMed:2201907;Dbxref=PMID:10642555,PMID:2201907 +P04911 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12915400;Dbxref=PMID:12915400 +P04911 UniProtKB Modified residue 5 5 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10082517;Dbxref=PMID:10082517 +P04911 UniProtKB Modified residue 8 8 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10082517,ECO:0000269|PubMed:11545749;Dbxref=PMID:10082517,PMID:11545749 +P04911 UniProtKB Modified residue 106 106 . . . Note=N5-methylglutamine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24352239;Dbxref=PMID:24352239 +P04911 UniProtKB Modified residue 129 129 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11140636;Dbxref=PMID:11140636 +P04911 UniProtKB Cross-link 127 127 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) +P04911 UniProtKB Mutagenesis 120 121 . . . Note=No effect. No effect%3B when associated with R-124 and R-127. KK->RR;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10642555,ECO:0000269|PubMed:2201907;Dbxref=PMID:10642555,PMID:2201907 +P04911 UniProtKB Mutagenesis 122 122 . . . Note=Causes hypersensitivity to DNA-damage-inducing agents and impairs sporulation. S->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15781691;Dbxref=PMID:15781691 +P04911 UniProtKB Mutagenesis 124 124 . . . Note=No effect%3B when associated with R-120%3B R-121 and R-127. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10642555;Dbxref=PMID:10642555 +P04911 UniProtKB Mutagenesis 127 127 . . . Note=No effect%3B when associated with R-120%3B R-121 and R-124. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10642555;Dbxref=PMID:10642555 +P04911 UniProtKB Mutagenesis 129 129 . . . Note=Causes hypersensitivity to DNA-damage-inducing agents. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11140636;Dbxref=PMID:11140636 +P04911 UniProtKB Mutagenesis 129 129 . . . Note=No effect. S->E%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11140636;Dbxref=PMID:11140636 +P04911 UniProtKB Helix 19 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WNN +P04911 UniProtKB Helix 29 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WNN +P04911 UniProtKB Beta strand 41 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WNN +P04911 UniProtKB Helix 48 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WNN +P04911 UniProtKB Beta strand 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WNN +P04911 UniProtKB Helix 82 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WNN +P04911 UniProtKB Helix 93 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WNN +P04911 UniProtKB Beta strand 102 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ID3 +P04911 UniProtKB Helix 115 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ID3 +##sequence-region P02294 1 131 +P02294 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02294 UniProtKB Chain 2 131 . . . ID=PRO_0000071939;Note=Histone H2B.2 +P02294 UniProtKB Modified residue 7 7 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16598039;Dbxref=PMID:16598039 +P02294 UniProtKB Modified residue 8 8 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16598039;Dbxref=PMID:16598039 +P02294 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15652479,ECO:0000269|PubMed:15970663;Dbxref=PMID:15652479,PMID:15970663 +P02294 UniProtKB Modified residue 12 12 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11545749,ECO:0000269|PubMed:15186774;Dbxref=PMID:11545749,PMID:15186774 +P02294 UniProtKB Modified residue 17 17 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11545749,ECO:0000269|PubMed:15186774,ECO:0000269|PubMed:16598039;Dbxref=PMID:11545749,PMID:15186774,PMID:16598039 +P02294 UniProtKB Cross-link 7 7 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate +P02294 UniProtKB Cross-link 8 8 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate +P02294 UniProtKB Cross-link 17 17 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02294 UniProtKB Cross-link 18 18 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02294 UniProtKB Cross-link 124 124 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12535538,ECO:0000269|PubMed:12535539,ECO:0000269|PubMed:14660635,ECO:0000269|PubMed:15280549;Dbxref=PMID:12535538,PMID:12535539,PMID:14660635,PMID:15280549 +P02294 UniProtKB Mutagenesis 7 8 . . . Note=Reduces sumoylation. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16598039;Dbxref=PMID:16598039 +P02294 UniProtKB Mutagenesis 11 11 . . . Note=Desensitizes cells to H(2)O(2) treatment. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15652479;Dbxref=PMID:15652479 +P02294 UniProtKB Mutagenesis 11 11 . . . Note=Induces apoptotic-like features including chromatin condensation. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15652479;Dbxref=PMID:15652479 +P02294 UniProtKB Mutagenesis 17 18 . . . Note=Reduces sumoylation. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16598039;Dbxref=PMID:16598039 +P02294 UniProtKB Mutagenesis 124 124 . . . Note=Impairs ubiquitin conjugation%2C DNA double-strand breaks formation during meiosis and histone H3-K79 methylation. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:14660635,ECO:0000269|PubMed:15280549;Dbxref=PMID:12152067,PMID:14660635,PMID:15280549 +P02294 UniProtKB Helix 42 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P02294 UniProtKB Turn 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P02294 UniProtKB Helix 60 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P02294 UniProtKB Beta strand 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P02294 UniProtKB Helix 95 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P02294 UniProtKB Helix 109 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +##sequence-region P40857 1 217 +P40857 UniProtKB Chain 1 217 . . . ID=PRO_0000203047;Note=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase PHS1 +P40857 UniProtKB Topological domain 1 11 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40857 UniProtKB Transmembrane 12 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40857 UniProtKB Topological domain 30 47 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40857 UniProtKB Transmembrane 48 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40857 UniProtKB Topological domain 67 76 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40857 UniProtKB Transmembrane 77 94 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40857 UniProtKB Topological domain 95 99 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40857 UniProtKB Transmembrane 100 117 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40857 UniProtKB Topological domain 118 142 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40857 UniProtKB Transmembrane 143 160 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40857 UniProtKB Topological domain 161 178 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40857 UniProtKB Transmembrane 179 196 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40857 UniProtKB Topological domain 197 217 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40857 UniProtKB Motif 214 217 . . . Note=Endoplasmic reticulum retention signal +P40857 UniProtKB Active site 149 149 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:18272525;Dbxref=PMID:18272525 +P40857 UniProtKB Active site 156 156 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:18272525;Dbxref=PMID:18272525 +P40857 UniProtKB Mutagenesis 149 149 . . . Note=No catalytic activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18272525;Dbxref=PMID:18272525 +P40857 UniProtKB Mutagenesis 156 156 . . . Note=No catalytic activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18272525;Dbxref=PMID:18272525 +##sequence-region P25333 1 603 +P25333 UniProtKB Chain 1 603 . . . ID=PRO_0000085987;Note=Serine/threonine-protein kinase HAL4/SAT4 +P25333 UniProtKB Domain 316 590 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P25333 UniProtKB Nucleotide binding 322 330 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P25333 UniProtKB Compositional bias 99 111 . . . Note=Ser-rich +P25333 UniProtKB Active site 449 449 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P25333 UniProtKB Binding site 353 353 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +##sequence-region Q04399 1 608 +Q04399 UniProtKB Chain 1 608 . . . ID=PRO_0000085585;Note=Putative multicopper oxidase GMC1 +Q04399 UniProtKB Domain 51 163 . . . Note=Plastocyanin-like 1 +Q04399 UniProtKB Domain 243 374 . . . Note=Plastocyanin-like 2 +Q04399 UniProtKB Domain 421 548 . . . Note=Plastocyanin-like 3 +Q04399 UniProtKB Metal binding 100 100 . . . Note=Copper 1%3B type 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04399 UniProtKB Metal binding 102 102 . . . Note=Copper 2%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04399 UniProtKB Metal binding 145 145 . . . Note=Copper 2%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04399 UniProtKB Metal binding 147 147 . . . Note=Copper 3%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04399 UniProtKB Metal binding 452 452 . . . Note=Copper 4%3B type 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04399 UniProtKB Metal binding 455 455 . . . Note=Copper 1%3B type 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04399 UniProtKB Metal binding 457 457 . . . Note=Copper 3%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04399 UniProtKB Metal binding 530 530 . . . Note=Copper 3%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04399 UniProtKB Metal binding 531 531 . . . Note=Copper 4%3B type 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04399 UniProtKB Metal binding 532 532 . . . Note=Copper 2%3B type 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04399 UniProtKB Metal binding 536 536 . . . Note=Copper 4%3B type 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38736 1 223 +P38736 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38736 UniProtKB Chain 2 223 . . . ID=PRO_0000212557;Note=Golgi SNAP receptor complex member 1 +P38736 UniProtKB Topological domain 2 204 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38736 UniProtKB Transmembrane 205 222 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38736 UniProtKB Topological domain 223 223 . . . Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38736 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38736 UniProtKB Modified residue 164 164 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P39717 1 880 +P39717 UniProtKB Chain 1 880 . . . ID=PRO_0000119071;Note=Guanine nucleotide-binding protein subunit beta 2 +P39717 UniProtKB Repeat 291 339 . . . Note=Kelch 1 +P39717 UniProtKB Repeat 377 425 . . . Note=Kelch 2 +P39717 UniProtKB Repeat 501 552 . . . Note=Kelch 3 +P39717 UniProtKB Repeat 691 738 . . . Note=Kelch 4 +P39717 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39717 UniProtKB Natural variant 215 215 . . . Note=In strain: Sigma 1278B. Y->H +P39717 UniProtKB Natural variant 221 221 . . . Note=In strain: Sigma 1278B. L->P +P39717 UniProtKB Natural variant 552 552 . . . Note=In strain: Sigma 1278B. S->R +P39717 UniProtKB Natural variant 674 674 . . . Note=In strain: Sigma 1278B. A->T +P39717 UniProtKB Natural variant 777 777 . . . Note=In strain: Sigma 1278B. P->S +P39717 UniProtKB Sequence conflict 661 661 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39717 UniProtKB Sequence conflict 802 802 . . . Note=C->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39717 UniProtKB Sequence conflict 814 815 . . . Note=ED->AA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08969 1 168 +Q08969 UniProtKB Chain 1 168 . . . ID=PRO_0000083846;Note=Protein GRE1 +Q08969 UniProtKB Compositional bias 28 139 . . . Note=Gln-rich +##sequence-region P38715 1 327 +P38715 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7747971;Dbxref=PMID:7747971 +P38715 UniProtKB Chain 2 327 . . . ID=PRO_0000124678;Note=NADPH-dependent aldose reductase GRE3 +P38715 UniProtKB Nucleotide binding 219 286 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38715 UniProtKB Active site 49 49 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38715 UniProtKB Binding site 111 111 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38715 UniProtKB Site 78 78 . . . Note=Lowers pKa of active site Tyr;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53154 1 560 +P53154 UniProtKB Chain 1 560 . . . ID=PRO_0000213132;Note=Glycerol uptake protein 1 +P53154 UniProtKB Topological domain 1 43 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Transmembrane 44 64 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Topological domain 65 101 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Transmembrane 102 122 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Topological domain 123 131 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Transmembrane 132 152 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Topological domain 153 276 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Transmembrane 277 297 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Topological domain 298 322 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Transmembrane 323 343 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Topological domain 344 352 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Transmembrane 353 373 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Topological domain 374 432 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Transmembrane 433 449 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Topological domain 450 454 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Transmembrane 455 474 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Topological domain 475 485 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Transmembrane 486 506 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Topological domain 507 526 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Transmembrane 527 547 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Topological domain 548 560 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53154 UniProtKB Active site 447 447 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40531 1 326 +P40531 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P40531 UniProtKB Chain 2 326 . . . ID=PRO_0000083881;Note=Protein GVP36 +P40531 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P40531 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P40531 UniProtKB Modified residue 319 319 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40531 UniProtKB Cross-link 13 13 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P40531 UniProtKB Cross-link 305 305 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P40531 UniProtKB Cross-link 313 313 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q08484 1 637 +Q08484 UniProtKB Chain 1 637 . . . ID=PRO_0000208010;Note=GTPase-activating protein GYP1 +Q08484 UniProtKB Domain 280 508 . . . Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163 +Q08484 UniProtKB Compositional bias 117 129 . . . Note=His-rich +Q08484 UniProtKB Modified residue 69 69 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08484 UniProtKB Modified residue 250 250 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q08484 UniProtKB Helix 251 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 270 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 283 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 286 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 304 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Beta strand 323 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 330 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 341 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 349 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 354 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Turn 372 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 380 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 393 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 398 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Turn 404 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 409 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 415 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 434 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 445 461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 463 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 477 485 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Turn 486 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 489 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 494 508 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 571 585 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 587 590 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 595 602 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +Q08484 UniProtKB Helix 612 629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FKM +##sequence-region P48566 1 633 +P48566 UniProtKB Chain 1 633 . . . ID=PRO_0000208012;Note=GTPase-activating protein GYP3 +P48566 UniProtKB Domain 223 456 . . . Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163 +P48566 UniProtKB Modified residue 147 147 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48566 UniProtKB Modified residue 484 484 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48566 UniProtKB Mutagenesis 282 282 . . . Note=Reduced GAP activity. R->F%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12913108;Dbxref=PMID:12913108 +##sequence-region Q12753 1 694 +Q12753 UniProtKB Chain 1 694 . . . ID=PRO_0000194933;Note=Transcriptional activator HAA1 +Q12753 UniProtKB DNA binding 1 40 . . . Note=Copper-fist;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055 +Q12753 UniProtKB Metal binding 11 11 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055 +Q12753 UniProtKB Metal binding 14 14 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055 +Q12753 UniProtKB Metal binding 23 23 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055 +Q12753 UniProtKB Metal binding 25 25 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055 +Q12753 UniProtKB Modified residue 125 125 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12753 UniProtKB Modified residue 231 231 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12753 UniProtKB Modified residue 241 241 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:18407956 +Q12753 UniProtKB Modified residue 291 291 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P41546 1 238 +P41546 UniProtKB Chain 1 238 . . . ID=PRO_0000076518;Note=Transcriptional activator HAC1 +P41546 UniProtKB Domain 39 102 . . . Note=bZIP +P41546 UniProtKB Region 41 61 . . . Note=Basic motif;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41546 UniProtKB Region 67 74 . . . Note=Leucine-zipper;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41546 UniProtKB Alternative sequence 221 238 . . . ID=VSP_020905;Note=In isoform U. EAQSGLNSFELNDFFITS->AVITMTRKLQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41546 UniProtKB Sequence conflict 181 181 . . . Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P42950 1 618 +P42950 UniProtKB Chain 1 618 . . . ID=PRO_0000114998;Note=Glucose starvation modulator protein 1 +P42950 UniProtKB Domain 466 538 . . . Note=PAS +P42950 UniProtKB DNA binding 20 48 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P42950 UniProtKB Sequence conflict 611 611 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32835 1 219 +P32835 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P32835 UniProtKB Chain 2 219 . . . ID=PRO_0000208733;Note=GTP-binding nuclear protein GSP1/CNR1 +P32835 UniProtKB Nucleotide binding 20 27 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62825 +P32835 UniProtKB Nucleotide binding 124 127 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62825 +P32835 UniProtKB Nucleotide binding 152 154 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62825 +P32835 UniProtKB Binding site 70 70 . . . Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62825 +P32835 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P32835 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P32835 UniProtKB Beta strand 12 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P32835 UniProtKB Helix 25 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P32835 UniProtKB Beta strand 46 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P32835 UniProtKB Beta strand 59 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P32835 UniProtKB Helix 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P32835 UniProtKB Helix 78 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P32835 UniProtKB Beta strand 87 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P32835 UniProtKB Helix 97 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P32835 UniProtKB Helix 103 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P32835 UniProtKB Beta strand 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICQ +P32835 UniProtKB Beta strand 119 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P32835 UniProtKB Beta strand 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P32835 UniProtKB Helix 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P32835 UniProtKB Helix 141 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P32835 UniProtKB Beta strand 147 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P32835 UniProtKB Turn 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P32835 UniProtKB Turn 157 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P32835 UniProtKB Helix 161 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P32835 UniProtKB Helix 200 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +P32835 UniProtKB Turn 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M1I +##sequence-region Q07729 1 489 +Q07729 UniProtKB Chain 1 489 . . . ID=PRO_0000122302;Note=Probable guanine deaminase +Q07729 UniProtKB Region 102 105 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2T3 +Q07729 UniProtKB Region 231 232 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2T3 +Q07729 UniProtKB Region 258 261 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2T3 +Q07729 UniProtKB Metal binding 100 100 . . . Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2T3 +Q07729 UniProtKB Metal binding 102 102 . . . Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2T3 +Q07729 UniProtKB Metal binding 258 258 . . . Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2T3 +Q07729 UniProtKB Metal binding 348 348 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2T3 +Q07729 UniProtKB Binding site 348 348 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2T3 +##sequence-region P53551 1 258 +P53551 UniProtKB Chain 1 258 . . . ID=PRO_0000196001;Note=Histone H1 +P53551 UniProtKB Domain 43 117 . . . Note=H15 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00837 +P53551 UniProtKB Domain 176 251 . . . Note=H15 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00837 +P53551 UniProtKB Modified residue 174 174 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P53551 UniProtKB Sequence conflict 8 8 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53551 UniProtKB Helix 47 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UHM +P53551 UniProtKB Helix 66 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UHM +P53551 UniProtKB Turn 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UHM +P53551 UniProtKB Beta strand 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UHM +P53551 UniProtKB Helix 86 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UHM +P53551 UniProtKB Beta strand 102 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UHM +P53551 UniProtKB Beta strand 112 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UHM +P53551 UniProtKB Helix 180 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USS +P53551 UniProtKB Helix 191 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YQA +P53551 UniProtKB Helix 199 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USS +P53551 UniProtKB Turn 210 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USS +P53551 UniProtKB Helix 220 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USS +P53551 UniProtKB Beta strand 235 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USS +P53551 UniProtKB Beta strand 243 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YQA +P53551 UniProtKB Beta strand 247 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1USS +##sequence-region P14064 1 554 +P14064 UniProtKB Chain 1 554 . . . ID=PRO_0000083900;Note=Transcriptional activator HAP4 +P14064 UniProtKB Region 1 327 . . . Note=Probably encodes all the information necessary to anchor HAP4 to HAP2/3 +P14064 UniProtKB Region 124 300 . . . Note=Activation domain 1 +P14064 UniProtKB Region 359 476 . . . Note=Activation domain 2 +P14064 UniProtKB Compositional bias 54 80 . . . Note=Arg/Lys-rich (basic) +P14064 UniProtKB Compositional bias 90 113 . . . Note=Asn-rich +P14064 UniProtKB Compositional bias 107 113 . . . Note=Poly-Asn +P14064 UniProtKB Compositional bias 424 471 . . . Note=Asp/Glu-rich (acidic) +P14064 UniProtKB Compositional bias 519 549 . . . Note=Asp/Glu-rich (acidic) +P14064 UniProtKB Mutagenesis 148 151 . . . Note=Greatly diminishes transcriptional activation. FLKF->SSKS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15075264;Dbxref=PMID:15075264 +P14064 UniProtKB Mutagenesis 390 394 . . . Note=Greatly diminishes transcriptional activation. IWNYL->SSNSS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15075264;Dbxref=PMID:15075264 +P14064 UniProtKB Mutagenesis 427 430 . . . Note=Greatly diminishes transcriptional activation. YLFL->SSSS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15075264;Dbxref=PMID:15075264 +P14064 UniProtKB Mutagenesis 456 459 . . . Note=Greatly diminishes transcriptional activation. FSYL->SSSS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15075264;Dbxref=PMID:15075264 +P14064 UniProtKB Mutagenesis 466 467 . . . Note=Abolishes transcriptional activation. LM->SS +P14064 UniProtKB Mutagenesis 466 466 . . . Note=Greatly diminishes transcriptional activation. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15075264;Dbxref=PMID:15075264 +P14064 UniProtKB Mutagenesis 467 467 . . . Note=Abolishes transcriptional activation. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15075264;Dbxref=PMID:15075264 +P14064 UniProtKB Sequence conflict 160 160 . . . Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12341 1 374 +Q12341 UniProtKB Chain 1 374 . . . ID=PRO_0000083903;Note=Histone acetyltransferase type B catalytic subunit +Q12341 UniProtKB Domain 135 303 . . . Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532 +Q12341 UniProtKB Region 42 44 . . . Note=Interaction with histone H4 N-terminus;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250 +Q12341 UniProtKB Region 194 196 . . . Note=Interaction with histone H4 N-terminus;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250 +Q12341 UniProtKB Region 197 205 . . . Note=Interaction with HAT2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24835250,ECO:0000269|PubMed:8858151;Dbxref=PMID:24835250,PMID:8858151 +Q12341 UniProtKB Region 220 222 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24835250,ECO:0000269|PubMed:9727486;Dbxref=PMID:24835250,PMID:9727486 +Q12341 UniProtKB Region 227 233 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24835250,ECO:0000269|PubMed:9727486;Dbxref=PMID:24835250,PMID:9727486 +Q12341 UniProtKB Compositional bias 314 317 . . . Note=Poly-Leu +Q12341 UniProtKB Active site 255 255 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:24835250;Dbxref=PMID:24835250 +Q12341 UniProtKB Binding site 258 258 . . . Note=Acetyl-CoA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24835250,ECO:0000269|PubMed:9727486;Dbxref=PMID:24835250,PMID:9727486 +Q12341 UniProtKB Binding site 267 267 . . . Note=Acetyl-CoA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9727486;Dbxref=PMID:9727486 +Q12341 UniProtKB Site 174 174 . . . Note=Interaction with histone H4 N-terminus;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250 +Q12341 UniProtKB Modified residue 354 354 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12341 UniProtKB Mutagenesis 197 197 . . . Note=Abolishes interaction with HAT2. W->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250 +Q12341 UniProtKB Mutagenesis 199 199 . . . Note=Abolishes interaction with HAT2. Y->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250 +Q12341 UniProtKB Mutagenesis 202 202 . . . Note=Impairs interaction with HAT2. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250 +Q12341 UniProtKB Mutagenesis 205 205 . . . Note=Abolishes interaction with HAT2. F->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250 +Q12341 UniProtKB Mutagenesis 214 214 . . . Note=Impairs interaction with HAT2. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250 +Q12341 UniProtKB Sequence conflict 87 87 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12341 UniProtKB Helix 8 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Beta strand 12 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Helix 15 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Beta strand 19 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Helix 37 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Turn 41 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BOB +Q12341 UniProtKB Beta strand 45 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Beta strand 53 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Turn 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Beta strand 65 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Beta strand 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Beta strand 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Helix 83 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Beta strand 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Helix 101 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Helix 117 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Beta strand 121 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Beta strand 133 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Helix 144 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Helix 155 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Beta strand 175 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Turn 182 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Beta strand 187 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Helix 202 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Beta strand 213 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Helix 224 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Beta strand 228 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Helix 231 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Beta strand 249 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Helix 259 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Helix 278 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Helix 290 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +Q12341 UniProtKB Helix 304 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +##sequence-region P38523 1 228 +##sequence-region P41921 1 483 +P41921 UniProtKB Chain 1 483 . . . ID=PRO_0000067972;Note=Glutathione reductase +P41921 UniProtKB Nucleotide binding 53 61 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41921 UniProtKB Active site 472 472 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41921 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P41921 UniProtKB Disulfide bond 61 66 . . . Note=Redox-active;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41921 UniProtKB Alternative sequence 1 16 . . . ID=VSP_058124;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41921 UniProtKB Sequence conflict 315 315 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41921 UniProtKB Sequence conflict 428 428 . . . Note=C->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41921 UniProtKB Beta strand 23 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 33 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 49 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 59 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 66 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Turn 83 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 105 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 132 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 147 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 157 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 170 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 187 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 198 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 207 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 222 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 228 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 238 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 254 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 261 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 273 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 282 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 295 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 303 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 329 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 333 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 342 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 360 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 374 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 382 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 389 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 398 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 401 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 411 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 422 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Turn 430 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Beta strand 434 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 445 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 462 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +P41921 UniProtKB Helix 476 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HQM +##sequence-region P32836 1 220 +P32836 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32835 +P32836 UniProtKB Chain 2 220 . . . ID=PRO_0000208734;Note=GTP-binding nuclear protein GSP2/CNR2 +P32836 UniProtKB Nucleotide binding 21 28 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62825 +P32836 UniProtKB Nucleotide binding 125 128 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62825 +P32836 UniProtKB Nucleotide binding 153 155 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62825 +P32836 UniProtKB Binding site 71 71 . . . Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62825 +P32836 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32835 +P32836 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32835 +##sequence-region Q00582 1 310 +Q00582 UniProtKB Chain 1 310 . . . ID=PRO_0000122486;Note=GTP-binding protein GTR1 +Q00582 UniProtKB Nucleotide binding 13 20 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q00582 UniProtKB Nucleotide binding 61 65 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00582 UniProtKB Nucleotide binding 126 129 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00582 UniProtKB Beta strand 8 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Helix 19 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Helix 33 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Beta strand 43 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Turn 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Beta strand 55 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Helix 66 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Turn 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Helix 77 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Beta strand 85 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Helix 98 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Beta strand 120 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Helix 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Helix 133 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Turn 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Beta strand 160 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Helix 170 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Helix 186 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Beta strand 202 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Turn 210 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Beta strand 215 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Helix 242 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Helix 258 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Beta strand 264 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Turn 270 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Beta strand 273 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Beta strand 282 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Helix 295 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +Q00582 UniProtKB Turn 302 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +##sequence-region P53290 1 341 +P53290 UniProtKB Chain 1 341 . . . ID=PRO_0000122487;Note=GTP-binding protein GTR2 +P53290 UniProtKB Nucleotide binding 16 23 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53290 UniProtKB Nucleotide binding 124 127 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53290 UniProtKB Beta strand 12 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Helix 24 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Helix 36 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Turn 42 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ARZ +P53290 UniProtKB Beta strand 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Beta strand 54 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Beta strand 58 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Beta strand 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Helix 74 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Beta strand 84 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Helix 98 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Beta strand 118 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Helix 132 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Beta strand 150 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Beta strand 159 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Beta strand 166 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Helix 170 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Helix 186 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Helix 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Beta strand 199 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Beta strand 216 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Helix 225 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Beta strand 270 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Beta strand 280 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Beta strand 287 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +P53290 UniProtKB Helix 303 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R7W +##sequence-region P39996 1 337 +P39996 UniProtKB Chain 1 337 . . . ID=PRO_0000202611;Note=Glutathione transferase 3 +P39996 UniProtKB Topological domain 1 239 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39996 UniProtKB Transmembrane 240 260 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39996 UniProtKB Topological domain 261 313 . . . Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39996 UniProtKB Transmembrane 314 336 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39996 UniProtKB Topological domain 337 337 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39996 UniProtKB Modified residue 66 66 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39996 UniProtKB Modified residue 72 72 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39996 UniProtKB Modified residue 99 99 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39996 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P38970 1 855 +P38970 UniProtKB Chain 1 855 . . . ID=PRO_0000085988;Note=Serine/threonine-protein kinase HAL5 +P38970 UniProtKB Domain 503 837 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38970 UniProtKB Nucleotide binding 509 517 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38970 UniProtKB Compositional bias 369 377 . . . Note=Poly-Gln +P38970 UniProtKB Active site 688 688 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P38970 UniProtKB Binding site 546 546 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38970 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38970 UniProtKB Modified residue 19 19 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38970 UniProtKB Modified residue 68 68 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38970 UniProtKB Modified residue 72 72 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38970 UniProtKB Modified residue 160 160 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38970 UniProtKB Modified residue 273 273 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38970 UniProtKB Modified residue 277 277 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38970 UniProtKB Modified residue 324 324 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38970 UniProtKB Modified residue 333 333 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38970 UniProtKB Modified residue 336 336 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38970 UniProtKB Modified residue 358 358 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38970 UniProtKB Modified residue 391 391 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38970 UniProtKB Modified residue 395 395 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P53973 1 706 +P53973 UniProtKB Chain 1 706 . . . ID=PRO_0000114738;Note=Histone deacetylase HDA1 +P53973 UniProtKB Region 67 396 . . . Note=Histone deacetylase +P53973 UniProtKB Active site 206 206 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53973 UniProtKB Helix 457 473 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Beta strand 483 485 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Helix 487 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Beta strand 490 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Helix 496 498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Beta strand 500 508 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Beta strand 511 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Turn 518 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Helix 525 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Beta strand 529 531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Helix 535 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Turn 543 545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Beta strand 547 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Beta strand 558 561 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Helix 563 579 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Turn 580 583 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Beta strand 590 595 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Helix 596 598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Helix 599 608 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Turn 612 614 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Beta strand 615 623 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Helix 637 644 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Beta strand 646 650 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Helix 667 669 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Beta strand 672 674 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +P53973 UniProtKB Helix 680 696 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J8J +##sequence-region P38199 1 381 +P38199 UniProtKB Chain 1 381 . . . ID=PRO_0000050161;Note=Heterogeneous nuclear rnp K-like protein 2 +P38199 UniProtKB Domain 43 107 . . . Note=KH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117 +P38199 UniProtKB Domain 156 221 . . . Note=KH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117 +P38199 UniProtKB Domain 258 326 . . . Note=KH 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117 +P38199 UniProtKB Modified residue 358 358 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38199 UniProtKB Modified residue 360 360 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38199 UniProtKB Modified residue 362 362 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38199 UniProtKB Sequence conflict 362 362 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12361 1 961 +Q12361 UniProtKB Chain 1 961 . . . ID=PRO_0000195084;Note=G protein-coupled receptor GPR1 +Q12361 UniProtKB Topological domain 1 56 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12361 UniProtKB Transmembrane 57 79 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12361 UniProtKB Topological domain 80 91 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12361 UniProtKB Transmembrane 92 114 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12361 UniProtKB Topological domain 115 133 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12361 UniProtKB Transmembrane 134 156 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12361 UniProtKB Topological domain 157 178 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12361 UniProtKB Transmembrane 179 198 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12361 UniProtKB Topological domain 199 250 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12361 UniProtKB Transmembrane 251 273 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12361 UniProtKB Topological domain 274 619 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12361 UniProtKB Transmembrane 620 642 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12361 UniProtKB Topological domain 643 822 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12361 UniProtKB Transmembrane 823 843 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12361 UniProtKB Topological domain 844 961 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12361 UniProtKB Compositional bias 501 547 . . . Note=Poly-Asn +Q12361 UniProtKB Modified residue 373 373 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12361 UniProtKB Modified residue 903 903 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +##sequence-region P24814 1 1151 +P24814 UniProtKB Chain 1 1151 . . . ID=PRO_0000119968;Note=SCF E3 ubiquitin ligase complex F-box protein GRR1 +P24814 UniProtKB Domain 314 361 . . . Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080 +P24814 UniProtKB Repeat 399 423 . . . Note=LRR 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034 +P24814 UniProtKB Repeat 424 449 . . . Note=LRR 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034 +P24814 UniProtKB Repeat 450 475 . . . Note=LRR 3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034 +P24814 UniProtKB Repeat 476 501 . . . Note=LRR 4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034 +P24814 UniProtKB Repeat 502 527 . . . Note=LRR 5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034 +P24814 UniProtKB Repeat 528 553 . . . Note=LRR 6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034 +P24814 UniProtKB Repeat 554 582 . . . Note=LRR 7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034 +P24814 UniProtKB Repeat 583 608 . . . Note=LRR 8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034 +P24814 UniProtKB Repeat 609 634 . . . Note=LRR 9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034 +P24814 UniProtKB Repeat 635 660 . . . Note=LRR 10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034 +P24814 UniProtKB Repeat 661 685 . . . Note=LRR 11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034 +P24814 UniProtKB Repeat 686 714 . . . Note=LRR 12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034 +P24814 UniProtKB Repeat 715 740 . . . Note=LRR 13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922034;Dbxref=PMID:1922034 +P24814 UniProtKB Compositional bias 38 49 . . . Note=Poly-Asn +P24814 UniProtKB Compositional bias 1045 1124 . . . Note=Asn-rich +P24814 UniProtKB Modified residue 199 199 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P24814 UniProtKB Modified residue 300 300 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q04697 1 403 +Q04697 UniProtKB Chain 1 403 . . . ID=PRO_0000083865;Note=Glucose-signaling factor 2 +Q04697 UniProtKB Topological domain 1 177 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04697 UniProtKB Transmembrane 178 198 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04697 UniProtKB Topological domain 199 403 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04697 UniProtKB Coiled coil 330 388 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04697 UniProtKB Glycosylation 89 89 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04697 UniProtKB Glycosylation 173 173 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40582 1 234 +P40582 UniProtKB Chain 1 234 . . . ID=PRO_0000185987;Note=Glutathione S-transferase 1 +P40582 UniProtKB Domain 3 90 . . . Note=GST N-terminal +P40582 UniProtKB Domain 96 234 . . . Note=GST C-terminal +##sequence-region Q12390 1 233 +Q12390 UniProtKB Chain 1 233 . . . ID=PRO_0000185988;Note=Glutathione S-transferase 2 +Q12390 UniProtKB Domain 17 101 . . . Note=GST N-terminal +Q12390 UniProtKB Domain 106 233 . . . Note=GST C-terminal +Q12390 UniProtKB Region 85 86 . . . Note=Glutathione binding +Q12390 UniProtKB Binding site 29 29 . . . Note=Glutathione%3B via amide nitrogen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19851333;Dbxref=PMID:19851333 +Q12390 UniProtKB Binding site 58 58 . . . Note=Glutathione;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19851333;Dbxref=PMID:19851333 +Q12390 UniProtKB Binding site 72 72 . . . Note=Glutathione%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19851333;Dbxref=PMID:19851333 +Q12390 UniProtKB Binding site 133 133 . . . Note=Glutathione;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19851333;Dbxref=PMID:19851333 +Q12390 UniProtKB Mutagenesis 27 27 . . . Note=Reduced enzyme activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19851333;Dbxref=PMID:19851333 +Q12390 UniProtKB Mutagenesis 27 27 . . . Note=Loss of enzyme activity. G->C%2CF%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19851333;Dbxref=PMID:19851333 +Q12390 UniProtKB Mutagenesis 129 129 . . . Note=Reduced enzyme activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19851333;Dbxref=PMID:19851333 +Q12390 UniProtKB Mutagenesis 133 133 . . . Note=Loss of enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19851333;Dbxref=PMID:19851333 +Q12390 UniProtKB Beta strand 20 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +Q12390 UniProtKB Helix 28 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +Q12390 UniProtKB Helix 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +Q12390 UniProtKB Beta strand 47 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +Q12390 UniProtKB Helix 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +Q12390 UniProtKB Helix 57 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +Q12390 UniProtKB Helix 61 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +Q12390 UniProtKB Beta strand 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +Q12390 UniProtKB Beta strand 82 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +Q12390 UniProtKB Helix 86 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +Q12390 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +Q12390 UniProtKB Helix 107 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +Q12390 UniProtKB Helix 125 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +Q12390 UniProtKB Turn 141 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +Q12390 UniProtKB Helix 149 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +Q12390 UniProtKB Beta strand 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +Q12390 UniProtKB Helix 183 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +Q12390 UniProtKB Helix 207 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +Q12390 UniProtKB Helix 220 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IBH +##sequence-region P32806 1 458 +P32806 UniProtKB Chain 1 458 . . . ID=PRO_0000208013;Note=GTPase-activating protein GYP6 +P32806 UniProtKB Domain 33 316 . . . Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163 +P32806 UniProtKB Modified residue 436 436 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32806 UniProtKB Sequence conflict 413 413 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P43570 1 497 +P43570 UniProtKB Chain 1 497 . . . ID=PRO_0000208018;Note=GTPase-activating protein GYP8 +P43570 UniProtKB Domain 69 281 . . . Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163 +##sequence-region Q96VH4 1 193 +Q96VH4 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q96VH4 UniProtKB Chain 2 193 . . . ID=PRO_0000248448;Note=Putative nitroreductase HBN1 +Q96VH4 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region Q12096 1 491 +Q12096 UniProtKB Chain 1 491 . . . ID=PRO_0000087536;Note=Glucose N-acetyltransferase 1 +Q12096 UniProtKB Topological domain 1 10 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12096 UniProtKB Transmembrane 11 31 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12096 UniProtKB Topological domain 32 491 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12096 UniProtKB Motif 198 200 . . . Note=DXD +Q12096 UniProtKB Glycosylation 136 136 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12096 UniProtKB Glycosylation 177 177 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12096 UniProtKB Glycosylation 187 187 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12096 UniProtKB Glycosylation 425 425 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P46984 1 123 +P46984 UniProtKB Chain 1 123 . . . ID=PRO_0000203021;Note=EKC/KEOPS complex subunit GON7 +P46984 UniProtKB Beta strand 6 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA +P46984 UniProtKB Turn 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA +P46984 UniProtKB Beta strand 14 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA +P46984 UniProtKB Helix 66 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA +P46984 UniProtKB Helix 99 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA +##sequence-region P53130 1 126 +P53130 UniProtKB Chain 1 126 . . . ID=PRO_0000202745;Note=Heterotrimeric G protein gamma subunit GPG1 +##sequence-region P23797 1 304 +P23797 UniProtKB Chain 1 304 . . . ID=PRO_0000207170;Note=N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase +P23797 UniProtKB Topological domain 1 20 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23797 UniProtKB Transmembrane 21 38 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23797 UniProtKB Topological domain 39 304 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04080 1 534 +Q04080 UniProtKB Chain 1 534 . . . ID=PRO_0000218608;Note=GPI transamidase component GPI17 +Q04080 UniProtKB Topological domain 1 8 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04080 UniProtKB Transmembrane 9 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04080 UniProtKB Topological domain 30 472 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04080 UniProtKB Transmembrane 473 493 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04080 UniProtKB Topological domain 494 534 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04080 UniProtKB Glycosylation 100 100 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04080 UniProtKB Glycosylation 170 170 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04080 UniProtKB Glycosylation 228 228 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04080 UniProtKB Glycosylation 247 247 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04080 UniProtKB Glycosylation 299 299 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38211 1 433 +P38211 UniProtKB Chain 1 433 . . . ID=PRO_0000014309;Note=GPI mannosyltransferase 2 +P38211 UniProtKB Topological domain 1 1 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Transmembrane 2 22 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Topological domain 23 109 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Transmembrane 110 130 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Topological domain 131 161 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Transmembrane 162 182 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Topological domain 183 215 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Transmembrane 216 236 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Topological domain 237 243 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Transmembrane 244 264 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Topological domain 265 318 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Transmembrane 319 339 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Topological domain 340 350 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Transmembrane 351 371 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Topological domain 372 409 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Transmembrane 410 430 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Topological domain 431 433 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Glycosylation 69 69 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Glycosylation 101 101 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38211 UniProtKB Sequence conflict 187 187 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38211 UniProtKB Sequence conflict 187 187 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40367 1 830 +P40367 UniProtKB Signal peptide 1 32 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Chain 33 830 . . . ID=PRO_0000203059;Note=GPI ethanolamine phosphate transferase 2 +P40367 UniProtKB Topological domain 33 321 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Transmembrane 322 342 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Topological domain 343 405 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Transmembrane 406 426 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Topological domain 427 439 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Transmembrane 440 460 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Topological domain 461 469 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Transmembrane 470 490 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Topological domain 491 533 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Transmembrane 534 554 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Topological domain 555 598 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Transmembrane 599 619 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Topological domain 620 651 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Transmembrane 652 672 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Topological domain 673 682 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Transmembrane 683 703 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Topological domain 704 724 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Transmembrane 725 745 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Topological domain 746 768 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Transmembrane 769 789 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Topological domain 790 805 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Transmembrane 806 826 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Topological domain 827 830 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Glycosylation 145 145 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Glycosylation 185 185 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Glycosylation 298 298 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Glycosylation 506 506 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40367 UniProtKB Mutagenesis 153 154 . . . Note=In GPI7-2%3B temperature-sensitive mutant that shows defects in cell separation and a daughter cell-specific growth defect. DD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15452134;Dbxref=PMID:15452134 +##sequence-region P47122 1 385 +P47122 UniProtKB Chain 1 385 . . . ID=PRO_0000203101;Note=GPN-loop GTPase 1 +P47122 UniProtKB Nucleotide binding 13 18 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9 +P47122 UniProtKB Nucleotide binding 173 176 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9 +P47122 UniProtKB Motif 70 72 . . . Note=Gly-Pro-Asn (GPN)-loop%3B involved in dimer interface;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9 +P47122 UniProtKB Site 72 72 . . . Note=Stabilizes the phosphate intermediate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UYR9 +P47122 UniProtKB Modified residue 304 304 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47122 UniProtKB Modified residue 308 308 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47122 UniProtKB Modified residue 313 313 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P47122 UniProtKB Modified residue 352 352 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P47122 UniProtKB Cross-link 369 369 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P47122 UniProtKB Mutagenesis 106 106 . . . Note=Impairs nuclear localization of RNAPII. Completely abolishes RNAPII binding. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21844196;Dbxref=PMID:21844196 +P47122 UniProtKB Mutagenesis 110 110 . . . Note=Impairs nuclear localization of RNAPII%2C but does not impair RNAPII binding. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21844196;Dbxref=PMID:21844196 +P47122 UniProtKB Mutagenesis 112 112 . . . Note=Impairs heterodimer formation with GPN2 and GPN3. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23324351;Dbxref=PMID:23324351 +P47122 UniProtKB Beta strand 4 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Helix 16 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Beta strand 35 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Beta strand 51 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Turn 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Helix 60 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCI +P47122 UniProtKB Helix 73 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Helix 86 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Turn 96 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Beta strand 101 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Helix 112 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Helix 118 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Beta strand 133 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Helix 141 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Helix 147 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Beta strand 168 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Helix 175 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Helix 182 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Helix 216 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Beta strand 232 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Turn 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +P47122 UniProtKB Helix 245 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HCN +##sequence-region P38143 1 162 +P38143 UniProtKB Chain 1 162 . . . ID=PRO_0000066642;Note=Glutathione peroxidase-like peroxiredoxin 2 +P38143 UniProtKB Active site 37 37 . . . Note=Cysteine sulfenic acid (-SOH) intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16251189;Dbxref=PMID:16251189 +P38143 UniProtKB Disulfide bond 37 83 . . . Note=Redox-active;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16251189;Dbxref=PMID:16251189 +P38143 UniProtKB Mutagenesis 37 37 . . . Note=Prevents oxidation of the protein. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16251189;Dbxref=PMID:16251189 +P38143 UniProtKB Mutagenesis 83 83 . . . Note=Prevents oxidation of the protein. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16251189;Dbxref=PMID:16251189 +##sequence-region Q12068 1 342 +Q12068 UniProtKB Chain 1 342 . . . ID=PRO_0000215576;Note=NADPH-dependent methylglyoxal reductase GRE2 +Q12068 UniProtKB Nucleotide binding 7 12 . . . Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24879127;Dbxref=PMID:24879127 +Q12068 UniProtKB Nucleotide binding 57 58 . . . Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24879127;Dbxref=PMID:24879127 +Q12068 UniProtKB Active site 169 169 . . . Note=Proton donor;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24879127;Dbxref=PMID:24879127 +Q12068 UniProtKB Binding site 32 32 . . . Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24879127;Dbxref=PMID:24879127 +Q12068 UniProtKB Binding site 36 36 . . . Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24879127;Dbxref=PMID:24879127 +Q12068 UniProtKB Binding site 165 165 . . . Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24879127;Dbxref=PMID:24879127 +Q12068 UniProtKB Binding site 169 169 . . . Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24879127;Dbxref=PMID:24879127 +Q12068 UniProtKB Binding site 199 199 . . . Note=NADP%3B via amide nitrogen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24879127;Dbxref=PMID:24879127 +Q12068 UniProtKB Binding site 216 216 . . . Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24879127;Dbxref=PMID:24879127 +Q12068 UniProtKB Modified residue 333 333 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12068 UniProtKB Mutagenesis 9 9 . . . Note=Alters cofactor preference of the enzyme to be able to use as well NAD instead of NADP. N->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20480039;Dbxref=PMID:20480039 +Q12068 UniProtKB Beta strand 3 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Turn 7 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Helix 11 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Beta strand 27 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Helix 34 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Beta strand 50 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Turn 61 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Helix 65 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Turn 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Beta strand 77 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Beta strand 89 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Helix 92 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Helix 97 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Turn 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Beta strand 121 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Helix 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Helix 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Beta strand 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Helix 156 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Helix 161 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Turn 183 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Beta strand 190 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Beta strand 198 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Helix 206 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Helix 215 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Beta strand 236 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Helix 242 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Turn 257 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Beta strand 262 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Beta strand 268 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Helix 272 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Turn 284 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Turn 299 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Beta strand 307 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Helix 311 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +Q12068 UniProtKB Helix 324 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVC +##sequence-region Q08220 1 491 +Q08220 UniProtKB Chain 1 491 . . . ID=PRO_0000211266;Note=Glutathione synthetase +Q08220 UniProtKB Nucleotide binding 382 391 . . . Note=ATP +Q08220 UniProtKB Nucleotide binding 415 418 . . . Note=ATP +Q08220 UniProtKB Region 150 153 . . . Note=Substrate binding +Q08220 UniProtKB Region 228 230 . . . Note=Substrate binding +Q08220 UniProtKB Region 285 288 . . . Note=Substrate binding +Q08220 UniProtKB Region 478 479 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08220 UniProtKB Metal binding 146 146 . . . Note=Magnesium +Q08220 UniProtKB Metal binding 148 148 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08220 UniProtKB Metal binding 386 386 . . . Note=Magnesium +Q08220 UniProtKB Binding site 128 128 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12467574;Dbxref=PMID:12467574 +Q08220 UniProtKB Binding site 146 146 . . . Note=ATP +Q08220 UniProtKB Binding site 234 234 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12467574;Dbxref=PMID:12467574 +Q08220 UniProtKB Binding site 324 324 . . . Note=ATP +Q08220 UniProtKB Binding site 393 393 . . . Note=ATP +Q08220 UniProtKB Binding site 442 442 . . . Note=ATP +Q08220 UniProtKB Binding site 467 467 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08220 UniProtKB Binding site 469 469 . . . Note=ATP +Q08220 UniProtKB Binding site 475 475 . . . Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08220 UniProtKB Helix 8 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 34 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 40 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 46 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 51 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 55 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 85 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Turn 97 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 101 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 123 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 139 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 155 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 183 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 191 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 219 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 231 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 249 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 254 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 261 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Turn 265 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 270 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Turn 273 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 278 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 290 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 296 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 308 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 316 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 324 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 333 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Turn 337 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 343 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 356 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 360 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 363 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 376 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 379 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 394 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 397 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Helix 406 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 412 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 428 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 433 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 439 451 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 456 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 472 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 477 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 483 485 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +Q08220 UniProtKB Beta strand 488 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M0W +##sequence-region Q04806 1 366 +Q04806 UniProtKB Chain 1 366 . . . ID=PRO_0000203338;Note=Glutathione S-transferase omega-like 3 +Q04806 UniProtKB Domain 197 349 . . . Note=GST C-terminal +Q04806 UniProtKB Active site 46 46 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P40956 1 396 +P40956 UniProtKB Chain 1 396 . . . ID=PRO_0000074226;Note=Protein GTS1 +P40956 UniProtKB Domain 14 141 . . . Note=Arf-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288 +P40956 UniProtKB Domain 193 234 . . . Note=UBA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212 +P40956 UniProtKB Zinc finger 30 53 . . . Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288 +P40956 UniProtKB Compositional bias 234 237 . . . Note=Poly-Ser +P40956 UniProtKB Compositional bias 311 396 . . . Note=Gln-rich +P40956 UniProtKB Compositional bias 319 327 . . . Note=Poly-Gln +P40956 UniProtKB Modified residue 153 153 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40956 UniProtKB Modified residue 181 181 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40956 UniProtKB Modified residue 184 184 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P40956 UniProtKB Modified residue 187 187 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40956 UniProtKB Modified residue 240 240 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40956 UniProtKB Modified residue 249 249 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38625 1 525 +P38625 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7483834;Dbxref=PMID:7483834 +P38625 UniProtKB Chain 2 525 . . . ID=PRO_0000140258;Note=GMP synthase [glutamine-hydrolyzing] +P38625 UniProtKB Domain 13 202 . . . Note=Glutamine amidotransferase type-1 +P38625 UniProtKB Domain 203 400 . . . Note=GMPS ATP-PPase +P38625 UniProtKB Nucleotide binding 231 237 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38625 UniProtKB Active site 89 89 . . . Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38625 UniProtKB Active site 176 176 . . . Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38625 UniProtKB Active site 178 178 . . . Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38625 UniProtKB Cross-link 241 241 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38625 UniProtKB Cross-link 426 426 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38625 UniProtKB Sequence conflict 325 325 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P46943 1 645 +P46943 UniProtKB Chain 1 645 . . . ID=PRO_0000091560;Note=Translation factor GUF1%2C mitochondrial +P46943 UniProtKB Domain 44 228 . . . Note=tr-type G +P46943 UniProtKB Nucleotide binding 53 60 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03137 +P46943 UniProtKB Nucleotide binding 120 124 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03137 +P46943 UniProtKB Nucleotide binding 174 177 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03137 +P46943 UniProtKB Sequence conflict 260 260 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46943 UniProtKB Sequence conflict 354 354 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46943 UniProtKB Sequence conflict 374 374 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46943 UniProtKB Sequence conflict 559 559 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P42944 1 551 +P42944 UniProtKB Chain 1 551 . . . ID=PRO_0000083488;Note=Protein GZF3 +P42944 UniProtKB Zinc finger 131 155 . . . Note=GATA-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00094 +##sequence-region Q12180 1 1030 +Q12180 UniProtKB Chain 1 1030 . . . ID=PRO_0000233012;Note=Halotolerance protein 9 +Q12180 UniProtKB DNA binding 136 166 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +Q12180 UniProtKB Modified residue 221 221 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12180 UniProtKB Modified residue 937 937 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region Q05580 1 639 +Q05580 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q05580 UniProtKB Chain 2 639 . . . ID=PRO_0000253811;Note=E3 ubiquitin-protein ligase HEL2 +Q05580 UniProtKB Domain 222 292 . . . Note=LIM zinc-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125 +Q05580 UniProtKB Zinc finger 64 104 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +Q05580 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q05580 UniProtKB Modified residue 57 57 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q05580 UniProtKB Modified residue 354 354 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P36014 1 167 +P36014 UniProtKB Chain 1 167 . . . ID=PRO_0000066641;Note=Glutathione peroxidase-like peroxiredoxin 1 +P36014 UniProtKB Active site 36 36 . . . Note=Cysteine sulfenic acid (-SOH) intermediate;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:20572871,ECO:0000305|PubMed:22659048;Dbxref=PMID:20572871,PMID:22659048 +P36014 UniProtKB Disulfide bond 36 82 . . . Note=Redox-active;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:20572871;Dbxref=PMID:20572871 +P36014 UniProtKB Mutagenesis 36 36 . . . Note=Prevents oxidation of the protein. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20572871;Dbxref=PMID:20572871 +##sequence-region Q07845 1 632 +Q07845 UniProtKB Chain 1 632 . . . ID=PRO_0000087597;Note=Polynucleotide 5'-hydroxyl-kinase GRC3 +Q07845 UniProtKB Nucleotide binding 246 253 . . . Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q07845 UniProtKB Mutagenesis 252 252 . . . Note=Abolishes kinase activity and termination by RNA polymerase I. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20814424;Dbxref=PMID:20814424 +Q07845 UniProtKB Mutagenesis 253 253 . . . Note=Abolishes kinase activity and termination by RNA polymerase I. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20814424;Dbxref=PMID:20814424 +##sequence-region P47026 1 490 +P47026 UniProtKB Chain 1 490 . . . ID=PRO_0000215188;Note=GPI-anchored wall transfer protein 1 +P47026 UniProtKB Topological domain 1 19 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Transmembrane 20 40 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Topological domain 41 54 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Transmembrane 55 75 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Topological domain 76 76 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Transmembrane 77 97 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Topological domain 98 128 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Transmembrane 129 149 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Topological domain 150 157 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Transmembrane 158 178 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Topological domain 179 199 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Transmembrane 200 220 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Topological domain 221 231 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Transmembrane 232 252 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Topological domain 253 257 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Transmembrane 258 278 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Topological domain 279 301 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Transmembrane 302 322 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Topological domain 323 356 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Transmembrane 357 377 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Topological domain 378 390 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Transmembrane 391 411 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Topological domain 412 435 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Transmembrane 436 456 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Topological domain 457 460 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Transmembrane 461 481 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Topological domain 482 490 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47026 UniProtKB Mutagenesis 8 8 . . . Note=In gwt1-10%3B impairs the transport of detergent-resistant microdomain-associated membrane proteins TAT2 and FUR4. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16361252;Dbxref=PMID:16361252 +P47026 UniProtKB Mutagenesis 63 64 . . . Note=In gwt1-20%3B temperature sensitive mutant that induces a delay in export of GPI-anchored proteins. WV->RA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12714589;Dbxref=PMID:12714589 +P47026 UniProtKB Mutagenesis 132 132 . . . Note=Resistant to the drug 1-[4-butylbenzyl]isoquinoline (BIQ). G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12753194;Dbxref=PMID:12753194 +P47026 UniProtKB Mutagenesis 209 209 . . . Note=In gwt1-28%3B temperature sensitive mutant that induces a delay in export of GPI-anchored proteins%3B when associated with D-259. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12714589;Dbxref=PMID:12714589 +P47026 UniProtKB Mutagenesis 259 259 . . . Note=In gwt1-28%3B temperature sensitive mutant that induces a delay in export of GPI-anchored proteins%3B when associated with P-209. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12714589;Dbxref=PMID:12714589 +P47026 UniProtKB Mutagenesis 330 330 . . . Note=In gwt1-16%3B temperature sensitive mutant that induces a delay in export of GPI-anchored proteins%3B when associated with P-362 and A-479. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12714589;Dbxref=PMID:12714589 +P47026 UniProtKB Mutagenesis 362 362 . . . Note=In gwt1-16%3B temperature sensitive mutant that induces a delay in export of GPI-anchored proteins%3B when associated with S-330 and A-479. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12714589;Dbxref=PMID:12714589 +P47026 UniProtKB Mutagenesis 397 397 . . . Note=Resistant to the drug 1-[4-butylbenzyl]isoquinoline (BIQ). V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12753194;Dbxref=PMID:12753194 +P47026 UniProtKB Mutagenesis 479 479 . . . Note=In gwt1-16%3B temperature sensitive mutant that induces a delay in export of GPI-anchored proteins%3B when associated with S-330 and P-362. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12714589;Dbxref=PMID:12714589 +##sequence-region P53258 1 950 +P53258 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53258 UniProtKB Chain 2 950 . . . ID=PRO_0000208011;Note=GTPase-activating protein GYP2 +P53258 UniProtKB Domain 29 116 . . . Note=GRAM +P53258 UniProtKB Domain 244 432 . . . Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163 +P53258 UniProtKB Domain 602 637 . . . Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P53258 UniProtKB Domain 638 673 . . . Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P53258 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53258 UniProtKB Modified residue 764 764 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53258 UniProtKB Modified residue 871 871 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +##sequence-region Q12344 1 894 +Q12344 UniProtKB Chain 1 894 . . . ID=PRO_0000240365;Note=GTPase-activating protein GYP5 +Q12344 UniProtKB Domain 451 630 . . . Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163 +Q12344 UniProtKB Coiled coil 732 872 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12344 UniProtKB Modified residue 25 25 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12344 UniProtKB Modified residue 30 30 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12344 UniProtKB Modified residue 89 89 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12344 UniProtKB Modified residue 389 389 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12344 UniProtKB Mutagenesis 496 496 . . . Note=Loss of GAP activity. R->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12189143;Dbxref=PMID:12189143 +##sequence-region P27472 1 705 +P27472 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23337 +P27472 UniProtKB Chain 2 705 . . . ID=PRO_0000194774;Note=Glycogen [starch] synthase isoform 2 +P27472 UniProtKB Binding site 20 20 . . . Note=UDP-glucose;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P27472 UniProtKB Modified residue 159 159 . . . Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27472 UniProtKB Modified residue 363 363 . . . Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27472 UniProtKB Modified residue 467 467 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P27472 UniProtKB Modified residue 651 651 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +P27472 UniProtKB Modified residue 655 655 . . . Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:9584169;Dbxref=PMID:15665377,PMID:18407956,PMID:9584169 +P27472 UniProtKB Modified residue 661 661 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27472 UniProtKB Modified residue 663 663 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27472 UniProtKB Modified residue 668 668 . . . Note=Phosphothreonine%3B by PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9584169;Dbxref=PMID:9584169 +P27472 UniProtKB Sequence conflict 248 248 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27472 UniProtKB Sequence conflict 535 535 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27472 UniProtKB Sequence conflict 622 622 . . . Note=F->FF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27472 UniProtKB Beta strand 4 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Turn 15 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 23 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 43 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Turn 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 54 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KQM +P27472 UniProtKB Helix 74 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Turn 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 90 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 102 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 109 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 115 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 135 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 160 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 170 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 175 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 187 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 196 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 203 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 209 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 213 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 218 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 228 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 241 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 249 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 259 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 264 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 273 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NCH +P27472 UniProtKB Helix 281 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Turn 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 309 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 312 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Turn 323 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 328 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 350 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 361 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 366 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Turn 400 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KQ2 +P27472 UniProtKB Beta strand 407 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 413 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 419 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 442 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 450 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 454 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 471 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 486 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 492 498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 500 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 507 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 513 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 525 528 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 532 538 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 543 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 551 554 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Beta strand 557 559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 561 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 580 592 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 593 597 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 599 617 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 619 624 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +P27472 UniProtKB Helix 635 638 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NB0 +##sequence-region Q06201 1 188 +Q06201 UniProtKB Chain 1 188 . . . ID=PRO_0000247355;Note=Grand meiotic recombination cluster protein 2 +##sequence-region P36125 1 273 +P36125 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P36125 UniProtKB Chain 2 273 . . . ID=PRO_0000203205;Note=Protein GMH1 +P36125 UniProtKB Topological domain 2 89 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36125 UniProtKB Transmembrane 90 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36125 UniProtKB Topological domain 111 134 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36125 UniProtKB Transmembrane 135 155 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36125 UniProtKB Topological domain 156 175 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36125 UniProtKB Transmembrane 176 196 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36125 UniProtKB Topological domain 197 216 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36125 UniProtKB Transmembrane 217 237 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36125 UniProtKB Topological domain 238 242 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36125 UniProtKB Transmembrane 243 263 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36125 UniProtKB Topological domain 264 273 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36125 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P41911 1 440 +P41911 UniProtKB Transit peptide 1 16 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41911 UniProtKB Chain 17 440 . . . ID=PRO_0000043410;Note=Glycerol-3-phosphate dehydrogenase [NAD(+)] 2%2C mitochondrial +P41911 UniProtKB Nucleotide binding 90 95 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41911 UniProtKB Region 359 360 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41911 UniProtKB Active site 294 294 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41911 UniProtKB Binding site 178 178 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41911 UniProtKB Binding site 201 201 . . . Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41911 UniProtKB Binding site 201 201 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41911 UniProtKB Binding site 234 234 . . . Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41911 UniProtKB Binding site 359 359 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41911 UniProtKB Binding site 388 388 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41911 UniProtKB Modified residue 70 70 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P41911 UniProtKB Modified residue 72 72 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P41911 UniProtKB Modified residue 75 75 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P53961 1 229 +P53961 UniProtKB Chain 1 229 . . . ID=PRO_0000087556;Note=Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI15 +P53961 UniProtKB Transmembrane 59 79 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53961 UniProtKB Transmembrane 101 121 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53961 UniProtKB Sequence conflict 10 10 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P49018 1 411 +P49018 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P49018 UniProtKB Chain 23 411 . . . ID=PRO_0000026532;Note=GPI-anchor transamidase +P49018 UniProtKB Topological domain 23 376 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P49018 UniProtKB Transmembrane 377 397 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P49018 UniProtKB Topological domain 398 411 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P49018 UniProtKB Active site 157 157 . . . . +P49018 UniProtKB Active site 199 199 . . . . +P49018 UniProtKB Glycosylation 256 256 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P49018 UniProtKB Glycosylation 346 346 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P49018 UniProtKB Disulfide bond 85 85 . . . Note=Interchain (with C-194 in GPI16);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49018 UniProtKB Mutagenesis 54 54 . . . Note=Partial loss of activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10727241;Dbxref=PMID:10727241 +P49018 UniProtKB Mutagenesis 60 60 . . . Note=No loss of activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10727241;Dbxref=PMID:10727241 +P49018 UniProtKB Mutagenesis 60 60 . . . Note=No loss of activity. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10727241;Dbxref=PMID:10727241 +P49018 UniProtKB Mutagenesis 85 85 . . . Note=No loss of activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10727241;Dbxref=PMID:10727241 +P49018 UniProtKB Mutagenesis 157 157 . . . Note=Loss of activity. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10727241,ECO:0000269|PubMed:10793132;Dbxref=PMID:10727241,PMID:10793132 +P49018 UniProtKB Mutagenesis 199 199 . . . Note=Loss of activity. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10727241,ECO:0000269|PubMed:10793132;Dbxref=PMID:10727241,PMID:10793132 +##sequence-region P16474 1 682 +P16474 UniProtKB Signal peptide 1 42 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16474 UniProtKB Chain 43 682 . . . ID=PRO_0000013587;Note=78 kDa glucose-regulated protein homolog +P16474 UniProtKB Motif 679 682 . . . Note=Prevents secretion from ER +P16474 UniProtKB Beta strand 53 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Beta strand 59 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Beta strand 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Beta strand 82 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Beta strand 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Beta strand 95 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Helix 99 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Helix 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Helix 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Helix 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Turn 119 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Helix 127 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Beta strand 137 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Beta strand 146 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Helix 162 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Beta strand 187 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Helix 198 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Beta strand 214 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Helix 221 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Turn 229 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Beta strand 238 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Beta strand 250 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Beta strand 261 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Helix 275 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Helix 298 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +P16474 UniProtKB Helix 302 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Turn 319 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Beta strand 323 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Beta strand 336 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Helix 344 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Helix 359 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Helix 373 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Beta strand 378 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Helix 384 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Helix 389 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Turn 399 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Turn 410 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Helix 413 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QFU +P16474 UniProtKB Beta strand 444 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X +P16474 UniProtKB Turn 449 451 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X +P16474 UniProtKB Beta strand 452 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X +P16474 UniProtKB Beta strand 462 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X +P16474 UniProtKB Beta strand 481 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X +P16474 UniProtKB Helix 493 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X +P16474 UniProtKB Beta strand 496 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X +P16474 UniProtKB Beta strand 517 523 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X +P16474 UniProtKB Beta strand 527 535 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X +P16474 UniProtKB Turn 536 538 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X +P16474 UniProtKB Beta strand 541 547 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X +P16474 UniProtKB Helix 555 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X +P16474 UniProtKB Helix 569 580 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H0X +##sequence-region P32477 1 678 +P32477 UniProtKB Chain 1 678 . . . ID=PRO_0000192572;Note=Glutamate--cysteine ligase +P32477 UniProtKB Sequence conflict 299 299 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32477 UniProtKB Sequence conflict 492 492 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32477 UniProtKB Sequence conflict 526 527 . . . Note=IL->MV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32477 UniProtKB Sequence conflict 542 542 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32477 UniProtKB Sequence conflict 550 550 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32477 UniProtKB Helix 12 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 16 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 19 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Beta strand 46 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Turn 60 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Beta strand 64 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 74 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Turn 78 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 83 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Beta strand 91 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Beta strand 101 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Beta strand 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 117 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Beta strand 149 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Turn 160 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Beta strand 168 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Turn 179 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 196 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Beta strand 214 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 240 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 244 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Beta strand 252 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 259 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Beta strand 266 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 276 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 289 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Beta strand 306 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 314 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Turn 326 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Turn 336 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 340 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 348 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Beta strand 361 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 377 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 388 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 404 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 423 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Turn 430 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 435 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Beta strand 447 451 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Beta strand 467 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 480 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Turn 500 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 510 519 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 525 528 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Beta strand 530 535 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Beta strand 537 539 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LVV +P32477 UniProtKB Beta strand 545 549 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 550 555 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Turn 557 559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 561 564 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 566 572 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 580 585 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Turn 587 589 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LVV +P32477 UniProtKB Helix 590 603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 610 619 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Beta strand 626 629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 632 646 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +P32477 UniProtKB Helix 650 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LVV +P32477 UniProtKB Helix 654 669 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IG5 +##sequence-region P48239 1 356 +P48239 UniProtKB Chain 1 356 . . . ID=PRO_0000202833;Note=Glutathione S-transferase omega-like 1 +P48239 UniProtKB Coiled coil 214 257 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48239 UniProtKB Active site 31 31 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P36156 1 370 +P36156 UniProtKB Chain 1 370 . . . ID=PRO_0000086922;Note=Glutathione S-transferase omega-like 2 +P36156 UniProtKB Domain 201 353 . . . Note=GST C-terminal +P36156 UniProtKB Active site 46 46 . . . Note=Nucleophile;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16709151;Dbxref=PMID:16709151 +P36156 UniProtKB Mutagenesis 46 46 . . . Note=Completely inactive as thiol transferase. No activity recovered against 1-chloro-2%2C4-dinitrobenzene (CDNB). C->S%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16709151;Dbxref=PMID:16709151 +P36156 UniProtKB Mutagenesis 51 51 . . . Note=No effect on thiol transferase activity. No effect on thiol transferase activity%3B when associated with D-173. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16709151;Dbxref=PMID:16709151 +P36156 UniProtKB Mutagenesis 173 173 . . . Note=No effect on thiol transferase activity. E->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16709151;Dbxref=PMID:16709151 +P36156 UniProtKB Mutagenesis 174 174 . . . Note=No effect on thiol transferase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16709151;Dbxref=PMID:16709151 +P36156 UniProtKB Mutagenesis 246 246 . . . Note=No effect on thiol transferase activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16709151;Dbxref=PMID:16709151 +P36156 UniProtKB Mutagenesis 280 280 . . . Note=No effect on thiol transferase activity. G->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16709151;Dbxref=PMID:16709151 +P36156 UniProtKB Mutagenesis 287 287 . . . Note=Abolishes thiol transferase activity. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16709151;Dbxref=PMID:16709151 +P36156 UniProtKB Beta strand 37 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Helix 47 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Turn 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Beta strand 65 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Helix 95 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Turn 101 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Helix 106 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKD +P36156 UniProtKB Turn 126 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Turn 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Helix 141 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Beta strand 160 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Turn 164 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Beta strand 168 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Helix 174 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Helix 184 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Helix 192 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Turn 202 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Helix 205 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Turn 219 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Helix 222 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Helix 232 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Helix 269 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Helix 285 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Turn 298 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Helix 301 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Helix 312 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Helix 317 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Helix 331 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Helix 339 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Turn 351 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +P36156 UniProtKB Beta strand 363 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LKB +##sequence-region P00815 1 799 +P00815 UniProtKB Chain 1 799 . . . ID=PRO_0000135914;Note=Histidine biosynthesis trifunctional protein +P00815 UniProtKB Region 1 229 . . . Note=Phosphoribosyl-AMP cyclohydrolase +P00815 UniProtKB Region 230 312 . . . Note=Phosphoribosyl-ATP pyrophosphohydrolase +P00815 UniProtKB Region 313 799 . . . Note=Histidinol dehydrogenase +P00815 UniProtKB Active site 687 687 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00815 UniProtKB Active site 688 688 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00815 UniProtKB Metal binding 618 618 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00815 UniProtKB Metal binding 621 621 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00815 UniProtKB Metal binding 721 721 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00815 UniProtKB Metal binding 780 780 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00815 UniProtKB Sequence conflict 53 53 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00815 UniProtKB Sequence conflict 386 386 . . . Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00815 UniProtKB Sequence conflict 402 403 . . . Note=AL->VF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00815 UniProtKB Sequence conflict 441 441 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00815 UniProtKB Sequence conflict 794 794 . . . Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53187 1 214 +P53187 UniProtKB Chain 1 214 . . . ID=PRO_0000084027;Note=Homologous-pairing protein 2 +P53187 UniProtKB Coiled coil 97 160 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53187 UniProtKB Sequence conflict 71 71 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12214 1 470 +Q12214 UniProtKB Chain 1 470 . . . ID=PRO_0000114726;Note=Histone deacetylase HOS1 +Q12214 UniProtKB Region 47 392 . . . Note=Histone deacetylase +Q12214 UniProtKB Active site 211 211 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12214 UniProtKB Modified residue 110 110 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q01448 1 625 +Q01448 UniProtKB Chain 1 625 . . . ID=PRO_0000084039;Note=Histone promoter control protein 2 +Q01448 UniProtKB Modified residue 47 47 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q01448 UniProtKB Modified residue 49 49 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q01448 UniProtKB Modified residue 435 435 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q05905 1 244 +Q05905 UniProtKB Chain 1 244 . . . ID=PRO_0000245329;Note=Protein HRI1 +Q05905 UniProtKB Modified residue 143 143 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q05905 UniProtKB Beta strand 3 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Beta strand 23 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Beta strand 32 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Turn 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Beta strand 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Beta strand 50 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Helix 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Beta strand 61 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Beta strand 67 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Beta strand 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Helix 81 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Beta strand 95 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Beta strand 107 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Beta strand 123 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Beta strand 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Beta strand 155 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Beta strand 165 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Beta strand 175 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Helix 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Beta strand 191 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Beta strand 204 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Helix 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Beta strand 229 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +Q05905 UniProtKB Beta strand 235 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RBY +##sequence-region Q05549 1 1077 +Q05549 UniProtKB Chain 1 1077 . . . ID=PRO_0000253813;Note=ATP-dependent helicase HRQ1 +Q05549 UniProtKB Domain 299 483 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q05549 UniProtKB Domain 521 678 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q05549 UniProtKB Nucleotide binding 312 319 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q05549 UniProtKB Motif 423 426 . . . Note=DEAH box +Q05549 UniProtKB Mutagenesis 318 318 . . . Note=Impairs helicase and ATPase activities. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23026052,ECO:0000269|PubMed:24682993;Dbxref=PMID:23026052,PMID:24682993 +##sequence-region P09950 1 548 +P09950 UniProtKB Transit peptide 1 22 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P09950 UniProtKB Chain 23 548 . . . ID=PRO_0000001245;Note=5-aminolevulinate synthase%2C mitochondrial +P09950 UniProtKB Compositional bias 26 62 . . . Note=Ala-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00001 +P09950 UniProtKB Active site 337 337 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079 +P09950 UniProtKB Binding site 91 91 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079 +P09950 UniProtKB Binding site 204 204 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079 +P09950 UniProtKB Binding site 223 223 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079 +P09950 UniProtKB Binding site 256 256 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079 +P09950 UniProtKB Binding site 284 284 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079 +P09950 UniProtKB Binding site 334 334 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079 +P09950 UniProtKB Binding site 366 366 . . . Note=Pyridoxal phosphate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079 +P09950 UniProtKB Binding site 367 367 . . . Note=Pyridoxal phosphate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079 +P09950 UniProtKB Binding site 452 452 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079 +P09950 UniProtKB Modified residue 337 337 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P18079 +P09950 UniProtKB Mutagenesis 275 275 . . . Note=Lethal in combination with a MCX1 disruption. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25957689;Dbxref=PMID:25957689 +P09950 UniProtKB Sequence conflict 181 181 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P28789 1 327 +P28789 UniProtKB Chain 1 327 . . . ID=PRO_0000143045;Note=Porphobilinogen deaminase +P28789 UniProtKB Modified residue 251 251 . . . Note=S-(dipyrrolylmethanemethyl)cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q12276 1 1246 +Q12276 UniProtKB Chain 1 1246 . . . ID=PRO_0000237668;Note=HMG2-induced ER-remodeling protein 1 +Q12276 UniProtKB Compositional bias 139 283 . . . Note=Ser-rich +Q12276 UniProtKB Modified residue 102 102 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q12276 UniProtKB Modified residue 128 128 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q12276 UniProtKB Modified residue 277 277 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12276 UniProtKB Modified residue 1013 1013 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12276 UniProtKB Modified residue 1130 1130 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12276 UniProtKB Modified residue 1200 1200 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12276 UniProtKB Modified residue 1204 1204 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12276 UniProtKB Modified residue 1207 1207 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P41809 1 1802 +P41809 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41809 UniProtKB Chain 22 1802 . . . ID=PRO_0000021444;Note=Signaling mucin HKR1 +P41809 UniProtKB Topological domain 22 1485 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41809 UniProtKB Transmembrane 1486 1506 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41809 UniProtKB Topological domain 1507 1802 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41809 UniProtKB Repeat 453 480 . . . Note=1%3B approximate +P41809 UniProtKB Repeat 481 508 . . . Note=2 +P41809 UniProtKB Repeat 509 536 . . . Note=3 +P41809 UniProtKB Repeat 537 564 . . . Note=4 +P41809 UniProtKB Repeat 565 592 . . . Note=5 +P41809 UniProtKB Repeat 593 620 . . . Note=6 +P41809 UniProtKB Repeat 621 648 . . . Note=7 +P41809 UniProtKB Repeat 649 676 . . . Note=8 +P41809 UniProtKB Repeat 677 704 . . . Note=9 +P41809 UniProtKB Repeat 705 732 . . . Note=10 +P41809 UniProtKB Repeat 733 760 . . . Note=11 +P41809 UniProtKB Repeat 761 788 . . . Note=12 +P41809 UniProtKB Region 453 788 . . . Note=12 X 28 AA tandem repeats of S-[AV]-[P]-V-A-V-S-S-T-Y-T-S-S-P-S-A-P-A-A-I-S-S-T-Y-T-S-S-P +P41809 UniProtKB Compositional bias 23 1478 . . . Note=Ser/Thr-rich +P41809 UniProtKB Glycosylation 24 24 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41809 UniProtKB Glycosylation 1252 1252 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41809 UniProtKB Glycosylation 1293 1293 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41809 UniProtKB Glycosylation 1342 1342 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41809 UniProtKB Glycosylation 1400 1400 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41809 UniProtKB Sequence conflict 582 582 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41809 UniProtKB Sequence conflict 594 594 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CY07 1 175 +P0CY07 UniProtKB Chain 1 175 . . . ID=PRO_0000410462;Note=Silenced mating-type protein ALPHA1 +P0CY07 UniProtKB DNA binding 88 144 . . . Note=Alpha box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00655 +##sequence-region P54839 1 491 +P54839 UniProtKB Chain 1 491 . . . ID=PRO_0000213758;Note=Hydroxymethylglutaryl-CoA synthase +P54839 UniProtKB Active site 127 127 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10116 +P54839 UniProtKB Active site 159 159 . . . Note=Acyl-thioester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10116 +P54839 UniProtKB Active site 296 296 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10116 +P54839 UniProtKB Modified residue 276 276 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P40480 1 1083 +P40480 UniProtKB Chain 1 1083 . . . ID=PRO_0000066998;Note=Protein HOS4 +P40480 UniProtKB Repeat 329 359 . . . Note=ANK 1 +P40480 UniProtKB Repeat 363 392 . . . Note=ANK 2 +P40480 UniProtKB Repeat 398 427 . . . Note=ANK 3 +P40480 UniProtKB Repeat 532 561 . . . Note=ANK 4 +P40480 UniProtKB Repeat 593 622 . . . Note=ANK 5 +P40480 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40480 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40480 UniProtKB Modified residue 37 37 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40480 UniProtKB Modified residue 67 67 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40480 UniProtKB Modified residue 290 290 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40480 UniProtKB Modified residue 507 507 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40480 UniProtKB Modified residue 698 698 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40480 UniProtKB Modified residue 700 700 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40480 UniProtKB Modified residue 778 778 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P48570 1 428 +P48570 UniProtKB Chain 1 428 . . . ID=PRO_0000140454;Note=Homocitrate synthase%2C cytosolic isozyme +P48570 UniProtKB Domain 23 276 . . . Note=Pyruvate carboxyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01151 +P48570 UniProtKB Modified residue 385 385 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48570 UniProtKB Modified residue 396 396 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P48570 UniProtKB Modified residue 401 401 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P48570 UniProtKB Modified residue 410 410 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P36078 1 116 +P36078 UniProtKB Chain 1 116 . . . ID=PRO_0000203165;Note=Helper of Tim protein 13 +P36078 UniProtKB Zinc finger 10 94 . . . Note=CHY-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00601 +P36078 UniProtKB Sequence conflict 71 71 . . . Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q99332 1 602 +Q99332 UniProtKB Chain 1 602 . . . ID=PRO_0000227934;Note=Protein HPH1 +Q99332 UniProtKB Transmembrane 575 595 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99332 UniProtKB Compositional bias 163 420 . . . Note=Ser-rich +Q99332 UniProtKB Modified residue 167 167 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q99332 UniProtKB Modified residue 342 342 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P17629 1 752 +P17629 UniProtKB Chain 1 752 . . . ID=PRO_0000084046;Note=THO complex subunit HPR1 +P17629 UniProtKB Modified residue 234 234 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P17629 UniProtKB Sequence conflict 404 404 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47171 1 1648 +P47171 UniProtKB Chain 1 1648 . . . ID=PRO_0000203124;Note=Histone transcription regulator 3 +P47171 UniProtKB Modified residue 302 302 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47171 UniProtKB Modified residue 304 304 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P48353 1 224 +P48353 UniProtKB Chain 1 224 . . . ID=PRO_0000071120;Note=Protein HLJ1 +P48353 UniProtKB Domain 18 87 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +P48353 UniProtKB Modified residue 109 109 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q04429 1 423 +Q04429 UniProtKB Chain 1 423 . . . ID=PRO_0000083991;Note=Protein HLR1 +##sequence-region P12683 1 1054 +P12683 UniProtKB Chain 1 1054 . . . ID=PRO_0000114456;Note=3-hydroxy-3-methylglutaryl-coenzyme A reductase 1 +P12683 UniProtKB Topological domain 1 28 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12683 UniProtKB Transmembrane 29 49 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12683 UniProtKB Topological domain 50 187 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12683 UniProtKB Transmembrane 188 208 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12683 UniProtKB Topological domain 209 217 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12683 UniProtKB Transmembrane 218 238 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12683 UniProtKB Topological domain 239 246 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12683 UniProtKB Transmembrane 247 267 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12683 UniProtKB Topological domain 268 309 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12683 UniProtKB Transmembrane 310 330 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12683 UniProtKB Topological domain 331 336 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12683 UniProtKB Transmembrane 337 357 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12683 UniProtKB Topological domain 358 400 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12683 UniProtKB Transmembrane 401 421 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12683 UniProtKB Topological domain 422 498 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12683 UniProtKB Transmembrane 499 519 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12683 UniProtKB Topological domain 520 1054 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12683 UniProtKB Domain 189 357 . . . Note=SSD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00199 +P12683 UniProtKB Region 525 617 . . . Note=Linker +P12683 UniProtKB Region 618 1054 . . . Note=Catalytic +P12683 UniProtKB Active site 714 714 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12683 UniProtKB Active site 848 848 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12683 UniProtKB Active site 924 924 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12683 UniProtKB Active site 1020 1020 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10003 +P12683 UniProtKB Modified residue 552 552 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P12683 UniProtKB Glycosylation 115 115 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12683 UniProtKB Glycosylation 181 181 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12683 UniProtKB Glycosylation 452 452 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12683 UniProtKB Glycosylation 490 490 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CY13 1 119 +P0CY13 UniProtKB Chain 1 119 . . . ID=PRO_0000410463;Note=Silenced mating-type protein A2 +P0CY13 UniProtKB DNA binding 38 100 . . . Note=Homeobox%3B TALE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00108 +##sequence-region Q12398 1 434 +Q12398 UniProtKB Chain 1 434 . . . ID=PRO_0000224147;Note=Probable transcription factor HMS1 +Q12398 UniProtKB Domain 266 341 . . . Note=bHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981 +##sequence-region P40545 1 261 +P40545 UniProtKB Chain 1 261 . . . ID=PRO_0000141963;Note=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase +P40545 UniProtKB Sequence conflict 243 243 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40545 UniProtKB Beta strand 7 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Helix 41 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Beta strand 57 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Helix 66 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Turn 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Beta strand 80 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Turn 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Helix 91 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Turn 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Helix 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Helix 116 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Helix 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Beta strand 131 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Beta strand 144 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Turn 150 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Beta strand 154 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Helix 162 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Turn 169 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Beta strand 173 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Helix 191 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Beta strand 208 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Helix 220 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Beta strand 232 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Helix 241 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Beta strand 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +P40545 UniProtKB Helix 250 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AGK +##sequence-region P33734 1 552 +P33734 UniProtKB Chain 1 552 . . . ID=PRO_0000152476;Note=Imidazole glycerol phosphate synthase hisHF +P33734 UniProtKB Domain 3 218 . . . Note=Glutamine amidotransferase type-1 +P33734 UniProtKB Region 236 552 . . . Note=Cyclase +P33734 UniProtKB Region 364 365 . . . Note=PRFAR binding +P33734 UniProtKB Region 402 404 . . . Note=PRFAR binding +P33734 UniProtKB Region 474 475 . . . Note=PRFAR binding +P33734 UniProtKB Region 500 501 . . . Note=PRFAR binding +P33734 UniProtKB Region 523 524 . . . Note=PRFAR binding +P33734 UniProtKB Active site 83 83 . . . Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33734 UniProtKB Active site 193 193 . . . Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33734 UniProtKB Active site 195 195 . . . Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33734 UniProtKB Active site 245 245 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33734 UniProtKB Active site 404 404 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33734 UniProtKB Binding site 83 83 . . . Note=Glutamine (covalent) +P33734 UniProtKB Binding site 332 332 . . . Note=Substrate%3B via amide nitrogen +P33734 UniProtKB Binding site 469 469 . . . Note=Substrate +P33734 UniProtKB Mutagenesis 239 239 . . . Note=1000-fold decrease in catalytic efficiency. Uncoupling of glutaminase activity from the cyclase activity. R->A%2CH%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12795596;Dbxref=PMID:12795596 +P33734 UniProtKB Mutagenesis 258 258 . . . Note=No activity. Uncoupling of glutaminase activity from the cyclase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12795596;Dbxref=PMID:12795596 +P33734 UniProtKB Mutagenesis 258 258 . . . Note=Small reduction of activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12795596;Dbxref=PMID:12795596 +P33734 UniProtKB Mutagenesis 360 360 . . . Note=Almost no effect on activity. K->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12795596;Dbxref=PMID:12795596 +P33734 UniProtKB Sequence conflict 54 54 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33734 UniProtKB Beta strand 3 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 15 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 27 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 34 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OX6 +P33734 UniProtKB Beta strand 45 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 53 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 66 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 79 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 84 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 90 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 104 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Turn 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 119 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 143 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 155 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 167 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 176 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 187 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 194 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 198 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 221 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 232 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 240 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 250 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OX5 +P33734 UniProtKB Beta strand 254 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 277 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 292 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 307 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 311 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Turn 320 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 327 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 346 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 359 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 365 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 386 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 396 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 399 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 405 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 413 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 433 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Turn 441 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 445 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 451 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 465 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 471 473 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Turn 474 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 482 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 496 498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 505 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Beta strand 518 523 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 524 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +P33734 UniProtKB Helix 533 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JVN +##sequence-region P38635 1 335 +P38635 UniProtKB Chain 1 335 . . . ID=PRO_0000122322;Note=Histidinol-phosphatase +P38635 UniProtKB Sequence conflict 30 30 . . . Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38635 UniProtKB Sequence conflict 191 191 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38635 UniProtKB Sequence conflict 195 195 . . . Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03937 1 162 +Q03937 UniProtKB Chain 1 162 . . . ID=PRO_0000252301;Note=Meiosis-specific protein HED1 +##sequence-region P51979 1 1187 +P51979 UniProtKB Chain 1 1187 . . . ID=PRO_0000102090;Note=ATP-dependent DNA helicase MER3 +P51979 UniProtKB Domain 148 322 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P51979 UniProtKB Domain 360 542 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P51979 UniProtKB Domain 616 922 . . . Note=SEC63 +P51979 UniProtKB Nucleotide binding 161 168 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P51979 UniProtKB Zinc finger 1039 1054 . . . Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P51979 UniProtKB Motif 268 271 . . . Note=DEIH box +P51979 UniProtKB Mutagenesis 166 166 . . . Note=Decrease in activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11376001;Dbxref=PMID:11376001 +P51979 UniProtKB Sequence conflict 552 552 . . . Note=T->TAA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P06633 1 220 +P06633 UniProtKB Chain 1 220 . . . ID=PRO_0000158250;Note=Imidazoleglycerol-phosphate dehydratase +P06633 UniProtKB Natural variant 8 8 . . . Note=In strain: CLIB 219. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P06633 UniProtKB Natural variant 30 30 . . . Note=In strain: CLIB 219%2C CLIB 410%2C CLIB 413 and YIIc17 haplotype Ha2. I->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P06633 UniProtKB Natural variant 92 92 . . . Note=In strain: YIIc12 and YIIc17 haplotype Ha1. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P06633 UniProtKB Natural variant 216 216 . . . Note=In strain: YIIc17 haplotype Ha2. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P06633 UniProtKB Sequence conflict 109 111 . . . Note=GAV->LA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06633 UniProtKB Sequence conflict 109 111 . . . Note=GAV->LA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P02293 1 131 +P02293 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02293 UniProtKB Chain 2 131 . . . ID=PRO_0000071938;Note=Histone H2B.1 +P02293 UniProtKB Modified residue 7 7 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16598039;Dbxref=PMID:16598039 +P02293 UniProtKB Modified residue 8 8 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16598039;Dbxref=PMID:16598039 +P02293 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15652479,ECO:0000269|PubMed:15970663;Dbxref=PMID:15652479,PMID:15970663 +P02293 UniProtKB Modified residue 12 12 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11545749,ECO:0000269|PubMed:15186774;Dbxref=PMID:11545749,PMID:15186774 +P02293 UniProtKB Modified residue 17 17 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11545749,ECO:0000269|PubMed:15186774,ECO:0000269|PubMed:16598039;Dbxref=PMID:11545749,PMID:15186774,PMID:16598039 +P02293 UniProtKB Cross-link 7 7 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate +P02293 UniProtKB Cross-link 8 8 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate +P02293 UniProtKB Cross-link 17 17 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02293 UniProtKB Cross-link 18 18 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02293 UniProtKB Cross-link 124 124 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10642555,ECO:0000269|PubMed:12535538,ECO:0000269|PubMed:12535539,ECO:0000269|PubMed:14660635,ECO:0000269|PubMed:15280549,ECO:0000269|PubMed:16432255;Dbxref=PMID:10642555,PMID:12535538,PMID:12535539,PMID:14660635,PMID:15280549,PMID:16432255 +P02293 UniProtKB Mutagenesis 7 8 . . . Note=Reduces sumoylation. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16598039;Dbxref=PMID:16598039 +P02293 UniProtKB Mutagenesis 11 11 . . . Note=Desensitizes cells to H(2)O(2) treatment. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15652479;Dbxref=PMID:15652479 +P02293 UniProtKB Mutagenesis 11 11 . . . Note=Induces apoptotic-like features including chromatin condensation. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15652479;Dbxref=PMID:15652479 +P02293 UniProtKB Mutagenesis 17 18 . . . Note=Reduces sumoylation. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16598039;Dbxref=PMID:16598039 +P02293 UniProtKB Mutagenesis 48 48 . . . Note=Confers UV-radiation sensitivity%3B when associated with F-87 and S-88. V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11973294;Dbxref=PMID:11973294 +P02293 UniProtKB Mutagenesis 87 87 . . . Note=Confers UV-radiation sensitivity%3B when associated with F-48 and S-88. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11973294;Dbxref=PMID:11973294 +P02293 UniProtKB Mutagenesis 88 88 . . . Note=Confers UV-radiation sensitivity%3B when associated with F-48 and F-87. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11973294;Dbxref=PMID:11973294 +P02293 UniProtKB Mutagenesis 124 124 . . . Note=Impairs ubiquitin conjugation%2C DNA double-strand brakes formation during meiosis and histone H3-K79 methylation. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10642555,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:14660635,ECO:0000269|PubMed:15280549,ECO:0000269|PubMed:15632126;Dbxref=PMID:10642555,PMID:12152067,PMID:14660635,PMID:15280549,PMID:15632126 +P02293 UniProtKB Helix 42 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B +P02293 UniProtKB Beta strand 57 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B +P02293 UniProtKB Helix 60 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B +P02293 UniProtKB Beta strand 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B +P02293 UniProtKB Helix 95 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B +P02293 UniProtKB Helix 108 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B +##sequence-region P13434 1 144 +P13434 UniProtKB Chain 1 144 . . . ID=PRO_0000204630;Note=Transcriptional activator HAP3 +P13434 UniProtKB DNA binding 42 48 . . . . +P13434 UniProtKB Region 69 80 . . . Note=Subunit association domain (SAD) +##sequence-region P32769 1 611 +P32769 UniProtKB Chain 1 611 . . . ID=PRO_0000091490;Note=Elongation factor 1 alpha-like protein +P32769 UniProtKB Domain 165 390 . . . Note=tr-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P32769 UniProtKB Nucleotide binding 174 181 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32769 UniProtKB Nucleotide binding 251 255 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32769 UniProtKB Nucleotide binding 313 316 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32769 UniProtKB Region 174 181 . . . Note=G1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P32769 UniProtKB Region 230 234 . . . Note=G2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P32769 UniProtKB Region 251 254 . . . Note=G3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P32769 UniProtKB Region 313 316 . . . Note=G4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P32769 UniProtKB Region 352 354 . . . Note=G5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P32769 UniProtKB Modified residue 124 124 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P32769 UniProtKB Mutagenesis 176 176 . . . Note=Loss of function. V->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11909951;Dbxref=PMID:11909951 +P32769 UniProtKB Mutagenesis 255 255 . . . Note=Loss of function. H->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11909951;Dbxref=PMID:11909951 +P32769 UniProtKB Sequence conflict 92 94 . . . Note=NGS->MGV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32769 UniProtKB Helix 157 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 167 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Helix 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Helix 180 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Helix 196 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Helix 219 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P27 +P32769 UniProtKB Beta strand 237 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 246 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Helix 256 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Helix 259 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 270 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Helix 291 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 308 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Helix 315 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Helix 322 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Helix 343 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 346 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 353 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 359 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Helix 366 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Helix 377 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 397 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 402 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 419 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 435 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Turn 440 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 443 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Turn 453 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 464 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 473 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Helix 483 485 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 491 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 504 512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 524 529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 532 547 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 564 571 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Turn 583 585 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Turn 587 590 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 591 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +P32769 UniProtKB Beta strand 599 609 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3P26 +##sequence-region Q07653 1 1046 +Q07653 UniProtKB Chain 1 1046 . . . ID=PRO_0000233010;Note=Protein HBT1 +Q07653 UniProtKB Compositional bias 151 254 . . . Note=His-rich +Q07653 UniProtKB Compositional bias 967 1001 . . . Note=His-rich +Q07653 UniProtKB Modified residue 41 41 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q07653 UniProtKB Modified residue 303 303 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07653 UniProtKB Modified residue 363 363 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07653 UniProtKB Modified residue 491 491 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07653 UniProtKB Modified residue 561 561 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07653 UniProtKB Modified residue 671 671 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07653 UniProtKB Modified residue 855 855 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07653 UniProtKB Modified residue 857 857 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07653 UniProtKB Modified residue 1005 1005 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07653 UniProtKB Modified residue 1034 1034 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198 +##sequence-region P25364 1 564 +P25364 UniProtKB Chain 1 564 . . . ID=PRO_0000091902;Note=Forkhead transcription factor HCM1 +P25364 UniProtKB DNA binding 108 199 . . . Note=Fork-head;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00089 +P25364 UniProtKB Modified residue 342 342 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25364 UniProtKB Modified residue 496 496 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25364 UniProtKB Mutagenesis 155 155 . . . Note=No recognition of DNA-binding site and no suppression of calmodulin mutants%3B when associated with A-159%3B A-162 and A-163. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9920414;Dbxref=PMID:9920414 +P25364 UniProtKB Mutagenesis 159 159 . . . Note=No recognition of DNA-binding site and no suppression of calmodulin mutants%3B when associated with A-155%3B A-162 and A-163. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9920414;Dbxref=PMID:9920414 +P25364 UniProtKB Mutagenesis 162 162 . . . Note=No recognition of DNA-binding site and no suppression of calmodulin mutants%3B when associated with A-155%3B A-159 and A-163. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9920414;Dbxref=PMID:9920414 +P25364 UniProtKB Mutagenesis 163 163 . . . Note=No recognition of DNA-binding site and no suppression of calmodulin mutants%3B when associated with A-155%3B A-159 and A-162. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9920414;Dbxref=PMID:9920414 +P25364 UniProtKB Sequence conflict 129 130 . . . Note=KL->NV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06623 1 655 +Q06623 UniProtKB Chain 1 655 . . . ID=PRO_0000083932;Note=HDA1 complex subunit 3 +Q06623 UniProtKB Coiled coil 482 632 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06623 UniProtKB Beta strand 29 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Helix 39 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Helix 53 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Turn 62 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Helix 68 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Helix 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Helix 105 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Helix 114 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Beta strand 131 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Helix 141 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Beta strand 156 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Beta strand 175 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Turn 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Beta strand 200 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Helix 214 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Beta strand 235 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Helix 244 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Helix 260 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Helix 273 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Turn 282 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Helix 285 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Turn 290 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Helix 293 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Helix 296 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +Q06623 UniProtKB Helix 319 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HGT +##sequence-region Q12060 1 488 +Q12060 UniProtKB Chain 1 488 . . . ID=PRO_0000083959;Note=Transcriptional coactivator HFI1/ADA1 +Q12060 UniProtKB Sequence conflict 19 19 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12373 1 385 +Q12373 UniProtKB Chain 1 385 . . . ID=PRO_0000227731;Note=HAT1-interacting factor 1 +Q12373 UniProtKB Repeat 186 220 . . . Note=TPR 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12373 UniProtKB Repeat 229 262 . . . Note=TPR 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12373 UniProtKB Repeat 289 322 . . . Note=TPR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12373 UniProtKB Region 80 199 . . . Note=Important for interaction with heterotetrameric histone H3 and H4 and for interaction with dimeric histone H2A and H2B;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24946827,ECO:0000269|PubMed:27618665;Dbxref=PMID:24946827,PMID:27618665 +Q12373 UniProtKB Region 248 332 . . . Note=Interaction with dimeric histone H2A and H2B;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618665;Dbxref=PMID:27618665 +Q12373 UniProtKB Compositional bias 97 184 . . . Note=Glu-rich +Q12373 UniProtKB Modified residue 174 174 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12373 UniProtKB Mutagenesis 80 158 . . . Note=Abolishes interaction with heterotetrameric histone H3 and H4 and with dimeric histone H2A and H2B. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618665;Dbxref=PMID:27618665 +Q12373 UniProtKB Mutagenesis 85 198 . . . Note=Abolishes interaction with histones H2A%2C H2B%2C H3 and H4. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24946827,ECO:0000269|PubMed:27618665;Dbxref=PMID:24946827,PMID:27618665 +Q12373 UniProtKB Mutagenesis 95 158 . . . Note=Mildly decreases interaction with heterotetrameric histone H3 and H4 and abolishes interaction with dimeric histone H2A and H2B. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618665;Dbxref=PMID:27618665 +Q12373 UniProtKB Mutagenesis 135 158 . . . Note=Minimal decrease of interaction with heterotetrameric histone H3 and H4 and with dimeric histone H2A and H2B. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24946827,ECO:0000269|PubMed:27618665;Dbxref=PMID:24946827,PMID:27618665 +Q12373 UniProtKB Mutagenesis 248 248 . . . Note=Strongly reduces affinity for dimeric histone H2A and H2B%3B when associated with A-250%3B A-288%3B A-291 and 332-A--A-342. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618665;Dbxref=PMID:27618665 +Q12373 UniProtKB Mutagenesis 250 250 . . . Note=Strongly reduces affinity for dimeric histone H2A and H2B%3B when associated with A-248%3B A-288%3B A-291 and 332-A--A-342. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618665;Dbxref=PMID:27618665 +Q12373 UniProtKB Mutagenesis 288 288 . . . Note=Strongly reduces affinity for dimeric histone H2A and H2B%3B when associated with A-248%3B A-250%3B A-291 and 332-A--A-342. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618665;Dbxref=PMID:27618665 +Q12373 UniProtKB Mutagenesis 291 291 . . . Note=Strongly reduces affinity for dimeric histone H2A and H2B%3B when associated with A-248%3B A-250%3B A-288 and 332-A--A-342. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618665;Dbxref=PMID:27618665 +Q12373 UniProtKB Mutagenesis 332 342 . . . Note=Strongly reduces affinity for dimeric histone H2A and H2B%3B when associated with A-248%3B A-250%3B A-288 and A-291. QIQDDIDEVQE->AIQAAIDAVQA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618665;Dbxref=PMID:27618665 +Q12373 UniProtKB Helix 14 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0 +Q12373 UniProtKB Helix 38 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0 +Q12373 UniProtKB Beta strand 54 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0 +Q12373 UniProtKB Helix 61 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0 +Q12373 UniProtKB Helix 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0 +Q12373 UniProtKB Helix 167 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0 +Q12373 UniProtKB Turn 175 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BT1 +Q12373 UniProtKB Helix 186 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0 +Q12373 UniProtKB Helix 194 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0 +Q12373 UniProtKB Helix 202 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0 +Q12373 UniProtKB Beta strand 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BT1 +Q12373 UniProtKB Helix 229 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0 +Q12373 UniProtKB Helix 252 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0 +Q12373 UniProtKB Helix 273 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0 +Q12373 UniProtKB Helix 298 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0 +Q12373 UniProtKB Helix 323 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NQ0 +##sequence-region P53834 1 153 +P53834 UniProtKB Chain 1 153 . . . ID=PRO_0000215823;Note=Hsp90 co-chaperone HCH1 +##sequence-region Q03281 1 663 +Q03281 UniProtKB Chain 1 663 . . . ID=PRO_0000202596;Note=Inner nuclear membrane protein HEH2 +Q03281 UniProtKB Transmembrane 317 337 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03281 UniProtKB Motif 124 137 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03281 UniProtKB Compositional bias 85 90 . . . Note=Poly-Ser +Q03281 UniProtKB Modified residue 123 123 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03281 UniProtKB Mutagenesis 1 133 . . . Note=No interaction with SRP1%3B when associated with missing 309-I--E-663. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16929305;Dbxref=PMID:16929305 +Q03281 UniProtKB Mutagenesis 1 52 . . . Note=Interaction with SRP1%3B when associated with missing 309-I--E-663. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16929305;Dbxref=PMID:16929305 +Q03281 UniProtKB Mutagenesis 124 137 . . . Note=No interaction with SRP1%3B when associated with missing 309-I--E-663. Mislocalized to the endoplasmic reticulum. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16929305;Dbxref=PMID:16929305 +Q03281 UniProtKB Mutagenesis 126 126 . . . Note=Mislocalized to the endoplasmic reticulum. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16929305;Dbxref=PMID:16929305 +Q03281 UniProtKB Mutagenesis 309 663 . . . Note=Interaction with SRP1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16929305;Dbxref=PMID:16929305 +Q03281 UniProtKB Turn 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVZ +Q03281 UniProtKB Helix 113 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PVZ +##sequence-region P36113 1 551 +P36113 UniProtKB Chain 1 551 . . . ID=PRO_0000056339;Note=E3 ubiquitin-protein ligase HEL1 +P36113 UniProtKB Zinc finger 179 223 . . . Note=RING-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +P36113 UniProtKB Zinc finger 242 314 . . . Note=IBR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36113 UniProtKB Zinc finger 341 370 . . . Note=RING-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +P36113 UniProtKB Active site 354 354 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y4X5 +##sequence-region P06174 1 275 +P06174 UniProtKB Chain 1 275 . . . ID=PRO_0000135254;Note=Uroporphyrinogen-III synthase +P06174 UniProtKB Sequence conflict 231 275 . . . Note=HLRVASIGPTTKKYLDDNDVTSDVVSPKPDPKSLLDAIELYQRHK->IYGLRHRTYH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P46973 1 164 +P46973 UniProtKB Chain 1 164 . . . ID=PRO_0000173556;Note=Protein HIT1 +P46973 UniProtKB Zinc finger 8 49 . . . Note=HIT-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00453 +P46973 UniProtKB Sequence conflict 36 37 . . . Note=AA->RR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46973 UniProtKB Turn 9 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N95 +P46973 UniProtKB Beta strand 13 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N95 +P46973 UniProtKB Turn 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N95 +P46973 UniProtKB Beta strand 26 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N95 +P46973 UniProtKB Helix 30 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N95 +P46973 UniProtKB Beta strand 36 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N95 +P46973 UniProtKB Helix 77 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJF +P46973 UniProtKB Helix 87 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJF +P46973 UniProtKB Helix 96 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJF +P46973 UniProtKB Beta strand 119 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJF +P46973 UniProtKB Helix 123 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJF +P46973 UniProtKB Turn 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJF +P46973 UniProtKB Helix 146 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJF +##sequence-region P0CY11 1 126 +P0CY11 UniProtKB Chain 1 126 . . . ID=PRO_0000410465;Note=Silenced mating-type protein A1 +P0CY11 UniProtKB DNA binding 70 126 . . . Note=Homeobox;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00108 +##sequence-region Q06629 1 674 +Q06629 UniProtKB Chain 1 674 . . . ID=PRO_0000083930;Note=HDA1 complex subunit 2 +Q06629 UniProtKB Coiled coil 468 637 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P05373 1 342 +P05373 UniProtKB Chain 1 342 . . . ID=PRO_0000140534;Note=Delta-aminolevulinic acid dehydratase +P05373 UniProtKB Active site 210 210 . . . Note=Schiff-base intermediate with substrate +P05373 UniProtKB Active site 263 263 . . . Note=Schiff-base intermediate with substrate +P05373 UniProtKB Metal binding 133 133 . . . Note=Zinc%3B catalytic +P05373 UniProtKB Metal binding 135 135 . . . Note=Zinc%3B catalytic +P05373 UniProtKB Metal binding 143 143 . . . Note=Zinc%3B catalytic +P05373 UniProtKB Binding site 220 220 . . . Note=Substrate 1 +P05373 UniProtKB Binding site 232 232 . . . Note=Substrate 1 +P05373 UniProtKB Binding site 290 290 . . . Note=Substrate 2 +P05373 UniProtKB Binding site 329 329 . . . Note=Substrate 2 +P05373 UniProtKB Modified residue 254 254 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P05373 UniProtKB Sequence conflict 291 291 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05373 UniProtKB Helix 14 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Helix 19 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Beta strand 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Helix 25 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Beta strand 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EB3 +P05373 UniProtKB Helix 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Beta strand 41 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Beta strand 54 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Beta strand 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W31 +P05373 UniProtKB Beta strand 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Helix 68 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Beta strand 85 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Helix 103 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Helix 111 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Beta strand 126 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Turn 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Beta strand 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OHL +P05373 UniProtKB Beta strand 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W31 +P05373 UniProtKB Beta strand 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Helix 154 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Beta strand 174 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Helix 185 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Turn 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Beta strand 203 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Beta strand 213 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7P +P05373 UniProtKB Helix 217 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Beta strand 228 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Turn 233 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Helix 242 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Beta strand 258 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Helix 266 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Helix 269 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Turn 279 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Beta strand 284 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Helix 290 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Helix 307 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Beta strand 324 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +P05373 UniProtKB Helix 331 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1H7N +##sequence-region P11353 1 328 +P11353 UniProtKB Chain 1 328 . . . ID=PRO_0000109878;Note=Oxygen-dependent coproporphyrinogen-III oxidase +P11353 UniProtKB Region 57 66 . . . Note=Important for dimerization;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11353 UniProtKB Region 133 135 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11353 UniProtKB Region 266 302 . . . Note=Important for dimerization;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11353 UniProtKB Region 285 290 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11353 UniProtKB Active site 131 131 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11353 UniProtKB Binding site 117 117 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11353 UniProtKB Site 201 201 . . . Note=Important for dimerization;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11353 UniProtKB Disulfide bond 193 193 . . . Note=Interchain;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15194705;Dbxref=PMID:15194705 +P11353 UniProtKB Sequence conflict 226 226 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11353 UniProtKB Helix 7 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL +P11353 UniProtKB Helix 12 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Beta strand 35 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Beta strand 40 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL +P11353 UniProtKB Helix 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL +P11353 UniProtKB Beta strand 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Beta strand 55 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Beta strand 62 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Helix 80 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Helix 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Beta strand 99 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL +P11353 UniProtKB Beta strand 109 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Beta strand 129 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Beta strand 144 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Helix 164 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Helix 185 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Helix 193 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Beta strand 204 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL +P11353 UniProtKB Beta strand 209 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Helix 221 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Helix 235 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Turn 245 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Helix 253 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Helix 265 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TXN +P11353 UniProtKB Helix 275 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL +P11353 UniProtKB Helix 288 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL +P11353 UniProtKB Helix 292 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL +P11353 UniProtKB Beta strand 297 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL +P11353 UniProtKB Helix 312 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TKL +##sequence-region P04912 1 132 +P04912 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12915400;Dbxref=PMID:12915400 +P04912 UniProtKB Chain 2 132 . . . ID=PRO_0000055327;Note=Histone H2A.2 +P04912 UniProtKB Motif 129 130 . . . Note=[ST]-Q motif +P04912 UniProtKB Site 120 120 . . . Note=Not ubiquitinated;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04912 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12915400;Dbxref=PMID:12915400 +P04912 UniProtKB Modified residue 5 5 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10082517;Dbxref=PMID:10082517 +P04912 UniProtKB Modified residue 8 8 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10082517,ECO:0000269|PubMed:11545749;Dbxref=PMID:10082517,PMID:11545749 +P04912 UniProtKB Modified residue 106 106 . . . Note=N5-methylglutamine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24352239;Dbxref=PMID:24352239 +P04912 UniProtKB Modified residue 129 129 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:11140636;Dbxref=PMID:18407956,PMID:11140636 +P04912 UniProtKB Cross-link 127 127 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) +P04912 UniProtKB Mutagenesis 129 129 . . . Note=Causes hypersensitivity to DNA-damage-inducing agents. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11140636;Dbxref=PMID:11140636 +P04912 UniProtKB Mutagenesis 129 129 . . . Note=No effect. S->E%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11140636;Dbxref=PMID:11140636 +P04912 UniProtKB Helix 19 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P04912 UniProtKB Helix 29 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P04912 UniProtKB Turn 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P04912 UniProtKB Beta strand 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P04912 UniProtKB Helix 49 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P04912 UniProtKB Beta strand 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P04912 UniProtKB Helix 82 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P04912 UniProtKB Helix 93 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P04912 UniProtKB Turn 99 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P04912 UniProtKB Beta strand 102 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P04912 UniProtKB Helix 115 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +##sequence-region Q12692 1 134 +Q12692 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:16543223;Dbxref=PMID:22814378,PMID:16543223 +Q12692 UniProtKB Chain 2 134 . . . ID=PRO_0000055340;Note=Histone H2A.Z +Q12692 UniProtKB Region 98 108 . . . Note=Interaction with VPS72;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16299513;Dbxref=PMID:16299513 +Q12692 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:16543223;Dbxref=PMID:22814378,PMID:16543223 +Q12692 UniProtKB Modified residue 4 4 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16543222,ECO:0000269|PubMed:16543223;Dbxref=PMID:16543222,PMID:16543223 +Q12692 UniProtKB Modified residue 9 9 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16543222,ECO:0000269|PubMed:16543223;Dbxref=PMID:16543222,PMID:16543223 +Q12692 UniProtKB Modified residue 11 11 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16543222,ECO:0000269|PubMed:16543223;Dbxref=PMID:16543222,PMID:16543223 +Q12692 UniProtKB Modified residue 15 15 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16543222,ECO:0000269|PubMed:16543223;Dbxref=PMID:16543222,PMID:16543223 +Q12692 UniProtKB Helix 25 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B +Q12692 UniProtKB Helix 35 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B +Q12692 UniProtKB Helix 54 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B +Q12692 UniProtKB Beta strand 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B +Q12692 UniProtKB Helix 89 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B +Q12692 UniProtKB Helix 100 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B +##sequence-region P61830 1 136 +P61830 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7035169,ECO:0000269|PubMed:782914;Dbxref=PMID:7035169,PMID:782914 +P61830 UniProtKB Chain 2 136 . . . ID=PRO_0000221370;Note=Histone H3 +P61830 UniProtKB Modified residue 5 5 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11742990,ECO:0000269|PubMed:11751634,ECO:0000269|PubMed:11752412,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:12353038,ECO:0000269|PubMed:12845608,ECO:0000269|PubMed:15949446,ECO:0000269|PubMed:16122352,ECO:0000269|PubMed:16168379,ECO:0000269|PubMed:16185711,ECO:0000269|PubMed:17194708;Dbxref=PMID:11742990,PMID:11751634,PMID:11752412,PMID:12152067,PMID:12353038,PMID:12845608,PMID:15949446,PMID:16122352,PMID:16168379,PMID:16185711,PMID:17194708 +P61830 UniProtKB Modified residue 5 5 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11742990,ECO:0000269|PubMed:11751634,ECO:0000269|PubMed:11752412,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:12353038,ECO:0000269|PubMed:12845608,ECO:0000269|PubMed:15949446,ECO:0000269|PubMed:16122352,ECO:0000269|PubMed:16168379,ECO:0000269|PubMed:16185711,ECO:0000269|PubMed:17194708;Dbxref=PMID:11742990,PMID:11751634,PMID:11752412,PMID:12152067,PMID:12353038,PMID:12845608,PMID:15949446,PMID:16122352,PMID:16168379,PMID:16185711,PMID:17194708 +P61830 UniProtKB Modified residue 5 5 . . . Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11742990,ECO:0000269|PubMed:11751634,ECO:0000269|PubMed:11752412,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:12353038,ECO:0000269|PubMed:12845608,ECO:0000269|PubMed:15949446,ECO:0000269|PubMed:16122352,ECO:0000269|PubMed:16168379,ECO:0000269|PubMed:16185711,ECO:0000269|PubMed:17194708;Dbxref=PMID:11742990,PMID:11751634,PMID:11752412,PMID:12152067,PMID:12353038,PMID:12845608,PMID:15949446,PMID:16122352,PMID:16168379,PMID:16185711,PMID:17194708 +P61830 UniProtKB Modified residue 10 10 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11545749,ECO:0000269|PubMed:16122352,ECO:0000269|PubMed:17194708,ECO:0000269|PubMed:9606197;Dbxref=PMID:11545749,PMID:16122352,PMID:17194708,PMID:9606197 +P61830 UniProtKB Modified residue 10 10 . . . Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17194708;Dbxref=PMID:17194708 +P61830 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10911986,ECO:0000269|PubMed:10975519,ECO:0000269|PubMed:15719021;Dbxref=PMID:10911986,PMID:10975519,PMID:15719021 +P61830 UniProtKB Modified residue 15 15 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17194708;Dbxref=PMID:17194708 +P61830 UniProtKB Modified residue 15 15 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10082517,ECO:0000269|PubMed:10911986,ECO:0000269|PubMed:11545749,ECO:0000269|PubMed:15719021,ECO:0000269|PubMed:16122352,ECO:0000269|PubMed:17194708,ECO:0000269|PubMed:9606197;Dbxref=PMID:10082517,PMID:10911986,PMID:11545749,PMID:15719021,PMID:16122352,PMID:17194708,PMID:9606197 +P61830 UniProtKB Modified residue 19 19 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11545749,ECO:0000269|PubMed:16122352,ECO:0000269|PubMed:17194708,ECO:0000269|PubMed:9606197;Dbxref=PMID:11545749,PMID:16122352,PMID:17194708,PMID:9606197 +P61830 UniProtKB Modified residue 19 19 . . . Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17194708;Dbxref=PMID:17194708 +P61830 UniProtKB Modified residue 24 24 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11545749,ECO:0000269|PubMed:17194708;Dbxref=PMID:11545749,PMID:17194708 +P61830 UniProtKB Modified residue 24 24 . . . Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17194708;Dbxref=PMID:17194708 +P61830 UniProtKB Modified residue 28 28 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17194708;Dbxref=PMID:17194708 +P61830 UniProtKB Modified residue 28 28 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17194708;Dbxref=PMID:17194708 +P61830 UniProtKB Modified residue 28 28 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11545749,ECO:0000269|PubMed:17194708;Dbxref=PMID:11545749,PMID:17194708 +P61830 UniProtKB Modified residue 28 28 . . . Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17194708;Dbxref=PMID:17194708 +P61830 UniProtKB Modified residue 37 37 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11839797,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:12629047,ECO:0000269|PubMed:12773564,ECO:0000269|PubMed:12917322,ECO:0000269|PubMed:15798214,ECO:0000269|PubMed:17194708;Dbxref=PMID:11839797,PMID:12152067,PMID:12629047,PMID:12773564,PMID:12917322,PMID:15798214,PMID:17194708 +P61830 UniProtKB Modified residue 37 37 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11839797,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:12629047,ECO:0000269|PubMed:12773564,ECO:0000269|PubMed:12917322,ECO:0000269|PubMed:15798214,ECO:0000269|PubMed:17194708;Dbxref=PMID:11839797,PMID:12152067,PMID:12629047,PMID:12773564,PMID:12917322,PMID:15798214,PMID:17194708 +P61830 UniProtKB Modified residue 37 37 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17189264,ECO:0000269|PubMed:17194708;Dbxref=PMID:17189264,PMID:17194708 +P61830 UniProtKB Modified residue 37 37 . . . Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11839797,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:12629047,ECO:0000269|PubMed:12773564,ECO:0000269|PubMed:12917322,ECO:0000269|PubMed:15798214,ECO:0000269|PubMed:17194708;Dbxref=PMID:11839797,PMID:12152067,PMID:12629047,PMID:12773564,PMID:12917322,PMID:15798214,PMID:17194708 +P61830 UniProtKB Modified residue 57 57 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15888442,ECO:0000269|PubMed:16015338,ECO:0000269|PubMed:16260619,ECO:0000269|PubMed:17194708,ECO:0000269|PubMed:17320445;Dbxref=PMID:15888442,PMID:16015338,PMID:16260619,PMID:17194708,PMID:17320445 +P61830 UniProtKB Modified residue 65 65 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17194708;Dbxref=PMID:17194708 +P61830 UniProtKB Modified residue 80 80 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12080090,ECO:0000269|PubMed:12097318,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:12574507,ECO:0000269|PubMed:15632126,ECO:0000269|PubMed:17194708;Dbxref=PMID:12080090,PMID:12097318,PMID:12152067,PMID:12574507,PMID:15632126,PMID:17194708 +P61830 UniProtKB Modified residue 80 80 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12080090,ECO:0000269|PubMed:12097318,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:12574507,ECO:0000269|PubMed:15632126,ECO:0000269|PubMed:17194708;Dbxref=PMID:12080090,PMID:12097318,PMID:12152067,PMID:12574507,PMID:15632126,PMID:17194708 +P61830 UniProtKB Modified residue 80 80 . . . Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12080090,ECO:0000269|PubMed:12097318,ECO:0000269|PubMed:12152067,ECO:0000269|PubMed:12574507,ECO:0000269|PubMed:15632126,ECO:0000269|PubMed:17194708;Dbxref=PMID:12080090,PMID:12097318,PMID:12152067,PMID:12574507,PMID:15632126,PMID:17194708 +P61830 UniProtKB Mutagenesis 11 11 . . . Note=Impairs histone H3 phosphorylation and reduces transcription of some GCN5 regulated genes. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10911986,ECO:0000269|PubMed:10975519;Dbxref=PMID:10911986,PMID:10975519 +P61830 UniProtKB Mutagenesis 53 53 . . . Note=Lethal. R->A%2CK%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16260619;Dbxref=PMID:16260619 +P61830 UniProtKB Mutagenesis 57 57 . . . Note=Increases sensitivity to genotoxic agents inducing DNA breaks during replication. K->A%2CQ%2CR;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15888442,ECO:0000269|PubMed:16015338,ECO:0000269|PubMed:16260619;Dbxref=PMID:15888442,PMID:16015338,PMID:16260619 +P61830 UniProtKB Mutagenesis 80 80 . . . Note=Compromises telomeric silencing. K->A%2CP%2CQ;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12080090,ECO:0000269|PubMed:16260619;Dbxref=PMID:12080090,PMID:16260619 +P61830 UniProtKB Mutagenesis 119 119 . . . Note=Lethal. T->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16260619;Dbxref=PMID:16260619 +P61830 UniProtKB Sequence conflict 124 124 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P61830 UniProtKB Beta strand 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RSN +P61830 UniProtKB Beta strand 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNW +P61830 UniProtKB Helix 46 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P61830 UniProtKB Helix 66 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P61830 UniProtKB Helix 87 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P61830 UniProtKB Beta strand 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P61830 UniProtKB Helix 124 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IDC +##sequence-region P02309 1 103 +P02309 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02309 UniProtKB Chain 2 103 . . . ID=PRO_0000158377;Note=Histone H4 +P02309 UniProtKB DNA binding 17 21 . . . . +P02309 UniProtKB Modified residue 6 6 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.19 +P02309 UniProtKB Modified residue 13 13 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.19 +P02309 UniProtKB Modified residue 17 17 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11080160,ECO:0000269|PubMed:15150415,ECO:0000269|PubMed:17289592;Dbxref=PMID:11080160,PMID:15150415,PMID:17289592 +P02309 UniProtKB Modified residue 61 61 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P02309 UniProtKB Modified residue 65 65 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P02309 UniProtKB Modified residue 80 80 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16768447;Dbxref=PMID:16768447 +P02309 UniProtKB Sequence conflict 46 46 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02309 UniProtKB Beta strand 4 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E3K +P02309 UniProtKB Beta strand 16 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZD +P02309 UniProtKB Helix 26 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P02309 UniProtKB Helix 32 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSX +P02309 UniProtKB Turn 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSX +P02309 UniProtKB Turn 46 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L5A +P02309 UniProtKB Helix 51 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P02309 UniProtKB Beta strand 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P02309 UniProtKB Helix 84 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P02309 UniProtKB Beta strand 97 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +##sequence-region Q01766 1 294 +Q01766 UniProtKB Chain 1 294 . . . ID=PRO_0000083893;Note=Halotolerance protein HAL1 +Q01766 UniProtKB Modified residue 266 266 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P0CE41 1 1502 +P0CE41 UniProtKB Chain 1 1502 . . . ID=PRO_0000114945;Note=Heme-responsive zinc finger transcription factor HAP1 +P0CE41 UniProtKB Repeat 280 285 . . . Note=HRM 1 +P0CE41 UniProtKB Repeat 299 304 . . . Note=HRM 2 +P0CE41 UniProtKB Repeat 323 328 . . . Note=HRM 3 +P0CE41 UniProtKB Repeat 347 352 . . . Note=HRM 4 +P0CE41 UniProtKB Repeat 389 394 . . . Note=HRM 5 +P0CE41 UniProtKB Repeat 415 420 . . . Note=HRM 6 +P0CE41 UniProtKB Repeat 1192 1197 . . . Note=HRM 7 +P0CE41 UniProtKB DNA binding 64 93 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P0CE41 UniProtKB Region 244 444 . . . Note=Heme-responsive%3B required for HMC formation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CE41 UniProtKB Coiled coil 105 134 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE41 UniProtKB Compositional bias 177 189 . . . Note=Poly-Gln +P0CE41 UniProtKB Metal binding 64 64 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CE41 UniProtKB Metal binding 64 64 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CE41 UniProtKB Metal binding 67 67 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CE41 UniProtKB Metal binding 74 74 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CE41 UniProtKB Metal binding 81 81 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CE41 UniProtKB Metal binding 81 81 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CE41 UniProtKB Metal binding 84 84 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CE41 UniProtKB Metal binding 93 93 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P06774 1 265 +P06774 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P06774 UniProtKB Chain 2 265 . . . ID=PRO_0000198781;Note=Transcriptional activator HAP2 +P06774 UniProtKB DNA binding 192 217 . . . Note=NFYA/HAP2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00966 +P06774 UniProtKB Region 23 180 . . . Note=Interaction with the HAP2-HAP3-HAP5 heteromer +P06774 UniProtKB Motif 162 185 . . . Note=Subunit association domain (SAD) +P06774 UniProtKB Compositional bias 120 133 . . . Note=Poly-Gln +P06774 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P06774 UniProtKB Modified residue 52 52 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06774 UniProtKB Modified residue 265 265 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06774 UniProtKB Mutagenesis 199 199 . . . Note=Favors CCACC binding over CCAAT. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8223474;Dbxref=PMID:8223474 +##sequence-region Q02516 1 242 +Q02516 UniProtKB Chain 1 242 . . . ID=PRO_0000218260;Note=Transcriptional activator HAP5 +Q02516 UniProtKB Modified residue 7 7 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q03532 1 505 +Q03532 UniProtKB Chain 1 505 . . . ID=PRO_0000055046;Note=ATP-dependent RNA helicase HAS1 +Q03532 UniProtKB Domain 73 249 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q03532 UniProtKB Domain 263 433 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q03532 UniProtKB Nucleotide binding 86 93 . . . Note=ATP +Q03532 UniProtKB Motif 42 70 . . . Note=Q motif +Q03532 UniProtKB Motif 196 199 . . . Note=DEAD box +Q03532 UniProtKB Motif 275 291 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03532 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +Q03532 UniProtKB Mutagenesis 92 92 . . . Note=Lethal in vivo and impairs ATPase with 2-5%25 of wild-type ATPase activity%2C a 20-fold higher KM for ATP and unables RNA/DNA heteroduplexes unwinding activity in vitro. Leads to 13%25 of wild-type ATPase activity and higher RNA/DNA heteroduplexes unwinding activity in vitro%3B when associated with A-389. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15049817,ECO:0000269|PubMed:15718299;Dbxref=PMID:15049817,PMID:15718299 +Q03532 UniProtKB Mutagenesis 105 105 . . . Note=Decreases the amount of 40S ribosomal subunits at 37 degrees Celsius%3B when associated with S-315 and S-393. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15049817;Dbxref=PMID:15049817 +Q03532 UniProtKB Mutagenesis 228 228 . . . Note=Slow growth at 18 and 16 degrees Celsius%2C no growth at 14 degrees Celsius and drastic decrease of the amount of 40S ribosomal subunits at 30 degrees Celsius in vivo. Leads to 70-80%25 of wild-type ATPase activity%2C a 2-fold lower KM for ATP and a slightly reduced RNA/DNA heteroduplexes unwinding activity in vitro. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718299;Dbxref=PMID:15718299 +Q03532 UniProtKB Mutagenesis 230 230 . . . Note=Lethal in vivo and leads to 70-80%25 of wild-type ATPase activity%2C a 2-fold lower KM for ATP and a reduced RNA/DNA heteroduplexes unwinding activity in vitro. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718299;Dbxref=PMID:15718299 +Q03532 UniProtKB Mutagenesis 315 315 . . . Note=Decreases the amount of 40S ribosomal subunits at 37 degrees Celsius%3B when associated with Y-105 and S-393. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15049817;Dbxref=PMID:15049817 +Q03532 UniProtKB Mutagenesis 375 375 . . . Note=Lethal in vivo and leads to 70-80%25 of wild-type ATPase activity%2C a 2-fold lower KM for ATP and a reduced RNA/DNA heteroduplexes unwinding activity in vitro. H->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718299;Dbxref=PMID:15718299 +Q03532 UniProtKB Mutagenesis 376 376 . . . Note=Lethal in vivo and leads to less than 30%25 of wild-type ATPase activity and a 2-fold lower KM for ATP in vitro. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718299;Dbxref=PMID:15718299 +Q03532 UniProtKB Mutagenesis 389 389 . . . Note=Increases 3-fold the ATPase activity and a higher RNA/DNA heteroduplexes unwinding activity in vitro. Leads to 13%25 of wild-type ATPase activity and lower RNA/DNA heteroduplexes unwinding activity in vitro%3B when associated with A-92. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15718299;Dbxref=PMID:15718299 +Q03532 UniProtKB Mutagenesis 393 393 . . . Note=Decreases the amount of 40S ribosomal subunits at 37 degrees Celsius%3B when associated with Y-105 and S-315. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15049817;Dbxref=PMID:15049817 +##sequence-region P39984 1 401 +P39984 UniProtKB Chain 1 401 . . . ID=PRO_0000051014;Note=Histone acetyltransferase type B subunit 2 +P39984 UniProtKB Repeat 116 147 . . . Note=WD 1 +P39984 UniProtKB Repeat 158 189 . . . Note=WD 2 +P39984 UniProtKB Repeat 206 237 . . . Note=WD 3 +P39984 UniProtKB Repeat 249 280 . . . Note=WD 4 +P39984 UniProtKB Repeat 293 324 . . . Note=WD 5 +P39984 UniProtKB Repeat 350 381 . . . Note=WD 6 +P39984 UniProtKB Region 335 339 . . . Note=Interaction with the histone H4 N-terminus;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250 +P39984 UniProtKB Site 266 266 . . . Note=Important for interaction with HAT1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250 +P39984 UniProtKB Mutagenesis 266 266 . . . Note=Abolishes interaction with HAT1. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835250;Dbxref=PMID:24835250 +P39984 UniProtKB Helix 10 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 25 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSX +P39984 UniProtKB Beta strand 53 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 71 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Helix 82 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 108 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 121 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 130 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 143 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Turn 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 151 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 165 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 170 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 175 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 185 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 191 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 200 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 211 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 223 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 231 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 244 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 254 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 264 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 276 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 288 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 298 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 305 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 310 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 320 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Helix 325 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Helix 334 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 344 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 355 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 362 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 367 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Beta strand 375 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +P39984 UniProtKB Turn 387 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PSW +##sequence-region P34243 1 683 +P34243 UniProtKB Chain 1 683 . . . ID=PRO_0000080726;Note=DNA polymerase alpha-associated DNA helicase A +P34243 UniProtKB Nucleotide binding 229 236 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P16622 1 393 +P16622 UniProtKB Transit peptide 1 31 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3042776;Dbxref=PMID:3042776 +P16622 UniProtKB Chain 32 393 . . . ID=PRO_0000008879;Note=Ferrochelatase%2C mitochondrial +P16622 UniProtKB Active site 351 351 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P16622 UniProtKB Sequence conflict 34 34 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16622 UniProtKB Beta strand 39 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Helix 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Helix 55 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Beta strand 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Beta strand 73 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Helix 76 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Helix 104 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Helix 124 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Beta strand 129 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Helix 142 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Turn 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Beta strand 156 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Turn 168 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Helix 171 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Beta strand 191 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Helix 203 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Helix 225 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Beta strand 229 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Helix 239 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Turn 243 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Helix 248 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Turn 263 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Beta strand 269 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Beta strand 278 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Beta strand 284 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1L8X +P16622 UniProtKB Helix 287 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Helix 295 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Beta strand 301 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Helix 313 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Helix 317 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Helix 330 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Beta strand 333 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Helix 343 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Helix 367 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +P16622 UniProtKB Helix 383 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LBQ +##sequence-region P35843 1 434 +P35843 UniProtKB Chain 1 434 . . . ID=PRO_0000100385;Note=Protein HES1 +##sequence-region Q04458 1 532 +Q04458 UniProtKB Chain 1 532 . . . ID=PRO_0000056597;Note=Fatty aldehyde dehydrogenase HFD1 +Q04458 UniProtKB Transmembrane 134 152 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04458 UniProtKB Nucleotide binding 214 219 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04458 UniProtKB Active site 236 236 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007 +Q04458 UniProtKB Active site 273 273 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007 +Q04458 UniProtKB Modified residue 111 111 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P39982 1 102 +P39982 UniProtKB Chain 1 102 . . . ID=PRO_0000202603;Note=Hypersensitivity to hygromycin-B protein 1 +P39982 UniProtKB Topological domain 1 17 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39982 UniProtKB Transmembrane 18 38 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39982 UniProtKB Topological domain 39 69 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39982 UniProtKB Transmembrane 70 90 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39982 UniProtKB Topological domain 91 102 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32480 1 875 +P32480 UniProtKB Chain 1 875 . . . ID=PRO_0000051017;Note=Protein HIR2 +P32480 UniProtKB Repeat 10 47 . . . Note=WD 1 +P32480 UniProtKB Repeat 118 158 . . . Note=WD 2 +P32480 UniProtKB Repeat 163 201 . . . Note=WD 3 +P32480 UniProtKB Repeat 237 277 . . . Note=WD 4 +P32480 UniProtKB Repeat 278 316 . . . Note=WD 5 +P32480 UniProtKB Repeat 320 359 . . . Note=WD 6 +P32480 UniProtKB Repeat 546 587 . . . Note=WD 7 +P32480 UniProtKB Repeat 589 626 . . . Note=WD 8 +P32480 UniProtKB Modified residue 713 713 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32480 UniProtKB Sequence conflict 284 285 . . . Note=KG->NF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32480 UniProtKB Sequence conflict 373 374 . . . Note=KK->FL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P00498 1 297 +P00498 UniProtKB Chain 1 297 . . . ID=PRO_0000151958;Note=ATP phosphoribosyltransferase +P00498 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region Q04344 1 158 +Q04344 UniProtKB Chain 1 158 . . . ID=PRO_0000109800;Note=Hit family protein 1 +Q04344 UniProtKB Domain 26 129 . . . Note=HIT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00464 +Q04344 UniProtKB Motif 114 118 . . . Note=Histidine triad motif +Q04344 UniProtKB Active site 116 116 . . . Note=Tele-AMP-histidine intermediate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11805111;Dbxref=PMID:11805111 +Q04344 UniProtKB Mutagenesis 116 116 . . . Note=Loss of enzymatic activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11805111;Dbxref=PMID:11805111 +##sequence-region P49775 1 206 +P49775 UniProtKB Chain 1 206 . . . ID=PRO_0000109801;Note=Bis(5'-adenosyl)-triphosphatase +P49775 UniProtKB Domain 3 115 . . . Note=HIT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00464 +P49775 UniProtKB Motif 96 100 . . . Note=Histidine triad motif +P49775 UniProtKB Active site 98 98 . . . Note=Tele-AMP-histidine intermediate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12028594;Dbxref=PMID:12028594 +P49775 UniProtKB Mutagenesis 98 98 . . . Note=Fails to reduce intracellular dinucleoside polyphosphate levels. H->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12028594;Dbxref=PMID:12028594 +##sequence-region P40481 1 377 +P40481 UniProtKB Chain 1 377 . . . ID=PRO_0000202964;Note=Histidine protein methyltransferase 1 +##sequence-region Q05787 1 833 +Q05787 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05787 UniProtKB Chain 21 833 . . . ID=PRO_0000240369;Note=ERAD-associated E3 ubiquitin-protein ligase component HRD3 +Q05787 UniProtKB Transmembrane 768 788 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05787 UniProtKB Repeat 103 139 . . . Note=Sel1-like 1 +Q05787 UniProtKB Repeat 143 186 . . . Note=Sel1-like 2 +Q05787 UniProtKB Repeat 187 222 . . . Note=Sel1-like 3 +Q05787 UniProtKB Repeat 413 445 . . . Note=Sel1-like 4 +Q05787 UniProtKB Repeat 552 595 . . . Note=Sel1-like 5 +Q05787 UniProtKB Repeat 596 627 . . . Note=Sel1-like 6 +Q05787 UniProtKB Repeat 628 663 . . . Note=Sel1-like 7 +Q05787 UniProtKB Compositional bias 809 819 . . . Note=Poly-Gln +Q05787 UniProtKB Glycosylation 101 101 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05787 UniProtKB Glycosylation 123 123 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05787 UniProtKB Glycosylation 142 142 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05787 UniProtKB Glycosylation 429 429 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05787 UniProtKB Glycosylation 611 611 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q99383 1 534 +Q99383 UniProtKB Chain 1 534 . . . ID=PRO_0000081658;Note=Nuclear polyadenylated RNA-binding protein 4 +Q99383 UniProtKB Domain 159 241 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q99383 UniProtKB Domain 243 320 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q99383 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q99383 UniProtKB Modified residue 3 3 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q99383 UniProtKB Modified residue 206 206 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q99383 UniProtKB Modified residue 458 458 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q99383 UniProtKB Modified residue 462 462 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q99383 UniProtKB Helix 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK +Q99383 UniProtKB Beta strand 160 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK +Q99383 UniProtKB Helix 172 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK +Q99383 UniProtKB Turn 180 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK +Q99383 UniProtKB Beta strand 185 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK +Q99383 UniProtKB Turn 194 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK +Q99383 UniProtKB Beta strand 203 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK +Q99383 UniProtKB Helix 211 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK +Q99383 UniProtKB Beta strand 223 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM8 +Q99383 UniProtKB Helix 236 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK +Q99383 UniProtKB Beta strand 243 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK +Q99383 UniProtKB Helix 256 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK +Q99383 UniProtKB Beta strand 265 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM8 +Q99383 UniProtKB Beta strand 270 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK +Q99383 UniProtKB Beta strand 277 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK +Q99383 UniProtKB Beta strand 284 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK +Q99383 UniProtKB Helix 294 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK +Q99383 UniProtKB Beta strand 304 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK +Q99383 UniProtKB Beta strand 308 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK +Q99383 UniProtKB Beta strand 313 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CJK +##sequence-region P29295 1 494 +P29295 UniProtKB Chain 1 494 . . . ID=PRO_0000192859;Note=Casein kinase I homolog HRR25 +P29295 UniProtKB Domain 9 278 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P29295 UniProtKB Nucleotide binding 15 23 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P29295 UniProtKB Compositional bias 395 494 . . . Note=Gln/Pro-rich +P29295 UniProtKB Active site 128 128 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P29295 UniProtKB Binding site 38 38 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P29295 UniProtKB Modified residue 143 143 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P29295 UniProtKB Beta strand 9 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Beta strand 22 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Turn 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Beta strand 34 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Turn 42 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XHL +P29295 UniProtKB Helix 49 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Turn 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Beta strand 68 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Beta strand 77 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Beta strand 85 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Helix 89 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Turn 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Helix 102 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Helix 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CZO +P29295 UniProtKB Beta strand 134 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Helix 139 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Beta strand 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Turn 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Helix 177 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Helix 182 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Helix 192 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Turn 212 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Helix 224 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Helix 237 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Turn 241 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Helix 246 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Helix 266 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Turn 276 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Helix 289 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Helix 330 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Helix 339 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Turn 345 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Helix 361 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Helix 367 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P29295 UniProtKB Helix 379 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +##sequence-region Q06674 1 414 +Q06674 UniProtKB Chain 1 414 . . . ID=PRO_0000233013;Note=Protein HIM1 +##sequence-region P32479 1 840 +P32479 UniProtKB Chain 1 840 . . . ID=PRO_0000051016;Note=Protein HIR1 +P32479 UniProtKB Repeat 15 54 . . . Note=WD 1 +P32479 UniProtKB Repeat 77 116 . . . Note=WD 2 +P32479 UniProtKB Repeat 135 174 . . . Note=WD 3 +P32479 UniProtKB Repeat 177 216 . . . Note=WD 4 +P32479 UniProtKB Repeat 230 273 . . . Note=WD 5 +P32479 UniProtKB Repeat 312 350 . . . Note=WD 6 +P32479 UniProtKB Repeat 354 393 . . . Note=WD 7 +P32479 UniProtKB Region 1 389 . . . Note=Mediates transcriptional repression +P32479 UniProtKB Region 304 840 . . . Note=Interaction with ASF1 +P32479 UniProtKB Region 392 840 . . . Note=Mediates transcriptional repression%2C self-association and interaction with HIR2 +P32479 UniProtKB Modified residue 610 610 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P32479 UniProtKB Sequence conflict 32 32 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32479 UniProtKB Sequence conflict 260 260 . . . Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32479 UniProtKB Sequence conflict 260 260 . . . Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32479 UniProtKB Sequence conflict 340 340 . . . Note=W->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P07172 1 385 +P07172 UniProtKB Chain 1 385 . . . ID=PRO_0000153509;Note=Histidinol-phosphate aminotransferase +P07172 UniProtKB Modified residue 230 230 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07172 UniProtKB Sequence conflict 110 112 . . . Note=PGK->RE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07172 UniProtKB Sequence conflict 125 125 . . . Note=Y->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07172 UniProtKB Sequence conflict 142 142 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07172 UniProtKB Sequence conflict 294 294 . . . Note=R->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40037 1 129 +P40037 UniProtKB Chain 1 129 . . . ID=PRO_0000170312;Note=Protein HMF1 +P40037 UniProtKB Cross-link 52 52 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P40037 UniProtKB Beta strand 5 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1 +P40037 UniProtKB Beta strand 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1 +P40037 UniProtKB Beta strand 22 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1 +P40037 UniProtKB Beta strand 29 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1 +P40037 UniProtKB Helix 49 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1 +P40037 UniProtKB Helix 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1 +P40037 UniProtKB Beta strand 74 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1 +P40037 UniProtKB Helix 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1 +P40037 UniProtKB Helix 87 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1 +P40037 UniProtKB Beta strand 98 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1 +P40037 UniProtKB Beta strand 104 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1 +P40037 UniProtKB Helix 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1 +P40037 UniProtKB Beta strand 118 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD1 +##sequence-region Q03973 1 246 +Q03973 UniProtKB Chain 1 246 . . . ID=PRO_0000048564;Note=High mobility group protein 1 +Q03973 UniProtKB DNA binding 106 179 . . . Note=HMG box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267 +Q03973 UniProtKB Compositional bias 228 241 . . . Note=Poly-Lys +##sequence-region P19807 1 563 +P19807 UniProtKB Chain 1 563 . . . ID=PRO_0000054155;Note=Choline transport protein +P19807 UniProtKB Topological domain 1 57 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Transmembrane 58 78 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Topological domain 79 87 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Transmembrane 88 108 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Topological domain 109 182 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Transmembrane 183 203 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Topological domain 204 205 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Transmembrane 206 226 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Topological domain 227 255 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Transmembrane 256 276 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Topological domain 277 293 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Transmembrane 294 314 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Topological domain 315 342 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Transmembrane 343 363 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Topological domain 364 398 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Transmembrane 399 417 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Topological domain 418 426 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Transmembrane 427 445 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Topological domain 446 465 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Transmembrane 466 486 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Topological domain 487 491 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Transmembrane 492 512 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Topological domain 513 563 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Modified residue 22 22 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P19807 UniProtKB Modified residue 42 42 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P19807 UniProtKB Glycosylation 7 7 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Glycosylation 20 20 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Glycosylation 248 248 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19807 UniProtKB Glycosylation 341 341 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47124 1 396 +P47124 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9434768;Dbxref=PMID:9434768 +P47124 UniProtKB Chain 2 396 . . . ID=PRO_0000080564;Note=Putative glycosyltransferase HOC1 +P47124 UniProtKB Topological domain 2 13 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47124 UniProtKB Transmembrane 14 34 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47124 UniProtKB Topological domain 35 396 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47124 UniProtKB Glycosylation 37 37 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47124 UniProtKB Sequence conflict 393 393 . . . Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q9URQ5 1 78 +Q9URQ5 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q9URQ5 UniProtKB Chain 2 78 . . . ID=PRO_0000084085;Note=High temperature lethal protein 1 +Q9URQ5 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P45820 1 110 +P45820 UniProtKB Chain 1 110 . . . ID=PRO_0000202728;Note=Putative uncharacterized protein HUR1 +P45820 UniProtKB Transmembrane 18 34 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32874 1 2273 +P32874 UniProtKB Transit peptide 1 104 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32874 UniProtKB Chain 105 2273 . . . ID=PRO_0000146771;Note=Acetyl-CoA carboxylase%2C mitochondrial +P32874 UniProtKB Domain 134 635 . . . Note=Biotin carboxylation +P32874 UniProtKB Domain 292 484 . . . Note=ATP-grasp;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 +P32874 UniProtKB Domain 763 837 . . . Note=Biotinyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066 +P32874 UniProtKB Domain 1532 1867 . . . Note=CoA carboxyltransferase N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01136 +P32874 UniProtKB Domain 1871 2187 . . . Note=CoA carboxyltransferase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01137 +P32874 UniProtKB Nucleotide binding 332 337 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 +P32874 UniProtKB Region 1532 2187 . . . Note=Carboxyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01138 +P32874 UniProtKB Active site 459 459 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32874 UniProtKB Binding site 1776 1776 . . . Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32874 UniProtKB Binding site 2080 2080 . . . Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32874 UniProtKB Binding site 2082 2082 . . . Note=Coenzyme A;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32874 UniProtKB Modified residue 804 804 . . . Note=N6-biotinyllysine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250,ECO:0000255|PROSITE-ProRule:PRU01066 +P32874 UniProtKB Sequence conflict 661 661 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32874 UniProtKB Sequence conflict 1027 1027 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38074 1 348 +P38074 UniProtKB Chain 1 348 . . . ID=PRO_0000212341;Note=Protein arginine N-methyltransferase 1 +P38074 UniProtKB Domain 20 322 . . . Note=SAM-dependent MTase PRMT-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01015 +P38074 UniProtKB Active site 132 132 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63009 +P38074 UniProtKB Active site 141 141 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63009 +P38074 UniProtKB Binding site 33 33 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63009 +P38074 UniProtKB Binding site 42 42 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63009 +P38074 UniProtKB Binding site 66 66 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63009 +P38074 UniProtKB Binding site 88 88 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63009 +P38074 UniProtKB Binding site 117 117 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63009 +P38074 UniProtKB Mutagenesis 18 18 . . . Note=Cold-sensitive%3B reduces catalytic activity more than 20-fold at 14 degrees Celsius. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10652296;Dbxref=PMID:10652296 +P38074 UniProtKB Mutagenesis 68 68 . . . Note=Reduces catalytic activity between 5- to 25-fold. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10652296;Dbxref=PMID:10652296 +P38074 UniProtKB Mutagenesis 68 68 . . . Note=Abolishes catalytic activity. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10652296;Dbxref=PMID:10652296 +P38074 UniProtKB Helix 30 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Helix 40 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Beta strand 61 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Helix 71 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Beta strand 82 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Helix 92 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Turn 106 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Beta strand 109 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Turn 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Beta strand 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Beta strand 126 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Helix 144 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Beta strand 155 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Beta strand 165 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Helix 176 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Helix 197 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Beta strand 206 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Helix 212 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Beta strand 220 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Turn 227 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Helix 232 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Beta strand 236 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Beta strand 250 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Beta strand 272 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Beta strand 286 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Beta strand 302 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Beta strand 315 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Helix 334 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +P38074 UniProtKB Beta strand 339 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6Q +##sequence-region P32339 1 317 +P32339 UniProtKB Chain 1 317 . . . ID=PRO_0000209704;Note=Heme-binding protein HMX1 +P32339 UniProtKB Topological domain 1 289 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32339 UniProtKB Transmembrane 290 310 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32339 UniProtKB Sequence conflict 128 128 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32339 UniProtKB Sequence conflict 285 285 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32339 UniProtKB Sequence conflict 310 310 . . . Note=V->VK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53096 1 452 +P53096 UniProtKB Chain 1 452 . . . ID=PRO_0000114723;Note=Probable histone deacetylase HOS2 +P53096 UniProtKB Region 26 340 . . . Note=Histone deacetylase +P53096 UniProtKB Active site 197 197 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53096 UniProtKB Mutagenesis 196 197 . . . Note=Leads to hyperacetylation. HH->AA +P53096 UniProtKB Sequence conflict 352 364 . . . Note=PFRDSFGPDYSLY->HSGTHSGRIIHFI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02959 1 697 +Q02959 UniProtKB Chain 1 697 . . . ID=PRO_0000114727;Note=Histone deacetylase HOS3 +Q02959 UniProtKB Region 40 440 . . . Note=Histone deacetylase +Q02959 UniProtKB Active site 196 196 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02959 UniProtKB Modified residue 582 582 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02959 UniProtKB Modified residue 583 583 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02959 UniProtKB Modified residue 613 613 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02959 UniProtKB Modified residue 629 629 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +##sequence-region P32478 1 413 +P32478 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1570286,ECO:0000269|PubMed:9301021;Dbxref=PMID:1570286,PMID:9301021 +P32478 UniProtKB Propeptide 19 72 . . . ID=PRO_0000033260;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10234784,ECO:0000269|PubMed:1570286,ECO:0000269|PubMed:18657192,ECO:0000269|PubMed:9301021;Dbxref=PMID:10234784,PMID:1570286,PMID:18657192,PMID:9301021 +P32478 UniProtKB Chain 73 413 . . . ID=PRO_0000033261;Note=Cell wall mannoprotein HSP150 +P32478 UniProtKB Repeat 73 89 . . . Note=PIR1/2/3 1;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32478 UniProtKB Repeat 97 115 . . . Note=PIR1/2/3 2;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32478 UniProtKB Repeat 116 134 . . . Note=PIR1/2/3 3;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32478 UniProtKB Repeat 140 158 . . . Note=PIR1/2/3 4;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32478 UniProtKB Repeat 164 182 . . . Note=PIR1/2/3 5;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32478 UniProtKB Repeat 188 206 . . . Note=PIR1/2/3 6;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32478 UniProtKB Repeat 207 225 . . . Note=PIR1/2/3 7;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32478 UniProtKB Repeat 226 244 . . . Note=PIR1/2/3 8;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32478 UniProtKB Repeat 245 263 . . . Note=PIR1/2/3 9;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32478 UniProtKB Repeat 264 282 . . . Note=PIR1/2/3 10;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32478 UniProtKB Repeat 283 300 . . . Note=PIR1/2/3 11;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +P32478 UniProtKB Site 72 73 . . . Note=Cleavage%3B by KEX2 +P32478 UniProtKB Site 81 81 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32478 UniProtKB Site 107 107 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32478 UniProtKB Site 126 126 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32478 UniProtKB Site 150 150 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32478 UniProtKB Site 174 174 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32478 UniProtKB Site 198 198 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32478 UniProtKB Site 217 217 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32478 UniProtKB Site 236 236 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32478 UniProtKB Site 255 255 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32478 UniProtKB Site 274 274 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32478 UniProtKB Site 292 292 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32478 UniProtKB Natural variant 96 96 . . . Note=In strain: B1%2C TD04/1a and TD04/1b. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657192;Dbxref=PMID:18657192 +P32478 UniProtKB Natural variant 116 163 . . . Note=In strain: B1%2C TD04/1a and TD04/1b. Missing +P32478 UniProtKB Natural variant 175 175 . . . Note=In strain: TD04/1a and TD04/1b. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657192;Dbxref=PMID:18657192 +P32478 UniProtKB Natural variant 176 176 . . . Note=In strain: TD04/1b. Q->QAATTTASVSTKSSAAAVSQIGDGQIQATTKTTAAAVSQIGDGQIQ +P32478 UniProtKB Natural variant 199 199 . . . Note=In strain: B1%2C TD04/1a and TD04/1b. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657192;Dbxref=PMID:18657192 +P32478 UniProtKB Natural variant 226 244 . . . Note=In strain: B1%2C TD04/1a and TD04/1b. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657192;Dbxref=PMID:18657192 +P32478 UniProtKB Natural variant 297 297 . . . Note=In strain: B1%2C TD04/1a and TD04/1b. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657192;Dbxref=PMID:18657192 +P32478 UniProtKB Sequence conflict 47 47 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32478 UniProtKB Sequence conflict 121 123 . . . Note=QIG->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32478 UniProtKB Sequence conflict 152 175 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32478 UniProtKB Sequence conflict 211 211 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32478 UniProtKB Sequence conflict 211 211 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32478 UniProtKB Sequence conflict 219 219 . . . Note=Q->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32478 UniProtKB Sequence conflict 219 219 . . . Note=Q->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32478 UniProtKB Sequence conflict 226 226 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32478 UniProtKB Sequence conflict 226 226 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P34244 1 1518 +P34244 UniProtKB Chain 1 1518 . . . ID=PRO_0000086148;Note=Probable serine/threonine-protein kinase HSL1 +P34244 UniProtKB Domain 81 369 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P34244 UniProtKB Nucleotide binding 87 95 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P34244 UniProtKB Active site 239 239 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P34244 UniProtKB Binding site 110 110 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P34244 UniProtKB Modified residue 511 511 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P34244 UniProtKB Modified residue 629 629 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P34244 UniProtKB Modified residue 685 685 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34244 UniProtKB Modified residue 837 837 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34244 UniProtKB Modified residue 866 866 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34244 UniProtKB Modified residue 1220 1220 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P34244 UniProtKB Modified residue 1250 1250 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34244 UniProtKB Modified residue 1284 1284 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P34244 UniProtKB Modified residue 1287 1287 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P34244 UniProtKB Modified residue 1325 1325 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P34244 UniProtKB Sequence conflict 1482 1482 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P34244 UniProtKB Sequence conflict 1482 1482 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P34244 UniProtKB Sequence conflict 1482 1482 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32590 1 693 +P32590 UniProtKB Chain 1 693 . . . ID=PRO_0000078397;Note=Heat shock protein homolog SSE2 +P32590 UniProtKB Sequence conflict 160 167 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40985 1 892 +P40985 UniProtKB Chain 1 892 . . . ID=PRO_0000084094;Note=Probable E3 ubiquitin-protein ligase HUL4 +P40985 UniProtKB Domain 792 892 . . . Note=HECT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00104 +P40985 UniProtKB Active site 860 860 . . . Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00104 +P40985 UniProtKB Sequence conflict 362 362 . . . Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40985 UniProtKB Sequence conflict 410 410 . . . Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40985 UniProtKB Sequence conflict 418 418 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40985 UniProtKB Sequence conflict 514 519 . . . Note=GKSVDV->RQIRRR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40985 UniProtKB Sequence conflict 589 607 . . . Note=ESSRSWFAIDPPNFDKSKG->KKAHVHGLPLTLQILTNQR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40985 UniProtKB Sequence conflict 705 705 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40985 UniProtKB Sequence conflict 723 724 . . . Note=KH->ND;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53982 1 420 +P53982 UniProtKB Chain 1 420 . . . ID=PRO_0000083588;Note=Isocitrate dehydrogenase [NADP] +P53982 UniProtKB Nucleotide binding 75 77 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53982 UniProtKB Nucleotide binding 310 315 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53982 UniProtKB Region 94 100 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53982 UniProtKB Metal binding 252 252 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53982 UniProtKB Metal binding 275 275 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53982 UniProtKB Binding site 77 77 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53982 UniProtKB Binding site 82 82 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53982 UniProtKB Binding site 109 109 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53982 UniProtKB Binding site 132 132 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53982 UniProtKB Binding site 260 260 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53982 UniProtKB Binding site 328 328 . . . Note=NADP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53982 UniProtKB Site 139 139 . . . Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53982 UniProtKB Site 212 212 . . . Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P48362 1 394 +P48362 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P48362 UniProtKB Chain 2 394 . . . ID=PRO_0000083966;Note=Protein HGH1 +P48362 UniProtKB Compositional bias 371 389 . . . Note=Asp/Glu-rich (highly acidic) +P48362 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P06775 1 603 +P06775 UniProtKB Chain 1 603 . . . ID=PRO_0000054154;Note=Histidine permease +P06775 UniProtKB Topological domain 1 95 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Transmembrane 96 116 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Topological domain 117 121 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Transmembrane 122 142 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Topological domain 143 165 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Transmembrane 166 185 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Topological domain 186 203 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Transmembrane 204 223 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Topological domain 224 236 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Transmembrane 237 255 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Topological domain 256 279 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Transmembrane 280 297 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Topological domain 298 321 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Transmembrane 322 342 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Topological domain 343 376 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Transmembrane 377 396 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Topological domain 397 423 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Transmembrane 424 442 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Topological domain 443 451 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Transmembrane 452 472 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Topological domain 473 491 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Transmembrane 492 510 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Topological domain 511 530 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Transmembrane 531 549 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Topological domain 550 603 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06775 UniProtKB Modified residue 76 76 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P12684 1 1045 +P12684 UniProtKB Chain 1 1045 . . . ID=PRO_0000114457;Note=3-hydroxy-3-methylglutaryl-coenzyme A reductase 2 +P12684 UniProtKB Topological domain 1 24 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Transmembrane 25 45 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Topological domain 46 186 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Transmembrane 187 207 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Topological domain 208 216 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Transmembrane 217 237 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Topological domain 238 243 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Transmembrane 244 264 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Topological domain 265 301 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Transmembrane 302 322 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Topological domain 323 324 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Transmembrane 325 345 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Topological domain 346 402 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Transmembrane 403 423 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Topological domain 424 497 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Transmembrane 498 518 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Topological domain 519 1045 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Domain 188 356 . . . Note=SSD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00199 +P12684 UniProtKB Region 524 613 . . . Note=Linker +P12684 UniProtKB Region 614 1045 . . . Note=Catalytic +P12684 UniProtKB Active site 710 710 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12684 UniProtKB Active site 844 844 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12684 UniProtKB Active site 920 920 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12684 UniProtKB Active site 1016 1016 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10003 +P12684 UniProtKB Modified residue 565 565 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P12684 UniProtKB Glycosylation 115 115 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Glycosylation 150 150 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Glycosylation 158 158 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Glycosylation 179 179 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Glycosylation 428 428 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Glycosylation 455 455 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12684 UniProtKB Sequence conflict 29 29 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53389 1 586 +P53389 UniProtKB Chain 1 586 . . . ID=PRO_0000084026;Note=Protein HOL1 +P53389 UniProtKB Topological domain 1 66 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Transmembrane 67 87 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Topological domain 88 103 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Transmembrane 104 124 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Topological domain 125 130 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Transmembrane 131 151 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Topological domain 152 189 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Transmembrane 190 210 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Topological domain 211 219 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Transmembrane 220 240 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Topological domain 241 362 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Transmembrane 363 383 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Topological domain 384 413 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Transmembrane 414 434 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Topological domain 435 448 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Transmembrane 449 469 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Topological domain 470 477 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Transmembrane 478 498 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Topological domain 499 508 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Transmembrane 509 529 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Topological domain 530 544 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Transmembrane 545 565 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Topological domain 566 586 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53389 UniProtKB Sequence conflict 510 510 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q05164 1 967 +Q05164 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05164 UniProtKB Chain 24 946 . . . ID=PRO_0000268177;Note=Haze protective factor 1 +Q05164 UniProtKB Propeptide 947 967 . . . ID=PRO_0000268178;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05164 UniProtKB Repeat 93 105 . . . Note=1-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q05164 UniProtKB Repeat 106 118 . . . Note=1-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q05164 UniProtKB Repeat 119 131 . . . Note=1-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q05164 UniProtKB Repeat 132 144 . . . Note=1-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q05164 UniProtKB Repeat 153 165 . . . Note=1-5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q05164 UniProtKB Repeat 166 178 . . . Note=1-6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q05164 UniProtKB Repeat 179 191 . . . Note=1-7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q05164 UniProtKB Repeat 192 204 . . . Note=1-8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q05164 UniProtKB Repeat 205 217 . . . Note=1-9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q05164 UniProtKB Repeat 218 230 . . . Note=1-10%3B approximate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q05164 UniProtKB Repeat 234 247 . . . Note=1-11%3B approximate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q05164 UniProtKB Repeat 248 259 . . . Note=1-12%3B approximate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q05164 UniProtKB Repeat 266 278 . . . Note=1-13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q05164 UniProtKB Repeat 745 780 . . . Note=2-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q05164 UniProtKB Repeat 781 815 . . . Note=2-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q05164 UniProtKB Repeat 816 854 . . . Note=2-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q05164 UniProtKB Repeat 855 893 . . . Note=2-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q05164 UniProtKB Repeat 894 902 . . . Note=2-5%3B truncated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q05164 UniProtKB Region 93 278 . . . Note=13 X approximate repeats%2C Ser-rich +Q05164 UniProtKB Region 745 902 . . . Note=4.5 X approximate tandem repeats%2C Thr-rich +Q05164 UniProtKB Lipidation 946 946 . . . Note=GPI-anchor amidated alanine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05164 UniProtKB Glycosylation 28 28 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05164 UniProtKB Glycosylation 35 35 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05164 UniProtKB Glycosylation 493 493 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05164 UniProtKB Glycosylation 601 601 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05164 UniProtKB Glycosylation 638 638 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38753 1 452 +P38753 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38753 UniProtKB Chain 2 452 . . . ID=PRO_0000202885;Note=Class E vacuolar protein-sorting machinery protein HSE1 +P38753 UniProtKB Domain 15 145 . . . Note=VHS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00218 +P38753 UniProtKB Domain 162 181 . . . Note=UIM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213 +P38753 UniProtKB Domain 217 276 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P38753 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38753 UniProtKB Modified residue 162 162 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38753 UniProtKB Helix 289 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW +P38753 UniProtKB Helix 296 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW +P38753 UniProtKB Helix 316 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW +P38753 UniProtKB Helix 322 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW +P38753 UniProtKB Helix 332 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW +P38753 UniProtKB Helix 335 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW +P38753 UniProtKB Turn 372 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PJW +##sequence-region P10961 1 833 +P10961 UniProtKB Chain 1 833 . . . ID=PRO_0000124581;Note=Heat shock factor protein +P10961 UniProtKB DNA binding 172 277 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3044612;Dbxref=PMID:3044612 +P10961 UniProtKB Region 350 402 . . . Note=Involved in trimerization +P10961 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P10961 UniProtKB Modified residue 97 97 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P10961 UniProtKB Modified residue 450 450 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P10961 UniProtKB Modified residue 458 458 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P10961 UniProtKB Modified residue 471 471 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P10961 UniProtKB Modified residue 478 478 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P10961 UniProtKB Modified residue 528 528 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P10961 UniProtKB Sequence conflict 522 522 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10961 UniProtKB Sequence conflict 557 580 . . . Note=FDIESNNDRKISEIPFDDEEEEET->LISNLIMTAKFQKFLLMTKKKKKP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10961 UniProtKB Sequence conflict 831 831 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q99181 1 213 +Q99181 UniProtKB Chain 1 213 . . . ID=PRO_0000081613;Note=Protein HSH49 +Q99181 UniProtKB Domain 9 88 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q99181 UniProtKB Domain 108 185 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q99181 UniProtKB Beta strand 10 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSL +Q99181 UniProtKB Helix 22 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSL +Q99181 UniProtKB Turn 30 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSL +Q99181 UniProtKB Beta strand 35 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSL +Q99181 UniProtKB Turn 44 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSL +Q99181 UniProtKB Beta strand 51 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSL +Q99181 UniProtKB Helix 60 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSL +Q99181 UniProtKB Turn 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSL +Q99181 UniProtKB Beta strand 82 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSL +Q99181 UniProtKB Beta strand 108 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB +Q99181 UniProtKB Helix 121 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB +Q99181 UniProtKB Beta strand 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB +Q99181 UniProtKB Beta strand 139 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB +Q99181 UniProtKB Beta strand 148 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB +Q99181 UniProtKB Helix 158 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB +Q99181 UniProtKB Beta strand 171 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB +Q99181 UniProtKB Beta strand 176 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB +Q99181 UniProtKB Turn 192 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB +Q99181 UniProtKB Helix 196 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LSB +##sequence-region P22943 1 109 +P22943 UniProtKB Chain 1 109 . . . ID=PRO_0000084081;Note=12 kDa heat shock protein +P22943 UniProtKB Modified residue 21 21 . . . Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +P22943 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P22943 UniProtKB Modified residue 59 59 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P22943 UniProtKB Modified residue 73 73 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P22943 UniProtKB Modified residue 97 97 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P22943 UniProtKB Natural variant 46 46 . . . Note=In strain: Ar5-H12. P->T +P22943 UniProtKB Helix 8 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9Q +P22943 UniProtKB Helix 25 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9Q +P22943 UniProtKB Helix 53 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9Q +P22943 UniProtKB Helix 58 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9Q +P22943 UniProtKB Beta strand 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LJL +P22943 UniProtKB Beta strand 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LJL +P22943 UniProtKB Helix 74 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9Q +##sequence-region P53687 1 447 +P53687 UniProtKB Chain 1 447 . . . ID=PRO_0000110283;Note=NAD-dependent histone deacetylase HST3 +P53687 UniProtKB Domain 43 349 . . . Note=Deacetylase sirtuin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53687 UniProtKB Nucleotide binding 60 79 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53687 UniProtKB Nucleotide binding 151 154 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53687 UniProtKB Nucleotide binding 282 284 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53687 UniProtKB Nucleotide binding 312 314 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53687 UniProtKB Active site 187 187 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53687 UniProtKB Metal binding 195 195 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53687 UniProtKB Metal binding 198 198 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53687 UniProtKB Metal binding 220 220 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53687 UniProtKB Metal binding 223 223 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53687 UniProtKB Binding site 333 333 . . . Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53687 UniProtKB Sequence conflict 418 418 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32485 1 435 +P32485 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32485 UniProtKB Chain 2 435 . . . ID=PRO_0000186331;Note=Mitogen-activated protein kinase HOG1 +P32485 UniProtKB Domain 23 302 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32485 UniProtKB Nucleotide binding 29 37 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32485 UniProtKB Motif 174 176 . . . Note=TXY +P32485 UniProtKB Compositional bias 364 379 . . . Note=Ala-rich +P32485 UniProtKB Active site 144 144 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P32485 UniProtKB Binding site 52 52 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32485 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32485 UniProtKB Modified residue 174 174 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12637550;Dbxref=PMID:12637550 +P32485 UniProtKB Modified residue 176 176 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:12637550;Dbxref=PMID:19779198,PMID:12637550 +P32485 UniProtKB Mutagenesis 52 52 . . . Note=Impairs catalytic activity%2C nuclear translocation%2C expression of CTT1 and increases sensitivity to osmotic shock. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16896207,ECO:0000269|PubMed:17363249,ECO:0000269|PubMed:7523111,ECO:0000269|PubMed:8943326;Dbxref=PMID:16896207,PMID:17363249,PMID:7523111,PMID:8943326 +P32485 UniProtKB Mutagenesis 68 68 . . . Note=Activates HOG1 in a constitutive manner%2C without the need of a stimulating stress. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11309396;Dbxref=PMID:11309396 +P32485 UniProtKB Mutagenesis 144 144 . . . Note=Impairs catalytic activity and nuclear translocation. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16896207;Dbxref=PMID:16896207 +P32485 UniProtKB Mutagenesis 170 170 . . . Note=Activates HOG1 in a constitutive manner%2C without the need of a stimulating stress. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11309396;Dbxref=PMID:11309396 +P32485 UniProtKB Mutagenesis 174 174 . . . Note=Impairs catalytic activity%2C expression of CTT1 and increases sensitivity to osmotic shock. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12637550,ECO:0000269|PubMed:7523111;Dbxref=PMID:12637550,PMID:7523111 +P32485 UniProtKB Mutagenesis 176 176 . . . Note=Impairs expression of CTT1 and increases sensitivity to osmotic shock. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12637550,ECO:0000269|PubMed:7523111;Dbxref=PMID:12637550,PMID:7523111 +P32485 UniProtKB Mutagenesis 314 314 . . . Note=Activates HOG1 in a constitutive manner%2C without the need of a stimulating stress. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11309396;Dbxref=PMID:11309396 +P32485 UniProtKB Mutagenesis 318 318 . . . Note=Activates HOG1 in a constitutive manner%2C without the need of a stimulating stress. F->L%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11309396;Dbxref=PMID:11309396 +P32485 UniProtKB Mutagenesis 320 320 . . . Note=Activates HOG1 in a constitutive manner%2C without the need of a stimulating stress. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11309396;Dbxref=PMID:11309396 +P32485 UniProtKB Mutagenesis 322 322 . . . Note=Activates HOG1 in a constitutive manner%2C without the need of a stimulating stress. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11309396;Dbxref=PMID:11309396 +P32485 UniProtKB Mutagenesis 332 332 . . . Note=Activates HOG1 in a constitutive manner%2C without the need of a stimulating stress. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11309396;Dbxref=PMID:11309396 +P32485 UniProtKB Mutagenesis 391 391 . . . Note=Activates HOG1 in a constitutive manner%2C without the need of a stimulating stress. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11309396;Dbxref=PMID:11309396 +P32485 UniProtKB Sequence conflict 9 9 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32485 UniProtKB Sequence conflict 409 435 . . . Note=VSDHVAANDTITDYGNQAIQYANEFQQ->GQRSCSCK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12122 1 440 +Q12122 UniProtKB Domain 37 290 . . . Note=Pyruvate carboxyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01151 +Q12122 UniProtKB Modified residue 399 399 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P48570 +Q12122 UniProtKB Modified residue 410 410 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12122 UniProtKB Sequence conflict 199 199 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03213 1 719 +Q03213 UniProtKB Chain 1 719 . . . ID=PRO_0000203317;Note=High-osmolarity-induced transcription protein 1 +Q03213 UniProtKB Modified residue 146 146 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03213 UniProtKB Modified residue 153 153 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03213 UniProtKB Mutagenesis 30 30 . . . Note=Impairs HOT1 phosphorylation%3B when associated with A-70%3B A-153%3B A-360 and A-410. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12743037;Dbxref=PMID:12743037 +Q03213 UniProtKB Mutagenesis 70 70 . . . Note=Impairs HOT1 phosphorylation%3B when associated with A-30%3B A-153%3B A-360 and A-410. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12743037;Dbxref=PMID:12743037 +Q03213 UniProtKB Mutagenesis 153 153 . . . Note=Impairs HOT1 phosphorylation%3B when associated with A-30%3B A-70%3B A-360 and A-410. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12743037;Dbxref=PMID:12743037 +Q03213 UniProtKB Mutagenesis 360 360 . . . Note=Impairs HOT1 phosphorylation%3B when associated with A-30%3B A-70%3B A-153 and A-410. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12743037;Dbxref=PMID:12743037 +Q03213 UniProtKB Mutagenesis 410 410 . . . Note=Impairs HOT1 phosphorylation%3B when associated with A-30%3B A-70%3B A-153 and A-360. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12743037;Dbxref=PMID:12743037 +##sequence-region P39734 1 528 +P39734 UniProtKB Chain 1 528 . . . ID=PRO_0000202415;Note=Protein HPH2 +P39734 UniProtKB Transmembrane 505 521 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39734 UniProtKB Compositional bias 308 328 . . . Note=Poly-Ser +P39734 UniProtKB Compositional bias 512 517 . . . Note=Poly-Ile +##sequence-region Q12347 1 344 +Q12347 UniProtKB Chain 1 344 . . . ID=PRO_0000245842;Note=F-box protein HRT3 +Q12347 UniProtKB Repeat 14 47 . . . Note=TPR +Q12347 UniProtKB Domain 98 148 . . . Note=F-box +##sequence-region P15992 1 214 +P15992 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:2673926;Dbxref=PMID:22814378,PMID:2673926 +P15992 UniProtKB Chain 2 214 . . . ID=PRO_0000126004;Note=Heat shock protein 26 +P15992 UniProtKB Domain 86 207 . . . Note=sHSP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00285 +P15992 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P15992 UniProtKB Modified residue 42 42 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P15992 UniProtKB Modified residue 90 90 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P15992 UniProtKB Modified residue 163 163 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P15992 UniProtKB Modified residue 208 208 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P15992 UniProtKB Modified residue 211 211 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P15992 UniProtKB Sequence conflict 32 32 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15992 UniProtKB Sequence conflict 207 207 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15992 UniProtKB Sequence conflict 212 212 . . . Note=W->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25619 1 332 +P25619 UniProtKB Chain 1 332 . . . ID=PRO_0000196284;Note=30 kDa heat shock protein +P25619 UniProtKB Topological domain 1 34 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25619 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25619 UniProtKB Topological domain 56 65 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25619 UniProtKB Transmembrane 66 86 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25619 UniProtKB Topological domain 87 121 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25619 UniProtKB Transmembrane 122 142 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25619 UniProtKB Topological domain 143 157 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25619 UniProtKB Transmembrane 158 178 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25619 UniProtKB Topological domain 179 181 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25619 UniProtKB Transmembrane 182 202 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25619 UniProtKB Topological domain 203 215 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25619 UniProtKB Transmembrane 216 236 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25619 UniProtKB Topological domain 237 248 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25619 UniProtKB Transmembrane 249 269 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25619 UniProtKB Topological domain 270 332 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25619 UniProtKB Compositional bias 290 332 . . . Note=Glu-rich (acidic) +P25619 UniProtKB Modified residue 308 308 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25619 UniProtKB Modified residue 331 331 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q08992 1 237 +Q08992 UniProtKB Chain 1 237 . . . ID=PRO_0000270555;Note=Probable glutathione-independent glyoxalase HSP32 +Q08992 UniProtKB Active site 138 138 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04432 +Q08992 UniProtKB Active site 139 139 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04432 +Q08992 UniProtKB Active site 170 170 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04432 +##sequence-region P40325 1 198 +P40325 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40325 UniProtKB Chain 2 198 . . . ID=PRO_0000202865;Note=Proline-rich protein HUA1 +P40325 UniProtKB Compositional bias 27 92 . . . Note=Pro-rich +P40325 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40325 UniProtKB Cross-link 3 3 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P40325 UniProtKB Cross-link 18 18 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region Q6Q546 1 73 +Q6Q546 UniProtKB Chain 1 73 . . . ID=PRO_0000114879;Note=Ubiquitin-like modifier HUB1 +Q6Q546 UniProtKB Domain 1 73 . . . Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 +Q6Q546 UniProtKB Sequence conflict 12 12 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q6Q546 UniProtKB Beta strand 1 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLU +Q6Q546 UniProtKB Turn 9 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M94 +Q6Q546 UniProtKB Beta strand 13 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLU +Q6Q546 UniProtKB Helix 24 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLU +Q6Q546 UniProtKB Helix 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLU +Q6Q546 UniProtKB Beta strand 42 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLU +Q6Q546 UniProtKB Helix 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLU +Q6Q546 UniProtKB Beta strand 67 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLU +##sequence-region Q12345 1 250 +Q12345 UniProtKB Chain 1 250 . . . ID=PRO_0000084155;Note=Ino eighty subunit 3 +Q12345 UniProtKB Modified residue 157 157 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12345 UniProtKB Modified residue 211 211 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P39730 1 1002 +P39730 UniProtKB Chain 1 1002 . . . ID=PRO_0000137296;Note=Eukaryotic translation initiation factor 5B +P39730 UniProtKB Domain 403 621 . . . Note=tr-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P39730 UniProtKB Nucleotide binding 415 420 . . . Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24686316;Dbxref=PMID:24686316 +P39730 UniProtKB Nucleotide binding 437 439 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0S8G9 +P39730 UniProtKB Nucleotide binding 530 533 . . . Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24686316;Dbxref=PMID:24686316 +P39730 UniProtKB Nucleotide binding 599 600 . . . Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24686316;Dbxref=PMID:24686316 +P39730 UniProtKB Region 412 419 . . . Note=G1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P39730 UniProtKB Region 437 441 . . . Note=G2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P39730 UniProtKB Region 476 479 . . . Note=G3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P39730 UniProtKB Region 530 533 . . . Note=G4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P39730 UniProtKB Region 598 600 . . . Note=G5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P39730 UniProtKB Compositional bias 361 371 . . . Note=Poly-Glu +P39730 UniProtKB Metal binding 415 415 . . . Note=Monovalent cation;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0S8G9 +P39730 UniProtKB Metal binding 419 419 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0S8G9 +P39730 UniProtKB Metal binding 437 437 . . . Note=Monovalent cation%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0S8G9 +P39730 UniProtKB Metal binding 439 439 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0S8G9 +P39730 UniProtKB Binding site 431 431 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0S8G9 +P39730 UniProtKB Modified residue 405 405 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39730 UniProtKB Mutagenesis 439 439 . . . Note=Impairs the GTPase activity%2C but not the ribosome joining function. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12507428;Dbxref=PMID:12507428 +P39730 UniProtKB Mutagenesis 479 479 . . . Note=Reduces GTP binding and impairs subunit joining and ribosome-dependent GTP hydrolysis. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17913624;Dbxref=PMID:17913624 +P39730 UniProtKB Mutagenesis 480 480 . . . Note=Impairs the GTPase activity%2C but not the ribosome joining function. H->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12471154,ECO:0000269|PubMed:12507428;Dbxref=PMID:12471154,PMID:12507428 +P39730 UniProtKB Sequence conflict 266 266 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39730 UniProtKB Sequence conflict 293 293 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39730 UniProtKB Sequence conflict 460 460 . . . Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39730 UniProtKB Sequence conflict 471 471 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39730 UniProtKB Sequence conflict 641 641 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39730 UniProtKB Sequence conflict 722 722 . . . Note=L->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39730 UniProtKB Sequence conflict 970 970 . . . Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39730 UniProtKB Beta strand 407 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 414 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI +P39730 UniProtKB Helix 421 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Beta strand 428 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI +P39730 UniProtKB Beta strand 439 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI +P39730 UniProtKB Beta strand 442 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 449 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 457 461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Beta strand 469 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Beta strand 478 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 481 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 487 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 490 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Beta strand 495 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Turn 503 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 509 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Beta strand 525 530 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 532 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 546 551 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 555 573 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Turn 574 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Beta strand 578 581 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 582 584 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Turn 588 590 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Beta strand 591 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Turn 599 601 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 605 619 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Turn 621 624 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Beta strand 631 640 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Turn 641 643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Beta strand 644 657 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Beta strand 661 666 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Beta strand 669 681 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 685 688 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Beta strand 692 709 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Beta strand 720 723 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI +P39730 UniProtKB Beta strand 726 728 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 730 746 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Beta strand 750 752 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI +P39730 UniProtKB Beta strand 755 761 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 762 774 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Beta strand 779 781 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Beta strand 784 787 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 789 796 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 798 801 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 803 805 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI +P39730 UniProtKB Beta strand 807 812 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 817 826 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Beta strand 829 835 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Helix 836 851 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N3S +P39730 UniProtKB Beta strand 866 879 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI +P39730 UniProtKB Beta strand 881 892 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI +P39730 UniProtKB Beta strand 896 903 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI +P39730 UniProtKB Turn 904 907 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI +P39730 UniProtKB Beta strand 908 922 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI +P39730 UniProtKB Beta strand 925 931 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI +P39730 UniProtKB Beta strand 939 944 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI +P39730 UniProtKB Turn 954 956 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI +P39730 UniProtKB Beta strand 963 965 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI +P39730 UniProtKB Helix 969 974 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI +P39730 UniProtKB Helix 978 981 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI +P39730 UniProtKB Helix 986 999 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WBI +##sequence-region Q04432 1 237 +Q04432 UniProtKB Chain 1 237 . . . ID=PRO_0000157852;Note=Glutathione-independent glyoxalase HSP31 +Q04432 UniProtKB Active site 138 138 . . . Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:14745011,ECO:0000305|PubMed:15130476;Dbxref=PMID:14745011,PMID:15130476 +Q04432 UniProtKB Active site 139 139 . . . Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:14745011,ECO:0000305|PubMed:15130476;Dbxref=PMID:14745011,PMID:15130476 +Q04432 UniProtKB Active site 170 170 . . . Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:14745011,ECO:0000305|PubMed:15130476;Dbxref=PMID:14745011,PMID:15130476 +Q04432 UniProtKB Modified residue 138 138 . . . Note=Cysteine sulfinic acid (-SO2H);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14745011;Dbxref=PMID:14745011 +Q04432 UniProtKB Sequence conflict 31 31 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q04432 UniProtKB Beta strand 5 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Helix 28 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Beta strand 44 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Beta strand 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QVZ +Q04432 UniProtKB Helix 58 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Turn 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Helix 68 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Helix 80 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Helix 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Beta strand 100 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Helix 110 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Helix 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Helix 118 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Beta strand 133 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Helix 140 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Turn 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Beta strand 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Turn 156 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Helix 167 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Helix 176 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Helix 187 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Beta strand 209 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Beta strand 215 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Helix 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +Q04432 UniProtKB Helix 224 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QYX +##sequence-region Q12329 1 375 +Q12329 UniProtKB Chain 1 375 . . . ID=PRO_0000126005;Note=Heat shock protein 42 +Q12329 UniProtKB Domain 237 356 . . . Note=sHSP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00285 +Q12329 UniProtKB Modified residue 182 182 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12329 UniProtKB Modified residue 213 213 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12329 UniProtKB Modified residue 214 214 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12329 UniProtKB Modified residue 215 215 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12329 UniProtKB Modified residue 223 223 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q05931 1 657 +Q05931 UniProtKB Mutagenesis 462 462 . . . Note=Decreased interaction with ISU1. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15958384;Dbxref=PMID:15958384 +Q05931 UniProtKB Mutagenesis 472 472 . . . Note=10-fold decrease in interaction with ISU1. V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15958384;Dbxref=PMID:15958384 +##sequence-region P38790 1 280 +P38790 UniProtKB Chain 1 280 . . . ID=PRO_0000202898;Note=Hydroxyacyl-thioester dehydratase type 2%2C mitochondrial +##sequence-region P53119 1 910 +P53119 UniProtKB Chain 1 910 . . . ID=PRO_0000084095;Note=Probable E3 ubiquitin-protein ligase HUL5 +P53119 UniProtKB Domain 810 910 . . . Note=HECT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00104 +P53119 UniProtKB Active site 878 878 . . . Note=Glycyl thioester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00104 +P53119 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P39924 1 564 +P39924 UniProtKB Chain 1 564 . . . ID=PRO_0000050402;Note=Hexose transporter HXT13 +P39924 UniProtKB Topological domain 1 52 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Transmembrane 53 73 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Topological domain 74 109 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Transmembrane 110 130 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Topological domain 131 136 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Transmembrane 137 157 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Topological domain 158 167 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Transmembrane 168 188 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Topological domain 189 194 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Transmembrane 195 215 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Topological domain 216 229 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Transmembrane 230 250 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Topological domain 251 333 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Transmembrane 334 350 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Topological domain 351 356 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Transmembrane 357 374 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Topological domain 375 381 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Transmembrane 382 402 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Topological domain 403 424 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Transmembrane 425 445 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Topological domain 446 462 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Transmembrane 463 483 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Topological domain 484 484 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Transmembrane 485 505 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39924 UniProtKB Topological domain 506 564 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P54854 1 567 +P54854 UniProtKB Chain 1 567 . . . ID=PRO_0000050404;Note=Hexose transporter HXT15 +P54854 UniProtKB Topological domain 1 55 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Transmembrane 56 76 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Topological domain 77 112 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Transmembrane 113 133 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Topological domain 134 139 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Transmembrane 140 160 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Topological domain 161 170 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Transmembrane 171 191 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Topological domain 192 197 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Transmembrane 198 218 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Topological domain 219 232 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Transmembrane 233 253 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Topological domain 254 336 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Transmembrane 337 353 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Topological domain 354 359 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Transmembrane 360 377 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Topological domain 378 384 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Transmembrane 385 405 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Topological domain 406 427 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Transmembrane 428 448 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Topological domain 449 465 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Transmembrane 466 486 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Topological domain 487 487 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Transmembrane 488 508 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54854 UniProtKB Topological domain 509 567 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32465 1 570 +P32465 UniProtKB Chain 1 570 . . . ID=PRO_0000050391;Note=Low-affinity glucose transporter HXT1 +P32465 UniProtKB Topological domain 1 60 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Transmembrane 61 81 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Topological domain 82 116 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Transmembrane 117 137 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Topological domain 138 143 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Transmembrane 144 164 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Topological domain 165 174 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Transmembrane 175 195 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Topological domain 196 201 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Transmembrane 202 222 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Topological domain 223 236 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Transmembrane 237 257 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Topological domain 258 340 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Transmembrane 341 357 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Topological domain 358 363 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Transmembrane 364 381 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Topological domain 382 388 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Transmembrane 389 409 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Topological domain 410 431 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Transmembrane 432 452 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Topological domain 453 469 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Transmembrane 470 490 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Topological domain 491 491 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Transmembrane 492 512 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Topological domain 513 570 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32465 UniProtKB Modified residue 38 38 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32465 UniProtKB Modified residue 44 44 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32465 UniProtKB Glycosylation 228 228 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32465 UniProtKB Sequence conflict 70 70 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32465 UniProtKB Sequence conflict 469 469 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32466 1 567 +P32466 UniProtKB Chain 1 567 . . . ID=PRO_0000050393;Note=Low-affinity glucose transporter HXT3 +P32466 UniProtKB Topological domain 1 57 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Transmembrane 58 78 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Topological domain 79 113 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Transmembrane 114 134 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Topological domain 135 140 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Transmembrane 141 161 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Topological domain 162 171 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Transmembrane 172 192 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Topological domain 193 198 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Transmembrane 199 219 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Topological domain 220 233 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Transmembrane 234 254 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Topological domain 255 337 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Transmembrane 338 354 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Topological domain 355 360 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Transmembrane 361 378 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Topological domain 379 385 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Transmembrane 386 406 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Topological domain 407 428 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Transmembrane 429 449 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Topological domain 450 466 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Transmembrane 467 487 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Topological domain 488 488 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Transmembrane 489 509 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Topological domain 510 567 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P32466 UniProtKB Glycosylation 225 225 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32466 UniProtKB Glycosylation 416 416 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38695 1 592 +P38695 UniProtKB Chain 1 592 . . . ID=PRO_0000050395;Note=Probable glucose transporter HXT5 +P38695 UniProtKB Topological domain 1 81 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Transmembrane 82 102 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Topological domain 103 137 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Transmembrane 138 158 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Topological domain 159 164 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Transmembrane 165 185 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Topological domain 186 195 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Transmembrane 196 216 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Topological domain 217 222 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Transmembrane 223 243 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Topological domain 244 257 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Transmembrane 258 278 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Topological domain 279 361 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Transmembrane 362 378 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Topological domain 379 384 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Transmembrane 385 402 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Topological domain 403 409 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Transmembrane 410 430 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Topological domain 431 452 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Transmembrane 453 473 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Topological domain 474 490 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Transmembrane 491 511 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Topological domain 512 512 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Transmembrane 513 533 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Topological domain 534 592 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Glycosylation 126 126 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Glycosylation 249 249 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38695 UniProtKB Cross-link 61 61 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region P39004 1 570 +P39004 UniProtKB Chain 1 570 . . . ID=PRO_0000050397;Note=High-affinity hexose transporter HXT7 +P39004 UniProtKB Topological domain 1 60 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Transmembrane 61 81 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Topological domain 82 116 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Transmembrane 117 137 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Topological domain 138 143 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Transmembrane 144 164 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Topological domain 165 174 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Transmembrane 175 195 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Topological domain 196 201 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Transmembrane 202 222 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Topological domain 223 236 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Transmembrane 237 257 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Topological domain 258 340 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Transmembrane 341 357 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Topological domain 358 363 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Transmembrane 364 381 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Topological domain 382 388 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Transmembrane 389 409 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Topological domain 410 431 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Transmembrane 432 452 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Topological domain 453 469 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Transmembrane 470 490 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Topological domain 491 491 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Transmembrane 492 512 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Topological domain 513 570 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Modified residue 556 556 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39004 UniProtKB Glycosylation 91 91 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Glycosylation 228 228 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39004 UniProtKB Cross-link 560 560 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region P32464 1 399 +P32464 UniProtKB Chain 1 399 . . . ID=PRO_0000209836;Note=Protein HYM1 +##sequence-region P41734 1 238 +P41734 UniProtKB Chain 1 238 . . . ID=PRO_0000084126;Note=Isoamyl acetate-hydrolyzing esterase +P41734 UniProtKB Active site 12 12 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41734 UniProtKB Active site 187 187 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41734 UniProtKB Active site 190 190 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41734 UniProtKB Binding site 53 53 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41734 UniProtKB Binding site 83 83 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41734 UniProtKB Beta strand 4 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Helix 12 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Turn 16 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Helix 32 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Turn 40 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Beta strand 44 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Helix 56 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Beta strand 73 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Turn 82 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Beta strand 86 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Helix 95 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Beta strand 115 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Helix 126 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Helix 134 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Helix 145 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Helix 169 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Helix 178 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Beta strand 185 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Helix 193 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Helix 212 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Helix 216 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Helix 226 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +P41734 UniProtKB Turn 234 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MIL +##sequence-region P46958 1 469 +P46958 UniProtKB Chain 1 469 . . . ID=PRO_0000084152;Note=IME2-dependent-signaling protein +P46958 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P46958 UniProtKB Modified residue 13 13 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P46958 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46958 UniProtKB Modified residue 27 27 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46958 UniProtKB Modified residue 39 39 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46958 UniProtKB Modified residue 122 122 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46958 UniProtKB Modified residue 130 130 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P46958 UniProtKB Modified residue 136 136 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P46958 UniProtKB Modified residue 147 147 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46958 UniProtKB Modified residue 148 148 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46958 UniProtKB Sequence conflict 268 268 . . . Note=G->GF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46958 UniProtKB Sequence conflict 282 282 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46958 UniProtKB Sequence conflict 361 361 . . . Note=R->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40060 1 125 +P40060 UniProtKB Chain 1 125 . . . ID=PRO_0000084157;Note=Ino eighty subunit 5 +P40060 UniProtKB Modified residue 124 124 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P20459 1 304 +P20459 UniProtKB Chain 1 304 . . . ID=PRO_0000137389;Note=Eukaryotic translation initiation factor 2 subunit alpha +P20459 UniProtKB Domain 17 88 . . . Note=S1 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180 +P20459 UniProtKB Modified residue 52 52 . . . Note=Phosphoserine%3B by GCN2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1739968;Dbxref=PMID:1739968 +P20459 UniProtKB Modified residue 292 292 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P20459 UniProtKB Modified residue 294 294 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P20459 UniProtKB Mutagenesis 52 52 . . . Note=Strongly impairs derepression of GCN4 expression in amino acid-starved cells. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1739968;Dbxref=PMID:1739968 +P20459 UniProtKB Mutagenesis 52 52 . . . Note=Weakly impairs derepression of GCN4 expression in amino acid-starved cells. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1739968;Dbxref=PMID:1739968 +P20459 UniProtKB Sequence conflict 258 258 . . . Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20459 UniProtKB Beta strand 8 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19 +P20459 UniProtKB Beta strand 19 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19 +P20459 UniProtKB Beta strand 31 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19 +P20459 UniProtKB Turn 37 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19 +P20459 UniProtKB Beta strand 43 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19 +P20459 UniProtKB Helix 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q46 +P20459 UniProtKB Helix 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q46 +P20459 UniProtKB Beta strand 67 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19 +P20459 UniProtKB Turn 78 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19 +P20459 UniProtKB Beta strand 82 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19 +P20459 UniProtKB Helix 92 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19 +P20459 UniProtKB Helix 123 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19 +P20459 UniProtKB Helix 131 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19 +P20459 UniProtKB Helix 141 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19 +P20459 UniProtKB Helix 152 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19 +P20459 UniProtKB Helix 163 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2A19 +##sequence-region P28817 1 500 +P28817 UniProtKB Chain 1 500 . . . ID=PRO_0000109357;Note=3-hydroxyisobutyryl-CoA hydrolase%2C mitochondrial +P28817 UniProtKB Binding site 124 124 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28817 UniProtKB Binding site 149 149 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28817 UniProtKB Binding site 172 172 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28817 UniProtKB Binding site 180 180 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28817 UniProtKB Modified residue 326 326 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P28817 UniProtKB Sequence conflict 139 139 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CY09 1 210 +P0CY09 UniProtKB Chain 1 210 . . . ID=PRO_0000410464;Note=Silenced mating-type protein ALPHA2 +P0CY09 UniProtKB DNA binding 129 191 . . . Note=Homeobox%3B TALE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00108 +P0CY09 UniProtKB Region 1 102 . . . Note=N-terminal domain +P0CY09 UniProtKB Region 103 128 . . . Note=Flexible linker +P0CY09 UniProtKB Region 190 210 . . . Note=C-terminal tail +P0CY09 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0CY08 +P0CY09 UniProtKB Sequence conflict 56 56 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0CY09 UniProtKB Sequence conflict 56 56 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0CY09 UniProtKB Sequence conflict 56 56 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12039 1 706 +Q12039 UniProtKB Chain 1 692 . . . ID=PRO_0000013297;Note=ATP-dependent DNA helicase HMI1%2C mitochondrial +Q12039 UniProtKB Propeptide 693 706 . . . ID=PRO_0000013298;Note=Cleaved upon import into mitochondrion +Q12039 UniProtKB Domain 5 277 . . . Note=UvrD-like helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00560 +Q12039 UniProtKB Domain 278 593 . . . Note=UvrD-like helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00617 +Q12039 UniProtKB Nucleotide binding 29 34 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00560 +Q12039 UniProtKB Binding site 275 275 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12039 UniProtKB Mutagenesis 704 704 . . . Note=Impaired import into mitochondrion. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10669756;Dbxref=PMID:10669756 +Q12039 UniProtKB Mutagenesis 705 705 . . . Note=Impaired import into mitochondrion. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10669756;Dbxref=PMID:10669756 +##sequence-region P20050 1 605 +P20050 UniProtKB Chain 1 605 . . . ID=PRO_0000126123;Note=Meiosis-specific protein HOP1 +P20050 UniProtKB Domain 20 250 . . . Note=HORMA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00109 +P20050 UniProtKB Zinc finger 348 364 . . . . +P20050 UniProtKB Natural variant 595 595 . . . Note=In allele HOP1-628%3B TS. S->N +##sequence-region Q05827 1 59 +Q05827 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05827 UniProtKB Chain 20 59 . . . ID=PRO_0000021448;Note=Protein HOR7 +Q05827 UniProtKB Compositional bias 22 28 . . . Note=Poly-Ser +##sequence-region Q06592 1 156 +Q06592 UniProtKB Chain 1 156 . . . ID=PRO_0000074633;Note=Histone acetyltransferase HPA2 +Q06592 UniProtKB Domain 9 156 . . . Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532 +Q06592 UniProtKB Region 93 106 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10600387;Dbxref=PMID:10600387 +Q06592 UniProtKB Site 139 139 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10600387;Dbxref=PMID:10600387 +Q06592 UniProtKB Beta strand 9 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM +Q06592 UniProtKB Helix 16 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM +Q06592 UniProtKB Helix 19 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM +Q06592 UniProtKB Helix 39 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM +Q06592 UniProtKB Turn 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSO +Q06592 UniProtKB Beta strand 56 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM +Q06592 UniProtKB Beta strand 69 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM +Q06592 UniProtKB Beta strand 87 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM +Q06592 UniProtKB Helix 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM +Q06592 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM +Q06592 UniProtKB Helix 104 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM +Q06592 UniProtKB Beta strand 124 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM +Q06592 UniProtKB Helix 133 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM +Q06592 UniProtKB Beta strand 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM +Q06592 UniProtKB Beta strand 147 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSM +##sequence-region Q04178 1 221 +Q04178 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q04178 UniProtKB Chain 2 221 . . . ID=PRO_0000257807;Note=Hypoxanthine-guanine phosphoribosyltransferase +Q04178 UniProtKB Nucleotide binding 110 118 . . . Note=GMP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18245832;Dbxref=PMID:18245832 +Q04178 UniProtKB Nucleotide binding 188 194 . . . Note=GMP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18245832;Dbxref=PMID:18245832 +Q04178 UniProtKB Active site 114 114 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04178 UniProtKB Binding site 85 85 . . . Note=GMP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18245832;Dbxref=PMID:18245832 +Q04178 UniProtKB Binding site 159 159 . . . Note=GMP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18245832;Dbxref=PMID:18245832 +Q04178 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q04178 UniProtKB Beta strand 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JKY +Q04178 UniProtKB Helix 11 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU +Q04178 UniProtKB Turn 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU +Q04178 UniProtKB Beta strand 31 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU +Q04178 UniProtKB Helix 37 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU +Q04178 UniProtKB Beta strand 60 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU +Q04178 UniProtKB Beta strand 85 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU +Q04178 UniProtKB Helix 94 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU +Q04178 UniProtKB Beta strand 105 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU +Q04178 UniProtKB Helix 117 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU +Q04178 UniProtKB Turn 141 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU +Q04178 UniProtKB Helix 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU +Q04178 UniProtKB Beta strand 150 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU +Q04178 UniProtKB Helix 169 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU +Q04178 UniProtKB Turn 175 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU +Q04178 UniProtKB Beta strand 178 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU +Q04178 UniProtKB Beta strand 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JKY +Q04178 UniProtKB Helix 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU +Q04178 UniProtKB Helix 198 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XBU +##sequence-region P38922 1 454 +P38922 UniProtKB Chain 1 454 . . . ID=PRO_0000081612;Note=Protein HRB1 +P38922 UniProtKB Domain 161 237 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P38922 UniProtKB Domain 261 338 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P38922 UniProtKB Domain 376 453 . . . Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P38922 UniProtKB Compositional bias 13 127 . . . Note=Arg-rich +P38922 UniProtKB Modified residue 343 343 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38922 UniProtKB Modified residue 355 355 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38922 UniProtKB Beta strand 161 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZR +P38922 UniProtKB Helix 174 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZR +P38922 UniProtKB Helix 182 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZR +P38922 UniProtKB Beta strand 187 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZR +P38922 UniProtKB Beta strand 203 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZR +P38922 UniProtKB Helix 212 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZR +P38922 UniProtKB Turn 218 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZR +P38922 UniProtKB Beta strand 232 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZR +P38922 UniProtKB Beta strand 263 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZS +P38922 UniProtKB Helix 274 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZS +P38922 UniProtKB Beta strand 289 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZS +P38922 UniProtKB Beta strand 304 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZS +P38922 UniProtKB Helix 311 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZS +P38922 UniProtKB Beta strand 325 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZS +P38922 UniProtKB Beta strand 333 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZS +P38922 UniProtKB Helix 359 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT +P38922 UniProtKB Turn 364 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT +P38922 UniProtKB Beta strand 368 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT +P38922 UniProtKB Beta strand 376 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT +P38922 UniProtKB Helix 389 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT +P38922 UniProtKB Turn 397 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT +P38922 UniProtKB Beta strand 402 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT +P38922 UniProtKB Beta strand 415 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT +P38922 UniProtKB Helix 426 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT +P38922 UniProtKB Turn 436 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT +P38922 UniProtKB Beta strand 447 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZT +##sequence-region Q08109 1 551 +Q08109 UniProtKB Chain 1 551 . . . ID=PRO_0000240367;Note=ERAD-associated E3 ubiquitin-protein ligase HRD1 +Q08109 UniProtKB Topological domain 1 8 . . . Note=Cytoplasmic +Q08109 UniProtKB Transmembrane 9 29 . . . Note=Helical%3B Name%3D1 +Q08109 UniProtKB Topological domain 30 45 . . . Note=Lumenal +Q08109 UniProtKB Transmembrane 46 66 . . . Note=Helical%3B Name%3D2 +Q08109 UniProtKB Topological domain 67 82 . . . Note=Cytoplasmic +Q08109 UniProtKB Transmembrane 83 103 . . . Note=Helical%3B Name%3D3 +Q08109 UniProtKB Topological domain 104 104 . . . Note=Lumenal +Q08109 UniProtKB Transmembrane 105 125 . . . Note=Helical%3B Name%3D4 +Q08109 UniProtKB Topological domain 126 144 . . . Note=Cytoplasmic +Q08109 UniProtKB Transmembrane 145 165 . . . Note=Helical%3B Name%3D5 +Q08109 UniProtKB Topological domain 166 184 . . . Note=Lumenal +Q08109 UniProtKB Transmembrane 185 205 . . . Note=Helical%3B Name%3D6 +Q08109 UniProtKB Topological domain 206 551 . . . Note=Cytoplasmic +Q08109 UniProtKB Zinc finger 349 400 . . . Note=RING-type%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +Q08109 UniProtKB Region 517 551 . . . Note=Interaction with USA1 +Q08109 UniProtKB Compositional bias 413 483 . . . Note=Thr-rich +Q08109 UniProtKB Mutagenesis 399 399 . . . Note=Stabilizes HRD1. Reduced interaction with substrate. Formation of oligomer with or without USA1. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11018054,ECO:0000269|PubMed:11139575,ECO:0000269|PubMed:11146622,ECO:0000269|PubMed:20005842,ECO:0000269|PubMed:21074049;Dbxref=PMID:11018054,PMID:11139575,PMID:11146622,PMID:20005842,PMID:21074049 +##sequence-region Q08732 1 759 +Q08732 UniProtKB Chain 1 759 . . . ID=PRO_0000086002;Note=Serine/threonine-protein kinase HRK1 +Q08732 UniProtKB Domain 215 722 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q08732 UniProtKB Nucleotide binding 221 229 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q08732 UniProtKB Compositional bias 628 647 . . . Note=Poly-Gln +Q08732 UniProtKB Compositional bias 648 653 . . . Note=Poly-His +Q08732 UniProtKB Active site 340 340 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q08732 UniProtKB Binding site 244 244 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q08732 UniProtKB Modified residue 37 37 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q08732 UniProtKB Modified residue 382 382 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q08732 UniProtKB Modified residue 472 472 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q08732 UniProtKB Modified residue 495 495 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q08732 UniProtKB Modified residue 498 498 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P69852 1 69 +P69852 UniProtKB Chain 1 69 . . . ID=PRO_0000084079;Note=DASH complex subunit HSK3 +P69852 UniProtKB Coiled coil 1 39 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08914 1 237 +Q08914 UniProtKB Chain 1 237 . . . ID=PRO_0000270556;Note=Probable glutathione-independent glyoxalase HSP33 +Q08914 UniProtKB Active site 138 138 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:21139195;Dbxref=PMID:21139195 +Q08914 UniProtKB Active site 139 139 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:21139195;Dbxref=PMID:21139195 +Q08914 UniProtKB Active site 170 170 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:21139195;Dbxref=PMID:21139195 +Q08914 UniProtKB Beta strand 5 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Helix 28 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Turn 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Beta strand 44 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Helix 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MII +Q08914 UniProtKB Helix 62 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MII +Q08914 UniProtKB Helix 69 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MII +Q08914 UniProtKB Helix 82 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Helix 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Beta strand 100 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Helix 110 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Helix 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Helix 118 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Beta strand 133 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Helix 140 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Turn 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Beta strand 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Turn 156 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Helix 167 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Turn 173 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Helix 176 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Helix 187 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Turn 193 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Beta strand 209 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Beta strand 215 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Helix 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +Q08914 UniProtKB Helix 224 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KKL +##sequence-region P50079 1 448 +P50079 UniProtKB Chain 1 448 . . . ID=PRO_0000051034;Note=SVP1-like protein 2 +P50079 UniProtKB Repeat 222 262 . . . Note=WD 1 +P50079 UniProtKB Repeat 267 306 . . . Note=WD 2 +P50079 UniProtKB Glycosylation 61 61 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50079 UniProtKB Glycosylation 155 155 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50079 UniProtKB Glycosylation 256 256 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50079 UniProtKB Glycosylation 280 280 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50079 UniProtKB Glycosylation 315 315 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50079 UniProtKB Glycosylation 421 421 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q6Q5K6 1 68 +Q6Q5K6 UniProtKB Chain 1 68 . . . ID=PRO_0000240383;Note=MEC1-mediated checkpoint protein HUG1 +##sequence-region P04806 1 485 +P04806 UniProtKB Chain 1 485 . . . ID=PRO_0000197601;Note=Hexokinase-1 +P04806 UniProtKB Domain 21 468 . . . Note=Hexokinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084 +P04806 UniProtKB Nucleotide binding 86 91 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04806 UniProtKB Nucleotide binding 307 308 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04806 UniProtKB Nucleotide binding 344 348 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04806 UniProtKB Nucleotide binding 419 423 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04806 UniProtKB Region 75 209 . . . Note=Hexokinase small subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084 +P04806 UniProtKB Region 175 176 . . . Note=Substrate binding +P04806 UniProtKB Region 210 457 . . . Note=Hexokinase large subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084 +P04806 UniProtKB Region 210 211 . . . Note=Substrate binding +P04806 UniProtKB Binding site 111 111 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04806 UniProtKB Binding site 158 158 . . . Note=Substrate%3B via carbonyl oxygen +P04806 UniProtKB Binding site 237 237 . . . Note=Substrate +P04806 UniProtKB Binding site 269 269 . . . Note=Substrate +P04806 UniProtKB Binding site 302 302 . . . Note=Substrate +P04806 UniProtKB Modified residue 245 245 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P04806 UniProtKB Modified residue 272 272 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P04806 UniProtKB Sequence conflict 61 61 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04806 UniProtKB Sequence conflict 103 103 . . . Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04806 UniProtKB Sequence conflict 194 194 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04806 UniProtKB Sequence conflict 244 244 . . . Note=V->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04806 UniProtKB Sequence conflict 356 357 . . . Note=EN->VF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04806 UniProtKB Sequence conflict 364 364 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04806 UniProtKB Sequence conflict 388 388 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04806 UniProtKB Sequence conflict 444 444 . . . Note=D->EN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04806 UniProtKB Sequence conflict 479 480 . . . Note=SL->VS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04806 UniProtKB Helix 21 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 38 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Beta strand 57 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Beta strand 80 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Beta strand 89 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Beta strand 101 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 116 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 125 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Beta strand 151 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 188 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 197 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Beta strand 202 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 211 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Beta strand 226 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 244 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 248 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Beta strand 263 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 270 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Turn 273 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Beta strand 278 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 284 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Beta strand 293 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 300 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 307 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Turn 323 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Beta strand 326 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Turn 334 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 345 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 359 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 375 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 398 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Beta strand 410 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 419 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 427 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Turn 444 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Beta strand 449 454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Turn 458 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Helix 461 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +P04806 UniProtKB Beta strand 480 482 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B8A +##sequence-region P04807 1 486 +P04807 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9718324;Dbxref=PMID:9718324 +P04807 UniProtKB Chain 2 486 . . . ID=PRO_0000197602;Note=Hexokinase-2 +P04807 UniProtKB Domain 21 469 . . . Note=Hexokinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084 +P04807 UniProtKB Nucleotide binding 86 91 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04807 UniProtKB Nucleotide binding 307 308 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04807 UniProtKB Nucleotide binding 344 348 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04807 UniProtKB Nucleotide binding 419 423 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04807 UniProtKB Region 75 209 . . . Note=Hexokinase small subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084 +P04807 UniProtKB Region 175 176 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04807 UniProtKB Region 210 458 . . . Note=Hexokinase large subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084 +P04807 UniProtKB Region 210 211 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04807 UniProtKB Binding site 111 111 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04807 UniProtKB Binding site 158 158 . . . Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04807 UniProtKB Binding site 237 237 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04807 UniProtKB Binding site 269 269 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04807 UniProtKB Binding site 302 302 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04807 UniProtKB Modified residue 15 15 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:8286332,ECO:0000269|PubMed:9718324;Dbxref=PMID:19779198,PMID:8286332,PMID:9718324 +P04807 UniProtKB Modified residue 38 38 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P04807 UniProtKB Modified residue 158 158 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:9047292;Dbxref=PMID:18407956,PMID:9047292 +P04807 UniProtKB Modified residue 245 245 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04807 UniProtKB Modified residue 272 272 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04806 +P04807 UniProtKB Sequence conflict 29 29 . . . Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04807 UniProtKB Sequence conflict 33 33 . . . Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04807 UniProtKB Sequence conflict 33 33 . . . Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04807 UniProtKB Sequence conflict 61 61 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04807 UniProtKB Sequence conflict 197 197 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04807 UniProtKB Sequence conflict 202 202 . . . Note=P->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04807 UniProtKB Sequence conflict 421 422 . . . Note=YN->ST;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04807 UniProtKB Sequence conflict 421 422 . . . Note=YN->ST;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04807 UniProtKB Sequence conflict 444 445 . . . Note=TS->PH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04807 UniProtKB Sequence conflict 444 445 . . . Note=TS->PH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04807 UniProtKB Sequence conflict 453 453 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04807 UniProtKB Sequence conflict 453 453 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04807 UniProtKB Sequence conflict 462 462 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04807 UniProtKB Sequence conflict 462 462 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04807 UniProtKB Helix 21 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8 +P04807 UniProtKB Helix 38 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8 +P04807 UniProtKB Beta strand 79 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8 +P04807 UniProtKB Beta strand 89 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8 +P04807 UniProtKB Beta strand 105 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8 +P04807 UniProtKB Helix 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8 +P04807 UniProtKB Helix 126 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8 +P04807 UniProtKB Beta strand 152 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Beta strand 159 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8 +P04807 UniProtKB Helix 189 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Beta strand 203 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Helix 211 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Beta strand 226 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Helix 244 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Helix 248 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8 +P04807 UniProtKB Beta strand 254 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Beta strand 264 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Turn 271 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Beta strand 278 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Helix 284 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Beta strand 293 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8 +P04807 UniProtKB Helix 300 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Helix 307 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Helix 310 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Beta strand 326 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Turn 334 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8 +P04807 UniProtKB Helix 345 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Beta strand 355 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Helix 359 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Helix 375 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Helix 398 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Beta strand 410 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Helix 419 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IG8 +P04807 UniProtKB Helix 427 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Helix 446 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Beta strand 449 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Turn 459 461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +P04807 UniProtKB Helix 462 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YHX +##sequence-region Q12134 1 243 +Q12134 UniProtKB Chain 1 243 . . . ID=PRO_0000270558;Note=Protein HUA2 +##sequence-region Q12520 1 339 +Q12520 UniProtKB Chain 1 339 . . . ID=PRO_0000213414;Note=UDP-galactose transporter homolog 1 +Q12520 UniProtKB Topological domain 1 4 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Transmembrane 5 25 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Topological domain 26 42 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Transmembrane 43 63 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Topological domain 64 106 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Transmembrane 107 127 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Topological domain 128 136 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Transmembrane 137 157 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Topological domain 158 174 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Transmembrane 175 192 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Topological domain 193 214 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Transmembrane 215 235 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Topological domain 236 245 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Transmembrane 246 266 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Topological domain 267 280 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Transmembrane 281 303 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Topological domain 304 307 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Transmembrane 308 327 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Topological domain 328 339 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12520 UniProtKB Glycosylation 165 165 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12385 1 394 +Q12385 UniProtKB Chain 1 394 . . . ID=PRO_0000080854;Note=1-acylglycerol-3-phosphate O-acyltransferase ICT1 +Q12385 UniProtKB Domain 74 381 . . . Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12385 UniProtKB Motif 374 379 . . . Note=HXXXXD motif +##sequence-region P15496 1 288 +P15496 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2681212;Dbxref=PMID:2681212 +P15496 UniProtKB Chain 2 288 . . . ID=PRO_0000205231;Note=Isopentenyl-diphosphate Delta-isomerase +P15496 UniProtKB Domain 102 259 . . . Note=Nudix hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00794 +P15496 UniProtKB Active site 139 139 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15496 UniProtKB Active site 207 207 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15496 UniProtKB Metal binding 93 93 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15496 UniProtKB Metal binding 104 104 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15496 UniProtKB Metal binding 205 205 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15496 UniProtKB Metal binding 207 207 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15496 UniProtKB Binding site 89 89 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15496 UniProtKB Binding site 123 123 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15496 UniProtKB Binding site 127 127 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15496 UniProtKB Binding site 140 140 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15496 UniProtKB Modified residue 7 7 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P15496 UniProtKB Mutagenesis 138 138 . . . Note=10-fold reduction in activity. C->S%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7908830;Dbxref=PMID:7908830 +P15496 UniProtKB Mutagenesis 139 139 . . . Note=Inactive. C->A%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7908830;Dbxref=PMID:7908830 +P15496 UniProtKB Mutagenesis 139 139 . . . Note=Reduces activity over 100000-fold. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7908830;Dbxref=PMID:7908830 +P15496 UniProtKB Mutagenesis 207 207 . . . Note=Inactive. E->Q%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7908830;Dbxref=PMID:7908830 +##sequence-region P09064 1 285 +P09064 UniProtKB Chain 1 285 . . . ID=PRO_0000137415;Note=Eukaryotic translation initiation factor 2 subunit beta +P09064 UniProtKB Zinc finger 236 262 . . . Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P09064 UniProtKB Compositional bias 16 23 . . . Note=Lys-rich (basic) +P09064 UniProtKB Compositional bias 49 56 . . . Note=Lys-rich (basic) +P09064 UniProtKB Compositional bias 82 89 . . . Note=Lys-rich (basic) +P09064 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P09064 UniProtKB Modified residue 69 69 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P09064 UniProtKB Modified residue 80 80 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P09064 UniProtKB Modified residue 92 92 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P09064 UniProtKB Modified residue 112 112 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P09064 UniProtKB Modified residue 116 116 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P09064 UniProtKB Modified residue 118 118 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P09064 UniProtKB Mutagenesis 16 23 . . . Note=Abolishes interaction with TIF5%3B when associated with 49-K--K-56 and 82-K--K-89. KKKKKTKK->AAAAATAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10075937;Dbxref=PMID:10075937 +P09064 UniProtKB Mutagenesis 49 56 . . . Note=Abolishes interaction with TIF5%3B when associated with 16-K--K-23 and 82-K--K-89. KKKKKKSK->AAAAAASA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10075937;Dbxref=PMID:10075937 +P09064 UniProtKB Mutagenesis 82 89 . . . Note=Abolishes interaction with TIF5%3B when associated with 16-K--K-23 and 49-K--K-56. KKKKKKTK->AAAAAATA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10075937;Dbxref=PMID:10075937 +P09064 UniProtKB Sequence conflict 141 141 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P10081 1 395 +P10081 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:9298649;Dbxref=PMID:22814378,PMID:9298649 +P10081 UniProtKB Chain 2 395 . . . ID=PRO_0000054968;Note=ATP-dependent RNA helicase eIF4A +P10081 UniProtKB Domain 53 222 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P10081 UniProtKB Domain 233 394 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P10081 UniProtKB Nucleotide binding 66 73 . . . Note=ATP +P10081 UniProtKB Motif 22 50 . . . Note=Q motif +P10081 UniProtKB Motif 170 173 . . . Note=DEAD box +P10081 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:9298649;Dbxref=PMID:22814378,PMID:9298649 +P10081 UniProtKB Modified residue 73 73 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P10081 UniProtKB Modified residue 77 77 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P10081 UniProtKB Modified residue 129 129 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P10081 UniProtKB Modified residue 146 146 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P10081 UniProtKB Mutagenesis 24 24 . . . Note=Lethal in vivo and reduces ATP binding and ATPase activity in vitro. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12535527;Dbxref=PMID:12535527 +P10081 UniProtKB Mutagenesis 42 42 . . . Note=Slow growth in vivo and reduces ATP binding and ATPase activity in vitro. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12535527;Dbxref=PMID:12535527 +P10081 UniProtKB Mutagenesis 46 46 . . . Note=Reduces ATP binding and ATPase activity in vitro. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12535527;Dbxref=PMID:12535527 +P10081 UniProtKB Mutagenesis 49 49 . . . Note=Reduces ATP binding and ATPase activity in vitro. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12535527;Dbxref=PMID:12535527 +P10081 UniProtKB Mutagenesis 49 49 . . . Note=Increases about 3-fold ATP binding but reduces about 2-fold ATPase activity in vitro. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12535527;Dbxref=PMID:12535527 +P10081 UniProtKB Mutagenesis 66 66 . . . Note=Slow growth. A->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1502180,ECO:0000269|PubMed:2046664;Dbxref=PMID:1502180,PMID:2046664 +P10081 UniProtKB Mutagenesis 66 66 . . . Note=Lethal and dominant negative if overexpressed in vivo. Impairs ATP hydrolysis%2C RNA-helicase and translation activity in vitro. A->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1502180,ECO:0000269|PubMed:2046664;Dbxref=PMID:1502180,PMID:2046664 +P10081 UniProtKB Mutagenesis 72 72 . . . Note=Lethal in vivo and reduces ATP binding and ATPase activity in vitro. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12535527;Dbxref=PMID:12535527 +P10081 UniProtKB Mutagenesis 79 79 . . . Note=In TIF1-1%3B no growth at 36 degrees Celsius. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2046664;Dbxref=PMID:2046664 +P10081 UniProtKB Mutagenesis 126 126 . . . Note=Lethal. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2046664;Dbxref=PMID:2046664 +P10081 UniProtKB Mutagenesis 127 127 . . . Note=Slow growth. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2046664;Dbxref=PMID:2046664 +P10081 UniProtKB Mutagenesis 145 145 . . . Note=Lethal. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2046664;Dbxref=PMID:2046664 +P10081 UniProtKB Mutagenesis 145 145 . . . Note=Slow growth. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2046664;Dbxref=PMID:2046664 +P10081 UniProtKB Mutagenesis 170 170 . . . Note=Lethal. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2046664;Dbxref=PMID:2046664 +P10081 UniProtKB Mutagenesis 173 173 . . . Note=Lethal. D->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2046664;Dbxref=PMID:2046664 +P10081 UniProtKB Mutagenesis 311 311 . . . Note=Slow growth. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2046664;Dbxref=PMID:2046664 +P10081 UniProtKB Mutagenesis 347 347 . . . Note=Lethal and dominant negative if overexpressed. R->E%2CG%2CI%2CS%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2046664;Dbxref=PMID:2046664 +P10081 UniProtKB Beta strand 13 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUU +P10081 UniProtKB Helix 24 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE +P10081 UniProtKB Helix 31 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE +P10081 UniProtKB Helix 47 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE +P10081 UniProtKB Beta strand 62 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE +P10081 UniProtKB Helix 72 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE +P10081 UniProtKB Beta strand 93 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE +P10081 UniProtKB Helix 100 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE +P10081 UniProtKB Turn 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE +P10081 UniProtKB Beta strand 121 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE +P10081 UniProtKB Helix 130 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUU +P10081 UniProtKB Beta strand 141 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE +P10081 UniProtKB Helix 147 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE +P10081 UniProtKB Beta strand 166 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE +P10081 UniProtKB Helix 172 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE +P10081 UniProtKB Helix 181 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE +P10081 UniProtKB Beta strand 196 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE +P10081 UniProtKB Helix 206 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE +P10081 UniProtKB Beta strand 220 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QDE +P10081 UniProtKB Beta strand 235 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK +P10081 UniProtKB Helix 244 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK +P10081 UniProtKB Helix 247 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK +P10081 UniProtKB Beta strand 263 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK +P10081 UniProtKB Helix 270 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK +P10081 UniProtKB Beta strand 287 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK +P10081 UniProtKB Helix 296 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK +P10081 UniProtKB Beta strand 312 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK +P10081 UniProtKB Helix 318 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK +P10081 UniProtKB Turn 321 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK +P10081 UniProtKB Beta strand 330 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK +P10081 UniProtKB Helix 341 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK +P10081 UniProtKB Beta strand 359 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK +P10081 UniProtKB Turn 366 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK +P10081 UniProtKB Helix 369 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK +P10081 UniProtKB Beta strand 383 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUU +P10081 UniProtKB Turn 391 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FUK +##sequence-region P39936 1 914 +P39936 UniProtKB Chain 1 914 . . . ID=PRO_0000213332;Note=Eukaryotic initiation factor 4F subunit p130 +P39936 UniProtKB Domain 567 810 . . . Note=MIF4G +P39936 UniProtKB Region 201 315 . . . Note=Interaction with PAB1 +P39936 UniProtKB Compositional bias 32 97 . . . Note=Asn-rich +P39936 UniProtKB Compositional bias 459 510 . . . Note=Arg/Ser-rich +P39936 UniProtKB Compositional bias 840 863 . . . Note=Arg/Ser-rich +P39936 UniProtKB Modified residue 74 74 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39936 UniProtKB Modified residue 196 196 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P39936 UniProtKB Modified residue 301 301 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P39936 UniProtKB Modified residue 503 503 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P39936 UniProtKB Modified residue 913 913 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P39936 UniProtKB Mutagenesis 233 236 . . . Note=In TIF4632-233%3B abolishes interaction with PAB1 and inhibits poly(A)-dependent translation. RLRK->AVAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9256432;Dbxref=PMID:9256432 +##sequence-region P47175 1 358 +P47175 UniProtKB Chain 1 358 . . . ID=PRO_0000124596;Note=Probable transcription factor HMS2 +P47175 UniProtKB DNA binding 12 116 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P09932 1 586 +P09932 UniProtKB Chain 1 586 . . . ID=PRO_0000084030;Note=Homothallic switching endonuclease +P09932 UniProtKB Domain 215 370 . . . Note=DOD-type homing endonuclease;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00273 +P09932 UniProtKB Sequence conflict 189 189 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09932 UniProtKB Sequence conflict 223 223 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09932 UniProtKB Sequence conflict 405 405 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09932 UniProtKB Sequence conflict 475 475 . . . Note=L->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39979 1 161 +P39979 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P39979 UniProtKB Chain 2 161 . . . ID=PRO_0000074634;Note=D-amino-acid N-acetyltransferase HPA3 +P39979 UniProtKB Domain 14 161 . . . Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532 +P39979 UniProtKB Region 98 111 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06592 +P39979 UniProtKB Site 144 144 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06592 +P39979 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P38348 1 480 +P38348 UniProtKB Chain 1 480 . . . ID=PRO_0000202532;Note=DNA mismatch repair protein HSM3 +P38348 UniProtKB Helix 10 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Beta strand 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A3T +P38348 UniProtKB Helix 29 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 52 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 73 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 89 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 98 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 110 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 126 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 134 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 150 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 167 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Turn 175 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 178 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 190 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Turn 209 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 214 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 221 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 231 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 254 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 257 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 261 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 264 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Turn 274 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 278 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 285 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Beta strand 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FP7 +P38348 UniProtKB Helix 304 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Turn 316 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLE +P38348 UniProtKB Helix 320 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 323 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 332 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 340 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 351 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 354 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 364 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 371 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 376 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 384 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 398 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 409 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 421 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 427 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 445 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 449 451 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +P38348 UniProtKB Helix 452 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VLD +##sequence-region P19882 1 572 +P19882 UniProtKB Transit peptide 1 25 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19882 UniProtKB Chain 26 572 . . . ID=PRO_0000005044;Note=Heat shock protein 60%2C mitochondrial +P19882 UniProtKB Modified residue 102 102 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P19882 UniProtKB Modified residue 485 485 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P22202 1 642 +P22202 UniProtKB Chain 1 642 . . . ID=PRO_0000078388;Note=Heat shock protein SSA4 +P22202 UniProtKB Modified residue 552 552 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P22202 UniProtKB Helix 637 639 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UPV +##sequence-region P33416 1 811 +P33416 UniProtKB Transit peptide 1 44 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33416 UniProtKB Chain 45 811 . . . ID=PRO_0000005500;Note=Heat shock protein 78%2C mitochondrial +P33416 UniProtKB Nucleotide binding 143 150 . . . Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33416 UniProtKB Nucleotide binding 541 548 . . . Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33416 UniProtKB Region 98 344 . . . Note=NBD1 +P33416 UniProtKB Region 467 658 . . . Note=NBD2 +P33416 UniProtKB Coiled coil 345 430 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33416 UniProtKB Mutagenesis 149 149 . . . Note=Abolishes ATPase activity. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11734006;Dbxref=PMID:11734006 +P33416 UniProtKB Mutagenesis 547 547 . . . Note=Impairs oligomerization. Reduces ATPase activity by 92%25. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11734006;Dbxref=PMID:11734006 +P33416 UniProtKB Sequence conflict 106 106 . . . Note=T->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33416 UniProtKB Sequence conflict 245 245 . . . Note=R->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33416 UniProtKB Sequence conflict 429 429 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33416 UniProtKB Sequence conflict 549 549 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33416 UniProtKB Sequence conflict 608 608 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53685 1 503 +P53685 UniProtKB Chain 1 503 . . . ID=PRO_0000110281;Note=NAD-dependent protein deacetylase HST1 +P53685 UniProtKB Domain 191 470 . . . Note=Deacetylase sirtuin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53685 UniProtKB Nucleotide binding 208 227 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53685 UniProtKB Nucleotide binding 290 293 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53685 UniProtKB Nucleotide binding 412 414 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53685 UniProtKB Nucleotide binding 437 439 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53685 UniProtKB Active site 310 310 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53685 UniProtKB Metal binding 318 318 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53685 UniProtKB Metal binding 321 321 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53685 UniProtKB Metal binding 342 342 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53685 UniProtKB Metal binding 345 345 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53685 UniProtKB Binding site 454 454 . . . Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53686 1 357 +P53686 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53686 UniProtKB Chain 2 357 . . . ID=PRO_0000110282;Note=NAD-dependent protein deacetylase HST2 +P53686 UniProtKB Domain 13 286 . . . Note=Deacetylase sirtuin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53686 UniProtKB Nucleotide binding 32 52 . . . Note=NAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14502267,ECO:0000269|PubMed:15150415;Dbxref=PMID:14502267,PMID:15150415 +P53686 UniProtKB Nucleotide binding 115 118 . . . Note=NAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14502267,ECO:0000269|PubMed:15150415;Dbxref=PMID:14502267,PMID:15150415 +P53686 UniProtKB Nucleotide binding 223 225 . . . Note=NAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14502267,ECO:0000269|PubMed:15150415;Dbxref=PMID:14502267,PMID:15150415 +P53686 UniProtKB Nucleotide binding 248 250 . . . Note=NAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14502267,ECO:0000269|PubMed:15150415;Dbxref=PMID:14502267,PMID:15150415 +P53686 UniProtKB Active site 135 135 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:20726530;Dbxref=PMID:20726530 +P53686 UniProtKB Metal binding 143 143 . . . Note=Zinc;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:14502267,ECO:0000269|PubMed:14604530,ECO:0000269|PubMed:15150415,ECO:0000269|PubMed:17289592;Dbxref=PMID:14502267,PMID:14604530,PMID:15150415,PMID:17289592 +P53686 UniProtKB Metal binding 146 146 . . . Note=Zinc;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:14502267,ECO:0000269|PubMed:14604530,ECO:0000269|PubMed:15150415,ECO:0000269|PubMed:17289592;Dbxref=PMID:14502267,PMID:14604530,PMID:15150415,PMID:17289592 +P53686 UniProtKB Metal binding 170 170 . . . Note=Zinc;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:14502267,ECO:0000269|PubMed:14604530,ECO:0000269|PubMed:15150415,ECO:0000269|PubMed:17289592;Dbxref=PMID:14502267,PMID:14604530,PMID:15150415,PMID:17289592 +P53686 UniProtKB Metal binding 173 173 . . . Note=Zinc;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00236,ECO:0000269|PubMed:14502267,ECO:0000269|PubMed:14604530,ECO:0000269|PubMed:15150415,ECO:0000269|PubMed:17289592;Dbxref=PMID:14502267,PMID:14604530,PMID:15150415,PMID:17289592 +P53686 UniProtKB Binding site 270 270 . . . Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14502267,ECO:0000269|PubMed:15150415;Dbxref=PMID:14502267,PMID:15150415 +P53686 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53686 UniProtKB Modified residue 340 340 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53686 UniProtKB Mutagenesis 117 117 . . . Note=Nearly or completely catalytically inactive. I->A%2CD%2CH%2CW%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17289592;Dbxref=PMID:17289592 +P53686 UniProtKB Mutagenesis 117 117 . . . Note=Near wild-type activity for deacetylation. Increases slightly the KM for NAD(+) to 25 uM. I->F%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17289592;Dbxref=PMID:17289592 +P53686 UniProtKB Beta strand 3 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZD +P53686 UniProtKB Helix 9 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Beta strand 27 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Helix 33 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Beta strand 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Turn 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Helix 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Helix 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Helix 63 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Helix 69 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Helix 77 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Beta strand 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Helix 95 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Beta strand 109 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Helix 120 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Helix 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Beta strand 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Beta strand 136 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Turn 144 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Helix 153 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Beta strand 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZD +P53686 UniProtKB Turn 171 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Beta strand 176 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Helix 191 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Beta strand 218 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Turn 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Helix 233 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Beta strand 242 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Helix 254 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Beta strand 264 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Helix 270 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Helix 284 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q1A +P53686 UniProtKB Helix 304 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q14 +##sequence-region P54862 1 567 +P54862 UniProtKB Chain 1 567 . . . ID=PRO_0000050401;Note=Hexose transporter HXT11 +P54862 UniProtKB Topological domain 1 56 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Transmembrane 57 77 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Topological domain 78 112 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Transmembrane 113 133 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Topological domain 134 139 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Transmembrane 140 160 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Topological domain 161 170 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Transmembrane 171 191 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Topological domain 192 197 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Transmembrane 198 218 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Topological domain 219 232 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Transmembrane 233 253 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Topological domain 254 336 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Transmembrane 337 353 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Topological domain 354 359 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Transmembrane 360 377 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Topological domain 378 384 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Transmembrane 385 405 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Topological domain 406 429 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Transmembrane 430 450 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Topological domain 451 467 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Transmembrane 468 488 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Topological domain 489 489 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Transmembrane 490 510 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Topological domain 511 567 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Glycosylation 87 87 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54862 UniProtKB Glycosylation 227 227 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P42833 1 540 +P42833 UniProtKB Chain 1 540 . . . ID=PRO_0000050403;Note=Hexose transporter HXT14 +P42833 UniProtKB Topological domain 1 56 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Transmembrane 57 76 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Topological domain 77 119 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Transmembrane 120 140 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Topological domain 141 146 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Transmembrane 147 167 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Topological domain 168 177 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Transmembrane 178 198 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Topological domain 199 204 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Transmembrane 205 225 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Topological domain 226 243 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Transmembrane 244 264 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Topological domain 265 357 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Transmembrane 358 374 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Topological domain 375 380 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Transmembrane 381 398 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Topological domain 399 405 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Transmembrane 406 426 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Topological domain 427 440 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Transmembrane 441 461 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Topological domain 462 478 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Transmembrane 479 499 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Topological domain 500 500 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Transmembrane 501 521 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42833 UniProtKB Topological domain 522 540 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47185 1 567 +P47185 UniProtKB Chain 1 567 . . . ID=PRO_0000050405;Note=Hexose transporter HXT16 +P47185 UniProtKB Topological domain 1 55 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Transmembrane 56 76 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Topological domain 77 112 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Transmembrane 113 133 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Topological domain 134 139 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Transmembrane 140 160 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Topological domain 161 170 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Transmembrane 171 191 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Topological domain 192 197 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Transmembrane 198 218 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Topological domain 219 232 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Transmembrane 233 253 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Topological domain 254 336 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Transmembrane 337 353 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Topological domain 354 359 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Transmembrane 360 377 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Topological domain 378 384 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Transmembrane 385 405 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Topological domain 406 427 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Transmembrane 428 448 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Topological domain 449 465 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Transmembrane 466 486 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Topological domain 487 487 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Transmembrane 488 508 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47185 UniProtKB Topological domain 509 567 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40886 1 569 +P40886 UniProtKB Chain 1 569 . . . ID=PRO_0000050398;Note=Hexose transporter HXT8 +P40886 UniProtKB Topological domain 1 61 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Transmembrane 62 82 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Topological domain 83 118 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Transmembrane 119 139 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Topological domain 140 145 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Transmembrane 146 166 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Topological domain 167 176 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Transmembrane 177 197 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Topological domain 198 203 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Transmembrane 204 224 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Topological domain 225 238 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Transmembrane 239 259 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Topological domain 260 342 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Transmembrane 343 359 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Topological domain 360 365 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Transmembrane 366 383 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Topological domain 384 390 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Transmembrane 391 411 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Topological domain 412 433 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Transmembrane 434 454 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Topological domain 455 471 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Transmembrane 472 492 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Topological domain 493 493 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Transmembrane 494 514 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Topological domain 515 569 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Glycosylation 92 92 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Glycosylation 102 102 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40886 UniProtKB Glycosylation 429 429 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53688 1 370 +P53688 UniProtKB Chain 1 370 . . . ID=PRO_0000110284;Note=NAD-dependent histone deacetylase HST4 +P53688 UniProtKB Domain 83 370 . . . Note=Deacetylase sirtuin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53688 UniProtKB Nucleotide binding 100 119 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53688 UniProtKB Nucleotide binding 184 187 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53688 UniProtKB Nucleotide binding 310 312 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53688 UniProtKB Nucleotide binding 340 342 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53688 UniProtKB Active site 213 213 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53688 UniProtKB Metal binding 221 221 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53688 UniProtKB Metal binding 224 224 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53688 UniProtKB Metal binding 251 251 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53688 UniProtKB Metal binding 254 254 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P53688 UniProtKB Binding site 363 363 . . . Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53892 1 351 +P53892 UniProtKB Chain 1 351 . . . ID=PRO_0000203413;Note=Protein IBD2 +P53892 UniProtKB Modified residue 100 100 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53892 UniProtKB Modified residue 106 106 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53892 UniProtKB Modified residue 211 211 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40499 1 491 +P40499 UniProtKB Chain 1 491 . . . ID=PRO_0000202975;Note=Protein ICE2 +P40499 UniProtKB Topological domain 1 13 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Transmembrane 14 34 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Topological domain 35 40 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Transmembrane 41 61 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Topological domain 62 74 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Transmembrane 75 95 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Topological domain 96 149 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Transmembrane 150 170 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Topological domain 171 184 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Transmembrane 185 205 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Topological domain 206 218 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Transmembrane 219 239 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Topological domain 240 294 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Transmembrane 295 315 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Topological domain 316 373 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Transmembrane 374 394 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Topological domain 395 413 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Transmembrane 414 434 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Topological domain 435 461 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Transmembrane 462 482 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Topological domain 483 491 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40499 UniProtKB Sequence conflict 93 93 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40051 1 511 +P40051 UniProtKB Chain 1 511 . . . ID=PRO_0000185098;Note=Intermediate cleaving peptidase 55 +P40051 UniProtKB Metal binding 327 327 . . . Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40051 UniProtKB Metal binding 338 338 . . . Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40051 UniProtKB Metal binding 338 338 . . . Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40051 UniProtKB Metal binding 417 417 . . . Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40051 UniProtKB Metal binding 444 444 . . . Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40051 UniProtKB Metal binding 467 467 . . . Note=Manganese 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40051 UniProtKB Metal binding 467 467 . . . Note=Manganese 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38284 1 255 +P38284 UniProtKB Chain 1 255 . . . ID=PRO_0000202499;Note=Increased copper sensitivity protein 2 +P38284 UniProtKB Compositional bias 13 189 . . . Note=Ser-rich +P38284 UniProtKB Modified residue 217 217 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P38284 UniProtKB Sequence conflict 90 90 . . . Note=T->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38284 UniProtKB Sequence conflict 90 90 . . . Note=T->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04329 1 127 +Q04329 UniProtKB Chain 1 127 . . . ID=PRO_0000203325;Note=Interacting with cytoskeleton protein 1 +##sequence-region P38274 1 827 +P38274 UniProtKB Chain 1 827 . . . ID=PRO_0000212347;Note=Protein arginine N-methyltransferase HSL7 +P38274 UniProtKB Domain 329 675 . . . Note=SAM-dependent MTase PRMT-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01015 +P38274 UniProtKB Region 354 355 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O14744 +P38274 UniProtKB Region 441 442 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O14744 +P38274 UniProtKB Active site 463 463 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O14744 +P38274 UniProtKB Active site 472 472 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O14744 +P38274 UniProtKB Binding site 345 345 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O14744 +P38274 UniProtKB Binding site 414 414 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O14744 +P38274 UniProtKB Site 348 348 . . . Note=Critical for specifying symmetric addition of methyl groups;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P46580 +P38274 UniProtKB Modified residue 317 317 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38274 UniProtKB Modified residue 614 614 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38274 UniProtKB Mutagenesis 387 387 . . . Note=Almost completely abolishes catalytic activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18515076;Dbxref=PMID:18515076 +P38274 UniProtKB Mutagenesis 387 387 . . . Note=Completely abolishes catalytic activity%3B when associated with V-389. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18515076;Dbxref=PMID:18515076 +P38274 UniProtKB Mutagenesis 389 389 . . . Note=Completely abolishes catalytic activity%3B when associated with V-387. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18515076;Dbxref=PMID:18515076 +##sequence-region P09435 1 649 +P09435 UniProtKB Chain 1 649 . . . ID=PRO_0000078387;Note=Heat shock protein SSA3 +P09435 UniProtKB Sequence conflict 620 620 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CS90 1 654 +P0CS90 UniProtKB Transit peptide 1 23 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2265609;Dbxref=PMID:2265609 +P0CS90 UniProtKB Chain 24 654 . . . ID=PRO_0000013553;Note=Heat shock protein SSC1%2C mitochondrial +P0CS90 UniProtKB Compositional bias 634 646 . . . Note=Asn-rich +P0CS90 UniProtKB Modified residue 330 330 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P0CS90 UniProtKB Mutagenesis 442 442 . . . Note=No interaction with TIM44. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12032075;Dbxref=PMID:12032075 +##sequence-region P39987 1 644 +##sequence-region P28834 1 360 +P28834 UniProtKB Transit peptide 1 11 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2198251;Dbxref=PMID:2198251 +P28834 UniProtKB Chain 12 360 . . . ID=PRO_0000014431;Note=Isocitrate dehydrogenase [NAD] subunit 1%2C mitochondrial +P28834 UniProtKB Metal binding 228 228 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28834 UniProtKB Binding site 109 109 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28834 UniProtKB Binding site 140 140 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28834 UniProtKB Binding site 228 228 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28834 UniProtKB Site 194 194 . . . Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28834 UniProtKB Beta strand 29 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Helix 38 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Beta strand 57 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Helix 71 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Beta strand 85 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Helix 95 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Helix 102 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Beta strand 114 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Beta strand 135 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Helix 145 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Beta strand 150 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Beta strand 158 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Helix 167 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Beta strand 188 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Turn 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Helix 201 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Beta strand 220 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Helix 227 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Helix 238 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Beta strand 242 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Helix 248 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Helix 265 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Beta strand 269 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Beta strand 278 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Turn 283 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Helix 289 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLV +P28834 UniProtKB Helix 300 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Helix 317 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Beta strand 332 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Helix 338 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28834 UniProtKB Helix 346 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +##sequence-region P41939 1 412 +P41939 UniProtKB Chain 1 412 . . . ID=PRO_0000083587;Note=Isocitrate dehydrogenase [NADP] cytoplasmic +P41939 UniProtKB Nucleotide binding 75 77 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41939 UniProtKB Nucleotide binding 310 315 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41939 UniProtKB Region 94 100 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41939 UniProtKB Metal binding 252 252 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41939 UniProtKB Metal binding 275 275 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41939 UniProtKB Binding site 77 77 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41939 UniProtKB Binding site 82 82 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41939 UniProtKB Binding site 109 109 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41939 UniProtKB Binding site 132 132 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41939 UniProtKB Binding site 260 260 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41939 UniProtKB Binding site 328 328 . . . Note=NADP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41939 UniProtKB Site 139 139 . . . Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41939 UniProtKB Site 212 212 . . . Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41939 UniProtKB Sequence conflict 24 27 . . . Note=HLIR->SFNQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41939 UniProtKB Sequence conflict 68 68 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41939 UniProtKB Sequence conflict 185 185 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41939 UniProtKB Sequence conflict 232 239 . . . Note=ARSYKEKF->LEVIKRSL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41939 UniProtKB Sequence conflict 267 267 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41939 UniProtKB Sequence conflict 306 307 . . . Note=EA->DR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41939 UniProtKB Sequence conflict 316 323 . . . Note=FRQHQQGK->LTDYDKGR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25038 1 676 +P25038 UniProtKB Domain 143 326 . . . Note=tr-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P25038 UniProtKB Nucleotide binding 152 159 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25038 UniProtKB Nucleotide binding 200 203 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25038 UniProtKB Nucleotide binding 254 257 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25038 UniProtKB Region 152 159 . . . Note=G1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P25038 UniProtKB Region 177 181 . . . Note=G2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P25038 UniProtKB Region 200 203 . . . Note=G3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P25038 UniProtKB Region 254 257 . . . Note=G4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P25038 UniProtKB Region 296 298 . . . Note=G5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P25038 UniProtKB Sequence conflict 462 462 . . . Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P19211 1 157 +P19211 UniProtKB Chain 1 157 . . . ID=PRO_0000142487;Note=Eukaryotic translation initiation factor 5A-2 +P19211 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P19211 UniProtKB Modified residue 7 7 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P19211 UniProtKB Modified residue 51 51 . . . Note=Hypusine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1903841;Dbxref=PMID:1903841 +##sequence-region Q12522 1 245 +Q12522 UniProtKB Chain 1 245 . . . ID=PRO_0000153742;Note=Eukaryotic translation initiation factor 6 +Q12522 UniProtKB Modified residue 174 174 . . . Note=Phosphoserine%3B by CK1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03132 +Q12522 UniProtKB Modified residue 175 175 . . . Note=Phosphoserine%3B by CK1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03132 +Q12522 UniProtKB Modified residue 231 231 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q12522 UniProtKB Beta strand 2 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Helix 13 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Beta strand 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Beta strand 24 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Helix 32 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Turn 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Beta strand 48 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Helix 59 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Beta strand 67 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Helix 78 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Beta strand 92 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Helix 104 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Beta strand 108 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Beta strand 112 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Helix 123 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Beta strand 135 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Helix 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Beta strand 151 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Beta strand 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Helix 167 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Beta strand 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Turn 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Helix 193 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Beta strand 197 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Beta strand 204 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +Q12522 UniProtKB Helix 212 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G62 +##sequence-region P06168 1 395 +P06168 UniProtKB Transit peptide 1 47 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06168 UniProtKB Chain 48 395 . . . ID=PRO_0000015634;Note=Ketol-acid reductoisomerase%2C mitochondrial +P06168 UniProtKB Nucleotide binding 84 93 . . . Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06168 UniProtKB Nucleotide binding 108 113 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06168 UniProtKB Nucleotide binding 146 150 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06168 UniProtKB Region 363 395 . . . Note=Hydrophilic +P06168 UniProtKB Active site 171 171 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06168 UniProtKB Metal binding 255 255 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06168 UniProtKB Metal binding 255 255 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06168 UniProtKB Metal binding 259 259 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06168 UniProtKB Modified residue 355 355 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P39567 1 403 +P39567 UniProtKB Chain 1 403 . . . ID=PRO_0000093681;Note=Putative inosine-5'-monophosphate dehydrogenase 1 +P39567 UniProtKB Domain 121 183 . . . Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +P39567 UniProtKB Domain 184 240 . . . Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +P39567 UniProtKB Nucleotide binding 278 280 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50097 +P39567 UniProtKB Nucleotide binding 328 330 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50097 +P39567 UniProtKB Region 368 370 . . . Note=IMP binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50097 +P39567 UniProtKB Active site 335 335 . . . Note=Thioimidate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50097 +P39567 UniProtKB Metal binding 330 330 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50097 +P39567 UniProtKB Metal binding 332 332 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50097 +P39567 UniProtKB Metal binding 335 335 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50097 +P39567 UniProtKB Binding site 333 333 . . . Note=IMP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50097 +##sequence-region P50095 1 523 +P50095 UniProtKB Chain 1 523 . . . ID=PRO_0000093683;Note=Inosine-5'-monophosphate dehydrogenase 3 +P50095 UniProtKB Domain 121 183 . . . Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50095 UniProtKB Domain 184 240 . . . Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50095 UniProtKB Nucleotide binding 278 280 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50095 UniProtKB Nucleotide binding 328 330 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50095 UniProtKB Region 368 370 . . . Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50095 UniProtKB Region 391 392 . . . Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50095 UniProtKB Region 415 419 . . . Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50095 UniProtKB Active site 335 335 . . . Note=Thioimidate intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50095 UniProtKB Active site 437 437 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50095 UniProtKB Metal binding 330 330 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50095 UniProtKB Metal binding 332 332 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50095 UniProtKB Metal binding 335 335 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50095 UniProtKB Metal binding 508 508 . . . Note=Potassium%3B via carbonyl oxygen%3B shared with tetrameric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50095 UniProtKB Metal binding 509 509 . . . Note=Potassium%3B via carbonyl oxygen%3B shared with tetrameric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50095 UniProtKB Metal binding 510 510 . . . Note=Potassium%3B via carbonyl oxygen%3B shared with tetrameric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50095 UniProtKB Binding site 333 333 . . . Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50095 UniProtKB Binding site 449 449 . . . Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50095 UniProtKB Mutagenesis 253 253 . . . Note=Increases drug-resistance to MPA. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16278936;Dbxref=PMID:16278936 +##sequence-region Q02888 1 182 +Q02888 UniProtKB Transit peptide 1 45 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02888 UniProtKB Chain 46 182 . . . ID=PRO_0000238621;Note=Inner membrane assembly complex subunit 17;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02888 UniProtKB Topological domain 46 107 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24942160;Dbxref=PMID:24942160 +Q02888 UniProtKB Transmembrane 108 127 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02888 UniProtKB Topological domain 128 182 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24942160;Dbxref=PMID:24942160 +Q02888 UniProtKB Coiled coil 128 158 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03824 1 705 +Q03824 UniProtKB Chain 1 705 . . . ID=PRO_0000203314;Note=Inheritance of peroxisomes protein 2 +Q03824 UniProtKB Transmembrane 215 231 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03824 UniProtKB Glycosylation 275 275 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03824 UniProtKB Glycosylation 343 343 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03824 UniProtKB Glycosylation 344 344 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03824 UniProtKB Glycosylation 379 379 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03824 UniProtKB Glycosylation 517 517 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03824 UniProtKB Glycosylation 569 569 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03824 UniProtKB Glycosylation 574 574 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12271 1 1107 +Q12271 UniProtKB Chain 1 1107 . . . ID=PRO_0000268681;Note=Polyphosphatidylinositol phosphatase INP53 +Q12271 UniProtKB Domain 142 482 . . . Note=SAC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00183 +Q12271 UniProtKB Compositional bias 957 989 . . . Note=Pro-rich +Q12271 UniProtKB Modified residue 497 497 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50942 +Q12271 UniProtKB Modified residue 986 986 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12271 UniProtKB Modified residue 1035 1035 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12271 UniProtKB Modified residue 1105 1105 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q12271 UniProtKB Mutagenesis 421 421 . . . Note=Reduces hydrolysis of PtdIns(4)P%3B when associated with A-424 and A-427. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12686590;Dbxref=PMID:12686590 +Q12271 UniProtKB Mutagenesis 424 424 . . . Note=Reduces hydrolysis of PtdIns(4)P%3B when associated with A-421 and A-427. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12686590;Dbxref=PMID:12686590 +Q12271 UniProtKB Mutagenesis 427 427 . . . Note=Reduces hydrolysis of PtdIns(4)P%3B when associated with A-421 and A-424. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12686590;Dbxref=PMID:12686590 +Q12271 UniProtKB Mutagenesis 746 746 . . . Note=Abolishes hydrolysis of PtdIns(4%2C5)P2%3B when associated with A-748. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12686590;Dbxref=PMID:12686590 +Q12271 UniProtKB Mutagenesis 748 748 . . . Note=Abolishes hydrolysis of PtdIns(4%2C5)P2%3B when associated with A-746. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12686590;Dbxref=PMID:12686590 +##sequence-region P00724 1 532 +P00724 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2113524;Dbxref=PMID:2113524 +P00724 UniProtKB Chain 20 532 . . . ID=PRO_0000033399;Note=Invertase 2 +P00724 UniProtKB Region 39 42 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00724 UniProtKB Region 102 103 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00724 UniProtKB Region 170 171 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00724 UniProtKB Active site 42 42 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10067,ECO:0000269|PubMed:2113524;Dbxref=PMID:2113524 +P00724 UniProtKB Binding site 60 60 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00724 UniProtKB Binding site 223 223 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00724 UniProtKB Binding site 311 311 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00724 UniProtKB Glycosylation 23 23 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881 +P00724 UniProtKB Glycosylation 64 64 . . . Note=N-linked (GlcNAc...) asparagine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881 +P00724 UniProtKB Glycosylation 97 97 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881 +P00724 UniProtKB Glycosylation 111 111 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881 +P00724 UniProtKB Glycosylation 118 118 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881 +P00724 UniProtKB Glycosylation 165 165 . . . Note=N-linked (GlcNAc...) asparagine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881 +P00724 UniProtKB Glycosylation 266 266 . . . Note=N-linked (GlcNAc...) asparagine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881 +P00724 UniProtKB Glycosylation 275 275 . . . Note=N-linked (GlcNAc...) asparagine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881 +P00724 UniProtKB Glycosylation 356 356 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881 +P00724 UniProtKB Glycosylation 369 369 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881 +P00724 UniProtKB Glycosylation 384 384 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881 +P00724 UniProtKB Glycosylation 398 398 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881 +P00724 UniProtKB Glycosylation 512 512 . . . Note=N-linked (GlcNAc...) asparagine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3284881;Dbxref=PMID:3284881 +P00724 UniProtKB Alternative sequence 1 20 . . . ID=VSP_019611;Note=In isoform Intracellular. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00724 UniProtKB Mutagenesis 42 42 . . . Note=Loss of activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2113524;Dbxref=PMID:2113524 +P00724 UniProtKB Sequence conflict 51 51 . . . Note=K->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00724 UniProtKB Sequence conflict 409 409 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00724 UniProtKB Beta strand 30 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 36 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Turn 50 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 54 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 73 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 86 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 100 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Helix 123 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 127 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 139 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 147 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 170 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Turn 178 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 182 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Helix 190 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 194 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 207 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 223 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 239 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 257 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 270 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 278 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 283 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 287 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Turn 297 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 303 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Turn 311 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 316 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 320 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 329 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 345 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 374 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 387 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 410 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 418 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 425 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Turn 431 434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 435 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Helix 446 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 465 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 471 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Turn 490 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 494 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 503 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 510 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +P00724 UniProtKB Beta strand 521 530 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQV +##sequence-region P28239 1 310 +P28239 UniProtKB Transit peptide 1 30 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28239 UniProtKB Chain 31 310 . . . ID=PRO_0000025413;Note=Inorganic pyrophosphatase%2C mitochondrial +P28239 UniProtKB Metal binding 152 152 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28239 UniProtKB Metal binding 157 157 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28239 UniProtKB Metal binding 157 157 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28239 UniProtKB Metal binding 189 189 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P32589 1 693 +P32589 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P32589 UniProtKB Chain 2 693 . . . ID=PRO_0000078396;Note=Heat shock protein homolog SSE1 +P32589 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P32589 UniProtKB Modified residue 242 242 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32589 UniProtKB Modified residue 660 660 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32589 UniProtKB Cross-link 195 195 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32589 UniProtKB Sequence conflict 269 270 . . . Note=TA->NT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32589 UniProtKB Sequence conflict 269 270 . . . Note=TA->NT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32589 UniProtKB Beta strand 5 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 11 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 23 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 34 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 44 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 51 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 68 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 81 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 90 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 98 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 109 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 115 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 140 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 151 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 167 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 174 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 197 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 209 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 220 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 234 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 257 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 261 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 282 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 291 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 297 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 303 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 311 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Turn 315 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 319 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 332 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 337 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 343 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 348 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Turn 368 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 371 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 385 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QXL +P32589 UniProtKB Beta strand 393 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 402 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 414 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 423 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 439 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 448 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 457 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 476 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 490 498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 505 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C7N +P32589 UniProtKB Beta strand 520 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C7N +P32589 UniProtKB Beta strand 529 532 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Beta strand 534 538 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 544 585 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Turn 586 589 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 590 592 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 595 611 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Turn 612 614 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 615 618 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +P32589 UniProtKB Helix 621 653 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D2F +##sequence-region P17709 1 500 +P17709 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +P17709 UniProtKB Chain 2 500 . . . ID=PRO_0000197603;Note=Glucokinase-1 +P17709 UniProtKB Domain 12 498 . . . Note=Hexokinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084 +P17709 UniProtKB Nucleotide binding 487 492 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17709 UniProtKB Region 74 216 . . . Note=Hexokinase small subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084 +P17709 UniProtKB Region 158 184 . . . Note=Glucose-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17709 UniProtKB Region 217 487 . . . Note=Hexokinase large subdomain;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01084 +P17709 UniProtKB Binding site 110 110 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17709 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +P17709 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P17709 UniProtKB Modified residue 470 470 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P43581 1 546 +P43581 UniProtKB Chain 1 546 . . . ID=PRO_0000050400;Note=Hexose transporter HXT10 +P43581 UniProtKB Topological domain 1 44 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Transmembrane 45 65 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Topological domain 66 100 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Transmembrane 101 121 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Topological domain 122 127 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Transmembrane 128 148 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Topological domain 149 158 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Transmembrane 159 179 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Topological domain 180 185 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Transmembrane 186 206 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Topological domain 207 220 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Transmembrane 221 241 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Topological domain 242 324 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Transmembrane 325 341 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Topological domain 342 347 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Transmembrane 348 365 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Topological domain 366 372 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Transmembrane 373 393 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Topological domain 394 415 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Transmembrane 416 436 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Topological domain 437 453 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Transmembrane 454 474 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Topological domain 475 475 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Transmembrane 476 496 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Topological domain 497 546 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43581 UniProtKB Glycosylation 75 75 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40441 1 457 +P40441 UniProtKB Chain 1 457 . . . ID=PRO_0000050408;Note=Putative hexose transporter 12 +P40441 UniProtKB Topological domain 1 2 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Transmembrane 3 23 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Topological domain 24 29 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Transmembrane 30 50 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Topological domain 51 60 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Transmembrane 61 81 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Topological domain 82 87 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Transmembrane 88 108 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Topological domain 109 122 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Transmembrane 123 143 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Topological domain 144 247 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Transmembrane 248 268 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Topological domain 269 274 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Transmembrane 275 295 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Topological domain 296 319 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Transmembrane 320 340 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Topological domain 341 353 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Transmembrane 354 374 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Topological domain 375 379 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Transmembrane 380 400 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Topological domain 401 457 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40441 UniProtKB Glycosylation 194 194 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53631 1 564 +P53631 UniProtKB Chain 1 564 . . . ID=PRO_0000050406;Note=Hexose transporter HXT17 +P53631 UniProtKB Topological domain 1 52 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Transmembrane 53 73 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Topological domain 74 109 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Transmembrane 110 130 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Topological domain 131 136 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Transmembrane 137 157 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Topological domain 158 167 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Transmembrane 168 188 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Topological domain 189 194 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Transmembrane 195 215 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Topological domain 216 229 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Transmembrane 230 250 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Topological domain 251 333 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Transmembrane 334 350 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Topological domain 351 356 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Transmembrane 357 374 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Topological domain 375 381 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Transmembrane 382 402 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Topological domain 403 424 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Transmembrane 425 445 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Topological domain 446 462 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Transmembrane 463 483 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Topological domain 484 484 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Transmembrane 485 505 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53631 UniProtKB Topological domain 506 564 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P23585 1 541 +P23585 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P23585 UniProtKB Chain 2 541 . . . ID=PRO_0000050392;Note=High-affinity glucose transporter HXT2 +P23585 UniProtKB Topological domain 2 49 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Transmembrane 50 70 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Topological domain 71 107 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Transmembrane 108 128 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Topological domain 129 134 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Transmembrane 135 155 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Topological domain 156 162 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Transmembrane 163 183 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Topological domain 184 192 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Transmembrane 193 213 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Topological domain 214 227 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Transmembrane 228 248 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Topological domain 249 327 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Transmembrane 328 347 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Topological domain 348 350 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Transmembrane 351 371 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Topological domain 372 379 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Transmembrane 380 400 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Topological domain 401 418 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Transmembrane 419 439 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Topological domain 440 456 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Transmembrane 457 477 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Topological domain 478 484 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Transmembrane 485 505 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Topological domain 506 541 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P23585 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P23585 UniProtKB Modified residue 13 13 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P23585 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P23585 UniProtKB Modified residue 20 20 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P23585 UniProtKB Modified residue 29 29 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P23585 UniProtKB Modified residue 32 32 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P23585 UniProtKB Modified residue 266 266 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Modified residue 539 539 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23585 UniProtKB Glycosylation 82 82 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32467 1 576 +P32467 UniProtKB Chain 1 576 . . . ID=PRO_0000050394;Note=Low-affinity glucose transporter HXT4 +P32467 UniProtKB Topological domain 1 66 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Transmembrane 67 87 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Topological domain 88 122 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Transmembrane 123 143 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Topological domain 144 149 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Transmembrane 150 170 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Topological domain 171 180 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Transmembrane 181 201 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Topological domain 202 207 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Transmembrane 208 228 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Topological domain 229 242 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Transmembrane 243 263 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Topological domain 264 346 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Transmembrane 347 363 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Topological domain 364 369 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Transmembrane 370 387 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Topological domain 388 394 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Transmembrane 395 415 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Topological domain 416 437 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Transmembrane 438 458 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Topological domain 459 475 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Transmembrane 476 496 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Topological domain 497 497 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Transmembrane 498 518 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Topological domain 519 576 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Glycosylation 425 425 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32467 UniProtKB Cross-link 45 45 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14557538;Dbxref=PMID:14557538 +##sequence-region P39003 1 570 +P39003 UniProtKB Chain 1 570 . . . ID=PRO_0000050396;Note=High-affinity hexose transporter HXT6 +P39003 UniProtKB Topological domain 1 60 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Transmembrane 61 81 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Topological domain 82 116 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Transmembrane 117 137 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Topological domain 138 143 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Transmembrane 144 164 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Topological domain 165 174 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Transmembrane 175 195 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Topological domain 196 201 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Transmembrane 202 222 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Topological domain 223 236 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Transmembrane 237 257 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Topological domain 258 340 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Transmembrane 341 357 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Topological domain 358 363 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Transmembrane 364 381 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Topological domain 382 388 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Transmembrane 389 409 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Topological domain 410 431 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Transmembrane 432 452 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Topological domain 453 469 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Transmembrane 470 490 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Topological domain 491 491 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Transmembrane 492 512 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Topological domain 513 570 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Glycosylation 91 91 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Glycosylation 228 228 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39003 UniProtKB Cross-link 560 560 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P39003 UniProtKB Sequence conflict 293 293 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40885 1 567 +P40885 UniProtKB Chain 1 567 . . . ID=PRO_0000050399;Note=Hexose transporter HXT9 +P40885 UniProtKB Topological domain 1 56 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Transmembrane 57 77 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Topological domain 78 112 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Transmembrane 113 133 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Topological domain 134 139 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Transmembrane 140 160 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Topological domain 161 170 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Transmembrane 171 191 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Topological domain 192 197 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Transmembrane 198 218 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Topological domain 219 232 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Transmembrane 233 253 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Topological domain 254 336 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Transmembrane 337 353 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Topological domain 354 359 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Transmembrane 360 377 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Topological domain 378 384 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Transmembrane 385 405 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Topological domain 406 429 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Transmembrane 430 450 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Topological domain 451 467 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Transmembrane 468 488 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Topological domain 489 489 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Transmembrane 490 510 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Topological domain 511 567 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Glycosylation 87 87 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40885 UniProtKB Glycosylation 227 227 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47125 1 453 +P47125 UniProtKB Chain 1 453 . . . ID=PRO_0000215208;Note=Indoleamine 2%2C3-dioxygenase +P47125 UniProtKB Metal binding 331 331 . . . Note=Iron (heme proximal ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P43598 1 195 +P43598 UniProtKB Chain 1 195 . . . ID=PRO_0000202687;Note=Inhibitor of glycogen debranching 1 +P43598 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43598 UniProtKB Modified residue 65 65 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43598 UniProtKB Modified residue 95 95 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43598 UniProtKB Modified residue 96 96 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43598 UniProtKB Modified residue 132 132 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43598 UniProtKB Modified residue 164 164 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P39522 1 585 +P39522 UniProtKB Metal binding 143 143 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39522 UniProtKB Metal binding 221 221 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39522 UniProtKB Sequence conflict 82 89 . . . Note=SQSIEKAG->MFSIIEKR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39522 UniProtKB Sequence conflict 238 238 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39522 UniProtKB Sequence conflict 242 242 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39522 UniProtKB Sequence conflict 492 492 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39522 UniProtKB Sequence conflict 520 520 . . . Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39522 UniProtKB Sequence conflict 551 551 . . . Note=R->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02821 1 542 +Q02821 UniProtKB Chain 1 542 . . . ID=PRO_0000120744;Note=Importin subunit alpha +Q02821 UniProtKB Domain 1 65 . . . Note=IBB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00561 +Q02821 UniProtKB Repeat 89 122 . . . Note=ARM 1%3B truncated;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485 +Q02821 UniProtKB Repeat 123 162 . . . Note=ARM 2;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485 +Q02821 UniProtKB Repeat 163 204 . . . Note=ARM 3;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485 +Q02821 UniProtKB Repeat 205 251 . . . Note=ARM 4;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485 +Q02821 UniProtKB Repeat 252 288 . . . Note=ARM 5;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485 +Q02821 UniProtKB Repeat 289 330 . . . Note=ARM 6;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485 +Q02821 UniProtKB Repeat 331 372 . . . Note=ARM 7;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485 +Q02821 UniProtKB Repeat 373 417 . . . Note=ARM 8;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485 +Q02821 UniProtKB Repeat 418 471 . . . Note=ARM 9;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485 +Q02821 UniProtKB Repeat 472 508 . . . Note=ARM 10%3B atypical;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00259,ECO:0000269|PubMed:8521485;Dbxref=PMID:8521485 +Q02821 UniProtKB Region 209 335 . . . Note=NLS binding site 1 +Q02821 UniProtKB Region 419 505 . . . Note=NLS binding site 2 +Q02821 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q02821 UniProtKB Mutagenesis 116 116 . . . Note=In SRP1-31%3B temperature-sensitive mutant%3B reduced growth rate and chromosome loss. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8041713;Dbxref=PMID:8041713 +Q02821 UniProtKB Mutagenesis 145 145 . . . Note=In SRP1-49%3B temperature-sensitive mutant%3B alteration in nucleolar and microtubule morphology. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8041713;Dbxref=PMID:8041713 +Q02821 UniProtKB Mutagenesis 219 219 . . . Note=In SRP1-1%3B temperature-sensitive mutant. P->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8041713;Dbxref=PMID:8041713 +Q02821 UniProtKB Mutagenesis 286 286 . . . Note=In SRP1-3%3B temperature-sensitive mutant. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8041713;Dbxref=PMID:8041713 +Q02821 UniProtKB Mutagenesis 360 360 . . . Note=In SRP1-2%3B temperature-sensitive mutant. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8041713;Dbxref=PMID:8041713 +Q02821 UniProtKB Mutagenesis 459 459 . . . Note=In SRP1-54%3B temperature-sensitive mutant%3B reduced growth rate. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8041713;Dbxref=PMID:8041713 +Q02821 UniProtKB Helix 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 89 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Beta strand 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XZR +Q02821 UniProtKB Helix 101 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Beta strand 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 123 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 132 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 145 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 163 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 175 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 187 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 205 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 217 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 223 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 229 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Beta strand 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 252 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 256 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 259 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 271 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Beta strand 286 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XZR +Q02821 UniProtKB Helix 289 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 301 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 307 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 313 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 331 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 342 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 355 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 373 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 385 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 397 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Turn 414 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 419 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 430 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Turn 437 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 442 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 472 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 482 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Helix 488 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Beta strand 492 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C1T +Q02821 UniProtKB Helix 495 508 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +Q02821 UniProtKB Beta strand 509 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1WA5 +##sequence-region P40069 1 1113 +P40069 UniProtKB Chain 1 1113 . . . ID=PRO_0000120776;Note=Importin subunit beta-4 +P40069 UniProtKB Repeat 3 35 . . . Note=HEAT 1;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Domain 25 92 . . . Note=Importin N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00115 +P40069 UniProtKB Repeat 40 74 . . . Note=HEAT 2;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 92 115 . . . Note=HEAT 3;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 120 147 . . . Note=HEAT 4;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 157 191 . . . Note=HEAT 5;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 208 244 . . . Note=HEAT 6;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 252 287 . . . Note=HEAT 7;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 296 348 . . . Note=HEAT 8;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 350 384 . . . Note=HEAT 9;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 388 428 . . . Note=HEAT 10;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 430 469 . . . Note=HEAT 11;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 472 513 . . . Note=HEAT 12;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 515 558 . . . Note=HEAT 13;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 560 605 . . . Note=HEAT 14;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 607 680 . . . Note=HEAT 15;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 683 737 . . . Note=HEAT 16;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 744 783 . . . Note=HEAT 17;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 790 856 . . . Note=HEAT 18;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 859 894 . . . Note=HEAT 19;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 902 934 . . . Note=HEAT 20;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 942 991 . . . Note=HEAT 21;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 999 1030 . . . Note=HEAT 22;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 1049 1084 . . . Note=HEAT 23;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Repeat 1085 1110 . . . Note=HEAT 24;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P32337,ECO:0000305|PubMed:23541588;Dbxref=PMID:23541588 +P40069 UniProtKB Modified residue 646 646 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P32581 1 645 +P32581 UniProtKB Chain 1 645 . . . ID=PRO_0000086023;Note=Meiosis induction protein kinase IME2/SME1 +P32581 UniProtKB Domain 38 386 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32581 UniProtKB Nucleotide binding 44 52 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32581 UniProtKB Active site 193 193 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P32581 UniProtKB Binding site 67 67 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +##sequence-region P25626 1 169 +P25626 UniProtKB Transit peptide 1 16 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25626 UniProtKB Chain 17 169 . . . ID=PRO_0000030477;Note=54S ribosomal protein IMG1%2C mitochondrial +##sequence-region P46972 1 177 +P46972 UniProtKB Chain 1 177 . . . ID=PRO_0000109538;Note=Mitochondrial inner membrane protease subunit 2 +P46972 UniProtKB Transmembrane 134 152 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46972 UniProtKB Active site 41 41 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46972 UniProtKB Active site 91 91 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46972 UniProtKB Mutagenesis 41 41 . . . Note=Abolishes enzymatic activity. S->A%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835 +P46972 UniProtKB Mutagenesis 91 91 . . . Note=Abolishes enzymatic activity. K->H%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835 +P46972 UniProtKB Mutagenesis 95 95 . . . Note=Reduces processing of CYB2 and presence of IMP1 and SOM1 in the IMP complex. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15118906;Dbxref=PMID:15118906 +P46972 UniProtKB Mutagenesis 123 123 . . . Note=Reduces processing of cytochrome c1%3B no effect on presence of IMP1 and SOM1 in the IMP complex. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15118906;Dbxref=PMID:15118906 +P46972 UniProtKB Mutagenesis 124 124 . . . Note=Abolishes enzymatic activity. D->N%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835 +P46972 UniProtKB Mutagenesis 131 131 . . . Note=Abolishes enzymatic activity. D->N%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835 +##sequence-region P53941 1 290 +P53941 UniProtKB Chain 1 290 . . . ID=PRO_0000120245;Note=U3 small nucleolar ribonucleoprotein protein IMP4 +P53941 UniProtKB Domain 86 267 . . . Note=Brix;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00034 +P53941 UniProtKB Mutagenesis 119 119 . . . Note=No effect on RNA binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489263;Dbxref=PMID:15489263 +P53941 UniProtKB Mutagenesis 201 201 . . . Note=No effect on RNA binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489263;Dbxref=PMID:15489263 +P53941 UniProtKB Mutagenesis 220 220 . . . Note=Loss of RNA binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489263;Dbxref=PMID:15489263 +P53941 UniProtKB Mutagenesis 253 253 . . . Note=Loss of RNA binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489263;Dbxref=PMID:15489263 +##sequence-region Q03694 1 420 +Q03694 UniProtKB Chain 1 420 . . . ID=PRO_0000203328;Note=Inheritance of peroxisomes protein 1 +Q03694 UniProtKB Modified residue 273 273 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region Q08630 1 104 +Q08630 UniProtKB Chain 1 104 . . . ID=PRO_0000299728;Note=Increased recombination centers protein 13 +Q08630 UniProtKB Transmembrane 63 83 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04772 1 201 +Q04772 UniProtKB Chain 1 201 . . . ID=PRO_0000166039;Note=Increased recombination centers protein 21 +Q04772 UniProtKB Domain 122 200 . . . Note=Cytochrome b5 heme-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279 +Q04772 UniProtKB Metal binding 158 158 . . . Note=Iron (heme axial ligand);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279 +Q04772 UniProtKB Metal binding 182 182 . . . Note=Iron (heme axial ligand);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279 +##sequence-region P47046 1 822 +P47046 UniProtKB Chain 1 822 . . . ID=PRO_0000203064;Note=Uncharacterized protein IRC8 +P47046 UniProtKB Topological domain 1 13 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47046 UniProtKB Transmembrane 14 34 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47046 UniProtKB Topological domain 35 44 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47046 UniProtKB Transmembrane 45 65 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47046 UniProtKB Topological domain 66 76 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47046 UniProtKB Transmembrane 77 97 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47046 UniProtKB Topological domain 98 120 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47046 UniProtKB Transmembrane 121 141 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47046 UniProtKB Topological domain 142 822 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47046 UniProtKB Modified residue 690 690 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P28241 1 369 +P28241 UniProtKB Transit peptide 1 15 . . . Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2198251,ECO:0000269|PubMed:7505425;Dbxref=PMID:2198251,PMID:7505425 +P28241 UniProtKB Chain 16 369 . . . ID=PRO_0000014434;Note=Isocitrate dehydrogenase [NAD] subunit 2%2C mitochondrial +P28241 UniProtKB Metal binding 237 237 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28241 UniProtKB Metal binding 263 263 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28241 UniProtKB Metal binding 267 267 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28241 UniProtKB Binding site 119 119 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28241 UniProtKB Binding site 129 129 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28241 UniProtKB Binding site 150 150 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28241 UniProtKB Binding site 237 237 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28241 UniProtKB Site 157 157 . . . Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28241 UniProtKB Site 204 204 . . . Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28241 UniProtKB Modified residue 105 105 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P28241 UniProtKB Modified residue 153 153 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P28241 UniProtKB Modified residue 327 327 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P28241 UniProtKB Modified residue 349 349 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P28241 UniProtKB Sequence conflict 25 25 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28241 UniProtKB Helix 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLV +P28241 UniProtKB Turn 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Helix 48 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Turn 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Beta strand 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Beta strand 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Beta strand 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Helix 86 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Beta strand 96 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Helix 114 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Beta strand 124 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Beta strand 145 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Beta strand 153 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Beta strand 168 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Helix 177 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Beta strand 197 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Turn 206 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Helix 210 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Beta strand 229 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Helix 236 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Helix 247 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Beta strand 253 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Helix 259 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Helix 277 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Beta strand 281 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Beta strand 290 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Helix 300 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Turn 303 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Helix 311 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Helix 327 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Helix 337 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Helix 350 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +P28241 UniProtKB Helix 358 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BLX +##sequence-region P40154 1 320 +P40154 UniProtKB Chain 1 320 . . . ID=PRO_0000084154;Note=Ino eighty subunit 2 +P40154 UniProtKB Modified residue 67 67 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40154 UniProtKB Modified residue 129 129 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P32617 1 166 +P32617 UniProtKB Chain 1 166 . . . ID=PRO_0000084158;Note=Chromatin-remodeling complex subunit IES6 +P32617 UniProtKB Sequence conflict 32 32 . . . Note=F->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47170 1 1584 +P47170 UniProtKB Chain 1 1584 . . . ID=PRO_0000203123;Note=Vacuolar membrane-associated protein IML1 +P47170 UniProtKB Domain 1198 1273 . . . Note=DEP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00066 +P47170 UniProtKB Modified residue 680 680 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P47170 UniProtKB Modified residue 737 737 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q05533 1 292 +Q05533 UniProtKB Chain 1 292 . . . ID=PRO_0000245568;Note=Inositol monophosphatase 2 +Q05533 UniProtKB Region 96 99 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05533 UniProtKB Metal binding 75 75 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05533 UniProtKB Metal binding 94 94 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05533 UniProtKB Metal binding 94 94 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05533 UniProtKB Metal binding 96 96 . . . Note=Magnesium 1%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05533 UniProtKB Metal binding 97 97 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05533 UniProtKB Metal binding 231 231 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05533 UniProtKB Binding site 75 75 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05533 UniProtKB Binding site 231 231 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53901 1 409 +P53901 UniProtKB Chain 1 409 . . . ID=PRO_0000203419;Note=Ingression protein 1 +P53901 UniProtKB Domain 1 134 . . . Note=C2 +P53901 UniProtKB Compositional bias 303 310 . . . Note=Poly-Asp +P53901 UniProtKB Modified residue 392 392 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53901 UniProtKB Mutagenesis 28 28 . . . Note=Impairs plasma membrane ingression%3B when associated with A-31. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18344988;Dbxref=PMID:18344988 +P53901 UniProtKB Mutagenesis 31 31 . . . Note=Impairs plasma membrane ingression%3B when associated with A-28. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18344988;Dbxref=PMID:18344988 +P53901 UniProtKB Sequence conflict 221 221 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P50942 1 1183 +P50942 UniProtKB Chain 1 1183 . . . ID=PRO_0000209745;Note=Polyphosphatidylinositol phosphatase INP52 +P50942 UniProtKB Domain 167 507 . . . Note=SAC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00183 +P50942 UniProtKB Modified residue 152 152 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P50942 UniProtKB Modified residue 522 522 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P50942 UniProtKB Modified residue 1005 1005 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198 +P50942 UniProtKB Modified residue 1016 1016 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P50942 UniProtKB Modified residue 1032 1032 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P50942 UniProtKB Modified residue 1095 1095 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12271 +P50942 UniProtKB Mutagenesis 631 631 . . . Note=Impairs completely enzyme activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10962003;Dbxref=PMID:10962003 +P50942 UniProtKB Mutagenesis 730 730 . . . Note=Impairs completely enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10962003;Dbxref=PMID:10962003 +P50942 UniProtKB Mutagenesis 771 771 . . . Note=Impairs completely enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10962003;Dbxref=PMID:10962003 +##sequence-region Q12072 1 812 +Q12072 UniProtKB Chain 1 812 . . . ID=PRO_0000240452;Note=ISWI one complex protein 2 +Q12072 UniProtKB Coiled coil 673 714 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12072 UniProtKB Compositional bias 761 807 . . . Note=Gln-rich +##sequence-region Q04213 1 475 +Q04213 UniProtKB Chain 1 475 . . . ID=PRO_0000203276;Note=ISWI one complex protein 4 +Q04213 UniProtKB Compositional bias 74 77 . . . Note=Poly-Glu +Q04213 UniProtKB Compositional bias 186 195 . . . Note=Poly-Glu +Q04213 UniProtKB Compositional bias 243 251 . . . Note=Poly-Glu +Q04213 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04213 UniProtKB Modified residue 9 9 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04213 UniProtKB Modified residue 65 65 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04213 UniProtKB Modified residue 73 73 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q04213 UniProtKB Modified residue 242 242 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P07250 1 355 +P07250 UniProtKB Chain 1 355 . . . ID=PRO_0000066873;Note=Inositol polyphosphate multikinase +P07250 UniProtKB Region 127 135 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07250 UniProtKB Compositional bias 282 301 . . . Note=Asp-rich (acidic) +P07250 UniProtKB Metal binding 133 133 . . . Note=Manganese;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17050532;Dbxref=PMID:17050532 +P07250 UniProtKB Metal binding 271 271 . . . Note=Calcium%3B via carbonyl oxygen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17050532;Dbxref=PMID:17050532 +P07250 UniProtKB Metal binding 274 274 . . . Note=Calcium;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17050532;Dbxref=PMID:17050532 +P07250 UniProtKB Metal binding 325 325 . . . Note=Manganese;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17050532;Dbxref=PMID:17050532 +P07250 UniProtKB Metal binding 334 334 . . . Note=Calcium%3B via carbonyl oxygen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17050532;Dbxref=PMID:17050532 +P07250 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P07250 UniProtKB Modified residue 97 97 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07250 UniProtKB Sequence conflict 109 109 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07250 UniProtKB Beta strand 28 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Helix 35 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Helix 62 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Beta strand 69 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Beta strand 113 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Turn 120 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Beta strand 125 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Helix 145 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Helix 159 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Beta strand 164 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Helix 176 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Helix 184 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Beta strand 194 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Helix 200 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Turn 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Helix 211 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Helix 226 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Beta strand 252 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Helix 267 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Turn 273 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Beta strand 319 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Beta strand 329 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +P07250 UniProtKB Helix 339 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IEW +##sequence-region P38954 1 527 +P38954 UniProtKB Chain 1 527 . . . ID=PRO_0000084224;Note=Inositolphosphotransferase 1 +P38954 UniProtKB Topological domain 1 24 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38954 UniProtKB Transmembrane 25 45 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38954 UniProtKB Topological domain 46 99 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38954 UniProtKB Transmembrane 100 120 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38954 UniProtKB Topological domain 121 152 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38954 UniProtKB Transmembrane 153 173 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38954 UniProtKB Topological domain 174 190 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38954 UniProtKB Transmembrane 191 211 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38954 UniProtKB Topological domain 212 219 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38954 UniProtKB Transmembrane 220 240 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38954 UniProtKB Topological domain 241 288 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38954 UniProtKB Transmembrane 289 309 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38954 UniProtKB Topological domain 310 435 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38954 UniProtKB Transmembrane 436 456 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38954 UniProtKB Topological domain 457 461 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38954 UniProtKB Transmembrane 462 482 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38954 UniProtKB Topological domain 483 527 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38954 UniProtKB Compositional bias 378 384 . . . Note=Poly-Ser +##sequence-region P47034 1 131 +P47034 UniProtKB Chain 1 131 . . . ID=PRO_0000203052;Note=Increased copper sensitivity protein 3 +P47034 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47034 UniProtKB Transmembrane 74 94 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P07260 1 213 +P07260 UniProtKB Chain 1 213 . . . ID=PRO_0000193653;Note=Eukaryotic translation initiation factor 4E +P07260 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592868;Dbxref=PMID:7592868 +P07260 UniProtKB Modified residue 15 15 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:7592868;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198,PMID:7592868 +P07260 UniProtKB Modified residue 22 22 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P07260 UniProtKB Modified residue 28 28 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07260 UniProtKB Modified residue 30 30 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P07260 UniProtKB Cross-link 114 114 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P07260 UniProtKB Beta strand 9 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RF8 +P07260 UniProtKB Beta strand 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Helix 26 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RF8 +P07260 UniProtKB Beta strand 36 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Helix 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Helix 58 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Beta strand 63 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Helix 72 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Turn 83 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Beta strand 92 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Turn 104 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Beta strand 112 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Beta strand 124 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Helix 127 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Turn 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Turn 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Beta strand 149 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Beta strand 161 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Helix 172 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Beta strand 189 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RF8 +P07260 UniProtKB Beta strand 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Helix 199 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +P07260 UniProtKB Beta strand 210 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AP8 +##sequence-region P39520 1 1085 +P39520 UniProtKB Chain 1 1085 . . . ID=PRO_0000084164;Note=Protein IFH1 +P39520 UniProtKB Compositional bias 122 163 . . . Note=Asp/Glu-rich (highly acidic) +P39520 UniProtKB Modified residue 208 208 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P39520 UniProtKB Modified residue 1041 1041 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P25605 1 309 +P25605 UniProtKB Transit peptide 1 24 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7483834;Dbxref=PMID:7483834 +P25605 UniProtKB Chain 25 309 . . . ID=PRO_0000015637;Note=Acetolactate synthase small subunit%2C mitochondrial +P25605 UniProtKB Domain 79 159 . . . Note=ACT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01007 +P25605 UniProtKB Compositional bias 25 30 . . . Note=Poly-Ser +##sequence-region P07342 1 687 +P07342 UniProtKB Transit peptide 1 90 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07342 UniProtKB Chain 91 687 . . . ID=PRO_0000035664;Note=Acetolactate synthase catalytic subunit%2C mitochondrial +P07342 UniProtKB Nucleotide binding 355 376 . . . Note=FAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12496246;Dbxref=PMID:12496246 +P07342 UniProtKB Nucleotide binding 407 426 . . . Note=FAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12496246;Dbxref=PMID:12496246 +P07342 UniProtKB Region 499 579 . . . Note=Thiamine pyrophosphate binding +P07342 UniProtKB Metal binding 550 550 . . . Note=Magnesium +P07342 UniProtKB Metal binding 577 577 . . . Note=Magnesium +P07342 UniProtKB Metal binding 579 579 . . . Note=Magnesium%3B via carbonyl oxygen +P07342 UniProtKB Binding site 139 139 . . . Note=Thiamine pyrophosphate +P07342 UniProtKB Binding site 241 241 . . . Note=FAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12496246;Dbxref=PMID:12496246 +P07342 UniProtKB Turn 88 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 94 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 109 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 119 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 139 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 157 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 165 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 171 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 184 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 193 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Turn 196 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IMS +P07342 UniProtKB Helix 206 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 211 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 214 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 223 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 226 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 244 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 251 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 264 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 272 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 279 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 300 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 308 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 316 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 331 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 335 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 348 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 358 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 368 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 379 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 385 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 390 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 402 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 410 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 415 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 420 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 427 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 445 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 467 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JSC +P07342 UniProtKB Helix 473 486 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 491 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 499 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 512 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IMS +P07342 UniProtKB Helix 528 538 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 542 549 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 550 556 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 557 559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 560 566 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 571 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 582 587 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 589 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IMS +P07342 UniProtKB Beta strand 594 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5IMS +P07342 UniProtKB Helix 605 612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 614 619 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 622 624 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Helix 625 634 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 639 645 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5INU +P07342 UniProtKB Beta strand 652 654 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FEM +P07342 UniProtKB Helix 669 682 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FEM +P07342 UniProtKB Turn 683 685 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FEM +##sequence-region P21954 1 428 +P21954 UniProtKB Transit peptide 1 16 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1989987;Dbxref=PMID:1989987 +P21954 UniProtKB Chain 17 428 . . . ID=PRO_0000014426;Note=Isocitrate dehydrogenase [NADP]%2C mitochondrial +P21954 UniProtKB Nucleotide binding 91 93 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21954 UniProtKB Nucleotide binding 327 332 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21954 UniProtKB Region 110 116 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21954 UniProtKB Metal binding 269 269 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21954 UniProtKB Metal binding 292 292 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21954 UniProtKB Binding site 93 93 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21954 UniProtKB Binding site 98 98 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21954 UniProtKB Binding site 125 125 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21954 UniProtKB Binding site 148 148 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21954 UniProtKB Binding site 277 277 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21954 UniProtKB Binding site 345 345 . . . Note=NADP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21954 UniProtKB Site 155 155 . . . Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21954 UniProtKB Site 229 229 . . . Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21954 UniProtKB Beta strand 26 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Helix 33 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Turn 47 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Beta strand 55 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Helix 62 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Turn 68 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Helix 71 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Beta strand 84 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Helix 96 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Helix 111 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Beta strand 121 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Beta strand 142 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Helix 153 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Beta strand 158 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Beta strand 164 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Turn 177 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Beta strand 183 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Beta strand 194 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Helix 203 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Beta strand 224 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Turn 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Helix 236 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Helix 253 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Beta strand 263 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Helix 268 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Beta strand 280 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Helix 288 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Beta strand 307 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Beta strand 315 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFX +P21954 UniProtKB Beta strand 320 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Helix 330 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Helix 347 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Helix 367 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Helix 392 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Helix 403 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +P21954 UniProtKB Helix 409 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QFY +##sequence-region P43579 1 692 +P43579 UniProtKB Chain 1 692 . . . ID=PRO_0000084153;Note=Ino eighty subunit 1 +P43579 UniProtKB Coiled coil 340 385 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43579 UniProtKB Modified residue 27 27 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43579 UniProtKB Modified residue 487 487 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43579 UniProtKB Modified residue 493 493 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43579 UniProtKB Modified residue 504 504 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43579 UniProtKB Modified residue 507 507 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43579 UniProtKB Sequence conflict 219 219 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08561 1 116 +Q08561 UniProtKB Chain 1 116 . . . ID=PRO_0000084156;Note=Ino eighty subunit 4 +##sequence-region P38912 1 153 +P38912 UniProtKB Chain 1 153 . . . ID=PRO_0000145113;Note=Eukaryotic translation initiation factor 1A +P38912 UniProtKB Domain 22 96 . . . Note=S1-like +P38912 UniProtKB Beta strand 33 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM +P38912 UniProtKB Beta strand 46 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM +P38912 UniProtKB Beta strand 56 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM +P38912 UniProtKB Helix 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM +P38912 UniProtKB Beta strand 76 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM +P38912 UniProtKB Beta strand 86 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM +P38912 UniProtKB Helix 98 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM +##sequence-region P32481 1 527 +P32481 UniProtKB Chain 1 527 . . . ID=PRO_0000137448;Note=Eukaryotic translation initiation factor 2 subunit gamma +P32481 UniProtKB Domain 98 307 . . . Note=tr-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P32481 UniProtKB Nucleotide binding 107 114 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32481 UniProtKB Nucleotide binding 193 197 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32481 UniProtKB Nucleotide binding 249 252 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32481 UniProtKB Region 107 114 . . . Note=G1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P32481 UniProtKB Region 135 139 . . . Note=G2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P32481 UniProtKB Region 193 196 . . . Note=G3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P32481 UniProtKB Region 249 252 . . . Note=G4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P32481 UniProtKB Region 284 286 . . . Note=G5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P32481 UniProtKB Compositional bias 155 179 . . . Note=Cys-rich +P32481 UniProtKB Modified residue 60 60 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32481 UniProtKB Modified residue 258 258 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P32481 UniProtKB Beta strand 425 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZGN +P32481 UniProtKB Beta strand 460 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZGN +P32481 UniProtKB Beta strand 469 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZGN +P32481 UniProtKB Beta strand 480 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZGN +P32481 UniProtKB Beta strand 498 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZGN +P32481 UniProtKB Beta strand 506 523 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZGN +##sequence-region P39935 1 952 +P39935 UniProtKB Chain 1 952 . . . ID=PRO_0000213331;Note=Eukaryotic initiation factor 4F subunit p150 +P39935 UniProtKB Domain 607 850 . . . Note=MIF4G +P39935 UniProtKB Region 188 299 . . . Note=Interaction with PAB1 +P39935 UniProtKB Compositional bias 173 200 . . . Note=Pro/Ser/Thr-rich +P39935 UniProtKB Compositional bias 375 384 . . . Note=Ala/Glu-rich +P39935 UniProtKB Compositional bias 488 553 . . . Note=Arg/Ser-rich +P39935 UniProtKB Compositional bias 869 872 . . . Note=Poly-Glu +P39935 UniProtKB Compositional bias 873 899 . . . Note=Arg/Ser-rich +P39935 UniProtKB Modified residue 181 181 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P39935 UniProtKB Modified residue 883 883 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P39935 UniProtKB Modified residue 888 888 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P39935 UniProtKB Modified residue 908 908 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39935 UniProtKB Modified residue 948 948 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P39935 UniProtKB Mutagenesis 214 217 . . . Note=In TIF4631-213%3B abolishes interaction with PAB1 and inhibits poly(A)-dependent translation. KLRK->AAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9256432;Dbxref=PMID:9256432 +P39935 UniProtKB Sequence conflict 7 7 . . . Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39935 UniProtKB Sequence conflict 37 37 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39935 UniProtKB Sequence conflict 110 110 . . . Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39935 UniProtKB Sequence conflict 207 207 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39935 UniProtKB Sequence conflict 361 361 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39935 UniProtKB Helix 411 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RF8 +P39935 UniProtKB Helix 427 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RF8 +P39935 UniProtKB Helix 443 445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RF8 +P39935 UniProtKB Helix 454 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RF8 +P39935 UniProtKB Helix 471 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RF8 +P39935 UniProtKB Helix 603 615 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO +P39935 UniProtKB Beta strand 619 621 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSX +P39935 UniProtKB Helix 622 634 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO +P39935 UniProtKB Helix 635 638 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO +P39935 UniProtKB Helix 643 658 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO +P39935 UniProtKB Helix 660 662 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO +P39935 UniProtKB Helix 663 676 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO +P39935 UniProtKB Helix 692 709 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO +P39935 UniProtKB Helix 733 755 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO +P39935 UniProtKB Helix 761 776 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO +P39935 UniProtKB Helix 781 798 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO +P39935 UniProtKB Helix 812 827 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO +P39935 UniProtKB Helix 834 848 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VSO +##sequence-region P23301 1 157 +P23301 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:8243648;Dbxref=PMID:22814378,PMID:8243648 +P23301 UniProtKB Chain 2 157 . . . ID=PRO_0000142488;Note=Eukaryotic translation initiation factor 5A-1 +P23301 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:8243648;Dbxref=PMID:22814378,PMID:8243648 +P23301 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:8243648,ECO:0000269|PubMed:8325852;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198,PMID:8243648,PMID:8325852 +P23301 UniProtKB Modified residue 10 10 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P23301 UniProtKB Modified residue 51 51 . . . Note=Hypusine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19120453;Dbxref=PMID:19120453 +P23301 UniProtKB Modified residue 74 74 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P23301 UniProtKB Cross-link 86 86 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P23301 UniProtKB Mutagenesis 22 22 . . . Note=Temperature-sensitive growth phenotype%3B when associated with F-93. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 24 24 . . . Note=Temperature-sensitive growth phenotype. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 39 39 . . . Note=Temperature-sensitive growth phenotype. Lethal%3B when associated with L-83 and D-118 or with I-66 and D-118 or with D-118 and I-142 or with L-116 and D-118. C->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10229683,ECO:0000269|PubMed:18341589;Dbxref=PMID:10229683,PMID:18341589 +P23301 UniProtKB Mutagenesis 50 50 . . . Note=Lethal. G->A%2CP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 51 51 . . . Note=Impairs association to the ribosome and cell growth. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16215987,ECO:0000269|PubMed:16914118,ECO:0000269|PubMed:18341589,ECO:0000269|PubMed:19120453,ECO:0000269|PubMed:19424157;Dbxref=PMID:16215987,PMID:16914118,PMID:18341589,PMID:19120453,PMID:19424157 +P23301 UniProtKB Mutagenesis 52 52 . . . Note=Lethal. H->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 53 53 . . . Note=Lethal. G->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 54 54 . . . Note=Lethal. H->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 56 56 . . . Note=Temperature-sensitive growth phenotype. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 56 56 . . . Note=Lethal. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 57 57 . . . Note=Temperature-sensitive growth phenotype. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 63 63 . . . Note=Impairs programmed ribosomal frameshifting. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19424157;Dbxref=PMID:19424157 +P23301 UniProtKB Mutagenesis 66 66 . . . Note=Temperature-sensitive growth phenotype. Lethal%3B when associated with Y-39 and D-118. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 83 83 . . . Note=Temperature-sensitive growth phenotype. Lethal%3B when associated with Y-39 and D-118. P->S%2CL;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10229683,ECO:0000269|PubMed:18341589;Dbxref=PMID:10229683,PMID:18341589 +P23301 UniProtKB Mutagenesis 93 93 . . . Note=Lethal. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 102 102 . . . Note=Temperature-sensitive growth phenotype. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16408210;Dbxref=PMID:16408210 +P23301 UniProtKB Mutagenesis 116 116 . . . Note=Temperature-sensitive growth phenotype%3B when associated with D-118. Lethal%3B when associated with Y-39 and D-118. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 118 118 . . . Note=Temperature-sensitive growth phenotype%3B when associated with L-116 or W-122 or F-140 or I-142. Lethal%3B when associated with Y-39 and I-66 or with Y-39 and L-83 or with Y-39 and L-116 or with Y-39 and F-140 or with Y-39 and I-142 or with N-120 and D-124. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 118 118 . . . Note=Temperature-sensitive growth phenotype%3B when associated with W-122. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 120 120 . . . Note=Lethal%3B when associated with D-118 and D-124. L->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 122 122 . . . Note=Temperature-sensitive growth phenotype%3B when associated with V-118. D->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 124 124 . . . Note=Lethal%3B when associated with D-118 and N-120. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 140 140 . . . Note=Temperature-sensitive growth phenotype%3B when associated with D-118. Lethal%3B when associated with Y-39 and D-118. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 142 142 . . . Note=Temperature-sensitive growth phenotype%3B when associated with D-118. Lethal%3B when associated with Y-39 and D-118. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18341589;Dbxref=PMID:18341589 +P23301 UniProtKB Mutagenesis 149 149 . . . Note=In ts1159%3B temperature-sensitive growth phenotype and impairs programmed ribosomal frameshifting. S->P;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18341589,ECO:0000269|PubMed:19424157,ECO:0000269|PubMed:9582285;Dbxref=PMID:18341589,PMID:19424157,PMID:9582285 +P23301 UniProtKB Beta strand 19 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0 +P23301 UniProtKB Turn 23 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0 +P23301 UniProtKB Beta strand 31 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0 +P23301 UniProtKB Beta strand 37 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0 +P23301 UniProtKB Beta strand 50 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0 +P23301 UniProtKB Beta strand 56 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0 +P23301 UniProtKB Beta strand 70 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0 +P23301 UniProtKB Beta strand 87 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0 +P23301 UniProtKB Turn 96 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0 +P23301 UniProtKB Beta strand 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0 +P23301 UniProtKB Helix 120 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0 +P23301 UniProtKB Beta strand 135 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0 +P23301 UniProtKB Beta strand 144 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ER0 +##sequence-region Q9P305 1 131 +Q9P305 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q9P305 UniProtKB Chain 2 131 . . . ID=PRO_0000245365;Note=mRNA stability protein IGO2 +Q9P305 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q9P305 UniProtKB Modified residue 6 6 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q9P305 UniProtKB Modified residue 63 63 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +Q9P305 UniProtKB Modified residue 108 108 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q9P305 UniProtKB Modified residue 119 119 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P47042 1 667 +P47042 UniProtKB Chain 1 667 . . . ID=PRO_0000086138;Note=Probable serine/threonine-protein kinase IKS1 +P47042 UniProtKB Domain 173 530 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P47042 UniProtKB Nucleotide binding 179 187 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P47042 UniProtKB Active site 350 350 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P47042 UniProtKB Binding site 205 205 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P47042 UniProtKB Modified residue 96 96 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P47155 1 203 +P47155 UniProtKB Chain 1 203 . . . ID=PRO_0000203115;Note=Protein ILM1 +P47155 UniProtKB Topological domain 1 3 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47155 UniProtKB Transmembrane 4 24 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47155 UniProtKB Topological domain 25 58 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47155 UniProtKB Transmembrane 59 79 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47155 UniProtKB Topological domain 80 92 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47155 UniProtKB Transmembrane 93 113 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47155 UniProtKB Topological domain 114 114 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47155 UniProtKB Transmembrane 115 135 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47155 UniProtKB Topological domain 136 203 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38217 1 918 +P38217 UniProtKB Chain 1 918 . . . ID=PRO_0000120770;Note=Importin subunit beta-2 +P38217 UniProtKB Repeat 11 38 . . . Note=HEAT 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973 +P38217 UniProtKB Repeat 43 92 . . . Note=HEAT 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973 +P38217 UniProtKB Repeat 103 137 . . . Note=HEAT 3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973 +P38217 UniProtKB Repeat 145 181 . . . Note=HEAT 4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973 +P38217 UniProtKB Repeat 190 222 . . . Note=HEAT 5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973 +P38217 UniProtKB Repeat 235 263 . . . Note=HEAT 6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973 +P38217 UniProtKB Repeat 275 303 . . . Note=HEAT 7;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973 +P38217 UniProtKB Repeat 320 413 . . . Note=HEAT 8;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973 +P38217 UniProtKB Repeat 421 449 . . . Note=HEAT 9;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973 +P38217 UniProtKB Repeat 461 488 . . . Note=HEAT 10;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973 +P38217 UniProtKB Repeat 501 534 . . . Note=HEAT 11;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973 +P38217 UniProtKB Repeat 542 577 . . . Note=HEAT 12;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973 +P38217 UniProtKB Repeat 583 620 . . . Note=HEAT 13;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973 +P38217 UniProtKB Repeat 628 678 . . . Note=HEAT 14;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973 +P38217 UniProtKB Repeat 694 725 . . . Note=HEAT 15;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973 +P38217 UniProtKB Repeat 777 814 . . . Note=HEAT 17;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973 +P38217 UniProtKB Repeat 825 858 . . . Note=HEAT 18;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973 +P38217 UniProtKB Repeat 867 900 . . . Note=HEAT 19;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92973 +P38217 UniProtKB Compositional bias 373 392 . . . Note=Asp/Glu-rich (acidic) +##sequence-region P21190 1 360 +P21190 UniProtKB Chain 1 360 . . . ID=PRO_0000084181;Note=Meiosis-inducing protein 1 +##sequence-region P41833 1 600 +P41833 UniProtKB Chain 1 600 . . . ID=PRO_0000207634;Note=N6-adenosine-methyltransferase IME4 +P41833 UniProtKB Mutagenesis 348 348 . . . Note=Impairs ability to sporulate. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12384598;Dbxref=PMID:12384598 +P41833 UniProtKB Mutagenesis 351 351 . . . Note=Impairs ability to sporulate. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12384598;Dbxref=PMID:12384598 +##sequence-region P53219 1 342 +P53219 UniProtKB Transit peptide 1 38 . . . Note=Mitochondrion +P53219 UniProtKB Propeptide 39 46 . . . ID=PRO_0000410798;Note=Removed in mature form +P53219 UniProtKB Chain 47 342 . . . ID=PRO_0000202791;Note=Abhydrolase domain-containing protein IMO32 +P53219 UniProtKB Domain 75 326 . . . Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53219 UniProtKB Active site 152 152 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53219 UniProtKB Active site 319 319 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P32899 1 183 +P32899 UniProtKB Chain 1 183 . . . ID=PRO_0000132712;Note=U3 small nucleolar ribonucleoprotein protein IMP3 +P32899 UniProtKB Domain 109 175 . . . Note=S4 RNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00182 +##sequence-region P40573 1 187 +P40573 UniProtKB Chain 1 187 . . . ID=PRO_0000076520;Note=Transcriptional activator of sulfur metabolism MET28 +P40573 UniProtKB Domain 105 168 . . . Note=bZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P40573 UniProtKB Region 106 136 . . . Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P40573 UniProtKB Region 137 151 . . . Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +##sequence-region Q03081 1 177 +Q03081 UniProtKB Chain 1 177 . . . ID=PRO_0000046808;Note=Transcriptional regulator MET31 +Q03081 UniProtKB Zinc finger 95 117 . . . Note=C2H2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +##sequence-region P47169 1 1442 +P47169 UniProtKB Chain 1 1442 . . . ID=PRO_0000199968;Note=Sulfite reductase [NADPH] subunit beta +P47169 UniProtKB Domain 682 831 . . . Note=Flavodoxin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00088 +P47169 UniProtKB Metal binding 1300 1300 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47169 UniProtKB Metal binding 1306 1306 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47169 UniProtKB Metal binding 1345 1345 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47169 UniProtKB Metal binding 1349 1349 . . . Note=Iron (siroheme axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47169 UniProtKB Metal binding 1349 1349 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47169 UniProtKB Modified residue 903 903 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P05694 1 767 +P05694 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7483834;Dbxref=PMID:7483834 +P05694 UniProtKB Chain 2 767 . . . ID=PRO_0000098704;Note=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase +P05694 UniProtKB Metal binding 655 655 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05694 UniProtKB Metal binding 657 657 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05694 UniProtKB Metal binding 737 737 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05694 UniProtKB Modified residue 89 89 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P05694 UniProtKB Modified residue 242 242 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P05694 UniProtKB Modified residue 566 566 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P05694 UniProtKB Modified residue 629 629 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P05694 UniProtKB Modified residue 706 706 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P05694 UniProtKB Sequence conflict 72 80 . . . Note=LSLLFNVIP->FVFVVQCHS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05694 UniProtKB Sequence conflict 407 407 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P10659 1 382 +P10659 UniProtKB Chain 1 382 . . . ID=PRO_0000174451;Note=S-adenosylmethionine synthase 1 +P10659 UniProtKB Nucleotide binding 166 168 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00266 +P10659 UniProtKB Nucleotide binding 234 237 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00266 +P10659 UniProtKB Nucleotide binding 251 252 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817 +P10659 UniProtKB Metal binding 10 10 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13444 +P10659 UniProtKB Metal binding 44 44 . . . Note=Potassium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817 +P10659 UniProtKB Binding site 16 16 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00266 +P10659 UniProtKB Binding site 57 57 . . . Note=Methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817 +P10659 UniProtKB Binding site 100 100 . . . Note=Methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817 +P10659 UniProtKB Binding site 245 245 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00266 +P10659 UniProtKB Binding site 245 245 . . . Note=Methionine%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817 +P10659 UniProtKB Binding site 268 268 . . . Note=ATP%3B via amide nitrogen%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817 +P10659 UniProtKB Binding site 272 272 . . . Note=ATP%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817 +P10659 UniProtKB Binding site 276 276 . . . Note=ATP%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13444 +P10659 UniProtKB Binding site 276 276 . . . Note=Methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817 +P10659 UniProtKB Sequence conflict 246 246 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10659 UniProtKB Sequence conflict 357 357 . . . Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04922 1 465 +Q04922 UniProtKB Chain 1 465 . . . ID=PRO_0000253803;Note=Mitochondrial F-box protein MFB1 +Q04922 UniProtKB Domain 14 60 . . . Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080 +##sequence-region P32787 1 269 +P32787 UniProtKB Transit peptide 1 30 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32787 UniProtKB Chain 31 269 . . . ID=PRO_0000021719;Note=Mitochondrial genome maintenance protein MGM101 +##sequence-region P28321 1 313 +P28321 UniProtKB Chain 1 313 . . . ID=PRO_0000203164;Note=Monoglyceride lipase +P28321 UniProtKB Active site 123 123 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35678 +P28321 UniProtKB Active site 251 251 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35678 +P28321 UniProtKB Active site 281 281 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35678 +P28321 UniProtKB Sequence conflict 244 244 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28321 UniProtKB Sequence conflict 290 290 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P28321 UniProtKB Beta strand 16 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Beta strand 23 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Beta strand 34 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Beta strand 40 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Helix 53 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Helix 57 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Beta strand 68 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Turn 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Helix 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Helix 92 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Beta strand 117 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Helix 124 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Turn 137 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Beta strand 143 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Beta strand 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Helix 156 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Helix 164 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Turn 171 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Helix 186 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Helix 193 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Turn 203 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Helix 212 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Helix 229 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Helix 232 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Beta strand 243 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Beta strand 252 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Helix 256 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Beta strand 269 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Turn 283 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +P28321 UniProtKB Helix 289 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZWN +##sequence-region P32266 1 881 +P32266 UniProtKB Transit peptide 1 59 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12707284;Dbxref=PMID:12707284 +P32266 UniProtKB Chain 60 881 . . . ID=PRO_0000007400;Note=Dynamin-like GTPase MGM1 large isoform +P32266 UniProtKB Chain 140 881 . . . ID=PRO_0000007401;Note=Dynamin-like GTPase MGM1 small isoform +P32266 UniProtKB Topological domain 60 72 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32266 UniProtKB Transmembrane 73 92 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32266 UniProtKB Topological domain 93 881 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32266 UniProtKB Domain 207 505 . . . Note=Dynamin-type G +P32266 UniProtKB Domain 780 872 . . . Note=GED;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00720 +P32266 UniProtKB Nucleotide binding 217 224 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32266 UniProtKB Nucleotide binding 317 321 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32266 UniProtKB Nucleotide binding 385 388 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32266 UniProtKB Compositional bias 149 178 . . . Note=Asp-rich (acidic) +P32266 UniProtKB Mutagenesis 1 1 . . . Note=Abolishes translation. M->A +P32266 UniProtKB Mutagenesis 39 39 . . . Note=No effect on translation. M->A +P32266 UniProtKB Mutagenesis 79 79 . . . Note=Loss of function%3B most MGM1 processed to s-MGM1. G->D%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15096522;Dbxref=PMID:15096522 +P32266 UniProtKB Mutagenesis 81 81 . . . Note=No effect on translation. M->A +P32266 UniProtKB Mutagenesis 92 92 . . . Note=No effect on translation. M->A +P32266 UniProtKB Mutagenesis 223 223 . . . Note=Loss of stability. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12566426;Dbxref=PMID:12566426 +P32266 UniProtKB Mutagenesis 224 224 . . . Note=Loss of GTPase activity. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10037792,ECO:0000269|PubMed:12566426;Dbxref=PMID:10037792,PMID:12566426 +P32266 UniProtKB Mutagenesis 224 224 . . . Note=Loss of GTPase activity. S->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10037792,ECO:0000269|PubMed:12566426;Dbxref=PMID:10037792,PMID:12566426 +P32266 UniProtKB Mutagenesis 244 244 . . . Note=Loss of GTPase activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12566426;Dbxref=PMID:12566426 +P32266 UniProtKB Mutagenesis 294 294 . . . Note=In mdm17%3B loss of function at 37 degrees Celsius. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10037792;Dbxref=PMID:10037792 +P32266 UniProtKB Mutagenesis 824 824 . . . Note=Loss of GED function. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12566426;Dbxref=PMID:12566426 +P32266 UniProtKB Mutagenesis 854 854 . . . Note=Loss of GED function. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12566426;Dbxref=PMID:12566426 +P32266 UniProtKB Sequence conflict 4 4 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32266 UniProtKB Sequence conflict 129 129 . . . Note=G->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32266 UniProtKB Sequence conflict 170 170 . . . Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P26188 1 188 +P26188 UniProtKB Chain 1 188 . . . ID=PRO_0000139362;Note=Methylated-DNA--protein-cysteine methyltransferase +P26188 UniProtKB Active site 151 151 . . . Note=Nucleophile%3B methyl group acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10017 +P26188 UniProtKB Binding site 120 120 . . . Note=DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26188 UniProtKB Binding site 121 121 . . . Note=DNA%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26188 UniProtKB Binding site 134 134 . . . Note=DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26188 UniProtKB Binding site 157 157 . . . Note=DNA%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q04472 1 501 +Q04472 UniProtKB Chain 1 501 . . . ID=PRO_0000203293;Note=Mitochondrial inner membrane i-AAA protease supercomplex subunit MGR3 +Q04472 UniProtKB Topological domain 1 77 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18843051;Dbxref=PMID:18843051 +Q04472 UniProtKB Transmembrane 78 95 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04472 UniProtKB Topological domain 96 501 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18843051;Dbxref=PMID:18843051 +Q04472 UniProtKB Repeat 109 144 . . . Note=TPR 1 +Q04472 UniProtKB Repeat 154 187 . . . Note=TPR 2 +Q04472 UniProtKB Repeat 386 420 . . . Note=TPR 3 +Q04472 UniProtKB Repeat 440 473 . . . Note=TPR 4 +##sequence-region P36046 1 403 +P36046 UniProtKB Transit peptide 1 31 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15620710;Dbxref=PMID:15620710 +P36046 UniProtKB Chain 32 403 . . . ID=PRO_0000203135;Note=Mitochondrial intermembrane space import and assembly protein 40 +P36046 UniProtKB Topological domain 33 46 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36046 UniProtKB Transmembrane 47 66 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36046 UniProtKB Topological domain 67 403 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36046 UniProtKB Domain 304 348 . . . Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +P36046 UniProtKB Motif 307 317 . . . Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +P36046 UniProtKB Motif 330 340 . . . Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +P36046 UniProtKB Disulfide bond 296 298 . . . Note=Redox-active;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19667201;Dbxref=PMID:19667201 +P36046 UniProtKB Disulfide bond 307 340 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU01150,ECO:0000269|PubMed:19667201;Dbxref=PMID:19667201 +P36046 UniProtKB Disulfide bond 317 330 . . . Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU01150,ECO:0000269|PubMed:19667201;Dbxref=PMID:19667201 +P36046 UniProtKB Mutagenesis 296 296 . . . Note=Loss of function%3B when associated with S-298. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15364952,ECO:0000269|PubMed:15620710;Dbxref=PMID:15364952,PMID:15620710 +P36046 UniProtKB Mutagenesis 298 298 . . . Note=Loss of function%3B when associated with S-296. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15364952,ECO:0000269|PubMed:15620710;Dbxref=PMID:15364952,PMID:15620710 +P36046 UniProtKB Mutagenesis 307 307 . . . Note=Loss of function%3B when associated with S-317. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15364952,ECO:0000269|PubMed:15620710;Dbxref=PMID:15364952,PMID:15620710 +P36046 UniProtKB Mutagenesis 317 317 . . . Note=Loss of function%3B when associated with S-307. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15364952;Dbxref=PMID:15364952 +P36046 UniProtKB Mutagenesis 330 330 . . . Note=Loss of function%3B when associated with S-340. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15364952;Dbxref=PMID:15364952 +P36046 UniProtKB Mutagenesis 340 340 . . . Note=Loss of function%3B when associated with S-330. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15364952;Dbxref=PMID:15364952 +P36046 UniProtKB Helix 282 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A3C +P36046 UniProtKB Turn 287 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A3C +P36046 UniProtKB Helix 297 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A3C +P36046 UniProtKB Turn 300 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A3C +P36046 UniProtKB Helix 308 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A3C +P36046 UniProtKB Beta strand 323 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A3C +P36046 UniProtKB Turn 326 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A3C +P36046 UniProtKB Helix 331 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A3C +P36046 UniProtKB Turn 345 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A3C +##sequence-region P50945 1 234 +P50945 UniProtKB Chain 1 234 . . . ID=PRO_0000203438;Note=MICOS complex subunit MIC27 +P50945 UniProtKB Topological domain 1 100 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50945 UniProtKB Transmembrane 101 120 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50945 UniProtKB Topological domain 121 141 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50945 UniProtKB Transmembrane 142 161 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50945 UniProtKB Topological domain 162 234 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39943 1 394 +P39943 UniProtKB Chain 1 394 . . . ID=PRO_0000046886;Note=Transcription corepressor MIG3 +P39943 UniProtKB Zinc finger 17 39 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P39943 UniProtKB Zinc finger 45 69 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P39943 UniProtKB Compositional bias 163 296 . . . Note=Ser-rich +##sequence-region Q08176 1 113 +Q08176 UniProtKB Chain 1 113 . . . ID=PRO_0000218767;Note=Mitochondrial import protein 1 +Q08176 UniProtKB Transmembrane 39 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04341 1 121 +Q04341 UniProtKB Chain 1 121 . . . ID=PRO_0000242621;Note=Mitochondrial intermembrane space cysteine motif-containing protein MIX14 +Q04341 UniProtKB Domain 14 56 . . . Note=CHCH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q04341 UniProtKB Domain 60 105 . . . Note=CHCH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q04341 UniProtKB Motif 17 27 . . . Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q04341 UniProtKB Motif 38 48 . . . Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q04341 UniProtKB Motif 63 73 . . . Note=Cx9C motif 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q04341 UniProtKB Motif 87 97 . . . Note=Cx9C motif 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q04341 UniProtKB Disulfide bond 17 48 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q04341 UniProtKB Disulfide bond 27 38 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q04341 UniProtKB Disulfide bond 63 97 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q04341 UniProtKB Disulfide bond 73 87 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +##sequence-region P38920 1 769 +P38920 UniProtKB Chain 1 769 . . . ID=PRO_0000178008;Note=DNA mismatch repair protein MLH1 +P38920 UniProtKB Region 1 335 . . . Note=DNA- and ATP-binding +P38920 UniProtKB Region 501 756 . . . Note=Interaction with PMS1 +P38920 UniProtKB Modified residue 441 441 . . . Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38920 UniProtKB Natural variant 240 240 . . . Note=In strain: SK1. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773 +P38920 UniProtKB Natural variant 242 242 . . . Note=In strain: YJM326 and YJM339. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773 +P38920 UniProtKB Natural variant 271 271 . . . Note=In strain: EAY1066%2C EAY1068%2C M2-8%2C M7-8%2C M5-7%2C SK1%2C YJM269%2C YJM280%2C YJM320%2C YJM326%2C YJM339 and YJM627. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773 +P38920 UniProtKB Natural variant 309 309 . . . Note=In strain: M2-8. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773 +P38920 UniProtKB Natural variant 321 321 . . . Note=In strain: EAY1066. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773 +P38920 UniProtKB Natural variant 333 333 . . . Note=In strain: SK1. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773 +P38920 UniProtKB Natural variant 375 375 . . . Note=In strain: YJM339. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773 +P38920 UniProtKB Natural variant 452 452 . . . Note=In strain: EAY1068%2C M2-8%2C M7-8%2C M5-7%2C YJM269 and YJM627. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773 +P38920 UniProtKB Natural variant 465 465 . . . Note=In strain: EAY1066 and YJM280. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773 +P38920 UniProtKB Natural variant 470 470 . . . Note=In strain: YJM339. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773 +P38920 UniProtKB Natural variant 607 607 . . . Note=In strain: EAY1068%2C M2-8%2C M7-8%2C M5-7 and YJM627. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773 +P38920 UniProtKB Natural variant 678 678 . . . Note=In strain: SK1%2C YJM320 and YJM339. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773 +P38920 UniProtKB Natural variant 703 703 . . . Note=In strain: SK1%2C YJM320 and YJM339. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773 +P38920 UniProtKB Natural variant 761 761 . . . Note=In strain: EAY1066%2C EAY1068%2C M2-8%2C M7-8%2C M5-7%2C SK1%2C YJM145%2C YJM269%2C YJM320%2C YJM339 and YJM627%3B forms a non-functional heterodimer with PMS1 from strain S288c%2C resulting in an accumulation of mutations in spore progeny of crosses between these strains. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773 +P38920 UniProtKB Mutagenesis 31 31 . . . Note=Reduces ATPase activity by 98%25. Displays 3300-fold increase in spontaneous mutation accumulation. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10938116,ECO:0000269|PubMed:11717305;Dbxref=PMID:10938116,PMID:11717305 +P38920 UniProtKB Mutagenesis 35 35 . . . Note=Abolishes ATP binding%2C reducing ATPase activity by 95%25. Displays 9800-fold increase in spontaneous mutation accumulation. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11717305;Dbxref=PMID:11717305 +P38920 UniProtKB Mutagenesis 41 41 . . . Note=Defective in a mismatch repair assay. Abolishes heterodimer formation. Displays an increases spontaneous mutation accumulation. A->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11555625,ECO:0000269|PubMed:9234704;Dbxref=PMID:11555625,PMID:9234704 +P38920 UniProtKB Mutagenesis 41 41 . . . Note=Reduces heterodimer formation. Displays an weak increase in spontaneous mutation accumulation. A->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11555625,ECO:0000269|PubMed:9234704;Dbxref=PMID:11555625,PMID:9234704 +P38920 UniProtKB Mutagenesis 41 41 . . . Note=Fully functional in a mismatch repair assay. A->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11555625,ECO:0000269|PubMed:9234704;Dbxref=PMID:11555625,PMID:9234704 +P38920 UniProtKB Mutagenesis 64 64 . . . Note=Defective in a mismatch repair assay. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625 +P38920 UniProtKB Mutagenesis 65 65 . . . Note=Defective in a mismatch repair assay. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625 +P38920 UniProtKB Mutagenesis 96 96 . . . Note=Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234704;Dbxref=PMID:9234704 +P38920 UniProtKB Mutagenesis 97 97 . . . Note=Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234704;Dbxref=PMID:9234704 +P38920 UniProtKB Mutagenesis 98 98 . . . Note=Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. G->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10938116,ECO:0000269|PubMed:9234704;Dbxref=PMID:10938116,PMID:9234704 +P38920 UniProtKB Mutagenesis 98 98 . . . Note=Abolishes heterodimer formation. Displays an increase in spontaneous mutation accumulation. G->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10938116,ECO:0000269|PubMed:9234704;Dbxref=PMID:10938116,PMID:9234704 +P38920 UniProtKB Mutagenesis 99 99 . . . Note=Defective in a mismatch repair assay. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625 +P38920 UniProtKB Mutagenesis 104 104 . . . Note=Defective in a mismatch repair assay. I->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625 +P38920 UniProtKB Mutagenesis 114 114 . . . Note=Defective in a mismatch repair assay. T->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625 +P38920 UniProtKB Mutagenesis 214 214 . . . Note=Partially defective in a mismatch repair assay. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625 +P38920 UniProtKB Mutagenesis 216 216 . . . Note=Fully functional in a mismatch repair assay. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625 +P38920 UniProtKB Mutagenesis 265 265 . . . Note=Partially defective in a mismatch repair assay. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625 +P38920 UniProtKB Mutagenesis 265 265 . . . Note=Partially defective in a mismatch repair assay. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625 +P38920 UniProtKB Mutagenesis 273 273 . . . Note=Strongly reduces DNA-binding and displays 12000-fold increase in spontaneous mutation accumulation%3B when associated with E-274. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12682353;Dbxref=PMID:12682353 +P38920 UniProtKB Mutagenesis 274 274 . . . Note=Reduces DNA-binding and displays a 1700-fold increase in spontaneous mutation accumulation. Strongly reduces DNA-binding and displays 12000-fold increase in spontaneous mutation accumulation%3B when associated with E-273. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12682353;Dbxref=PMID:12682353 +P38920 UniProtKB Mutagenesis 326 326 . . . Note=Partially defective in a mismatch repair assay. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625 +P38920 UniProtKB Mutagenesis 326 326 . . . Note=Fully functional in a mismatch repair assay. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625 +P38920 UniProtKB Mutagenesis 552 552 . . . Note=Defective in a mismatch repair assay. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625 +P38920 UniProtKB Mutagenesis 672 672 . . . Note=Defective in a mismatch repair assay. R->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625 +P38920 UniProtKB Mutagenesis 694 694 . . . Note=Fully functional in a mismatch repair assay. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625 +P38920 UniProtKB Mutagenesis 764 764 . . . Note=Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234704;Dbxref=PMID:9234704 +P38920 UniProtKB Mutagenesis 764 764 . . . Note=No effect. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234704;Dbxref=PMID:9234704 +P38920 UniProtKB Mutagenesis 766 766 . . . Note=Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234704;Dbxref=PMID:9234704 +P38920 UniProtKB Mutagenesis 767 767 . . . Note=Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234704;Dbxref=PMID:9234704 +P38920 UniProtKB Mutagenesis 769 769 . . . Note=No effect. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234704;Dbxref=PMID:9234704 +P38920 UniProtKB Mutagenesis 769 769 . . . Note=Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234704;Dbxref=PMID:9234704 +P38920 UniProtKB Sequence conflict 258 258 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38920 UniProtKB Sequence conflict 288 288 . . . Note=N->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38920 UniProtKB Sequence conflict 708 708 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38920 UniProtKB Helix 512 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Helix 527 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Beta strand 537 543 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Turn 544 547 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Beta strand 548 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Beta strand 556 561 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Helix 562 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Beta strand 582 585 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Helix 591 593 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Helix 597 601 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Helix 610 622 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Helix 624 631 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Beta strand 634 639 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Helix 644 646 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Beta strand 647 654 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Helix 666 675 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Helix 682 697 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Helix 714 733 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Helix 735 742 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Helix 747 752 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Beta strand 753 758 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P38920 UniProtKB Helix 759 765 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +##sequence-region P40457 1 1679 +P40457 UniProtKB Chain 1 1679 . . . ID=PRO_0000096502;Note=Protein MLP2 +P40457 UniProtKB Coiled coil 32 176 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40457 UniProtKB Coiled coil 233 466 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40457 UniProtKB Coiled coil 516 1064 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40457 UniProtKB Coiled coil 1099 1491 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40457 UniProtKB Motif 417 433 . . . Note=Bipartite nuclear localization signal 1 +P40457 UniProtKB Motif 639 655 . . . Note=Bipartite nuclear localization signal 2 +P40457 UniProtKB Motif 1433 1449 . . . Note=Bipartite nuclear localization signal 3 +P40457 UniProtKB Compositional bias 467 470 . . . Note=Poly-Leu +P40457 UniProtKB Compositional bias 1393 1508 . . . Note=Glu-rich +P40457 UniProtKB Modified residue 1512 1512 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40457 UniProtKB Modified residue 1670 1670 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P53102 1 219 +P53102 UniProtKB Chain 1 219 . . . ID=PRO_0000096522;Note=Meiotic nuclear division protein 1 +P53102 UniProtKB Coiled coil 88 181 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P24720 1 663 +P24720 UniProtKB Chain 1 663 . . . ID=PRO_0000096524;Note=Protein MNE1 +##sequence-region P18408 1 261 +P18408 UniProtKB Chain 1 261 . . . ID=PRO_0000100662;Note=Phosphoadenosine phosphosulfate reductase +P18408 UniProtKB Sequence conflict 242 261 . . . Note=KTECGIHEASRFAQFLKQDA->RPSVEFMKPADSRNF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18408 UniProtKB Beta strand 3 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Helix 7 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Beta strand 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Helix 14 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Helix 30 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Beta strand 42 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Helix 52 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Turn 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Beta strand 72 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Helix 83 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Helix 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Beta strand 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Helix 115 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Helix 126 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Helix 131 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Helix 140 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Beta strand 153 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Helix 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Helix 165 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Beta strand 172 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Turn 177 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Beta strand 181 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Turn 186 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Helix 192 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Helix 208 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Helix 220 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Turn 232 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Turn 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +P18408 UniProtKB Helix 251 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OQ2 +##sequence-region Q07684 1 458 +Q07684 UniProtKB Chain 1 458 . . . ID=PRO_0000242483;Note=Morphogenetic regulator of filamentous growth protein 1 +Q07684 UniProtKB Compositional bias 5 64 . . . Note=Pro-rich +##sequence-region P53152 1 137 +P53152 UniProtKB Chain 1 137 . . . ID=PRO_0000082598;Note=Ubiquitin-conjugating enzyme variant MMS2 +P53152 UniProtKB Modified residue 71 71 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53152 UniProtKB Mutagenesis 8 8 . . . Note=Strongly reduces UBC13 binding and interferes with error-free DNA repair. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11440714;Dbxref=PMID:11440714 +P53152 UniProtKB Helix 6 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P53152 UniProtKB Beta strand 26 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P53152 UniProtKB Beta strand 40 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P53152 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P53152 UniProtKB Turn 52 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P53152 UniProtKB Beta strand 57 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P53152 UniProtKB Turn 66 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P53152 UniProtKB Beta strand 74 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P53152 UniProtKB Beta strand 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GMI +P53152 UniProtKB Turn 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P53152 UniProtKB Helix 98 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P53152 UniProtKB Helix 109 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +P53152 UniProtKB Helix 123 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JAT +##sequence-region P38888 1 796 +P38888 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38888 UniProtKB Chain 21 796 . . . ID=PRO_0000210324;Note=ER degradation-enhancing alpha-mannosidase-like protein 1 +P38888 UniProtKB Active site 372 372 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31723 +P38888 UniProtKB Metal binding 495 495 . . . Note=Calcium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32906 +P38888 UniProtKB Glycosylation 86 86 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38888 UniProtKB Glycosylation 517 517 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38888 UniProtKB Glycosylation 672 672 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38888 UniProtKB Glycosylation 762 762 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P41821 1 548 +P41821 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41821 UniProtKB Chain 21 548 . . . ID=PRO_0000096483;Note=Stretch-activated cation channel MID1 +P41821 UniProtKB Topological domain 21 341 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41821 UniProtKB Transmembrane 342 358 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41821 UniProtKB Topological domain 359 548 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41821 UniProtKB Compositional bias 431 450 . . . Note=Cys-rich +P41821 UniProtKB Compositional bias 487 506 . . . Note=Cys-rich +P41821 UniProtKB Glycosylation 32 32 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41821 UniProtKB Glycosylation 70 70 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41821 UniProtKB Glycosylation 112 112 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41821 UniProtKB Glycosylation 125 125 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41821 UniProtKB Glycosylation 159 159 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41821 UniProtKB Glycosylation 175 175 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41821 UniProtKB Glycosylation 228 228 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41821 UniProtKB Glycosylation 238 238 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41821 UniProtKB Glycosylation 265 265 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41821 UniProtKB Glycosylation 282 282 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41821 UniProtKB Glycosylation 285 285 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41821 UniProtKB Glycosylation 291 291 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41821 UniProtKB Glycosylation 324 324 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41821 UniProtKB Mutagenesis 356 356 . . . Note=Significantly low viability and relatively normal Ca(2+) accumulation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14697255;Dbxref=PMID:14697255 +P41821 UniProtKB Mutagenesis 356 356 . . . Note=Substitution by hydrophilic amino acids causes lethality and low Ca(2+) accumulation. F->H%2CQ%2CD%2CE%2CK%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14697255;Dbxref=PMID:14697255 +P41821 UniProtKB Mutagenesis 356 356 . . . Note=Substitution by hydrophobic%2C large amino acids does not cause lethality nor low Ca(2+) accumulation. F->L%2CW%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14697255;Dbxref=PMID:14697255 +P41821 UniProtKB Mutagenesis 417 417 . . . Note=Non-functional. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11796727;Dbxref=PMID:11796727 +P41821 UniProtKB Mutagenesis 431 431 . . . Note=Non-functional. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11796727;Dbxref=PMID:11796727 +P41821 UniProtKB Mutagenesis 434 434 . . . Note=Non-functional. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11796727;Dbxref=PMID:11796727 +P41821 UniProtKB Mutagenesis 491 491 . . . Note=Functionally impaired. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11796727;Dbxref=PMID:11796727 +P41821 UniProtKB Mutagenesis 498 498 . . . Note=Non-functional. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11796727;Dbxref=PMID:11796727 +P41821 UniProtKB Mutagenesis 506 506 . . . Note=Functionally impaired. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11796727;Dbxref=PMID:11796727 +P41821 UniProtKB Mutagenesis 531 531 . . . Note=Functionally impaired. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11796727;Dbxref=PMID:11796727 +##sequence-region P53035 1 382 +P53035 UniProtKB Chain 1 382 . . . ID=PRO_0000046882;Note=Regulatory protein MIG2 +P53035 UniProtKB Zinc finger 17 39 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P53035 UniProtKB Zinc finger 45 69 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +##sequence-region P32491 1 506 +P32491 UniProtKB Chain 1 506 . . . ID=PRO_0000086333;Note=MAP kinase kinase MKK2/SSP33 +P32491 UniProtKB Domain 214 481 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32491 UniProtKB Nucleotide binding 220 228 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32491 UniProtKB Active site 342 342 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P32491 UniProtKB Binding site 243 243 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32491 UniProtKB Sequence conflict 252 252 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P34072 1 584 +P34072 UniProtKB Chain 1 584 . . . ID=PRO_0000096494;Note=Negative regulator of RAS-cAMP pathway +P34072 UniProtKB Modified residue 25 25 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P34072 UniProtKB Modified residue 247 247 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P34072 UniProtKB Modified residue 276 276 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P34072 UniProtKB Modified residue 442 442 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198 +P34072 UniProtKB Modified residue 518 518 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06580 1 163 +Q06580 UniProtKB Chain 1 163 . . . ID=PRO_0000198766;Note=Myosin light chain 2 +Q06580 UniProtKB Domain 15 50 . . . Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +Q06580 UniProtKB Domain 92 127 . . . Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +Q06580 UniProtKB Calcium binding 28 39 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +##sequence-region P32047 1 452 +P32047 UniProtKB Chain 1 452 . . . ID=PRO_0000096499;Note=Protein MLF3 +P32047 UniProtKB Compositional bias 211 214 . . . Note=Poly-Thr +P32047 UniProtKB Compositional bias 271 274 . . . Note=Poly-Ser +P32047 UniProtKB Modified residue 8 8 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P32047 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32047 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32047 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32047 UniProtKB Modified residue 74 74 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32047 UniProtKB Modified residue 79 79 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32047 UniProtKB Modified residue 121 121 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32047 UniProtKB Modified residue 145 145 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32047 UniProtKB Modified residue 156 156 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32047 UniProtKB Modified residue 160 160 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32047 UniProtKB Modified residue 169 169 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32047 UniProtKB Modified residue 171 171 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P32047 UniProtKB Modified residue 173 173 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32047 UniProtKB Modified residue 183 183 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32047 UniProtKB Modified residue 189 189 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32047 UniProtKB Modified residue 227 227 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32047 UniProtKB Modified residue 228 228 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32047 UniProtKB Modified residue 257 257 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32047 UniProtKB Modified residue 265 265 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32047 UniProtKB Modified residue 295 295 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32047 UniProtKB Modified residue 297 297 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32047 UniProtKB Modified residue 320 320 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32047 UniProtKB Modified residue 353 353 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32047 UniProtKB Modified residue 439 439 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q12372 1 583 +Q12372 UniProtKB Chain 1 583 . . . ID=PRO_0000054157;Note=S-methylmethionine permease 1 +Q12372 UniProtKB Topological domain 1 77 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Transmembrane 78 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Topological domain 97 101 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Transmembrane 102 123 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Topological domain 124 143 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Transmembrane 144 164 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Topological domain 165 182 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Transmembrane 183 203 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Topological domain 204 215 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Transmembrane 216 236 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Topological domain 237 254 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Transmembrane 255 274 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Topological domain 275 298 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Transmembrane 299 319 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Topological domain 320 356 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Transmembrane 357 377 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Topological domain 378 402 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Transmembrane 403 423 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Topological domain 424 428 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Transmembrane 429 449 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Topological domain 450 473 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Transmembrane 474 494 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Topological domain 495 505 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Transmembrane 506 526 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Topological domain 527 583 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12372 UniProtKB Modified residue 6 6 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08986 +Q12372 UniProtKB Modified residue 21 21 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12372 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q06324 1 491 +Q06324 UniProtKB Chain 1 491 . . . ID=PRO_0000245841;Note=Mitochondrial MYO2 receptor-related protein 1 +Q06324 UniProtKB Region 300 439 . . . Note=Interaction with MYO2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201867;Dbxref=PMID:15201867 +Q06324 UniProtKB Coiled coil 295 384 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06324 UniProtKB Modified residue 12 12 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06324 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06324 UniProtKB Modified residue 37 37 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P46982 1 586 +P46982 UniProtKB Signal peptide 1 29 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46982 UniProtKB Chain 30 586 . . . ID=PRO_0000203019;Note=Alpha-1%2C2-mannosyltransferase MNN5 +P46982 UniProtKB Glycosylation 113 113 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46982 UniProtKB Glycosylation 136 136 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46982 UniProtKB Glycosylation 259 259 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46982 UniProtKB Glycosylation 264 264 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46982 UniProtKB Sequence conflict 395 395 . . . Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39107 1 395 +P39107 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9434768;Dbxref=PMID:9434768 +P39107 UniProtKB Chain 2 395 . . . ID=PRO_0000193670;Note=Mannan polymerase complexes subunit MNN9 +P39107 UniProtKB Topological domain 2 17 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39107 UniProtKB Transmembrane 18 33 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39107 UniProtKB Topological domain 34 395 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39107 UniProtKB Mutagenesis 236 236 . . . Note=Reduced activity of the M-Pol I complex. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12235155;Dbxref=PMID:12235155 +P39107 UniProtKB Helix 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Turn 108 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Beta strand 116 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Helix 128 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Helix 141 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Beta strand 144 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Helix 154 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Helix 175 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Beta strand 180 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Helix 204 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Beta strand 229 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Beta strand 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Helix 246 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Beta strand 256 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Turn 269 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Beta strand 273 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Helix 288 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Turn 308 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Helix 317 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Beta strand 331 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Beta strand 338 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Helix 345 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Helix 364 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +P39107 UniProtKB Beta strand 379 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZF8 +##sequence-region P40549 1 630 +P40549 UniProtKB Chain 1 630 . . . ID=PRO_0000080560;Note=Alpha-1%2C3-mannosyltransferase MNT3 +P40549 UniProtKB Topological domain 1 14 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40549 UniProtKB Transmembrane 15 31 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40549 UniProtKB Topological domain 32 630 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40549 UniProtKB Glycosylation 34 34 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40549 UniProtKB Glycosylation 168 168 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53745 1 580 +P53745 UniProtKB Chain 1 580 . . . ID=PRO_0000080561;Note=Probable alpha-1%2C3-mannosyltransferase MNT4 +P53745 UniProtKB Topological domain 1 10 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53745 UniProtKB Transmembrane 11 29 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53745 UniProtKB Topological domain 30 580 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53745 UniProtKB Glycosylation 132 132 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53745 UniProtKB Glycosylation 167 167 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53745 UniProtKB Glycosylation 223 223 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53745 UniProtKB Glycosylation 349 349 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53745 UniProtKB Sequence conflict 50 50 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53745 UniProtKB Sequence conflict 87 87 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53745 UniProtKB Sequence conflict 134 134 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53745 UniProtKB Sequence conflict 206 206 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53745 UniProtKB Sequence conflict 254 267 . . . Note=LNYPPQELWFLDVK->PGTELELRPQFTG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P43563 1 287 +P43563 UniProtKB Chain 1 287 . . . ID=PRO_0000193583;Note=CBK1 kinase activator protein MOB2 +P43563 UniProtKB Modified residue 33 33 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43563 UniProtKB Modified residue 59 59 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43563 UniProtKB Modified residue 76 76 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43563 UniProtKB Turn 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P43563 UniProtKB Helix 122 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P43563 UniProtKB Helix 183 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P43563 UniProtKB Turn 196 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P43563 UniProtKB Helix 211 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P43563 UniProtKB Helix 234 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P43563 UniProtKB Helix 238 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P43563 UniProtKB Helix 243 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P43563 UniProtKB Turn 265 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +P43563 UniProtKB Helix 272 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LQS +##sequence-region P23641 1 311 +P23641 UniProtKB Chain 1 311 . . . ID=PRO_0000090635;Note=Mitochondrial phosphate carrier protein +P23641 UniProtKB Initiator methionine 1 1 . . . Note=Removed%3B alternate;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P23641 UniProtKB Chain 2 311 . . . ID=PRO_0000423225;Note=Mitochondrial phosphate carrier protein%2C N-terminally processed +P23641 UniProtKB Topological domain 1 19 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23641 UniProtKB Transmembrane 20 40 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23641 UniProtKB Topological domain 41 62 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23641 UniProtKB Transmembrane 63 83 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23641 UniProtKB Topological domain 84 115 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23641 UniProtKB Transmembrane 116 136 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23641 UniProtKB Topological domain 137 165 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23641 UniProtKB Transmembrane 166 186 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23641 UniProtKB Topological domain 187 214 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23641 UniProtKB Transmembrane 215 235 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23641 UniProtKB Topological domain 236 253 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23641 UniProtKB Transmembrane 254 274 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23641 UniProtKB Topological domain 275 311 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23641 UniProtKB Repeat 15 100 . . . Note=Solcar 1 +P23641 UniProtKB Repeat 114 197 . . . Note=Solcar 2 +P23641 UniProtKB Repeat 212 297 . . . Note=Solcar 3 +P23641 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine%3B in Mitochondrial phosphate carrier protein%2C N-terminally processed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P23641 UniProtKB Modified residue 4 4 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P23641 UniProtKB Modified residue 145 145 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P23641 UniProtKB Sequence conflict 2 2 . . . Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47083 1 593 +P47083 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P47083 UniProtKB Chain 2 593 . . . ID=PRO_0000121534;Note=U3 small nucleolar RNA-associated protein MPP10 +P47083 UniProtKB Compositional bias 226 229 . . . Note=Poly-Glu +P47083 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P47083 UniProtKB Modified residue 176 176 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P47083 UniProtKB Modified residue 177 177 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P47083 UniProtKB Modified residue 181 181 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q03667 1 156 +Q03667 UniProtKB Transit peptide 1 21 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03667 UniProtKB Chain 22 156 . . . ID=PRO_0000203267;Note=Mitochondrial intermembrane space cysteine motif-containing protein MIX17 +Q03667 UniProtKB Domain 115 156 . . . Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q03667 UniProtKB Motif 118 128 . . . Note=Cx9C motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q03667 UniProtKB Compositional bias 32 36 . . . Note=Poly-Gln +Q03667 UniProtKB Compositional bias 96 99 . . . Note=Poly-Gln +Q03667 UniProtKB Disulfide bond 118 149 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03667 UniProtKB Disulfide bond 128 139 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38162 1 196 +P38162 UniProtKB Chain 1 196 . . . ID=PRO_0000202439;Note=Mitochondrial intermembrane space cysteine motif-containing protein MIX23 +P38162 UniProtKB Motif 99 114 . . . Note=Cx14C motif +P38162 UniProtKB Motif 178 192 . . . Note=Cx13C motif +##sequence-region Q06211 1 1407 +Q06211 UniProtKB Chain 1 1407 . . . ID=PRO_0000257820;Note=E3 ubiquitin-protein ligase linker protein MMS1 +Q06211 UniProtKB Region 1 600 . . . Note=Required for interaction with MMS22 +Q06211 UniProtKB Modified residue 1294 1294 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +##sequence-region Q12205 1 849 +Q12205 UniProtKB Chain 1 849 . . . ID=PRO_0000247229;Note=Putative endoplasmic reticulum mannosidase MNL2 +Q12205 UniProtKB Topological domain 1 12 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12205 UniProtKB Transmembrane 13 32 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12205 UniProtKB Topological domain 33 849 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12205 UniProtKB Glycosylation 45 45 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12205 UniProtKB Disulfide bond 559 598 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32906 +##sequence-region P46985 1 422 +P46985 UniProtKB Chain 1 422 . . . ID=PRO_0000215165;Note=Probable alpha-1%2C6-mannosyltransferase MNN11 +P46985 UniProtKB Topological domain 1 31 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46985 UniProtKB Transmembrane 32 52 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46985 UniProtKB Topological domain 53 422 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46985 UniProtKB Sequence conflict 298 298 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38069 1 597 +P38069 UniProtKB Chain 1 597 . . . ID=PRO_0000065676;Note=Alpha-1%2C2-mannosyltransferase MNN2 +P38069 UniProtKB Topological domain 1 12 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38069 UniProtKB Transmembrane 13 28 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38069 UniProtKB Topological domain 29 597 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38069 UniProtKB Glycosylation 34 34 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38069 UniProtKB Glycosylation 363 363 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38069 UniProtKB Glycosylation 473 473 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38069 UniProtKB Sequence conflict 287 287 . . . Note=T->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53129 1 644 +P53129 UniProtKB Chain 1 644 . . . ID=PRO_0000202744;Note=Vacuolar fusion protein MON1 +P53129 UniProtKB Modified residue 22 22 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53129 UniProtKB Modified residue 71 71 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53129 UniProtKB Sequence conflict 113 113 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53129 UniProtKB Sequence conflict 113 113 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53311 1 146 +P53311 UniProtKB Transit peptide 1 20 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53311 UniProtKB Chain 21 146 . . . ID=PRO_0000212800;Note=Mitochondrial pyruvate carrier 3 +P53311 UniProtKB Transmembrane 23 39 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53311 UniProtKB Transmembrane 55 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53311 UniProtKB Transmembrane 78 94 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CD99 1 609 +P0CD99 UniProtKB Chain 1 609 . . . ID=PRO_0000050424;Note=Alpha-glucosides permease MPH2 +P0CD99 UniProtKB Topological domain 1 106 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CD99 UniProtKB Transmembrane 107 127 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD99 UniProtKB Topological domain 128 142 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CD99 UniProtKB Transmembrane 143 163 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD99 UniProtKB Topological domain 164 178 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CD99 UniProtKB Transmembrane 179 199 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD99 UniProtKB Topological domain 200 200 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CD99 UniProtKB Transmembrane 201 221 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD99 UniProtKB Topological domain 222 234 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CD99 UniProtKB Transmembrane 235 255 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD99 UniProtKB Topological domain 256 270 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CD99 UniProtKB Transmembrane 271 291 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD99 UniProtKB Topological domain 292 363 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CD99 UniProtKB Transmembrane 364 384 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD99 UniProtKB Topological domain 385 397 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CD99 UniProtKB Transmembrane 398 418 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD99 UniProtKB Topological domain 419 426 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CD99 UniProtKB Transmembrane 427 447 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD99 UniProtKB Topological domain 448 459 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CD99 UniProtKB Transmembrane 460 480 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD99 UniProtKB Topological domain 481 492 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CD99 UniProtKB Transmembrane 493 513 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD99 UniProtKB Topological domain 514 525 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CD99 UniProtKB Transmembrane 526 546 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CD99 UniProtKB Topological domain 547 609 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P23748 1 554 +P23748 UniProtKB Chain 1 554 . . . ID=PRO_0000198662;Note=M-phase inducer phosphatase +P23748 UniProtKB Domain 261 373 . . . Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173 +P23748 UniProtKB Active site 320 320 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23748 UniProtKB Sequence conflict 238 239 . . . Note=ND->MT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23748 UniProtKB Sequence conflict 241 248 . . . Note=FPRISPET->SLEFLQKR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23748 UniProtKB Sequence conflict 365 367 . . . Note=FDN->LT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23748 UniProtKB Sequence conflict 475 554 . . . Note=ILSKSSMSSNSNLSTSHMLLMDGLDTPSYFSFEDERGNHQQVSGDEEQDGDFTFVGSDREDLPRPARRSLFPSLETEDKK->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53379 1 596 +P53379 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53379 UniProtKB Propeptide 23 65 . . . ID=PRO_0000025835;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53379 UniProtKB Chain 66 575 . . . ID=PRO_0000025836;Note=Aspartic proteinase MKC7 +P53379 UniProtKB Propeptide 576 596 . . . ID=PRO_0000025837;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53379 UniProtKB Domain 81 468 . . . Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103 +P53379 UniProtKB Compositional bias 532 536 . . . Note=Poly-Ser +P53379 UniProtKB Compositional bias 567 570 . . . Note=Poly-Ser +P53379 UniProtKB Active site 99 99 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +P53379 UniProtKB Active site 360 360 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +P53379 UniProtKB Lipidation 575 575 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53379 UniProtKB Glycosylation 180 180 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53379 UniProtKB Glycosylation 190 190 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53379 UniProtKB Glycosylation 219 219 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53379 UniProtKB Glycosylation 229 229 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53379 UniProtKB Glycosylation 232 232 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53379 UniProtKB Glycosylation 286 286 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53379 UniProtKB Glycosylation 346 346 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53379 UniProtKB Glycosylation 471 471 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53379 UniProtKB Glycosylation 517 517 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53379 UniProtKB Sequence conflict 546 546 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53379 UniProtKB Sequence conflict 571 571 . . . Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06164 1 1454 +Q06164 UniProtKB Chain 1 1454 . . . ID=PRO_0000257821;Note=E3 ubiquitin-protein ligase substrate receptor MMS22 +Q06164 UniProtKB Region 1201 1454 . . . Note=Required for interaction with MMS1 +##sequence-region P40577 1 368 +P40577 UniProtKB Chain 1 368 . . . ID=PRO_0000096523;Note=Anaphase-promoting complex subunit MND2 +P40577 UniProtKB Modified residue 293 293 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P39106 1 762 +P39106 UniProtKB Chain 1 762 . . . ID=PRO_0000080558;Note=Alpha-1%2C3-mannosyltransferase MNN1 +P39106 UniProtKB Topological domain 1 16 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39106 UniProtKB Transmembrane 17 33 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39106 UniProtKB Topological domain 34 762 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39106 UniProtKB Glycosylation 50 50 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39106 UniProtKB Glycosylation 225 225 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39106 UniProtKB Glycosylation 254 254 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39106 UniProtKB Glycosylation 383 383 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39106 UniProtKB Sequence conflict 338 338 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36044 1 1178 +P36044 UniProtKB Chain 1 1178 . . . ID=PRO_0000096525;Note=Protein MNN4 +P36044 UniProtKB Topological domain 1 27 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36044 UniProtKB Transmembrane 28 48 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36044 UniProtKB Topological domain 49 1178 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36044 UniProtKB Repeat 1042 1049 . . . Note=1 +P36044 UniProtKB Repeat 1050 1057 . . . Note=2 +P36044 UniProtKB Repeat 1058 1065 . . . Note=3 +P36044 UniProtKB Repeat 1066 1073 . . . Note=4 +P36044 UniProtKB Repeat 1074 1081 . . . Note=5 +P36044 UniProtKB Repeat 1082 1089 . . . Note=6 +P36044 UniProtKB Repeat 1090 1097 . . . Note=7%3B approximate +P36044 UniProtKB Repeat 1098 1105 . . . Note=8 +P36044 UniProtKB Repeat 1106 1113 . . . Note=9%3B approximate +P36044 UniProtKB Repeat 1114 1121 . . . Note=10%3B approximate +P36044 UniProtKB Repeat 1122 1129 . . . Note=11%3B approximate +P36044 UniProtKB Repeat 1130 1137 . . . Note=12 +P36044 UniProtKB Repeat 1138 1144 . . . Note=13%3B approximate +P36044 UniProtKB Repeat 1145 1152 . . . Note=14%3B approximate +P36044 UniProtKB Repeat 1153 1160 . . . Note=15%3B approximate +P36044 UniProtKB Repeat 1161 1168 . . . Note=16%3B approximate +P36044 UniProtKB Repeat 1169 1174 . . . Note=17%3B truncated +P36044 UniProtKB Region 1042 1174 . . . Note=17 X 8 AA tandem repeats of K-K-K-K-E-E-E-E +P36044 UniProtKB Compositional bias 37 40 . . . Note=Poly-Ile +P36044 UniProtKB Compositional bias 1032 1174 . . . Note=Arg/Glu/Lys-rich (highly charged) +P36044 UniProtKB Compositional bias 1042 1045 . . . Note=Poly-Lys +P36044 UniProtKB Compositional bias 1046 1049 . . . Note=Poly-Glu +P36044 UniProtKB Compositional bias 1050 1053 . . . Note=Poly-Lys +P36044 UniProtKB Compositional bias 1054 1057 . . . Note=Poly-Glu +P36044 UniProtKB Compositional bias 1058 1061 . . . Note=Poly-Lys +P36044 UniProtKB Compositional bias 1062 1065 . . . Note=Poly-Glu +P36044 UniProtKB Compositional bias 1066 1069 . . . Note=Poly-Lys +P36044 UniProtKB Compositional bias 1070 1073 . . . Note=Poly-Glu +P36044 UniProtKB Compositional bias 1074 1077 . . . Note=Poly-Lys +P36044 UniProtKB Compositional bias 1078 1081 . . . Note=Poly-Glu +P36044 UniProtKB Compositional bias 1082 1085 . . . Note=Poly-Lys +P36044 UniProtKB Compositional bias 1086 1089 . . . Note=Poly-Glu +P36044 UniProtKB Compositional bias 1094 1097 . . . Note=Poly-Glu +P36044 UniProtKB Compositional bias 1098 1101 . . . Note=Poly-Lys +P36044 UniProtKB Compositional bias 1102 1105 . . . Note=Poly-Glu +P36044 UniProtKB Compositional bias 1134 1137 . . . Note=Poly-Glu +P36044 UniProtKB Compositional bias 1157 1160 . . . Note=Poly-Glu +P36044 UniProtKB Compositional bias 1165 1168 . . . Note=Poly-Glu +##sequence-region P35724 1 969 +P35724 UniProtKB Chain 1 969 . . . ID=PRO_0000201537;Note=Manganese resistance protein MNR2 +P35724 UniProtKB Topological domain 1 912 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35724 UniProtKB Transmembrane 913 933 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35724 UniProtKB Topological domain 934 941 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35724 UniProtKB Transmembrane 942 962 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35724 UniProtKB Topological domain 963 969 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35724 UniProtKB Modified residue 114 114 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P35724 UniProtKB Modified residue 175 175 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P35724 UniProtKB Modified residue 177 177 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35724 UniProtKB Modified residue 182 182 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35724 UniProtKB Modified residue 383 383 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35724 UniProtKB Modified residue 571 571 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P35724 UniProtKB Modified residue 576 576 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P35724 UniProtKB Modified residue 582 582 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P53059 1 558 +P53059 UniProtKB Chain 1 558 . . . ID=PRO_0000080559;Note=Alpha-1%2C3-mannosyltransferase MNT2 +P53059 UniProtKB Topological domain 1 6 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53059 UniProtKB Transmembrane 7 27 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53059 UniProtKB Topological domain 28 558 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53059 UniProtKB Glycosylation 187 187 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53157 1 130 +P53157 UniProtKB Chain 1 130 . . . ID=PRO_0000212805;Note=Mitochondrial pyruvate carrier 1 +P53157 UniProtKB Transmembrane 23 45 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53157 UniProtKB Transmembrane 55 77 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12411 1 609 +Q12411 UniProtKB Chain 1 609 . . . ID=PRO_0000096556;Note=Sporulation-specific protein 21 +Q12411 UniProtKB Coiled coil 283 342 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12411 UniProtKB Coiled coil 357 393 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12411 UniProtKB Coiled coil 424 483 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12411 UniProtKB Compositional bias 65 162 . . . Note=Ser-rich +##sequence-region Q01926 1 470 +Q01926 UniProtKB Transit peptide 1 32 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01926 UniProtKB Chain 33 470 . . . ID=PRO_0000021753;Note=Magnesium transporter MRS2%2C mitochondrial +Q01926 UniProtKB Topological domain 33 314 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01926 UniProtKB Transmembrane 315 333 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01926 UniProtKB Topological domain 334 344 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01926 UniProtKB Transmembrane 345 361 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01926 UniProtKB Topological domain 362 470 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01926 UniProtKB Motif 332 335 . . . Note=YGMN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01926 UniProtKB Mutagenesis 97 97 . . . Note=No effect on Mg(2+) import. D->A%2CF%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23999289;Dbxref=PMID:23999289 +Q01926 UniProtKB Mutagenesis 309 309 . . . Note=Increases Mg(2+) import into mitochondria. M->E%2CG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23999289;Dbxref=PMID:23999289 +Q01926 UniProtKB Mutagenesis 309 309 . . . Note=Decreases Mg(2+) import into mitochondria. M->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23999289;Dbxref=PMID:23999289 +Q01926 UniProtKB Mutagenesis 315 315 . . . Note=No effect on Mg(2+) import. V->E%2CF%2CG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23999289;Dbxref=PMID:23999289 +Q01926 UniProtKB Sequence conflict 371 371 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01926 UniProtKB Sequence conflict 371 371 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01926 UniProtKB Sequence conflict 448 448 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01926 UniProtKB Sequence conflict 448 448 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01926 UniProtKB Helix 59 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG +Q01926 UniProtKB Beta strand 63 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG +Q01926 UniProtKB Beta strand 75 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG +Q01926 UniProtKB Helix 84 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG +Q01926 UniProtKB Helix 95 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG +Q01926 UniProtKB Beta strand 111 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG +Q01926 UniProtKB Beta strand 119 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG +Q01926 UniProtKB Beta strand 126 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG +Q01926 UniProtKB Beta strand 135 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG +Q01926 UniProtKB Helix 143 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG +Q01926 UniProtKB Helix 170 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG +Q01926 UniProtKB Helix 210 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG +Q01926 UniProtKB Helix 244 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG +Q01926 UniProtKB Helix 263 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RKG +##sequence-region P47084 1 519 +P47084 UniProtKB Transit peptide 1 35 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47084 UniProtKB Chain 36 519 . . . ID=PRO_0000203081;Note=MIOREX complex component 12 +##sequence-region P53869 1 86 +P53869 UniProtKB Chain 1 86 . . . ID=PRO_0000203390;Note=MIOREX complex component 7 +##sequence-region Q07980 1 695 +Q07980 UniProtKB Chain 1 695 . . . ID=PRO_0000245569;Note=DNA mismatch repair protein MLH2 +##sequence-region P38257 1 691 +P38257 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38257 UniProtKB Chain 2 691 . . . ID=PRO_0000096516;Note=Crossover junction endonuclease MMS4 +P38257 UniProtKB Region 598 691 . . . Note=Interaction with MUS81 +P38257 UniProtKB Coiled coil 364 391 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38257 UniProtKB Coiled coil 507 529 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38257 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38257 UniProtKB Modified residue 48 48 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38257 UniProtKB Modified residue 49 49 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38257 UniProtKB Modified residue 61 61 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38257 UniProtKB Mutagenesis 173 173 . . . Note=In allele MMS4-1%3B loss of activity. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9604884;Dbxref=PMID:9604884 +##sequence-region P40484 1 314 +P40484 UniProtKB Chain 1 314 . . . ID=PRO_0000193582;Note=DBF2 kinase activator protein MOB1 +P40484 UniProtKB Compositional bias 48 55 . . . Note=Poly-Asn +P40484 UniProtKB Metal binding 179 179 . . . Note=Zinc +P40484 UniProtKB Metal binding 184 184 . . . Note=Zinc +P40484 UniProtKB Metal binding 261 261 . . . Note=Zinc +P40484 UniProtKB Metal binding 266 266 . . . Note=Zinc +P40484 UniProtKB Modified residue 34 34 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40484 UniProtKB Modified residue 36 36 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40484 UniProtKB Modified residue 80 80 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40484 UniProtKB Modified residue 229 229 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40484 UniProtKB Mutagenesis 105 105 . . . Note=No effect. T->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16934835;Dbxref=PMID:16934835 +P40484 UniProtKB Mutagenesis 107 107 . . . Note=No effect. S->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16934835;Dbxref=PMID:16934835 +P40484 UniProtKB Beta strand 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN +P40484 UniProtKB Helix 127 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN +P40484 UniProtKB Helix 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN +P40484 UniProtKB Helix 153 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN +P40484 UniProtKB Helix 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN +P40484 UniProtKB Turn 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN +P40484 UniProtKB Beta strand 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN +P40484 UniProtKB Beta strand 193 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN +P40484 UniProtKB Helix 210 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN +P40484 UniProtKB Turn 228 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN +P40484 UniProtKB Helix 243 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN +P40484 UniProtKB Helix 248 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN +P40484 UniProtKB Helix 267 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN +P40484 UniProtKB Helix 276 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN +P40484 UniProtKB Helix 298 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN +P40484 UniProtKB Helix 305 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJN +##sequence-region P54785 1 490 +P54785 UniProtKB Chain 1 490 . . . ID=PRO_0000046807;Note=Transcriptional activator/repressor MOT3 +P54785 UniProtKB Zinc finger 346 368 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P54785 UniProtKB Zinc finger 374 397 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P54785 UniProtKB Region 98 295 . . . Note=Prion domain (PrD) +P54785 UniProtKB Compositional bias 8 35 . . . Note=Poly-Gln +P54785 UniProtKB Compositional bias 98 104 . . . Note=Poly-Asn +P54785 UniProtKB Compositional bias 143 157 . . . Note=Poly-Asn +P54785 UniProtKB Compositional bias 173 177 . . . Note=Poly-Ala +P54785 UniProtKB Compositional bias 240 245 . . . Note=Poly-His +P54785 UniProtKB Compositional bias 417 420 . . . Note=Poly-Ser +P54785 UniProtKB Compositional bias 421 433 . . . Note=Poly-Asn +P54785 UniProtKB Compositional bias 441 450 . . . Note=Poly-Ala +P54785 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P41940 1 361 +P41940 UniProtKB Chain 1 361 . . . ID=PRO_0000068741;Note=Mannose-1-phosphate guanyltransferase +P41940 UniProtKB Modified residue 153 153 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P41940 UniProtKB Cross-link 244 244 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P41940 UniProtKB Sequence conflict 50 50 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40562 1 993 +P40562 UniProtKB Chain 1 993 . . . ID=PRO_0000055193;Note=ATP-dependent DNA helicase MPH1 +P40562 UniProtKB Domain 94 261 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P40562 UniProtKB Domain 507 655 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P40562 UniProtKB Nucleotide binding 107 114 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P40562 UniProtKB Motif 209 212 . . . Note=DEAH box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +##sequence-region P0CE00 1 602 +P0CE00 UniProtKB Chain 1 602 . . . ID=PRO_0000391710;Note=Alpha-glucosides permease MPH3 +P0CE00 UniProtKB Topological domain 1 106 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Transmembrane 107 127 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Topological domain 128 142 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Transmembrane 143 163 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Topological domain 164 178 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Transmembrane 179 199 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Topological domain 200 200 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Transmembrane 201 221 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Topological domain 222 234 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Transmembrane 235 255 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Topological domain 256 270 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Transmembrane 271 291 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Topological domain 292 363 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Transmembrane 364 384 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Topological domain 385 397 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Transmembrane 398 418 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Topological domain 419 426 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Transmembrane 427 447 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Topological domain 448 459 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Transmembrane 460 480 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Topological domain 481 492 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Transmembrane 493 513 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Topological domain 514 525 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Transmembrane 526 546 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE00 UniProtKB Topological domain 547 602 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53725 1 186 +P53725 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53725 UniProtKB Chain 2 186 . . . ID=PRO_0000203474;Note=M-phase phosphoprotein 6 homolog +P53725 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53725 UniProtKB Modified residue 42 42 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53725 UniProtKB Modified residue 150 150 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P53159 1 387 +P53159 UniProtKB Chain 1 387 . . . ID=PRO_0000202760;Note=Monopolar spindle protein 2 +P53159 UniProtKB Transmembrane 311 327 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53159 UniProtKB Coiled coil 117 232 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08471 1 629 +Q08471 UniProtKB Chain 1 629 . . . ID=PRO_0000237651;Note=G1-specific transcription factors activator MSA1 +Q08471 UniProtKB Compositional bias 317 333 . . . Note=Asn-rich +Q08471 UniProtKB Compositional bias 446 475 . . . Note=Gln-rich +Q08471 UniProtKB Modified residue 268 268 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P08593 1 268 +P08593 UniProtKB Chain 1 268 . . . ID=PRO_0000096602;Note=Protein MSS18 +##sequence-region P40990 1 351 +P40990 UniProtKB Repeat 155 188 . . . Note=TPR 1 +P40990 UniProtKB Repeat 260 294 . . . Note=TPR 2 +P40990 UniProtKB Sequence conflict 286 351 . . . Note=TGMEIMDLECFFGFFDCCVKEENFKGARDCLESVKKLGNDKDKKTMINVFLESRKDSIKLLDKARL->RVWNMT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07938 1 337 +Q07938 UniProtKB Chain 1 337 . . . ID=PRO_0000184556;Note=S-methyl-5'-thioadenosine phosphorylase +Q07938 UniProtKB Region 88 89 . . . Note=Phosphate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03155 +Q07938 UniProtKB Region 121 122 . . . Note=Phosphate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03155 +Q07938 UniProtKB Region 254 256 . . . Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03155 +Q07938 UniProtKB Binding site 41 41 . . . Note=Phosphate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03155 +Q07938 UniProtKB Binding site 230 230 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03155 +Q07938 UniProtKB Binding site 231 231 . . . Note=Phosphate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03155 +Q07938 UniProtKB Site 212 212 . . . Note=Important for substrate specificity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03155 +Q07938 UniProtKB Site 267 267 . . . Note=Important for substrate specificity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03155 +Q07938 UniProtKB Sequence conflict 55 55 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q07938 UniProtKB Sequence conflict 157 157 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03218 1 510 +Q03218 UniProtKB Transmembrane 165 185 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03218 UniProtKB Transmembrane 194 214 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03218 UniProtKB Transmembrane 241 261 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03218 UniProtKB Transmembrane 286 306 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03218 UniProtKB Transmembrane 333 353 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03218 UniProtKB Transmembrane 356 376 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03218 UniProtKB Sequence conflict 408 408 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08970 1 484 +Q08970 UniProtKB Transit peptide 1 56 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08970 UniProtKB Chain 57 484 . . . ID=PRO_0000255968;Note=Mitochondrial metal transporter 2 +Q08970 UniProtKB Transmembrane 132 152 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08970 UniProtKB Transmembrane 158 178 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08970 UniProtKB Transmembrane 209 229 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08970 UniProtKB Transmembrane 256 276 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08970 UniProtKB Transmembrane 316 336 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08970 UniProtKB Sequence conflict 17 17 . . . Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P07884 1 428 +P07884 UniProtKB Chain 1 428 . . . ID=PRO_0000019025;Note=tRNA dimethylallyltransferase%2C mitochondrial +P07884 UniProtKB Nucleotide binding 21 28 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07884 UniProtKB Zinc finger 373 409 . . . Note=Matrin-type +P07884 UniProtKB Region 23 28 . . . Note=Substrate binding +P07884 UniProtKB Region 46 49 . . . Note=Interaction with substrate tRNA +P07884 UniProtKB Region 170 174 . . . Note=Interaction with substrate tRNA +P07884 UniProtKB Region 199 207 . . . Note=Core aggregation region +P07884 UniProtKB Region 210 232 . . . Note=Interaction with isopentenylpyrophosphate transferase +P07884 UniProtKB Region 256 258 . . . Note=Interaction with substrate tRNA +P07884 UniProtKB Region 284 302 . . . Note=Interaction with substrate tRNA +P07884 UniProtKB Region 294 301 . . . Note=Interaction with substrate tRNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07884 UniProtKB Site 112 112 . . . Note=Interaction with substrate tRNA +P07884 UniProtKB Site 193 193 . . . Note=Interaction with substrate tRNA +P07884 UniProtKB Alternative sequence 1 11 . . . ID=VSP_018811;Note=In isoform II. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07884 UniProtKB Sequence conflict 313 313 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07884 UniProtKB Sequence conflict 375 375 . . . Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07884 UniProtKB Beta strand 15 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Beta strand 23 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 27 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Beta strand 40 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Turn 47 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Beta strand 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Turn 55 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Turn 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Beta strand 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 85 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Turn 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Beta strand 105 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 113 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Beta strand 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 135 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Beta strand 144 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 149 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 158 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 169 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 186 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Beta strand 198 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 210 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 229 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Turn 241 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 247 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 253 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 261 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 278 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 304 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Turn 308 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Beta strand 312 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Turn 320 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Turn 324 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 328 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 351 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 359 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 363 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Beta strand 372 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Beta strand 385 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 391 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +P07884 UniProtKB Helix 401 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EPH +##sequence-region P38191 1 138 +P38191 UniProtKB Chain 1 138 . . . ID=PRO_0000212410;Note=Protein yippee-like MOH1 +P38191 UniProtKB Domain 41 138 . . . Note=Yippee;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01128 +P38191 UniProtKB Metal binding 45 45 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01128 +P38191 UniProtKB Metal binding 48 48 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01128 +P38191 UniProtKB Metal binding 101 101 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01128 +P38191 UniProtKB Metal binding 104 104 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01128 +##sequence-region P32333 1 1867 +P32333 UniProtKB Chain 1 1867 . . . ID=PRO_0000074335;Note=TATA-binding protein-associated factor MOT1 +P32333 UniProtKB Repeat 289 326 . . . Note=HEAT 1 +P32333 UniProtKB Repeat 445 482 . . . Note=HEAT 2 +P32333 UniProtKB Repeat 541 578 . . . Note=HEAT 3 +P32333 UniProtKB Repeat 1108 1145 . . . Note=HEAT 4 +P32333 UniProtKB Repeat 1188 1225 . . . Note=HEAT 5 +P32333 UniProtKB Domain 1284 1457 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P32333 UniProtKB Repeat 1495 1537 . . . Note=HEAT 6 +P32333 UniProtKB Domain 1639 1787 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P32333 UniProtKB Nucleotide binding 1297 1304 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P32333 UniProtKB Motif 195 211 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32333 UniProtKB Motif 1408 1411 . . . Note=DEGH box +P32333 UniProtKB Modified residue 93 93 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32333 UniProtKB Modified residue 677 677 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P32333 UniProtKB Mutagenesis 1226 1226 . . . Note=Temperature sensitive in mot1-301. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16387868;Dbxref=PMID:16387868 +P32333 UniProtKB Mutagenesis 1303 1303 . . . Note=No ATPase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11880621;Dbxref=PMID:11880621 +##sequence-region P32829 1 692 +P32829 UniProtKB Chain 1 692 . . . ID=PRO_0000138680;Note=Double-strand break repair protein MRE11 +P32829 UniProtKB Active site 125 125 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32829 UniProtKB Natural variant 380 380 . . . Note=In strain: SK1. P->S +P32829 UniProtKB Natural variant 659 659 . . . Note=In strain: SK1. P->S +##sequence-region P53166 1 561 +P53166 UniProtKB Transit peptide 1 26 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53166 UniProtKB Chain 27 561 . . . ID=PRO_0000041929;Note=ATP-dependent RNA helicase MRH4%2C mitochondrial +P53166 UniProtKB Domain 151 339 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P53166 UniProtKB Domain 370 561 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P53166 UniProtKB Nucleotide binding 164 171 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P53166 UniProtKB Motif 117 141 . . . Note=Q motif +P53166 UniProtKB Motif 287 290 . . . Note=DEAD box +P53166 UniProtKB Natural variant 67 67 . . . Note=In strain: DBY947. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12702275;Dbxref=PMID:12702275 +P53166 UniProtKB Natural variant 438 438 . . . Note=In strain: DBY947. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12702275;Dbxref=PMID:12702275 +##sequence-region P40185 1 145 +P40185 UniProtKB Transit peptide 1 17 . . . Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11003673,ECO:0000269|Ref.5;Dbxref=PMID:11003673 +P40185 UniProtKB Chain 18 145 . . . ID=PRO_0000036209;Note=Protein MMF1%2C mitochondrial +P40185 UniProtKB Beta strand 21 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW +P40185 UniProtKB Beta strand 38 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW +P40185 UniProtKB Beta strand 45 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW +P40185 UniProtKB Helix 65 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW +P40185 UniProtKB Helix 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW +P40185 UniProtKB Beta strand 90 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW +P40185 UniProtKB Helix 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW +P40185 UniProtKB Helix 103 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW +P40185 UniProtKB Beta strand 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW +P40185 UniProtKB Beta strand 120 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW +P40185 UniProtKB Helix 130 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW +P40185 UniProtKB Beta strand 134 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QUW +##sequence-region P50108 1 393 +P50108 UniProtKB Chain 1 393 . . . ID=PRO_0000215164;Note=Probable alpha-1%2C6-mannosyltransferase MNN10 +P50108 UniProtKB Topological domain 1 52 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50108 UniProtKB Transmembrane 53 73 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50108 UniProtKB Topological domain 74 393 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50108 UniProtKB Sequence conflict 238 238 . . . Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53163 1 194 +P53163 UniProtKB Transit peptide 1 33 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15221522;Dbxref=PMID:15221522 +P53163 UniProtKB Chain 34 194 . . . ID=PRO_0000030460;Note=54S ribosomal protein L12%2C mitochondrial +P53163 UniProtKB Glycosylation 34 34 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53163 UniProtKB Sequence conflict 34 34 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32906 1 549 +P32906 UniProtKB Chain 1 549 . . . ID=PRO_0000210319;Note=Endoplasmic reticulum mannosyl-oligosaccharide 1%2C2-alpha-mannosidase +P32906 UniProtKB Topological domain 1 4 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32906 UniProtKB Transmembrane 5 24 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32906 UniProtKB Topological domain 25 354 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32906 UniProtKB Active site 399 399 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31723 +P32906 UniProtKB Metal binding 525 525 . . . Note=Calcium;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10675327;Dbxref=PMID:10675327 +P32906 UniProtKB Glycosylation 96 96 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6I +P32906 UniProtKB Glycosylation 155 155 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6I +P32906 UniProtKB Glycosylation 224 224 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6I +P32906 UniProtKB Disulfide bond 340 385 . . . Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1DL2,ECO:0000244|PDB:1G6I,ECO:0000269|PubMed:10675327;Dbxref=PMID:10675327 +P32906 UniProtKB Disulfide bond 468 471 . . . Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1DL2,ECO:0000244|PDB:1G6I,ECO:0000269|PubMed:10675327;Dbxref=PMID:10675327 +P32906 UniProtKB Natural variant 40 40 . . . Note=D->Y +P32906 UniProtKB Natural variant 376 376 . . . Note=D->L +P32906 UniProtKB Helix 35 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Beta strand 61 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Turn 65 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Beta strand 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 84 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Beta strand 99 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 102 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Beta strand 125 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 130 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 156 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 172 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Beta strand 176 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Beta strand 184 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Turn 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 205 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 212 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 225 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 235 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 244 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Beta strand 253 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Turn 258 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Turn 272 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 275 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 291 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Beta strand 309 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Turn 313 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Beta strand 318 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Turn 324 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6I +P32906 UniProtKB Beta strand 334 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 337 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 342 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 356 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 372 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Beta strand 399 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Beta strand 417 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 425 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 435 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 451 467 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Beta strand 468 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Turn 474 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Beta strand 482 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 498 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 504 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Beta strand 520 523 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Beta strand 529 531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +P32906 UniProtKB Helix 535 540 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DL2 +##sequence-region P47123 1 218 +P47123 UniProtKB Chain 1 218 . . . ID=PRO_0000215203;Note=Nuclear import protein MOG1 +P47123 UniProtKB Beta strand 34 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Helix 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Beta strand 43 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Beta strand 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Helix 54 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Beta strand 64 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Beta strand 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Beta strand 86 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Helix 100 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Helix 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Beta strand 117 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Turn 130 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Beta strand 133 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Beta strand 154 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Helix 164 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Beta strand 168 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Helix 180 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Turn 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Helix 193 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Beta strand 210 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +P47123 UniProtKB Helix 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EQ6 +##sequence-region P53583 1 542 +P53583 UniProtKB Chain 1 542 . . . ID=PRO_0000096549;Note=Protein MPA43 +P53583 UniProtKB Sequence conflict 46 53 . . . Note=KKSWKFWQ->RSHGNLA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38857 1 129 +P38857 UniProtKB Chain 1 129 . . . ID=PRO_0000212801;Note=Mitochondrial pyruvate carrier 2 +P38857 UniProtKB Transmembrane 23 39 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38857 UniProtKB Transmembrane 55 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38857 UniProtKB Transmembrane 75 91 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12404 1 318 +Q12404 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12404 UniProtKB Chain 22 318 . . . ID=PRO_0000034220;Note=Protein disulfide-isomerase MPD1 +Q12404 UniProtKB Domain 22 158 . . . Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +Q12404 UniProtKB Motif 315 318 . . . Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10138 +Q12404 UniProtKB Glycosylation 47 47 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12404 UniProtKB Glycosylation 307 307 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12404 UniProtKB Disulfide bond 59 62 . . . Note=Redox-active;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +Q12404 UniProtKB Helix 36 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Beta strand 45 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Beta strand 50 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Helix 60 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Helix 66 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Turn 76 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Beta strand 80 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Turn 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Helix 93 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Beta strand 103 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Beta strand 132 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Helix 142 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Beta strand 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Helix 163 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Helix 166 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Beta strand 174 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Helix 189 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Beta strand 202 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Helix 209 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Helix 226 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Beta strand 246 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Turn 252 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Beta strand 256 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Helix 267 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Beta strand 283 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +Q12404 UniProtKB Helix 289 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ED3 +##sequence-region P35728 1 441 +P35728 UniProtKB Chain 1 441 . . . ID=PRO_0000076265;Note=Protein MPE1 +P35728 UniProtKB Domain 5 78 . . . Note=DWNN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00612 +P35728 UniProtKB Zinc finger 180 197 . . . Note=CCHC-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +P35728 UniProtKB Modified residue 221 221 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P40364 1 252 +P40364 UniProtKB Chain 1 252 . . . ID=PRO_0000203056;Note=Mitochondrial peculiar membrane protein 1 +##sequence-region P54199 1 764 +P54199 UniProtKB Chain 1 764 . . . ID=PRO_0000086391;Note=Serine/threonine-protein kinase MPS1 +P54199 UniProtKB Domain 440 720 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P54199 UniProtKB Nucleotide binding 446 454 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P54199 UniProtKB Compositional bias 273 282 . . . Note=Poly-Ser +P54199 UniProtKB Compositional bias 309 315 . . . Note=Poly-Ser +P54199 UniProtKB Active site 563 563 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P54199 UniProtKB Binding site 468 468 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P54199 UniProtKB Mutagenesis 580 580 . . . Note=Loss of activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7737118;Dbxref=PMID:7737118 +P54199 UniProtKB Sequence conflict 146 146 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54199 UniProtKB Sequence conflict 211 213 . . . Note=TKR->RRE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54199 UniProtKB Sequence conflict 211 213 . . . Note=TKR->RRE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47069 1 682 +P47069 UniProtKB Chain 1 682 . . . ID=PRO_0000076266;Note=Spindle pole body assembly component MPS3 +P47069 UniProtKB Topological domain 1 154 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47069 UniProtKB Transmembrane 155 175 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47069 UniProtKB Topological domain 176 682 . . . Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47069 UniProtKB Domain 427 616 . . . Note=SUN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00802 +P47069 UniProtKB Nucleotide binding 187 194 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47069 UniProtKB Region 171 682 . . . Note=Interaction with CDC31;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12486115;Dbxref=PMID:12486115 +P47069 UniProtKB Region 431 650 . . . Note=Interaction with JEM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12493774;Dbxref=PMID:12493774 +P47069 UniProtKB Coiled coil 241 273 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47069 UniProtKB Compositional bias 55 129 . . . Note=Asp-rich +P47069 UniProtKB Compositional bias 391 429 . . . Note=Gln-rich +P47069 UniProtKB Mutagenesis 465 465 . . . Note=Lethal%3B when associated with E-466. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 466 466 . . . Note=Lethal%3B when associated with E-465. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 472 472 . . . Note=In mps3-1%3B defective in spindle pole body assembly and duplication. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12486115;Dbxref=PMID:12486115 +P47069 UniProtKB Mutagenesis 476 476 . . . Note=Lethal. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 477 477 . . . Note=Defective in spindle pole body duplication at 37 degrees Celsius. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 487 487 . . . Note=Defective in spindle pole body duplication at 37 degrees Celsius. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 489 489 . . . Note=Lethal. I->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 494 494 . . . Note=Lethal%3B when associated with A-495%3B A-496%3B A-497 and A-498. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 495 495 . . . Note=Lethal%3B when associated with A-494%3B A-496%3B A-497 and A-498. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 496 496 . . . Note=Lethal%3B when associated with A-494%3B A-495%3B A-497 and A-498. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 497 497 . . . Note=Lethal%3B when associated with A-494%3B A-495%3B A-496 and A-498. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 498 498 . . . Note=Lethal%3B when associated with A-494%3B A-495%3B A-496 and A-497. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 500 500 . . . Note=Lethal. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 502 502 . . . Note=Defective in spindle pole body duplication at 37 degrees Celsius. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 504 504 . . . Note=Lethal. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 512 512 . . . Note=Lethal. H->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 517 517 . . . Note=Lethal. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 523 523 . . . Note=Lethal. L->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 540 540 . . . Note=Defective in spindle pole body duplication at 37 degrees Celsius. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 572 572 . . . Note=Defective in spindle pole body duplication at 37 degrees Celsius%3B when associated with L-573. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 573 573 . . . Note=Defective in spindle pole body duplication at 37 degrees Celsius%3B when associated with L-572. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 590 590 . . . Note=Lethal. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 592 592 . . . Note=Defective in spindle pole body duplication at 37 degrees Celsius. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 593 593 . . . Note=Lethal%3B when associated with D-594. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 594 594 . . . Note=Lethal%3B when associated with A-593. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 597 597 . . . Note=In nep98-7%3B defective in spindle organization during nuclear division and in G2/M progression. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12493774;Dbxref=PMID:12493774 +P47069 UniProtKB Mutagenesis 599 599 . . . Note=Lethal. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 604 604 . . . Note=Lethal. I->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 605 605 . . . Note=Lethal%3B when associated with Q-606. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 606 606 . . . Note=Lethal%3B when associated with C-605. L->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 611 611 . . . Note=Lethal. I->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +P47069 UniProtKB Mutagenesis 613 613 . . . Note=Lethal. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923827;Dbxref=PMID:16923827 +##sequence-region P39016 1 859 +P39016 UniProtKB Chain 1 859 . . . ID=PRO_0000075923;Note=Suppressor protein MPT5 +P39016 UniProtKB Domain 188 596 . . . Note=PUM-HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00318 +P39016 UniProtKB Repeat 209 247 . . . Note=Pumilio 1 +P39016 UniProtKB Repeat 248 283 . . . Note=Pumilio 2 +P39016 UniProtKB Repeat 284 320 . . . Note=Pumilio 3 +P39016 UniProtKB Repeat 325 362 . . . Note=Pumilio 4 +P39016 UniProtKB Repeat 363 400 . . . Note=Pumilio 5 +P39016 UniProtKB Repeat 401 438 . . . Note=Pumilio 6 +P39016 UniProtKB Repeat 439 474 . . . Note=Pumilio 7 +P39016 UniProtKB Repeat 503 539 . . . Note=Pumilio 8 +P39016 UniProtKB Compositional bias 647 653 . . . Note=Poly-Asn +P39016 UniProtKB Modified residue 662 662 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P39016 UniProtKB Modified residue 834 834 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39016 UniProtKB Modified residue 838 838 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39016 UniProtKB Helix 205 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 210 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 215 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 222 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Turn 235 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 238 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 250 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 253 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 262 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Turn 270 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 275 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 286 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 289 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 298 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 312 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Turn 324 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 329 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 341 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 354 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 358 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 369 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 379 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 392 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 406 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Turn 409 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 415 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 426 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 429 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 441 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 444 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 453 473 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 488 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 509 512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 518 526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 528 530 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 532 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 554 575 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Helix 576 579 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +P39016 UniProtKB Beta strand 580 582 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZV +P39016 UniProtKB Helix 585 598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5BZ1 +##sequence-region P25336 1 1018 +P25336 UniProtKB Chain 1 1018 . . . ID=PRO_0000115195;Note=DNA mismatch repair protein MSH3 +P25336 UniProtKB Nucleotide binding 791 798 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25336 UniProtKB Region 126 256 . . . Note=Mispair-binding domain +P25336 UniProtKB Motif 4 11 . . . Note=PIP box +P25336 UniProtKB Mutagenesis 4 4 . . . Note=Partially functional in a mismatch repair assay%3B when associated with 10-AA-11. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11005803;Dbxref=PMID:11005803 +P25336 UniProtKB Mutagenesis 10 11 . . . Note=Partially functional in a mismatch repair assay%3B when associated with A-4. FF->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11005803;Dbxref=PMID:11005803 +P25336 UniProtKB Mutagenesis 158 158 . . . Note=Alters DNA-binding activity and impairs MSH2-MSH3-mediated DNA mismatch repair%3B when associated with ALA-160. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17157869;Dbxref=PMID:17157869 +P25336 UniProtKB Mutagenesis 160 160 . . . Note=Alters DNA-binding activity and impairs MSH2-MSH3-mediated DNA mismatch repair%3B when associated with ALA-158. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17157869;Dbxref=PMID:17157869 +P25336 UniProtKB Mutagenesis 203 203 . . . Note=No effect. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17157869;Dbxref=PMID:17157869 +P25336 UniProtKB Mutagenesis 226 226 . . . Note=No effect. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17157869;Dbxref=PMID:17157869 +P25336 UniProtKB Mutagenesis 247 247 . . . Note=Impairs MSH2-MSH3-mediated DNA mismatch repair. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17157869;Dbxref=PMID:17157869 +P25336 UniProtKB Mutagenesis 796 796 . . . Note=Defective in MMR and in NHTR. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644 +##sequence-region P53045 1 309 +P53045 UniProtKB Chain 1 309 . . . ID=PRO_0000117039;Note=Methylsterol monooxygenase +P53045 UniProtKB Transmembrane 56 76 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53045 UniProtKB Motif 160 164 . . . Note=Histidine box-1 +P53045 UniProtKB Motif 173 177 . . . Note=Histidine box-2 +P53045 UniProtKB Motif 257 263 . . . Note=Histidine box-3 +P53045 UniProtKB Cross-link 96 96 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P53045 UniProtKB Sequence conflict 302 302 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P22148 1 382 +P22148 UniProtKB Chain 1 382 . . . ID=PRO_0000096598;Note=Protein MSN1 +P22148 UniProtKB Region 12 26 . . . Note=Leucine-zipper +P22148 UniProtKB Motif 266 271 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22148 UniProtKB Sequence conflict 360 360 . . . Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P52918 1 1224 +P52918 UniProtKB Chain 1 1224 . . . ID=PRO_0000096599;Note=Protein MSN5 +P52918 UniProtKB Sequence conflict 886 886 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P52918 UniProtKB Sequence conflict 1011 1011 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P33748 1 704 +P33748 UniProtKB Chain 1 704 . . . ID=PRO_0000046810;Note=Zinc finger protein MSN2 +P33748 UniProtKB Zinc finger 647 665 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P33748 UniProtKB Zinc finger 676 698 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P33748 UniProtKB Motif 261 269 . . . Note=9aaTAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618436;Dbxref=PMID:27618436 +P33748 UniProtKB Compositional bias 1 109 . . . Note=Asp-rich (acidic) +P33748 UniProtKB Compositional bias 260 279 . . . Note=Asp-rich (acidic) +P33748 UniProtKB Modified residue 288 288 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P33748 UniProtKB Modified residue 304 304 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P33748 UniProtKB Modified residue 451 451 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P33748 UniProtKB Modified residue 582 582 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33748 UniProtKB Modified residue 633 633 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P40029 1 184 +P40029 UniProtKB Chain 1 184 . . . ID=PRO_0000138630;Note=Peptide methionine sulfoxide reductase +P40029 UniProtKB Modified residue 58 58 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40029 UniProtKB Helix 2 4 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM +P40029 UniProtKB Beta strand 7 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIL +P40029 UniProtKB Turn 13 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM +P40029 UniProtKB Beta strand 17 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM +P40029 UniProtKB Helix 26 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM +P40029 UniProtKB Helix 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM +P40029 UniProtKB Beta strand 41 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM +P40029 UniProtKB Helix 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIL +P40029 UniProtKB Helix 64 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIL +P40029 UniProtKB Beta strand 75 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM +P40029 UniProtKB Turn 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM +P40029 UniProtKB Helix 89 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM +P40029 UniProtKB Beta strand 104 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIL +P40029 UniProtKB Beta strand 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIL +P40029 UniProtKB Helix 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM +P40029 UniProtKB Beta strand 119 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM +P40029 UniProtKB Helix 125 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM +P40029 UniProtKB Helix 139 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM +P40029 UniProtKB Beta strand 149 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM +P40029 UniProtKB Helix 159 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PIM +##sequence-region Q03825 1 758 +Q03825 UniProtKB Chain 1 758 . . . ID=PRO_0000203315;Note=Transcription activator MSS11 +Q03825 UniProtKB Domain 51 83 . . . Note=LisH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00126 +Q03825 UniProtKB Compositional bias 290 329 . . . Note=Poly-Gln +Q03825 UniProtKB Compositional bias 605 637 . . . Note=Poly-Asn +Q03825 UniProtKB Compositional bias 653 656 . . . Note=Poly-Ser +Q03825 UniProtKB Mutagenesis 133 134 . . . Note=Reduces ability to activate transcription and to induce invasive growth. FL->GA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12492858;Dbxref=PMID:12492858 +Q03825 UniProtKB Mutagenesis 137 138 . . . Note=Reduces ability to activate transcription and to induce invasive growth. WW->GA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12492858;Dbxref=PMID:12492858 +Q03825 UniProtKB Mutagenesis 140 141 . . . Note=Reduces ability to activate transcription and to induce invasive growth. IF->GA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12492858;Dbxref=PMID:12492858 +Q03825 UniProtKB Mutagenesis 144 145 . . . Note=Reduces ability to activate transcription and to induce invasive growth. LF->GA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12492858;Dbxref=PMID:12492858 +##sequence-region P36066 1 463 +P36066 UniProtKB Chain 1 463 . . . ID=PRO_0000203149;Note=Protein MRG3-like +P36066 UniProtKB Transmembrane 54 74 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36066 UniProtKB Repeat 84 118 . . . Note=TPR 1 +P36066 UniProtKB Repeat 128 161 . . . Note=TPR 2 +P36066 UniProtKB Repeat 358 389 . . . Note=TPR 3 +P36066 UniProtKB Repeat 409 442 . . . Note=TPR 4 +P36066 UniProtKB Sequence conflict 252 252 . . . Note=Y->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q3E829 1 80 +Q3E829 UniProtKB Chain 1 80 . . . ID=PRO_0000240877;Note=MHF histone-fold complex subunit 2 +Q3E829 UniProtKB Helix 5 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R +Q3E829 UniProtKB Turn 12 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R +Q3E829 UniProtKB Turn 24 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R +Q3E829 UniProtKB Helix 27 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R +Q3E829 UniProtKB Helix 66 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R +##sequence-region P38341 1 106 +P38341 UniProtKB Chain 1 106 . . . ID=PRO_0000202527;Note=MICOS complex subunit MIC12 +P38341 UniProtKB Topological domain 1 10 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38341 UniProtKB Transmembrane 11 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38341 UniProtKB Topological domain 28 106 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36112 1 540 +P36112 UniProtKB Transit peptide 1 17 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36112 UniProtKB Chain 18 540 . . . ID=PRO_0000203197;Note=MICOS complex subunit MIC60 +P36112 UniProtKB Topological domain 18 37 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36112 UniProtKB Transmembrane 38 57 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36112 UniProtKB Topological domain 58 540 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36112 UniProtKB Coiled coil 173 268 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40850 1 830 +P40850 UniProtKB Chain 1 830 . . . ID=PRO_0000096495;Note=Protein MKT1 +P40850 UniProtKB Modified residue 358 358 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40850 UniProtKB Modified residue 362 362 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40850 UniProtKB Modified residue 371 371 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40850 UniProtKB Cross-link 4 4 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P40850 UniProtKB Natural variant 30 30 . . . Note=In strain: 2574%2C ATCC 24657 / D273-10B%2C ATCC 200060 / W303%2C Sigma 1278B%2C YJM 1129%2C YJM 270%2C YJM 627 and YJM 789. D->G +P40850 UniProtKB Natural variant 453 453 . . . Note=In strain: ATCC 24657 / D273-10B%2C ATCC 200060 / W303%2C Sigma 1278B%2C YJM 1129%2C YJM 270%2C YJM 627 and YJM 789. K->R +P40850 UniProtKB Sequence conflict 809 830 . . . Note=IDENVFKLFTKAVEFTTTALSS->TMKTCLNYH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08925 1 612 +Q08925 UniProtKB Chain 1 612 . . . ID=PRO_0000082038;Note=RNA-binding protein MRN1 +Q08925 UniProtKB Domain 201 274 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q08925 UniProtKB Domain 292 379 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q08925 UniProtKB Domain 431 504 . . . Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q08925 UniProtKB Domain 522 602 . . . Note=RRM 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q08925 UniProtKB Compositional bias 6 19 . . . Note=Poly-Asn +Q08925 UniProtKB Compositional bias 22 28 . . . Note=Poly-Asn +Q08925 UniProtKB Compositional bias 45 48 . . . Note=Poly-Ser +Q08925 UniProtKB Compositional bias 413 419 . . . Note=Poly-Ala +##sequence-region P33201 1 236 +P33201 UniProtKB Chain 1 236 . . . ID=PRO_0000154815;Note=Ribosome assembly factor MRT4 +P33201 UniProtKB Mutagenesis 68 68 . . . Note=Bypasses the requirement for phosphatase YVH1 for the release of MRT4. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19797078;Dbxref=PMID:19797078 +##sequence-region Q05648 1 414 +Q05648 UniProtKB Transit peptide 1 29 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05648 UniProtKB Chain 30 414 . . . ID=PRO_0000229731;Note=MIOREX complex component 10 +Q05648 UniProtKB Topological domain 30 373 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23022099;Dbxref=PMID:23022099 +Q05648 UniProtKB Transmembrane 374 394 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05648 UniProtKB Topological domain 395 414 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23022099;Dbxref=PMID:23022099 +##sequence-region P40050 1 688 +P40050 UniProtKB Transit peptide 1 46 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40050 UniProtKB Chain 47 688 . . . ID=PRO_0000202635;Note=MIOREX complex component 1 +##sequence-region P48564 1 524 +P48564 UniProtKB Transit peptide 1 34 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48564 UniProtKB Chain 35 524 . . . ID=PRO_0000203374;Note=MIOREX complex component 6 +##sequence-region P15424 1 664 +P15424 UniProtKB Transit peptide 1 26 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15424 UniProtKB Chain 27 664 . . . ID=PRO_0000030812;Note=ATP-dependent RNA helicase MSS116%2C mitochondrial +P15424 UniProtKB Domain 139 326 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P15424 UniProtKB Domain 355 512 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P15424 UniProtKB Nucleotide binding 152 159 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P15424 UniProtKB Motif 106 134 . . . Note=Q motif +P15424 UniProtKB Motif 267 270 . . . Note=DEAD box +P15424 UniProtKB Beta strand 89 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 104 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 115 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Turn 123 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TYW +P15424 UniProtKB Helix 131 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Beta strand 142 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 158 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Turn 173 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Beta strand 183 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 190 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Beta strand 215 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 224 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Beta strand 237 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 243 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Beta strand 258 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TYY +P15424 UniProtKB Beta strand 263 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 269 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Turn 275 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 278 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Beta strand 300 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 311 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Turn 316 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Beta strand 322 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Beta strand 333 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Beta strand 342 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 354 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Turn 370 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Beta strand 375 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 383 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Turn 398 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Beta strand 403 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 412 424 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Beta strand 426 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 434 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Beta strand 437 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TZ0 +P15424 UniProtKB Beta strand 447 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Beta strand 455 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TYY +P15424 UniProtKB Helix 459 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 469 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TYN +P15424 UniProtKB Beta strand 474 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 482 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 485 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Beta strand 501 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 509 518 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 523 539 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 541 544 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 548 556 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 558 562 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Beta strand 570 572 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Helix 574 580 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Beta strand 583 585 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TYW +P15424 UniProtKB Helix 586 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +P15424 UniProtKB Beta strand 592 594 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5X +##sequence-region Q08818 1 692 +Q08818 UniProtKB Transit peptide 1 30 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08818 UniProtKB Chain 31 692 . . . ID=PRO_0000042820;Note=Meiotic sister-chromatid recombination protein 6%2C mitochondrial +##sequence-region P25846 1 959 +P25846 UniProtKB Transit peptide 1 21 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7961998;Dbxref=PMID:7961998 +P25846 UniProtKB Chain 22 959 . . . ID=PRO_0000115179;Note=DNA mismatch repair protein MSH1%2C mitochondrial +P25846 UniProtKB Nucleotide binding 771 778 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25846 UniProtKB Mutagenesis 105 105 . . . Note=Increases the rate of point mutations 35-fold and displays a significant decrease in respiration-competent cells during a time course. F->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15611870,ECO:0000269|PubMed:16337661;Dbxref=PMID:15611870,PMID:16337661 +P25846 UniProtKB Mutagenesis 776 776 . . . Note=Increases the rate of point mutations 19-fold and displays a moderate decrease in respiration-competent cells during a time course. G->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11862493,ECO:0000269|PubMed:15611870,ECO:0000269|PubMed:16337661;Dbxref=PMID:11862493,PMID:15611870,PMID:16337661 +P25846 UniProtKB Mutagenesis 813 813 . . . Note=Slightly increases the frequency of point mutations and repeat-mediated deletion rates in mtDNA. R->W;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11862493,ECO:0000269|PubMed:16337661;Dbxref=PMID:11862493,PMID:16337661 +P25846 UniProtKB Sequence conflict 437 437 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25846 UniProtKB Sequence conflict 695 695 . . . Note=E->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40965 1 878 +P40965 UniProtKB Chain 1 878 . . . ID=PRO_0000115201;Note=MutS protein homolog 4 +P40965 UniProtKB Nucleotide binding 634 641 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40965 UniProtKB Sequence conflict 811 812 . . . Note=IH->MD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12175 1 901 +Q12175 UniProtKB Chain 1 901 . . . ID=PRO_0000115206;Note=MutS protein homolog 5 +Q12175 UniProtKB Nucleotide binding 643 650 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12175 UniProtKB Mutagenesis 643 644 . . . Note=Abolishes function%3B no effect on interaction with MSH4. GA->DV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9374523;Dbxref=PMID:9374523 +Q12175 UniProtKB Mutagenesis 648 648 . . . Note=Abolishes function%3B no effect on interaction with MSH4. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9374523;Dbxref=PMID:9374523 +##sequence-region P40567 1 111 +P40567 UniProtKB Chain 1 111 . . . ID=PRO_0000081895;Note=U2 small nuclear ribonucleoprotein B'' +P40567 UniProtKB Domain 28 106 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P40567 UniProtKB Beta strand 30 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40567 UniProtKB Helix 41 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40567 UniProtKB Turn 66 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40567 UniProtKB Beta strand 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40567 UniProtKB Helix 79 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40567 UniProtKB Beta strand 100 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P53604 1 210 +P53604 UniProtKB Chain 1 210 . . . ID=PRO_0000096600;Note=Protein MSO1 +P53604 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53604 UniProtKB Modified residue 102 102 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P53604 UniProtKB Alternative sequence 1 1 . . . ID=VSP_058125;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P20676 1 1076 +P20676 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P20676 UniProtKB Chain 2 1076 . . . ID=PRO_0000204902;Note=Nucleoporin NUP1 +P20676 UniProtKB Repeat 336 338 . . . Note=FXF 1 +P20676 UniProtKB Repeat 384 386 . . . Note=FXF 2 +P20676 UniProtKB Repeat 406 409 . . . Note=FXFG 1 +P20676 UniProtKB Repeat 422 425 . . . Note=FXFG 2 +P20676 UniProtKB Repeat 448 451 . . . Note=FXFG 3 +P20676 UniProtKB Repeat 484 487 . . . Note=FXFG 4 +P20676 UniProtKB Repeat 510 513 . . . Note=FXFG 5 +P20676 UniProtKB Repeat 525 528 . . . Note=FXFG 6 +P20676 UniProtKB Repeat 543 546 . . . Note=FXFG 7 +P20676 UniProtKB Repeat 571 574 . . . Note=FXFG 8 +P20676 UniProtKB Repeat 591 593 . . . Note=FXF 3 +P20676 UniProtKB Repeat 614 616 . . . Note=FXF 4 +P20676 UniProtKB Repeat 636 638 . . . Note=FXF 5 +P20676 UniProtKB Repeat 657 659 . . . Note=FXF 6 +P20676 UniProtKB Repeat 671 674 . . . Note=FXFG 9 +P20676 UniProtKB Repeat 689 691 . . . Note=FXF 7 +P20676 UniProtKB Repeat 708 711 . . . Note=FXFG 10 +P20676 UniProtKB Repeat 727 730 . . . Note=FXFG 11 +P20676 UniProtKB Repeat 753 755 . . . Note=FXF 8 +P20676 UniProtKB Repeat 800 803 . . . Note=FXFG 12 +P20676 UniProtKB Repeat 819 821 . . . Note=FXF 9 +P20676 UniProtKB Repeat 866 868 . . . Note=FXF 10 +P20676 UniProtKB Repeat 885 888 . . . Note=FXFG 13 +P20676 UniProtKB Repeat 929 931 . . . Note=FXF 11 +P20676 UniProtKB Repeat 1008 1009 . . . Note=FG 1 +P20676 UniProtKB Repeat 1027 1028 . . . Note=FG 2 +P20676 UniProtKB Repeat 1038 1039 . . . Note=FG 3 +P20676 UniProtKB Region 1040 1076 . . . Note=Interaction with KAP95 +P20676 UniProtKB Compositional bias 81 84 . . . Note=Poly-Asn +P20676 UniProtKB Compositional bias 718 723 . . . Note=Poly-Thr +P20676 UniProtKB Compositional bias 830 833 . . . Note=Poly-Thr +P20676 UniProtKB Compositional bias 881 1022 . . . Note=Asn-rich +P20676 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P20676 UniProtKB Modified residue 54 54 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P20676 UniProtKB Modified residue 161 161 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P20676 UniProtKB Modified residue 381 381 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P20676 UniProtKB Modified residue 383 383 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P20676 UniProtKB Modified residue 637 637 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P20676 UniProtKB Helix 1004 1006 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +P20676 UniProtKB Turn 1007 1009 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +##sequence-region Q02199 1 472 +Q02199 UniProtKB Chain 1 472 . . . ID=PRO_0000204867;Note=Nucleoporin NUP49/NSP49 +Q02199 UniProtKB Repeat 2 3 . . . Note=FG 1 +Q02199 UniProtKB Repeat 14 17 . . . Note=GLFG 1 +Q02199 UniProtKB Repeat 33 34 . . . Note=FG 2 +Q02199 UniProtKB Repeat 48 51 . . . Note=GLFG 2 +Q02199 UniProtKB Repeat 65 66 . . . Note=FG 3 +Q02199 UniProtKB Repeat 77 78 . . . Note=FG 4 +Q02199 UniProtKB Repeat 86 89 . . . Note=GLFG 3 +Q02199 UniProtKB Repeat 101 104 . . . Note=GLFG 4 +Q02199 UniProtKB Repeat 113 116 . . . Note=SLFG 1 +Q02199 UniProtKB Repeat 125 128 . . . Note=GLFG 5 +Q02199 UniProtKB Repeat 148 151 . . . Note=GLFG 6 +Q02199 UniProtKB Repeat 159 162 . . . Note=SLFG 2 +Q02199 UniProtKB Repeat 175 178 . . . Note=GLFG 7%3B approximate +Q02199 UniProtKB Repeat 185 188 . . . Note=SLFG 3 +Q02199 UniProtKB Repeat 199 202 . . . Note=GLFG 8 +Q02199 UniProtKB Repeat 210 213 . . . Note=SLFG 4 +Q02199 UniProtKB Repeat 233 236 . . . Note=GLFG 9 +Q02199 UniProtKB Compositional bias 13 207 . . . Note=Gly-rich +Q02199 UniProtKB Compositional bias 67 73 . . . Note=Poly-Gln +Q02199 UniProtKB Compositional bias 90 226 . . . Note=Asn-rich +Q02199 UniProtKB Compositional bias 216 226 . . . Note=Poly-Asn +Q02199 UniProtKB Compositional bias 238 289 . . . Note=Gln-rich +Q02199 UniProtKB Compositional bias 238 249 . . . Note=Poly-Gln +##sequence-region Q12454 1 224 +Q12454 UniProtKB Chain 1 224 . . . ID=PRO_0000244442;Note=Putative tyrosine-protein phosphatase OCA6 +Q12454 UniProtKB Active site 114 114 . . . Note=Phosphocysteine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12454 UniProtKB Modified residue 2 2 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12454 UniProtKB Sequence conflict 208 208 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P31755 1 480 +P31755 UniProtKB Chain 1 480 . . . ID=PRO_0000080563;Note=Initiation-specific alpha-1%2C6-mannosyltransferase +P31755 UniProtKB Topological domain 1 15 . . . Note=Cytoplasmic;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1628616;Dbxref=PMID:1628616 +P31755 UniProtKB Transmembrane 16 30 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255,ECO:0000303;evidence=ECO:0000255,ECO:0000303|PubMed:1628616;Dbxref=PMID:1628616 +P31755 UniProtKB Topological domain 31 480 . . . Note=Lumenal;Ontology_term=ECO:0000269,ECO:0000303;evidence=ECO:0000269|PubMed:8601597,ECO:0000303|PubMed:1628616;Dbxref=PMID:8601597,PMID:1628616 +P31755 UniProtKB Motif 187 189 . . . Note=DXD motif;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:17042779;Dbxref=PMID:17042779 +P31755 UniProtKB Glycosylation 203 203 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31755 UniProtKB Glycosylation 281 281 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31755 UniProtKB Glycosylation 341 341 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31755 UniProtKB Glycosylation 393 393 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31755 UniProtKB Mutagenesis 187 187 . . . Note=Loss of mannosyltransferase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17042779;Dbxref=PMID:17042779 +##sequence-region Q99297 1 307 +Q99297 UniProtKB Chain 1 307 . . . ID=PRO_0000090649;Note=Mitochondrial 2-oxodicarboxylate carrier 2 +Q99297 UniProtKB Transmembrane 10 30 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99297 UniProtKB Transmembrane 76 95 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99297 UniProtKB Transmembrane 122 142 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99297 UniProtKB Transmembrane 171 191 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99297 UniProtKB Transmembrane 215 235 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99297 UniProtKB Transmembrane 280 300 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99297 UniProtKB Repeat 10 106 . . . Note=Solcar 1 +Q99297 UniProtKB Repeat 116 200 . . . Note=Solcar 2 +Q99297 UniProtKB Repeat 209 299 . . . Note=Solcar 3 +##sequence-region P38325 1 134 +P38325 UniProtKB Chain 1 134 . . . ID=PRO_0000202518;Note=Mitochondrial outer membrane protein OM14 +P38325 UniProtKB Transmembrane 71 87 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38325 UniProtKB Transmembrane 105 123 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38325 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38325 UniProtKB Modified residue 15 15 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region Q07521 1 108 +Q07521 UniProtKB Chain 1 108 . . . ID=PRO_0000299776;Note=Putative uncharacterized protein OPI6 +##sequence-region Q06593 1 877 +Q06593 UniProtKB Chain 1 877 . . . ID=PRO_0000262733;Note=Oligopeptide transporter 2 +Q06593 UniProtKB Topological domain 1 167 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Transmembrane 168 188 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Topological domain 189 189 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Transmembrane 190 210 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Topological domain 211 240 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Transmembrane 241 261 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Topological domain 262 272 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Transmembrane 273 293 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Topological domain 294 334 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Transmembrane 335 355 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Topological domain 356 374 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Transmembrane 375 395 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Topological domain 396 404 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Transmembrane 405 425 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Topological domain 426 480 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Transmembrane 481 501 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Topological domain 502 553 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Transmembrane 554 574 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Topological domain 575 582 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Transmembrane 583 603 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Topological domain 604 614 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Transmembrane 615 635 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Topological domain 636 671 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Transmembrane 672 692 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Topological domain 693 730 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Transmembrane 731 751 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Topological domain 752 766 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Transmembrane 767 789 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Topological domain 790 811 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Transmembrane 812 832 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Topological domain 833 877 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Glycosylation 374 374 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06593 UniProtKB Glycosylation 860 860 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P50874 1 479 +P50874 UniProtKB Chain 1 479 . . . ID=PRO_0000127096;Note=Origin recognition complex subunit 5 +P50874 UniProtKB Nucleotide binding 37 44 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06144 1 216 +Q06144 UniProtKB Chain 1 216 . . . ID=PRO_0000215646;Note=Protein ORM2 +Q06144 UniProtKB Topological domain 1 78 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06144 UniProtKB Transmembrane 79 99 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06144 UniProtKB Topological domain 100 103 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06144 UniProtKB Transmembrane 104 124 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06144 UniProtKB Topological domain 125 148 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06144 UniProtKB Transmembrane 149 169 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06144 UniProtKB Topological domain 170 177 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06144 UniProtKB Transmembrane 178 198 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06144 UniProtKB Topological domain 199 216 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06144 UniProtKB Modified residue 9 9 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06144 UniProtKB Modified residue 15 15 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06144 UniProtKB Modified residue 18 18 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q06144 UniProtKB Modified residue 22 22 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06144 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53224 +Q06144 UniProtKB Modified residue 51 51 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53224 +Q06144 UniProtKB Mutagenesis 9 9 . . . Note=Induces dysregulation of sphingolipid synthesis%3B when associated with A-15%2C A-18%2C A-36 and 46-A--A-48. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20182505;Dbxref=PMID:20182505 +Q06144 UniProtKB Mutagenesis 15 15 . . . Note=Induces dysregulation of sphingolipid synthesis%3B when associated with A-9%2C A-18%2C A-36 and 46-A--A-48. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20182505;Dbxref=PMID:20182505 +Q06144 UniProtKB Mutagenesis 18 18 . . . Note=Induces dysregulation of sphingolipid synthesis%3B when associated with A-9%2C A-15%2C A-36 and 46-A--A-48. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20182505;Dbxref=PMID:20182505 +Q06144 UniProtKB Mutagenesis 36 36 . . . Note=Induces dysregulation of sphingolipid synthesis%3B when associated with A-9%2C A-15%2C A-18 and 46-A--A-48. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20182505;Dbxref=PMID:20182505 +Q06144 UniProtKB Mutagenesis 46 48 . . . Note=Induces dysregulation of sphingolipid synthesis%3B when associated with A-9%2C A-15%2C A-18%2C and A-36. SSS->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20182505;Dbxref=PMID:20182505 +##sequence-region P21375 1 501 +P21375 UniProtKB Transit peptide 1 32 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9587404;Dbxref=PMID:9587404 +P21375 UniProtKB Chain 33 501 . . . ID=PRO_0000158668;Note=Fumarate reductase 2 +P21375 UniProtKB Nucleotide binding 37 51 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21375 UniProtKB Active site 281 281 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21375 UniProtKB Active site 304 304 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21375 UniProtKB Sequence conflict 106 107 . . . Note=LH->FD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21375 UniProtKB Sequence conflict 170 170 . . . Note=A->AR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21375 UniProtKB Sequence conflict 191 192 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21375 UniProtKB Sequence conflict 439 439 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21375 UniProtKB Sequence conflict 456 457 . . . Note=SV->TL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03723 1 332 +Q03723 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03723 UniProtKB Chain 25 332 . . . ID=PRO_0000058098;Note=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST6 +Q03723 UniProtKB Topological domain 25 188 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03723 UniProtKB Transmembrane 189 209 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03723 UniProtKB Transmembrane 217 237 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03723 UniProtKB Transmembrane 268 288 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03723 UniProtKB Transmembrane 303 323 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03723 UniProtKB Topological domain 324 332 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03723 UniProtKB Domain 35 162 . . . Note=Thioredoxin +Q03723 UniProtKB Disulfide bond 78 81 . . . Note=Redox-active;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03723 UniProtKB Mutagenesis 78 78 . . . Note=Alters glycosyltransferase efficiency towards a subset of target proteins%3B when associated with S-81. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19549845;Dbxref=PMID:19549845 +Q03723 UniProtKB Mutagenesis 81 81 . . . Note=Alters glycosyltransferase efficiency towards a subset of target proteins%3B when associated with S-78. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19549845;Dbxref=PMID:19549845 +Q03723 UniProtKB Sequence conflict 33 33 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03723 UniProtKB Helix 31 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4 +Q03723 UniProtKB Beta strand 41 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4 +Q03723 UniProtKB Turn 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4 +Q03723 UniProtKB Helix 50 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4 +Q03723 UniProtKB Beta strand 61 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4 +Q03723 UniProtKB Helix 79 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4 +Q03723 UniProtKB Beta strand 104 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4 +Q03723 UniProtKB Turn 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4 +Q03723 UniProtKB Helix 115 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4 +Q03723 UniProtKB Beta strand 128 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4 +Q03723 UniProtKB Helix 137 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4 +Q03723 UniProtKB Turn 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4 +Q03723 UniProtKB Beta strand 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4 +Q03723 UniProtKB Helix 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4 +Q03723 UniProtKB Helix 163 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GA4 +##sequence-region Q02795 1 286 +Q02795 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8175708;Dbxref=PMID:8175708 +Q02795 UniProtKB Chain 20 286 . . . ID=PRO_0000021962;Note=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit SWP1 +Q02795 UniProtKB Topological domain 20 194 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02795 UniProtKB Transmembrane 195 215 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02795 UniProtKB Topological domain 216 228 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02795 UniProtKB Transmembrane 229 249 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02795 UniProtKB Topological domain 250 252 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02795 UniProtKB Transmembrane 253 273 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02795 UniProtKB Topological domain 274 286 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08692 1 278 +Q08692 UniProtKB Chain 1 278 . . . ID=PRO_0000268695;Note=Outer spore wall protein 1 +##sequence-region P43558 1 301 +P43558 UniProtKB Chain 1 301 . . . ID=PRO_0000202672;Note=Ubiquitin thioesterase OTU1 +P43558 UniProtKB Domain 109 229 . . . Note=OTU;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00139 +P43558 UniProtKB Zinc finger 270 294 . . . Note=C2H2-type +P43558 UniProtKB Region 4 80 . . . Note=UBX-like;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5VVQ6 +P43558 UniProtKB Region 114 120 . . . Note=Cys-loop;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5VVQ6 +P43558 UniProtKB Region 169 179 . . . Note=Variable-loop;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5VVQ6 +P43558 UniProtKB Region 218 222 . . . Note=His-loop;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5VVQ6 +P43558 UniProtKB Region 243 248 . . . Note=S2 site;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5VVQ6 +P43558 UniProtKB Active site 117 117 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96FW1 +P43558 UniProtKB Active site 120 120 . . . Note=Nucleophile;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43558 UniProtKB Active site 222 222 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5VVQ6 +P43558 UniProtKB Active site 294 294 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96FW1 +P43558 UniProtKB Binding site 221 221 . . . Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5VVQ6 +P43558 UniProtKB Cross-link 160 160 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P43558 UniProtKB Mutagenesis 120 120 . . . Note=Loss of function. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16427015;Dbxref=PMID:16427015 +P43558 UniProtKB Beta strand 1 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KDL +P43558 UniProtKB Beta strand 10 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KDL +P43558 UniProtKB Helix 22 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KDL +P43558 UniProtKB Beta strand 34 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KDL +P43558 UniProtKB Turn 39 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KDL +P43558 UniProtKB Beta strand 43 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KDL +P43558 UniProtKB Helix 54 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KDL +P43558 UniProtKB Helix 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KDL +P43558 UniProtKB Beta strand 68 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KDL +P43558 UniProtKB Beta strand 98 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4 +P43558 UniProtKB Turn 102 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4 +P43558 UniProtKB Beta strand 107 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4 +P43558 UniProtKB Helix 120 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4 +P43558 UniProtKB Helix 136 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4 +P43558 UniProtKB Turn 150 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4 +P43558 UniProtKB Helix 155 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4 +P43558 UniProtKB Helix 162 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4 +P43558 UniProtKB Helix 178 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4 +P43558 UniProtKB Beta strand 191 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4 +P43558 UniProtKB Turn 197 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4 +P43558 UniProtKB Beta strand 201 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4 +P43558 UniProtKB Turn 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4 +P43558 UniProtKB Beta strand 211 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4 +P43558 UniProtKB Beta strand 223 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4 +P43558 UniProtKB Turn 229 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4 +P43558 UniProtKB Helix 242 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BY4 +##sequence-region P32336 1 851 +P32336 UniProtKB Chain 1 851 . . . ID=PRO_0000057981;Note=Protein NUD1 +P32336 UniProtKB Repeat 544 566 . . . Note=LRR 1 +P32336 UniProtKB Repeat 567 588 . . . Note=LRR 2 +P32336 UniProtKB Repeat 589 609 . . . Note=LRR 3 +P32336 UniProtKB Repeat 621 642 . . . Note=LRR 4 +P32336 UniProtKB Repeat 643 664 . . . Note=LRR 5 +P32336 UniProtKB Compositional bias 223 248 . . . Note=Asn-rich +P32336 UniProtKB Compositional bias 223 239 . . . Note=Poly-Asn +P32336 UniProtKB Compositional bias 266 274 . . . Note=Poly-Ser +P32336 UniProtKB Modified residue 388 388 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32336 UniProtKB Modified residue 392 392 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32336 UniProtKB Modified residue 417 417 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32336 UniProtKB Modified residue 419 419 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32336 UniProtKB Cross-link 357 357 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32336 UniProtKB Sequence conflict 5 6 . . . Note=TQ->SE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38738 1 679 +P38738 UniProtKB Chain 1 679 . . . ID=PRO_0000202881;Note=Oxidant-induced cell-cycle arrest protein 5 +P38738 UniProtKB Domain 50 441 . . . Note=Rab-GAP TBC +P38738 UniProtKB Compositional bias 263 271 . . . Note=Poly-Asn +P38738 UniProtKB Compositional bias 609 637 . . . Note=Ser-rich +##sequence-region P16387 1 420 +P16387 UniProtKB Transit peptide 1 33 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2684159;Dbxref=PMID:2684159 +P16387 UniProtKB Chain 34 420 . . . ID=PRO_0000020452;Note=Pyruvate dehydrogenase E1 component subunit alpha%2C mitochondrial +P16387 UniProtKB Modified residue 313 313 . . . Note=Phosphoserine%3B by PDK1 and PDK2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18180296;Dbxref=PMID:15665377,PMID:17330950,PMID:17761666,PMID:18407956,PMID:19779198,PMID:18180296 +P16387 UniProtKB Sequence conflict 76 76 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P16547 1 393 +P16547 UniProtKB Chain 1 393 . . . ID=PRO_0000058041;Note=Mitochondrial outer membrane protein OM45 +P16547 UniProtKB Topological domain 1 4 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16547 UniProtKB Transmembrane 5 22 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16547 UniProtKB Topological domain 23 393 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16547 UniProtKB Sequence conflict 51 51 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06810 1 360 +Q06810 UniProtKB Chain 1 360 . . . ID=PRO_0000268694;Note=Protein OPY2 +Q06810 UniProtKB Transmembrane 92 112 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06810 UniProtKB Region 266 345 . . . Note=STE50-binding +Q06810 UniProtKB Compositional bias 2 86 . . . Note=Ser-rich +Q06810 UniProtKB Compositional bias 147 159 . . . Note=Asp-rich +Q06810 UniProtKB Modified residue 285 285 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06810 UniProtKB Modified residue 348 348 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q06810 UniProtKB Glycosylation 172 172 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06810 UniProtKB Glycosylation 185 185 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06810 UniProtKB Sequence conflict 234 234 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P54784 1 914 +P54784 UniProtKB Chain 1 914 . . . ID=PRO_0000127074;Note=Origin recognition complex subunit 1 +P54784 UniProtKB Domain 48 188 . . . Note=BAH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00370 +P54784 UniProtKB Nucleotide binding 479 486 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54784 UniProtKB Nucleotide binding 726 733 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54784 UniProtKB Compositional bias 281 292 . . . Note=Poly-Glu +P54784 UniProtKB Compositional bias 759 768 . . . Note=Poly-Asp +P54784 UniProtKB Modified residue 237 237 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P54784 UniProtKB Helix 6 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Beta strand 11 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Beta strand 18 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Beta strand 38 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Turn 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Beta strand 55 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Turn 61 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Beta strand 65 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Turn 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Beta strand 83 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Helix 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Helix 98 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Helix 107 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Helix 116 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Beta strand 131 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Helix 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Beta strand 146 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Helix 155 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Helix 162 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Turn 167 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Beta strand 170 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Turn 179 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZBX +P54784 UniProtKB Beta strand 182 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZBX +P54784 UniProtKB Helix 189 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +P54784 UniProtKB Helix 201 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M4Z +##sequence-region Q99380 1 36 +Q99380 UniProtKB Chain 1 36 . . . ID=PRO_0000058093;Note=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST4 +Q99380 UniProtKB Topological domain 1 9 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12810948;Dbxref=PMID:12810948 +Q99380 UniProtKB Transmembrane 10 28 . . . Note=Helical +Q99380 UniProtKB Topological domain 29 36 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12810948;Dbxref=PMID:12810948 +Q99380 UniProtKB Mutagenesis 18 18 . . . Note=Severe growth defect%3B abolishes interaction with OST3 and STT3. M->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948 +Q99380 UniProtKB Mutagenesis 18 18 . . . Note=No effect on interaction between OST3 and STT3. M->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948 +Q99380 UniProtKB Mutagenesis 19 19 . . . Note=Severe growth defect%3B abolishes interaction with OST3. M->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948 +Q99380 UniProtKB Mutagenesis 19 19 . . . Note=Disrupts interaction between OST3 and STT3. M->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948 +Q99380 UniProtKB Mutagenesis 20 20 . . . Note=Severe growth defect. T->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948 +Q99380 UniProtKB Mutagenesis 20 20 . . . Note=Severe growth defect%3B abolishes interaction with OST3%3B disrupts interaction between OST3 and STT3. T->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948 +Q99380 UniProtKB Mutagenesis 21 21 . . . Note=Abolishes interaction with OST3 and STT3%3B disrupts interaction between OST3 and STT3. L->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948 +Q99380 UniProtKB Mutagenesis 23 23 . . . Note=Severe growth defect. V->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948 +Q99380 UniProtKB Mutagenesis 23 23 . . . Note=Severe growth defect%3B abolishes interaction with OST3%3B disrupts interaction between OST3 and STT3. V->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948 +Q99380 UniProtKB Mutagenesis 24 24 . . . Note=Severe growth defect. I->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948 +Q99380 UniProtKB Mutagenesis 24 24 . . . Note=Disrupts interaction between OST3 and STT3. I->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677492,ECO:0000269|PubMed:12810948;Dbxref=PMID:10677492,PMID:12810948 +Q99380 UniProtKB Mutagenesis 25 25 . . . Note=Severe growth defect. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10677492;Dbxref=PMID:10677492 +Q99380 UniProtKB Helix 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RKL +Q99380 UniProtKB Helix 9 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RKL +##sequence-region P53136 1 463 +P53136 UniProtKB Chain 1 463 . . . ID=PRO_0000202748;Note=Ribosome biogenesis protein NSA1 +P53136 UniProtKB Beta strand 1 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Helix 8 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 12 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 33 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Helix 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 47 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 57 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Turn 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 66 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 102 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Helix 120 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUM +P53136 UniProtKB Beta strand 140 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 154 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 162 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 173 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 188 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 198 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 203 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 212 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 226 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 248 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 269 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 277 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Turn 284 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 291 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Helix 298 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 303 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Helix 328 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 332 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 342 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 351 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Turn 357 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 366 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Turn 371 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 374 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 383 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Turn 389 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 394 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +P53136 UniProtKB Beta strand 404 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUI +##sequence-region P52891 1 726 +P52891 UniProtKB Chain 1 726 . . . ID=PRO_0000204884;Note=Nucleoporin NUP84 +P52891 UniProtKB Coiled coil 563 583 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52891 UniProtKB Helix 8 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 12 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 36 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 61 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 102 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 114 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 145 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 160 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 166 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 171 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 193 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 206 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Turn 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 225 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Turn 228 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Beta strand 235 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 240 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Beta strand 254 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 258 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 274 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 282 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 310 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 324 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 336 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 344 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 356 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 383 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 406 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 426 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 429 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P52891 UniProtKB Helix 437 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +##sequence-region P07991 1 424 +P07991 UniProtKB Chain 1 424 . . . ID=PRO_0000120499;Note=Ornithine aminotransferase +P07991 UniProtKB Modified residue 272 272 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07991 UniProtKB Cross-link 390 390 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P07991 UniProtKB Sequence conflict 8 8 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07991 UniProtKB Sequence conflict 8 8 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07991 UniProtKB Sequence conflict 38 38 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07991 UniProtKB Sequence conflict 38 38 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07991 UniProtKB Sequence conflict 99 99 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07991 UniProtKB Sequence conflict 212 212 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07991 UniProtKB Sequence conflict 385 385 . . . Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P20967 1 1014 +P20967 UniProtKB Transit peptide 1 30 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20967 UniProtKB Chain 31 1014 . . . ID=PRO_0000020436;Note=2-oxoglutarate dehydrogenase%2C mitochondrial +P20967 UniProtKB Sequence conflict 325 327 . . . Note=SEF->LNL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20967 UniProtKB Sequence conflict 513 513 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20967 UniProtKB Sequence conflict 568 568 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P16451 1 410 +P16451 UniProtKB Transit peptide 1 30 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2682658;Dbxref=PMID:2682658 +P16451 UniProtKB Chain 31 410 . . . ID=PRO_0000020487;Note=Pyruvate dehydrogenase complex protein X component%2C mitochondrial +P16451 UniProtKB Domain 32 108 . . . Note=Lipoyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066 +P16451 UniProtKB Domain 169 210 . . . Note=Peripheral subunit-binding (PSBD);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01170 +P16451 UniProtKB Modified residue 73 73 . . . Note=N6-lipoyllysine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250,ECO:0000255|PROSITE-ProRule:PRU01066 +P16451 UniProtKB Sequence conflict 378 378 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06668 1 471 +Q06668 UniProtKB Transit peptide 1 39 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06668 UniProtKB Chain 40 471 . . . ID=PRO_0000268693;Note=Methyltransferase OMS1%2C mitochondrial +Q06668 UniProtKB Topological domain 40 103 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15355998;Dbxref=PMID:15355998 +Q06668 UniProtKB Transmembrane 104 123 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06668 UniProtKB Topological domain 124 471 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15355998;Dbxref=PMID:15355998 +##sequence-region A0A023PZI1 1 117 +A0A023PZI1 UniProtKB Chain 1 117 . . . ID=PRO_0000431061;Note=Putative uncharacterized protein OPI11 +##sequence-region P87286 1 144 +P87286 UniProtKB Chain 1 144 . . . ID=PRO_0000299777;Note=Putative uncharacterized protein OPI7 +P87286 UniProtKB Compositional bias 9 82 . . . Note=Ser-rich +##sequence-region P38271 1 328 +P38271 UniProtKB Chain 1 328 . . . ID=PRO_0000058074;Note=Protein OPY1 +P38271 UniProtKB Domain 215 318 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +##sequence-region Q02630 1 1113 +Q02630 UniProtKB Chain 1 1113 . . . ID=PRO_0000204835;Note=Nucleoporin NUP116/NSP116 +Q02630 UniProtKB Repeat 2 3 . . . Note=FG 1 +Q02630 UniProtKB Repeat 17 18 . . . Note=FG 2 +Q02630 UniProtKB Repeat 24 25 . . . Note=FG 3 +Q02630 UniProtKB Repeat 40 41 . . . Note=FG 4 +Q02630 UniProtKB Repeat 55 58 . . . Note=GLFG 1%3B approximate +Q02630 UniProtKB Repeat 66 67 . . . Note=FG 5 +Q02630 UniProtKB Repeat 79 80 . . . Note=FG 6 +Q02630 UniProtKB Repeat 94 95 . . . Note=FG 7 +Q02630 UniProtKB Repeat 167 168 . . . Note=FG 8 +Q02630 UniProtKB Repeat 189 190 . . . Note=FG 9 +Q02630 UniProtKB Repeat 205 208 . . . Note=GLFG 2 +Q02630 UniProtKB Repeat 214 217 . . . Note=GLFG 3%3B approximate +Q02630 UniProtKB Repeat 224 227 . . . Note=GLFG 4%3B approximate +Q02630 UniProtKB Repeat 235 238 . . . Note=GLFG 5 +Q02630 UniProtKB Repeat 249 250 . . . Note=FG 10 +Q02630 UniProtKB Repeat 259 262 . . . Note=GLFG 6 +Q02630 UniProtKB Repeat 276 279 . . . Note=GLFG 7 +Q02630 UniProtKB Repeat 288 291 . . . Note=GLFG 8 +Q02630 UniProtKB Repeat 297 298 . . . Note=FG 11 +Q02630 UniProtKB Repeat 306 309 . . . Note=GLFG 9%3B approximate +Q02630 UniProtKB Repeat 327 330 . . . Note=GLFG 10%3B approximate +Q02630 UniProtKB Repeat 339 342 . . . Note=GLFG 11%3B approximate +Q02630 UniProtKB Repeat 351 352 . . . Note=FG 12 +Q02630 UniProtKB Repeat 359 362 . . . Note=GLFG 12 +Q02630 UniProtKB Repeat 370 371 . . . Note=FG 13 +Q02630 UniProtKB Repeat 382 385 . . . Note=GLFG 13 +Q02630 UniProtKB Repeat 395 398 . . . Note=GLFG 14 +Q02630 UniProtKB Repeat 407 410 . . . Note=GLFG 15 +Q02630 UniProtKB Repeat 420 423 . . . Note=GLFG 16 +Q02630 UniProtKB Repeat 431 432 . . . Note=FG 14 +Q02630 UniProtKB Repeat 439 442 . . . Note=GLFG 17 +Q02630 UniProtKB Repeat 448 451 . . . Note=GLFG 18 +Q02630 UniProtKB Repeat 470 471 . . . Note=FG 15 +Q02630 UniProtKB Repeat 482 485 . . . Note=GLFG 19 +Q02630 UniProtKB Repeat 497 500 . . . Note=GLFG 20 +Q02630 UniProtKB Repeat 510 511 . . . Note=FG 16 +Q02630 UniProtKB Repeat 525 526 . . . Note=FG 17 +Q02630 UniProtKB Repeat 532 533 . . . Note=FG 18 +Q02630 UniProtKB Repeat 572 575 . . . Note=GLFG 21 +Q02630 UniProtKB Repeat 585 588 . . . Note=GLFG 22 +Q02630 UniProtKB Repeat 604 607 . . . Note=GLFG 23 +Q02630 UniProtKB Repeat 616 617 . . . Note=FG 19 +Q02630 UniProtKB Repeat 630 633 . . . Note=GLFG 24%3B approximate +Q02630 UniProtKB Repeat 648 651 . . . Note=GLFG 25 +Q02630 UniProtKB Repeat 665 668 . . . Note=GLFG 26 +Q02630 UniProtKB Repeat 683 686 . . . Note=GLFG 27 +Q02630 UniProtKB Domain 967 1109 . . . Note=Peptidase S59;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00765 +Q02630 UniProtKB Region 110 166 . . . Note=GLE2 binding sequence (GLEBS) +Q02630 UniProtKB Region 160 362 . . . Note=Interaction with MEX67%2C not KAP95;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11104765;Dbxref=PMID:11104765 +Q02630 UniProtKB Region 362 535 . . . Note=Sufficient for interaction with MEX67 and KAP95;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11104765;Dbxref=PMID:11104765 +Q02630 UniProtKB Region 536 732 . . . Note=Interaction with KAP95%2C not MEX67 +Q02630 UniProtKB Region 967 1113 . . . Note=Interaction with NUP82 NPC subcomplex +Q02630 UniProtKB Region 969 1108 . . . Note=Nucleoporin RNA-binding motif (NRM) +Q02630 UniProtKB Compositional bias 27 50 . . . Note=Gln-rich +Q02630 UniProtKB Compositional bias 27 32 . . . Note=Poly-Gln +Q02630 UniProtKB Compositional bias 164 712 . . . Note=Gly-rich +Q02630 UniProtKB Compositional bias 263 304 . . . Note=Asn-rich +Q02630 UniProtKB Compositional bias 280 567 . . . Note=Gln-rich +Q02630 UniProtKB Compositional bias 475 478 . . . Note=Poly-Gln +Q02630 UniProtKB Compositional bias 669 707 . . . Note=Asn-rich +Q02630 UniProtKB Compositional bias 669 672 . . . Note=Poly-Asn +Q02630 UniProtKB Compositional bias 716 740 . . . Note=Gln-rich +Q02630 UniProtKB Compositional bias 729 735 . . . Note=Poly-Gln +Q02630 UniProtKB Modified residue 886 886 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02630 UniProtKB Sequence conflict 26 26 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q02630 UniProtKB Sequence conflict 536 536 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q02630 UniProtKB Sequence conflict 720 720 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q02630 UniProtKB Sequence conflict 1018 1018 . . . Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q02630 UniProtKB Sequence conflict 1023 1023 . . . Note=I->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q02630 UniProtKB Beta strand 970 974 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +Q02630 UniProtKB Helix 976 981 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +Q02630 UniProtKB Beta strand 988 990 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +Q02630 UniProtKB Beta strand 994 997 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +Q02630 UniProtKB Turn 998 1000 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +Q02630 UniProtKB Beta strand 1001 1007 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +Q02630 UniProtKB Turn 1019 1022 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +Q02630 UniProtKB Beta strand 1023 1027 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +Q02630 UniProtKB Beta strand 1030 1034 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +Q02630 UniProtKB Beta strand 1042 1044 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AIV +Q02630 UniProtKB Beta strand 1051 1056 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +Q02630 UniProtKB Turn 1063 1065 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +Q02630 UniProtKB Helix 1075 1084 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +Q02630 UniProtKB Beta strand 1088 1095 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +Q02630 UniProtKB Turn 1097 1099 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +Q02630 UniProtKB Beta strand 1102 1107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +##sequence-region P33895 1 451 +P33895 UniProtKB Chain 1 451 . . . ID=PRO_0000057995;Note=Kinetochore protein NUF2 +P33895 UniProtKB Coiled coil 153 291 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33895 UniProtKB Coiled coil 341 371 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33895 UniProtKB Coiled coil 398 432 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33895 UniProtKB Mutagenesis 338 338 . . . Note=Temperature-sensitive. T->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8188751;Dbxref=PMID:8188751 +P33895 UniProtKB Mutagenesis 340 340 . . . Note=Temperature-sensitive. I->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8188751;Dbxref=PMID:8188751 +P33895 UniProtKB Mutagenesis 383 383 . . . Note=Temperature-sensitive. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8188751;Dbxref=PMID:8188751 +P33895 UniProtKB Mutagenesis 410 410 . . . Note=Temperature-sensitive. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8188751;Dbxref=PMID:8188751 +P33895 UniProtKB Mutagenesis 441 441 . . . Note=Temperature-sensitive. K->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8188751;Dbxref=PMID:8188751 +P33895 UniProtKB Mutagenesis 446 446 . . . Note=Temperature-sensitive. M->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8188751;Dbxref=PMID:8188751 +P33895 UniProtKB Sequence conflict 240 240 . . . Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33895 UniProtKB Beta strand 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P33895 UniProtKB Helix 13 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P33895 UniProtKB Turn 30 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P33895 UniProtKB Helix 40 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P33895 UniProtKB Helix 57 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P33895 UniProtKB Beta strand 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P33895 UniProtKB Helix 79 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P33895 UniProtKB Helix 109 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P33895 UniProtKB Helix 116 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P33895 UniProtKB Helix 407 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +##sequence-region Q12255 1 253 +Q12255 UniProtKB Chain 1 253 . . . ID=PRO_0000206780;Note=Vacuolar v-SNARE NYV1 +Q12255 UniProtKB Topological domain 1 231 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12255 UniProtKB Transmembrane 232 252 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12255 UniProtKB Topological domain 253 253 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12255 UniProtKB Domain 167 227 . . . Note=v-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00290 +Q12255 UniProtKB Beta strand 7 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0 +Q12255 UniProtKB Beta strand 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0 +Q12255 UniProtKB Beta strand 26 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0 +Q12255 UniProtKB Helix 43 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0 +Q12255 UniProtKB Helix 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0 +Q12255 UniProtKB Beta strand 65 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0 +Q12255 UniProtKB Beta strand 74 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0 +Q12255 UniProtKB Beta strand 90 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0 +Q12255 UniProtKB Helix 104 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0 +Q12255 UniProtKB Helix 124 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0 +Q12255 UniProtKB Turn 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FZ0 +##sequence-region P25366 1 362 +P25366 UniProtKB Chain 1 362 . . . ID=PRO_0000202581;Note=Protein OCA4 +##sequence-region P19262 1 463 +P19262 UniProtKB Domain 73 148 . . . Note=Lipoyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066 +P19262 UniProtKB Repeat 185 190 . . . Note=1 +P19262 UniProtKB Repeat 191 196 . . . Note=2 +P19262 UniProtKB Repeat 197 202 . . . Note=3 +P19262 UniProtKB Repeat 204 209 . . . Note=4%3B approximate +P19262 UniProtKB Region 185 209 . . . Note=4 X 6 AA approximate tandem repeats of A-[SP]-K-K-E-[AV] +P19262 UniProtKB Active site 435 435 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19262 UniProtKB Active site 439 439 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19262 UniProtKB Modified residue 114 114 . . . Note=N6-lipoyllysine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066 +P19262 UniProtKB Modified residue 340 340 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P19262 UniProtKB Sequence conflict 170 208 . . . Note=PSQGVAARENSSEETASKKEAAPKKEAAPKKEVTEPKKA->HRKVSPQGKTQVRKRLQRKKLLQRKKPLQRKKLQNQKRT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19262 UniProtKB Sequence conflict 441 445 . . . Note=REAVT->EKLLS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19262 UniProtKB Sequence conflict 460 463 . . . Note=MLLW->CCYGDLKFAAHTNLIS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P12695 1 482 +P12695 UniProtKB Transit peptide 1 28 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3050999;Dbxref=PMID:3050999 +P12695 UniProtKB Chain 29 482 . . . ID=PRO_0000020483;Note=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex%2C mitochondrial +P12695 UniProtKB Domain 34 110 . . . Note=Lipoyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066 +P12695 UniProtKB Domain 175 212 . . . Note=Peripheral subunit-binding (PSBD);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01170 +P12695 UniProtKB Active site 455 455 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12695 UniProtKB Active site 459 459 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12695 UniProtKB Modified residue 75 75 . . . Note=N6-lipoyllysine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU01066,ECO:0000269|PubMed:3050999;Dbxref=PMID:3050999 +##sequence-region P54790 1 616 +P54790 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P54790 UniProtKB Chain 2 616 . . . ID=PRO_0000127086;Note=Origin recognition complex subunit 3 +P54790 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region Q12375 1 292 +Q12375 UniProtKB Chain 1 292 . . . ID=PRO_0000090684;Note=Mitochondrial ornithine transporter 1 +Q12375 UniProtKB Transmembrane 14 34 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12375 UniProtKB Transmembrane 69 89 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12375 UniProtKB Transmembrane 104 124 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12375 UniProtKB Transmembrane 171 187 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12375 UniProtKB Transmembrane 213 233 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12375 UniProtKB Transmembrane 267 287 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12375 UniProtKB Repeat 11 97 . . . Note=Solcar 1 +Q12375 UniProtKB Repeat 105 196 . . . Note=Solcar 2 +Q12375 UniProtKB Repeat 211 292 . . . Note=Solcar 3 +Q12375 UniProtKB Sequence conflict 105 105 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12375 UniProtKB Sequence conflict 105 105 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12375 UniProtKB Sequence conflict 105 105 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P48439 1 350 +P48439 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7622558;Dbxref=PMID:7622558 +P48439 UniProtKB Chain 23 350 . . . ID=PRO_0000020275;Note=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3 +P48439 UniProtKB Transmembrane 186 203 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48439 UniProtKB Transmembrane 218 237 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48439 UniProtKB Transmembrane 272 288 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48439 UniProtKB Transmembrane 310 329 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48439 UniProtKB Domain 29 171 . . . Note=Thioredoxin +P48439 UniProtKB Disulfide bond 73 76 . . . Note=Redox-active;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P05150 1 338 +P05150 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P05150 UniProtKB Chain 2 338 . . . ID=PRO_0000113082;Note=Ornithine carbamoyltransferase +P05150 UniProtKB Region 67 71 . . . Note=Ornithine and carbamoyl phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05150 UniProtKB Region 145 148 . . . Note=Ornithine and carbamoyl phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05150 UniProtKB Region 249 253 . . . Note=Ornithine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05150 UniProtKB Region 288 291 . . . Note=Ornithine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05150 UniProtKB Active site 289 289 . . . . +P05150 UniProtKB Binding site 118 118 . . . Note=Carbamoyl phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05150 UniProtKB Binding site 118 118 . . . Note=Ornithine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05150 UniProtKB Binding site 145 145 . . . Note=Carbamoyl phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05150 UniProtKB Binding site 185 185 . . . Note=Ornithine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05150 UniProtKB Binding site 316 316 . . . Note=Carbamoyl phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05150 UniProtKB Binding site 316 316 . . . Note=Ornithine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05150 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P05150 UniProtKB Mutagenesis 68 68 . . . Note=Reduces activity by 95%25. Reduces affinity for ornithine 2-fold. T->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12679340;Dbxref=PMID:12679340 +P05150 UniProtKB Mutagenesis 181 181 . . . Note=Loss of activity. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12679340;Dbxref=PMID:12679340 +P05150 UniProtKB Mutagenesis 182 182 . . . Note=Reduces activity by 33%25. Reduces affinity for ornithine 30-fold. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12679340;Dbxref=PMID:12679340 +P05150 UniProtKB Mutagenesis 184 184 . . . Note=Reduces activity by 50%25. Reduces affinity for ornithine 20-fold. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12679340;Dbxref=PMID:12679340 +P05150 UniProtKB Mutagenesis 185 185 . . . Note=No effect on activity. Reduces affinity for ornithine 200-fold. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12679340;Dbxref=PMID:12679340 +P05150 UniProtKB Mutagenesis 256 256 . . . Note=Reduces activity by 50%25. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12679340;Dbxref=PMID:12679340 +P05150 UniProtKB Mutagenesis 263 263 . . . Note=Reduces activity by 70%25. Reduces affinity for ornithine 18-fold. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12679340;Dbxref=PMID:12679340 +P05150 UniProtKB Mutagenesis 289 289 . . . Note=Reduces activity by 90%25. Reduces affinity for ornithine 6-fold. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12679340;Dbxref=PMID:12679340 +P05150 UniProtKB Mutagenesis 290 290 . . . Note=Reduces activity by 86%25. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12679340;Dbxref=PMID:12679340 +##sequence-region P52593 1 1655 +P52593 UniProtKB Chain 1 1655 . . . ID=PRO_0000204856;Note=Nucleoporin NUP188 +P52593 UniProtKB Region 250 271 . . . Note=Leucine-zipper +P52593 UniProtKB Coiled coil 35 62 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52593 UniProtKB Compositional bias 485 489 . . . Note=Poly-Ser +P52593 UniProtKB Compositional bias 533 545 . . . Note=Gln-rich +P52593 UniProtKB Compositional bias 533 541 . . . Note=Poly-Gln +P52593 UniProtKB Compositional bias 1385 1391 . . . Note=Poly-Leu +P52593 UniProtKB Compositional bias 1504 1507 . . . Note=Poly-Leu +P52593 UniProtKB Modified residue 340 340 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P52593 UniProtKB Cross-link 406 406 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q02803 1 292 +Q02803 UniProtKB Chain 1 292 . . . ID=PRO_0000220871;Note=Ornithine decarboxylase antizyme +##sequence-region P21957 1 404 +P21957 UniProtKB Chain 1 404 . . . ID=PRO_0000058061;Note=Transcriptional repressor OPI1 +P21957 UniProtKB Region 109 138 . . . Note=Basic motif +P21957 UniProtKB Region 139 160 . . . Note=Leucine-zipper +P21957 UniProtKB Motif 200 206 . . . Note=FFAT +P21957 UniProtKB Compositional bias 89 93 . . . Note=Poly-Asp +P21957 UniProtKB Compositional bias 193 198 . . . Note=Poly-Asp +P21957 UniProtKB Compositional bias 286 298 . . . Note=Poly-Gln +P21957 UniProtKB Compositional bias 306 310 . . . Note=Poly-Gln +P21957 UniProtKB Compositional bias 377 381 . . . Note=Poly-Gln +P21957 UniProtKB Compositional bias 384 387 . . . Note=Poly-Gln +P21957 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P54791 1 529 +P54791 UniProtKB Chain 1 529 . . . ID=PRO_0000127091;Note=Origin recognition complex subunit 4 +P54791 UniProtKB Modified residue 9 9 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P33400 1 625 +P33400 UniProtKB Chain 1 625 . . . ID=PRO_0000046847;Note=pH-response transcription factor pacC/RIM101 +P33400 UniProtKB Zinc finger 146 171 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P33400 UniProtKB Zinc finger 182 206 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P33400 UniProtKB Zinc finger 212 234 . . . Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P33400 UniProtKB Motif 228 234 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33400 UniProtKB Motif 450 453 . . . Note=YPX[LI] motif 1 +P33400 UniProtKB Motif 620 623 . . . Note=YPX[LI] motif 2 +P33400 UniProtKB Compositional bias 76 120 . . . Note=Ser-rich +P33400 UniProtKB Compositional bias 131 140 . . . Note=Poly-Asp +P33400 UniProtKB Compositional bias 579 601 . . . Note=Asp/Glu-rich (acidic) +P33400 UniProtKB Mutagenesis 153 153 . . . Note=Abolishes transcriptional activation of target genes. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8367297;Dbxref=PMID:8367297 +P33400 UniProtKB Mutagenesis 189 189 . . . Note=Abolishes transcriptional activation of target genes. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8367297;Dbxref=PMID:8367297 +P33400 UniProtKB Mutagenesis 217 217 . . . Note=Abolishes transcriptional activation of target genes. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8367297;Dbxref=PMID:8367297 +P33400 UniProtKB Mutagenesis 255 255 . . . Note=Reduces transcriptional activation of target genes. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8367297;Dbxref=PMID:8367297 +P33400 UniProtKB Sequence conflict 68 68 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33400 UniProtKB Sequence conflict 90 90 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33400 UniProtKB Sequence conflict 111 111 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33400 UniProtKB Sequence conflict 249 249 . . . Note=W->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33400 UniProtKB Sequence conflict 261 261 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33400 UniProtKB Sequence conflict 276 276 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33400 UniProtKB Sequence conflict 308 308 . . . Note=Q->QQQQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33400 UniProtKB Sequence conflict 358 358 . . . Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33400 UniProtKB Sequence conflict 486 486 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33400 UniProtKB Sequence conflict 519 519 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38351 1 445 +P38351 UniProtKB Chain 1 445 . . . ID=PRO_0000058174;Note=RNA polymerase II-associated protein 1 +P38351 UniProtKB Compositional bias 363 445 . . . Note=Asp/Glu-rich (acidic) +P38351 UniProtKB Modified residue 147 147 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38351 UniProtKB Modified residue 422 422 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q12033 1 661 +Q12033 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12033 UniProtKB Chain 2 661 . . . ID=PRO_0000218885;Note=pH-response regulator protein palA/RIM20 +Q12033 UniProtKB Domain 3 371 . . . Note=BRO1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00526 +Q12033 UniProtKB Coiled coil 388 422 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12033 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12033 UniProtKB Mutagenesis 292 293 . . . Note=In RIM20-292%3B prevents cleavage of RIM101. DN->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11698381;Dbxref=PMID:11698381 +##sequence-region P37304 1 830 +P37304 UniProtKB Chain 1 830 . . . ID=PRO_0000058220;Note=Protein PAM1 +P37304 UniProtKB Coiled coil 379 400 . . . . +P37304 UniProtKB Coiled coil 481 514 . . . . +P37304 UniProtKB Compositional bias 515 522 . . . Note=Poly-Gln +P37304 UniProtKB Compositional bias 810 830 . . . Note=Arg/Lys-rich (highly basic) +P37304 UniProtKB Modified residue 659 659 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P37304 UniProtKB Modified residue 732 732 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P37304 UniProtKB Modified residue 767 767 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P37304 UniProtKB Sequence conflict 256 256 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53010 1 1115 +P53010 UniProtKB Chain 1 1115 . . . ID=PRO_0000058222;Note=PAN2-PAN3 deadenylation complex catalytic subunit PAN2 +P53010 UniProtKB Repeat 27 66 . . . Note=WD 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03182 +P53010 UniProtKB Repeat 112 153 . . . Note=WD 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03182 +P53010 UniProtKB Repeat 155 194 . . . Note=WD 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03182 +P53010 UniProtKB Repeat 197 236 . . . Note=WD 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03182 +P53010 UniProtKB Repeat 295 334 . . . Note=WD 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03182 +P53010 UniProtKB Domain 474 855 . . . Note=USP;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03182,ECO:0000305|PubMed:24880344;Dbxref=PMID:24880344 +P53010 UniProtKB Domain 907 1079 . . . Note=Exonuclease;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03182 +P53010 UniProtKB Region 337 473 . . . Note=Linker;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03182,ECO:0000305|PubMed:24880344;Dbxref=PMID:24880344 +P53010 UniProtKB Metal binding 660 660 . . . Note=Zinc;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4Q8G,ECO:0000269|PubMed:24880344;Dbxref=PMID:24880344 +P53010 UniProtKB Metal binding 662 662 . . . Note=Zinc%3B via pros nitrogen;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4Q8G,ECO:0000269|PubMed:24880344;Dbxref=PMID:24880344 +P53010 UniProtKB Metal binding 713 713 . . . Note=Zinc;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4Q8G,ECO:0000269|PubMed:24880344;Dbxref=PMID:24880344 +P53010 UniProtKB Metal binding 716 716 . . . Note=Zinc;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4Q8G,ECO:0000269|PubMed:24880344;Dbxref=PMID:24880344 +P53010 UniProtKB Metal binding 910 910 . . . Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000250,ECO:0000255,ECO:0000305;evidence=ECO:0000250|UniProtKB:O95453,ECO:0000255|HAMAP-Rule:MF_03182,ECO:0000305|PubMed:24880344;Dbxref=PMID:24880344 +P53010 UniProtKB Metal binding 912 912 . . . Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000250,ECO:0000255,ECO:0000305;evidence=ECO:0000250|UniProtKB:O95453,ECO:0000255|HAMAP-Rule:MF_03182,ECO:0000305|PubMed:24880344;Dbxref=PMID:24880344 +P53010 UniProtKB Metal binding 1020 1020 . . . Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:O95453,ECO:0000255|HAMAP-Rule:MF_03182 +P53010 UniProtKB Metal binding 1071 1071 . . . Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000250,ECO:0000255,ECO:0000305;evidence=ECO:0000250|UniProtKB:O95453,ECO:0000255|HAMAP-Rule:MF_03182,ECO:0000305|PubMed:24880344;Dbxref=PMID:24880344 +P53010 UniProtKB Mutagenesis 912 912 . . . Note=Abolishes nuclease activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24872509;Dbxref=PMID:24872509 +P53010 UniProtKB Mutagenesis 1020 1020 . . . Note=Abolishes nuclease activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24880344;Dbxref=PMID:24880344 +P53010 UniProtKB Turn 460 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Helix 477 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Helix 488 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Helix 497 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Beta strand 502 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Turn 512 515 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Helix 516 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Helix 527 536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Helix 546 559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Beta strand 560 562 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Helix 568 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Helix 595 600 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Turn 603 605 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Beta strand 610 613 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Helix 618 636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Beta strand 637 639 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Helix 643 648 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Beta strand 650 657 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Beta strand 659 661 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Beta strand 666 675 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Helix 696 703 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Beta strand 704 712 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Turn 714 716 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Beta strand 719 728 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Beta strand 733 739 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Helix 743 751 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Beta strand 752 754 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Beta strand 758 765 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Beta strand 768 774 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Helix 775 777 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Beta strand 782 797 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Beta strand 803 813 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Turn 814 817 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Beta strand 818 825 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Beta strand 828 832 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Helix 834 838 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Beta strand 845 854 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Helix 857 859 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8G +P53010 UniProtKB Helix 865 867 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Helix 873 876 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Helix 897 899 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Beta strand 906 915 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Beta strand 937 946 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Beta strand 948 950 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Turn 951 954 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Beta strand 956 962 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Helix 973 976 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Beta strand 983 986 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Turn 988 990 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Turn 994 996 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Helix 997 1008 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Beta strand 1011 1013 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Helix 1017 1024 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Helix 1030 1032 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Helix 1036 1039 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Helix 1049 1056 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Helix 1068 1087 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +P53010 UniProtKB Helix 1091 1105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q8H +##sequence-region P36102 1 679 +P36102 UniProtKB Chain 1 679 . . . ID=PRO_0000058223;Note=PAN2-PAN3 deadenylation complex subunit PAN3 +P36102 UniProtKB Zinc finger 8 37 . . . Note=C3H1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03181 +P36102 UniProtKB Nucleotide binding 376 383 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03181 +P36102 UniProtKB Nucleotide binding 430 431 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03181 +P36102 UniProtKB Region 275 548 . . . Note=Pseudokinase domain;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03181,ECO:0000305|PubMed:24880344;Dbxref=PMID:24880344 +P36102 UniProtKB Region 588 679 . . . Note=Knob domain;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03181,ECO:0000305|PubMed:24880344;Dbxref=PMID:24880344 +P36102 UniProtKB Coiled coil 549 587 . . . Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03181,ECO:0000305|PubMed:24880344;Dbxref=PMID:24880344 +P36102 UniProtKB Motif 143 163 . . . Note=PABPC-interacting motif-2 (PAM-2);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17595167;Dbxref=PMID:17595167 +P36102 UniProtKB Binding site 325 325 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03181 +P36102 UniProtKB Modified residue 57 57 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36102 UniProtKB Modified residue 252 252 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36102 UniProtKB Mutagenesis 156 156 . . . Note=Significantly decreases interaction with PAN1. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17595167;Dbxref=PMID:17595167 +P36102 UniProtKB Helix 6 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CYK +P36102 UniProtKB Helix 15 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CYK +P36102 UniProtKB Helix 24 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CYK +##sequence-region Q03050 1 120 +Q03050 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03050 UniProtKB Chain 21 120 . . . ID=PRO_0000253888;Note=Seripauperin-10 +##sequence-region P0CE89 1 120 +P0CE89 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE89 UniProtKB Chain 21 120 . . . ID=PRO_0000392929;Note=Seripauperin-14 +P0CE89 UniProtKB Sequence conflict 84 84 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CE88 1 120 +P0CE88 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE88 UniProtKB Chain 21 120 . . . ID=PRO_0000203778;Note=Seripauperin-1 +P0CE88 UniProtKB Sequence conflict 25 25 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0CE88 UniProtKB Sequence conflict 84 84 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0CE88 UniProtKB Sequence conflict 100 100 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0CE88 UniProtKB Sequence conflict 108 108 . . . Note=S->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07987 1 124 +Q07987 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07987 UniProtKB Chain 21 124 . . . ID=PRO_0000033241;Note=Seripauperin-23 +##sequence-region P0CE90 1 120 +P0CE90 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE90 UniProtKB Chain 21 120 . . . ID=PRO_0000203783;Note=Seripauperin-6 +##sequence-region P53298 1 406 +P53298 UniProtKB Chain 1 406 . . . ID=PRO_0000058039;Note=Central kinetochore subunit OKP1 +P53298 UniProtKB Coiled coil 239 285 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53298 UniProtKB Modified residue 70 70 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P28273 1 1286 +P28273 UniProtKB Chain 1 1286 . . . ID=PRO_0000208582;Note=5-oxoprolinase +P28273 UniProtKB Modified residue 930 930 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P28273 UniProtKB Modified residue 1077 1077 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P28273 UniProtKB Mutagenesis 11 11 . . . Note=Impairs ATPase and 5-oxoprolinase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20402795;Dbxref=PMID:20402795 +P28273 UniProtKB Mutagenesis 324 324 . . . Note=Impairs ATPase and 5-oxoprolinase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20402795;Dbxref=PMID:20402795 +P28273 UniProtKB Mutagenesis 497 497 . . . Note=Impairs ATPase and 5-oxoprolinase activity%3B when associated with A-498. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20402795;Dbxref=PMID:20402795 +P28273 UniProtKB Mutagenesis 498 498 . . . Note=Impairs ATPase and 5-oxoprolinase activity%3B when associated with A-497. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20402795;Dbxref=PMID:20402795 +##sequence-region P40897 1 799 +P40897 UniProtKB Chain 1 799 . . . ID=PRO_0000213788;Note=Oligopeptide transporter 1 +P40897 UniProtKB Topological domain 1 108 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Transmembrane 109 129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Topological domain 130 135 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Topological domain 157 177 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Transmembrane 178 198 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Topological domain 199 210 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Transmembrane 211 231 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Topological domain 232 276 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Transmembrane 277 297 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Topological domain 298 313 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Transmembrane 314 334 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Topological domain 335 359 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Transmembrane 360 380 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Topological domain 381 428 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Transmembrane 429 449 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Topological domain 450 482 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Transmembrane 483 503 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Topological domain 504 508 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Transmembrane 509 529 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Topological domain 530 540 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Transmembrane 541 561 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Topological domain 562 590 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Transmembrane 591 611 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Topological domain 612 659 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Transmembrane 660 680 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Topological domain 681 736 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Transmembrane 737 757 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Topological domain 758 799 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Modified residue 48 48 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40897 UniProtKB Modified residue 50 50 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40897 UniProtKB Modified residue 51 51 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40897 UniProtKB Glycosylation 46 46 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40897 UniProtKB Glycosylation 640 640 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32833 1 620 +P32833 UniProtKB Chain 1 620 . . . ID=PRO_0000127082;Note=Origin recognition complex subunit 2 +P32833 UniProtKB Modified residue 60 60 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32833 UniProtKB Modified residue 187 187 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32833 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P33751 1 242 +P33751 UniProtKB Transit peptide 1 58 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03197 +P33751 UniProtKB Chain 59 242 . . . ID=PRO_0000134984;Note=Flavin prenyltransferase PAD1%2C mitochondrial;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03197 +P33751 UniProtKB Nucleotide binding 63 65 . . . Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03197 +P33751 UniProtKB Nucleotide binding 140 143 . . . Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03197 +P33751 UniProtKB Binding site 89 89 . . . Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03197 +P33751 UniProtKB Binding site 175 175 . . . Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03197 +P33751 UniProtKB Binding site 205 205 . . . Note=DMAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03197 +P33751 UniProtKB Binding site 221 221 . . . Note=DMAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03197 +P33751 UniProtKB Sequence conflict 76 76 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32567 1 862 +P32567 UniProtKB Chain 1 862 . . . ID=PRO_0000209887;Note=Phosphatidic acid phosphohydrolase 1 +P32567 UniProtKB Region 19 104 . . . Note=N-LIP +P32567 UniProtKB Motif 398 402 . . . Note=DXDXT motif +P32567 UniProtKB Modified residue 110 110 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16968695;Dbxref=PMID:16968695 +P32567 UniProtKB Modified residue 114 114 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16968695;Dbxref=PMID:16968695 +P32567 UniProtKB Modified residue 168 168 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16968695;Dbxref=PMID:16968695 +P32567 UniProtKB Modified residue 511 511 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32567 UniProtKB Modified residue 602 602 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:16968695,ECO:0000269|PubMed:21081492;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:16968695,PMID:21081492 +P32567 UniProtKB Modified residue 723 723 . . . Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16968695,ECO:0000269|PubMed:21081492;Dbxref=PMID:16968695,PMID:21081492 +P32567 UniProtKB Modified residue 744 744 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:16968695,ECO:0000269|PubMed:21081492;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:16968695,PMID:21081492 +P32567 UniProtKB Modified residue 748 748 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:16968695;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:16968695 +P32567 UniProtKB Modified residue 773 773 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32567 UniProtKB Modified residue 774 774 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32567 UniProtKB Modified residue 810 810 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32567 UniProtKB Modified residue 814 814 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32567 UniProtKB Modified residue 816 816 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32567 UniProtKB Modified residue 844 844 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32567 UniProtKB Modified residue 847 847 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32567 UniProtKB Mutagenesis 8 8 . . . Note=Impairs membrane recruitiment%3B when associated with A-11 and A-15. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20876142;Dbxref=PMID:20876142 +P32567 UniProtKB Mutagenesis 11 11 . . . Note=Impairs membrane recruitiment%3B when associated with A-8 and A-15. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20876142;Dbxref=PMID:20876142 +P32567 UniProtKB Mutagenesis 15 15 . . . Note=Impairs membrane recruitiment%3B when associated with A-8 and A-11. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20876142;Dbxref=PMID:20876142 +P32567 UniProtKB Mutagenesis 80 80 . . . Note=Impairs phosphatidate phosphatase activity. G->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17971454,ECO:0000269|PubMed:21422231;Dbxref=PMID:17971454,PMID:21422231 +P32567 UniProtKB Mutagenesis 398 398 . . . Note=Impairs phosphatidate phosphatase activity. D->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17971454,ECO:0000269|PubMed:21422231;Dbxref=PMID:17971454,PMID:21422231 +P32567 UniProtKB Mutagenesis 400 400 . . . Note=Impairs phosphatidate phosphatase activity. D->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17971454,ECO:0000269|PubMed:21422231;Dbxref=PMID:17971454,PMID:21422231 +##sequence-region P36129 1 213 +P36129 UniProtKB Chain 1 213 . . . ID=PRO_0000203208;Note=Putative uncharacterized protein OPI8 +##sequence-region P38826 1 435 +P38826 UniProtKB Chain 1 435 . . . ID=PRO_0000127102;Note=Origin recognition complex subunit 6 +P38826 UniProtKB Modified residue 146 146 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q12447 1 191 +Q12447 UniProtKB Chain 1 191 . . . ID=PRO_0000245843;Note=Polyamine N-acetyltransferase 1 +Q12447 UniProtKB Domain 12 179 . . . Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532 +##sequence-region Q05518 1 499 +Q05518 UniProtKB Chain 1 499 . . . ID=PRO_0000253820;Note=Protein PAL1 +Q05518 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05518 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05518 UniProtKB Modified residue 47 47 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05518 UniProtKB Modified residue 49 49 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05518 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q05518 UniProtKB Modified residue 114 114 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05518 UniProtKB Modified residue 121 121 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05518 UniProtKB Modified residue 153 153 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05518 UniProtKB Modified residue 304 304 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05518 UniProtKB Modified residue 307 307 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05518 UniProtKB Cross-link 135 135 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q05518 UniProtKB Cross-link 138 138 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q05518 UniProtKB Cross-link 292 292 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q05518 UniProtKB Cross-link 328 328 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q05518 UniProtKB Cross-link 445 445 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q05518 UniProtKB Sequence conflict 227 227 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53179 1 542 +P53179 UniProtKB Chain 1 542 . . . ID=PRO_0000058194;Note=pH-response regulator protein palF/RIM8 +P53179 UniProtKB Compositional bias 244 250 . . . Note=Poly-Ser +P53179 UniProtKB Cross-link 521 521 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P48565 1 533 +P48565 UniProtKB Chain 1 533 . . . ID=PRO_0000058205;Note=pH-response regulator protein palH/RIM21 +P48565 UniProtKB Topological domain 1 94 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48565 UniProtKB Transmembrane 95 115 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48565 UniProtKB Topological domain 116 127 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48565 UniProtKB Transmembrane 128 148 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48565 UniProtKB Topological domain 149 178 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48565 UniProtKB Transmembrane 179 199 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48565 UniProtKB Topological domain 200 209 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48565 UniProtKB Transmembrane 210 230 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48565 UniProtKB Topological domain 231 247 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48565 UniProtKB Transmembrane 248 268 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48565 UniProtKB Topological domain 269 280 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48565 UniProtKB Transmembrane 281 301 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48565 UniProtKB Topological domain 302 307 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48565 UniProtKB Transmembrane 308 328 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48565 UniProtKB Topological domain 329 533 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48565 UniProtKB Modified residue 409 409 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q04734 1 239 +Q04734 UniProtKB Chain 1 239 . . . ID=PRO_0000058216;Note=pH-response regulator protein palI/RIM9 +Q04734 UniProtKB Topological domain 1 3 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04734 UniProtKB Transmembrane 4 24 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04734 UniProtKB Topological domain 25 90 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04734 UniProtKB Transmembrane 91 111 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04734 UniProtKB Topological domain 112 128 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04734 UniProtKB Transmembrane 129 149 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04734 UniProtKB Topological domain 150 155 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04734 UniProtKB Transmembrane 156 176 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04734 UniProtKB Topological domain 177 239 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36147 1 197 +P36147 UniProtKB Transit peptide 1 14 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36147 UniProtKB Chain 15 197 . . . ID=PRO_0000043179;Note=Presequence translocated-associated motor subunit PAM17%2C mitochondrial +P36147 UniProtKB Transmembrane 64 84 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36147 UniProtKB Transmembrane 103 123 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32521 1 1480 +P32521 UniProtKB Chain 1 1480 . . . ID=PRO_0000058221;Note=Actin cytoskeleton-regulatory complex protein PAN1 +P32521 UniProtKB Repeat 142 153 . . . Note=1-1 +P32521 UniProtKB Repeat 164 175 . . . Note=1-2 +P32521 UniProtKB Repeat 188 199 . . . Note=1-3 +P32521 UniProtKB Repeat 215 226 . . . Note=1-4 +P32521 UniProtKB Repeat 235 246 . . . Note=1-5 +P32521 UniProtKB Domain 270 359 . . . Note=EH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00077 +P32521 UniProtKB Repeat 328 350 . . . Note=2-1 +P32521 UniProtKB Repeat 392 403 . . . Note=1-6 +P32521 UniProtKB Repeat 409 420 . . . Note=1-7 +P32521 UniProtKB Repeat 422 433 . . . Note=1-8 +P32521 UniProtKB Repeat 446 457 . . . Note=1-9 +P32521 UniProtKB Repeat 467 478 . . . Note=1-10 +P32521 UniProtKB Repeat 498 509 . . . Note=1-11 +P32521 UniProtKB Repeat 510 518 . . . Note=1-12 +P32521 UniProtKB Repeat 538 548 . . . Note=1-13 +P32521 UniProtKB Repeat 549 556 . . . Note=1-14 +P32521 UniProtKB Repeat 564 575 . . . Note=1-15 +P32521 UniProtKB Domain 600 689 . . . Note=EH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00077 +P32521 UniProtKB Repeat 658 680 . . . Note=2-2 +P32521 UniProtKB Repeat 1084 1089 . . . Note=3-1 +P32521 UniProtKB Repeat 1090 1095 . . . Note=3-2 +P32521 UniProtKB Repeat 1096 1101 . . . Note=3-3 +P32521 UniProtKB Repeat 1102 1107 . . . Note=3-4 +P32521 UniProtKB Repeat 1108 1113 . . . Note=3-5 +P32521 UniProtKB Repeat 1114 1119 . . . Note=3-6 +P32521 UniProtKB Repeat 1120 1125 . . . Note=3-7 +P32521 UniProtKB Repeat 1315 1320 . . . Note=4-1 +P32521 UniProtKB Repeat 1321 1326 . . . Note=4-2 +P32521 UniProtKB Repeat 1327 1332 . . . Note=4-3 +P32521 UniProtKB Repeat 1340 1345 . . . Note=4-4 +P32521 UniProtKB Repeat 1346 1350 . . . Note=4-5 +P32521 UniProtKB Repeat 1355 1360 . . . Note=4-6 +P32521 UniProtKB Repeat 1361 1366 . . . Note=4-7 +P32521 UniProtKB Repeat 1372 1377 . . . Note=4-8 +P32521 UniProtKB Region 142 575 . . . Note=15 X 12 AA tandem repeats of [SPNAG]-[IL]-[QKNGT]-[PSA]-[QT]-[GQAPISTLYK]-T-G-[YFGML]-[YVMGAQL]-[QVLNPAG]-[ASQPN] +P32521 UniProtKB Region 328 680 . . . Note=2 X 23 AA repeats of F-A-L-[AG]-M-H-L-[IV]-[NY]-[DG]-[VK]-L-[QN]-G-[DK]-[TP]-I-P-[YN]-[EV]-L-[DP]-S +P32521 UniProtKB Region 1084 1125 . . . Note=7 X 6 AA tandem repeats of Q-[PS]-T-Q-P-V +P32521 UniProtKB Region 1315 1377 . . . Note=8 X 6 AA repeats of [ATVSP]-P-[LVI]-P-[SPQILA]-[VAS] +P32521 UniProtKB Coiled coil 1131 1190 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32521 UniProtKB Compositional bias 13 22 . . . Note=Poly-Gln +P32521 UniProtKB Compositional bias 29 34 . . . Note=Poly-Gln +P32521 UniProtKB Compositional bias 98 106 . . . Note=Poly-Gln +P32521 UniProtKB Compositional bias 1400 1406 . . . Note=Poly-Pro +P32521 UniProtKB Compositional bias 1452 1455 . . . Note=Poly-Glu +P32521 UniProtKB Compositional bias 1474 1480 . . . Note=Poly-Pro +P32521 UniProtKB Modified residue 241 241 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32521 UniProtKB Modified residue 570 570 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32521 UniProtKB Modified residue 747 747 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32521 UniProtKB Modified residue 757 757 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32521 UniProtKB Modified residue 993 993 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32521 UniProtKB Modified residue 995 995 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P32521 UniProtKB Modified residue 1003 1003 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32521 UniProtKB Modified residue 1180 1180 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32521 UniProtKB Modified residue 1250 1250 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32521 UniProtKB Modified residue 1253 1253 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32521 UniProtKB Modified residue 1281 1281 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32521 UniProtKB Modified residue 1321 1321 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32521 UniProtKB Sequence conflict 235 235 . . . Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32521 UniProtKB Sequence conflict 266 273 . . . Note=ITAQDQAK->YYCPRSGKN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32521 UniProtKB Sequence conflict 474 487 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32521 UniProtKB Sequence conflict 653 657 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32521 UniProtKB Sequence conflict 1291 1291 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32521 UniProtKB Sequence conflict 1396 1480 . . . Note=GGVLPPPPPLPTQQASTSEPIIAHVDNYNGAEKGTGAYGSDSDDDVLSIPESVGTDEEEEGAQPVSTAGIPSIPPAGIPPPPPLP->EAFCLHPHLYQLNKLPLQNLLSLTLITTMVLKKARAHMDPILMMTFYRFLNQLVQMKRKKGHNQFLLQVSHQFHLQVFLHPHPFHEDLICFL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40459 1 309 +P40459 UniProtKB Chain 1 309 . . . ID=PRO_0000128298;Note=Pantoate--beta-alanine ligase +##sequence-region Q08202 1 246 +Q08202 UniProtKB Chain 1 246 . . . ID=PRO_0000245260;Note=Protein OPI10 +##sequence-region O94084 1 285 +O94084 UniProtKB Chain 1 285 . . . ID=PRO_0000299778;Note=Putative uncharacterized protein OPI9 +O94084 UniProtKB Transmembrane 197 217 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O94084 UniProtKB Compositional bias 10 141 . . . Note=Gly-rich +O94084 UniProtKB Compositional bias 232 250 . . . Note=Gly-rich +##sequence-region P54964 1 269 +P54964 UniProtKB Domain 55 227 . . . Note=Exonuclease +P54964 UniProtKB Active site 184 184 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54964 UniProtKB Sequence conflict 100 100 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54964 UniProtKB Sequence conflict 124 127 . . . Note=GLTA->ESHP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54964 UniProtKB Sequence conflict 181 181 . . . Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P54964 UniProtKB Sequence conflict 223 269 . . . Note=SIAQLQWYMDNYLKPPQETESVESIGSEQPESPSSSTSSLKRQRTDF->HSSIAMVHGQLLEATTGNRVGRVNRI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12451 1 1283 +Q12451 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q12451 UniProtKB Chain 2 1283 . . . ID=PRO_0000100388;Note=Oxysterol-binding protein homolog 2 +Q12451 UniProtKB Repeat 106 134 . . . Note=ANK 1 +Q12451 UniProtKB Repeat 206 235 . . . Note=ANK 2 +Q12451 UniProtKB Domain 289 386 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +Q12451 UniProtKB Motif 745 751 . . . Note=FFAT +Q12451 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q12451 UniProtKB Modified residue 7 7 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q12451 UniProtKB Modified residue 422 422 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +Q12451 UniProtKB Modified residue 445 445 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12451 UniProtKB Modified residue 451 451 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12451 UniProtKB Modified residue 455 455 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12451 UniProtKB Modified residue 458 458 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12451 UniProtKB Modified residue 459 459 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12451 UniProtKB Modified residue 486 486 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12451 UniProtKB Modified residue 488 488 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12451 UniProtKB Modified residue 512 512 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12451 UniProtKB Modified residue 515 515 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12451 UniProtKB Modified residue 717 717 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12451 UniProtKB Modified residue 783 783 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12451 UniProtKB Modified residue 787 787 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12451 UniProtKB Modified residue 825 825 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12451 UniProtKB Modified residue 1151 1151 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q02201 1 448 +Q02201 UniProtKB Chain 1 448 . . . ID=PRO_0000100390;Note=Oxysterol-binding protein homolog 6 +Q02201 UniProtKB Region 64 69 . . . Note=Phosphatidylinositol 4-phosphate binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4PH7,ECO:0000269|PubMed:26206936;Dbxref=PMID:26206936 +Q02201 UniProtKB Region 64 69 . . . Note=Phosphatidylserine binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4B2Z,ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110 +Q02201 UniProtKB Region 126 129 . . . Note=Phosphatidylinositol 4-phosphate binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4PH7,ECO:0000269|PubMed:26206936;Dbxref=PMID:26206936 +Q02201 UniProtKB Region 157 158 . . . Note=Phosphatidylinositol 4-phosphate binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4PH7,ECO:0000269|PubMed:26206936;Dbxref=PMID:26206936 +Q02201 UniProtKB Binding site 129 129 . . . Note=Phosphatidylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4B2Z,ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110 +Q02201 UniProtKB Binding site 183 183 . . . Note=Phosphatidylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4B2Z,ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110 +Q02201 UniProtKB Binding site 351 351 . . . Note=Phosphatidylinositol 4-phosphate;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4PH7,ECO:0000269|PubMed:26206936;Dbxref=PMID:26206936 +Q02201 UniProtKB Binding site 355 355 . . . Note=Phosphatidylinositol 4-phosphate;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4PH7,ECO:0000269|PubMed:26206936;Dbxref=PMID:26206936 +Q02201 UniProtKB Binding site 359 359 . . . Note=Phosphatidylinositol 4-phosphate;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4PH7,ECO:0000269|PubMed:26206936;Dbxref=PMID:26206936 +Q02201 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q02201 UniProtKB Mutagenesis 69 69 . . . Note=Strongly reduced binding to phosphatidylserine. L->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110 +Q02201 UniProtKB Mutagenesis 69 69 . . . Note=Strongly reduced binding to phosphatidylserine and phosphatidylinositol 4-phosphate (PI4P). L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26206936;Dbxref=PMID:26206936 +Q02201 UniProtKB Mutagenesis 69 69 . . . Note=Does not affect binding to phosphatidylserine. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110 +Q02201 UniProtKB Mutagenesis 71 71 . . . Note=Abolished binding to phosphatidylserine. T->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110 +Q02201 UniProtKB Mutagenesis 73 73 . . . Note=Strongly reduced binding to phosphatidylserine. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110 +Q02201 UniProtKB Mutagenesis 126 126 . . . Note=Strongly reduced binding to phosphatidylserine. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110 +Q02201 UniProtKB Mutagenesis 129 129 . . . Note=Strongly reduced binding to phosphatidylserine. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110 +Q02201 UniProtKB Mutagenesis 157 158 . . . Note=Strongly reduced binding to phosphatidylinositol 4-phosphate (PI4P). Does not affect binding to phosphatidylserine. HH->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26206936;Dbxref=PMID:26206936 +Q02201 UniProtKB Mutagenesis 157 157 . . . Note=Does not affect binding to phosphatidylserine. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110 +Q02201 UniProtKB Mutagenesis 158 158 . . . Note=Does not affect binding to phosphatidylserine. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110 +Q02201 UniProtKB Mutagenesis 182 182 . . . Note=Does not affect binding to phosphatidylserine. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110 +Q02201 UniProtKB Mutagenesis 351 351 . . . Note=Does not affect binding to phosphatidylserine. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23934110;Dbxref=PMID:23934110 +Q02201 UniProtKB Mutagenesis 351 351 . . . Note=Strongly reduced binding to phosphatidylinositol 4-phosphate (PI4P). Does not affect binding to phosphatidylserine. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26206936;Dbxref=PMID:26206936 +Q02201 UniProtKB Helix 37 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Helix 45 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Helix 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 74 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Helix 79 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Helix 90 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Helix 102 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Turn 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 126 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 135 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 147 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Turn 157 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 161 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Helix 169 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 173 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 181 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 187 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 197 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 210 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 222 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 227 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 233 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 238 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 248 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 258 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 263 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 277 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 287 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 302 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Turn 307 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Helix 320 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Helix 328 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Helix 333 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Helix 344 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 375 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Beta strand 387 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Helix 400 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Helix 421 424 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Helix 427 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B2Z +Q02201 UniProtKB Helix 436 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PH7 +##sequence-region P38122 1 312 +P38122 UniProtKB Chain 1 312 . . . ID=PRO_0000184927;Note=3-methyl-2-oxobutanoate hydroxymethyltransferase +##sequence-region P50946 1 238 +P50946 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P50946 UniProtKB Chain 2 238 . . . ID=PRO_0000203439;Note=Putative tyrosine-protein phosphatase OCA1 +P50946 UniProtKB Active site 168 168 . . . Note=Phosphocysteine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50946 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P50946 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P50946 UniProtKB Natural variant 66 66 . . . Note=In strain: SK1. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +##sequence-region P36163 1 345 +P36163 UniProtKB Chain 1 345 . . . ID=PRO_0000203225;Note=Mitochondrial metalloendopeptidase OMA1 +P36163 UniProtKB Topological domain 1 67 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36163 UniProtKB Transmembrane 68 88 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36163 UniProtKB Topological domain 89 223 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36163 UniProtKB Transmembrane 224 244 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36163 UniProtKB Topological domain 245 345 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36163 UniProtKB Active site 204 204 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P36163 UniProtKB Metal binding 203 203 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P36163 UniProtKB Metal binding 207 207 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P36163 UniProtKB Metal binding 257 257 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P36163 UniProtKB Mutagenesis 204 204 . . . Note=Loss of protease activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12963738;Dbxref=PMID:12963738 +P36163 UniProtKB Mutagenesis 207 207 . . . Note=Loss of protease activity. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12963738;Dbxref=PMID:12963738 +P36163 UniProtKB Mutagenesis 212 212 . . . Note=Loss of protease activity. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12963738;Dbxref=PMID:12963738 +##sequence-region P33767 1 430 +P33767 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33767 UniProtKB Chain 21 430 . . . ID=PRO_0000021961;Note=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1 +P33767 UniProtKB Topological domain 21 393 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33767 UniProtKB Transmembrane 394 414 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33767 UniProtKB Topological domain 415 430 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33767 UniProtKB Glycosylation 60 60 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33767 UniProtKB Glycosylation 332 332 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12202 1 724 +Q12202 UniProtKB Chain 1 724 . . . ID=PRO_0000076276;Note=Outer spore wall protein 2 +##sequence-region P43611 1 510 +P43611 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43611 UniProtKB Chain 24 510 . . . ID=PRO_0000202694;Note=Outer spore wall protein 7 +P43611 UniProtKB Modified residue 354 354 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region P32263 1 286 +P32263 UniProtKB Chain 1 286 . . . ID=PRO_0000187328;Note=Pyrroline-5-carboxylate reductase +P32263 UniProtKB Modified residue 246 246 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32263 UniProtKB Modified residue 279 279 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32263 UniProtKB Cross-link 171 171 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P40960 1 533 +P40960 UniProtKB Chain 1 533 . . . ID=PRO_0000051114;Note=WD repeat-containing protein PAC11 +P40960 UniProtKB Repeat 380 422 . . . Note=WD 1 +P40960 UniProtKB Repeat 432 475 . . . Note=WD 2 +P40960 UniProtKB Sequence conflict 140 140 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40960 UniProtKB Beta strand 76 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HT6 +##sequence-region P39937 1 518 +P39937 UniProtKB Chain 1 518 . . . ID=PRO_0000083526;Note=Protein PAC2 +P39937 UniProtKB Domain 23 67 . . . Note=CAP-Gly;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00045 +P39937 UniProtKB Repeat 153 174 . . . Note=LRR 1 +P39937 UniProtKB Repeat 179 201 . . . Note=LRR 2 +P39937 UniProtKB Repeat 204 227 . . . Note=LRR 3 +P39937 UniProtKB Repeat 229 252 . . . Note=LRR 4 +P39937 UniProtKB Repeat 255 276 . . . Note=LRR 5 +P39937 UniProtKB Repeat 277 298 . . . Note=LRR 6 +P39937 UniProtKB Repeat 299 319 . . . Note=LRR 7 +P39937 UniProtKB Repeat 324 345 . . . Note=LRR 8 +##sequence-region P41543 1 476 +P41543 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7860628;Dbxref=PMID:7860628 +P41543 UniProtKB Chain 23 476 . . . ID=PRO_0000021960;Note=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 +P41543 UniProtKB Topological domain 23 449 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41543 UniProtKB Transmembrane 450 470 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41543 UniProtKB Topological domain 471 476 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41543 UniProtKB Glycosylation 18 18 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41543 UniProtKB Glycosylation 99 99 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41543 UniProtKB Glycosylation 217 217 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41543 UniProtKB Glycosylation 336 336 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41543 UniProtKB Glycosylation 400 400 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P46964 1 130 +P46964 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7593165;Dbxref=PMID:7593165 +P46964 UniProtKB Chain 2 130 . . . ID=PRO_0000124032;Note=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2 +P46964 UniProtKB Topological domain 2 46 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46964 UniProtKB Transmembrane 47 67 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46964 UniProtKB Topological domain 68 71 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46964 UniProtKB Transmembrane 72 92 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46964 UniProtKB Topological domain 93 109 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46964 UniProtKB Transmembrane 110 130 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46964 UniProtKB Mutagenesis 16 16 . . . Note=In OST2-3%3B ts%3B reduced activity. S->P +P46964 UniProtKB Mutagenesis 25 25 . . . Note=In OST2-3%3B ts%3B reduced activity. E->G +P46964 UniProtKB Mutagenesis 31 31 . . . Note=In OST2-1%3B ts%3B reduced activity. K->M +P46964 UniProtKB Mutagenesis 48 48 . . . Note=In OST2-2%3B ts%3B reduced activity. D->V +P46964 UniProtKB Mutagenesis 61 61 . . . Note=In OST2-3%3B ts%3B reduced activity. Q->R +P46964 UniProtKB Mutagenesis 62 62 . . . Note=In OST2-1%3B ts%3B reduced activity. C->S +P46964 UniProtKB Mutagenesis 69 69 . . . Note=In OST2-6%3B ts%3B reduced activity. R->C +P46964 UniProtKB Mutagenesis 80 80 . . . Note=In OST2-1%3B ts%3B reduced activity. G->E +P46964 UniProtKB Mutagenesis 86 86 . . . Note=In OST2-4%3B ts%3B reduced activity. G->R +P46964 UniProtKB Mutagenesis 112 112 . . . Note=In OST2-6%3B ts%3B reduced activity. A->S +P46964 UniProtKB Mutagenesis 113 113 . . . Note=In OST2-6%3B ts%3B reduced activity. E->K +P46964 UniProtKB Mutagenesis 113 113 . . . Note=In OST2-5%3B ts%3B reduced activity. E->V +P46964 UniProtKB Mutagenesis 119 119 . . . Note=In OST2-2%3B ts%3B reduced activity. L->S +P46964 UniProtKB Mutagenesis 123 123 . . . Note=In OST2-2%3B ts%3B reduced activity. F->L +P46964 UniProtKB Mutagenesis 127 127 . . . Note=In OST2-1%3B ts%3B reduced activity. H->Y +##sequence-region Q08952 1 273 +Q08952 UniProtKB Chain 1 273 . . . ID=PRO_0000058123;Note=Oxidation resistance protein 1 +Q08952 UniProtKB Domain 100 273 . . . Note=TLD +Q08952 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q08952 UniProtKB Modified residue 178 178 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P41816 1 400 +P41816 UniProtKB Chain 1 400 . . . ID=PRO_0000194475;Note=NADPH dehydrogenase 3 +P41816 UniProtKB Active site 197 197 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41816 UniProtKB Binding site 38 38 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41816 UniProtKB Binding site 192 192 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41816 UniProtKB Binding site 192 192 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41816 UniProtKB Binding site 195 195 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41816 UniProtKB Binding site 244 244 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41816 UniProtKB Binding site 349 349 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41816 UniProtKB Binding site 376 376 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41816 UniProtKB Sequence conflict 78 78 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38725 1 120 +P38725 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38725 UniProtKB Chain 26 120 . . . ID=PRO_0000033245;Note=Seripauperin-13 +##sequence-region P0CE91 1 120 +P0CE91 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE91 UniProtKB Chain 21 120 . . . ID=PRO_0000392930;Note=Seripauperin-18 +##sequence-region P0CE87 1 164 +P0CE87 UniProtKB Chain 1 164 . . . ID=PRO_0000392932;Note=Seripauperin-22 +P0CE87 UniProtKB Alternative sequence 1 40 . . . ID=VSP_038856;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25610 1 124 +P25610 UniProtKB Chain 1 124 . . . ID=PRO_0000203780;Note=Seripauperin-3 +P25610 UniProtKB Transmembrane 7 24 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25610 UniProtKB Sequence conflict 64 64 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40091 1 420 +P40091 UniProtKB Chain 1 420 . . . ID=PRO_0000058300;Note=Protein PEA2 +P40091 UniProtKB Modified residue 230 230 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40091 UniProtKB Natural variant 90 90 . . . Note=In strain: CLIB 219. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P40091 UniProtKB Natural variant 117 117 . . . Note=In strain: CLIB 630. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P40091 UniProtKB Natural variant 157 157 . . . Note=In strain: CLIB 219. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P40091 UniProtKB Natural variant 161 161 . . . Note=In strain: CLIB 630. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P40091 UniProtKB Natural variant 165 165 . . . Note=In strain: CLIB 630. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P40091 UniProtKB Natural variant 171 171 . . . Note=In strain: CLIB 630. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P40091 UniProtKB Natural variant 189 189 . . . Note=In strain: CLIB 382. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P40091 UniProtKB Natural variant 210 210 . . . Note=In strain: CLIB 413 haplotype Ha2. I->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P40091 UniProtKB Natural variant 249 249 . . . Note=In strain: CLIB 556. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P40091 UniProtKB Natural variant 253 253 . . . Note=In strain: Sigma 1278B. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P40091 UniProtKB Natural variant 325 325 . . . Note=In strain: CLIB 219. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P40091 UniProtKB Natural variant 355 355 . . . Note=In strain: R12. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P40091 UniProtKB Natural variant 384 384 . . . Note=In strain: CLIB 219. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P40091 UniProtKB Natural variant 409 409 . . . Note=In strain: CLIB 410%2C CLIB 413 and Sigma 1278B. L->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +##sequence-region P25625 1 357 +P25625 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25625 UniProtKB Chain 22 357 . . . ID=PRO_0000202569;Note=Protein PER1 +P25625 UniProtKB Topological domain 23 113 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25625 UniProtKB Transmembrane 114 134 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25625 UniProtKB Topological domain 135 155 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25625 UniProtKB Transmembrane 156 176 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25625 UniProtKB Topological domain 177 189 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25625 UniProtKB Transmembrane 190 210 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25625 UniProtKB Topological domain 211 212 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25625 UniProtKB Transmembrane 213 233 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25625 UniProtKB Topological domain 234 248 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25625 UniProtKB Transmembrane 249 269 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25625 UniProtKB Topological domain 270 293 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25625 UniProtKB Transmembrane 294 314 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25625 UniProtKB Topological domain 315 324 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25625 UniProtKB Transmembrane 325 345 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25625 UniProtKB Topological domain 346 357 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12144 1 273 +Q12144 UniProtKB Chain 1 273 . . . ID=PRO_0000247231;Note=Pore and endoplasmic reticulum protein of 33 kDa +Q12144 UniProtKB Topological domain 1 24 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12144 UniProtKB Transmembrane 25 45 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12144 UniProtKB Topological domain 46 56 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12144 UniProtKB Transmembrane 57 74 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12144 UniProtKB Topological domain 75 98 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12144 UniProtKB Transmembrane 99 119 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12144 UniProtKB Topological domain 120 126 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12144 UniProtKB Transmembrane 127 147 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12144 UniProtKB Topological domain 148 176 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12144 UniProtKB Transmembrane 177 197 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12144 UniProtKB Topological domain 198 199 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12144 UniProtKB Transmembrane 200 220 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12144 UniProtKB Topological domain 221 273 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q92316 1 86 +Q92316 UniProtKB Chain 1 86 . . . ID=PRO_0000058099;Note=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST5 +Q92316 UniProtKB Topological domain 1 27 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q92316 UniProtKB Transmembrane 28 48 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q92316 UniProtKB Transmembrane 57 77 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q92316 UniProtKB Topological domain 78 86 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q92316 UniProtKB Sequence conflict 46 46 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40219 1 148 +P40219 UniProtKB Chain 1 148 . . . ID=PRO_0000203308;Note=Outer spore wall protein 5 +P40219 UniProtKB Topological domain 1 7 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40219 UniProtKB Transmembrane 8 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40219 UniProtKB Topological domain 29 29 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40219 UniProtKB Transmembrane 30 50 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40219 UniProtKB Topological domain 51 148 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40219 UniProtKB Modified residue 102 102 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P39952 1 402 +P39952 UniProtKB Transit peptide 1 42 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9171337;Dbxref=PMID:9171337 +P39952 UniProtKB Chain 43 402 . . . ID=PRO_0000020362;Note=Mitochondrial inner membrane protein OXA1 +P39952 UniProtKB Topological domain 43 118 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9171337;Dbxref=PMID:9171337 +P39952 UniProtKB Transmembrane 119 139 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39952 UniProtKB Topological domain 140 199 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39952 UniProtKB Transmembrane 200 220 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39952 UniProtKB Topological domain 221 239 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39952 UniProtKB Transmembrane 240 260 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39952 UniProtKB Topological domain 261 275 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39952 UniProtKB Transmembrane 276 292 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39952 UniProtKB Topological domain 293 297 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39952 UniProtKB Transmembrane 298 316 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39952 UniProtKB Topological domain 317 402 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39952 UniProtKB Mutagenesis 128 128 . . . Note=Leads to respiratory deficiency. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20025673;Dbxref=PMID:20025673 +P39952 UniProtKB Mutagenesis 129 129 . . . Note=Leads to a defect in complex V assembly and subsequent respiratory deficiency. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20025673;Dbxref=PMID:20025673 +P39952 UniProtKB Mutagenesis 213 213 . . . Note=Leads to a defect in complex V assembly and subsequent respiratory deficiency. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20025673;Dbxref=PMID:20025673 +P39952 UniProtKB Mutagenesis 229 229 . . . Note=Leads to a defect in complexes IV and V assembly%2C and subsequent respiratory deficiency. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20025673;Dbxref=PMID:20025673 +P39952 UniProtKB Mutagenesis 240 240 . . . Note=Leads to a defect in complex IV assembly and subsequent respiratory deficiency. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20025673;Dbxref=PMID:20025673 +P39952 UniProtKB Mutagenesis 249 249 . . . Note=Leads to respiratory deficiency. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20025673;Dbxref=PMID:20025673 +P39952 UniProtKB Mutagenesis 250 250 . . . Note=Leads to respiratory deficiency. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20025673;Dbxref=PMID:20025673 +P39952 UniProtKB Mutagenesis 300 300 . . . Note=Leads to a defect in complex V assembly and subsequent respiratory deficiency. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20025673;Dbxref=PMID:20025673 +P39952 UniProtKB Mutagenesis 301 301 . . . Note=Leads to respiratory deficiency. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20025673;Dbxref=PMID:20025673 +P39952 UniProtKB Sequence conflict 108 108 . . . Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03558 1 400 +Q03558 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8454584;Dbxref=PMID:8454584 +Q03558 UniProtKB Chain 2 400 . . . ID=PRO_0000194474;Note=NADPH dehydrogenase 2 +Q03558 UniProtKB Active site 197 197 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03558 UniProtKB Binding site 38 38 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03558 UniProtKB Binding site 192 192 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03558 UniProtKB Binding site 192 192 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03558 UniProtKB Binding site 195 195 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03558 UniProtKB Binding site 244 244 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03558 UniProtKB Binding site 349 349 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03558 UniProtKB Binding site 376 376 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03558 UniProtKB Modified residue 353 353 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03558 UniProtKB Modified residue 379 379 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03558 UniProtKB Sequence conflict 90 90 . . . Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04430 1 367 +Q04430 UniProtKB Chain 1 367 . . . ID=PRO_0000253828;Note=Pantothenate kinase CAB1 +Q04430 UniProtKB Mutagenesis 351 351 . . . Note=Leads to thermo-sensitivity. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19266201;Dbxref=PMID:19266201 +##sequence-region P25644 1 796 +P25644 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P25644 UniProtKB Chain 2 796 . . . ID=PRO_0000058235;Note=DNA topoisomerase 2-associated protein PAT1 +P25644 UniProtKB Compositional bias 114 235 . . . Note=Pro-rich +P25644 UniProtKB Compositional bias 133 192 . . . Note=Gln-rich +P25644 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P25644 UniProtKB Modified residue 456 456 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25644 UniProtKB Modified residue 457 457 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25644 UniProtKB Sequence conflict 688 688 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25644 UniProtKB Helix 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BRW +P25644 UniProtKB Helix 38 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BRW +P25644 UniProtKB Helix 475 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Helix 505 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Turn 511 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Beta strand 517 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Helix 522 526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Helix 530 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Helix 536 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Helix 545 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Helix 559 561 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Helix 563 568 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Turn 570 572 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Helix 578 599 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Beta strand 600 602 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Helix 605 617 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Helix 621 625 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Helix 628 642 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Turn 650 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJJ +P25644 UniProtKB Helix 656 673 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Helix 677 680 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Helix 684 693 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Helix 702 713 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Helix 717 726 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Helix 728 749 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Beta strand 751 753 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJJ +P25644 UniProtKB Helix 756 782 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Beta strand 785 788 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +P25644 UniProtKB Beta strand 791 794 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OGP +##sequence-region P35994 1 123 +P35994 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35994 UniProtKB Chain 21 123 . . . ID=PRO_0000033247;Note=Seripauperin-16 +##sequence-region P53427 1 120 +P53427 UniProtKB Chain 1 120 . . . ID=PRO_0000203781;Note=Seripauperin-4 +P53427 UniProtKB Transmembrane 7 24 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39545 1 55 +P39545 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39545 UniProtKB Chain 21 55 . . . ID=PRO_0000203784;Note=Seripauperin-7 +##sequence-region Q12524 1 340 +Q12524 UniProtKB Transit peptide 1 7 . . . Note=Peroxisome;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10922370;Dbxref=PMID:10922370 +Q12524 UniProtKB Chain 8 340 . . . ID=PRO_0000036186;Note=Peroxisomal coenzyme A diphosphatase 1%2C peroxisomal +Q12524 UniProtKB Domain 37 199 . . . Note=Nudix hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00794 +Q12524 UniProtKB Motif 77 99 . . . Note=Nudix box +Q12524 UniProtKB Metal binding 93 93 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12524 UniProtKB Metal binding 97 97 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38126 1 564 +P38126 UniProtKB Chain 1 564 . . . ID=PRO_0000084789;Note=Pachytene checkpoint protein 2 +P38126 UniProtKB Nucleotide binding 314 321 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53124 1 433 +P53124 UniProtKB Chain 1 433 . . . ID=PRO_0000202740;Note=PHO85 cyclin-10 +P53124 UniProtKB Helix 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P53124 UniProtKB Helix 262 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P53124 UniProtKB Helix 291 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P53124 UniProtKB Helix 310 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P53124 UniProtKB Helix 325 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P53124 UniProtKB Beta strand 340 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P53124 UniProtKB Beta strand 348 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P53124 UniProtKB Helix 356 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P53124 UniProtKB Helix 359 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P53124 UniProtKB Helix 381 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P53124 UniProtKB Helix 392 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P53124 UniProtKB Helix 415 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +##sequence-region P24867 1 279 +P24867 UniProtKB Chain 1 279 . . . ID=PRO_0000080499;Note=PHO85 cyclin-1 +P24867 UniProtKB Domain 19 152 . . . Note=Cyclin N-terminal +P24867 UniProtKB Region 29 36 . . . Note=Required for degradation by DMA1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23264631;Dbxref=PMID:23264631 +P24867 UniProtKB Modified residue 39 39 . . . Note=Phosphothreonine%3B by PHO85;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23264631;Dbxref=PMID:23264631 +P24867 UniProtKB Modified residue 43 43 . . . Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23264631;Dbxref=PMID:23264631 +P24867 UniProtKB Cross-link 82 82 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23264631;Dbxref=PMID:23264631 +P24867 UniProtKB Cross-link 121 121 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23264631;Dbxref=PMID:23264631 +P24867 UniProtKB Mutagenesis 33 33 . . . Note=Stabilizes PCL1. P->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23264631;Dbxref=PMID:23264631 +P24867 UniProtKB Mutagenesis 39 39 . . . Note=In pcl1-2A%3B stabilizes PCL1%3B when associated with A-43. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23264631;Dbxref=PMID:23264631 +P24867 UniProtKB Mutagenesis 43 43 . . . Note=In pcl1-2A%3B stabilizes PCL1%3B when associated with A-39. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23264631;Dbxref=PMID:23264631 +##sequence-region Q08966 1 492 +Q08966 UniProtKB Chain 1 492 . . . ID=PRO_0000271787;Note=PHO85 cyclin-8 +Q08966 UniProtKB Compositional bias 25 33 . . . Note=Poly-Asp +Q08966 UniProtKB Compositional bias 83 92 . . . Note=Poly-Gln +Q08966 UniProtKB Modified residue 32 32 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08966 UniProtKB Sequence conflict 234 234 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P15873 1 258 +P15873 UniProtKB Chain 1 258 . . . ID=PRO_0000149176;Note=Proliferating cell nuclear antigen +P15873 UniProtKB DNA binding 61 80 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15873 UniProtKB Cross-link 127 127 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15166219;Dbxref=PMID:15166219 +P15873 UniProtKB Cross-link 164 164 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15166219,ECO:0000269|PubMed:15542864;Dbxref=PMID:15166219,PMID:15542864 +P15873 UniProtKB Cross-link 164 164 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12226657;Dbxref=PMID:12226657 +P15873 UniProtKB Beta strand 2 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Helix 9 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Turn 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 24 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 34 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 44 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Helix 54 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 57 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JNE +P15873 UniProtKB Beta strand 66 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Helix 72 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Turn 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 86 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 97 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 106 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 111 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Helix 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V62 +P15873 UniProtKB Beta strand 134 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Helix 141 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 156 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 166 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 177 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 185 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P15873 UniProtKB Beta strand 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V60 +P15873 UniProtKB Helix 191 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 195 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 203 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Helix 209 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Helix 216 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 223 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 231 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 235 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 244 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +P15873 UniProtKB Beta strand 254 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PLQ +##sequence-region P40345 1 661 +P40345 UniProtKB Chain 1 661 . . . ID=PRO_0000058268;Note=Phospholipid:diacylglycerol acyltransferase +P40345 UniProtKB Topological domain 1 80 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40345 UniProtKB Transmembrane 81 101 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40345 UniProtKB Topological domain 102 661 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40345 UniProtKB Active site 324 324 . . . Note=Acyl-ester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40345 UniProtKB Active site 567 567 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40345 UniProtKB Active site 618 618 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P37254 1 787 +P37254 UniProtKB Chain 1 787 . . . ID=PRO_0000154142;Note=Aminodeoxychorismate synthase +P37254 UniProtKB Domain 16 233 . . . Note=Glutamine amidotransferase type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +P37254 UniProtKB Region 304 787 . . . Note=PABB component +P37254 UniProtKB Compositional bias 10 14 . . . Note=Poly-Gln +P37254 UniProtKB Active site 112 112 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +P37254 UniProtKB Active site 207 207 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +P37254 UniProtKB Active site 209 209 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00605 +P37254 UniProtKB Sequence conflict 85 85 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37254 UniProtKB Sequence conflict 171 171 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37254 UniProtKB Sequence conflict 171 171 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37254 UniProtKB Sequence conflict 533 533 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37254 UniProtKB Sequence conflict 586 586 . . . Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37254 UniProtKB Sequence conflict 590 591 . . . Note=CE->FV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37254 UniProtKB Sequence conflict 721 721 . . . Note=G->GL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37254 UniProtKB Sequence conflict 722 722 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37254 UniProtKB Sequence conflict 735 737 . . . Note=NGD->FGF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38794 1 229 +P38794 UniProtKB Chain 1 229 . . . ID=PRO_0000080501;Note=PHO85 cyclin-5 +##sequence-region P53259 1 346 +P53259 UniProtKB Transit peptide 1 73 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53259 UniProtKB Chain 74 346 . . . ID=PRO_0000027392;Note=Rhomboid protein 1%2C mitochondrial +P53259 UniProtKB Transmembrane 109 129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53259 UniProtKB Transmembrane 145 165 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53259 UniProtKB Transmembrane 203 223 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53259 UniProtKB Transmembrane 246 266 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53259 UniProtKB Transmembrane 275 295 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53259 UniProtKB Transmembrane 308 328 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53259 UniProtKB Active site 256 256 . . . Note=Nucleophile +P53259 UniProtKB Active site 313 313 . . . . +P53259 UniProtKB Mutagenesis 202 202 . . . Note=Abolishes protease activity. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12901865;Dbxref=PMID:12901865 +P53259 UniProtKB Mutagenesis 252 252 . . . Note=Does not abolish protease activity. S->A%2CI;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12417197,ECO:0000269|PubMed:12901865;Dbxref=PMID:12417197,PMID:12901865 +P53259 UniProtKB Mutagenesis 254 256 . . . Note=Abolishes protease activity. GAS->AAI;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12417197;Dbxref=PMID:12417197 +P53259 UniProtKB Mutagenesis 256 256 . . . Note=Abolishes protease activity. S->A%2CI%2CG;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12417197,ECO:0000269|PubMed:12774122,ECO:0000269|PubMed:12901865;Dbxref=PMID:12417197,PMID:12774122,PMID:12901865 +P53259 UniProtKB Mutagenesis 313 313 . . . Note=Abolishes protease activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12901865;Dbxref=PMID:12901865 +##sequence-region P26263 1 563 +P26263 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169 +P26263 UniProtKB Chain 2 563 . . . ID=PRO_0000090772;Note=Pyruvate decarboxylase isozyme 3 +P26263 UniProtKB Region 390 476 . . . Note=Thiamine pyrophosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26263 UniProtKB Metal binding 444 444 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26263 UniProtKB Metal binding 471 471 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26263 UniProtKB Metal binding 473 473 . . . Note=Magnesium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26263 UniProtKB Binding site 28 28 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26263 UniProtKB Binding site 115 115 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26263 UniProtKB Binding site 477 477 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26263 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169 +P26263 UniProtKB Modified residue 223 223 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169 +P26263 UniProtKB Modified residue 266 266 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169 +P26263 UniProtKB Modified residue 353 353 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169 +P26263 UniProtKB Modified residue 522 522 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169 +P26263 UniProtKB Cross-link 212 212 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169 +P26263 UniProtKB Cross-link 233 233 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169 +P26263 UniProtKB Cross-link 269 269 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169 +P26263 UniProtKB Cross-link 505 505 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06169 +##sequence-region P22434 1 369 +P22434 UniProtKB Chain 1 369 . . . ID=PRO_0000206791;Note=3'%2C5'-cyclic-nucleotide phosphodiesterase 1 +P22434 UniProtKB Sequence conflict 94 94 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22434 UniProtKB Beta strand 4 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Beta strand 14 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Beta strand 18 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Beta strand 35 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Helix 44 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Beta strand 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Beta strand 69 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Helix 76 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Beta strand 86 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Helix 92 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Turn 97 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Helix 102 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Helix 110 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Beta strand 121 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Helix 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Helix 135 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Helix 141 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Beta strand 153 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Helix 159 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Beta strand 170 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Helix 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Beta strand 186 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Beta strand 200 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Turn 217 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Beta strand 222 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Turn 233 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Beta strand 238 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Turn 250 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Helix 256 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Helix 270 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Beta strand 273 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Helix 288 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Helix 297 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Turn 314 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Beta strand 321 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Helix 336 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Beta strand 357 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +P22434 UniProtKB Beta strand 365 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OJV +##sequence-region P06776 1 526 +P06776 UniProtKB Chain 1 526 . . . ID=PRO_0000198851;Note=3'%2C5'-cyclic-nucleotide phosphodiesterase 2 +P06776 UniProtKB Active site 265 265 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06776 UniProtKB Metal binding 269 269 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06776 UniProtKB Metal binding 302 302 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06776 UniProtKB Metal binding 303 303 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06776 UniProtKB Metal binding 303 303 . . . Note=Divalent metal cation 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06776 UniProtKB Metal binding 400 400 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06776 UniProtKB Sequence conflict 82 82 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06776 UniProtKB Sequence conflict 349 350 . . . Note=QL->LK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03266 1 374 +Q03266 UniProtKB Chain 1 374 . . . ID=PRO_0000203350;Note=Aminodeoxychorismate lyase +Q03266 UniProtKB Beta strand 27 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 35 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Beta strand 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Beta strand 47 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 60 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 72 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 86 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Beta strand 100 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 108 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 122 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 144 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 165 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Beta strand 178 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Beta strand 191 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 202 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 213 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 223 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Beta strand 232 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 246 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 256 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Beta strand 283 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Beta strand 293 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Turn 310 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Beta strand 313 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 321 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 329 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Beta strand 339 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Helix 347 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Beta strand 355 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Turn 361 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +Q03266 UniProtKB Beta strand 364 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K6N +##sequence-region P53632 1 584 +P53632 UniProtKB Chain 1 584 . . . ID=PRO_0000120314;Note=Poly(A) RNA polymerase protein 2 +P53632 UniProtKB Domain 371 431 . . . Note=PAP-associated +P53632 UniProtKB Metal binding 236 236 . . . Note=Magnesium or manganese%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53632 UniProtKB Metal binding 238 238 . . . Note=Magnesium or manganese%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53632 UniProtKB Mutagenesis 131 133 . . . Note=In TRF4-131%3B slow growth. EDE->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546 +P53632 UniProtKB Mutagenesis 140 142 . . . Note=In TRF4-140%3B slow growth. ERE->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546 +P53632 UniProtKB Mutagenesis 182 185 . . . Note=In TRF4-182%3B lethal. EIKD->AIAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546 +P53632 UniProtKB Mutagenesis 194 194 . . . Note=In TRF4-194%3B lethal%3B when associated with A-195%3B A-196 and A-198. R->A +P53632 UniProtKB Mutagenesis 195 198 . . . Note=In TRF4-194%3B lethal. EEIE->AIAA +P53632 UniProtKB Mutagenesis 217 219 . . . Note=In TRF4-217%3B slow growth. DAD->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546 +P53632 UniProtKB Mutagenesis 224 225 . . . Note=In TRF4-224%3B lethal. GS->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546 +P53632 UniProtKB Mutagenesis 236 238 . . . Note=In TRF4-236%3B lethal. DID->AIA;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10926539,ECO:0000269|PubMed:11861546,ECO:0000269|PubMed:16431988;Dbxref=PMID:10926539,PMID:11861546,PMID:16431988 +P53632 UniProtKB Mutagenesis 275 277 . . . Note=In TRF4-275%3B temperature sensitive. KAR->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546 +P53632 UniProtKB Mutagenesis 282 282 . . . Note=In TRF4-282%3B lethal%3B when associated with A-285. K->A +P53632 UniProtKB Mutagenesis 285 285 . . . Note=In TRF4-282%3B lethal%3B when associated with A-282. E->A +P53632 UniProtKB Mutagenesis 309 310 . . . Note=In TRF4-309%3B lethal. RE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546 +P53632 UniProtKB Mutagenesis 332 333 . . . Note=In TRF4-332%3B temperature sensitive. RR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546 +P53632 UniProtKB Mutagenesis 378 378 . . . Note=In TRF4-378%3B lethal%3B when associated with A-381. E->A +P53632 UniProtKB Mutagenesis 381 381 . . . Note=In TRF4-378%3B lethal%3B when associated with A-378. E->A +P53632 UniProtKB Mutagenesis 425 425 . . . Note=In TRF4-425%3B lethal%3B when associated with A-428 and A-429. D->A +P53632 UniProtKB Mutagenesis 428 429 . . . Note=In TRF4-425%3B lethal%3B when associated with A-425. DE->AA +P53632 UniProtKB Mutagenesis 444 445 . . . Note=In TRF4-444%3B lethal. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546 +P53632 UniProtKB Mutagenesis 467 469 . . . Note=In TRF4-467%3B temperature sensitive. KDR->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546 +P53632 UniProtKB Mutagenesis 486 487 . . . Note=In TRF4-486%3B lethal. RD->AA +P53632 UniProtKB Mutagenesis 490 492 . . . Note=In TRF4-486%3B lethal. DER->AAA +P53632 UniProtKB Mutagenesis 502 502 . . . Note=In TRF4-502%3B lethal%3B when associated with A-504. E->A +P53632 UniProtKB Mutagenesis 504 504 . . . Note=In TRF4-502%3B lethal%3B when associated with A-502. E->A +P53632 UniProtKB Mutagenesis 508 510 . . . Note=In TRF4-508%3B lethal. KKR->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546 +P53632 UniProtKB Mutagenesis 559 560 . . . Note=In TRF4-559%3B slow growth. KR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546 +P53632 UniProtKB Mutagenesis 560 560 . . . Note=In TRF4-559%3B slow growth%3B when associated with A-559. R->A +P53632 UniProtKB Mutagenesis 572 574 . . . Note=In TRF4-572%3B slow growth. EDD->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11861546;Dbxref=PMID:11861546 +P53632 UniProtKB Beta strand 122 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P53632 UniProtKB Helix 162 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Helix 175 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Helix 194 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Beta strand 220 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Turn 225 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Beta strand 237 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Helix 247 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Helix 250 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Beta strand 271 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Beta strand 279 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Turn 286 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Beta strand 290 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Helix 303 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Helix 318 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Helix 337 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Helix 344 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Helix 359 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Helix 368 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Helix 372 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Turn 389 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Beta strand 392 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Beta strand 401 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Helix 406 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Helix 410 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Beta strand 418 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Beta strand 423 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Beta strand 428 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Turn 433 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Helix 440 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Helix 466 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +P53632 UniProtKB Turn 476 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NYB +##sequence-region P29468 1 568 +P29468 UniProtKB Chain 1 568 . . . ID=PRO_0000051621;Note=Poly(A) polymerase +P29468 UniProtKB Nucleotide binding 87 89 . . . Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751 +P29468 UniProtKB Nucleotide binding 99 102 . . . Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751 +P29468 UniProtKB Nucleotide binding 100 102 . . . Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751 +P29468 UniProtKB Nucleotide binding 233 234 . . . Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751 +P29468 UniProtKB Metal binding 100 100 . . . Note=Magnesium 1%3B catalytic +P29468 UniProtKB Metal binding 100 100 . . . Note=Magnesium 2%3B catalytic +P29468 UniProtKB Metal binding 102 102 . . . Note=Magnesium 1%3B catalytic +P29468 UniProtKB Metal binding 102 102 . . . Note=Magnesium 2%3B catalytic +P29468 UniProtKB Metal binding 154 154 . . . Note=Magnesium 2%3B catalytic +P29468 UniProtKB Binding site 154 154 . . . Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751 +P29468 UniProtKB Binding site 215 215 . . . Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751 +P29468 UniProtKB Binding site 224 224 . . . Note=ATP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751 +P29468 UniProtKB Site 140 140 . . . Note=Interaction with RNA +P29468 UniProtKB Site 145 145 . . . Note=Interaction with RNA +P29468 UniProtKB Site 294 294 . . . Note=Interaction with RNA +P29468 UniProtKB Site 314 314 . . . Note=Interaction with RNA +P29468 UniProtKB Site 315 315 . . . Note=Interaction with RNA +P29468 UniProtKB Site 387 387 . . . Note=Interaction with RNA +P29468 UniProtKB Site 392 392 . . . Note=Interaction with RNA +P29468 UniProtKB Site 487 487 . . . Note=Interaction with RNA +P29468 UniProtKB Modified residue 452 452 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P29468 UniProtKB Modified residue 550 550 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P29468 UniProtKB Mutagenesis 154 154 . . . Note=Loss of enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751 +P29468 UniProtKB Mutagenesis 189 189 . . . Note=Slightly reduced rate of adenylyltransfer. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751 +P29468 UniProtKB Mutagenesis 215 215 . . . Note=Reduces rate of adenylyltransfer about four-fold. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751 +P29468 UniProtKB Mutagenesis 226 226 . . . Note=Reduces rate of adenylyltransfer by half. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17850751;Dbxref=PMID:17850751 +P29468 UniProtKB Mutagenesis 485 485 . . . Note=Abolishes interaction with FIP1%3B when associated with Y-489. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18537269;Dbxref=PMID:18537269 +P29468 UniProtKB Mutagenesis 489 489 . . . Note=Abolishes interaction with FIP1%3B when associated with R-485. V->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18537269;Dbxref=PMID:18537269 +P29468 UniProtKB Helix 5 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Beta strand 8 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Q66 +P29468 UniProtKB Helix 20 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 42 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 74 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Beta strand 83 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 88 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Beta strand 101 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 113 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Beta strand 130 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Beta strand 139 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Beta strand 143 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Beta strand 151 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Beta strand 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 174 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 182 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 204 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 226 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 233 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 252 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Beta strand 272 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Beta strand 281 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FA0 +P29468 UniProtKB Turn 289 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 293 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Beta strand 305 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Turn 312 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 318 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 345 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 354 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Beta strand 359 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 372 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Beta strand 399 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Beta strand 409 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Beta strand 417 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 420 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Beta strand 428 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FA0 +P29468 UniProtKB Helix 431 434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 435 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FA0 +P29468 UniProtKB Turn 444 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Q66 +P29468 UniProtKB Helix 451 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Q66 +P29468 UniProtKB Beta strand 458 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Beta strand 475 477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2O1P +P29468 UniProtKB Helix 482 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Turn 497 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Beta strand 502 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 514 516 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +P29468 UniProtKB Helix 519 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HHP +##sequence-region Q12515 1 295 +Q12515 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12515 UniProtKB Chain 2 295 . . . ID=PRO_0000240879;Note=Protein PAR32 +Q12515 UniProtKB Compositional bias 54 58 . . . Note=Poly-Asn +Q12515 UniProtKB Compositional bias 274 283 . . . Note=Poly-Lys +Q12515 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12515 UniProtKB Modified residue 36 36 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12515 UniProtKB Modified residue 39 39 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12515 UniProtKB Modified residue 47 47 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12515 UniProtKB Modified residue 123 123 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12515 UniProtKB Modified residue 138 138 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12515 UniProtKB Modified residue 141 141 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12515 UniProtKB Modified residue 147 147 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12515 UniProtKB Modified residue 246 246 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q12515 UniProtKB Sequence conflict 135 135 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40186 1 285 +P40186 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12174291;Dbxref=PMID:12174291 +P40186 UniProtKB Chain 2 285 . . . ID=PRO_0000202991;Note=PHO85 cyclin-7 +P40186 UniProtKB Modified residue 69 69 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P17967 1 522 +P17967 UniProtKB Signal peptide 1 28 . . . Note=Or 22;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17967 UniProtKB Chain 29 522 . . . ID=PRO_0000034218;Note=Protein disulfide-isomerase +P17967 UniProtKB Domain 29 141 . . . Note=Thioredoxin 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +P17967 UniProtKB Domain 356 485 . . . Note=Thioredoxin 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +P17967 UniProtKB Motif 519 522 . . . Note=Prevents secretion from ER +P17967 UniProtKB Active site 61 61 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P17967 UniProtKB Active site 64 64 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P17967 UniProtKB Active site 406 406 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P17967 UniProtKB Active site 409 409 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P17967 UniProtKB Site 62 62 . . . Note=Contributes to redox potential value;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P17967 UniProtKB Site 63 63 . . . Note=Contributes to redox potential value;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P17967 UniProtKB Site 126 126 . . . Note=Lowers pKa of C-terminal Cys of first active site;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P17967 UniProtKB Site 407 407 . . . Note=Contributes to redox potential value;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P17967 UniProtKB Site 408 408 . . . Note=Contributes to redox potential value;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P17967 UniProtKB Site 471 471 . . . Note=Lowers pKa of C-terminal Cys of second active site;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P17967 UniProtKB Glycosylation 82 82 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17967 UniProtKB Glycosylation 117 117 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17967 UniProtKB Glycosylation 155 155 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17967 UniProtKB Glycosylation 174 174 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17967 UniProtKB Glycosylation 425 425 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17967 UniProtKB Disulfide bond 61 64 . . . Note=Redox-active;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00691,ECO:0000269|PubMed:16413482;Dbxref=PMID:16413482 +P17967 UniProtKB Disulfide bond 406 409 . . . Note=Redox-active;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00691,ECO:0000269|PubMed:16413482;Dbxref=PMID:16413482 +P17967 UniProtKB Sequence conflict 33 52 . . . Note=AVVKLATDSFNEYIQSHDLV->LSLSWPPTLSMNTFSRTTWW;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Sequence conflict 83 83 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Sequence conflict 83 83 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Sequence conflict 114 114 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Sequence conflict 143 143 . . . Note=V->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Sequence conflict 146 146 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Sequence conflict 168 168 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Sequence conflict 168 168 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Sequence conflict 197 197 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Sequence conflict 215 215 . . . Note=V->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Sequence conflict 226 226 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Sequence conflict 226 226 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Sequence conflict 333 333 . . . Note=E->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Sequence conflict 351 351 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Sequence conflict 455 455 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Sequence conflict 458 458 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Sequence conflict 458 458 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Sequence conflict 505 505 . . . Note=A->AEADAEAEA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Sequence conflict 505 505 . . . Note=A->AEADAEAEA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17967 UniProtKB Turn 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 42 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Beta strand 50 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 62 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Turn 78 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Beta strand 84 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Turn 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 94 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Beta strand 104 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Beta strand 119 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 128 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Beta strand 142 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 149 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Beta strand 162 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 171 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Turn 184 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Beta strand 189 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Beta strand 201 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Beta strand 209 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 220 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 226 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 246 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Beta strand 259 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 267 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Turn 284 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Beta strand 289 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 295 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 301 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Beta strand 311 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Turn 319 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Beta strand 323 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 332 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 346 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Beta strand 377 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Turn 383 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 386 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Beta strand 397 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 407 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Beta strand 431 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 437 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Beta strand 448 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 473 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +P17967 UniProtKB Helix 490 501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B5E +##sequence-region P40530 1 394 +P40530 UniProtKB Transit peptide 1 20 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40530 UniProtKB Chain 21 394 . . . ID=PRO_0000213686;Note=[Pyruvate dehydrogenase (acetyl-transferring)] kinase 1%2C mitochondrial +P40530 UniProtKB Domain 126 386 . . . Note=Histidine kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00107 +P40530 UniProtKB Nucleotide binding 267 274 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40530 UniProtKB Nucleotide binding 323 324 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40530 UniProtKB Nucleotide binding 347 352 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40530 UniProtKB Binding site 304 304 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40530 UniProtKB Modified residue 148 148 . . . Note=Phosphohistidine%3B by autocatalysis;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00107 +##sequence-region P12383 1 1068 +P12383 UniProtKB Chain 1 1068 . . . ID=PRO_0000114961;Note=Transcription factor PDR1 +P12383 UniProtKB DNA binding 46 72 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P12383 UniProtKB Motif 1054 1062 . . . Note=9aaTAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618436;Dbxref=PMID:27618436 +P12383 UniProtKB Modified residue 21 21 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P12383 UniProtKB Modified residue 930 930 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P12383 UniProtKB Modified residue 942 942 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P12383 UniProtKB Modified residue 948 948 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P12383 UniProtKB Sequence conflict 411 411 . . . Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12383 UniProtKB Sequence conflict 411 411 . . . Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12383 UniProtKB Sequence conflict 530 530 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12383 UniProtKB Sequence conflict 820 820 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12383 UniProtKB Sequence conflict 820 820 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12383 UniProtKB Sequence conflict 921 921 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12383 UniProtKB Sequence conflict 921 921 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12383 UniProtKB Sequence conflict 981 981 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12383 UniProtKB Sequence conflict 981 981 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12383 UniProtKB Sequence conflict 1015 1019 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12383 UniProtKB Sequence conflict 1015 1019 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P33200 1 976 +P33200 UniProtKB Chain 1 976 . . . ID=PRO_0000114962;Note=Transcription factor PDR3 +P33200 UniProtKB DNA binding 15 41 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P33200 UniProtKB Sequence conflict 355 355 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P33302 1 1511 +P33302 UniProtKB Chain 1 1511 . . . ID=PRO_0000093442;Note=Pleiotropic ABC efflux transporter of multiple drugs +P33302 UniProtKB Topological domain 1 517 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Transmembrane 518 542 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Topological domain 543 558 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Transmembrane 559 579 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Topological domain 580 611 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Transmembrane 612 628 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Topological domain 629 631 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Transmembrane 632 650 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Topological domain 651 665 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Transmembrane 666 685 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Topological domain 686 774 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Transmembrane 775 793 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Topological domain 794 1237 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Transmembrane 1238 1260 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Topological domain 1261 1291 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Transmembrane 1292 1313 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Topological domain 1314 1324 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Transmembrane 1325 1349 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Topological domain 1350 1354 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Transmembrane 1355 1379 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Topological domain 1380 1388 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Transmembrane 1389 1407 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Topological domain 1408 1476 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Transmembrane 1477 1499 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Topological domain 1500 1511 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Domain 161 410 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P33302 UniProtKB Domain 869 1112 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P33302 UniProtKB Nucleotide binding 905 912 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P33302 UniProtKB Compositional bias 784 787 . . . Note=Poly-Phe +P33302 UniProtKB Modified residue 22 22 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33302 UniProtKB Modified residue 49 49 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P33302 UniProtKB Modified residue 51 51 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33302 UniProtKB Modified residue 54 54 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P33302 UniProtKB Modified residue 58 58 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33302 UniProtKB Modified residue 61 61 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P33302 UniProtKB Modified residue 837 837 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956 +P33302 UniProtKB Modified residue 840 840 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P33302 UniProtKB Modified residue 841 841 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P33302 UniProtKB Modified residue 849 849 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P33302 UniProtKB Modified residue 850 850 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P33302 UniProtKB Modified residue 854 854 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P33302 UniProtKB Glycosylation 734 734 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Glycosylation 1447 1447 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33302 UniProtKB Cross-link 825 825 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12872131,ECO:0000269|PubMed:14557538;Dbxref=PMID:12872131,PMID:14557538 +P33302 UniProtKB Mutagenesis 183 183 . . . Note=Activates ER-associated degradation. L->P +P33302 UniProtKB Mutagenesis 257 257 . . . Note=Alters drug specificity. T->I +P33302 UniProtKB Mutagenesis 302 302 . . . Note=Confers generalized drug resistance. G->D +P33302 UniProtKB Mutagenesis 648 648 . . . Note=Alters drug specificity. S->F +P33302 UniProtKB Mutagenesis 905 905 . . . Note=Inactivates drug transport. G->S +P33302 UniProtKB Mutagenesis 908 908 . . . Note=Inactivates drug transport. G->S +P33302 UniProtKB Mutagenesis 1009 1009 . . . Note=Confers generalized drug resistance. G->C +P33302 UniProtKB Mutagenesis 1040 1040 . . . Note=Alters drug specificity. G->D +P33302 UniProtKB Mutagenesis 1048 1048 . . . Note=Alters drug specificity. S->V +P33302 UniProtKB Mutagenesis 1289 1289 . . . Note=Alters drug specificity. E->K +P33302 UniProtKB Mutagenesis 1311 1311 . . . Note=Alters drug specificity. Y->S +P33302 UniProtKB Mutagenesis 1360 1360 . . . Note=Alters drug specificity. S->F +P33302 UniProtKB Mutagenesis 1393 1393 . . . Note=Alters drug specificity. T->I +P33302 UniProtKB Mutagenesis 1427 1427 . . . Note=Activates ER-associated degradation. C->Y +P33302 UniProtKB Sequence conflict 171 171 . . . Note=N->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33302 UniProtKB Sequence conflict 190 190 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33302 UniProtKB Sequence conflict 214 214 . . . Note=D->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33302 UniProtKB Sequence conflict 308 308 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33302 UniProtKB Sequence conflict 340 345 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33302 UniProtKB Sequence conflict 476 476 . . . Note=R->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33302 UniProtKB Sequence conflict 648 648 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33302 UniProtKB Sequence conflict 770 770 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53224 1 222 +P53224 UniProtKB Chain 1 222 . . . ID=PRO_0000215645;Note=Protein ORM1 +P53224 UniProtKB Topological domain 1 85 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53224 UniProtKB Transmembrane 86 106 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53224 UniProtKB Topological domain 107 109 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53224 UniProtKB Transmembrane 110 130 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53224 UniProtKB Topological domain 131 162 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53224 UniProtKB Transmembrane 163 183 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53224 UniProtKB Topological domain 184 184 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53224 UniProtKB Transmembrane 185 205 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53224 UniProtKB Topological domain 206 222 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53224 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P53224 UniProtKB Modified residue 32 32 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53224 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53224 UniProtKB Mutagenesis 29 29 . . . Note=Induces dysregulation of sphingolipid synthesis%3B when associated with 32-A--A-36 and 51-A--A-53. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20182505;Dbxref=PMID:20182505 +P53224 UniProtKB Mutagenesis 32 36 . . . Note=Induces dysregulation of sphingolipid synthesis%3B when associated with A-29 and 51-A--A-53. SASSS->AAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20182505;Dbxref=PMID:20182505 +P53224 UniProtKB Mutagenesis 51 53 . . . Note=Induces dysregulation of sphingolipid synthesis%3B when associated with A-29 and 32-A--A-36. SSS->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20182505;Dbxref=PMID:20182505 +##sequence-region P35845 1 1188 +P35845 UniProtKB Chain 1 1188 . . . ID=PRO_0000100387;Note=Oxysterol-binding protein homolog 1 +P35845 UniProtKB Repeat 51 80 . . . Note=ANK 1 +P35845 UniProtKB Repeat 96 125 . . . Note=ANK 2 +P35845 UniProtKB Repeat 196 225 . . . Note=ANK 3 +P35845 UniProtKB Domain 330 379 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +P35845 UniProtKB Motif 716 722 . . . Note=FFAT +P35845 UniProtKB Compositional bias 434 472 . . . Note=Asn/Asp-rich +P35845 UniProtKB Modified residue 394 394 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P35845 UniProtKB Modified residue 490 490 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P35845 UniProtKB Modified residue 500 500 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P35845 UniProtKB Modified residue 678 678 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P35845 UniProtKB Modified residue 683 683 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35845 UniProtKB Modified residue 691 691 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35845 UniProtKB Modified residue 692 692 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35845 UniProtKB Modified residue 694 694 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P35845 UniProtKB Modified residue 708 708 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P35845 UniProtKB Modified residue 712 712 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P35845 UniProtKB Mutagenesis 719 719 . . . Note=Abolishes function. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12727870;Dbxref=PMID:12727870 +P35845 UniProtKB Sequence conflict 244 244 . . . Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35845 UniProtKB Sequence conflict 248 248 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35845 UniProtKB Sequence conflict 248 248 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35845 UniProtKB Sequence conflict 424 424 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35845 UniProtKB Sequence conflict 464 464 . . . Note=D->NNN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35845 UniProtKB Sequence conflict 468 469 . . . Note=YD->DY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35845 UniProtKB Sequence conflict 495 496 . . . Note=TP->AS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35845 UniProtKB Helix 13 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28 +P35845 UniProtKB Helix 29 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28 +P35845 UniProtKB Helix 46 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28 +P35845 UniProtKB Helix 55 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28 +P35845 UniProtKB Helix 65 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28 +P35845 UniProtKB Helix 100 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28 +P35845 UniProtKB Helix 110 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28 +P35845 UniProtKB Helix 134 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28 +P35845 UniProtKB Helix 141 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28 +P35845 UniProtKB Helix 171 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28 +P35845 UniProtKB Helix 183 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28 +P35845 UniProtKB Turn 194 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28 +P35845 UniProtKB Helix 200 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28 +P35845 UniProtKB Helix 210 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28 +P35845 UniProtKB Helix 233 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28 +P35845 UniProtKB Helix 249 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28 +P35845 UniProtKB Helix 252 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H28 +##sequence-region P38713 1 996 +P38713 UniProtKB Chain 1 996 . . . ID=PRO_0000100389;Note=Oxysterol-binding protein homolog 3 +P38713 UniProtKB Domain 221 315 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +P38713 UniProtKB Motif 514 520 . . . Note=FFAT +P38713 UniProtKB Modified residue 190 190 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38713 UniProtKB Modified residue 193 193 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38713 UniProtKB Modified residue 210 210 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38713 UniProtKB Modified residue 323 323 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38713 UniProtKB Modified residue 324 324 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38713 UniProtKB Modified residue 325 325 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38713 UniProtKB Modified residue 352 352 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38713 UniProtKB Modified residue 605 605 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38713 UniProtKB Beta strand 223 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP +P38713 UniProtKB Beta strand 240 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP +P38713 UniProtKB Turn 248 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP +P38713 UniProtKB Beta strand 252 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP +P38713 UniProtKB Beta strand 266 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP +P38713 UniProtKB Helix 270 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP +P38713 UniProtKB Beta strand 273 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP +P38713 UniProtKB Turn 279 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP +P38713 UniProtKB Beta strand 283 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP +P38713 UniProtKB Beta strand 292 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP +P38713 UniProtKB Helix 300 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP +P38713 UniProtKB Helix 312 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAP +P38713 UniProtKB Helix 643 649 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 650 653 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Helix 655 657 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Helix 662 664 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 665 669 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Helix 670 675 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Helix 676 678 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Turn 679 681 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Helix 682 687 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Helix 693 703 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Helix 704 708 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Helix 711 715 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 717 719 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 726 731 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Helix 732 734 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 736 744 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Turn 745 748 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 749 771 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 773 788 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Turn 789 791 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 794 798 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 802 805 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 807 810 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 813 816 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 818 824 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 829 834 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 838 841 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 846 852 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 862 867 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Turn 868 870 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 871 874 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Turn 875 877 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 880 883 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Helix 891 893 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Turn 894 896 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Helix 899 904 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Turn 909 914 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Helix 920 922 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Helix 924 930 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Helix 934 953 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 961 967 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Beta strand 970 973 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +P38713 UniProtKB Helix 980 985 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IC4 +##sequence-region P38755 1 437 +P38755 UniProtKB Chain 1 437 . . . ID=PRO_0000100391;Note=Oxysterol-binding protein homolog 7 +P38755 UniProtKB Region 64 69 . . . Note=Phosphatidylinositol 4-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02201 +P38755 UniProtKB Region 64 69 . . . Note=Phosphatidylserine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02201 +P38755 UniProtKB Region 126 129 . . . Note=Phosphatidylinositol 4-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02201 +P38755 UniProtKB Region 157 158 . . . Note=Phosphatidylinositol 4-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02201 +P38755 UniProtKB Binding site 129 129 . . . Note=Phosphatidylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02201 +P38755 UniProtKB Binding site 183 183 . . . Note=Phosphatidylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02201 +P38755 UniProtKB Binding site 351 351 . . . Note=Phosphatidylinositol 4-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02201 +P38755 UniProtKB Binding site 355 355 . . . Note=Phosphatidylinositol 4-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02201 +P38755 UniProtKB Binding site 359 359 . . . Note=Phosphatidylinositol 4-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02201 +P38755 UniProtKB Cross-link 276 276 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P38747 1 307 +P38747 UniProtKB Chain 1 307 . . . ID=PRO_0000202883;Note=OTU domain-containing protein 2 +P38747 UniProtKB Domain 167 307 . . . Note=OTU;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00139 +##sequence-region P38787 1 379 +P38787 UniProtKB Chain 1 379 . . . ID=PRO_0000157328;Note=2-dehydropantoate 2-reductase +P38787 UniProtKB Nucleotide binding 13 18 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38787 UniProtKB Active site 224 224 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38787 UniProtKB Binding site 119 119 . . . Note=NADP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38787 UniProtKB Binding site 119 119 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38787 UniProtKB Binding site 228 228 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38787 UniProtKB Binding site 232 232 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38787 UniProtKB Binding site 316 316 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38787 UniProtKB Binding site 328 328 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q07362 1 185 +Q07362 UniProtKB Chain 1 185 . . . ID=PRO_0000262746;Note=Protein PBP4 +Q07362 UniProtKB Compositional bias 56 62 . . . Note=Poly-Gln +##sequence-region P08018 1 668 +P08018 UniProtKB Chain 1 668 . . . ID=PRO_0000086483;Note=MAP kinase kinase PBS2 +P08018 UniProtKB Domain 360 623 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P08018 UniProtKB Nucleotide binding 366 374 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P08018 UniProtKB Compositional bias 91 101 . . . Note=Pro-rich +P08018 UniProtKB Active site 485 485 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P08018 UniProtKB Binding site 389 389 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P08018 UniProtKB Modified residue 68 68 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P08018 UniProtKB Modified residue 269 269 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P08018 UniProtKB Modified residue 514 514 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:7624781;Dbxref=PMID:18407956,PMID:7624781 +P08018 UniProtKB Modified residue 518 518 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7624781;Dbxref=PMID:7624781 +P08018 UniProtKB Mutagenesis 96 96 . . . Note=In PBS2-13%3B loss of SH3-domain interaction. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7624781;Dbxref=PMID:7624781 +P08018 UniProtKB Mutagenesis 389 389 . . . Note=Loss of activity. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7624781;Dbxref=PMID:7624781 +P08018 UniProtKB Mutagenesis 514 514 . . . Note=Loss of phosphorylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7624781;Dbxref=PMID:7624781 +P08018 UniProtKB Mutagenesis 518 518 . . . Note=Loss of phosphorylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7624781;Dbxref=PMID:7624781 +P08018 UniProtKB Sequence conflict 222 223 . . . Note=GL->AV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08018 UniProtKB Sequence conflict 222 223 . . . Note=GL->AV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25693 1 308 +P25693 UniProtKB Chain 1 308 . . . ID=PRO_0000080500;Note=PHO85 cyclin-2 +P25693 UniProtKB Domain 18 146 . . . Note=Cyclin N-terminal +##sequence-region Q12477 1 304 +Q12477 UniProtKB Chain 1 304 . . . ID=PRO_0000271788;Note=PHO85 cyclin-9 +Q12477 UniProtKB Domain 19 146 . . . Note=Cyclin N-terminal +##sequence-region P13259 1 424 +P13259 UniProtKB Chain 1 424 . . . ID=PRO_0000208460;Note=Choline-phosphate cytidylyltransferase +P13259 UniProtKB Nucleotide binding 111 119 . . . Note=CTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13259 UniProtKB Nucleotide binding 195 196 . . . Note=CTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13259 UniProtKB Nucleotide binding 223 227 . . . Note=CTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13259 UniProtKB Binding site 149 149 . . . Note=CTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13259 UniProtKB Binding site 149 149 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13259 UniProtKB Binding site 178 178 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13259 UniProtKB Binding site 200 200 . . . Note=CTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13259 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +P13259 UniProtKB Modified residue 59 59 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P13259 UniProtKB Modified residue 346 346 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198 +P13259 UniProtKB Modified residue 401 401 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13259 UniProtKB Sequence conflict 90 90 . . . Note=P->PG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13259 UniProtKB Sequence conflict 105 105 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13259 UniProtKB Sequence conflict 192 192 . . . Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32896 1 925 +P32896 UniProtKB Chain 1 925 . . . ID=PRO_0000126137;Note=Protein PDC2 +P32896 UniProtKB Domain 63 138 . . . Note=HTH CENPB-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00583 +P32896 UniProtKB Compositional bias 538 562 . . . Note=Asn/Ser-rich +P32896 UniProtKB Compositional bias 890 895 . . . Note=Poly-Ala +P32896 UniProtKB Sequence conflict 113 113 . . . Note=H->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32896 UniProtKB Sequence conflict 113 113 . . . Note=H->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32896 UniProtKB Sequence conflict 174 174 . . . Note=D->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32896 UniProtKB Sequence conflict 174 174 . . . Note=D->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q99220 1 542 +Q99220 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99220 UniProtKB Chain 22 542 . . . ID=PRO_0000042758;Note=Protein OS-9 homolog +Q99220 UniProtKB Domain 115 190 . . . Note=PRKCSH +Q99220 UniProtKB Motif 539 542 . . . Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10138 +Q99220 UniProtKB Binding site 137 137 . . . Note=Carbohydrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99220 UniProtKB Binding site 194 194 . . . Note=Carbohydrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99220 UniProtKB Binding site 200 200 . . . Note=Carbohydrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99220 UniProtKB Binding site 223 223 . . . Note=Carbohydrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99220 UniProtKB Binding site 229 229 . . . Note=Carbohydrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99220 UniProtKB Glycosylation 52 52 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99220 UniProtKB Glycosylation 74 74 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99220 UniProtKB Glycosylation 380 380 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99220 UniProtKB Disulfide bond 117 130 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99220 UniProtKB Disulfide bond 193 227 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99220 UniProtKB Disulfide bond 208 239 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99220 UniProtKB Mutagenesis 127 127 . . . Note=Decrease of ER lumenal misfolded protein degradation. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16168372;Dbxref=PMID:16168372 +Q99220 UniProtKB Mutagenesis 137 137 . . . Note=Decrease of ER lumenal misfolded protein degradation. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16168372;Dbxref=PMID:16168372 +Q99220 UniProtKB Mutagenesis 139 139 . . . Note=Decrease of ER lumenal misfolded protein degradation. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16168372;Dbxref=PMID:16168372 +Q99220 UniProtKB Mutagenesis 200 200 . . . Note=Decrease of ER lumenal misfolded protein degradation. No effect on interaction with CDC48%2C HRD3%2C KAR2%2C UBX2%2C HRD1 or EMP47. R->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16168370,ECO:0000269|PubMed:16168372,ECO:0000269|PubMed:16873065;Dbxref=PMID:16168370,PMID:16168372,PMID:16873065 +Q99220 UniProtKB Mutagenesis 223 223 . . . Note=Decrease of ER lumenal misfolded protein degradation. E->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16168370,ECO:0000269|PubMed:16168372;Dbxref=PMID:16168370,PMID:16168372 +Q99220 UniProtKB Mutagenesis 229 229 . . . Note=Decrease of ER lumenal misfolded protein degradation. Y->A%2CF;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16168370,ECO:0000269|PubMed:16168372;Dbxref=PMID:16168370,PMID:16168372 +Q99220 UniProtKB Sequence conflict 25 25 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q99220 UniProtKB Beta strand 276 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA +Q99220 UniProtKB Beta strand 286 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA +Q99220 UniProtKB Beta strand 299 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA +Q99220 UniProtKB Helix 305 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA +Q99220 UniProtKB Beta strand 310 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA +Q99220 UniProtKB Helix 315 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA +Q99220 UniProtKB Beta strand 347 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA +Q99220 UniProtKB Beta strand 361 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA +Q99220 UniProtKB Beta strand 371 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA +Q99220 UniProtKB Beta strand 375 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA +Q99220 UniProtKB Beta strand 391 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YMA +##sequence-region P04147 1 577 +P04147 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P04147 UniProtKB Chain 2 577 . . . ID=PRO_0000081720;Note=Polyadenylate-binding protein%2C cytoplasmic and nuclear +P04147 UniProtKB Domain 38 116 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P04147 UniProtKB Domain 126 203 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P04147 UniProtKB Domain 219 296 . . . Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P04147 UniProtKB Domain 322 399 . . . Note=RRM 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P04147 UniProtKB Domain 489 568 . . . Note=PABC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00641 +P04147 UniProtKB Region 9 61 . . . Note=Required and sufficient for nuclear export;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04147 UniProtKB Region 281 317 . . . Note=Required and sufficient for nuclear import;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04147 UniProtKB Region 473 577 . . . Note=Interaction with SUP35 +P04147 UniProtKB Motif 12 17 . . . Note=Nuclear export signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P04147 UniProtKB Compositional bias 422 431 . . . Note=Poly-Ala +P04147 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P04147 UniProtKB Modified residue 107 107 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23865587;Dbxref=PMID:23865587 +P04147 UniProtKB Modified residue 249 249 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P04147 UniProtKB Modified residue 332 332 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04147 UniProtKB Modified residue 405 405 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04147 UniProtKB Cross-link 7 7 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P04147 UniProtKB Cross-link 337 337 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P04147 UniProtKB Mutagenesis 12 12 . . . Note=Impairs nuclear export%3B when associated with A-15. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15630021;Dbxref=PMID:15630021 +P04147 UniProtKB Mutagenesis 15 15 . . . Note=Impairs nuclear export%3B when associated with A-12. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15630021;Dbxref=PMID:15630021 +P04147 UniProtKB Mutagenesis 79 79 . . . Note=In PAB1-14%3B fails to bind poly(U)%2C but not poly(A) RNA%3B when associated with Q-166%3B Q-259 and Q-362. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9193001;Dbxref=PMID:9193001 +P04147 UniProtKB Mutagenesis 83 83 . . . Note=In PAB1-16%3B reduces affinity for oligo(A) about 100-fold%2C impairs poly(A)-dependent translation%2C but still interacts with eIF4G%3B when associated with V-170. In PAB1-15%3B fails to bind RNA%3B when associated with V-170%3B V-263 and V-366. Y->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9193001,ECO:0000269|PubMed:9418852;Dbxref=PMID:9193001,PMID:9418852 +P04147 UniProtKB Mutagenesis 134 136 . . . Note=In PAB1-134. HPD->DKS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10357826;Dbxref=PMID:10357826 +P04147 UniProtKB Mutagenesis 148 148 . . . Note=In PAB1-148%3B greatly reduces poly(A)-dependent translation and moderately reduces stimulation of cap-dependent translation in vitro%3B when associated with N-151. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10357826;Dbxref=PMID:10357826 +P04147 UniProtKB Mutagenesis 151 151 . . . Note=In PAB1-148%3B greatly reduces poly(A)-dependent translation and moderately reduces stimulation of cap-dependent translation in vitro%3B when associated with A-148. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10357826;Dbxref=PMID:10357826 +P04147 UniProtKB Mutagenesis 157 159 . . . Note=In PAB1-157%3B greatly reduces poly(A)-dependent translation and stimulation of cap-dependent translation in vitro. IAT->VVC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10357826;Dbxref=PMID:10357826 +P04147 UniProtKB Mutagenesis 166 166 . . . Note=In PAB1-14%3B fails to bind poly(U)%2C but not poly(A) RNA%3B when associated with A-79%3B Q-259 and Q-362. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9193001;Dbxref=PMID:9193001 +P04147 UniProtKB Mutagenesis 170 170 . . . Note=In PAB1-6%3B selectively reduces poly(A) RNA binding. In PAB1-16%3B reduces affinity for oligo(A) about 100-fold%2C impairs poly(A)-dependent translation%2C but still interacts with eIF4G%3B when associated with V-83. In PAB1-15%3B fails to bind RNA%3B when associated with V-83%3B V-263 and V-366. F->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9193001,ECO:0000269|PubMed:9418852;Dbxref=PMID:9193001,PMID:9418852 +P04147 UniProtKB Mutagenesis 175 177 . . . Note=In PAB1-175%3B greatly reduces poly(A)-dependent translation and stimulation of cap-dependent translation in vitro. EEG->TQE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10357826;Dbxref=PMID:10357826 +P04147 UniProtKB Mutagenesis 180 181 . . . Note=In PAB1-180%3B abolishes poly(A)-dependent translation and greatly reduces stimulation of cap-dependent translation in vitro. Impairs interaction with eIF4G. KE->ER;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10357826;Dbxref=PMID:10357826 +P04147 UniProtKB Mutagenesis 184 186 . . . Note=In PAB1-184%3B abolishes poly(A)-dependent translation and moderately reduces stimulation of cap-dependent translation in vitro. Impairs interaction with eIF4G. DAL->EKM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10357826;Dbxref=PMID:10357826 +P04147 UniProtKB Mutagenesis 193 197 . . . Note=In PAB1-193%3B moderately reduces stimulation of cap-dependent translation in vitro. GQEIY->DRKVF;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10357826;Dbxref=PMID:10357826 +P04147 UniProtKB Mutagenesis 199 202 . . . Note=In PAB1-199%3B moderately reduces poly(A)-dependent translation and stimulation of cap-dependent translation in vitro. APHL->GRFK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10357826;Dbxref=PMID:10357826 +P04147 UniProtKB Mutagenesis 259 259 . . . Note=In PAB1-14%3B fails to bind poly(U)%2C but not poly(A) RNA%3B when associated with A-79%3B Q-166 and Q-362. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9193001;Dbxref=PMID:9193001 +P04147 UniProtKB Mutagenesis 263 263 . . . Note=In PAB1-7. In PAB1-15%3B fails to bind RNA%3B when associated with V-83%3B V-170 and V-366. F->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9193001;Dbxref=PMID:9193001 +P04147 UniProtKB Mutagenesis 362 362 . . . Note=In PAB1-14%3B fails to bind poly(U)%2C but not poly(A) RNA%3B when associated with A-79%3B Q-166 and Q-259. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9193001;Dbxref=PMID:9193001 +P04147 UniProtKB Mutagenesis 366 366 . . . Note=In PAB1-8%3B selectively reduces poly(U) RNA binding. In PAB1-15%3B fails to bind RNA%3B when associated with V-83%3B V-170 and V-263. F->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9193001;Dbxref=PMID:9193001 +P04147 UniProtKB Sequence conflict 426 426 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04147 UniProtKB Helix 503 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IFW +P04147 UniProtKB Helix 518 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IFW +P04147 UniProtKB Helix 524 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IFW +P04147 UniProtKB Helix 539 546 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IFW +P04147 UniProtKB Helix 549 568 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IFW +##sequence-region P53343 1 120 +P53343 UniProtKB Chain 1 120 . . . ID=PRO_0000203786;Note=Seripauperin-12 +P53343 UniProtKB Transmembrane 7 24 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12370 1 124 +Q12370 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12370 UniProtKB Chain 21 124 . . . ID=PRO_0000033248;Note=Seripauperin-17 +Q12370 UniProtKB Sequence conflict 115 115 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08322 1 120 +Q08322 UniProtKB Chain 1 120 . . . ID=PRO_0000245258;Note=Seripauperin-20 +Q08322 UniProtKB Transmembrane 7 25 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38155 1 120 +P38155 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38155 UniProtKB Chain 21 120 . . . ID=PRO_0000033242;Note=Seripauperin-24 +##sequence-region P0CE92 1 120 +P0CE92 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE92 UniProtKB Chain 21 120 . . . ID=PRO_0000203785;Note=Seripauperin-8 +##sequence-region P25580 1 416 +P25580 UniProtKB Chain 1 416 . . . ID=PRO_0000058243;Note=Protein PBN1 +P25580 UniProtKB Topological domain 1 385 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25580 UniProtKB Transmembrane 386 405 . . . Note=Helical%3B Signal-anchor for type III membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25580 UniProtKB Topological domain 406 416 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25580 UniProtKB Glycosylation 24 24 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25580 UniProtKB Glycosylation 85 85 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25580 UniProtKB Glycosylation 120 120 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25580 UniProtKB Glycosylation 212 212 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25580 UniProtKB Glycosylation 365 365 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P10963 1 549 +P10963 UniProtKB Chain 1 549 . . . ID=PRO_0000203875;Note=Phosphoenolpyruvate carboxykinase (ATP) +P10963 UniProtKB Nucleotide binding 250 257 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10963 UniProtKB Sequence conflict 95 107 . . . Note=PCSERTWSINRER->HVLKEHGLSTVK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10963 UniProtKB Sequence conflict 123 123 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10963 UniProtKB Sequence conflict 322 322 . . . Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10963 UniProtKB Sequence conflict 357 357 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10963 UniProtKB Sequence conflict 431 431 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10963 UniProtKB Sequence conflict 544 549 . . . Note=AGPQFE->DWSSIRVNETC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40038 1 420 +P40038 UniProtKB Chain 1 420 . . . ID=PRO_0000202631;Note=PHO85 cyclin-6 +P40038 UniProtKB Modified residue 61 61 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40038 UniProtKB Modified residue 281 281 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40038 UniProtKB Modified residue 312 312 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40038 UniProtKB Modified residue 317 317 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40550 1 1411 +P40550 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7629127;Dbxref=PMID:7629127 +P40550 UniProtKB Chain 2 1411 . . . ID=PRO_0000093444;Note=ATP-dependent permease PDR11 +P40550 UniProtKB Topological domain 2 388 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Transmembrane 389 409 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Topological domain 410 418 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Transmembrane 419 439 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Topological domain 440 471 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Transmembrane 472 492 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Topological domain 493 494 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Transmembrane 495 515 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Topological domain 516 524 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Transmembrane 525 545 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Topological domain 546 636 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Transmembrane 637 657 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Topological domain 658 1090 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Transmembrane 1091 1111 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Topological domain 1112 1117 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Transmembrane 1118 1138 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Topological domain 1139 1175 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Transmembrane 1176 1196 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Topological domain 1197 1204 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Transmembrane 1205 1225 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Topological domain 1226 1230 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Transmembrane 1231 1251 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Topological domain 1252 1355 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Transmembrane 1356 1376 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Topological domain 1377 1411 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Domain 31 273 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P40550 UniProtKB Domain 751 979 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P40550 UniProtKB Nucleotide binding 782 789 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P40550 UniProtKB Compositional bias 708 713 . . . Note=Poly-Ser +P40550 UniProtKB Compositional bias 1046 1049 . . . Note=Poly-Leu +P40550 UniProtKB Glycosylation 595 595 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Glycosylation 1289 1289 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Glycosylation 1324 1324 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40550 UniProtKB Glycosylation 1346 1346 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04182 1 1529 +Q04182 UniProtKB Chain 1 1529 . . . ID=PRO_0000093446;Note=ATP-dependent permease PDR15 +Q04182 UniProtKB Topological domain 1 531 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Transmembrane 532 552 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Topological domain 553 567 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Transmembrane 568 588 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Topological domain 589 617 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Transmembrane 618 638 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Topological domain 639 642 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Transmembrane 643 663 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Topological domain 664 699 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Transmembrane 700 720 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Topological domain 721 783 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Transmembrane 784 804 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Topological domain 805 1219 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Transmembrane 1220 1240 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Topological domain 1241 1312 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Transmembrane 1313 1333 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Topological domain 1334 1340 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Transmembrane 1341 1361 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Topological domain 1362 1368 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Transmembrane 1369 1389 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Topological domain 1390 1396 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Transmembrane 1397 1417 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Topological domain 1418 1492 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Transmembrane 1493 1513 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Topological domain 1514 1529 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Domain 171 420 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q04182 UniProtKB Domain 884 1127 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q04182 UniProtKB Nucleotide binding 920 927 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q04182 UniProtKB Compositional bias 13 24 . . . Note=Poly-Ser +Q04182 UniProtKB Compositional bias 66 69 . . . Note=Poly-Ser +Q04182 UniProtKB Compositional bias 794 797 . . . Note=Poly-Phe +Q04182 UniProtKB Glycosylation 558 558 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04182 UniProtKB Glycosylation 744 744 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53756 1 1333 +P53756 UniProtKB Chain 1 1333 . . . ID=PRO_0000093466;Note=ABC transporter ATP-binding protein/permease PDR18 +P53756 UniProtKB Transmembrane 13 33 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Transmembrane 392 412 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Transmembrane 425 445 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Transmembrane 474 494 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Transmembrane 499 519 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Transmembrane 534 554 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Transmembrane 642 662 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Transmembrane 1071 1091 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Transmembrane 1092 1112 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Transmembrane 1150 1170 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Transmembrane 1178 1198 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Transmembrane 1210 1230 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Transmembrane 1235 1255 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Domain 30 281 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P53756 UniProtKB Domain 729 971 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P53756 UniProtKB Nucleotide binding 765 772 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P53756 UniProtKB Glycosylation 48 48 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Glycosylation 144 144 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Glycosylation 205 205 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Glycosylation 350 350 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Glycosylation 697 697 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Glycosylation 733 733 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Glycosylation 958 958 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53756 UniProtKB Glycosylation 1320 1320 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04264 1 1277 +Q04264 UniProtKB Chain 1 1277 . . . ID=PRO_0000058280;Note=Sister chromatid cohesion protein PDS5 +Q04264 UniProtKB Repeat 393 429 . . . Note=HEAT +Q04264 UniProtKB Modified residue 1231 1231 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04264 UniProtKB Modified residue 1233 1233 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04264 UniProtKB Beta strand 19 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 25 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Beta strand 44 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 53 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 62 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 70 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 95 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 120 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 136 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 145 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 165 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 168 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 187 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 215 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 228 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 254 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 274 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 281 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 293 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 315 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 320 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 328 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 335 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 345 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 358 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 372 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 387 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 397 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 406 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 412 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Beta strand 437 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 440 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 449 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 456 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 462 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 483 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 499 526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 527 529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Turn 530 532 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Beta strand 535 539 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 540 555 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 561 574 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 577 587 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 593 607 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 626 640 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Beta strand 643 646 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 648 653 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 662 678 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Turn 680 682 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 683 690 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q04264 UniProtKB Helix 692 696 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +##sequence-region P36139 1 283 +P36139 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3 +P36139 UniProtKB Chain 2 283 . . . ID=PRO_0000058317;Note=Protein PET10 +P36139 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3 +##sequence-region Q12462 1 236 +Q12462 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7721939,ECO:0000269|PubMed:7860627;Dbxref=PMID:7721939,PMID:7860627 +Q12462 UniProtKB Chain 2 236 . . . ID=PRO_0000105974;Note=Peroxisomal membrane protein PMP27 +##sequence-region P53112 1 341 +P53112 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53112 UniProtKB Chain 2 341 . . . ID=PRO_0000058329;Note=Peroxisomal membrane protein PEX14 +P53112 UniProtKB Motif 86 94 . . . Note=SH3-binding +P53112 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53112 UniProtKB Modified residue 313 313 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53112 UniProtKB Mutagenesis 87 90 . . . Note=Loss of interaction with SH3 domain of PEX13. No effect on membrane association. PTLP->ATLA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10087260;Dbxref=PMID:10087260 +##sequence-region P24004 1 1043 +P24004 UniProtKB Chain 1 1043 . . . ID=PRO_0000084606;Note=Peroxisomal ATPase PEX1 +P24004 UniProtKB Nucleotide binding 461 468 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P24004 UniProtKB Nucleotide binding 738 745 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P24004 UniProtKB Region 453 626 . . . Note=AAA-cassette D1 +P24004 UniProtKB Region 733 926 . . . Note=AAA-cassette D2 +P24004 UniProtKB Mutagenesis 467 467 . . . Note=In PEX1pA1%3B no effect. K->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15634331,ECO:0000269|PubMed:16007078,ECO:0000269|PubMed:7725796;Dbxref=PMID:15634331,PMID:16007078,PMID:7725796 +P24004 UniProtKB Mutagenesis 525 525 . . . Note=In PEX1pB1%3B no effect. D->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15634331,ECO:0000269|PubMed:16007078;Dbxref=PMID:15634331,PMID:16007078 +P24004 UniProtKB Mutagenesis 744 744 . . . Note=In PEX1pA2%3B decreased binding to PEX6. Results in accumulation of PEX5 on peroxisomal membranes. K->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15634331,ECO:0000269|PubMed:16007078,ECO:0000269|PubMed:7725796;Dbxref=PMID:15634331,PMID:16007078,PMID:7725796 +P24004 UniProtKB Mutagenesis 797 797 . . . Note=In PEX1pB2%3B results in accumulation of PEX5 on peroxisomal membranes. D->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15634331,ECO:0000269|PubMed:16007078;Dbxref=PMID:15634331,PMID:16007078 +P24004 UniProtKB Sequence conflict 354 354 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03370 1 554 +Q03370 UniProtKB Chain 1 554 . . . ID=PRO_0000252269;Note=Peroxisomal membrane protein PEX29 +Q03370 UniProtKB Topological domain 1 145 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03370 UniProtKB Transmembrane 146 166 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03370 UniProtKB Topological domain 167 172 . . . Note=Peroxisomal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03370 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03370 UniProtKB Topological domain 194 264 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03370 UniProtKB Transmembrane 265 285 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03370 UniProtKB Topological domain 286 287 . . . Note=Peroxisomal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03370 UniProtKB Transmembrane 288 308 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03370 UniProtKB Topological domain 309 554 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39108 1 375 +P39108 UniProtKB Chain 1 375 . . . ID=PRO_0000051120;Note=Peroxisomal targeting signal 2 receptor +P39108 UniProtKB Repeat 58 89 . . . Note=WD 1 +P39108 UniProtKB Repeat 102 133 . . . Note=WD 2 +P39108 UniProtKB Repeat 172 203 . . . Note=WD 3 +P39108 UniProtKB Repeat 218 249 . . . Note=WD 4 +P39108 UniProtKB Repeat 281 312 . . . Note=WD 5 +P39108 UniProtKB Repeat 340 372 . . . Note=WD 6 +P39108 UniProtKB Beta strand 2 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 9 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 23 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Helix 31 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 38 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 51 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 63 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 75 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 83 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 97 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 107 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 114 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 120 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 129 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 140 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Helix 148 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Helix 158 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 177 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 189 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 197 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 210 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 223 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 235 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 245 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 274 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 281 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 286 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 298 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 308 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Turn 326 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Turn 330 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 334 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 345 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 352 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 358 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P39108 UniProtKB Beta strand 366 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +##sequence-region P48363 1 199 +P48363 UniProtKB Chain 1 199 . . . ID=PRO_0000153659;Note=Prefoldin subunit 3 +P48363 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region Q04493 1 163 +Q04493 UniProtKB Chain 1 163 . . . ID=PRO_0000153668;Note=Prefoldin subunit 5 +##sequence-region P53170 1 491 +P53170 UniProtKB Domain 153 480 . . . Note=Histidine kinase +P53170 UniProtKB Nucleotide binding 300 307 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53170 UniProtKB Nucleotide binding 359 360 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53170 UniProtKB Nucleotide binding 383 446 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53170 UniProtKB Binding site 341 341 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53170 UniProtKB Sequence conflict 224 225 . . . Note=SI->VY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53170 UniProtKB Sequence conflict 224 225 . . . Note=SI->VY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53860 1 351 +P53860 UniProtKB Chain 1 351 . . . ID=PRO_0000210745;Note=Phosphatidylinositol transfer protein PDR16 +P53860 UniProtKB Domain 135 295 . . . Note=CRAL-TRIO;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00056 +P53860 UniProtKB Beta strand 19 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Helix 42 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Beta strand 61 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Beta strand 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Helix 79 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Helix 87 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Turn 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M8Z +P53860 UniProtKB Helix 101 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Helix 125 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Helix 133 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Helix 137 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Beta strand 144 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Beta strand 156 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Helix 162 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Helix 171 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Beta strand 195 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Helix 221 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Beta strand 237 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Helix 247 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Helix 257 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Helix 262 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Beta strand 268 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FMM +P53860 UniProtKB Helix 274 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Helix 280 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Helix 285 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Beta strand 289 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Helix 297 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +P53860 UniProtKB Helix 330 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J7Q +##sequence-region P38075 1 228 +P38075 UniProtKB Chain 1 228 . . . ID=PRO_0000167787;Note=Pyridoxamine 5'-phosphate oxidase +P38075 UniProtKB Nucleotide binding 73 76 . . . Note=FMN;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7 +P38075 UniProtKB Nucleotide binding 88 89 . . . Note=FMN;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7 +P38075 UniProtKB Nucleotide binding 95 96 . . . Note=FMN;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7 +P38075 UniProtKB Nucleotide binding 153 154 . . . Note=FMN;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7 +P38075 UniProtKB Region 20 23 . . . Note=Pyridoxal 5'-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AFI7 +P38075 UniProtKB Region 205 207 . . . Note=Pyridoxal 5'-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AFI7 +P38075 UniProtKB Binding site 78 78 . . . Note=Pyridoxal 5'-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NVS9 +P38075 UniProtKB Binding site 118 118 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AFI7 +P38075 UniProtKB Binding site 136 136 . . . Note=Pyridoxal 5'-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NVS9 +P38075 UniProtKB Binding site 140 140 . . . Note=Pyridoxal 5'-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NVS9 +P38075 UniProtKB Binding site 144 144 . . . Note=Pyridoxal 5'-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NVS9 +P38075 UniProtKB Binding site 199 199 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AFI7 +P38075 UniProtKB Binding site 209 209 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AFI7 +P38075 UniProtKB Cross-link 29 29 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P38075 UniProtKB Helix 28 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0 +P38075 UniProtKB Helix 35 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0 +P38075 UniProtKB Beta strand 57 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0 +P38075 UniProtKB Turn 65 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0 +P38075 UniProtKB Beta strand 69 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0 +P38075 UniProtKB Beta strand 82 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0 +P38075 UniProtKB Beta strand 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0 +P38075 UniProtKB Helix 95 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0 +P38075 UniProtKB Beta strand 105 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0 +P38075 UniProtKB Turn 113 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0 +P38075 UniProtKB Beta strand 117 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0 +P38075 UniProtKB Helix 130 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0 +P38075 UniProtKB Helix 142 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0 +P38075 UniProtKB Beta strand 156 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0 +P38075 UniProtKB Helix 160 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0 +P38075 UniProtKB Beta strand 186 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0 +P38075 UniProtKB Beta strand 208 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0 +P38075 UniProtKB Beta strand 222 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CI0 +##sequence-region P25362 1 215 +P25362 UniProtKB Chain 1 215 . . . ID=PRO_0000192043;Note=Protein PET18 +P25362 UniProtKB Sequence conflict 40 40 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25362 UniProtKB Sequence conflict 104 104 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25362 UniProtKB Sequence conflict 122 122 . . . Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P80667 1 386 +P80667 UniProtKB Chain 1 386 . . . ID=PRO_0000058324;Note=Peroxisomal membrane protein PAS20 +P80667 UniProtKB Topological domain 1 263 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P80667 UniProtKB Transmembrane 264 280 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P80667 UniProtKB Topological domain 281 386 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P80667 UniProtKB Domain 306 372 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P80667 UniProtKB Helix 305 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1R +P80667 UniProtKB Beta strand 309 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1R +P80667 UniProtKB Turn 322 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1R +P80667 UniProtKB Beta strand 333 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1R +P80667 UniProtKB Beta strand 346 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1R +P80667 UniProtKB Turn 355 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NM7 +P80667 UniProtKB Beta strand 359 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1R +P80667 UniProtKB Helix 364 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1R +P80667 UniProtKB Beta strand 367 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1R +##sequence-region P50091 1 288 +P50091 UniProtKB Chain 1 288 . . . ID=PRO_0000202855;Note=Peroxisomal membrane protein PEX21 +P50091 UniProtKB Helix 198 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P50091 UniProtKB Helix 225 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P50091 UniProtKB Helix 235 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P50091 UniProtKB Beta strand 247 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P50091 UniProtKB Beta strand 262 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P50091 UniProtKB Turn 265 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +P50091 UniProtKB Beta strand 269 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W15 +##sequence-region P25584 1 144 +P25584 UniProtKB Chain 1 144 . . . ID=PRO_0000202551;Note=Peroxisomal membrane protein PEX34 +P25584 UniProtKB Transmembrane 18 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25584 UniProtKB Transmembrane 52 73 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25584 UniProtKB Transmembrane 109 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47116 1 818 +P47116 UniProtKB Chain 1 818 . . . ID=PRO_0000086591;Note=Serine/threonine-protein kinase PTK2/STK2 +P47116 UniProtKB Domain 255 562 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P47116 UniProtKB Nucleotide binding 261 269 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P47116 UniProtKB Active site 388 388 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P47116 UniProtKB Binding site 285 285 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P47116 UniProtKB Modified residue 56 56 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P47116 UniProtKB Modified residue 59 59 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47116 UniProtKB Modified residue 80 80 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P47116 UniProtKB Modified residue 623 623 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P47116 UniProtKB Modified residue 632 632 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47116 UniProtKB Modified residue 694 694 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47116 UniProtKB Modified residue 700 700 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47116 UniProtKB Modified residue 711 711 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P47116 UniProtKB Modified residue 737 737 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P47116 UniProtKB Modified residue 752 752 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P47116 UniProtKB Modified residue 755 755 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P47116 UniProtKB Modified residue 778 778 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47116 UniProtKB Modified residue 781 781 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47116 UniProtKB Sequence conflict 801 801 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P29461 1 750 +P29461 UniProtKB Chain 1 750 . . . ID=PRO_0000094856;Note=Tyrosine-protein phosphatase 2 +P29461 UniProtKB Domain 383 737 . . . Note=Tyrosine-protein phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00160 +P29461 UniProtKB Active site 666 666 . . . Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00160,ECO:0000255|PROSITE-ProRule:PRU10044 +P29461 UniProtKB Modified residue 258 258 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P29461 UniProtKB Modified residue 430 430 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P29461 UniProtKB Sequence conflict 371 371 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29461 UniProtKB Sequence conflict 474 475 . . . Note=KL->NV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29461 UniProtKB Sequence conflict 660 661 . . . Note=SP->GA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P07244 1 802 +P07244 UniProtKB Chain 1 802 . . . ID=PRO_0000074941;Note=Bifunctional purine biosynthetic protein ADE5%2C7 +P07244 UniProtKB Domain 114 330 . . . Note=ATP-grasp +P07244 UniProtKB Nucleotide binding 140 203 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07244 UniProtKB Region 1 450 . . . Note=GARS +P07244 UniProtKB Region 451 802 . . . Note=AIRS +P07244 UniProtKB Metal binding 298 298 . . . Note=Manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07244 UniProtKB Metal binding 300 300 . . . Note=Manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07244 UniProtKB Modified residue 455 455 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P07244 UniProtKB Modified residue 458 458 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07244 UniProtKB Sequence conflict 28 28 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P54113 1 591 +P54113 UniProtKB Chain 1 591 . . . ID=PRO_0000192159;Note=Bifunctional purine biosynthesis protein ADE16 +##sequence-region P53294 1 404 +P53294 UniProtKB Chain 1 404 . . . ID=PRO_0000162757;Note=tRNA pseudouridine(31) synthase +P53294 UniProtKB Active site 168 168 . . . . +P53294 UniProtKB Mutagenesis 168 168 . . . Note=Loss of function. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11406626;Dbxref=PMID:11406626 +##sequence-region Q12069 1 462 +Q12069 UniProtKB Transit peptide 1 24 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12069 UniProtKB Chain 25 462 . . . ID=PRO_0000162756;Note=tRNA pseudouridine(32) synthase%2C mitochondrial +Q12069 UniProtKB Domain 127 188 . . . Note=S4 RNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00182 +Q12069 UniProtKB Active site 238 238 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12069 UniProtKB Sequence conflict 458 458 . . . Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P09368 1 476 +P09368 UniProtKB Sequence conflict 50 50 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09368 UniProtKB Sequence conflict 185 185 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P03962 1 267 +P03962 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P03962 UniProtKB Chain 2 267 . . . ID=PRO_0000134692;Note=Orotidine 5'-phosphate decarboxylase +P03962 UniProtKB Region 59 61 . . . Note=Substrate binding +P03962 UniProtKB Region 91 100 . . . Note=Substrate binding +P03962 UniProtKB Active site 93 93 . . . Note=Proton donor +P03962 UniProtKB Binding site 37 37 . . . Note=Substrate +P03962 UniProtKB Binding site 217 217 . . . Note=Substrate +P03962 UniProtKB Binding site 235 235 . . . Note=Substrate +P03962 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P03962 UniProtKB Cross-link 93 93 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P03962 UniProtKB Cross-link 209 209 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P03962 UniProtKB Cross-link 253 253 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P03962 UniProtKB Natural variant 160 160 . . . Note=In strain: +D4. A->S +P03962 UniProtKB Mutagenesis 59 59 . . . Note=Reduces Kcat 100-fold. Reduces substrate affinity 900-fold. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278904;Dbxref=PMID:11278904 +P03962 UniProtKB Mutagenesis 91 91 . . . Note=Reduces activity over 100000-fold. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278904;Dbxref=PMID:11278904 +P03962 UniProtKB Mutagenesis 93 93 . . . Note=Reduces activity over 100000-fold. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278904;Dbxref=PMID:11278904 +P03962 UniProtKB Mutagenesis 96 96 . . . Note=Reduces Kcat over 100000-fold. Reduces substrate affinity 11-fold. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278904;Dbxref=PMID:11278904 +P03962 UniProtKB Mutagenesis 215 215 . . . Note=No effect. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278904;Dbxref=PMID:11278904 +P03962 UniProtKB Sequence conflict 71 73 . . . Note=EGT->RIR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03962 UniProtKB Helix 6 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Helix 16 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Beta strand 32 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Helix 41 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Helix 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Beta strand 56 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Helix 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Turn 70 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Helix 74 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Beta strand 87 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Helix 98 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Turn 108 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Helix 112 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Beta strand 117 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Helix 123 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Helix 128 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Beta strand 146 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Helix 162 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Turn 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Beta strand 179 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Helix 191 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Beta strand 198 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Beta strand 203 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Turn 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DQW +P03962 UniProtKB Helix 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Beta strand 217 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Helix 220 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Beta strand 229 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Helix 235 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +P03962 UniProtKB Helix 244 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GDM +##sequence-region Q9ZZX9 1 128 +Q9ZZX9 UniProtKB Chain 1 128 . . . ID=PRO_0000299678;Note=Putative uncharacterized protein Q0010%2C mitochondrial +##sequence-region Q9ZZW4 1 58 +Q9ZZW4 UniProtKB Chain 1 58 . . . ID=PRO_0000299682;Note=Putative uncharacterized protein Q0142%2C mitochondrial +##sequence-region Q9ZZW2 1 109 +Q9ZZW2 UniProtKB Chain 1 109 . . . ID=PRO_0000299684;Note=Putative uncharacterized protein Q0144%2C mitochondrial +##sequence-region P43122 1 407 +P43122 UniProtKB Transit peptide 1 30 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03179 +P43122 UniProtKB Chain 31 407 . . . ID=PRO_0000096988;Note=tRNA N6-adenosine threonylcarbamoyltransferase%2C mitochondrial;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03179 +P43122 UniProtKB Region 170 174 . . . Note=Substrate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03179,ECO:0000269|PubMed:25084372;Dbxref=PMID:25084372 +P43122 UniProtKB Region 328 329 . . . Note=Substrate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03179,ECO:0000269|PubMed:25084372;Dbxref=PMID:25084372 +P43122 UniProtKB Metal binding 145 145 . . . Note=Divalent metal cation;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03179,ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P43122 UniProtKB Metal binding 149 149 . . . Note=Divalent metal cation;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03179,ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P43122 UniProtKB Metal binding 361 361 . . . Note=Divalent metal cation;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03179,ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P43122 UniProtKB Binding site 203 203 . . . Note=Substrate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03179,ECO:0000269|PubMed:25084372;Dbxref=PMID:25084372 +P43122 UniProtKB Binding site 217 217 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03179,ECO:0000269|PubMed:25084372;Dbxref=PMID:25084372 +P43122 UniProtKB Binding site 221 221 . . . Note=Substrate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03179,ECO:0000269|PubMed:25084372;Dbxref=PMID:25084372 +P43122 UniProtKB Binding site 360 360 . . . Note=Substrate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03179,ECO:0000269|PubMed:25084372;Dbxref=PMID:25084372 +P43122 UniProtKB Mutagenesis 39 39 . . . Note=Severely impairs t(6)A37 formation. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P43122 UniProtKB Mutagenesis 43 43 . . . Note=Severely impairs t(6)A37 formation. No effect on dimer formation. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P43122 UniProtKB Mutagenesis 44 44 . . . Note=Severely impairs t(6)A37 formation. No effect on dimer formation. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P43122 UniProtKB Mutagenesis 77 77 . . . Note=Severely impairs t(6)A37 formation. No effect on dimer formation. I->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P43122 UniProtKB Mutagenesis 104 104 . . . Note=Reduces enzyme activity by 35%25. Partially impairs dimer formation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P43122 UniProtKB Mutagenesis 130 130 . . . Note=Severely impairs t(6)A37 formation. Partially impairs dimer formation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P43122 UniProtKB Mutagenesis 134 134 . . . Note=Severely impairs t(6)A37 formation. Prevents dimerization. V->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P43122 UniProtKB Mutagenesis 145 145 . . . Note=Severely impairs t(6)A37 formation. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P43122 UniProtKB Mutagenesis 149 149 . . . Note=Severely impairs t(6)A37 formation. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P43122 UniProtKB Mutagenesis 172 172 . . . Note=Severely impairs t(6)A37 formation. S->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P43122 UniProtKB Mutagenesis 207 207 . . . Note=Severely impairs t(6)A37 formation. No effect on dimer formation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P43122 UniProtKB Mutagenesis 258 258 . . . Note=Severely impairs t(6)A37 formation. No effect on dimer formation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P43122 UniProtKB Mutagenesis 361 361 . . . Note=Severely impairs t(6)A37 formation. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P43122 UniProtKB Beta strand 34 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Beta strand 41 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Beta strand 60 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Helix 82 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Beta strand 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Beta strand 109 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Beta strand 115 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Helix 119 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Beta strand 140 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Helix 145 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Helix 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Turn 155 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Beta strand 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WUH +P43122 UniProtKB Beta strand 164 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Beta strand 176 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Beta strand 187 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Helix 198 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Beta strand 213 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Helix 216 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Beta strand 227 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Beta strand 253 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Helix 259 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Turn 276 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Helix 281 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Turn 311 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Beta strand 320 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Helix 326 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Helix 330 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Turn 340 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Beta strand 344 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Beta strand 350 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WUH +P43122 UniProtKB Helix 356 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Helix 364 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Beta strand 379 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Turn 394 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +P43122 UniProtKB Beta strand 402 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4K25 +##sequence-region P41903 1 349 +P41903 UniProtKB Chain 1 349 . . . ID=PRO_0000202158;Note=Peroxisomal acyl-coenzyme A thioester hydrolase 1 +P41903 UniProtKB Motif 347 349 . . . Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41903 UniProtKB Active site 259 259 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41903 UniProtKB Active site 282 282 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41903 UniProtKB Active site 333 333 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41903 UniProtKB Beta strand 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TBU +P41903 UniProtKB Beta strand 21 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TBU +P41903 UniProtKB Helix 42 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TBU +P41903 UniProtKB Beta strand 62 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TBU +P41903 UniProtKB Beta strand 81 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TBU +P41903 UniProtKB Beta strand 91 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TBU +P41903 UniProtKB Beta strand 105 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TBU +##sequence-region P25339 1 888 +P25339 UniProtKB Chain 1 888 . . . ID=PRO_0000075925;Note=Pumilio homology domain family member 4 +P25339 UniProtKB Domain 539 888 . . . Note=PUM-HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00318 +P25339 UniProtKB Repeat 563 598 . . . Note=Pumilio 1 +P25339 UniProtKB Repeat 599 634 . . . Note=Pumilio 2 +P25339 UniProtKB Repeat 635 671 . . . Note=Pumilio 3 +P25339 UniProtKB Repeat 672 707 . . . Note=Pumilio 4 +P25339 UniProtKB Repeat 708 743 . . . Note=Pumilio 5 +P25339 UniProtKB Repeat 744 783 . . . Note=Pumilio 6 +P25339 UniProtKB Repeat 784 821 . . . Note=Pumilio 7 +P25339 UniProtKB Repeat 823 861 . . . Note=Pumilio 8 +P25339 UniProtKB Compositional bias 8 38 . . . Note=Asp/Glu-rich (acidic) +P25339 UniProtKB Compositional bias 471 542 . . . Note=Asn-rich +P25339 UniProtKB Compositional bias 521 535 . . . Note=Poly-Asn +P25339 UniProtKB Modified residue 205 205 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P25339 UniProtKB Modified residue 212 212 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P25339 UniProtKB Modified residue 252 252 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25339 UniProtKB Modified residue 256 256 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25339 UniProtKB Sequence conflict 595 595 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25339 UniProtKB Sequence conflict 595 595 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25339 UniProtKB Turn 555 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 561 563 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Turn 564 566 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 568 571 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Beta strand 572 574 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DZS +P25339 UniProtKB Helix 575 587 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 590 600 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 601 603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 604 608 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 613 623 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 626 636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 637 639 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 640 645 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 649 659 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 663 673 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 674 676 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 677 681 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 686 696 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 699 711 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 713 717 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 722 732 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 735 746 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 749 753 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 758 772 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 777 785 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 786 788 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 789 793 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 798 806 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 809 821 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 824 832 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 837 851 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 853 863 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 864 866 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 869 873 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Helix 875 881 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BWT +P25339 UniProtKB Beta strand 883 885 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DZS +##sequence-region Q06991 1 263 +Q06991 UniProtKB Chain 1 263 . . . ID=PRO_0000247353;Note=Protein PUN1 +Q06991 UniProtKB Topological domain 1 6 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06991 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06991 UniProtKB Topological domain 28 143 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06991 UniProtKB Transmembrane 144 164 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06991 UniProtKB Topological domain 165 172 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06991 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06991 UniProtKB Topological domain 194 223 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06991 UniProtKB Transmembrane 224 244 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06991 UniProtKB Topological domain 245 263 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06991 UniProtKB Glycosylation 100 100 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06991 UniProtKB Glycosylation 209 209 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06991 UniProtKB Cross-link 260 260 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q06991 UniProtKB Sequence conflict 42 42 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38972 1 1358 +P38972 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38972 UniProtKB Chain 2 1358 . . . ID=PRO_0000100405;Note=Phosphoribosylformylglycinamidine synthase +P38972 UniProtKB Domain 1093 1358 . . . Note=Glutamine amidotransferase type-1 +P38972 UniProtKB Nucleotide binding 345 356 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38972 UniProtKB Nucleotide binding 424 426 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38972 UniProtKB Active site 1187 1187 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38972 UniProtKB Active site 1319 1319 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38972 UniProtKB Active site 1321 1321 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38972 UniProtKB Metal binding 720 720 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38972 UniProtKB Metal binding 762 762 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38972 UniProtKB Metal binding 766 766 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38972 UniProtKB Metal binding 930 930 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38972 UniProtKB Binding site 719 719 . . . Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38972 UniProtKB Binding site 932 932 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38972 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38972 UniProtKB Sequence conflict 84 84 . . . Note=A->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38972 UniProtKB Sequence conflict 219 220 . . . Note=DS->EC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38972 UniProtKB Sequence conflict 226 226 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38972 UniProtKB Sequence conflict 492 492 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38972 UniProtKB Sequence conflict 499 499 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38972 UniProtKB Sequence conflict 551 551 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38972 UniProtKB Sequence conflict 604 604 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38972 UniProtKB Sequence conflict 1169 1170 . . . Note=SQ->TSSK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38972 UniProtKB Sequence conflict 1298 1298 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53167 1 370 +P53167 UniProtKB Chain 1 370 . . . ID=PRO_0000057532;Note=tRNA pseudouridine(27/28) synthase +P53167 UniProtKB Active site 56 56 . . . Note=Nucleophile +P53167 UniProtKB Binding site 111 111 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53167 UniProtKB Mutagenesis 56 56 . . . Note=Abolishes catalytic activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17684231;Dbxref=PMID:17684231 +P53167 UniProtKB Sequence conflict 136 136 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53167 UniProtKB Sequence conflict 136 136 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P11154 1 1178 +P11154 UniProtKB Chain 1 1178 . . . ID=PRO_0000146824;Note=Pyruvate carboxylase 1 +P11154 UniProtKB Domain 18 470 . . . Note=Biotin carboxylation +P11154 UniProtKB Domain 140 337 . . . Note=ATP-grasp;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 +P11154 UniProtKB Domain 557 824 . . . Note=Pyruvate carboxyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01151 +P11154 UniProtKB Domain 1094 1169 . . . Note=Biotinyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066 +P11154 UniProtKB Region 565 569 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11154 UniProtKB Active site 312 312 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11154 UniProtKB Metal binding 566 566 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11154 UniProtKB Metal binding 734 734 . . . Note=Divalent metal cation%3B via carbamate group;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11154 UniProtKB Metal binding 764 764 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11154 UniProtKB Metal binding 766 766 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11154 UniProtKB Binding site 136 136 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11154 UniProtKB Binding site 220 220 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11154 UniProtKB Binding site 255 255 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11154 UniProtKB Binding site 638 638 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11154 UniProtKB Binding site 898 898 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11154 UniProtKB Modified residue 734 734 . . . Note=N6-carboxylysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11154 UniProtKB Modified residue 1135 1135 . . . Note=N6-biotinyllysine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU01066,ECO:0000269|PubMed:3042770;Dbxref=PMID:3042770 +P11154 UniProtKB Sequence conflict 462 462 . . . Note=T->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11154 UniProtKB Sequence conflict 493 493 . . . Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11154 UniProtKB Sequence conflict 595 595 . . . Note=R->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11154 UniProtKB Sequence conflict 619 619 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11154 UniProtKB Sequence conflict 664 664 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11154 UniProtKB Sequence conflict 772 772 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11154 UniProtKB Sequence conflict 879 879 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11154 UniProtKB Sequence conflict 909 909 . . . Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P28272 1 314 +P28272 UniProtKB Chain 1 314 . . . ID=PRO_0000148506;Note=Dihydroorotate dehydrogenase (fumarate) +P28272 UniProtKB Nucleotide binding 46 47 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28272 UniProtKB Nucleotide binding 252 253 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28272 UniProtKB Nucleotide binding 274 275 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28272 UniProtKB Region 70 74 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28272 UniProtKB Region 196 197 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28272 UniProtKB Active site 133 133 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28272 UniProtKB Binding site 46 46 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28272 UniProtKB Binding site 130 130 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28272 UniProtKB Binding site 130 130 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28272 UniProtKB Binding site 167 167 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28272 UniProtKB Binding site 195 195 . . . Note=FMN%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28272 UniProtKB Binding site 224 224 . . . Note=FMN%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28272 UniProtKB Cross-link 46 46 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P28272 UniProtKB Natural variant 58 58 . . . Note=In strain: CLIB 95%2C CLIB 219%2C CLIB 382%2C CLIB 388%2C CLIB 413%2C CLIB 556%2C CLIB 630%2C K1%2C R12%2C R13%2C YIIc12 and YIIc17. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +##sequence-region Q9ZZV8 1 51 +Q9ZZV8 UniProtKB Chain 1 51 . . . ID=PRO_0000299686;Note=Putative uncharacterized protein Q0297%2C mitochondrial +##sequence-region Q12355 1 444 +Q12355 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12355 UniProtKB Chain 20 419 . . . ID=PRO_0000033193;Note=Cell wall mannoprotein PST1 +Q12355 UniProtKB Propeptide 420 444 . . . ID=PRO_0000033194;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12355 UniProtKB Compositional bias 22 26 . . . Note=Poly-Ser +Q12355 UniProtKB Compositional bias 356 416 . . . Note=Ser-rich +Q12355 UniProtKB Lipidation 419 419 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12355 UniProtKB Glycosylation 57 57 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12355 UniProtKB Glycosylation 76 76 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12355 UniProtKB Glycosylation 83 83 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12355 UniProtKB Glycosylation 86 86 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12355 UniProtKB Glycosylation 196 196 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12355 UniProtKB Glycosylation 210 210 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17024473;Dbxref=PMID:17024473 +Q12355 UniProtKB Glycosylation 228 228 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17024473;Dbxref=PMID:17024473 +Q12355 UniProtKB Glycosylation 235 235 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17024473;Dbxref=PMID:17024473 +Q12355 UniProtKB Glycosylation 242 242 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17024473;Dbxref=PMID:17024473 +Q12355 UniProtKB Glycosylation 263 263 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12355 UniProtKB Glycosylation 268 268 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12355 UniProtKB Glycosylation 280 280 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12355 UniProtKB Glycosylation 292 292 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12355 UniProtKB Glycosylation 305 305 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12355 UniProtKB Glycosylation 329 329 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17024473;Dbxref=PMID:17024473 +##sequence-region P39927 1 425 +P39927 UniProtKB Chain 1 425 . . . ID=PRO_0000076294;Note=Protein PTI1 +P39927 UniProtKB Modified residue 272 272 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39927 UniProtKB Sequence conflict 300 300 . . . Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P27616 1 306 +P27616 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:9551557;Dbxref=PMID:22814378,PMID:9551557 +P27616 UniProtKB Chain 2 306 . . . ID=PRO_0000100929;Note=Phosphoribosylaminoimidazole-succinocarboxamide synthase +P27616 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:9551557;Dbxref=PMID:22814378,PMID:9551557 +P27616 UniProtKB Sequence conflict 185 185 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27616 UniProtKB Sequence conflict 185 185 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27616 UniProtKB Beta strand 14 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Beta strand 19 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Beta strand 30 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Helix 53 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Turn 68 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Beta strand 72 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Helix 85 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Helix 91 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Helix 96 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Beta strand 105 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Beta strand 116 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Helix 127 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Beta strand 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Beta strand 153 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Helix 176 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Helix 185 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Beta strand 211 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Turn 224 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Beta strand 228 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Turn 238 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Beta strand 241 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Turn 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Turn 258 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNU +P27616 UniProtKB Helix 261 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +P27616 UniProtKB Helix 282 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CNQ +##sequence-region Q05911 1 482 +Q05911 UniProtKB Chain 1 482 . . . ID=PRO_0000137899;Note=Adenylosuccinate lyase +Q05911 UniProtKB Region 14 15 . . . Note=Substrate binding%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05911 UniProtKB Region 82 84 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05911 UniProtKB Region 108 109 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05911 UniProtKB Active site 156 156 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05911 UniProtKB Active site 286 286 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05911 UniProtKB Binding site 238 238 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05911 UniProtKB Binding site 300 300 . . . Note=Substrate%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05911 UniProtKB Binding site 326 326 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05911 UniProtKB Binding site 331 331 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05911 UniProtKB Binding site 335 335 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q05911 UniProtKB Cross-link 196 196 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region Q35811 1 46 +Q35811 UniProtKB Chain 1 46 . . . ID=PRO_0000299681;Note=Putative uncharacterized protein Q0092%2C mitochondrial +##sequence-region Q9ZZW1 1 134 +Q9ZZW1 UniProtKB Chain 1 134 . . . ID=PRO_0000299685;Note=Putative uncharacterized protein Q0182%2C mitochondrial +##sequence-region P04046 1 510 +P04046 UniProtKB Chain 1 510 . . . ID=PRO_0000139647;Note=Amidophosphoribosyltransferase +P04046 UniProtKB Domain 2 239 . . . Note=Glutamine amidotransferase type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609 +P04046 UniProtKB Active site 2 2 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00609 +P04046 UniProtKB Metal binding 373 373 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04046 UniProtKB Metal binding 374 374 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04046 UniProtKB Sequence conflict 46 47 . . . Note=IY->VC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04046 UniProtKB Sequence conflict 46 47 . . . Note=IY->VC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04046 UniProtKB Sequence conflict 62 62 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04046 UniProtKB Sequence conflict 62 62 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04046 UniProtKB Sequence conflict 82 87 . . . Note=GSSANS->PLRLIL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04046 UniProtKB Sequence conflict 156 158 . . . Note=VFH->GFSN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04046 UniProtKB Sequence conflict 156 158 . . . Note=VFH->GFSN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04046 UniProtKB Sequence conflict 234 234 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04046 UniProtKB Sequence conflict 234 234 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04046 UniProtKB Sequence conflict 291 291 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04046 UniProtKB Sequence conflict 291 291 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38009 1 592 +P38009 UniProtKB Chain 1 592 . . . ID=PRO_0000192160;Note=Bifunctional purine biosynthesis protein ADE17 +P38009 UniProtKB Sequence conflict 389 389 . . . Note=R->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06244 1 254 +Q06244 UniProtKB Chain 1 254 . . . ID=PRO_0000162754;Note=21S rRNA pseudouridine(2819) synthase +Q06244 UniProtKB Active site 71 71 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P25502 1 979 +P25502 UniProtKB Chain 1 979 . . . ID=PRO_0000114968;Note=Proline utilization trans-activator +P25502 UniProtKB DNA binding 34 60 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P25502 UniProtKB Metal binding 34 34 . . . Note=Zinc 1 +P25502 UniProtKB Metal binding 34 34 . . . Note=Zinc 2 +P25502 UniProtKB Metal binding 37 37 . . . Note=Zinc 1 +P25502 UniProtKB Metal binding 44 44 . . . Note=Zinc 1 +P25502 UniProtKB Metal binding 50 50 . . . Note=Zinc 1 +P25502 UniProtKB Metal binding 50 50 . . . Note=Zinc 2 +P25502 UniProtKB Metal binding 53 53 . . . Note=Zinc 2 +P25502 UniProtKB Metal binding 60 60 . . . Note=Zinc 2 +P25502 UniProtKB Helix 35 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZME +P25502 UniProtKB Beta strand 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZME +P25502 UniProtKB Helix 51 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZME +P25502 UniProtKB Beta strand 68 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZME +P25502 UniProtKB Helix 73 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZME +##sequence-region P08525 1 94 +P08525 UniProtKB Chain 1 94 . . . ID=PRO_0000193551;Note=Cytochrome b-c1 complex subunit 8 +P08525 UniProtKB Beta strand 23 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08525 UniProtKB Helix 31 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08525 UniProtKB Beta strand 36 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PD4 +P08525 UniProtKB Turn 41 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08525 UniProtKB Beta strand 45 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08525 UniProtKB Helix 50 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08525 UniProtKB Helix 56 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08525 UniProtKB Helix 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P08525 UniProtKB Helix 86 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +##sequence-region P38230 1 334 +P38230 UniProtKB Chain 1 334 . . . ID=PRO_0000160912;Note=Probable quinone oxidoreductase +P38230 UniProtKB Beta strand 7 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Helix 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Beta strand 23 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Beta strand 37 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Helix 51 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Beta strand 63 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Beta strand 69 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Beta strand 90 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Beta strand 99 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Beta strand 109 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Helix 120 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Beta strand 151 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Helix 160 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Beta strand 175 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Helix 183 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Beta strand 195 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Turn 200 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Helix 205 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Turn 213 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Beta strand 218 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Helix 226 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Helix 230 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Beta strand 237 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Helix 248 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWA +P38230 UniProtKB Helix 258 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Turn 262 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Beta strand 267 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Helix 273 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Helix 280 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Beta strand 303 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Helix 309 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Helix 312 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +P38230 UniProtKB Beta strand 326 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QWB +##sequence-region P06838 1 210 +P06838 UniProtKB Chain 1 210 . . . ID=PRO_0000097149;Note=DNA repair protein RAD10 +P06838 UniProtKB DNA binding 133 153 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06838 UniProtKB Motif 17 23 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32641 1 659 +P32641 UniProtKB Chain 1 659 . . . ID=PRO_0000209953;Note=Checkpoint protein RAD24 +P32641 UniProtKB Nucleotide binding 109 116 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32641 UniProtKB Modified residue 652 652 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32641 UniProtKB Modified residue 654 654 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32641 UniProtKB Mutagenesis 115 115 . . . Note=Reduces NTP-binding and hydrolysis. Shows DNA damage sensitivity. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10913172;Dbxref=PMID:10913172 +P32641 UniProtKB Mutagenesis 115 115 . . . Note=No effect on NTP-binding and hydrolysis. Resistant to DNA damage. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10913172;Dbxref=PMID:10913172 +##sequence-region Q00578 1 843 +Q00578 UniProtKB Chain 1 843 . . . ID=PRO_0000101994;Note=DNA repair helicase RAD25 +Q00578 UniProtKB Domain 373 535 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q00578 UniProtKB Domain 589 743 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q00578 UniProtKB Nucleotide binding 386 393 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q00578 UniProtKB Motif 64 75 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q00578 UniProtKB Motif 487 491 . . . Note=DEVH box +Q00578 UniProtKB Compositional bias 302 309 . . . Note=Asp/Glu-rich (acidic) +Q00578 UniProtKB Modified residue 752 752 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q00578 UniProtKB Natural variant 427 427 . . . Note=In suppressor mutant. W->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1318786;Dbxref=PMID:1318786 +Q00578 UniProtKB Sequence conflict 9 9 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00578 UniProtKB Sequence conflict 48 48 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04231 1 177 +Q04231 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q04231 UniProtKB Chain 2 177 . . . ID=PRO_0000203263;Note=DNA repair protein RAD33 +Q04231 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q04231 UniProtKB Cross-link 19 19 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P14736 1 754 +P14736 UniProtKB Chain 1 754 . . . ID=PRO_0000218298;Note=DNA repair protein RAD4 +P14736 UniProtKB DNA binding 250 269 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14736 UniProtKB Sequence conflict 223 223 . . . Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14736 UniProtKB Sequence conflict 225 225 . . . Note=L->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14736 UniProtKB Sequence conflict 225 225 . . . Note=L->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14736 UniProtKB Turn 91 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M14 +P14736 UniProtKB Helix 124 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSH +P14736 UniProtKB Helix 134 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 165 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 172 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 177 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 193 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSH +P14736 UniProtKB Helix 230 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Turn 236 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 248 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 262 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 280 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 306 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 314 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Turn 322 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 326 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 337 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Turn 352 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 362 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 372 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 376 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 383 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 388 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 392 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 396 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 416 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 436 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSH +P14736 UniProtKB Helix 439 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 445 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 450 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 457 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 466 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 478 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 484 486 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 487 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 493 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Turn 498 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 501 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 510 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 529 532 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 534 536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 537 539 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 564 566 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 571 575 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 579 585 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 591 597 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Beta strand 601 603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YIR +P14736 UniProtKB Beta strand 607 615 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 616 618 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSH +P14736 UniProtKB Helix 619 627 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P14736 UniProtKB Helix 629 631 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +##sequence-region P06778 1 471 +P06778 UniProtKB Chain 1 471 . . . ID=PRO_0000173892;Note=DNA repair and recombination protein RAD52 +P06778 UniProtKB Alternative sequence 1 6 . . . ID=VSP_019613;Note=In isoform 3. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06778 UniProtKB Alternative sequence 1 4 . . . ID=VSP_019612;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P22216 1 821 +P22216 UniProtKB Chain 1 821 . . . ID=PRO_0000086595;Note=Serine/threonine-protein kinase RAD53 +P22216 UniProtKB Domain 66 116 . . . Note=FHA 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 +P22216 UniProtKB Domain 198 466 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P22216 UniProtKB Domain 601 664 . . . Note=FHA 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 +P22216 UniProtKB Nucleotide binding 204 212 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P22216 UniProtKB Active site 319 319 . . . Note=Proton acceptor +P22216 UniProtKB Binding site 227 227 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P22216 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P22216 UniProtKB Modified residue 175 175 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P22216 UniProtKB Modified residue 547 547 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P22216 UniProtKB Modified residue 560 560 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P22216 UniProtKB Modified residue 774 774 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P22216 UniProtKB Modified residue 793 793 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P22216 UniProtKB Sequence conflict 204 204 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22216 UniProtKB Helix 16 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G3G +P22216 UniProtKB Beta strand 31 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G +P22216 UniProtKB Beta strand 46 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G +P22216 UniProtKB Helix 52 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G +P22216 UniProtKB Beta strand 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G3G +P22216 UniProtKB Beta strand 64 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G +P22216 UniProtKB Beta strand 74 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G +P22216 UniProtKB Turn 82 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G3G +P22216 UniProtKB Beta strand 89 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G +P22216 UniProtKB Beta strand 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J4O +P22216 UniProtKB Beta strand 99 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G +P22216 UniProtKB Beta strand 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G3G +P22216 UniProtKB Beta strand 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G3G +P22216 UniProtKB Beta strand 120 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G3G +P22216 UniProtKB Beta strand 129 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G +P22216 UniProtKB Helix 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G +P22216 UniProtKB Beta strand 141 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G +P22216 UniProtKB Helix 149 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G6G +P22216 UniProtKB Beta strand 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K3N +P22216 UniProtKB Helix 193 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Beta strand 197 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Beta strand 211 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Turn 218 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Beta strand 223 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Helix 241 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Beta strand 259 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Beta strand 269 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Helix 281 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Helix 293 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Helix 322 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Beta strand 325 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Turn 330 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Beta strand 334 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Helix 359 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Helix 364 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Turn 384 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Helix 387 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Helix 413 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Helix 428 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Helix 437 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Helix 451 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Helix 457 461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Turn 464 467 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Helix 484 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PDP +P22216 UniProtKB Beta strand 551 557 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QU5 +P22216 UniProtKB Helix 563 565 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QU5 +P22216 UniProtKB Beta strand 572 575 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QU5 +P22216 UniProtKB Beta strand 578 582 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ +P22216 UniProtKB Beta strand 586 588 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QU5 +P22216 UniProtKB Beta strand 592 597 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ +P22216 UniProtKB Beta strand 601 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ +P22216 UniProtKB Beta strand 609 612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ +P22216 UniProtKB Beta strand 620 629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ +P22216 UniProtKB Beta strand 636 638 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FHQ +P22216 UniProtKB Beta strand 645 651 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ +P22216 UniProtKB Beta strand 653 655 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QU5 +P22216 UniProtKB Beta strand 657 659 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FHQ +P22216 UniProtKB Beta strand 662 664 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FHQ +P22216 UniProtKB Beta strand 666 671 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ +P22216 UniProtKB Beta strand 678 680 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ +P22216 UniProtKB Turn 684 687 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ +P22216 UniProtKB Beta strand 688 691 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QU5 +P22216 UniProtKB Beta strand 692 695 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ +P22216 UniProtKB Beta strand 703 707 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ +P22216 UniProtKB Beta strand 710 712 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ +P22216 UniProtKB Beta strand 716 718 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ +P22216 UniProtKB Helix 721 728 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DMZ +P22216 UniProtKB Beta strand 804 806 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YGV +P22216 UniProtKB Helix 811 813 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YGV +##sequence-region P38953 1 406 +P38953 UniProtKB Chain 1 406 . . . ID=PRO_0000122954;Note=DNA repair protein RAD55 +P38953 UniProtKB Nucleotide binding 43 50 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38953 UniProtKB Compositional bias 277 287 . . . Note=Ser-rich +P38953 UniProtKB Compositional bias 371 378 . . . Note=Ser-rich +P38953 UniProtKB Sequence conflict 110 110 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38953 UniProtKB Sequence conflict 197 197 . . . Note=F->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P06779 1 565 +P06779 UniProtKB Chain 1 565 . . . ID=PRO_0000097155;Note=DNA repair protein RAD7 +P06779 UniProtKB Region 1 200 . . . Note=Hydrophilic +P06779 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06779 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06779 UniProtKB Sequence conflict 278 279 . . . Note=LL->FV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06779 UniProtKB Sequence conflict 504 505 . . . Note=AC->RP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32864 1 603 +P32864 UniProtKB Chain 1 603 . . . ID=PRO_0000056693;Note=Rab proteins geranylgeranyltransferase component A +P32864 UniProtKB Modified residue 470 470 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950;Dbxref=PMID:15665377,PMID:17330950 +P32864 UniProtKB Sequence conflict 132 137 . . . Note=DLSPKI->MIFPRV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32864 UniProtKB Sequence conflict 300 300 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32864 UniProtKB Sequence conflict 300 300 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32864 UniProtKB Sequence conflict 300 300 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06891 1 181 +Q06891 UniProtKB Chain 1 181 . . . ID=PRO_0000283651;Note=Trans-acting factor D +Q06891 UniProtKB Natural variant 33 33 . . . Note=In strain: ATCC 7754. V->A +Q06891 UniProtKB Natural variant 36 36 . . . Note=In strain: ATCC 7754. K->R +Q06891 UniProtKB Natural variant 46 51 . . . Note=In strain: ATCC 7754. RIPRTI->KVPQTV +Q06891 UniProtKB Natural variant 67 68 . . . Note=In strain: ATCC 7754. RS->KF +Q06891 UniProtKB Natural variant 104 104 . . . Note=In strain: ATCC 7754. R->K +Q06891 UniProtKB Natural variant 116 116 . . . Note=In strain: ATCC 7754. L->S +Q06891 UniProtKB Natural variant 125 125 . . . Note=In strain: ATCC 7754. D->N +Q06891 UniProtKB Natural variant 136 136 . . . Note=In strain: ATCC 7754. I->T +Q06891 UniProtKB Natural variant 137 137 . . . Note=In strain: ATCC 4108. R->H +Q06891 UniProtKB Natural variant 144 144 . . . Note=In strain: ATCC 7754. N->D +Q06891 UniProtKB Natural variant 152 157 . . . Note=In strain: ATCC 7754. IYDRTC->NYGRTG +Q06891 UniProtKB Natural variant 162 162 . . . Note=In strain: ATCC 7754. N->D +Q06891 UniProtKB Natural variant 171 171 . . . Note=In strain: ATCC 7754. F->L +Q06891 UniProtKB Natural variant 180 180 . . . Note=In strain: ATCC 7754. P->S +##sequence-region P25635 1 923 +P25635 UniProtKB Chain 1 923 . . . ID=PRO_0000051179;Note=Periodic tryptophan protein 2 +P25635 UniProtKB Repeat 12 52 . . . Note=WD 1 +P25635 UniProtKB Repeat 53 93 . . . Note=WD 2 +P25635 UniProtKB Repeat 94 132 . . . Note=WD 3 +P25635 UniProtKB Repeat 144 183 . . . Note=WD 4 +P25635 UniProtKB Repeat 189 228 . . . Note=WD 5 +P25635 UniProtKB Repeat 258 297 . . . Note=WD 6 +P25635 UniProtKB Repeat 300 340 . . . Note=WD 7 +P25635 UniProtKB Repeat 343 382 . . . Note=WD 8 +P25635 UniProtKB Repeat 385 424 . . . Note=WD 9 +P25635 UniProtKB Repeat 428 470 . . . Note=WD 10 +P25635 UniProtKB Repeat 471 510 . . . Note=WD 11 +P25635 UniProtKB Repeat 513 552 . . . Note=WD 12 +P25635 UniProtKB Repeat 575 614 . . . Note=WD 13 +P25635 UniProtKB Repeat 676 714 . . . Note=WD 14 +P25635 UniProtKB Compositional bias 226 240 . . . Note=Asp/Glu-rich (acidic) +P25635 UniProtKB Compositional bias 862 923 . . . Note=Asp/Glu-rich (acidic) +P25635 UniProtKB Modified residue 225 225 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25635 UniProtKB Modified residue 232 232 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P25635 UniProtKB Modified residue 651 651 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P25635 UniProtKB Modified residue 664 664 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25635 UniProtKB Modified residue 912 912 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P25635 UniProtKB Modified residue 913 913 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P34230 1 853 +P34230 UniProtKB Chain 1 853 . . . ID=PRO_0000093315;Note=Peroxisomal long-chain fatty acid import protein 1 +P34230 UniProtKB Transmembrane 122 142 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P34230 UniProtKB Transmembrane 166 186 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P34230 UniProtKB Transmembrane 269 289 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P34230 UniProtKB Transmembrane 364 384 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P34230 UniProtKB Domain 127 417 . . . Note=ABC transmembrane type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P34230 UniProtKB Domain 472 747 . . . Note=ABC transporter;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P34230 UniProtKB Nucleotide binding 505 512 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P34230 UniProtKB Glycosylation 33 33 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34230 UniProtKB Glycosylation 39 39 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34230 UniProtKB Glycosylation 162 162 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34230 UniProtKB Glycosylation 230 230 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34230 UniProtKB Glycosylation 241 241 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34230 UniProtKB Glycosylation 267 267 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34230 UniProtKB Glycosylation 295 295 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34230 UniProtKB Glycosylation 560 560 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34230 UniProtKB Glycosylation 608 608 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34230 UniProtKB Glycosylation 620 620 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34230 UniProtKB Glycosylation 647 647 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34230 UniProtKB Glycosylation 836 836 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32327 1 1180 +P32327 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32327 UniProtKB Chain 2 1180 . . . ID=PRO_0000146825;Note=Pyruvate carboxylase 2 +P32327 UniProtKB Domain 19 471 . . . Note=Biotin carboxylation +P32327 UniProtKB Domain 141 338 . . . Note=ATP-grasp;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 +P32327 UniProtKB Domain 558 825 . . . Note=Pyruvate carboxyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01151 +P32327 UniProtKB Domain 1095 1170 . . . Note=Biotinyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066 +P32327 UniProtKB Region 566 570 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32327 UniProtKB Active site 313 313 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32327 UniProtKB Metal binding 567 567 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32327 UniProtKB Metal binding 735 735 . . . Note=Divalent metal cation%3B via carbamate group;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32327 UniProtKB Metal binding 765 765 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32327 UniProtKB Metal binding 767 767 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32327 UniProtKB Binding site 137 137 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32327 UniProtKB Binding site 221 221 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32327 UniProtKB Binding site 256 256 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32327 UniProtKB Binding site 639 639 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32327 UniProtKB Binding site 899 899 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32327 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32327 UniProtKB Modified residue 735 735 . . . Note=N6-carboxylysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32327 UniProtKB Modified residue 1136 1136 . . . Note=N6-biotinyllysine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250,ECO:0000255|PROSITE-ProRule:PRU01066 +P32327 UniProtKB Sequence conflict 15 15 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32327 UniProtKB Sequence conflict 132 132 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32327 UniProtKB Sequence conflict 238 238 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32327 UniProtKB Sequence conflict 268 268 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32327 UniProtKB Sequence conflict 546 546 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32327 UniProtKB Sequence conflict 642 642 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32327 UniProtKB Sequence conflict 771 773 . . . Note=GTA->STR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32327 UniProtKB Sequence conflict 831 831 . . . Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32327 UniProtKB Sequence conflict 839 839 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32327 UniProtKB Sequence conflict 1001 1001 . . . Note=Y->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32327 UniProtKB Sequence conflict 1155 1155 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32327 UniProtKB Sequence conflict 1178 1178 . . . Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32327 UniProtKB Sequence conflict 1180 1180 . . . Note=K->KVIFTR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P13298 1 226 +P13298 UniProtKB Chain 1 226 . . . ID=PRO_0000110804;Note=Orotate phosphoribosyltransferase 1 +P13298 UniProtKB Region 38 39 . . . Note=Orotate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13298 UniProtKB Region 76 77 . . . Note=5-phosphoribose 1-diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13298 UniProtKB Region 132 140 . . . Note=5-phosphoribose 1-diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13298 UniProtKB Binding site 30 30 . . . Note=5-phosphoribose 1-diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13298 UniProtKB Binding site 106 106 . . . Note=5-phosphoribose 1-diphosphate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13298 UniProtKB Binding site 107 107 . . . Note=5-phosphoribose 1-diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13298 UniProtKB Binding site 110 110 . . . Note=5-phosphoribose 1-diphosphate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13298 UniProtKB Binding site 112 112 . . . Note=5-phosphoribose 1-diphosphate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13298 UniProtKB Binding site 136 136 . . . Note=Orotate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13298 UniProtKB Binding site 164 164 . . . Note=Orotate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13298 UniProtKB Modified residue 213 213 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13298 UniProtKB Modified residue 225 225 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13298 UniProtKB Sequence conflict 150 150 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13298 UniProtKB Helix 7 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Beta strand 21 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Beta strand 30 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WN3 +P13298 UniProtKB Beta strand 34 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Helix 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Helix 47 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Beta strand 69 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Turn 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Helix 78 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Helix 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Beta strand 101 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Beta strand 118 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Beta strand 127 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Beta strand 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WN3 +P13298 UniProtKB Helix 139 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Beta strand 154 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Beta strand 166 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Helix 178 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Beta strand 190 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Helix 196 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Turn 204 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +P13298 UniProtKB Helix 209 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WML +##sequence-region P37299 1 77 +P37299 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1325905;Dbxref=PMID:1325905 +P37299 UniProtKB Chain 2 77 . . . ID=PRO_0000193563;Note=Cytochrome b-c1 complex subunit 10 +P37299 UniProtKB Transmembrane 25 45 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P07256 1 457 +P07256 UniProtKB Transit peptide 1 26 . . . Note=Mitochondrion +P07256 UniProtKB Chain 27 457 . . . ID=PRO_0000026788;Note=Cytochrome b-c1 complex subunit 1%2C mitochondrial +P07256 UniProtKB Beta strand 30 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Beta strand 47 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Turn 64 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 69 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 80 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Beta strand 92 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Beta strand 102 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EZV +P07256 UniProtKB Helix 113 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Turn 129 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 134 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 156 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Turn 169 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 173 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 182 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 190 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 203 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Beta strand 206 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 216 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Beta strand 247 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Beta strand 256 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 275 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Beta strand 287 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 295 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 302 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Turn 308 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Beta strand 313 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Beta strand 326 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 340 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 360 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 383 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 403 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Helix 415 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Turn 426 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Beta strand 432 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07256 UniProtKB Beta strand 440 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PD4 +P07256 UniProtKB Helix 445 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +##sequence-region P06777 1 1100 +P06777 UniProtKB Chain 1 1100 . . . ID=PRO_0000198857;Note=DNA repair protein RAD1 +P06777 UniProtKB Domain 821 901 . . . Note=ERCC4 +P06777 UniProtKB Compositional bias 1 110 . . . Note=Asp/Glu-rich (acidic) +P06777 UniProtKB Compositional bias 516 576 . . . Note=Arg/Lys-rich (basic) +P06777 UniProtKB Compositional bias 595 689 . . . Note=Asp/Glu-rich (acidic) +P06777 UniProtKB Compositional bias 1041 1100 . . . Note=Asp/Glu-rich (acidic) +P06777 UniProtKB Modified residue 613 613 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06777 UniProtKB Modified residue 1071 1071 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06777 UniProtKB Modified residue 1072 1072 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06777 UniProtKB Sequence conflict 223 223 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06777 UniProtKB Sequence conflict 883 883 . . . Note=C->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06777 UniProtKB Sequence conflict 886 886 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06777 UniProtKB Sequence conflict 912 912 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06777 UniProtKB Sequence conflict 924 924 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06777 UniProtKB Sequence conflict 1016 1016 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32628 1 398 +P32628 UniProtKB Chain 1 398 . . . ID=PRO_0000114902;Note=UV excision repair protein RAD23 +P32628 UniProtKB Domain 1 77 . . . Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 +P32628 UniProtKB Domain 146 186 . . . Note=UBA 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212 +P32628 UniProtKB Domain 355 395 . . . Note=UBA 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212 +P32628 UniProtKB Modified residue 94 94 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32628 UniProtKB Modified residue 121 121 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32628 UniProtKB Modified residue 139 139 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32628 UniProtKB Cross-link 49 49 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32628 UniProtKB Sequence conflict 277 277 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32628 UniProtKB Sequence conflict 277 277 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32628 UniProtKB Sequence conflict 277 277 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32628 UniProtKB Sequence conflict 277 277 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32628 UniProtKB Beta strand 4 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P32628 UniProtKB Beta strand 9 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NBW +P32628 UniProtKB Beta strand 13 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P32628 UniProtKB Helix 24 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P32628 UniProtKB Turn 34 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P32628 UniProtKB Helix 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P32628 UniProtKB Beta strand 43 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P32628 UniProtKB Turn 57 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P32628 UniProtKB Beta strand 67 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M62 +P32628 UniProtKB Helix 259 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P32628 UniProtKB Helix 273 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P32628 UniProtKB Helix 276 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P32628 UniProtKB Helix 290 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P32628 UniProtKB Helix 298 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P32628 UniProtKB Helix 355 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P32628 UniProtKB Turn 366 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P32628 UniProtKB Helix 371 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P32628 UniProtKB Turn 381 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +P32628 UniProtKB Helix 385 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QSF +##sequence-region P06839 1 778 +P06839 UniProtKB Chain 1 778 . . . ID=PRO_0000101983;Note=DNA repair helicase RAD3 +P06839 UniProtKB Domain 7 285 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P06839 UniProtKB Nucleotide binding 42 49 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P06839 UniProtKB Motif 235 238 . . . Note=DEAH box +P06839 UniProtKB Compositional bias 759 778 . . . Note=Asp/Glu-rich (acidic) +P06839 UniProtKB Metal binding 115 115 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06839 UniProtKB Metal binding 133 133 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06839 UniProtKB Metal binding 156 156 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06839 UniProtKB Metal binding 191 191 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06839 UniProtKB Mutagenesis 48 48 . . . Note=Abolishes ATPase and DNA helicase activities but not ATP-binding capacity. K->R%2CA;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16973432,ECO:0000269|PubMed:1719538,ECO:0000269|PubMed:2846277;Dbxref=PMID:16973432,PMID:1719538,PMID:2846277 +P06839 UniProtKB Mutagenesis 111 111 . . . Note=Confers an UV-sensitive phenotype. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16973432;Dbxref=PMID:16973432 +P06839 UniProtKB Mutagenesis 115 115 . . . Note=Confers an UV-sensitive phenotype. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16973432;Dbxref=PMID:16973432 +P06839 UniProtKB Sequence conflict 2 2 . . . Note=K->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12270 1 262 +Q12270 UniProtKB Chain 1 262 . . . ID=PRO_0000206193;Note=Rhomboid protein 2 +Q12270 UniProtKB Topological domain 1 16 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12270 UniProtKB Transmembrane 17 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12270 UniProtKB Topological domain 38 57 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12270 UniProtKB Transmembrane 58 78 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12270 UniProtKB Topological domain 79 89 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12270 UniProtKB Transmembrane 90 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12270 UniProtKB Topological domain 111 112 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12270 UniProtKB Transmembrane 113 133 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12270 UniProtKB Topological domain 134 151 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12270 UniProtKB Transmembrane 152 168 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12270 UniProtKB Topological domain 169 174 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12270 UniProtKB Transmembrane 175 191 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12270 UniProtKB Topological domain 192 262 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12270 UniProtKB Active site 124 124 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12270 UniProtKB Active site 179 179 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P50086 1 228 +P50086 UniProtKB Chain 1 228 . . . ID=PRO_0000067048;Note=Probable 26S proteasome regulatory subunit p28 +P50086 UniProtKB Repeat 1 30 . . . Note=ANK 1 +P50086 UniProtKB Repeat 35 64 . . . Note=ANK 2 +P50086 UniProtKB Repeat 71 100 . . . Note=ANK 3 +P50086 UniProtKB Repeat 106 135 . . . Note=ANK 4 +P50086 UniProtKB Repeat 139 168 . . . Note=ANK 5 +P50086 UniProtKB Repeat 173 203 . . . Note=ANK 6 +P50086 UniProtKB Helix 5 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P50086 UniProtKB Helix 15 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P50086 UniProtKB Helix 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P50086 UniProtKB Helix 39 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P50086 UniProtKB Helix 49 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P50086 UniProtKB Helix 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P50086 UniProtKB Helix 75 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P50086 UniProtKB Helix 85 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P50086 UniProtKB Beta strand 93 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P50086 UniProtKB Helix 110 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P50086 UniProtKB Helix 120 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P50086 UniProtKB Helix 143 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P50086 UniProtKB Helix 153 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P50086 UniProtKB Turn 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P50086 UniProtKB Helix 177 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P50086 UniProtKB Helix 187 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P50086 UniProtKB Helix 211 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P50086 UniProtKB Helix 220 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +##sequence-region P53037 1 1138 +P53037 UniProtKB Chain 1 1138 . . . ID=PRO_0000045200;Note=Phosphatidylserine decarboxylase proenzyme 2 +P53037 UniProtKB Chain 1 1042 . . . ID=PRO_0000045201;Note=Phosphatidylserine decarboxylase 2 beta chain;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03209 +P53037 UniProtKB Chain 1043 1138 . . . ID=PRO_0000045202;Note=Phosphatidylserine decarboxylase 2 alpha chain;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03209 +P53037 UniProtKB Domain 14 87 . . . Note=C2 1%3B degenerate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24366873;Dbxref=PMID:24366873 +P53037 UniProtKB Domain 500 583 . . . Note=C2 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03209 +P53037 UniProtKB Compositional bias 108 159 . . . Note=Ser-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00016 +P53037 UniProtKB Active site 899 899 . . . Note=Charge relay system%3B for autoendoproteolytic cleavage activity;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:B3L2V1,ECO:0000255|HAMAP-Rule:MF_03209 +P53037 UniProtKB Active site 956 956 . . . Note=Charge relay system%3B for autoendoproteolytic cleavage activity;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:B3L2V1,ECO:0000255|HAMAP-Rule:MF_03209 +P53037 UniProtKB Active site 1043 1043 . . . Note=Charge relay system%3B for autoendoproteolytic cleavage activity;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:B3L2V1,ECO:0000255|HAMAP-Rule:MF_03209 +P53037 UniProtKB Active site 1043 1043 . . . Note=Schiff-base intermediate with substrate%3B via pyruvic acid%3B for decarboxylase activity;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P0A8K1,ECO:0000255|HAMAP-Rule:MF_03209 +P53037 UniProtKB Site 1042 1043 . . . Note=Cleavage (non-hydrolytic)%3B by autocatalysis;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P0A8K1,ECO:0000255|HAMAP-Rule:MF_03209 +P53037 UniProtKB Modified residue 1043 1043 . . . Note=Pyruvic acid (Ser)%3B by autocatalysis;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P0A8K1,ECO:0000255|HAMAP-Rule:MF_03209 +P53037 UniProtKB Mutagenesis 1041 1043 . . . Note=No processing of the proenzyme%2C complete loss of activity. GGS->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20016005;Dbxref=PMID:20016005 +P53037 UniProtKB Sequence conflict 801 801 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53037 UniProtKB Sequence conflict 974 974 . . . Note=Y->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P31374 1 1356 +P31374 UniProtKB Chain 1 1356 . . . ID=PRO_0000086042;Note=Serine/threonine-protein kinase PSK1 +P31374 UniProtKB Domain 450 518 . . . Note=PAS 1 +P31374 UniProtKB Domain 738 807 . . . Note=PAS 2 +P31374 UniProtKB Domain 1096 1354 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P31374 UniProtKB Nucleotide binding 1102 1110 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P31374 UniProtKB Active site 1230 1230 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P31374 UniProtKB Binding site 1125 1125 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P31374 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P31374 UniProtKB Modified residue 192 192 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P31374 UniProtKB Modified residue 202 202 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P31374 UniProtKB Modified residue 255 255 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P31374 UniProtKB Modified residue 286 286 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P31374 UniProtKB Modified residue 327 327 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P31374 UniProtKB Modified residue 926 926 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P31374 UniProtKB Modified residue 1018 1018 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P31374 UniProtKB Modified residue 1023 1023 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P31374 UniProtKB Modified residue 1035 1035 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P31374 UniProtKB Modified residue 1055 1055 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P31374 UniProtKB Modified residue 1079 1079 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P31374 UniProtKB Sequence conflict 73 73 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31374 UniProtKB Sequence conflict 73 73 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31374 UniProtKB Sequence conflict 73 73 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31374 UniProtKB Sequence conflict 73 73 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02771 1 107 +##sequence-region P32606 1 800 +P32606 UniProtKB Chain 1 800 . . . ID=PRO_0000097082;Note=Putative mitochondrial translation system component PET127 +##sequence-region P32522 1 965 +P32522 UniProtKB Transmembrane 237 256 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32522 UniProtKB Repeat 310 344 . . . Note=PPR 1 +P32522 UniProtKB Repeat 345 379 . . . Note=PPR 2 +P32522 UniProtKB Repeat 380 414 . . . Note=PPR 3 +P32522 UniProtKB Repeat 415 450 . . . Note=PPR 4 +P32522 UniProtKB Repeat 451 486 . . . Note=PPR 5 +P32522 UniProtKB Repeat 487 523 . . . Note=PPR 6 +P32522 UniProtKB Repeat 524 558 . . . Note=PPR 7 +P32522 UniProtKB Repeat 559 595 . . . Note=PPR 8 +P32522 UniProtKB Repeat 596 630 . . . Note=PPR 9 +P32522 UniProtKB Repeat 680 714 . . . Note=PPR 10 +P32522 UniProtKB Repeat 723 763 . . . Note=PPR 11 +P32522 UniProtKB Repeat 774 808 . . . Note=PPR 12 +P32522 UniProtKB Repeat 809 844 . . . Note=PPR 13 +##sequence-region Q01329 1 785 +Q01329 UniProtKB Chain 1 785 . . . ID=PRO_0000097086;Note=Pre-tRNA-processing protein PTA1 +Q01329 UniProtKB Modified residue 500 500 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q04373 1 656 +Q04373 UniProtKB Chain 1 656 . . . ID=PRO_0000075926;Note=Pumilio homology domain family member 6 +Q04373 UniProtKB Domain 133 483 . . . Note=PUM-HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00318 +Q04373 UniProtKB Repeat 155 191 . . . Note=Pumilio 1 +Q04373 UniProtKB Repeat 192 227 . . . Note=Pumilio 2 +Q04373 UniProtKB Repeat 228 264 . . . Note=Pumilio 3 +Q04373 UniProtKB Repeat 340 376 . . . Note=Pumilio 4 +Q04373 UniProtKB Repeat 377 413 . . . Note=Pumilio 5 +Q04373 UniProtKB Repeat 415 450 . . . Note=Pumilio 6 +Q04373 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18791219;Dbxref=PMID:18791219 +Q04373 UniProtKB Modified residue 34 34 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18791219;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:18791219 +Q04373 UniProtKB Modified residue 34 34 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18791219;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:18791219 +Q04373 UniProtKB Modified residue 35 35 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18791219;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:18791219 +Q04373 UniProtKB Modified residue 35 35 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18791219;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:18791219 +Q04373 UniProtKB Mutagenesis 31 31 . . . Note=Increases translation repression of ASH1 mRNA. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18791219;Dbxref=PMID:18791219 +Q04373 UniProtKB Mutagenesis 34 34 . . . Note=Increases translation repression of ASH1 mRNA. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18791219;Dbxref=PMID:18791219 +Q04373 UniProtKB Mutagenesis 35 35 . . . Note=Increases translation repression of ASH1 mRNA. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18791219;Dbxref=PMID:18791219 +##sequence-region P80210 1 433 +P80210 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10417315,ECO:0000269|PubMed:8376380;Dbxref=PMID:10417315,PMID:8376380 +P80210 UniProtKB Chain 2 433 . . . ID=PRO_0000095138;Note=Adenylosuccinate synthetase +P80210 UniProtKB Nucleotide binding 11 17 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125 +P80210 UniProtKB Nucleotide binding 39 41 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125 +P80210 UniProtKB Nucleotide binding 337 339 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125 +P80210 UniProtKB Nucleotide binding 419 421 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125 +P80210 UniProtKB Region 12 15 . . . Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125 +P80210 UniProtKB Region 37 40 . . . Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125 +P80210 UniProtKB Region 305 311 . . . Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125 +P80210 UniProtKB Active site 12 12 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125 +P80210 UniProtKB Active site 40 40 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125 +P80210 UniProtKB Metal binding 12 12 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125 +P80210 UniProtKB Metal binding 39 39 . . . Note=Magnesium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125 +P80210 UniProtKB Binding site 134 134 . . . Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125 +P80210 UniProtKB Binding site 148 148 . . . Note=IMP%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125 +P80210 UniProtKB Binding site 230 230 . . . Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125 +P80210 UniProtKB Binding site 245 245 . . . Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125 +P80210 UniProtKB Binding site 309 309 . . . Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125 +P80210 UniProtKB Binding site 311 311 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03125 +P80210 UniProtKB Sequence conflict 237 237 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02256 1 364 +Q02256 UniProtKB Chain 1 364 . . . ID=PRO_0000094854;Note=Tyrosine-protein phosphatase YVH1 +Q02256 UniProtKB Domain 1 172 . . . Note=Tyrosine-protein phosphatase +Q02256 UniProtKB Active site 117 117 . . . Note=Phosphocysteine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02256 UniProtKB Modified residue 196 196 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q02256 UniProtKB Sequence conflict 71 71 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P21304 1 576 +P21304 UniProtKB Chain 1 576 . . . ID=PRO_0000051173;Note=Periodic tryptophan protein 1 +P21304 UniProtKB Repeat 207 252 . . . Note=WD 1 +P21304 UniProtKB Repeat 284 324 . . . Note=WD 2 +P21304 UniProtKB Repeat 329 369 . . . Note=WD 3 +P21304 UniProtKB Repeat 376 414 . . . Note=WD 4 +P21304 UniProtKB Repeat 420 461 . . . Note=WD 5 +P21304 UniProtKB Repeat 472 514 . . . Note=WD 6 +P21304 UniProtKB Modified residue 52 52 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +P21304 UniProtKB Modified residue 131 131 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P30620 1 661 +P30620 UniProtKB Chain 1 661 . . . ID=PRO_0000209130;Note=DNA cross-link repair protein PSO2/SNM1 +P30620 UniProtKB Zinc finger 145 169 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30620 UniProtKB Mutagenesis 252 252 . . . Note=Abrogates exonuclease activity. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12509272,ECO:0000269|PubMed:15590324;Dbxref=PMID:12509272,PMID:15590324 +P30620 UniProtKB Mutagenesis 256 256 . . . Note=In SNM1-2%3B increased sensitivity to DNA cross-linking agents at 36 degrees Celsius. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7526204;Dbxref=PMID:7526204 +##sequence-region P50896 1 841 +P50896 UniProtKB Chain 1 841 . . . ID=PRO_0000097068;Note=Protein PSP1 +P50896 UniProtKB Domain 653 765 . . . Note=PSP1 C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00744 +P50896 UniProtKB Compositional bias 98 101 . . . Note=Poly-Gln +P50896 UniProtKB Compositional bias 139 144 . . . Note=Poly-Asn +P50896 UniProtKB Compositional bias 314 320 . . . Note=Poly-Asn +P50896 UniProtKB Compositional bias 348 359 . . . Note=Poly-Gln +P50896 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P50896 UniProtKB Modified residue 34 34 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P50896 UniProtKB Modified residue 36 36 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P50896 UniProtKB Modified residue 237 237 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P50896 UniProtKB Modified residue 334 334 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P50896 UniProtKB Modified residue 520 520 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P50896 UniProtKB Sequence conflict 116 116 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P50896 UniProtKB Sequence conflict 122 133 . . . Note=QMSSSNSEPMSA->KCLRLIQSCVP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P50896 UniProtKB Sequence conflict 198 210 . . . Note=GSNFAAPSHSAGN->RAILLPHHTVLAT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P50896 UniProtKB Sequence conflict 732 732 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36082 1 127 +P36082 UniProtKB Chain 1 127 . . . ID=PRO_0000203169;Note=Putative platinum sensitivity protein 1 +##sequence-region Q12318 1 242 +Q12318 UniProtKB Chain 1 242 . . . ID=PRO_0000262753;Note=Platinum sensitivity protein 3 +Q12318 UniProtKB Helix 2 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EQ6 +Q12318 UniProtKB Helix 12 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Helix 27 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Beta strand 31 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Helix 35 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Beta strand 43 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Helix 55 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Beta strand 66 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Helix 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Beta strand 89 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Beta strand 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Helix 100 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Helix 114 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Beta strand 128 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Helix 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Helix 152 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Beta strand 174 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Helix 182 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Turn 189 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Helix 213 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +Q12318 UniProtKB Beta strand 220 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VU9 +##sequence-region P47065 1 347 +P47065 UniProtKB Chain 1 347 . . . ID=PRO_0000097083;Note=Protein PET130 +##sequence-region Q02772 1 108 +Q02772 UniProtKB Chain 1 108 . . . ID=PRO_0000022178;Note=Mitochondrial protein PET191 +Q02772 UniProtKB Domain 18 64 . . . Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q02772 UniProtKB Motif 21 32 . . . Note=Cx10C motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q02772 UniProtKB Motif 46 56 . . . Note=Cx9C motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q02772 UniProtKB Disulfide bond 21 56 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +Q02772 UniProtKB Disulfide bond 32 46 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +##sequence-region P07390 1 489 +P07390 UniProtKB Chain 1 489 . . . ID=PRO_0000097085;Note=COX3 mRNA-specific translational activator PET494 +P07390 UniProtKB Sequence conflict 68 68 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P34222 1 208 +P34222 UniProtKB Chain 1 208 . . . ID=PRO_0000120284;Note=Peptidyl-tRNA hydrolase 2 +P34222 UniProtKB Cross-link 152 152 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P04161 1 214 +P04161 UniProtKB Chain 1 214 . . . ID=PRO_0000074954;Note=Phosphoribosylglycinamide formyltransferase +P04161 UniProtKB Region 12 14 . . . Note=5'-phosphoribosylglycinamide binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04161 UniProtKB Region 105 108 . . . Note=10-formyltetrahydrofolate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04161 UniProtKB Active site 125 125 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04161 UniProtKB Binding site 123 123 . . . Note=10-formyltetrahydrofolate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04161 UniProtKB Binding site 167 167 . . . Note=10-formyltetrahydrofolate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04161 UniProtKB Binding site 197 197 . . . Note=5'-phosphoribosylglycinamide;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04161 UniProtKB Site 167 167 . . . Note=Raises pKa of active site His;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q12488 1 208 +Q12488 UniProtKB Chain 1 208 . . . ID=PRO_0000219040;Note=DNA replication complex GINS protein PSF1 +Q12488 UniProtKB Mutagenesis 84 84 . . . Note=In PSF1-1%3B temperature-sensitive mutant. Defective in DNA replication. Impaired chromatin binding of CDC45. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12730134;Dbxref=PMID:12730134 +##sequence-region P31115 1 442 +P31115 UniProtKB Chain 1 442 . . . ID=PRO_0000057519;Note=tRNA pseudouridine(38/39) synthase +P31115 UniProtKB Active site 151 151 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P31115 UniProtKB Binding site 222 222 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q08647 1 676 +Q08647 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q08647 UniProtKB Chain 2 676 . . . ID=PRO_0000152561;Note=Multisubstrate pseudouridine synthase 7 +Q08647 UniProtKB Domain 338 582 . . . Note=TRUD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00342 +Q08647 UniProtKB Active site 256 256 . . . Note=Nucleophile +Q08647 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q08647 UniProtKB Mutagenesis 256 256 . . . Note=Abolishes enzymatic activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14561887;Dbxref=PMID:14561887 +##sequence-region P39006 1 500 +P39006 UniProtKB Transit peptide 1 44 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208 +P39006 UniProtKB Chain 45 500 . . . ID=PRO_0000029843;Note=Phosphatidylserine decarboxylase proenzyme 1%2C mitochondrial +P39006 UniProtKB Chain 45 462 . . . ID=PRO_0000029844;Note=Phosphatidylserine decarboxylase 1 beta chain;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208 +P39006 UniProtKB Chain 463 500 . . . ID=PRO_0000029845;Note=Phosphatidylserine decarboxylase 1 alpha chain;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208 +P39006 UniProtKB Topological domain 45 79 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03208,ECO:0000305|PubMed:22984266;Dbxref=PMID:22984266 +P39006 UniProtKB Transmembrane 80 98 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208 +P39006 UniProtKB Topological domain 99 500 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03208,ECO:0000305|PubMed:22984266;Dbxref=PMID:22984266 +P39006 UniProtKB Active site 210 210 . . . Note=Charge relay system%3B for autoendoproteolytic cleavage activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208 +P39006 UniProtKB Active site 348 348 . . . Note=Charge relay system%3B for autoendoproteolytic cleavage activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208 +P39006 UniProtKB Active site 463 463 . . . Note=Charge relay system%3B for autoendoproteolytic cleavage activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208 +P39006 UniProtKB Active site 463 463 . . . Note=Schiff-base intermediate with substrate%3B via pyruvic acid%3B for decarboxylase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208 +P39006 UniProtKB Site 462 463 . . . Note=Cleavage (non-hydrolytic)%3B by autocatalysis;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208 +P39006 UniProtKB Modified residue 463 463 . . . Note=Pyruvic acid (Ser)%3B by autocatalysis;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208 +P39006 UniProtKB Mutagenesis 81 100 . . . Note=In PSD1deltaIM%3B Mislocalizes to the mitochondrial matrix. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22984266;Dbxref=PMID:22984266 +P39006 UniProtKB Mutagenesis 461 463 . . . Note=No processing of the proenzyme%2C complete loss of activity. LGS->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18644857;Dbxref=PMID:18644857 +P39006 UniProtKB Mutagenesis 461 461 . . . Note=No effect. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25829489;Dbxref=PMID:25829489 +P39006 UniProtKB Mutagenesis 462 462 . . . Note=Significantly impairs processing of the proenzyme%2C retains some activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25829489;Dbxref=PMID:25829489 +P39006 UniProtKB Mutagenesis 463 463 . . . Note=No processing of the proenzyme%2C complete loss of activity. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22984266,ECO:0000269|PubMed:25829489;Dbxref=PMID:22984266,PMID:25829489 +P39006 UniProtKB Mutagenesis 464 464 . . . Note=No effect. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25829489;Dbxref=PMID:25829489 +##sequence-region P25044 1 335 +P25044 UniProtKB Chain 1 335 . . . ID=PRO_0000094855;Note=Tyrosine-protein phosphatase 1 +P25044 UniProtKB Domain 15 328 . . . Note=Tyrosine-protein phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00160 +P25044 UniProtKB Active site 252 252 . . . Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00160,ECO:0000255|PROSITE-ProRule:PRU10044 +P25044 UniProtKB Modified residue 83 83 . . . Note=Phosphoserine%3B by CLK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10480872;Dbxref=PMID:10480872 +##sequence-region P40048 1 928 +P40048 UniProtKB Chain 1 928 . . . ID=PRO_0000094857;Note=Tyrosine-protein phosphatase 3 +P40048 UniProtKB Domain 111 232 . . . Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173 +P40048 UniProtKB Domain 502 878 . . . Note=Tyrosine-protein phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00160 +P40048 UniProtKB Compositional bias 308 311 . . . Note=Poly-Ser +P40048 UniProtKB Compositional bias 592 597 . . . Note=Poly-Thr +P40048 UniProtKB Compositional bias 702 715 . . . Note=Poly-Asn +P40048 UniProtKB Compositional bias 724 732 . . . Note=Poly-Asp +P40048 UniProtKB Active site 804 804 . . . Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00160,ECO:0000255|PROSITE-ProRule:PRU10044 +P40048 UniProtKB Modified residue 75 75 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950 +P40048 UniProtKB Modified residue 248 248 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40048 UniProtKB Modified residue 297 297 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40048 UniProtKB Modified residue 368 368 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40048 UniProtKB Sequence conflict 717 717 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40048 UniProtKB Sequence conflict 717 717 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40048 UniProtKB Sequence conflict 738 738 . . . Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40048 UniProtKB Sequence conflict 738 738 . . . Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40048 UniProtKB Sequence conflict 857 857 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40048 UniProtKB Sequence conflict 857 857 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40454 1 393 +P40454 UniProtKB Chain 1 393 . . . ID=PRO_0000202955;Note=Serine/threonine-protein phosphatase 2A activator 1 +P40454 UniProtKB Modified residue 341 341 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40454 UniProtKB Mutagenesis 205 205 . . . Note=Abolishes PPIase activity and fails to activate PP2A phosphatases. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16380387;Dbxref=PMID:16380387 +P40454 UniProtKB Turn 8 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 23 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 33 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 65 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 97 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 119 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 125 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Turn 139 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 146 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 170 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 200 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXP +P40454 UniProtKB Beta strand 205 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 210 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Beta strand 220 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 223 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Beta strand 226 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 230 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 236 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Turn 243 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 247 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 263 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 268 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 280 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Turn 295 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Helix 299 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +P40454 UniProtKB Beta strand 309 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXO +##sequence-region P32588 1 453 +P32588 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P32588 UniProtKB Chain 2 453 . . . ID=PRO_0000081745;Note=Nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1 +P32588 UniProtKB Domain 75 152 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P32588 UniProtKB Domain 162 240 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P32588 UniProtKB Domain 341 413 . . . Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P32588 UniProtKB Region 260 264 . . . Note=RNA-binding RGG-box;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32588 UniProtKB Compositional bias 8 16 . . . Note=Gln-rich +P32588 UniProtKB Compositional bias 243 288 . . . Note=Asn-rich +P32588 UniProtKB Compositional bias 442 453 . . . Note=Gln-rich +P32588 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P32588 UniProtKB Sequence conflict 268 268 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32588 UniProtKB Sequence conflict 268 268 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32588 UniProtKB Beta strand 76 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD3 +P32588 UniProtKB Helix 88 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD3 +P32588 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD3 +P32588 UniProtKB Beta strand 101 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD3 +P32588 UniProtKB Beta strand 115 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD3 +P32588 UniProtKB Helix 125 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD3 +P32588 UniProtKB Beta strand 146 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD3 +P32588 UniProtKB Beta strand 162 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD1 +P32588 UniProtKB Helix 175 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD1 +P32588 UniProtKB Beta strand 188 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD1 +P32588 UniProtKB Turn 197 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD1 +P32588 UniProtKB Beta strand 202 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD1 +P32588 UniProtKB Helix 213 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD1 +P32588 UniProtKB Beta strand 234 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MD1 +P32588 UniProtKB Beta strand 322 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LA4 +P32588 UniProtKB Helix 326 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LA4 +P32588 UniProtKB Beta strand 342 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LA4 +P32588 UniProtKB Helix 354 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LA4 +P32588 UniProtKB Beta strand 368 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LA4 +P32588 UniProtKB Turn 374 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LA4 +P32588 UniProtKB Beta strand 378 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LA4 +P32588 UniProtKB Helix 386 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LA4 +##sequence-region Q12221 1 1075 +Q12221 UniProtKB Chain 1 1075 . . . ID=PRO_0000262754;Note=mRNA-binding protein PUF2 +Q12221 UniProtKB Domain 316 402 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q12221 UniProtKB Domain 511 872 . . . Note=PUM-HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00318 +Q12221 UniProtKB Repeat 574 611 . . . Note=Pumilio 1 +Q12221 UniProtKB Repeat 612 647 . . . Note=Pumilio 2 +Q12221 UniProtKB Repeat 649 683 . . . Note=Pumilio 3 +Q12221 UniProtKB Repeat 684 719 . . . Note=Pumilio 4 +Q12221 UniProtKB Repeat 722 758 . . . Note=Pumilio 5 +Q12221 UniProtKB Repeat 760 800 . . . Note=Pumilio 6 +Q12221 UniProtKB Compositional bias 910 1063 . . . Note=Asn-rich +Q12221 UniProtKB Modified residue 72 72 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12221 UniProtKB Modified residue 198 198 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12221 UniProtKB Modified residue 872 872 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12221 UniProtKB Modified residue 876 876 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q07807 1 879 +Q07807 UniProtKB Chain 1 879 . . . ID=PRO_0000075924;Note=mRNA-binding protein PUF3 +Q07807 UniProtKB Domain 513 871 . . . Note=PUM-HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00318 +Q07807 UniProtKB Repeat 538 573 . . . Note=Pumilio 1 +Q07807 UniProtKB Repeat 574 609 . . . Note=Pumilio 2 +Q07807 UniProtKB Repeat 610 645 . . . Note=Pumilio 3 +Q07807 UniProtKB Repeat 646 681 . . . Note=Pumilio 4 +Q07807 UniProtKB Repeat 682 717 . . . Note=Pumilio 5 +Q07807 UniProtKB Repeat 718 759 . . . Note=Pumilio 6 +Q07807 UniProtKB Repeat 760 795 . . . Note=Pumilio 7 +Q07807 UniProtKB Repeat 807 844 . . . Note=Pumilio 8 +Q07807 UniProtKB Compositional bias 398 409 . . . Note=Poly-Gln +Q07807 UniProtKB Compositional bias 412 418 . . . Note=Poly-Gln +Q07807 UniProtKB Modified residue 83 83 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q07807 UniProtKB Modified residue 207 207 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q07807 UniProtKB Modified residue 210 210 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07807 UniProtKB Mutagenesis 553 553 . . . Note=Prevents binding to COX17 mRNA and its rapid decay and increases affinity to HO mRNA%2C a PUF5 target. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16244132;Dbxref=PMID:16244132 +Q07807 UniProtKB Helix 516 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 536 539 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 543 547 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 550 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 565 575 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 576 578 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 579 584 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Turn 586 588 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 589 598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 601 611 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 615 620 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 624 634 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 637 644 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 645 647 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 651 656 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 660 670 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 673 675 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Turn 677 679 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 680 683 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Turn 684 686 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 687 691 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 696 706 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 709 717 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Turn 718 721 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 723 728 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 732 740 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 748 762 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 765 769 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 774 784 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 787 794 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Turn 795 797 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 802 806 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 813 818 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 823 833 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 836 855 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +Q07807 UniProtKB Helix 865 874 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K49 +##sequence-region P21264 1 571 +P21264 UniProtKB Chain 1 571 . . . ID=PRO_0000075028;Note=Phosphoribosylaminoimidazole carboxylase +P21264 UniProtKB Domain 110 298 . . . Note=ATP-grasp;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 +P21264 UniProtKB Nucleotide binding 138 193 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 +P21264 UniProtKB Modified residue 37 37 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P21264 UniProtKB Sequence conflict 101 101 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21264 UniProtKB Sequence conflict 186 186 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21264 UniProtKB Sequence conflict 206 206 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21264 UniProtKB Sequence conflict 241 253 . . . Note=ENAIKSFPGCGIF->KMQSNFSRLWYI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21264 UniProtKB Sequence conflict 387 387 . . . Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21264 UniProtKB Sequence conflict 407 407 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21264 UniProtKB Sequence conflict 431 431 . . . Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21264 UniProtKB Sequence conflict 434 434 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21264 UniProtKB Sequence conflict 502 502 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P41909 1 870 +P41909 UniProtKB Chain 1 870 . . . ID=PRO_0000093314;Note=Peroxisomal long-chain fatty acid import protein 2 +P41909 UniProtKB Transmembrane 60 80 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P41909 UniProtKB Transmembrane 207 227 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P41909 UniProtKB Transmembrane 247 267 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P41909 UniProtKB Transmembrane 330 350 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P41909 UniProtKB Transmembrane 353 373 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P41909 UniProtKB Transmembrane 455 475 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P41909 UniProtKB Domain 210 501 . . . Note=ABC transmembrane type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P41909 UniProtKB Domain 608 866 . . . Note=ABC transporter;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P41909 UniProtKB Nucleotide binding 645 652 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P41909 UniProtKB Glycosylation 142 142 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41909 UniProtKB Glycosylation 281 281 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41909 UniProtKB Glycosylation 403 403 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36166 1 706 +P36166 UniProtKB Chain 1 706 . . . ID=PRO_0000075893;Note=Paxillin-like protein 1 +P36166 UniProtKB Domain 556 612 . . . Note=LIM zinc-binding 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125 +P36166 UniProtKB Domain 621 672 . . . Note=LIM zinc-binding 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125 +P36166 UniProtKB Modified residue 43 43 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36166 UniProtKB Modified residue 63 63 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P36166 UniProtKB Sequence conflict 688 688 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53335 1 271 +P53335 UniProtKB Chain 1 271 . . . ID=PRO_0000202871;Note=Protein PXR1 +P53335 UniProtKB Domain 25 72 . . . Note=G-patch;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00092 +P53335 UniProtKB Compositional bias 139 226 . . . Note=Lys-rich +P53335 UniProtKB Modified residue 230 230 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53335 UniProtKB Sequence conflict 148 148 . . . Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53335 UniProtKB Sequence conflict 151 151 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53335 UniProtKB Sequence conflict 165 167 . . . Note=DDK->ADQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53335 UniProtKB Sequence conflict 193 193 . . . Note=D->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P05737 1 244 +P05737 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:1544921,PMID:18782943 +P05737 UniProtKB Chain 2 244 . . . ID=PRO_0000104651;Note=60S ribosomal protein L7-A +P05737 UniProtKB Turn 23 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U51 +P05737 UniProtKB Helix 28 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Beta strand 82 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Beta strand 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Helix 97 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Beta strand 113 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Helix 121 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Turn 129 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Beta strand 134 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Helix 141 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Beta strand 156 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Beta strand 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P05737 UniProtKB Helix 166 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Helix 174 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Helix 181 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Helix 195 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Beta strand 215 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Beta strand 219 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Helix 223 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Beta strand 227 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Helix 233 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05737 UniProtKB Helix 236 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P17076 1 256 +P17076 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921 +P17076 UniProtKB Chain 2 256 . . . ID=PRO_0000136760;Note=60S ribosomal protein L8-A +P17076 UniProtKB Sequence conflict 113 113 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17076 UniProtKB Beta strand 35 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Helix 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Helix 54 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Beta strand 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Helix 73 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Turn 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Helix 84 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Helix 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Helix 102 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Beta strand 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U6F +P17076 UniProtKB Beta strand 133 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P17076 UniProtKB Helix 136 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Beta strand 149 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Helix 161 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Helix 166 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Beta strand 177 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Helix 183 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Turn 189 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Beta strand 196 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Helix 205 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Turn 222 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Helix 226 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P17076 UniProtKB Helix 240 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P10622 1 106 +P10622 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8476850;Dbxref=PMID:8476850 +P10622 UniProtKB Chain 2 106 . . . ID=PRO_0000157706;Note=60S acidic ribosomal protein P1-beta +P10622 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8476850;Dbxref=PMID:8476850 +P10622 UniProtKB Modified residue 96 96 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P53060 1 241 +P53060 UniProtKB Chain 1 241 . . . ID=PRO_0000202705;Note=Reduced meiotic recombination protein 1 +##sequence-region P36159 1 838 +P36159 UniProtKB Chain 1 838 . . . ID=PRO_0000155837;Note=Ribonuclease Z +P36159 UniProtKB Modified residue 824 824 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +##sequence-region P53118 1 685 +P53118 UniProtKB Chain 1 685 . . . ID=PRO_0000202735;Note=Putative lipase ROG1 +P53118 UniProtKB Active site 269 269 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10037 +P53118 UniProtKB Sequence conflict 514 514 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P51862 1 1356 +P51862 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P51862 UniProtKB Chain 2 1356 . . . ID=PRO_0000080969;Note=RHO1 GDP-GTP exchange protein 2 +P51862 UniProtKB Domain 659 846 . . . Note=DH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00062 +P51862 UniProtKB Domain 1034 1336 . . . Note=CNH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00795 +P51862 UniProtKB Compositional bias 252 265 . . . Note=Poly-Asn +P51862 UniProtKB Compositional bias 329 336 . . . Note=Poly-His +P51862 UniProtKB Compositional bias 632 635 . . . Note=Poly-Asp +P51862 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P51862 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P51862 UniProtKB Modified residue 193 193 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950 +P51862 UniProtKB Modified residue 223 223 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P51862 UniProtKB Modified residue 566 566 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P51862 UniProtKB Modified residue 628 628 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P32529 1 125 +P32529 UniProtKB Chain 1 125 . . . ID=PRO_0000121465;Note=DNA-directed RNA polymerase I subunit RPA12 +P32529 UniProtKB Zinc finger 10 33 . . . Note=C4-type +P32529 UniProtKB Zinc finger 82 122 . . . Note=TFIIS-type;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00472,ECO:0000269|PubMed:24153182,ECO:0000269|PubMed:24153184;Dbxref=PMID:24153182,PMID:24153184 +P32529 UniProtKB Region 1 69 . . . Note=Necessary and sufficient for recruitment into Pol I +P32529 UniProtKB Region 1 60 . . . Note=Interaction with RPA2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11918799;Dbxref=PMID:11918799 +P32529 UniProtKB Region 79 125 . . . Note=Required for RNA cleavage%2C but not essential for elongation activity +P32529 UniProtKB Mutagenesis 10 10 . . . Note=Severe growth defect. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11918799;Dbxref=PMID:11918799 +P32529 UniProtKB Mutagenesis 13 13 . . . Note=No effect. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11918799;Dbxref=PMID:11918799 +P32529 UniProtKB Mutagenesis 30 30 . . . Note=Limited growth defect. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11918799;Dbxref=PMID:11918799 +P32529 UniProtKB Mutagenesis 33 33 . . . Note=No effect. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11918799;Dbxref=PMID:11918799 +P32529 UniProtKB Beta strand 7 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P32529 UniProtKB Beta strand 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P32529 UniProtKB Helix 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P32529 UniProtKB Beta strand 24 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P32529 UniProtKB Turn 31 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P32529 UniProtKB Beta strand 36 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P32529 UniProtKB Beta strand 47 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P32529 UniProtKB Helix 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P32529 UniProtKB Helix 59 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P32529 UniProtKB Beta strand 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P32529 UniProtKB Beta strand 79 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P32529 UniProtKB Turn 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P32529 UniProtKB Beta strand 92 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P32529 UniProtKB Beta strand 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P32529 UniProtKB Beta strand 109 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P32529 UniProtKB Turn 115 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P32529 UniProtKB Beta strand 120 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +##sequence-region Q01080 1 415 +Q01080 UniProtKB Chain 1 415 . . . ID=PRO_0000073955;Note=DNA-directed RNA polymerase I subunit RPA49 +Q01080 UniProtKB Region 322 415 . . . Note=Interaction with DNA +Q01080 UniProtKB Modified residue 34 34 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q01080 UniProtKB Modified residue 151 151 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q01080 UniProtKB Mutagenesis 325 326 . . . Note=No effect on DNA binding. ED->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20797630;Dbxref=PMID:20797630 +Q01080 UniProtKB Mutagenesis 356 356 . . . Note=Loss of DNA binding%3B when associated with A-358. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20797630;Dbxref=PMID:20797630 +Q01080 UniProtKB Mutagenesis 358 358 . . . Note=Loss of DNA binding%3B when associated with A-356. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20797630;Dbxref=PMID:20797630 +Q01080 UniProtKB Mutagenesis 359 359 . . . Note=Loss of DNA binding. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20797630;Dbxref=PMID:20797630 +Q01080 UniProtKB Mutagenesis 365 365 . . . Note=Loss of DNA binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20797630;Dbxref=PMID:20797630 +Q01080 UniProtKB Mutagenesis 393 393 . . . Note=Loss of DNA binding. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20797630;Dbxref=PMID:20797630 +Q01080 UniProtKB Sequence conflict 66 66 . . . Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01080 UniProtKB Sequence conflict 157 157 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01080 UniProtKB Beta strand 11 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +Q01080 UniProtKB Beta strand 22 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +Q01080 UniProtKB Beta strand 37 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +Q01080 UniProtKB Beta strand 51 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +Q01080 UniProtKB Beta strand 58 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +Q01080 UniProtKB Helix 70 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +Q01080 UniProtKB Beta strand 74 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +Q01080 UniProtKB Turn 83 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +Q01080 UniProtKB Beta strand 87 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +Q01080 UniProtKB Beta strand 95 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +Q01080 UniProtKB Helix 103 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +Q01080 UniProtKB Helix 173 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Helix 198 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Helix 204 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Helix 210 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Helix 219 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Helix 227 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Helix 242 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Helix 253 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Helix 256 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Turn 274 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Helix 280 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Helix 292 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Beta strand 303 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Helix 309 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Beta strand 317 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Helix 322 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Turn 340 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Beta strand 343 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Helix 346 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Helix 357 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Beta strand 370 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Helix 376 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Helix 386 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +Q01080 UniProtKB Beta strand 392 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFI +##sequence-region P27999 1 122 +P27999 UniProtKB Chain 1 122 . . . ID=PRO_0000121474;Note=DNA-directed RNA polymerase II subunit RPB9 +P27999 UniProtKB Zinc finger 7 32 . . . Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27999 UniProtKB Zinc finger 71 111 . . . Note=TFIIS-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00472 +P27999 UniProtKB Metal binding 7 7 . . . Note=Zinc 1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:11313498,ECO:0000269|PubMed:11805306,ECO:0000269|PubMed:15537538,ECO:0000305|PubMed:11313499;Dbxref=PMID:11313498,PMID:11805306,PMID:15537538,PMID:11313499 +P27999 UniProtKB Metal binding 10 10 . . . Note=Zinc 1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:11313498,ECO:0000269|PubMed:11805306,ECO:0000269|PubMed:15537538,ECO:0000305|PubMed:11313499;Dbxref=PMID:11313498,PMID:11805306,PMID:15537538,PMID:11313499 +P27999 UniProtKB Metal binding 29 29 . . . Note=Zinc 1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:11313498,ECO:0000269|PubMed:11805306,ECO:0000269|PubMed:15537538,ECO:0000305|PubMed:11313499;Dbxref=PMID:11313498,PMID:11805306,PMID:15537538,PMID:11313499 +P27999 UniProtKB Metal binding 32 32 . . . Note=Zinc 1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:11313498,ECO:0000269|PubMed:11805306,ECO:0000269|PubMed:15537538,ECO:0000305|PubMed:11313499;Dbxref=PMID:11313498,PMID:11805306,PMID:15537538,PMID:11313499 +P27999 UniProtKB Metal binding 75 75 . . . Note=Zinc 2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:11313498,ECO:0000269|PubMed:11805306,ECO:0000269|PubMed:15537538,ECO:0000305|PubMed:11313499;Dbxref=PMID:11313498,PMID:11805306,PMID:15537538,PMID:11313499 +P27999 UniProtKB Metal binding 78 78 . . . Note=Zinc 2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:11313498,ECO:0000269|PubMed:11805306,ECO:0000269|PubMed:15537538,ECO:0000305|PubMed:11313499;Dbxref=PMID:11313498,PMID:11805306,PMID:15537538,PMID:11313499 +P27999 UniProtKB Metal binding 103 103 . . . Note=Zinc 2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:11313498,ECO:0000269|PubMed:11805306,ECO:0000269|PubMed:15537538,ECO:0000305|PubMed:11313499;Dbxref=PMID:11313498,PMID:11805306,PMID:15537538,PMID:11313499 +P27999 UniProtKB Metal binding 106 106 . . . Note=Zinc 2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:11313498,ECO:0000269|PubMed:11805306,ECO:0000269|PubMed:15537538,ECO:0000305|PubMed:11313499;Dbxref=PMID:11313498,PMID:11805306,PMID:15537538,PMID:11313499 +P27999 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P27999 UniProtKB Beta strand 8 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P27999 UniProtKB Beta strand 15 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P27999 UniProtKB Turn 20 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P27999 UniProtKB Beta strand 24 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P27999 UniProtKB Beta strand 30 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P27999 UniProtKB Beta strand 35 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P27999 UniProtKB Beta strand 41 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P27999 UniProtKB Turn 52 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50 +P27999 UniProtKB Helix 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P27999 UniProtKB Beta strand 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1N +P27999 UniProtKB Turn 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P27999 UniProtKB Beta strand 83 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P27999 UniProtKB Beta strand 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S16 +P27999 UniProtKB Beta strand 99 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P27999 UniProtKB Turn 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P27999 UniProtKB Beta strand 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P27999 UniProtKB Beta strand 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NVQ +##sequence-region P47076 1 161 +P47076 UniProtKB Chain 1 161 . . . ID=PRO_0000203077;Note=DNA-directed RNA polymerase III subunit RPC9 +P47076 UniProtKB Sequence conflict 159 159 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47076 UniProtKB Sequence conflict 159 159 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47076 UniProtKB Beta strand 2 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P47076 UniProtKB Helix 13 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P47076 UniProtKB Helix 31 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P47076 UniProtKB Helix 53 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P47076 UniProtKB Helix 100 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P47076 UniProtKB Helix 117 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P47076 UniProtKB Helix 131 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P47076 UniProtKB Beta strand 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P47076 UniProtKB Turn 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P47076 UniProtKB Helix 147 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +##sequence-region P05738 1 191 +P05738 UniProtKB Chain 1 191 . . . ID=PRO_0000131111;Note=60S ribosomal protein L9-A +P05738 UniProtKB Beta strand 3 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Beta strand 17 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Beta strand 24 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Beta strand 32 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Turn 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P05738 UniProtKB Beta strand 44 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Beta strand 52 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Helix 62 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Beta strand 86 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Beta strand 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Beta strand 100 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Beta strand 106 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Beta strand 111 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Helix 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Beta strand 124 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Beta strand 132 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Beta strand 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Beta strand 143 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Helix 151 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Beta strand 168 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M +P05738 UniProtKB Turn 172 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05738 UniProtKB Beta strand 178 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region Q02204 1 264 +Q02204 UniProtKB Transit peptide 1 75 . . . Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2060626,ECO:0000269|PubMed:7954901;Dbxref=PMID:2060626,PMID:7954901 +Q02204 UniProtKB Chain 76 264 . . . ID=PRO_0000030571;Note=54S ribosomal protein L13%2C mitochondrial +Q02204 UniProtKB Sequence conflict 108 108 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P22354 1 195 +P22354 UniProtKB Transit peptide 1 18 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2183197;Dbxref=PMID:2183197 +P22354 UniProtKB Chain 19 195 . . . ID=PRO_0000030573;Note=54S ribosomal protein L20%2C mitochondrial +P22354 UniProtKB Compositional bias 113 129 . . . Note=Arg/Lys-rich (basic) +P22354 UniProtKB Sequence conflict 187 187 . . . Note=R->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12508 1 421 +Q12508 UniProtKB Chain 1 421 . . . ID=PRO_0000097361;Note=Sporulation protein RMD5 +Q12508 UniProtKB Domain 176 236 . . . Note=CTLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00058 +##sequence-region P40993 1 198 +P40993 UniProtKB Chain 1 198 . . . ID=PRO_0000097366;Note=Ribonuclease MRP protein subunit SNM1 +P40993 UniProtKB Compositional bias 136 198 . . . Note=Lys/Ser-rich +##sequence-region Q02933 1 434 +Q02933 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02933 UniProtKB Chain 19 434 . . . ID=PRO_0000042717;Note=Ribonuclease T2-like +Q02933 UniProtKB Active site 87 87 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02933 UniProtKB Active site 156 156 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02933 UniProtKB Active site 160 160 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02933 UniProtKB Glycosylation 37 37 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02933 UniProtKB Glycosylation 70 70 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02933 UniProtKB Glycosylation 103 103 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02933 UniProtKB Glycosylation 123 123 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02933 UniProtKB Disulfide bond 27 46 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02933 UniProtKB Disulfide bond 35 94 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02933 UniProtKB Disulfide bond 45 171 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02933 UniProtKB Disulfide bond 102 163 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02933 UniProtKB Disulfide bond 241 277 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02933 UniProtKB Mutagenesis 87 87 . . . Note=Impairs cytosolic tRNA-cleaving activity%3B when associated with F-160. H->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19332891;Dbxref=PMID:19332891 +Q02933 UniProtKB Mutagenesis 160 160 . . . Note=Impairs cytosolic tRNA-cleaving activity%3B when associated with F-87. H->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19332891;Dbxref=PMID:19332891 +##sequence-region P25042 1 368 +P25042 UniProtKB Chain 1 368 . . . ID=PRO_0000048574;Note=Repressor ROX1 +P25042 UniProtKB DNA binding 10 83 . . . Note=HMG box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267 +P25042 UniProtKB Compositional bias 102 123 . . . Note=Gln-rich +##sequence-region P10964 1 1664 +P10964 UniProtKB Chain 1 1664 . . . ID=PRO_0000073930;Note=DNA-directed RNA polymerase I subunit RPA190 +P10964 UniProtKB Region 992 1004 . . . Note=Bridging helix;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P10964 UniProtKB Metal binding 62 62 . . . Note=Zinc 1;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4C2M,ECO:0000269|PubMed:24153182;Dbxref=PMID:24153182 +P10964 UniProtKB Metal binding 65 65 . . . Note=Zinc 1;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4C2M,ECO:0000269|PubMed:24153182;Dbxref=PMID:24153182 +P10964 UniProtKB Metal binding 72 72 . . . Note=Zinc 1;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4C2M,ECO:0000269|PubMed:24153182;Dbxref=PMID:24153182 +P10964 UniProtKB Metal binding 75 75 . . . Note=Zinc 1%3B via tele nitrogen;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4C2M,ECO:0000269|PubMed:24153182;Dbxref=PMID:24153182 +P10964 UniProtKB Metal binding 102 102 . . . Note=Zinc 2;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4C2M,ECO:0000269|PubMed:24153182;Dbxref=PMID:24153182 +P10964 UniProtKB Metal binding 105 105 . . . Note=Zinc 2;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4C2M,ECO:0000269|PubMed:24153182;Dbxref=PMID:24153182 +P10964 UniProtKB Metal binding 233 233 . . . Note=Zinc 2;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4C2M,ECO:0000269|PubMed:24153182;Dbxref=PMID:24153182 +P10964 UniProtKB Metal binding 236 236 . . . Note=Zinc 2;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4C2M,ECO:0000269|PubMed:24153182;Dbxref=PMID:24153182 +P10964 UniProtKB Metal binding 627 627 . . . Note=Magnesium%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04050 +P10964 UniProtKB Metal binding 629 629 . . . Note=Magnesium%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04050 +P10964 UniProtKB Metal binding 631 631 . . . Note=Magnesium%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04050 +P10964 UniProtKB Modified residue 889 889 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P10964 UniProtKB Modified residue 1636 1636 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P10964 UniProtKB Sequence conflict 158 158 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10964 UniProtKB Beta strand 10 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 21 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Turn 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Turn 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 77 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 91 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Turn 103 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 107 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 112 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 130 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 175 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Turn 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P10964 UniProtKB Helix 210 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Turn 234 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 242 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 247 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 251 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 258 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Turn 267 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 317 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 332 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 352 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 356 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 365 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 371 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 376 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 381 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Turn 408 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 415 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 440 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 456 461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 462 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P10964 UniProtKB Helix 466 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 472 486 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 488 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P10964 UniProtKB Beta strand 494 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 499 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 506 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Turn 513 515 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 516 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Turn 526 528 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 529 531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 533 537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 543 545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 551 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Turn 559 562 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 568 570 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 576 580 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 586 590 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 597 599 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 600 607 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 613 616 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 618 620 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 621 624 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 628 630 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 632 636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 641 649 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 653 656 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Turn 660 662 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 672 680 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 686 688 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 689 700 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 703 705 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 708 711 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P10964 UniProtKB Beta strand 718 723 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 725 727 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 728 739 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 742 744 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P10964 UniProtKB Beta strand 749 752 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 757 759 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 768 772 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 775 778 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 783 786 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 793 824 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 830 833 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 837 847 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 848 850 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 853 861 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 873 884 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 886 911 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Turn 912 915 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 916 918 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Turn 920 922 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 924 930 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 937 944 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 976 979 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Turn 986 988 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 992 1011 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1017 1027 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 1036 1039 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P10964 UniProtKB Beta strand 1045 1049 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1050 1052 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P10964 UniProtKB Helix 1057 1059 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1066 1070 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1073 1080 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1082 1088 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 1089 1092 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1093 1107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 1109 1111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P10964 UniProtKB Helix 1113 1115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1123 1126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Turn 1129 1131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1138 1150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1152 1155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 1157 1160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1163 1175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1185 1194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1196 1200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1218 1226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 1237 1242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 1244 1246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P10964 UniProtKB Helix 1248 1258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1263 1266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 1267 1275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 1288 1296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1299 1306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1310 1318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1320 1335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 1344 1346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P10964 UniProtKB Helix 1364 1366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1369 1378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 1382 1384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1389 1394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1442 1452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 1454 1462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Turn 1464 1466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 1469 1476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1485 1493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 1497 1499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 1504 1508 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P10964 UniProtKB Beta strand 1518 1523 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1526 1529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1530 1532 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Turn 1533 1535 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1538 1540 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 1542 1544 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1546 1553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1555 1572 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1579 1589 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Turn 1590 1592 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1600 1603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1609 1613 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1618 1627 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1637 1643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Helix 1650 1652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P10964 UniProtKB Beta strand 1653 1661 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +##sequence-region P40422 1 70 +P40422 UniProtKB Chain 1 70 . . . ID=PRO_0000159753;Note=DNA-directed RNA polymerases I%2C II%2C and III subunit RPABC4 +P40422 UniProtKB Zinc finger 31 51 . . . Note=C4-type +P40422 UniProtKB Metal binding 31 31 . . . Note=Zinc +P40422 UniProtKB Metal binding 34 34 . . . Note=Zinc +P40422 UniProtKB Metal binding 48 48 . . . Note=Zinc +P40422 UniProtKB Metal binding 51 51 . . . Note=Zinc +P40422 UniProtKB Beta strand 28 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ +P40422 UniProtKB Beta strand 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P40422 UniProtKB Beta strand 36 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1Q +P40422 UniProtKB Beta strand 41 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ +P40422 UniProtKB Beta strand 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1Q +P40422 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P40422 UniProtKB Beta strand 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ +P40422 UniProtKB Beta strand 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +##sequence-region P07703 1 335 +P07703 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P07703 UniProtKB Chain 2 335 . . . ID=PRO_0000132742;Note=DNA-directed RNA polymerases I and III subunit RPAC1 +P07703 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P07703 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07703 UniProtKB Helix 33 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Beta strand 41 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Beta strand 49 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Helix 61 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Beta strand 77 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Beta strand 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Helix 94 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Helix 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Beta strand 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P07703 UniProtKB Helix 122 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Turn 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Beta strand 132 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Helix 153 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Beta strand 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P07703 UniProtKB Beta strand 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Helix 164 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Beta strand 168 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Helix 175 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Turn 179 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Beta strand 185 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Beta strand 192 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Beta strand 201 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Turn 213 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Helix 217 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Beta strand 222 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Helix 242 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Turn 253 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Beta strand 256 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Turn 260 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Beta strand 264 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Helix 270 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Helix 278 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Helix 283 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Beta strand 289 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Beta strand 306 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P07703 UniProtKB Helix 310 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +##sequence-region P38902 1 120 +P38902 UniProtKB Chain 1 120 . . . ID=PRO_0000149315;Note=DNA-directed RNA polymerase II subunit RPB11 +P38902 UniProtKB Mutagenesis 108 108 . . . Note=Transcript termination readthrough. E->G%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16537912;Dbxref=PMID:16537912 +P38902 UniProtKB Mutagenesis 108 108 . . . Note=Transcript termination readthrough. Lethal. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16537912;Dbxref=PMID:16537912 +P38902 UniProtKB Mutagenesis 111 111 . . . Note=Transcript termination readthrough. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16537912;Dbxref=PMID:16537912 +P38902 UniProtKB Mutagenesis 114 114 . . . Note=Transcript termination readthrough. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16537912;Dbxref=PMID:16537912 +P38902 UniProtKB Helix 7 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P38902 UniProtKB Beta strand 18 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S2H +P38902 UniProtKB Beta strand 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P38902 UniProtKB Beta strand 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P38902 UniProtKB Beta strand 30 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P38902 UniProtKB Helix 40 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P38902 UniProtKB Beta strand 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VUM +P38902 UniProtKB Beta strand 56 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P38902 UniProtKB Beta strand 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ +P38902 UniProtKB Beta strand 70 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P38902 UniProtKB Helix 83 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P38902 UniProtKB Turn 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +##sequence-region P16370 1 318 +P16370 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P16370 UniProtKB Chain 2 318 . . . ID=PRO_0000132748;Note=DNA-directed RNA polymerase II subunit RPB3 +P16370 UniProtKB Metal binding 86 86 . . . Note=Zinc +P16370 UniProtKB Metal binding 88 88 . . . Note=Zinc +P16370 UniProtKB Metal binding 92 92 . . . Note=Zinc +P16370 UniProtKB Metal binding 95 95 . . . Note=Zinc +P16370 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P16370 UniProtKB Natural variant 30 30 . . . Note=In mutant RPB3-1. A->D +P16370 UniProtKB Mutagenesis 9 9 . . . Note=Transcript termination readthrough. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16537912;Dbxref=PMID:16537912 +P16370 UniProtKB Sequence conflict 175 175 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16370 UniProtKB Beta strand 5 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Beta strand 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ +P16370 UniProtKB Beta strand 15 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Beta strand 21 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Helix 27 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Beta strand 43 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Beta strand 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Helix 60 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Beta strand 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Helix 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Turn 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Beta strand 86 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Turn 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Beta strand 96 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Beta strand 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Beta strand 111 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Helix 115 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Beta strand 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Beta strand 128 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Beta strand 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14 +P16370 UniProtKB Beta strand 142 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Beta strand 152 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Turn 164 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Helix 168 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Beta strand 173 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Helix 184 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I3Q +P16370 UniProtKB Helix 197 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Helix 205 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Beta strand 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M3Y +P16370 UniProtKB Beta strand 215 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Beta strand 228 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Beta strand 236 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P16370 UniProtKB Helix 240 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +##sequence-region P34087 1 171 +P34087 UniProtKB Chain 1 171 . . . ID=PRO_0000073993;Note=DNA-directed RNA polymerase II subunit RPB7 +P34087 UniProtKB Mutagenesis 108 113 . . . Note=Lowers nucleic-acid binding of RPB4-RPB7 by 10-fold%3B no effect on association with Pol II core complex%3B abolishes transcriptional activity of Pol II. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11087726;Dbxref=PMID:11087726 +P34087 UniProtKB Mutagenesis 151 158 . . . Note=No effect on nucleic-acid binding of RPB4-RPB7 and on association with Pol II core complex%3B abolishes transcriptional activity of Pol II. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11087726;Dbxref=PMID:11087726 +P34087 UniProtKB Beta strand 2 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P34087 UniProtKB Helix 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P34087 UniProtKB Beta strand 19 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HOU +P34087 UniProtKB Helix 22 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P34087 UniProtKB Beta strand 37 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P34087 UniProtKB Turn 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P34087 UniProtKB Beta strand 43 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P34087 UniProtKB Helix 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P34087 UniProtKB Beta strand 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P34087 UniProtKB Beta strand 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P34087 UniProtKB Beta strand 71 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P34087 UniProtKB Beta strand 86 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P34087 UniProtKB Beta strand 98 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P34087 UniProtKB Beta strand 106 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P34087 UniProtKB Helix 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P34087 UniProtKB Beta strand 117 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HOY +P34087 UniProtKB Beta strand 125 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P34087 UniProtKB Beta strand 129 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P34087 UniProtKB Beta strand 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HOU +P34087 UniProtKB Beta strand 142 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P34087 UniProtKB Beta strand 156 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P34087 UniProtKB Beta strand 165 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VUM +##sequence-region Q12189 1 258 +Q12189 UniProtKB Chain 1 258 . . . ID=PRO_0000158524;Note=Ribose-5-phosphate isomerase +Q12189 UniProtKB Helix 20 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Turn 36 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Beta strand 41 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Helix 51 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Turn 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Helix 67 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Beta strand 74 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Helix 80 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Turn 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Beta strand 101 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Beta strand 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Helix 126 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Beta strand 136 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Helix 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Beta strand 150 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Beta strand 161 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Helix 167 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Helix 170 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Beta strand 184 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Turn 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Beta strand 195 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Beta strand 206 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Beta strand 213 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Helix 218 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Beta strand 231 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Beta strand 242 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +Q12189 UniProtKB Beta strand 253 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XTZ +##sequence-region P32496 1 274 +P32496 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901 +P32496 UniProtKB Chain 2 274 . . . ID=PRO_0000173851;Note=26S proteasome regulatory subunit RPN12 +P32496 UniProtKB Helix 8 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P32496 UniProtKB Helix 20 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P32496 UniProtKB Helix 52 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P32496 UniProtKB Helix 75 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P32496 UniProtKB Helix 101 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P32496 UniProtKB Helix 119 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P32496 UniProtKB Turn 138 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P32496 UniProtKB Helix 143 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P32496 UniProtKB Helix 157 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P32496 UniProtKB Helix 174 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P32496 UniProtKB Beta strand 198 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P32496 UniProtKB Helix 202 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P32496 UniProtKB Helix 215 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P32496 UniProtKB Beta strand 232 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P32496 UniProtKB Helix 259 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +##sequence-region Q12250 1 445 +Q12250 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901 +Q12250 UniProtKB Chain 2 445 . . . ID=PRO_0000173865;Note=26S proteasome regulatory subunit RPN5 +Q12250 UniProtKB Domain 231 404 . . . Note=PCI +Q12250 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901 +Q12250 UniProtKB Helix 32 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 37 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 42 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 49 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Turn 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 72 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 94 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 111 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 135 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 153 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Turn 161 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 165 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Turn 168 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 173 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 194 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 205 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 211 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 235 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 248 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 254 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 275 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 288 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 295 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 311 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Turn 326 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Beta strand 331 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 337 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Beta strand 357 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 362 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 373 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Beta strand 392 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Turn 395 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Beta strand 399 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12250 UniProtKB Helix 408 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +##sequence-region Q06103 1 429 +Q06103 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901 +Q06103 UniProtKB Chain 2 429 . . . ID=PRO_0000173845;Note=26S proteasome regulatory subunit RPN7 +Q06103 UniProtKB Repeat 131 164 . . . Note=TPR +Q06103 UniProtKB Domain 221 392 . . . Note=PCI +Q06103 UniProtKB Modified residue 8 8 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06103 UniProtKB Modified residue 77 77 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06103 UniProtKB Sequence conflict 8 8 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06103 UniProtKB Helix 25 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Beta strand 36 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 40 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Turn 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 60 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 96 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 127 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 147 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 164 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 169 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 184 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 204 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 224 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Turn 240 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 246 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 263 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 276 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 280 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Beta strand 283 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 286 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 301 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Turn 315 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Turn 320 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 323 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 326 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Beta strand 345 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 350 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 361 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 372 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Beta strand 379 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Turn 383 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Beta strand 387 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q06103 UniProtKB Helix 396 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +##sequence-region Q04062 1 393 +Q04062 UniProtKB Chain 1 393 . . . ID=PRO_0000173870;Note=26S proteasome regulatory subunit RPN9 +Q04062 UniProtKB Domain 282 352 . . . Note=PCI +Q04062 UniProtKB Helix 7 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 20 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 24 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 38 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 58 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 65 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 75 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 92 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Turn 115 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 122 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 143 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 165 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 185 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 207 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 231 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 239 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 249 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 263 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 278 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 284 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Beta strand 306 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MR3 +Q04062 UniProtKB Helix 310 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Turn 321 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Helix 324 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Beta strand 336 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Beta strand 340 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MR3 +Q04062 UniProtKB Turn 343 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Beta strand 347 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MR3 +Q04062 UniProtKB Helix 360 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q04062 UniProtKB Turn 385 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +##sequence-region P38061 1 130 +P38061 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P38061 UniProtKB Chain 2 130 . . . ID=PRO_0000131145;Note=60S ribosomal protein L32 +P38061 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38061 UniProtKB Turn 20 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P38061 UniProtKB Beta strand 37 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U55 +P38061 UniProtKB Turn 41 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P38061 UniProtKB Helix 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P38061 UniProtKB Turn 61 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P38061 UniProtKB Beta strand 68 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U53 +P38061 UniProtKB Beta strand 72 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P38061 UniProtKB Helix 79 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P38061 UniProtKB Helix 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P38061 UniProtKB Turn 89 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P38061 UniProtKB Beta strand 92 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P38061 UniProtKB Helix 102 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P38061 UniProtKB Beta strand 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P38061 UniProtKB Turn 122 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P51998 1 286 +P51998 UniProtKB Transit peptide 1 26 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626 +P51998 UniProtKB Chain 27 286 . . . ID=PRO_0000030541;Note=54S ribosomal protein YmL6%2C mitochondrial +P51998 UniProtKB Sequence conflict 30 30 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P51998 UniProtKB Sequence conflict 35 35 . . . Note=A->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P51998 UniProtKB Sequence conflict 53 53 . . . Note=E->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P51998 UniProtKB Sequence conflict 121 121 . . . Note=S->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P51998 UniProtKB Sequence conflict 156 156 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P51998 UniProtKB Sequence conflict 249 249 . . . Note=E->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P05319 1 106 +P05319 UniProtKB Chain 1 106 . . . ID=PRO_0000157681;Note=60S acidic ribosomal protein P2-alpha +P05319 UniProtKB Modified residue 16 16 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P05319 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P05319 UniProtKB Modified residue 43 43 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P05319 UniProtKB Modified residue 49 49 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P05319 UniProtKB Modified residue 96 96 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P05319 UniProtKB Cross-link 2 2 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P05319 UniProtKB Cross-link 48 48 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P02400 1 110 +P02400 UniProtKB Chain 1 110 . . . ID=PRO_0000157682;Note=60S acidic ribosomal protein P2-beta +P02400 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P02400 UniProtKB Modified residue 100 100 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P02400 UniProtKB Cross-link 49 49 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P02400 UniProtKB Sequence conflict 75 78 . . . Note=AAGA->GPAS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02400 UniProtKB Sequence conflict 86 87 . . . Note=DA->GD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02400 UniProtKB Sequence conflict 89 89 . . . Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12495 1 606 +Q12495 UniProtKB Chain 1 606 . . . ID=PRO_0000089272;Note=Chromatin assembly factor 1 subunit p90 +Q12495 UniProtKB Coiled coil 128 240 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12495 UniProtKB Compositional bias 122 236 . . . Note=Arg/Glu/Lys-rich (highly charged) +Q12495 UniProtKB Compositional bias 166 169 . . . Note=Poly-Lys +Q12495 UniProtKB Compositional bias 383 436 . . . Note=Asp/Glu-rich (acidic) +Q12495 UniProtKB Compositional bias 393 398 . . . Note=Poly-Glu +Q12495 UniProtKB Compositional bias 406 412 . . . Note=Poly-Glu +Q12495 UniProtKB Modified residue 78 78 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12495 UniProtKB Modified residue 94 94 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12495 UniProtKB Modified residue 509 509 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12495 UniProtKB Helix 527 537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EJO +Q12495 UniProtKB Helix 544 554 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EJO +Q12495 UniProtKB Helix 560 570 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EJO +Q12495 UniProtKB Beta strand 571 573 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EJO +Q12495 UniProtKB Beta strand 577 580 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JBM +Q12495 UniProtKB Beta strand 584 587 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EJO +Q12495 UniProtKB Helix 589 598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EJO +##sequence-region Q03195 1 608 +Q03195 UniProtKB Chain 1 608 . . . ID=PRO_0000268703;Note=Translation initiation factor RLI1 +Q03195 UniProtKB Domain 7 39 . . . Note=4Fe-4S ferredoxin-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00711 +Q03195 UniProtKB Domain 46 75 . . . Note=4Fe-4S ferredoxin-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00711 +Q03195 UniProtKB Domain 70 320 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q03195 UniProtKB Domain 345 568 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q03195 UniProtKB Nucleotide binding 110 117 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q03195 UniProtKB Nucleotide binding 385 392 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q03195 UniProtKB Modified residue 349 349 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03195 UniProtKB Mutagenesis 224 224 . . . Note=Lethal%3B when associated with D-225. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15277527;Dbxref=PMID:15277527 +Q03195 UniProtKB Mutagenesis 225 225 . . . Note=Lethal%3B when associated with D-224. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15277527;Dbxref=PMID:15277527 +Q03195 UniProtKB Mutagenesis 470 470 . . . Note=Lethal%3B when associated with D-471. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15277527;Dbxref=PMID:15277527 +Q03195 UniProtKB Mutagenesis 471 471 . . . Note=Lethal%3B when associated with D-470. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15277527;Dbxref=PMID:15277527 +Q03195 UniProtKB Mutagenesis 493 493 . . . Note=Lethal. Inhibits translation in vitro. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15277527;Dbxref=PMID:15277527 +##sequence-region Q12224 1 676 +Q12224 UniProtKB Chain 1 676 . . . ID=PRO_0000199440;Note=Transcription factor RLM1 +Q12224 UniProtKB Domain 3 57 . . . Note=MADS-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00251 +Q12224 UniProtKB DNA binding 58 87 . . . Note=Mef2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12224 UniProtKB Compositional bias 129 134 . . . Note=Poly-Asp +Q12224 UniProtKB Compositional bias 207 212 . . . Note=Poly-Gln +Q12224 UniProtKB Compositional bias 229 236 . . . Note=Poly-Ser +Q12224 UniProtKB Compositional bias 414 417 . . . Note=Poly-Asn +Q12224 UniProtKB Compositional bias 567 579 . . . Note=Poly-Asn +Q12224 UniProtKB Modified residue 120 120 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12224 UniProtKB Modified residue 164 164 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12224 UniProtKB Modified residue 374 374 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12224 UniProtKB Modified residue 377 377 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P36520 1 322 +P36520 UniProtKB Transit peptide 1 57 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626 +P36520 UniProtKB Chain 58 322 . . . ID=PRO_0000030468;Note=54S ribosomal protein L10%2C mitochondrial +P36520 UniProtKB Sequence conflict 68 68 . . . Note=D->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36520 UniProtKB Sequence conflict 71 71 . . . Note=T->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36520 UniProtKB Sequence conflict 182 182 . . . Note=F->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36520 UniProtKB Sequence conflict 188 188 . . . Note=I->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P23369 1 157 +P23369 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2017142;Dbxref=PMID:2017142 +P23369 UniProtKB Chain 2 157 . . . ID=PRO_0000087690;Note=54S ribosomal protein L25%2C mitochondrial +P23369 UniProtKB Sequence conflict 14 14 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23369 UniProtKB Sequence conflict 27 27 . . . Note=Y->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36531 1 177 +P36531 UniProtKB Transit peptide 1 14 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626 +P36531 UniProtKB Chain 15 177 . . . ID=PRO_0000030580;Note=54S ribosomal protein L36%2C mitochondrial +P36531 UniProtKB Region 36 118 . . . Note=Sufficient for general mitochondrial translation +P36531 UniProtKB Region 87 177 . . . Note=Sufficient for dosage suppression of COX2 mutation +##sequence-region P36533 1 70 +P36533 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626 +P36533 UniProtKB Chain 2 70 . . . ID=PRO_0000087693;Note=54S ribosomal protein L39%2C mitochondrial +P36533 UniProtKB Sequence conflict 29 29 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36533 UniProtKB Sequence conflict 38 38 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36533 UniProtKB Sequence conflict 47 47 . . . Note=V->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36534 1 297 +P36534 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P36534 UniProtKB Chain 2 297 . . . ID=PRO_0000030582;Note=54S ribosomal protein L40%2C mitochondrial +P36534 UniProtKB Domain 63 96 . . . Note=KOW +P36534 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P36534 UniProtKB Sequence conflict 179 179 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06090 1 140 +Q06090 UniProtKB Chain 1 140 . . . ID=PRO_0000030590;Note=54S ribosomal protein L51%2C mitochondrial +##sequence-region P43620 1 662 +P43620 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P43620 UniProtKB Chain 2 662 . . . ID=PRO_0000202698;Note=Sporulation protein RMD8 +P43620 UniProtKB Transmembrane 630 647 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43620 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P49166 1 88 +P49166 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3 +P49166 UniProtKB Chain 2 88 . . . ID=PRO_0000139722;Note=60S ribosomal protein L37-A +P49166 UniProtKB Zinc finger 19 37 . . . Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P49166 UniProtKB Metal binding 19 19 . . . Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22096102;Dbxref=PMID:22096102 +P49166 UniProtKB Metal binding 22 22 . . . Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22096102;Dbxref=PMID:22096102 +P49166 UniProtKB Metal binding 34 34 . . . Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22096102;Dbxref=PMID:22096102 +P49166 UniProtKB Metal binding 37 37 . . . Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22096102;Dbxref=PMID:22096102 +P49166 UniProtKB Sequence conflict 73 73 . . . Note=R->RR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P49166 UniProtKB Helix 5 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P49166 UniProtKB Beta strand 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P49166 UniProtKB Turn 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P49166 UniProtKB Beta strand 24 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P49166 UniProtKB Turn 29 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P49166 UniProtKB Turn 35 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P49166 UniProtKB Beta strand 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P49166 UniProtKB Helix 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U55 +P49166 UniProtKB Helix 51 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P49166 UniProtKB Helix 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P49166 UniProtKB Helix 70 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P49166 UniProtKB Turn 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P04650 1 51 +P04650 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P04650 UniProtKB Chain 2 51 . . . ID=PRO_0000127044;Note=60S ribosomal protein L39 +P04650 UniProtKB Helix 7 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04650 UniProtKB Helix 25 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04650 UniProtKB Turn 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P25348 1 183 +P25348 UniProtKB Transit peptide 1 71 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626 +P25348 UniProtKB Chain 72 183 . . . ID=PRO_0000030518;Note=54S ribosomal protein L32%2C mitochondrial +##sequence-region Q04598 1 105 +Q04598 UniProtKB Transit peptide 1 16 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04598 UniProtKB Chain 17 105 . . . ID=PRO_0000030523;Note=54S ribosomal protein L34%2C mitochondrial +##sequence-region P32387 1 263 +P32387 UniProtKB Transit peptide 1 45 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626 +P32387 UniProtKB Chain 46 263 . . . ID=PRO_0000030488;Note=54S ribosomal protein L41%2C mitochondrial +P32387 UniProtKB Sequence conflict 52 52 . . . Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32387 UniProtKB Sequence conflict 155 155 . . . Note=P->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32387 UniProtKB Sequence conflict 253 253 . . . Note=I->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32387 UniProtKB Sequence conflict 259 259 . . . Note=I->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32338 1 300 +P32338 UniProtKB Chain 1 300 . . . ID=PRO_0000046848;Note=Zinc finger protein RME1 +P32338 UniProtKB Zinc finger 178 199 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P32338 UniProtKB Zinc finger 206 234 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P32338 UniProtKB Zinc finger 256 281 . . . Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P32338 UniProtKB Mutagenesis 183 183 . . . Note=Inactivates RME1. C->S +P32338 UniProtKB Mutagenesis 213 213 . . . Note=Inactivates RME1. C->S +P32338 UniProtKB Mutagenesis 263 263 . . . Note=Inactivates RME1. C->S +##sequence-region Q02685 1 241 +Q02685 UniProtKB Chain 1 241 . . . ID=PRO_0000270571;Note=RecQ-mediated genome instability protein 1 +##sequence-region P40525 1 121 +P40525 UniProtKB Chain 1 121 . . . ID=PRO_0000131846;Note=60S ribosomal protein L34-B +##sequence-region P49167 1 78 +P49167 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P49167 UniProtKB Chain 2 78 . . . ID=PRO_0000215445;Note=60S ribosomal protein L38 +P49167 UniProtKB Beta strand 3 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P49167 UniProtKB Helix 8 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P49167 UniProtKB Beta strand 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P49167 UniProtKB Beta strand 22 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P49167 UniProtKB Beta strand 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P49167 UniProtKB Beta strand 37 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P49167 UniProtKB Beta strand 51 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P49167 UniProtKB Helix 59 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P49167 UniProtKB Beta strand 73 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P0CX87 1 25 +P0CX87 UniProtKB Chain 1 25 . . . ID=PRO_0000410448;Note=60S ribosomal protein L41-B +P0CX87 UniProtKB Compositional bias 2 23 . . . Note=Arg-rich +##sequence-region P0CX26 1 92 +P0CX26 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983894;Dbxref=PMID:11983894 +P0CX26 UniProtKB Chain 2 92 . . . ID=PRO_0000409759;Note=60S ribosomal protein L43-B +P0CX26 UniProtKB Zinc finger 39 60 . . . Note=C4-type +P0CX26 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region P0CX28 1 106 +P0CX28 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:365584;Dbxref=PMID:365584 +P0CX28 UniProtKB Chain 2 106 . . . ID=PRO_0000409760;Note=60S ribosomal protein L42-B +P0CX28 UniProtKB Modified residue 40 40 . . . Note=N6-methyllysine%3B by RKM3;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18957409,ECO:0000269|PubMed:22522802,ECO:0000269|PubMed:24517342;Dbxref=PMID:18957409,PMID:22522802,PMID:24517342 +P0CX28 UniProtKB Modified residue 55 55 . . . Note=N6-methyllysine%3B by RKM4;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18957409,ECO:0000269|PubMed:24517342;Dbxref=PMID:18957409,PMID:24517342 +P0CX28 UniProtKB Natural variant 56 56 . . . Note=Confers resistance to cycloheximide%2C an inhibitor of polypeptide elongation. P->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1729213;Dbxref=PMID:1729213 +P0CX28 UniProtKB Sequence conflict 40 41 . . . Note=KR->RK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0CX28 UniProtKB Sequence conflict 88 89 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02326 1 176 +Q02326 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +Q02326 UniProtKB Chain 2 176 . . . ID=PRO_0000171017;Note=60S ribosomal protein L6-A +Q02326 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +Q02326 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q02326 UniProtKB Cross-link 128 128 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05739 +Q02326 UniProtKB Beta strand 38 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS +Q02326 UniProtKB Turn 46 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS +Q02326 UniProtKB Beta strand 51 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS +Q02326 UniProtKB Beta strand 63 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS +Q02326 UniProtKB Helix 69 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS +Q02326 UniProtKB Beta strand 76 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS +Q02326 UniProtKB Helix 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS +Q02326 UniProtKB Beta strand 84 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS +Q02326 UniProtKB Turn 103 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS +Q02326 UniProtKB Helix 113 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS +Q02326 UniProtKB Helix 123 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS +Q02326 UniProtKB Helix 132 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS +Q02326 UniProtKB Helix 155 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS +Q02326 UniProtKB Turn 171 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JBS +##sequence-region P51401 1 191 +P51401 UniProtKB Chain 1 191 . . . ID=PRO_0000131112;Note=60S ribosomal protein L9-B +##sequence-region P05317 1 312 +P05317 UniProtKB Chain 1 312 . . . ID=PRO_0000154786;Note=60S acidic ribosomal protein P0 +P05317 UniProtKB Region 199 230 . . . Note=Interaction with P1A-P2B +P05317 UniProtKB Region 231 258 . . . Note=Interaction with P1B-P2A +P05317 UniProtKB Modified residue 68 68 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P05317 UniProtKB Modified residue 302 302 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:9843429;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:9843429 +P05317 UniProtKB Cross-link 14 14 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P05317 UniProtKB Cross-link 97 97 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P05317 UniProtKB Cross-link 144 144 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P05317 UniProtKB Sequence conflict 83 83 . . . Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05317 UniProtKB Sequence conflict 83 83 . . . Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05317 UniProtKB Sequence conflict 83 83 . . . Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05317 UniProtKB Helix 4 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05317 UniProtKB Beta strand 23 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05317 UniProtKB Helix 35 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05317 UniProtKB Beta strand 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P05317 UniProtKB Beta strand 50 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05317 UniProtKB Helix 56 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05317 UniProtKB Beta strand 68 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05317 UniProtKB Helix 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05317 UniProtKB Helix 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05317 UniProtKB Beta strand 82 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05317 UniProtKB Helix 93 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05317 UniProtKB Beta strand 186 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05317 UniProtKB Beta strand 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M +P05317 UniProtKB Turn 200 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05317 UniProtKB Helix 210 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05317 UniProtKB Turn 214 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region Q07915 1 199 +Q07915 UniProtKB Chain 1 199 . . . ID=PRO_0000136910;Note=Ribosome biogenesis protein RLP24 +Q07915 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P12687 1 371 +P12687 UniProtKB Transit peptide 1 27 . . . Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2060626,ECO:0000269|PubMed:2693936;Dbxref=PMID:2060626,PMID:2693936 +P12687 UniProtKB Chain 28 371 . . . ID=PRO_0000030503;Note=54S ribosomal protein L2%2C mitochondrial +P12687 UniProtKB Sequence conflict 28 29 . . . Note=AT->SG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12687 UniProtKB Sequence conflict 350 350 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36516 1 390 +P36516 UniProtKB Transit peptide 1 59 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3060376;Dbxref=PMID:3060376 +P36516 UniProtKB Chain 60 390 . . . ID=PRO_0000030569;Note=54S ribosomal protein L3%2C mitochondrial +P36516 UniProtKB Domain 139 205 . . . Note=RNase III;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00177 +P36516 UniProtKB Domain 302 372 . . . Note=DRBM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00266 +P36516 UniProtKB Sequence conflict 60 60 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P22353 1 238 +P22353 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2183197;Dbxref=PMID:2183197 +P22353 UniProtKB Chain 2 238 . . . ID=PRO_0000175550;Note=54S ribosomal protein L8%2C mitochondrial +P22353 UniProtKB Sequence conflict 2 2 . . . Note=T->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22353 UniProtKB Sequence conflict 82 82 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32388 1 137 +P32388 UniProtKB Chain 1 137 . . . ID=PRO_0000030583;Note=54S ribosomal protein MRP49%2C mitochondrial +##sequence-region P53724 1 139 +P53724 UniProtKB Chain 1 139 . . . ID=PRO_0000030584;Note=54S ribosomal protein L50%2C mitochondrial +##sequence-region P38330 1 731 +P38330 UniProtKB Modified residue 132 132 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P25299 1 296 +P25299 UniProtKB Chain 1 296 . . . ID=PRO_0000081807;Note=mRNA 3'-end-processing protein RNA15 +P25299 UniProtKB Domain 18 96 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P25299 UniProtKB Compositional bias 104 109 . . . Note=Poly-Gln +P25299 UniProtKB Compositional bias 111 128 . . . Note=Asn-rich +P25299 UniProtKB Beta strand 18 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2X1F +P25299 UniProtKB Helix 31 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2X1F +P25299 UniProtKB Beta strand 44 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2X1F +P25299 UniProtKB Turn 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2X1F +P25299 UniProtKB Beta strand 60 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2X1F +P25299 UniProtKB Helix 69 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2X1F +P25299 UniProtKB Beta strand 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM8 +P25299 UniProtKB Beta strand 90 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2X1F +P25299 UniProtKB Helix 99 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2X1F +P25299 UniProtKB Helix 139 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B +P25299 UniProtKB Turn 156 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B +P25299 UniProtKB Helix 161 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B +P25299 UniProtKB Helix 174 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B +P25299 UniProtKB Helix 192 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B +P25299 UniProtKB Helix 203 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B +P25299 UniProtKB Beta strand 217 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B +P25299 UniProtKB Helix 221 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B +P25299 UniProtKB Turn 225 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B +##sequence-region P11745 1 407 +P11745 UniProtKB Chain 1 407 . . . ID=PRO_0000056742;Note=Ran GTPase-activating protein 1 +P11745 UniProtKB Repeat 11 39 . . . Note=LRR 1 +P11745 UniProtKB Repeat 40 67 . . . Note=LRR 2 +P11745 UniProtKB Repeat 68 101 . . . Note=LRR 3 +P11745 UniProtKB Repeat 102 133 . . . Note=LRR 4 +P11745 UniProtKB Repeat 134 166 . . . Note=LRR 5 +P11745 UniProtKB Repeat 167 197 . . . Note=LRR 6 +P11745 UniProtKB Repeat 198 226 . . . Note=LRR 7 +P11745 UniProtKB Repeat 227 256 . . . Note=LRR 8 +P11745 UniProtKB Repeat 257 285 . . . Note=LRR 9 +P11745 UniProtKB Repeat 286 315 . . . Note=LRR 10 +P11745 UniProtKB Repeat 316 346 . . . Note=LRR 11 +P11745 UniProtKB Compositional bias 348 375 . . . Note=Asp/Glu-rich (acidic) +P11745 UniProtKB Modified residue 360 360 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P11745 UniProtKB Natural variant 17 17 . . . Note=In mutant RNA1-1. S->F +P11745 UniProtKB Natural variant 194 194 . . . Note=In mutant RNA1-1. A->V +P11745 UniProtKB Sequence conflict 42 42 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11745 UniProtKB Sequence conflict 222 222 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q05635 1 350 +Q05635 UniProtKB Chain 1 350 . . . ID=PRO_0000248383;Note=Ribonuclease H2 subunit B +Q05635 UniProtKB Sequence conflict 83 83 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P05747 1 59 +P05747 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:18782943 +P05747 UniProtKB Chain 2 59 . . . ID=PRO_0000219141;Note=60S ribosomal protein L29 +P05747 UniProtKB Cross-link 52 52 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P05747 UniProtKB Helix 12 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05747 UniProtKB Helix 37 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05747 UniProtKB Helix 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P0CX27 1 106 +P0CX27 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:365584;Dbxref=PMID:365584 +P0CX27 UniProtKB Chain 2 106 . . . ID=PRO_0000149147;Note=60S ribosomal protein L42-A +P0CX27 UniProtKB Modified residue 40 40 . . . Note=N6-methyllysine%3B by RKM3;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18957409,ECO:0000269|PubMed:22522802,ECO:0000269|PubMed:24517342;Dbxref=PMID:18957409,PMID:22522802,PMID:24517342 +P0CX27 UniProtKB Modified residue 55 55 . . . Note=N6-methyllysine%3B by RKM4;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18957409,ECO:0000269|PubMed:24517342;Dbxref=PMID:18957409,PMID:24517342 +P0CX27 UniProtKB Natural variant 56 56 . . . Note=Confers resistance to cycloheximide%2C an inhibitor of polypeptide elongation. P->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1729213;Dbxref=PMID:1729213 +P0CX27 UniProtKB Sequence conflict 40 41 . . . Note=KR->RK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0CX27 UniProtKB Sequence conflict 88 89 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0CX27 UniProtKB Beta strand 6 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX27 UniProtKB Turn 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX27 UniProtKB Beta strand 19 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX27 UniProtKB Helix 38 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX27 UniProtKB Beta strand 48 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX27 UniProtKB Beta strand 66 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX27 UniProtKB Turn 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX27 UniProtKB Beta strand 80 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX27 UniProtKB Beta strand 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region Q12213 1 244 +Q12213 UniProtKB Chain 1 244 . . . ID=PRO_0000104652;Note=60S ribosomal protein L7-B +##sequence-region P38064 1 232 +P38064 UniProtKB Transit peptide 1 41 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38064 UniProtKB Chain 42 232 . . . ID=PRO_0000030469;Note=54S ribosomal protein L16%2C mitochondrial +P38064 UniProtKB Sequence conflict 55 55 . . . Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38064 UniProtKB Sequence conflict 119 119 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38064 UniProtKB Sequence conflict 209 209 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36527 1 147 +P36527 UniProtKB Transit peptide 1 26 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626 +P36527 UniProtKB Chain 27 147 . . . ID=PRO_0000030575;Note=54S ribosomal protein L28%2C mitochondrial +P36527 UniProtKB Sequence conflict 28 29 . . . Note=RT->IF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36527 UniProtKB Sequence conflict 33 37 . . . Note=SSLSP->VILVI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36527 UniProtKB Sequence conflict 49 49 . . . Note=M->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36527 UniProtKB Sequence conflict 53 53 . . . Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P20084 1 86 +P20084 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626 +P20084 UniProtKB Chain 2 86 . . . ID=PRO_0000104619;Note=54S ribosomal protein L33%2C mitochondrial +P20084 UniProtKB Sequence conflict 81 86 . . . Note=EKRTID->GEENHRLKQRNKALDFLSS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36532 1 105 +P36532 UniProtKB Transit peptide 1 24 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626 +P36532 UniProtKB Chain 25 105 . . . ID=PRO_0000030581;Note=54S ribosomal protein L37%2C mitochondrial +P36532 UniProtKB Sequence conflict 27 27 . . . Note=V->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36532 UniProtKB Sequence conflict 30 30 . . . Note=C->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36532 UniProtKB Sequence conflict 35 35 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36532 UniProtKB Sequence conflict 41 41 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36532 UniProtKB Sequence conflict 54 54 . . . Note=E->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P35996 1 138 +P35996 UniProtKB Chain 1 138 . . . ID=PRO_0000030464;Note=54S ribosomal protein L38%2C mitochondrial +P35996 UniProtKB Chain 58 138 . . . ID=PRO_0000030465;Note=54S ribosomal protein L34%2C mitochondrial +P35996 UniProtKB Sequence conflict 60 60 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35996 UniProtKB Sequence conflict 69 70 . . . Note=CH->DI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P02406 1 149 +P02406 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P02406 UniProtKB Chain 2 149 . . . ID=PRO_0000104904;Note=60S ribosomal protein L28 +P02406 UniProtKB Motif 7 13 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2104804;Dbxref=PMID:2104804 +P02406 UniProtKB Motif 24 30 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2104804;Dbxref=PMID:2104804 +P02406 UniProtKB Cross-link 96 96 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P02406 UniProtKB Natural variant 38 38 . . . Note=Confers resistance to cycloheximide%2C an inhibitor of polypeptide elongation. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6304624;Dbxref=PMID:6304624 +P02406 UniProtKB Helix 3 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Helix 7 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Beta strand 14 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Helix 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Beta strand 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Turn 33 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Helix 42 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Turn 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Turn 65 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Beta strand 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Turn 75 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Helix 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Helix 84 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Beta strand 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Turn 104 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Beta strand 110 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Beta strand 124 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Helix 132 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02406 UniProtKB Beta strand 144 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P0CX85 1 120 +P0CX85 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983894;Dbxref=PMID:11983894 +P0CX85 UniProtKB Chain 2 120 . . . ID=PRO_0000410447;Note=60S ribosomal protein L35-B +P0CX85 UniProtKB Modified residue 13 13 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX85 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P14126 1 387 +P14126 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1544921,ECO:0000269|PubMed:6355773;Dbxref=PMID:1544921,PMID:6355773 +P14126 UniProtKB Chain 2 387 . . . ID=PRO_0000077251;Note=60S ribosomal protein L3 +P14126 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P14126 UniProtKB Modified residue 103 103 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P14126 UniProtKB Modified residue 156 156 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P14126 UniProtKB Modified residue 243 243 . . . Note=Pros-methylhistidine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20864530;Dbxref=PMID:20864530 +P14126 UniProtKB Modified residue 297 297 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14126 UniProtKB Cross-link 39 39 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P14126 UniProtKB Cross-link 136 136 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P14126 UniProtKB Sequence conflict 255 255 . . . Note=W->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14126 UniProtKB Helix 14 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Beta strand 23 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U52 +P14126 UniProtKB Beta strand 37 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U53 +P14126 UniProtKB Beta strand 44 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Turn 66 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Beta strand 70 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Beta strand 84 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Beta strand 100 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Helix 112 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Helix 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Turn 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Turn 129 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Helix 134 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Beta strand 139 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Helix 142 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Beta strand 156 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Helix 166 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Beta strand 178 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Beta strand 185 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U6F +P14126 UniProtKB Helix 188 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Turn 198 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Beta strand 201 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P14126 UniProtKB Helix 205 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Beta strand 214 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Beta strand 223 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Helix 229 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Beta strand 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Beta strand 255 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Beta strand 268 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Beta strand 274 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Turn 291 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Turn 297 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Turn 312 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Beta strand 321 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Beta strand 335 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Turn 349 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Beta strand 356 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Turn 364 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P14126 UniProtKB Helix 373 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P0CH09 1 128 +P0CH09 UniProtKB Chain 1 76 . . . ID=PRO_0000396455;Note=Ubiquitin +P0CH09 UniProtKB Chain 77 128 . . . ID=PRO_0000396456;Note=60S ribosomal protein L40-B +P0CH09 UniProtKB Domain 1 76 . . . Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 +P0CH09 UniProtKB Cross-link 76 76 . . . Note=Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) +P0CH09 UniProtKB Cross-link 93 93 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CH09 UniProtKB Mutagenesis 29 29 . . . Note=Deficiency in ubiquitin-protein conjugate formation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550 +P0CH09 UniProtKB Mutagenesis 48 48 . . . Note=Deficiency in ubiquitin-protein conjugate formation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550 +P0CH09 UniProtKB Mutagenesis 63 63 . . . Note=Deficiency in ubiquitin-protein conjugate formation. Loss of DNA repair function. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550 +##sequence-region P0CX86 1 25 +P0CX86 UniProtKB Chain 1 25 . . . ID=PRO_0000198074;Note=60S ribosomal protein L41-A +P0CX86 UniProtKB Compositional bias 2 23 . . . Note=Arg-rich +P0CX86 UniProtKB Helix 3 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM +##sequence-region P10664 1 362 +P10664 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921 +P10664 UniProtKB Chain 2 362 . . . ID=PRO_0000129367;Note=60S ribosomal protein L4-A +P10664 UniProtKB Region 277 362 . . . Note=C-terminal-extended nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P10664 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921 +P10664 UniProtKB Mutagenesis 95 95 . . . Note=Leads to a slower growth at higher temperatures but allows RPL4 assembly into the 60S subunit%3B when associated with E-98. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P10664 UniProtKB Mutagenesis 98 98 . . . Note=Leads to a slower growth at higher temperatures but allows RPL4 assembly into the 60S subunit%3B when associated with E-95. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P10664 UniProtKB Mutagenesis 289 289 . . . Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with A-290 and A-295. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P10664 UniProtKB Mutagenesis 290 290 . . . Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with A-289 and A-295. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P10664 UniProtKB Mutagenesis 295 295 . . . Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with A-289 and A-290. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P10664 UniProtKB Mutagenesis 314 314 . . . Note=Significantly diminished nuclear localization%3B when associated with A-315 and A-319. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P10664 UniProtKB Mutagenesis 315 315 . . . Note=Significantly diminished nuclear localization%3B when associated with A-314 and A-319. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P10664 UniProtKB Mutagenesis 319 319 . . . Note=Significantly diminished nuclear localization%3B when associated with A-314 and A-315. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P10664 UniProtKB Mutagenesis 332 332 . . . Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with A-334. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P10664 UniProtKB Mutagenesis 334 334 . . . Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with e-332. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P10664 UniProtKB Sequence conflict 38 38 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10664 UniProtKB Sequence conflict 144 144 . . . Note=K->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10664 UniProtKB Sequence conflict 157 157 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10664 UniProtKB Sequence conflict 224 224 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10664 UniProtKB Sequence conflict 241 241 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10664 UniProtKB Beta strand 6 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Beta strand 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4N +P10664 UniProtKB Beta strand 15 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U6F +P10664 UniProtKB Helix 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Helix 32 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Turn 43 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Turn 54 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Beta strand 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U6F +P10664 UniProtKB Beta strand 67 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Beta strand 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Beta strand 81 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Beta strand 94 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56 +P10664 UniProtKB Helix 115 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Helix 132 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Beta strand 143 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Beta strand 148 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Helix 154 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Helix 162 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Helix 175 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Beta strand 189 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Helix 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Beta strand 206 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Helix 215 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Turn 219 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4N +P10664 UniProtKB Beta strand 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M +P10664 UniProtKB Beta strand 226 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Helix 235 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Helix 240 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Beta strand 248 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Helix 252 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Beta strand 265 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Beta strand 280 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Helix 286 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Turn 292 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Beta strand 317 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Helix 321 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Helix 331 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P10664 UniProtKB Helix 339 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U51 +P10664 UniProtKB Helix 353 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P36517 1 319 +P36517 UniProtKB Transit peptide 1 14 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3060376;Dbxref=PMID:3060376 +P36517 UniProtKB Chain 15 319 . . . ID=PRO_0000030570;Note=54S ribosomal protein L4%2C mitochondrial +P36517 UniProtKB Sequence conflict 168 168 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36519 1 292 +P36519 UniProtKB Transit peptide 1 19 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626 +P36519 UniProtKB Chain 20 292 . . . ID=PRO_0000030545;Note=54S ribosomal protein L7%2C mitochondrial +P36519 UniProtKB Sequence conflict 23 23 . . . Note=C->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36519 UniProtKB Sequence conflict 33 33 . . . Note=V->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36519 UniProtKB Sequence conflict 85 85 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36528 1 281 +P36528 UniProtKB Transit peptide 1 19 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626 +P36528 UniProtKB Chain 20 281 . . . ID=PRO_0000030578;Note=54S ribosomal protein L17%2C mitochondrial +##sequence-region P53881 1 309 +P53881 UniProtKB Transit peptide 1 25 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53881 UniProtKB Chain 26 309 . . . ID=PRO_0000030487;Note=54S ribosomal protein L22%2C mitochondrial +P53881 UniProtKB Sequence conflict 151 151 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12487 1 163 +Q12487 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12487 UniProtKB Propeptide 2 4 . . . ID=PRO_0000030462;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9151978;Dbxref=PMID:9151978 +Q12487 UniProtKB Chain 5 163 . . . ID=PRO_0000030463;Note=54S ribosomal protein L23%2C mitochondrial +Q12487 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12487 UniProtKB Sequence conflict 5 5 . . . Note=I->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39975 1 231 +P39975 UniProtKB Chain 1 231 . . . ID=PRO_0000202600;Note=Sporulation protein RMD6 +P39975 UniProtKB Sequence conflict 28 28 . . . Note=Y->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CX42 1 137 +P0CX42 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:16096273;Dbxref=PMID:22814378,PMID:16096273 +P0CX42 UniProtKB Chain 2 137 . . . ID=PRO_0000409767;Note=60S ribosomal protein L23-B +P0CX42 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:16096273;Dbxref=PMID:22814378,PMID:16096273 +P0CX42 UniProtKB Modified residue 106 106 . . . Note=N6%2CN6-dimethyllysine%3B by RKM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17327221;Dbxref=PMID:17327221 +P0CX42 UniProtKB Modified residue 110 110 . . . Note=N6%2CN6-dimethyllysine%3B by RKM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17327221;Dbxref=PMID:17327221 +##sequence-region P04456 1 142 +P04456 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921 +P04456 UniProtKB Chain 2 142 . . . ID=PRO_0000129483;Note=60S ribosomal protein L25 +P04456 UniProtKB Cross-link 61 61 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15542864;Dbxref=PMID:15542864 +P04456 UniProtKB Sequence conflict 106 112 . . . Note=DVLKVNT->NI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04456 UniProtKB Beta strand 28 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P04456 UniProtKB Beta strand 48 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04456 UniProtKB Helix 59 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04456 UniProtKB Beta strand 63 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04456 UniProtKB Helix 70 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04456 UniProtKB Beta strand 81 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04456 UniProtKB Helix 92 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04456 UniProtKB Beta strand 107 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04456 UniProtKB Turn 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U55 +P04456 UniProtKB Beta strand 120 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04456 UniProtKB Helix 132 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P0C2H9 1 113 +P0C2H9 UniProtKB Chain 1 113 . . . ID=PRO_0000278968;Note=60S ribosomal protein L31-B +##sequence-region P29453 1 256 +P29453 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921 +P29453 UniProtKB Chain 2 256 . . . ID=PRO_0000136761;Note=60S ribosomal protein L8-B +P29453 UniProtKB Sequence conflict 114 115 . . . Note=AA->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P05318 1 106 +P05318 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:8476850;Dbxref=PMID:10601260,PMID:8476850 +P05318 UniProtKB Chain 2 106 . . . ID=PRO_0000157705;Note=60S acidic ribosomal protein P1-alpha +P05318 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:8476850;Dbxref=PMID:10601260,PMID:8476850 +P05318 UniProtKB Modified residue 96 96 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P05318 UniProtKB Sequence conflict 37 37 . . . Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05318 UniProtKB Sequence conflict 37 37 . . . Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05318 UniProtKB Sequence conflict 37 37 . . . Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region O14455 1 100 +O14455 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:18782943 +O14455 UniProtKB Chain 2 100 . . . ID=PRO_0000195021;Note=60S ribosomal protein L36-B +O14455 UniProtKB Sequence conflict 35 35 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CH08 1 128 +P0CH08 UniProtKB Chain 1 76 . . . ID=PRO_0000396454;Note=Ubiquitin +P0CH08 UniProtKB Chain 77 128 . . . ID=PRO_0000138775;Note=60S ribosomal protein L40-A +P0CH08 UniProtKB Domain 1 76 . . . Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 +P0CH08 UniProtKB Cross-link 76 76 . . . Note=Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) +P0CH08 UniProtKB Cross-link 93 93 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CH08 UniProtKB Mutagenesis 29 29 . . . Note=Deficiency in ubiquitin-protein conjugate formation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550 +P0CH08 UniProtKB Mutagenesis 48 48 . . . Note=Deficiency in ubiquitin-protein conjugate formation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550 +P0CH08 UniProtKB Mutagenesis 63 63 . . . Note=Deficiency in ubiquitin-protein conjugate formation. Loss of DNA repair function. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550 +P0CH08 UniProtKB Helix 80 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CH08 UniProtKB Beta strand 94 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CH08 UniProtKB Turn 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CH08 UniProtKB Turn 113 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CH08 UniProtKB Beta strand 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P0CX25 1 92 +P0CX25 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983894;Dbxref=PMID:11983894 +P0CX25 UniProtKB Chain 2 92 . . . ID=PRO_0000139838;Note=60S ribosomal protein L43-A +P0CX25 UniProtKB Zinc finger 39 60 . . . Note=C4-type +P0CX25 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX25 UniProtKB Helix 9 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX25 UniProtKB Turn 15 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX25 UniProtKB Helix 20 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX25 UniProtKB Turn 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX25 UniProtKB Beta strand 44 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX25 UniProtKB Beta strand 54 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX25 UniProtKB Turn 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX25 UniProtKB Beta strand 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX25 UniProtKB Beta strand 68 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX25 UniProtKB Helix 74 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P26321 1 297 +P26321 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:393511;Dbxref=PMID:393511 +P26321 UniProtKB Chain 2 297 . . . ID=PRO_0000131454;Note=60S ribosomal protein L5 +P26321 UniProtKB Modified residue 167 167 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P26321 UniProtKB Modified residue 176 176 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P26321 UniProtKB Modified residue 235 235 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P26321 UniProtKB Cross-link 164 164 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P26321 UniProtKB Sequence conflict 18 18 . . . Note=T->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P26321 UniProtKB Sequence conflict 112 112 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P26321 UniProtKB Sequence conflict 112 112 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P26321 UniProtKB Beta strand 4 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P26321 UniProtKB Helix 10 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Helix 21 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Helix 30 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Helix 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Beta strand 50 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Beta strand 59 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Beta strand 71 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Helix 80 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Beta strand 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P26321 UniProtKB Helix 95 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Beta strand 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Beta strand 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Beta strand 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Helix 159 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Helix 177 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P26321 UniProtKB Beta strand 180 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P26321 UniProtKB Turn 185 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Helix 192 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Helix 202 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Helix 216 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Helix 224 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Helix 233 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Helix 236 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Helix 262 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Beta strand 271 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Helix 279 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26321 UniProtKB Turn 293 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P05739 1 176 +P05739 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18782943;Dbxref=PMID:18782943 +P05739 UniProtKB Chain 2 176 . . . ID=PRO_0000171018;Note=60S ribosomal protein L6-B +P05739 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q02326 +P05739 UniProtKB Cross-link 128 128 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P05739 UniProtKB Sequence conflict 68 68 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38144 1 1129 +P38144 UniProtKB Chain 1 1129 . . . ID=PRO_0000074330;Note=ISWI chromatin-remodeling complex ATPase ISW1 +P38144 UniProtKB Domain 208 373 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P38144 UniProtKB Domain 506 657 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P38144 UniProtKB Domain 882 935 . . . Note=SANT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00624 +P38144 UniProtKB Domain 988 1052 . . . Note=SANT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00624 +P38144 UniProtKB Nucleotide binding 221 228 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P38144 UniProtKB Motif 324 327 . . . Note=DEAH box +P38144 UniProtKB Modified residue 694 694 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38144 UniProtKB Modified residue 846 846 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38144 UniProtKB Mutagenesis 227 227 . . . Note=Abolishes ATPase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10090725;Dbxref=PMID:10090725 +P38144 UniProtKB Helix 814 827 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Turn 828 830 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Helix 835 838 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Turn 839 841 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Turn 848 850 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Helix 851 862 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Beta strand 866 868 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Helix 870 882 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Helix 889 902 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Helix 907 911 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Beta strand 917 919 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Helix 920 932 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Turn 941 943 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Helix 944 968 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Helix 974 977 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Helix 994 1007 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Helix 1015 1024 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Helix 1027 1029 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Helix 1032 1035 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Helix 1039 1054 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P38144 UniProtKB Turn 1055 1058 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +##sequence-region Q08773 1 1120 +Q08773 UniProtKB Chain 1 1120 . . . ID=PRO_0000240453;Note=ISWI chromatin-remodeling complex ATPase ISW2 +Q08773 UniProtKB Domain 196 361 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q08773 UniProtKB Domain 494 645 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q08773 UniProtKB Domain 886 938 . . . Note=SANT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00624 +Q08773 UniProtKB Nucleotide binding 209 216 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q08773 UniProtKB Motif 312 315 . . . Note=DEAH box +Q08773 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08773 UniProtKB Modified residue 19 19 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08773 UniProtKB Modified residue 831 831 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q08773 UniProtKB Modified residue 1079 1079 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q08773 UniProtKB Modified residue 1082 1082 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q08773 UniProtKB Mutagenesis 215 215 . . . Note=Abolishes ATPase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10090725;Dbxref=PMID:10090725 +##sequence-region Q03419 1 316 +Q03419 UniProtKB Chain 1 316 . . . ID=PRO_0000240373;Note=ADIPOR-like receptor IZH1 +Q03419 UniProtKB Topological domain 1 89 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03419 UniProtKB Transmembrane 90 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03419 UniProtKB Topological domain 111 117 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03419 UniProtKB Transmembrane 118 138 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03419 UniProtKB Topological domain 139 156 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03419 UniProtKB Transmembrane 157 177 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03419 UniProtKB Topological domain 178 181 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03419 UniProtKB Transmembrane 182 202 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03419 UniProtKB Topological domain 203 218 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03419 UniProtKB Transmembrane 219 239 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03419 UniProtKB Topological domain 240 245 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03419 UniProtKB Transmembrane 246 266 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03419 UniProtKB Topological domain 267 279 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03419 UniProtKB Transmembrane 280 300 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03419 UniProtKB Topological domain 301 316 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03419 UniProtKB Glycosylation 79 79 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03419 UniProtKB Glycosylation 207 207 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03419 UniProtKB Sequence conflict 139 139 . . . Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q99393 1 312 +Q99393 UniProtKB Chain 1 312 . . . ID=PRO_0000240376;Note=ADIPOR-like receptor IZH4 +Q99393 UniProtKB Topological domain 1 64 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99393 UniProtKB Transmembrane 65 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99393 UniProtKB Topological domain 86 101 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99393 UniProtKB Transmembrane 102 122 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99393 UniProtKB Topological domain 123 141 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99393 UniProtKB Transmembrane 142 162 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99393 UniProtKB Topological domain 163 165 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99393 UniProtKB Transmembrane 166 186 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99393 UniProtKB Topological domain 187 201 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99393 UniProtKB Transmembrane 202 222 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99393 UniProtKB Topological domain 223 231 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99393 UniProtKB Transmembrane 232 252 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99393 UniProtKB Topological domain 253 277 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99393 UniProtKB Transmembrane 278 298 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99393 UniProtKB Topological domain 299 312 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99393 UniProtKB Sequence conflict 211 211 . . . Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40358 1 645 +P40358 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40358 UniProtKB Chain 23 645 . . . ID=PRO_0000043353;Note=DnaJ-like chaperone JEM1 +P40358 UniProtKB Topological domain 23 190 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9148890;Dbxref=PMID:9148890 +P40358 UniProtKB Transmembrane 191 211 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40358 UniProtKB Topological domain 212 645 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9148890;Dbxref=PMID:9148890 +P40358 UniProtKB Domain 538 608 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +P40358 UniProtKB Compositional bias 493 525 . . . Note=Gln-rich +##sequence-region P36224 1 373 +P36224 UniProtKB Chain 1 373 . . . ID=PRO_0000084289;Note=Nuclear migration protein JNM1 +P36224 UniProtKB Coiled coil 114 139 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36224 UniProtKB Coiled coil 200 245 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36224 UniProtKB Coiled coil 331 367 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36224 UniProtKB Modified residue 91 91 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36224 UniProtKB Sequence conflict 92 92 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36224 UniProtKB Sequence conflict 114 114 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36224 UniProtKB Sequence conflict 193 193 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36224 UniProtKB Sequence conflict 201 201 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36224 UniProtKB Sequence conflict 264 264 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P07170 1 222 +P07170 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P07170 UniProtKB Propeptide 2 2 . . . ID=PRO_0000016550;Note=Removed in mature form;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:3004985;Dbxref=PMID:3004985 +P07170 UniProtKB Chain 3 222 . . . ID=PRO_0000016551;Note=Adenylate kinase +P07170 UniProtKB Nucleotide binding 16 21 . . . Note=ATP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369,ECO:0000269|PubMed:8594191;Dbxref=PMID:7635152,PMID:7670369,PMID:8594191 +P07170 UniProtKB Nucleotide binding 63 65 . . . Note=AMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369;Dbxref=PMID:7635152,PMID:7670369 +P07170 UniProtKB Nucleotide binding 92 95 . . . Note=AMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369;Dbxref=PMID:7635152,PMID:7670369 +P07170 UniProtKB Nucleotide binding 143 144 . . . Note=ATP;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369,ECO:0000269|PubMed:8594191;Dbxref=PMID:7635152,PMID:7670369,PMID:8594191 +P07170 UniProtKB Region 36 65 . . . Note=NMPbind;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369;Dbxref=PMID:7635152,PMID:7670369 +P07170 UniProtKB Region 133 170 . . . Note=LID;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369;Dbxref=PMID:7635152,PMID:7670369 +P07170 UniProtKB Binding site 37 37 . . . Note=AMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369;Dbxref=PMID:7635152,PMID:7670369 +P07170 UniProtKB Binding site 42 42 . . . Note=AMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369;Dbxref=PMID:7635152,PMID:7670369 +P07170 UniProtKB Binding site 99 99 . . . Note=AMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369;Dbxref=PMID:7635152,PMID:7670369 +P07170 UniProtKB Binding site 134 134 . . . Note=ATP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369,ECO:0000269|PubMed:8594191;Dbxref=PMID:7635152,PMID:7670369,PMID:8594191 +P07170 UniProtKB Binding site 167 167 . . . Note=AMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369;Dbxref=PMID:7635152,PMID:7670369 +P07170 UniProtKB Binding site 178 178 . . . Note=AMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369;Dbxref=PMID:7635152,PMID:7670369 +P07170 UniProtKB Binding site 206 206 . . . Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:7635152,ECO:0000269|PubMed:7670369,ECO:0000269|PubMed:8594191;Dbxref=PMID:7635152,PMID:7670369,PMID:8594191 +P07170 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P07170 UniProtKB Modified residue 3 3 . . . Note=N-acetylserine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03168,ECO:0000269|PubMed:3004985;Dbxref=PMID:3004985 +P07170 UniProtKB Sequence conflict 95 95 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07170 UniProtKB Sequence conflict 139 139 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07170 UniProtKB Sequence conflict 222 222 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07170 UniProtKB Beta strand 8 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Helix 19 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Beta strand 33 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Helix 37 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Helix 50 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Helix 67 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Helix 82 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Beta strand 88 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Helix 97 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Beta strand 116 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Helix 124 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Beta strand 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Turn 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Beta strand 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Turn 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Turn 158 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Helix 172 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Helix 188 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Beta strand 199 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +P07170 UniProtKB Helix 208 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AKY +##sequence-region Q12055 1 197 +Q12055 UniProtKB Chain 1 197 . . . ID=PRO_0000153902;Note=Adenylate kinase isoenzyme 6 homolog FAP7 +Q12055 UniProtKB Nucleotide binding 17 22 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03173 +Q12055 UniProtKB Region 38 61 . . . Note=NMPbind;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03173 +Q12055 UniProtKB Region 113 123 . . . Note=LID;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03173 +Q12055 UniProtKB Motif 28 35 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12055 UniProtKB Binding site 44 44 . . . Note=AMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03173 +Q12055 UniProtKB Binding site 84 84 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03173 +Q12055 UniProtKB Binding site 110 110 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03173 +Q12055 UniProtKB Binding site 114 114 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03173 +Q12055 UniProtKB Modified residue 183 183 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12055 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12055 UniProtKB Modified residue 196 196 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12055 UniProtKB Mutagenesis 19 19 . . . Note=Sensitive to hydrogen peroxide. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10692169;Dbxref=PMID:10692169 +Q12055 UniProtKB Mutagenesis 20 20 . . . Note=Decreases the processing of 20S rRNA. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16287850;Dbxref=PMID:16287850 +Q12055 UniProtKB Mutagenesis 21 21 . . . Note=Sensitive to hydrogen peroxide. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10692169;Dbxref=PMID:10692169 +Q12055 UniProtKB Mutagenesis 82 82 . . . Note=Decreases the processing of 20S rRNA%3B when associated with A-84. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16287850;Dbxref=PMID:16287850 +Q12055 UniProtKB Mutagenesis 84 84 . . . Note=Decreases the processing of 20S rRNA%3B when associated with A-82. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16287850;Dbxref=PMID:16287850 +Q12055 UniProtKB Sequence conflict 80 80 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P06245 1 380 +P06245 UniProtKB Chain 1 380 . . . ID=PRO_0000086048;Note=cAMP-dependent protein kinase type 2 +P06245 UniProtKB Domain 70 324 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P06245 UniProtKB Domain 325 380 . . . Note=AGC-kinase C-terminal +P06245 UniProtKB Nucleotide binding 76 84 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P06245 UniProtKB Active site 193 193 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P06245 UniProtKB Binding site 99 99 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P06245 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P06245 UniProtKB Modified residue 224 224 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P06245 UniProtKB Sequence conflict 214 220 . . . Note=FAKEVQT->LRQRGTN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06245 UniProtKB Sequence conflict 260 260 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06245 UniProtKB Sequence conflict 289 289 . . . Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04746 1 504 +Q04746 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04746 UniProtKB Chain 20 504 . . . ID=PRO_0000203279;Note=Nuclear fusion protein KAR5 +Q04746 UniProtKB Topological domain 20 452 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9382856;Dbxref=PMID:9382856 +Q04746 UniProtKB Transmembrane 453 470 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04746 UniProtKB Topological domain 471 481 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9382856;Dbxref=PMID:9382856 +Q04746 UniProtKB Transmembrane 482 502 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04746 UniProtKB Topological domain 503 504 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9382856;Dbxref=PMID:9382856 +Q04746 UniProtKB Glycosylation 159 159 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04746 UniProtKB Glycosylation 206 206 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04746 UniProtKB Glycosylation 313 313 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04746 UniProtKB Glycosylation 404 404 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39962 1 524 +P39962 UniProtKB Chain 1 524 . . . ID=PRO_0000192858;Note=Casein kinase I homolog 3 +P39962 UniProtKB Domain 14 319 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P39962 UniProtKB Nucleotide binding 20 28 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P39962 UniProtKB Motif 444 447 . . . Note=YXXZ targeting signal +P39962 UniProtKB Active site 150 150 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P39962 UniProtKB Binding site 60 60 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P39962 UniProtKB Lipidation 517 517 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:14668479;Dbxref=PMID:14668479 +P39962 UniProtKB Lipidation 518 518 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:14668479;Dbxref=PMID:14668479 +P39962 UniProtKB Lipidation 519 519 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:14668479;Dbxref=PMID:14668479 +P39962 UniProtKB Lipidation 520 520 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:14668479;Dbxref=PMID:14668479 +P39962 UniProtKB Lipidation 522 522 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:14668479;Dbxref=PMID:14668479 +P39962 UniProtKB Lipidation 523 523 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:14668479;Dbxref=PMID:14668479 +P39962 UniProtKB Lipidation 524 524 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:14668479;Dbxref=PMID:14668479 +P39962 UniProtKB Mutagenesis 444 444 . . . Note=Impaired vacuolar targeting. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14668479;Dbxref=PMID:14668479 +P39962 UniProtKB Mutagenesis 446 446 . . . Note=Impaired vacuolar targeting. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14668479;Dbxref=PMID:14668479 +P39962 UniProtKB Mutagenesis 447 447 . . . Note=Impaired vacuolar targeting. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14668479;Dbxref=PMID:14668479 +##sequence-region P27466 1 446 +P27466 UniProtKB Chain 1 446 . . . ID=PRO_0000086090;Note=Calcium/calmodulin-dependent protein kinase I +P27466 UniProtKB Domain 37 299 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P27466 UniProtKB Nucleotide binding 43 51 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P27466 UniProtKB Region 312 323 . . . Note=Calmodulin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P27466 UniProtKB Active site 161 161 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P27466 UniProtKB Binding site 66 66 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P27466 UniProtKB Modified residue 343 343 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22517 +P27466 UniProtKB Modified residue 357 357 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22517 +P27466 UniProtKB Modified residue 417 417 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P27466 UniProtKB Modified residue 418 418 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P27466 UniProtKB Modified residue 420 420 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P27466 UniProtKB Modified residue 429 429 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P27466 UniProtKB Sequence conflict 53 54 . . . Note=QA->VR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27466 UniProtKB Sequence conflict 68 68 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27466 UniProtKB Sequence conflict 188 188 . . . Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27466 UniProtKB Sequence conflict 199 202 . . . Note=PAGS->AGTA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27466 UniProtKB Sequence conflict 237 243 . . . Note=SAFRAER->ATIDRK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P27466 UniProtKB Sequence conflict 271 271 . . . Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P34167 1 436 +P34167 UniProtKB Chain 1 436 . . . ID=PRO_0000081618;Note=Eukaryotic translation initiation factor 4B +P34167 UniProtKB Domain 101 183 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P34167 UniProtKB Repeat 190 210 . . . Note=1%3B approximate +P34167 UniProtKB Repeat 211 232 . . . Note=2 +P34167 UniProtKB Repeat 233 258 . . . Note=3 +P34167 UniProtKB Repeat 259 284 . . . Note=4 +P34167 UniProtKB Repeat 285 310 . . . Note=5 +P34167 UniProtKB Repeat 311 340 . . . Note=6 +P34167 UniProtKB Repeat 341 350 . . . Note=7%3B truncated +P34167 UniProtKB Region 190 350 . . . Note=7 X approximate tandem repeats +P34167 UniProtKB Modified residue 65 65 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P34167 UniProtKB Modified residue 71 71 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P34167 UniProtKB Mutagenesis 106 106 . . . Note=Retention of function. N->G%2CV%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8404866;Dbxref=PMID:8404866 +P34167 UniProtKB Mutagenesis 106 106 . . . Note=Loss of function. N->S%2CP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8404866;Dbxref=PMID:8404866 +P34167 UniProtKB Mutagenesis 150 150 . . . Note=Retention of function. A->S%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8404866;Dbxref=PMID:8404866 +P34167 UniProtKB Mutagenesis 150 150 . . . Note=Loss of function. A->Y%2CF%2CN%2CL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8404866;Dbxref=PMID:8404866 +##sequence-region P38431 1 405 +P38431 UniProtKB Chain 1 405 . . . ID=PRO_0000007791;Note=Eukaryotic translation initiation factor 5 +P38431 UniProtKB Domain 241 402 . . . Note=W2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00695 +P38431 UniProtKB Nucleotide binding 27 34 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38431 UniProtKB Compositional bias 152 156 . . . Note=Poly-Lys +P38431 UniProtKB Compositional bias 396 405 . . . Note=Asp/Glu-rich (acidic) +P38431 UniProtKB Modified residue 170 170 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38431 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38431 UniProtKB Modified residue 191 191 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38431 UniProtKB Modified residue 228 228 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38431 UniProtKB Modified residue 317 317 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38431 UniProtKB Modified residue 397 397 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38431 UniProtKB Alternative sequence 1 17 . . . ID=VSP_018724;Note=In isoform Short. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38431 UniProtKB Mutagenesis 343 364 . . . Note=In TIF5-12A%3B Abolishes binding to SUI3 and NIP1. LPKILVQLYNNDIISEEEIMRF->APKAAVQAANNDAASAAEAARA +P38431 UniProtKB Mutagenesis 388 398 . . . Note=In TIF5-7A%3B Abolishes binding to SUI3 and NIP1. FITWLETAESD->AATAAETAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10075937;Dbxref=PMID:10075937 +P38431 UniProtKB Helix 244 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL +P38431 UniProtKB Helix 269 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL +P38431 UniProtKB Helix 287 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL +P38431 UniProtKB Helix 300 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL +P38431 UniProtKB Helix 308 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL +P38431 UniProtKB Helix 318 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL +P38431 UniProtKB Helix 337 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL +P38431 UniProtKB Helix 343 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL +P38431 UniProtKB Helix 358 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL +P38431 UniProtKB Beta strand 370 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL +P38431 UniProtKB Helix 375 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL +P38431 UniProtKB Helix 386 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FUL +##sequence-region P53897 1 168 +P53897 UniProtKB Chain 1 168 . . . ID=PRO_0000203416;Note=mRNA stability protein IGO1 +P53897 UniProtKB Compositional bias 155 160 . . . Note=Poly-Ser +P53897 UniProtKB Modified residue 32 32 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53897 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:20471941;Dbxref=PMID:17330950,PMID:19779198,PMID:20471941 +##sequence-region P50094 1 524 +P50094 UniProtKB Chain 1 524 . . . ID=PRO_0000093684;Note=Inosine-5'-monophosphate dehydrogenase 4 +P50094 UniProtKB Domain 122 183 . . . Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50094 UniProtKB Domain 185 241 . . . Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50094 UniProtKB Nucleotide binding 279 281 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50094 UniProtKB Nucleotide binding 329 331 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50094 UniProtKB Region 369 371 . . . Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50094 UniProtKB Region 392 393 . . . Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50094 UniProtKB Region 416 420 . . . Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50094 UniProtKB Active site 336 336 . . . Note=Thioimidate intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50094 UniProtKB Active site 438 438 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50094 UniProtKB Metal binding 331 331 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50094 UniProtKB Metal binding 333 333 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50094 UniProtKB Metal binding 336 336 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50094 UniProtKB Metal binding 509 509 . . . Note=Potassium%3B via carbonyl oxygen%3B shared with tetrameric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50094 UniProtKB Metal binding 510 510 . . . Note=Potassium%3B via carbonyl oxygen%3B shared with tetrameric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50094 UniProtKB Metal binding 511 511 . . . Note=Potassium%3B via carbonyl oxygen%3B shared with tetrameric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50094 UniProtKB Binding site 334 334 . . . Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50094 UniProtKB Binding site 450 450 . . . Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P50094 UniProtKB Modified residue 125 125 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q06704 1 911 +Q06704 UniProtKB Chain 1 911 . . . ID=PRO_0000240370;Note=Golgin IMH1 +Q06704 UniProtKB Domain 861 909 . . . Note=GRIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00250 +Q06704 UniProtKB Coiled coil 101 280 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06704 UniProtKB Coiled coil 312 735 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06704 UniProtKB Coiled coil 766 814 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06704 UniProtKB Modified residue 308 308 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06704 UniProtKB Modified residue 660 660 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06704 UniProtKB Modified residue 827 827 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198 +Q06704 UniProtKB Modified residue 830 830 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06704 UniProtKB Mutagenesis 870 870 . . . Note=Impairs interaction with ARL1 and Golgi localization. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12620189;Dbxref=PMID:12620189 +##sequence-region P47031 1 731 +P47031 UniProtKB Chain 1 731 . . . ID=PRO_0000203051;Note=Mitochondrial outer membrane protein IML2 +P47031 UniProtKB Transmembrane 297 317 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47031 UniProtKB Transmembrane 339 359 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47031 UniProtKB Modified residue 265 265 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P47031 UniProtKB Modified residue 268 268 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P47031 UniProtKB Modified residue 378 378 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36114 +P47031 UniProtKB Modified residue 380 380 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47031 UniProtKB Modified residue 383 383 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P47031 UniProtKB Modified residue 392 392 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P32351 1 346 +P32351 UniProtKB Chain 1 346 . . . ID=PRO_0000084187;Note=Sugar utilization regulatory protein IMP2 +P32351 UniProtKB Modified residue 24 24 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P32351 UniProtKB Sequence conflict 181 181 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32351 UniProtKB Sequence conflict 279 279 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32351 UniProtKB Sequence conflict 282 282 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P11986 1 533 +P11986 UniProtKB Chain 1 533 . . . ID=PRO_0000195185;Note=Inositol-3-phosphate synthase +P11986 UniProtKB Modified residue 368 368 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P11986 UniProtKB Sequence conflict 14 14 . . . Note=V->RL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11986 UniProtKB Sequence conflict 14 14 . . . Note=V->RL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11986 UniProtKB Sequence conflict 60 60 . . . Note=L->FE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11986 UniProtKB Sequence conflict 60 60 . . . Note=L->FE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11986 UniProtKB Sequence conflict 66 93 . . . Note=LGIMLIGLGGNNGSTLVASVLANKHNVE->TRNYAHWVRWLQQWLTLWPRYWRISTMWS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11986 UniProtKB Sequence conflict 66 93 . . . Note=LGIMLIGLGGNNGSTLVASVLANKHNVE->TRNYAHWVRWLQQWLTLWPRYWRISTMWS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11986 UniProtKB Sequence conflict 98 98 . . . Note=E->AK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11986 UniProtKB Sequence conflict 98 98 . . . Note=E->AK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11986 UniProtKB Sequence conflict 140 141 . . . Note=ND->KH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11986 UniProtKB Sequence conflict 140 141 . . . Note=ND->KH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11986 UniProtKB Sequence conflict 201 201 . . . Note=N->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11986 UniProtKB Sequence conflict 201 201 . . . Note=N->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11986 UniProtKB Sequence conflict 444 444 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11986 UniProtKB Sequence conflict 444 444 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11986 UniProtKB Sequence conflict 476 497 . . . Note=NFYPVLTFLSYWLKAPLTRPGF->ELLSSFNLLELLVKSSINKNQDL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11986 UniProtKB Sequence conflict 524 533 . . . Note=NELRFEERLL->KRTKIRREIVVISFQRLSFSFSAYL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11986 UniProtKB Beta strand 11 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 19 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 25 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 43 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 64 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Turn 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 76 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 94 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 99 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 109 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 114 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1H +P11986 UniProtKB Beta strand 125 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 130 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 139 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 142 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 154 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 166 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 193 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JKI +P11986 UniProtKB Helix 216 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 239 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Turn 255 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 258 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 261 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 277 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 292 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 296 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1H +P11986 UniProtKB Helix 303 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 316 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 325 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 342 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 355 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 363 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 378 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Turn 385 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Turn 390 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 397 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 406 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 411 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 423 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 427 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 438 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 459 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 466 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1H +P11986 UniProtKB Helix 482 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Beta strand 488 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 503 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +P11986 UniProtKB Helix 528 531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P1J +##sequence-region P13902 1 151 +P13902 UniProtKB Chain 1 151 . . . ID=PRO_0000127254;Note=Protein INO4 +P13902 UniProtKB Domain 45 97 . . . Note=bHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981 +##sequence-region P53115 1 1489 +P53115 UniProtKB Chain 1 1489 . . . ID=PRO_0000074329;Note=Putative DNA helicase INO80 +P53115 UniProtKB Domain 476 601 . . . Note=DBINO;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00746 +P53115 UniProtKB Domain 718 890 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P53115 UniProtKB Domain 1303 1467 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P53115 UniProtKB Nucleotide binding 731 738 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P53115 UniProtKB Motif 841 844 . . . Note=DEAQ box +P53115 UniProtKB Compositional bias 188 193 . . . Note=Poly-Ala +P53115 UniProtKB Compositional bias 259 268 . . . Note=Poly-Glu +P53115 UniProtKB Compositional bias 300 306 . . . Note=Poly-Ser +P53115 UniProtKB Compositional bias 568 573 . . . Note=Poly-Glu +P53115 UniProtKB Compositional bias 675 682 . . . Note=Poly-Glu +P53115 UniProtKB Modified residue 65 65 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53115 UniProtKB Modified residue 115 115 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53115 UniProtKB Modified residue 133 133 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53115 UniProtKB Modified residue 610 610 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53115 UniProtKB Mutagenesis 737 737 . . . Note=Reduced ATPase activity of the INO80 complex. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10952318;Dbxref=PMID:10952318 +##sequence-region Q08227 1 384 +Q08227 UniProtKB Chain 1 384 . . . ID=PRO_0000268682;Note=Phosphatidylinositol 4%2C5-bisphosphate 5-phosphatase INP54 +##sequence-region P40015 1 477 +P40015 UniProtKB Chain 1 477 . . . ID=PRO_0000075695;Note=Inositol phosphosphingolipids phospholipase C +P40015 UniProtKB Topological domain 1 398 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40015 UniProtKB Transmembrane 399 417 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40015 UniProtKB Topological domain 418 424 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40015 UniProtKB Transmembrane 425 449 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40015 UniProtKB Topological domain 450 477 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40015 UniProtKB Active site 334 334 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40015 UniProtKB Metal binding 100 100 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40015 UniProtKB Site 233 233 . . . Note=Important for substrate recognition;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q12479 1 156 +Q12479 UniProtKB Chain 1 156 . . . ID=PRO_0000299700;Note=Putative increased recombination centers protein 11 +Q12479 UniProtKB Transmembrane 20 42 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07843 1 230 +Q07843 UniProtKB Chain 1 230 . . . ID=PRO_0000247128;Note=Increased recombination centers protein 19 +##sequence-region Q08416 1 157 +Q08416 UniProtKB Chain 1 157 . . . ID=PRO_0000237647;Note=Increased recombination centers protein 23 +Q08416 UniProtKB Topological domain 1 6 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08416 UniProtKB Transmembrane 7 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08416 UniProtKB Topological domain 30 33 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08416 UniProtKB Transmembrane 34 56 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08416 UniProtKB Topological domain 57 157 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06683 1 689 +Q06683 UniProtKB Chain 1 689 . . . ID=PRO_0000253816;Note=Putative ATP-dependent helicase IRC3 +Q06683 UniProtKB Domain 46 211 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q06683 UniProtKB Domain 265 438 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q06683 UniProtKB Nucleotide binding 59 66 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q06683 UniProtKB Motif 158 161 . . . Note=DEAH box +##sequence-region Q07821 1 250 +Q07821 UniProtKB Chain 1 250 . . . ID=PRO_0000077034;Note=Iron-sulfur assembly protein 1 +Q07821 UniProtKB Metal binding 178 178 . . . Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AAC8 +Q07821 UniProtKB Metal binding 242 242 . . . Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AAC8 +Q07821 UniProtKB Metal binding 244 244 . . . Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AAC8 +##sequence-region P32645 1 267 +P32645 UniProtKB Chain 1 267 . . . ID=PRO_0000084242;Note=Meiosis-specific protein ISC10 +##sequence-region P53193 1 184 +P53193 UniProtKB Transit peptide 1 10 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171977;Dbxref=PMID:11171977 +P53193 UniProtKB Chain 11 184 . . . ID=PRO_0000071163;Note=J-type co-chaperone JAC1%2C mitochondrial +P53193 UniProtKB Domain 13 82 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +P53193 UniProtKB Region 71 184 . . . Note=Interaction with ISU1 +P53193 UniProtKB Mutagenesis 32 32 . . . Note=In JAC1-1%3B temperature sensitive%3B causes growth defect at high temperatures. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9813017;Dbxref=PMID:9813017 +P53193 UniProtKB Mutagenesis 48 50 . . . Note=In JAC1-A3%3B temperature sensitive%3B causes growth defect at high temperatures. HPD->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171977;Dbxref=PMID:11171977 +P53193 UniProtKB Mutagenesis 104 117 . . . Note=In JAC1(LKDDEQ)%3B impairs interaction with ISU1%2C but does not affect stimulation of SSQ1 ATPase activity. LLLKVLDIHDELSQ->ALLAVLAIHAALSA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16551614;Dbxref=PMID:16551614 +P53193 UniProtKB Helix 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3 +P53193 UniProtKB Turn 19 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3 +P53193 UniProtKB Helix 33 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3 +P53193 UniProtKB Helix 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3 +P53193 UniProtKB Helix 62 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3 +P53193 UniProtKB Helix 72 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3 +P53193 UniProtKB Helix 91 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3 +P53193 UniProtKB Helix 102 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3 +P53193 UniProtKB Helix 121 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3 +P53193 UniProtKB Helix 151 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UO3 +##sequence-region P47156 1 728 +P47156 UniProtKB Chain 1 728 . . . ID=PRO_0000203116;Note=Histone demethylase JHD2 +P47156 UniProtKB Domain 4 47 . . . Note=JmjN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00537 +P47156 UniProtKB Domain 381 549 . . . Note=JmjC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00538 +P47156 UniProtKB Zinc finger 235 285 . . . Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 +P47156 UniProtKB Metal binding 427 427 . . . Note=Iron%3B catalytic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47156 UniProtKB Metal binding 430 430 . . . Note=Iron%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00538 +P47156 UniProtKB Metal binding 517 517 . . . Note=Iron%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00538 +P47156 UniProtKB Mutagenesis 427 427 . . . Note=Abolishes enzymatic activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17310255;Dbxref=PMID:17310255 +##sequence-region O13555 1 125 +O13555 UniProtKB Chain 1 125 . . . ID=PRO_0000299775;Note=Uncharacterized protein JIP3 +O13555 UniProtKB Compositional bias 2 91 . . . Note=Glu-rich +##sequence-region P07278 1 416 +P07278 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1339314,ECO:0000269|PubMed:3037314,ECO:0000269|PubMed:6243658;Dbxref=PMID:1339314,PMID:3037314,PMID:6243658 +P07278 UniProtKB Chain 2 416 . . . ID=PRO_0000205418;Note=cAMP-dependent protein kinase regulatory subunit +P07278 UniProtKB Nucleotide binding 184 301 . . . Note=cAMP 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21070946;Dbxref=PMID:21070946 +P07278 UniProtKB Nucleotide binding 302 416 . . . Note=cAMP 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21070946;Dbxref=PMID:21070946 +P07278 UniProtKB Region 2 183 . . . Note=Dimerization and phosphorylation +P07278 UniProtKB Region 8 45 . . . Note=Dimerization/docking domain (D/D) +P07278 UniProtKB Motif 142 146 . . . Note=Inhibitor sequence (IS) +P07278 UniProtKB Binding site 249 249 . . . Note=cAMP 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21070946;Dbxref=PMID:21070946 +P07278 UniProtKB Binding site 258 258 . . . Note=cAMP 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21070946;Dbxref=PMID:21070946 +P07278 UniProtKB Binding site 368 368 . . . Note=cAMP 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21070946;Dbxref=PMID:21070946 +P07278 UniProtKB Binding site 377 377 . . . Note=cAMP 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21070946;Dbxref=PMID:21070946 +P07278 UniProtKB Modified residue 3 3 . . . Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07278 UniProtKB Modified residue 4 4 . . . Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07278 UniProtKB Modified residue 9 9 . . . Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07278 UniProtKB Modified residue 68 68 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584 +P07278 UniProtKB Modified residue 70 70 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584 +P07278 UniProtKB Modified residue 74 74 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584 +P07278 UniProtKB Modified residue 77 77 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584 +P07278 UniProtKB Modified residue 79 79 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584 +P07278 UniProtKB Modified residue 81 81 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584 +P07278 UniProtKB Modified residue 83 83 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:20702584;Dbxref=PMID:19779198,PMID:20702584 +P07278 UniProtKB Modified residue 84 84 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584 +P07278 UniProtKB Modified residue 129 129 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584 +P07278 UniProtKB Modified residue 130 130 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584 +P07278 UniProtKB Modified residue 131 131 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584 +P07278 UniProtKB Modified residue 144 144 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584 +P07278 UniProtKB Modified residue 145 145 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:20702584,ECO:0000269|PubMed:3037314;Dbxref=PMID:18407956,PMID:19779198,PMID:20702584,PMID:3037314 +P07278 UniProtKB Modified residue 147 147 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584 +P07278 UniProtKB Modified residue 150 150 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:20702584;Dbxref=PMID:19779198,PMID:20702584 +P07278 UniProtKB Modified residue 160 160 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584 +P07278 UniProtKB Mutagenesis 129 129 . . . Note=Confers increased sensitivity to rapamycin and enhanced accumulation of glycogen upon TORC1 inhibition. T->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20702584;Dbxref=PMID:20702584 +P07278 UniProtKB Sequence conflict 264 264 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07278 UniProtKB Helix 173 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Turn 183 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Helix 190 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Beta strand 201 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Beta strand 210 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Beta strand 220 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Beta strand 229 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Beta strand 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Helix 249 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Beta strand 259 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Beta strand 268 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Helix 275 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Turn 281 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Helix 288 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Helix 294 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Helix 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Helix 308 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Beta strand 319 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Beta strand 328 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Beta strand 338 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Beta strand 346 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Turn 352 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Beta strand 355 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Helix 368 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Beta strand 378 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Beta strand 387 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Helix 394 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Turn 402 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +P07278 UniProtKB Helix 405 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF1 +##sequence-region P23292 1 546 +P23292 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P23292 UniProtKB Chain 2 546 . . . ID=PRO_0000192857;Note=Casein kinase I homolog 2 +P23292 UniProtKB Domain 76 360 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P23292 UniProtKB Nucleotide binding 82 90 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P23292 UniProtKB Active site 195 195 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P23292 UniProtKB Binding site 105 105 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P23292 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P23292 UniProtKB Modified residue 455 455 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P23292 UniProtKB Lipidation 545 545 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12370247,ECO:0000269|PubMed:15105419;Dbxref=PMID:12370247,PMID:15105419 +P23292 UniProtKB Lipidation 546 546 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12370247,ECO:0000269|PubMed:15105419;Dbxref=PMID:12370247,PMID:15105419 +P23292 UniProtKB Cross-link 465 465 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P23292 UniProtKB Mutagenesis 545 545 . . . Note=Impaired palmitoylation and plasma membrane localization. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15105419;Dbxref=PMID:15105419 +P23292 UniProtKB Mutagenesis 546 546 . . . Note=Impaired palmitoylation and plasma membrane localization. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15105419;Dbxref=PMID:15105419 +##sequence-region P19158 1 3079 +P19158 UniProtKB Chain 1 3079 . . . ID=PRO_0000056658;Note=Inhibitory regulator protein IRA2 +P19158 UniProtKB Domain 1701 1890 . . . Note=Ras-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00167 +P19158 UniProtKB Compositional bias 399 409 . . . Note=Poly-Ser +P19158 UniProtKB Compositional bias 412 416 . . . Note=Poly-Ser +P19158 UniProtKB Compositional bias 520 528 . . . Note=Poly-Ala +P19158 UniProtKB Compositional bias 2469 2472 . . . Note=Poly-Leu +P19158 UniProtKB Modified residue 635 635 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P19158 UniProtKB Sequence conflict 2309 2309 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19158 UniProtKB Sequence conflict 2317 2317 . . . Note=K->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12056 1 156 +Q12056 UniProtKB Transit peptide 1 26 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12056 UniProtKB Chain 27 156 . . . ID=PRO_0000019701;Note=Iron sulfur cluster assembly protein 2%2C mitochondrial +##sequence-region P47119 1 197 +P47119 UniProtKB Chain 1 197 . . . ID=PRO_0000178279;Note=Inosine triphosphate pyrophosphatase +P47119 UniProtKB Region 10 15 . . . Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03148 +P47119 UniProtKB Region 76 77 . . . Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03148 +P47119 UniProtKB Region 151 154 . . . Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03148 +P47119 UniProtKB Region 180 181 . . . Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03148 +P47119 UniProtKB Metal binding 45 45 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03148 +P47119 UniProtKB Metal binding 76 76 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03148 +P47119 UniProtKB Binding site 58 58 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03148 +P47119 UniProtKB Binding site 175 175 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03148 +##sequence-region P30605 1 584 +P30605 UniProtKB Chain 1 584 . . . ID=PRO_0000050455;Note=Myo-inositol transporter 1 +P30605 UniProtKB Topological domain 1 81 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Transmembrane 82 102 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Topological domain 103 129 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Transmembrane 130 150 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Topological domain 151 163 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Transmembrane 164 184 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Topological domain 185 186 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Transmembrane 187 207 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Topological domain 208 215 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Transmembrane 216 236 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Topological domain 237 246 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Transmembrane 247 267 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Topological domain 268 349 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Transmembrane 350 370 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Topological domain 371 376 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Transmembrane 377 397 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Topological domain 398 400 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Transmembrane 401 421 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Topological domain 422 441 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Transmembrane 442 462 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Topological domain 463 486 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Transmembrane 487 507 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Topological domain 508 510 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Transmembrane 511 531 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Topological domain 532 584 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Modified residue 12 12 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P30605 UniProtKB Modified residue 26 26 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P30605 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P30605 UniProtKB Modified residue 35 35 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P30605 UniProtKB Modified residue 37 37 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P30605 UniProtKB Modified residue 46 46 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198 +P30605 UniProtKB Glycosylation 371 371 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30605 UniProtKB Cross-link 573 573 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P30605 UniProtKB Sequence conflict 43 44 . . . Note=TL->HI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07959 1 543 +Q07959 UniProtKB Chain 1 543 . . . ID=PRO_0000240375;Note=ADIPOR-like receptor IZH3 +Q07959 UniProtKB Topological domain 1 259 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Transmembrane 260 280 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Topological domain 281 295 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Transmembrane 296 316 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Topological domain 317 330 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Transmembrane 331 353 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Topological domain 354 357 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Transmembrane 358 378 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Topological domain 379 395 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Transmembrane 396 416 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Topological domain 417 425 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Transmembrane 426 446 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Topological domain 447 505 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Transmembrane 506 526 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Topological domain 527 543 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Compositional bias 125 150 . . . Note=Ser-rich +Q07959 UniProtKB Glycosylation 45 45 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Glycosylation 123 123 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Glycosylation 153 153 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Glycosylation 256 256 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07959 UniProtKB Glycosylation 319 319 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40034 1 492 +P40034 UniProtKB Chain 1 492 . . . ID=PRO_0000202630;Note=JmjC domain-containing histone demethylation protein 1 +P40034 UniProtKB Domain 254 409 . . . Note=JmjC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00538 +P40034 UniProtKB Zinc finger 4 72 . . . Note=PHD-type%3B atypical +P40034 UniProtKB Metal binding 305 305 . . . Note=Iron%3B catalytic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40034 UniProtKB Metal binding 307 307 . . . Note=Iron%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00538 +P40034 UniProtKB Metal binding 377 377 . . . Note=Iron%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00538 +P40034 UniProtKB Binding site 302 302 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40034 UniProtKB Binding site 322 322 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40034 UniProtKB Mutagenesis 305 305 . . . Note=Abolishes histone demethylase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16362057;Dbxref=PMID:16362057 +##sequence-region P53863 1 590 +P53863 UniProtKB Chain 1 590 . . . ID=PRO_0000071162;Note=J protein JJJ1 +P53863 UniProtKB Domain 3 72 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +P53863 UniProtKB Zinc finger 338 362 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P53863 UniProtKB Zinc finger 549 573 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P53863 UniProtKB Modified residue 393 393 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53863 UniProtKB Modified residue 504 504 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P32767 1 1081 +P32767 UniProtKB Chain 1 1081 . . . ID=PRO_0000058276;Note=Importin beta-like protein KAP122 +##sequence-region P22517 1 447 +P22517 UniProtKB Chain 1 447 . . . ID=PRO_0000086105;Note=Calcium/calmodulin-dependent protein kinase II +P22517 UniProtKB Domain 47 309 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P22517 UniProtKB Nucleotide binding 53 61 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P22517 UniProtKB Region 323 334 . . . Note=Calmodulin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22517 UniProtKB Active site 171 171 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P22517 UniProtKB Binding site 76 76 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P22517 UniProtKB Modified residue 316 316 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22517 UniProtKB Modified residue 353 353 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P22517 UniProtKB Modified residue 354 354 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P22517 UniProtKB Modified residue 367 367 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P22517 UniProtKB Modified residue 371 371 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P22517 UniProtKB Modified residue 387 387 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22517 UniProtKB Modified residue 443 443 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P22517 UniProtKB Sequence conflict 282 282 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12494 1 1050 +Q12494 UniProtKB Chain 1 1050 . . . ID=PRO_0000255955;Note=Inositol hexakisphosphate kinase 1 +Q12494 UniProtKB Region 772 780 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12494 UniProtKB Modified residue 150 150 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12494 UniProtKB Modified residue 396 396 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12494 UniProtKB Modified residue 469 469 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12494 UniProtKB Modified residue 537 537 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198 +Q12494 UniProtKB Modified residue 539 539 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12494 UniProtKB Modified residue 566 566 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q12494 UniProtKB Modified residue 583 583 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12494 UniProtKB Modified residue 589 589 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q12494 UniProtKB Modified residue 646 646 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12494 UniProtKB Modified residue 664 664 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12494 UniProtKB Modified residue 670 670 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q08295 1 589 +Q08295 UniProtKB Chain 1 589 . . . ID=PRO_0000245259;Note=Oligo-1%2C6-glucosidase IMA2 +Q08295 UniProtKB Active site 215 215 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08295 UniProtKB Active site 277 277 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08295 UniProtKB Site 352 352 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P40884 1 581 +P40884 UniProtKB Chain 1 581 . . . ID=PRO_0000054331;Note=Oligo-1%2C6-glucosidase IMA5 +P40884 UniProtKB Active site 210 210 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40884 UniProtKB Active site 272 272 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40884 UniProtKB Site 347 347 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q06142 1 861 +Q06142 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q06142 UniProtKB Chain 2 861 . . . ID=PRO_0000120764;Note=Importin subunit beta-1 +Q06142 UniProtKB Repeat 3 35 . . . Note=HEAT 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Domain 25 106 . . . Note=Importin N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00115 +Q06142 UniProtKB Repeat 37 66 . . . Note=HEAT 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Repeat 90 129 . . . Note=HEAT 3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Repeat 134 164 . . . Note=HEAT 4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Repeat 177 208 . . . Note=HEAT 5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Repeat 219 255 . . . Note=HEAT 6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Repeat 260 306 . . . Note=HEAT 7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Repeat 317 362 . . . Note=HEAT 8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Repeat 367 395 . . . Note=HEAT 9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Repeat 402 442 . . . Note=HEAT 10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Repeat 452 484 . . . Note=HEAT 11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Repeat 496 530 . . . Note=HEAT 12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Repeat 536 586 . . . Note=HEAT 13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Repeat 592 629 . . . Note=HEAT 14;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Repeat 634 669 . . . Note=HEAT 15;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Repeat 675 713 . . . Note=HEAT 16;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Repeat 718 764 . . . Note=HEAT 17;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Repeat 773 812 . . . Note=HEAT 18;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Repeat 819 859 . . . Note=HEAT 19;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15878174;Dbxref=PMID:15878174 +Q06142 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q06142 UniProtKB Modified residue 836 836 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06142 UniProtKB Helix 3 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 19 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 37 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 55 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Turn 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 74 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 90 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 109 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 134 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 149 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Beta strand 166 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EA5 +Q06142 UniProtKB Helix 174 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 177 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 195 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 209 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 213 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 219 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 238 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 256 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 260 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 267 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 280 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 317 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 346 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 363 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 367 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 383 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Beta strand 397 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 402 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 419 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 425 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 443 445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Turn 448 451 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 452 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 467 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Beta strand 485 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 491 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 496 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Beta strand 509 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ND2 +Q06142 UniProtKB Helix 513 515 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 516 530 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 533 535 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 536 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 558 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 563 586 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 588 590 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 592 594 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 595 607 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Beta strand 608 610 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EA5 +Q06142 UniProtKB Helix 611 613 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 615 629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 630 633 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 634 649 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 654 669 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 671 674 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 675 690 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 698 713 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 714 717 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 718 732 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Beta strand 737 740 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 741 764 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Turn 765 767 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 769 772 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 773 775 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 776 788 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 790 793 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 796 812 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Beta strand 816 818 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BKU +Q06142 UniProtKB Helix 819 821 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 825 836 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Beta strand 838 840 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +Q06142 UniProtKB Helix 842 859 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPT +##sequence-region P32337 1 1089 +P32337 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32337 UniProtKB Chain 2 1089 . . . ID=PRO_0000120774;Note=Importin subunit beta-3 +P32337 UniProtKB Repeat 6 39 . . . Note=HEAT 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 44 78 . . . Note=HEAT 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 96 129 . . . Note=HEAT 3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 138 165 . . . Note=HEAT 4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 175 207 . . . Note=HEAT 5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 216 252 . . . Note=HEAT 6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 260 295 . . . Note=HEAT 7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 304 359 . . . Note=HEAT 8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 361 395 . . . Note=HEAT 9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 399 439 . . . Note=HEAT 10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 441 481 . . . Note=HEAT 11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 484 524 . . . Note=HEAT 12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 526 568 . . . Note=HEAT 13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 571 613 . . . Note=HEAT 14;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 615 689 . . . Note=HEAT 15;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 692 735 . . . Note=HEAT 16;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 742 781 . . . Note=HEAT 17;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 788 849 . . . Note=HEAT 18;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 852 890 . . . Note=HEAT 19;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 898 930 . . . Note=HEAT 20;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 938 978 . . . Note=HEAT 21;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 986 1017 . . . Note=HEAT 22;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 1028 1063 . . . Note=HEAT 23;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Repeat 1066 1089 . . . Note=HEAT 24;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23541588;Dbxref=PMID:23541588 +P32337 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32337 UniProtKB Modified residue 830 830 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32337 UniProtKB Sequence conflict 65 65 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32337 UniProtKB Sequence conflict 65 65 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32337 UniProtKB Sequence conflict 1077 1077 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32337 UniProtKB Sequence conflict 1077 1077 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32337 UniProtKB Helix 6 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 25 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Beta strand 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZJ7 +P32337 UniProtKB Turn 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 44 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 61 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 96 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 116 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Beta strand 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H2V +P32337 UniProtKB Helix 138 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 153 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 168 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 175 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 191 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 210 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 217 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 220 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 228 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 236 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 254 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 261 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 279 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 297 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 304 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 329 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 343 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 361 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 381 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Turn 395 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 399 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 406 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 414 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 422 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Turn 439 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 442 458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 465 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 484 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 488 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 491 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 507 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 525 531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 532 544 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 551 568 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 570 573 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Turn 574 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 577 588 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 597 613 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 614 620 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 621 632 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Beta strand 638 641 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Beta strand 646 648 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 649 651 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Beta strand 655 668 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 669 689 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 690 693 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 694 703 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 705 709 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 715 734 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 742 757 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Turn 758 760 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 764 781 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 788 809 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 829 849 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Turn 850 853 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 854 857 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 858 860 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 861 868 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Beta strand 870 872 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H2V +P32337 UniProtKB Helix 873 887 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 891 893 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3U +P32337 UniProtKB Helix 895 909 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 914 930 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Turn 933 935 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 936 949 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 958 960 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 961 977 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Turn 978 980 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 987 993 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 1002 1013 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Beta strand 1023 1027 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H2V +P32337 UniProtKB Helix 1029 1041 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 1053 1062 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 1066 1071 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 1072 1075 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +P32337 UniProtKB Helix 1078 1085 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3W3W +##sequence-region P53067 1 1004 +P53067 UniProtKB Chain 1 1004 . . . ID=PRO_0000120778;Note=Importin subunit beta-5 +P53067 UniProtKB Domain 21 100 . . . Note=Importin N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00115 +P53067 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P25642 1 146 +P25642 UniProtKB Transit peptide 1 38 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25642 UniProtKB Chain 39 146 . . . ID=PRO_0000030537;Note=54S ribosomal protein IMG2%2C mitochondrial +P25642 UniProtKB Sequence conflict 120 121 . . . Note=SV->LW;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38265 1 245 +P38265 UniProtKB Chain 1 245 . . . ID=PRO_0000084182;Note=Central kinetochore subunit IML3 +P38265 UniProtKB Beta strand 3 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Helix 16 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IT3 +P38265 UniProtKB Helix 21 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Beta strand 31 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Beta strand 46 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Helix 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Beta strand 72 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Beta strand 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Beta strand 85 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Helix 95 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Beta strand 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Helix 118 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Beta strand 130 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Beta strand 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Beta strand 145 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Helix 154 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Beta strand 160 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Helix 167 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Helix 183 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Helix 188 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Turn 200 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Beta strand 205 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Turn 211 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Beta strand 214 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Beta strand 221 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +P38265 UniProtKB Helix 230 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JE3 +##sequence-region P28627 1 190 +P28627 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8132591;Dbxref=PMID:8132591 +P28627 UniProtKB Chain 2 190 . . . ID=PRO_0000109537;Note=Mitochondrial inner membrane protease subunit 1 +P28627 UniProtKB Active site 40 40 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28627 UniProtKB Active site 84 84 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P28627 UniProtKB Mutagenesis 40 40 . . . Note=Abolishes enzymatic activity. S->A%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835 +P28627 UniProtKB Mutagenesis 84 84 . . . Note=Abolishes enzymatic activity. K->H%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835 +P28627 UniProtKB Mutagenesis 85 85 . . . Note=Reduces enzymatic activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835 +P28627 UniProtKB Mutagenesis 88 88 . . . Note=In pet ts2858%3B temperature-sensitive%3B abolishes processing of CYB2 and presence of SOM1 in the IMP complex. G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15118906,ECO:0000269|PubMed:1886606;Dbxref=PMID:15118906,PMID:1886606 +P28627 UniProtKB Mutagenesis 130 130 . . . Note=Abolishes processing of CYB2 and COX2 and presence of SOM1 in the IMP complex. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15118906;Dbxref=PMID:15118906 +P28627 UniProtKB Mutagenesis 131 131 . . . Note=Reduces enzymatic activity. D->E%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835 +P28627 UniProtKB Mutagenesis 131 131 . . . Note=Abolishes enzymatic activity. D->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835 +P28627 UniProtKB Mutagenesis 138 138 . . . Note=Abolishes enzymatic activity. D->N%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10608835;Dbxref=PMID:10608835 +P28627 UniProtKB Sequence conflict 178 178 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P26798 1 304 +P26798 UniProtKB Chain 1 304 . . . ID=PRO_0000127253;Note=Protein INO2 +P26798 UniProtKB Domain 236 290 . . . Note=bHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981 +##sequence-region Q06098 1 443 +Q06098 UniProtKB Chain 1 443 . . . ID=PRO_0000086038;Note=Serine/threonine-protein kinase ISR1 +Q06098 UniProtKB Domain 135 415 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q06098 UniProtKB Nucleotide binding 141 149 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q06098 UniProtKB Active site 280 280 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q06098 UniProtKB Binding site 169 169 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +##sequence-region Q04638 1 464 +Q04638 UniProtKB Chain 1 464 . . . ID=PRO_0000056340;Note=Translation termination inhibitor protein ITT1 +Q04638 UniProtKB Zinc finger 180 232 . . . Note=RING-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +Q04638 UniProtKB Zinc finger 272 338 . . . Note=IBR-type +Q04638 UniProtKB Zinc finger 402 431 . . . Note=RING-type 2%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +Q04638 UniProtKB Active site 415 415 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y4X5 +##sequence-region Q06214 1 492 +Q06214 UniProtKB Chain 1 492 . . . ID=PRO_0000257817;Note=WD repeat-containing protein JIP5 +Q06214 UniProtKB Repeat 127 166 . . . Note=WD 1 +Q06214 UniProtKB Repeat 178 217 . . . Note=WD 2 +Q06214 UniProtKB Repeat 236 274 . . . Note=WD 3 +Q06214 UniProtKB Repeat 276 317 . . . Note=WD 4 +Q06214 UniProtKB Repeat 365 405 . . . Note=WD 5 +Q06214 UniProtKB Compositional bias 449 488 . . . Note=Lys-rich +##sequence-region P40206 1 208 +P40206 UniProtKB Chain 1 208 . . . ID=PRO_0000203301;Note=Protein JLP2 +##sequence-region P47135 1 1091 +P47135 UniProtKB Chain 1 1091 . . . ID=PRO_0000075922;Note=Protein JSN1 +P47135 UniProtKB Domain 340 426 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P47135 UniProtKB Domain 557 913 . . . Note=PUM-HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00318 +P47135 UniProtKB Repeat 617 652 . . . Note=Pumilio 1 +P47135 UniProtKB Repeat 653 689 . . . Note=Pumilio 2 +P47135 UniProtKB Repeat 690 724 . . . Note=Pumilio 3 +P47135 UniProtKB Repeat 725 760 . . . Note=Pumilio 4 +P47135 UniProtKB Repeat 801 837 . . . Note=Pumilio 5 +P47135 UniProtKB Compositional bias 507 510 . . . Note=Poly-Asn +P47135 UniProtKB Compositional bias 515 518 . . . Note=Poly-Asn +P47135 UniProtKB Compositional bias 923 927 . . . Note=Poly-Gln +P47135 UniProtKB Compositional bias 967 970 . . . Note=Poly-Thr +P47135 UniProtKB Compositional bias 1065 1076 . . . Note=Poly-Asn +P47135 UniProtKB Modified residue 129 129 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47135 UniProtKB Modified residue 131 131 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P47135 UniProtKB Modified residue 160 160 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47135 UniProtKB Modified residue 168 168 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47135 UniProtKB Modified residue 913 913 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q02932 1 1032 +Q02932 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q02932 UniProtKB Chain 2 1032 . . . ID=PRO_0000255954;Note=Importin beta-like protein KAP120 +Q02932 UniProtKB Domain 31 103 . . . Note=Importin N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00115 +Q02932 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P36132 1 386 +P36132 UniProtKB Chain 1 386 . . . ID=PRO_0000096989;Note=tRNA N6-adenosine threonylcarbamoyltransferase +P36132 UniProtKB Region 162 166 . . . Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03180 +P36132 UniProtKB Metal binding 141 141 . . . Note=Divalent metal cation;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03180 +P36132 UniProtKB Metal binding 145 145 . . . Note=Divalent metal cation;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03180 +P36132 UniProtKB Metal binding 162 162 . . . Note=Divalent metal cation;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03180 +P36132 UniProtKB Metal binding 344 344 . . . Note=Divalent metal cation;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03180 +P36132 UniProtKB Binding site 194 194 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03180 +P36132 UniProtKB Binding site 209 209 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03180 +P36132 UniProtKB Binding site 213 213 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03180 +P36132 UniProtKB Binding site 315 315 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03180 +##sequence-region P38697 1 523 +P38697 UniProtKB Chain 1 523 . . . ID=PRO_0000093682;Note=Inosine-5'-monophosphate dehydrogenase 2 +P38697 UniProtKB Domain 121 183 . . . Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P38697 UniProtKB Domain 184 240 . . . Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P38697 UniProtKB Nucleotide binding 278 280 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P38697 UniProtKB Nucleotide binding 328 330 . . . Note=NAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P38697 UniProtKB Region 368 370 . . . Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P38697 UniProtKB Region 391 392 . . . Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P38697 UniProtKB Region 415 419 . . . Note=IMP binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P38697 UniProtKB Active site 335 335 . . . Note=Thioimidate intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P38697 UniProtKB Active site 437 437 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P38697 UniProtKB Metal binding 330 330 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P38697 UniProtKB Metal binding 332 332 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P38697 UniProtKB Metal binding 335 335 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P38697 UniProtKB Metal binding 508 508 . . . Note=Potassium%3B via carbonyl oxygen%3B shared with tetrameric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P38697 UniProtKB Metal binding 509 509 . . . Note=Potassium%3B via carbonyl oxygen%3B shared with tetrameric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P38697 UniProtKB Metal binding 510 510 . . . Note=Potassium%3B via carbonyl oxygen%3B shared with tetrameric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P38697 UniProtKB Binding site 333 333 . . . Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P38697 UniProtKB Binding site 449 449 . . . Note=IMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03156 +P38697 UniProtKB Mutagenesis 253 253 . . . Note=Reduces drug-resistance to MPA. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16278936;Dbxref=PMID:16278936 +P38697 UniProtKB Mutagenesis 335 335 . . . Note=Inactivates the proteins ability to provide drug-resistance in vivo. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15292516;Dbxref=PMID:15292516 +##sequence-region P40576 1 216 +P40576 UniProtKB Transit peptide 1 26 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40576 UniProtKB Chain 27 216 . . . ID=PRO_0000203007;Note=Inner membrane assembly complex subunit 22;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40576 UniProtKB Topological domain 27 43 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24942160;Dbxref=PMID:24942160 +P40576 UniProtKB Transmembrane 44 63 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40576 UniProtKB Topological domain 64 216 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:24942160;Dbxref=PMID:24942160 +P40576 UniProtKB Coiled coil 64 93 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08118 1 586 +Q08118 UniProtKB Chain 1 586 . . . ID=PRO_0000245270;Note=Uncharacterized protein IRC10 +##sequence-region Q6B0V8 1 119 +Q6B0V8 UniProtKB Chain 1 119 . . . ID=PRO_0000299816;Note=Putative increased recombination centers protein 16 +Q6B0V8 UniProtKB Transmembrane 53 73 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q6B0V8 UniProtKB Transmembrane 92 112 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43615 1 237 +P43615 UniProtKB Chain 1 237 . . . ID=PRO_0000202696;Note=Increased recombination centers protein 6 +P43615 UniProtKB Beta strand 9 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9 +P43615 UniProtKB Helix 16 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9 +P43615 UniProtKB Helix 19 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9 +P43615 UniProtKB Beta strand 39 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9 +P43615 UniProtKB Beta strand 51 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9 +P43615 UniProtKB Helix 64 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9 +P43615 UniProtKB Helix 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9 +P43615 UniProtKB Helix 77 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9 +P43615 UniProtKB Beta strand 83 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9 +P43615 UniProtKB Helix 92 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9 +P43615 UniProtKB Helix 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9 +P43615 UniProtKB Helix 101 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9 +P43615 UniProtKB Beta strand 113 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9 +P43615 UniProtKB Helix 125 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9 +P43615 UniProtKB Beta strand 138 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9 +P43615 UniProtKB Beta strand 143 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9 +P43615 UniProtKB Helix 165 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UC9 +##sequence-region Q03020 1 165 +Q03020 UniProtKB Transit peptide 1 27 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03020 UniProtKB Chain 28 165 . . . ID=PRO_0000019700;Note=Iron sulfur cluster assembly protein 1%2C mitochondrial +Q03020 UniProtKB Mutagenesis 63 63 . . . Note=In ISU1(LVF/SSS)%3B no growth and abolishes interaction with both JAC1 and NFS1%3B when associated with S-72 and S-94. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10588895;Dbxref=PMID:10588895 +Q03020 UniProtKB Mutagenesis 69 69 . . . Note=Fails to complement an isu1 deletion mutation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10588895;Dbxref=PMID:10588895 +Q03020 UniProtKB Mutagenesis 72 72 . . . Note=In ISU1(LVF/SSS)%3B no growth and abolishes interaction with both JAC1 and NFS1%3B when associated with S-63 and S-94. V->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10588895;Dbxref=PMID:10588895 +Q03020 UniProtKB Mutagenesis 94 94 . . . Note=In ISU1(LVF/SSS)%3B no growth and abolishes interaction with both JAC1 and NFS1%3B when associated with S-63 and S-72. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10588895;Dbxref=PMID:10588895 +Q03020 UniProtKB Mutagenesis 96 96 . . . Note=Fails to complement an isu1 deletion mutation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10588895;Dbxref=PMID:10588895 +Q03020 UniProtKB Mutagenesis 132 132 . . . Note=No growth. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15123690;Dbxref=PMID:15123690 +Q03020 UniProtKB Mutagenesis 133 133 . . . Note=Wild-type growth. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15123690;Dbxref=PMID:15123690 +Q03020 UniProtKB Mutagenesis 134 136 . . . Note=No growth%3B no interaction with frataxin and SSQ1. PVK->AAA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15123690,ECO:0000269|PubMed:25228696;Dbxref=PMID:15123690,PMID:25228696 +Q03020 UniProtKB Mutagenesis 134 134 . . . Note=Slow growth%3B no interaction with SSQ1. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15123690;Dbxref=PMID:15123690 +Q03020 UniProtKB Mutagenesis 135 135 . . . Note=Wild-type growth%3B no interaction with SSQ1. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15123690;Dbxref=PMID:15123690 +Q03020 UniProtKB Mutagenesis 136 136 . . . Note=No growth%3B no interaction with SSQ1. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15123690;Dbxref=PMID:15123690 +Q03020 UniProtKB Mutagenesis 139 139 . . . Note=Fails to complement an isu1 deletion mutation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10588895;Dbxref=PMID:10588895 +##sequence-region P38710 1 295 +P38710 UniProtKB Chain 1 295 . . . ID=PRO_0000142585;Note=Inositol monophosphatase 1 +P38710 UniProtKB Region 94 97 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38710 UniProtKB Metal binding 73 73 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38710 UniProtKB Metal binding 92 92 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38710 UniProtKB Metal binding 92 92 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38710 UniProtKB Metal binding 94 94 . . . Note=Magnesium 1%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38710 UniProtKB Metal binding 95 95 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38710 UniProtKB Metal binding 231 231 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38710 UniProtKB Binding site 73 73 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38710 UniProtKB Binding site 231 231 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P40559 1 946 +P40559 UniProtKB Chain 1 946 . . . ID=PRO_0000209741;Note=Phosphatidylinositol 4%2C5-bisphosphate 5-phosphatase INP51 +P40559 UniProtKB Domain 151 480 . . . Note=SAC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00183 +##sequence-region P01094 1 68 +P01094 UniProtKB Chain 1 68 . . . ID=PRO_0000195901;Note=Protease A inhibitor 3 +P01094 UniProtKB Region 1 32 . . . Note=Inhibitory domain +P01094 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.1 +P01094 UniProtKB Helix 4 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DPJ +##sequence-region P38803 1 334 +P38803 UniProtKB Chain 1 334 . . . ID=PRO_0000202904;Note=Pre-rRNA-processing protein IPI1 +##sequence-region P53877 1 555 +P53877 UniProtKB Chain 1 555 . . . ID=PRO_0000051484;Note=Pre-rRNA-processing protein IPI3 +P53877 UniProtKB Repeat 90 133 . . . Note=WD 1 +P53877 UniProtKB Repeat 137 176 . . . Note=WD 2 +P53877 UniProtKB Repeat 187 234 . . . Note=WD 3 +P53877 UniProtKB Repeat 342 383 . . . Note=WD 4 +P53877 UniProtKB Modified residue 388 388 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P18963 1 3092 +P18963 UniProtKB Chain 1 3092 . . . ID=PRO_0000056657;Note=Inhibitory regulator protein IRA1 +P18963 UniProtKB Domain 1709 1898 . . . Note=Ras-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00167 +P18963 UniProtKB Compositional bias 326 331 . . . Note=Poly-Ser +P18963 UniProtKB Compositional bias 379 383 . . . Note=Poly-Ser +P18963 UniProtKB Compositional bias 475 484 . . . Note=Poly-Asn +P18963 UniProtKB Compositional bias 1433 1437 . . . Note=Poly-Ile +P18963 UniProtKB Compositional bias 2039 2042 . . . Note=Poly-Glu +P18963 UniProtKB Modified residue 497 497 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P18963 UniProtKB Modified residue 915 915 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P18963 UniProtKB Modified residue 1342 1342 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P18963 UniProtKB Modified residue 1753 1753 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18963 UniProtKB Modified residue 3004 3004 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18963 UniProtKB Sequence conflict 361 361 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08522 1 113 +Q08522 UniProtKB Chain 1 113 . . . ID=PRO_0000299715;Note=Putative increased recombination centers protein 14 +##sequence-region P47056 1 224 +P47056 UniProtKB Signal peptide 1 26 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47056 UniProtKB Chain 27 224 . . . ID=PRO_0000203069;Note=Outer spore wall protein 6 +P47056 UniProtKB Topological domain 27 174 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47055 +P47056 UniProtKB Transmembrane 175 195 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47056 UniProtKB Topological domain 196 199 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47055 +P47056 UniProtKB Transmembrane 200 220 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47056 UniProtKB Topological domain 221 224 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47055 +P47056 UniProtKB Glycosylation 74 74 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P47056 UniProtKB Glycosylation 104 104 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +##sequence-region Q12425 1 185 +Q12425 UniProtKB Chain 1 185 . . . ID=PRO_0000077035;Note=Iron-sulfur assembly protein 2 +Q12425 UniProtKB Metal binding 89 89 . . . Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AAC8 +Q12425 UniProtKB Metal binding 175 175 . . . Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AAC8 +Q12425 UniProtKB Metal binding 177 177 . . . Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AAC8 +##sequence-region Q6Q560 1 94 +Q6Q560 UniProtKB Chain 1 94 . . . ID=PRO_0000245364;Note=Protein ISD11 +##sequence-region P21374 1 235 +P21374 UniProtKB Chain 1 235 . . . ID=PRO_0000192976;Note=Pre-mRNA-splicing factor ISY1 +P21374 UniProtKB Helix 4 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P21374 UniProtKB Helix 11 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P21374 UniProtKB Beta strand 29 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P21374 UniProtKB Helix 44 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P21374 UniProtKB Helix 72 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P53125 1 1264 +P53125 UniProtKB Chain 1 1264 . . . ID=PRO_0000084270;Note=Imitation switch two complex protein 1 +P53125 UniProtKB Domain 23 130 . . . Note=WAC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00475 +P53125 UniProtKB Domain 423 483 . . . Note=DDT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00063 +##sequence-region Q06667 1 281 +Q06667 UniProtKB Chain 1 281 . . . ID=PRO_0000110528;Note=Inositol-pentakisphosphate 2-kinase +Q06667 UniProtKB Motif 123 127 . . . Note=EXKPK motif +##sequence-region P00817 1 287 +P00817 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:340461;Dbxref=PMID:340461 +P00817 UniProtKB Chain 2 287 . . . ID=PRO_0000137588;Note=Inorganic pyrophosphatase +P00817 UniProtKB Active site 90 90 . . . Note=Proton donor;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1322842;Dbxref=PMID:1322842 +P00817 UniProtKB Metal binding 116 116 . . . Note=Magnesium 1 +P00817 UniProtKB Metal binding 121 121 . . . Note=Magnesium 1 +P00817 UniProtKB Metal binding 121 121 . . . Note=Magnesium 2 +P00817 UniProtKB Metal binding 153 153 . . . Note=Magnesium 1 +P00817 UniProtKB Binding site 79 79 . . . Note=Diphosphate +P00817 UniProtKB Modified residue 65 65 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P00817 UniProtKB Modified residue 251 251 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950;Dbxref=PMID:15665377,PMID:17330950 +P00817 UniProtKB Modified residue 266 266 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P00817 UniProtKB Modified residue 286 286 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P00817 UniProtKB Cross-link 239 239 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00817 UniProtKB Cross-link 279 279 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00817 UniProtKB Sequence conflict 41 41 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00817 UniProtKB Sequence conflict 72 72 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00817 UniProtKB Sequence conflict 75 75 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00817 UniProtKB Sequence conflict 124 124 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00817 UniProtKB Sequence conflict 137 137 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00817 UniProtKB Sequence conflict 187 187 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00817 UniProtKB Sequence conflict 225 225 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00817 UniProtKB Sequence conflict 267 267 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00817 UniProtKB Beta strand 3 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Beta strand 13 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPP +P00817 UniProtKB Beta strand 17 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Beta strand 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Turn 29 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Beta strand 35 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Turn 39 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Beta strand 43 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Beta strand 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Beta strand 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IK1 +P00817 UniProtKB Beta strand 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Beta strand 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PYP +P00817 UniProtKB Beta strand 91 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Beta strand 106 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Turn 109 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Beta strand 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Beta strand 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IHP +P00817 UniProtKB Beta strand 121 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Beta strand 126 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M38 +P00817 UniProtKB Beta strand 135 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Beta strand 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Beta strand 155 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Beta strand 163 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PYP +P00817 UniProtKB Helix 166 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Helix 172 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Helix 182 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Helix 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Helix 205 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Beta strand 210 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E6A +P00817 UniProtKB Helix 213 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Beta strand 245 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Helix 256 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Turn 259 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Beta strand 266 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +P00817 UniProtKB Helix 275 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E9G +##sequence-region Q12280 1 1495 +Q12280 UniProtKB Chain 1 1495 . . . ID=PRO_0000056652;Note=Ras GTPase-activating-like protein IQG1 +Q12280 UniProtKB Domain 108 217 . . . Note=Calponin-homology (CH);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00044 +Q12280 UniProtKB Domain 447 467 . . . Note=IQ 1 +Q12280 UniProtKB Domain 538 567 . . . Note=IQ 2 +Q12280 UniProtKB Domain 568 597 . . . Note=IQ 3 +Q12280 UniProtKB Domain 599 628 . . . Note=IQ 4 +Q12280 UniProtKB Domain 629 658 . . . Note=IQ 5 +Q12280 UniProtKB Domain 687 716 . . . Note=IQ 6 +Q12280 UniProtKB Domain 717 746 . . . Note=IQ 7 +Q12280 UniProtKB Domain 860 1071 . . . Note=Ras-GAP +Q12280 UniProtKB Coiled coil 759 798 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12280 UniProtKB Compositional bias 37 76 . . . Note=Ser-rich +Q12280 UniProtKB Modified residue 264 264 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12280 UniProtKB Modified residue 268 268 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12280 UniProtKB Modified residue 299 299 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12280 UniProtKB Mutagenesis 457 457 . . . Note=In IQG1-1%3B causes a defect in cytokinesis at 37 degrees Celsius. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11082046;Dbxref=PMID:11082046 +##sequence-region P40006 1 225 +P40006 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40006 UniProtKB Chain 25 225 . . . ID=PRO_0000014315;Note=Increased recombination centers protein 22 +P40006 UniProtKB Topological domain 25 169 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40006 UniProtKB Transmembrane 170 190 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40006 UniProtKB Topological domain 191 225 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32488 1 338 +P32488 UniProtKB Chain 1 338 . . . ID=PRO_0000096272;Note=Increasing suppression factor 1 +P32488 UniProtKB Modified residue 119 119 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P53843 1 298 +P53843 UniProtKB Chain 1 298 . . . ID=PRO_0000076227;Note=Vacuolar protein sorting-associated protein IST1 +P53843 UniProtKB Region 251 298 . . . Note=Interaction with VPS4 +P53843 UniProtKB Motif 286 296 . . . Note=MIT-interacting motif +P53843 UniProtKB Compositional bias 190 196 . . . Note=Poly-Ser +P53843 UniProtKB Helix 8 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY +P53843 UniProtKB Helix 50 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY +P53843 UniProtKB Helix 84 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY +P53843 UniProtKB Helix 93 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY +P53843 UniProtKB Beta strand 100 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY +P53843 UniProtKB Helix 105 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY +P53843 UniProtKB Helix 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY +P53843 UniProtKB Helix 125 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY +P53843 UniProtKB Helix 138 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY +P53843 UniProtKB Helix 153 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY +P53843 UniProtKB Helix 166 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY +P53843 UniProtKB Helix 184 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GGY +##sequence-region Q07532 1 353 +Q07532 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q07532 UniProtKB Chain 2 353 . . . ID=PRO_0000255269;Note=RNA polymerase II nuclear localization protein IWR1 +Q07532 UniProtKB Motif 10 43 . . . Note=Bipartite nuclear localization signal +Q07532 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P33417 1 597 +P33417 UniProtKB Chain 1 597 . . . ID=PRO_0000048573;Note=Intrastrand cross-link recognition protein +P33417 UniProtKB DNA binding 361 429 . . . Note=HMG box 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267 +P33417 UniProtKB DNA binding 434 502 . . . Note=HMG box 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267 +P33417 UniProtKB Compositional bias 52 118 . . . Note=Gln-rich +P33417 UniProtKB Compositional bias 281 336 . . . Note=Gln-rich +P33417 UniProtKB Compositional bias 565 580 . . . Note=Gln-rich +P33417 UniProtKB Modified residue 532 532 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P33417 UniProtKB Sequence conflict 73 73 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33417 UniProtKB Sequence conflict 93 93 . . . Note=Y->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33417 UniProtKB Sequence conflict 114 118 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33417 UniProtKB Sequence conflict 207 207 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33417 UniProtKB Sequence conflict 220 221 . . . Note=AA->TT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12442 1 317 +Q12442 UniProtKB Chain 1 317 . . . ID=PRO_0000218834;Note=ADIPOR-like receptor IZH2 +Q12442 UniProtKB Topological domain 1 78 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12442 UniProtKB Transmembrane 79 99 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12442 UniProtKB Topological domain 100 110 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12442 UniProtKB Transmembrane 111 131 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12442 UniProtKB Topological domain 132 153 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12442 UniProtKB Transmembrane 154 174 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12442 UniProtKB Topological domain 175 176 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12442 UniProtKB Transmembrane 177 197 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12442 UniProtKB Topological domain 198 212 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12442 UniProtKB Transmembrane 213 233 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12442 UniProtKB Topological domain 234 242 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12442 UniProtKB Transmembrane 243 263 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12442 UniProtKB Topological domain 264 276 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12442 UniProtKB Transmembrane 277 297 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12442 UniProtKB Topological domain 298 317 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43596 1 787 +P43596 UniProtKB Chain 1 787 . . . ID=PRO_0000202685;Note=ISWI one complex protein 3 +P43596 UniProtKB Helix 144 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 179 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Turn 192 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Turn 198 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 205 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Beta strand 219 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Beta strand 224 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Beta strand 229 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 238 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 245 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Turn 266 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 284 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 293 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Turn 306 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Turn 313 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Beta strand 326 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Turn 365 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 369 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 373 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 380 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 385 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 404 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 432 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 437 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Turn 454 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 462 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Turn 470 472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 473 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 483 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Turn 491 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 500 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 506 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Beta strand 514 516 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 525 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Turn 529 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Beta strand 539 543 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Turn 544 546 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Beta strand 547 550 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Beta strand 557 559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 569 580 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 586 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 594 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Beta strand 604 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 608 617 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Beta strand 627 629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 634 643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 645 648 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 694 696 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 697 726 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Beta strand 727 729 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Helix 735 739 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +P43596 UniProtKB Turn 740 743 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9Y +##sequence-region P0CT04 1 75 +P0CT04 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:387783;Dbxref=PMID:387783 +P0CT04 UniProtKB Chain 2 75 . . . ID=PRO_0000212790;Note=Protease B inhibitor 2 +P0CT04 UniProtKB Modified residue 74 74 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P0CT04 UniProtKB Sequence conflict 33 33 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P43610 1 853 +P43610 UniProtKB Chain 1 853 . . . ID=PRO_0000074385;Note=Uncharacterized ATP-dependent helicase IRC5 +P43610 UniProtKB Domain 234 401 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P43610 UniProtKB Domain 607 758 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P43610 UniProtKB Nucleotide binding 247 254 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P43610 UniProtKB Coiled coil 548 580 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43610 UniProtKB Motif 352 355 . . . Note=DEGH box +P43610 UniProtKB Compositional bias 41 91 . . . Note=Asp-rich +##sequence-region P36115 1 615 +P36115 UniProtKB Chain 1 615 . . . ID=PRO_0000203199;Note=Increased rDNA silencing protein 4 +P36115 UniProtKB Domain 460 571 . . . Note=EH +P36115 UniProtKB Compositional bias 122 282 . . . Note=Ser-rich +P36115 UniProtKB Modified residue 180 180 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q99312 1 450 +Q99312 UniProtKB Chain 1 450 . . . ID=PRO_0000084257;Note=IMP-specific 5'-nucleotidase 1 +##sequence-region Q12358 1 412 +Q12358 UniProtKB Chain 1 412 . . . ID=PRO_0000194022;Note=Alpha-ketoglutarate-dependent sulfonate dioxygenase +Q12358 UniProtKB Metal binding 218 218 . . . Note=Iron%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12358 UniProtKB Metal binding 220 220 . . . Note=Iron%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12358 UniProtKB Metal binding 367 367 . . . Note=Iron%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12358 UniProtKB Binding site 245 245 . . . Note=2-oxoglutarate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12358 UniProtKB Binding site 352 352 . . . Note=2-oxoglutarate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12358 UniProtKB Binding site 379 379 . . . Note=2-oxoglutarate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12358 UniProtKB Binding site 383 383 . . . Note=2-oxoglutarate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12358 UniProtKB Modified residue 52 52 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P05986 1 398 +P05986 UniProtKB Chain 1 398 . . . ID=PRO_0000086071;Note=cAMP-dependent protein kinase type 3 +P05986 UniProtKB Domain 88 342 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P05986 UniProtKB Domain 343 398 . . . Note=AGC-kinase C-terminal +P05986 UniProtKB Nucleotide binding 94 102 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P05986 UniProtKB Active site 211 211 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P05986 UniProtKB Binding site 117 117 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P05986 UniProtKB Modified residue 15 15 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P05986 UniProtKB Modified residue 55 55 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P05986 UniProtKB Sequence conflict 4 4 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05986 UniProtKB Sequence conflict 208 208 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P11927 1 433 +P11927 UniProtKB Chain 1 433 . . . ID=PRO_0000084295;Note=Cell division control protein KAR1 +P11927 UniProtKB Modified residue 233 233 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P11927 UniProtKB Sequence conflict 95 95 . . . Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11927 UniProtKB Sequence conflict 199 199 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11927 UniProtKB Helix 240 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OQP +##sequence-region P17119 1 729 +P17119 UniProtKB Chain 1 729 . . . ID=PRO_0000125391;Note=Kinesin-like protein KAR3 +P17119 UniProtKB Domain 386 723 . . . Note=Kinesin motor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283 +P17119 UniProtKB Nucleotide binding 474 481 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283 +P17119 UniProtKB Region 1 109 . . . Note=Globular +P17119 UniProtKB Coiled coil 110 357 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17119 UniProtKB Natural variant 378 378 . . . Note=In KAR3-894. N->K +P17119 UniProtKB Natural variant 462 462 . . . Note=In KAR3-891. S->L +P17119 UniProtKB Natural variant 521 521 . . . Note=In KAR3-893. E->D +P17119 UniProtKB Natural variant 550 550 . . . Note=In KAR3-899. R->S +P17119 UniProtKB Natural variant 558 558 . . . Note=In KAR3-8912. T->A +P17119 UniProtKB Natural variant 650 650 . . . Note=In KAR3-898. N->K +P17119 UniProtKB Natural variant 659 659 . . . Note=In KAR3-897. V->L +P17119 UniProtKB Mutagenesis 479 479 . . . Note=Poisons nuclear fusion. G->E +P17119 UniProtKB Helix 348 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ETP +P17119 UniProtKB Beta strand 386 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Turn 398 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Beta strand 406 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Turn 415 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Beta strand 419 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Helix 427 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Beta strand 433 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Helix 448 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Helix 460 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Beta strand 468 473 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Helix 480 485 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Turn 487 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Helix 491 506 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Helix 507 509 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Beta strand 512 523 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Beta strand 526 529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Beta strand 549 552 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Turn 553 556 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Beta strand 557 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Beta strand 566 570 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KAR +P17119 UniProtKB Helix 571 573 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Helix 574 581 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Helix 596 598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Beta strand 599 610 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Turn 612 614 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9U +P17119 UniProtKB Beta strand 617 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Helix 635 637 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Helix 640 663 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Turn 668 670 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ETP +P17119 UniProtKB Helix 675 677 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Helix 679 688 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Beta strand 693 700 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Helix 704 706 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Helix 707 720 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +P17119 UniProtKB Turn 723 725 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F9V +##sequence-region P32526 1 644 +P32526 UniProtKB Chain 1 644 . . . ID=PRO_0000084296;Note=Karyogamy protein KAR9 +P32526 UniProtKB Modified residue 496 496 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32526 UniProtKB Sequence conflict 641 641 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P23291 1 538 +P23291 UniProtKB Chain 1 538 . . . ID=PRO_0000192856;Note=Casein kinase I homolog 1 +P23291 UniProtKB Domain 69 353 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P23291 UniProtKB Nucleotide binding 75 83 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P23291 UniProtKB Active site 188 188 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P23291 UniProtKB Binding site 98 98 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P23291 UniProtKB Modified residue 522 522 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P23291 UniProtKB Modified residue 523 523 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P23291 UniProtKB Modified residue 527 527 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P23291 UniProtKB Lipidation 537 537 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23291 UniProtKB Lipidation 538 538 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23291 UniProtKB Sequence conflict 201 201 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23291 UniProtKB Sequence conflict 367 367 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P15700 1 204 +P15700 UniProtKB Chain 1 204 . . . ID=PRO_0000158947;Note=Uridylate kinase +P15700 UniProtKB Nucleotide binding 26 31 . . . Note=ATP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116 +P15700 UniProtKB Nucleotide binding 74 76 . . . Note=NMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116 +P15700 UniProtKB Nucleotide binding 104 107 . . . Note=NMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116 +P15700 UniProtKB Region 46 76 . . . Note=NMPbind;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116 +P15700 UniProtKB Region 141 151 . . . Note=LID;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116 +P15700 UniProtKB Binding site 52 52 . . . Note=NMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116 +P15700 UniProtKB Binding site 111 111 . . . Note=NMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116 +P15700 UniProtKB Binding site 142 142 . . . Note=ATP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116 +P15700 UniProtKB Binding site 148 148 . . . Note=NMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116 +P15700 UniProtKB Binding site 159 159 . . . Note=NMP;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116 +P15700 UniProtKB Binding site 187 187 . . . Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03172,ECO:0000269|PubMed:7877173,ECO:0000269|PubMed:8107116;Dbxref=PMID:7877173,PMID:8107116 +P15700 UniProtKB Mutagenesis 29 29 . . . Note=Abolishes catalytic activity. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1655742;Dbxref=PMID:1655742 +P15700 UniProtKB Turn 13 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ +P15700 UniProtKB Beta strand 17 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ +P15700 UniProtKB Helix 29 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ +P15700 UniProtKB Beta strand 43 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ +P15700 UniProtKB Helix 47 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ +P15700 UniProtKB Helix 63 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ +P15700 UniProtKB Helix 78 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ +P15700 UniProtKB Beta strand 99 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ +P15700 UniProtKB Helix 109 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ +P15700 UniProtKB Beta strand 123 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ +P15700 UniProtKB Helix 132 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ +P15700 UniProtKB Helix 153 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ +P15700 UniProtKB Helix 168 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ +P15700 UniProtKB Turn 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ +P15700 UniProtKB Beta strand 180 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ +P15700 UniProtKB Helix 189 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UKZ +##sequence-region P43614 1 200 +P43614 UniProtKB Chain 1 200 . . . ID=PRO_0000202695;Note=Beta-1%2C6-glucan synthesis-associated protein KEG1 +P43614 UniProtKB Topological domain 1 15 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43614 UniProtKB Transmembrane 16 36 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43614 UniProtKB Topological domain 37 44 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43614 UniProtKB Transmembrane 45 65 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43614 UniProtKB Topological domain 66 82 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43614 UniProtKB Transmembrane 83 103 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43614 UniProtKB Topological domain 104 145 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43614 UniProtKB Transmembrane 146 166 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43614 UniProtKB Topological domain 167 173 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43614 UniProtKB Transmembrane 174 194 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43614 UniProtKB Topological domain 195 200 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43614 UniProtKB Natural variant 3 3 . . . Note=In strain: KA31a. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17893149;Dbxref=PMID:17893149 +P43614 UniProtKB Natural variant 55 55 . . . Note=In strain: KA31a. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17893149;Dbxref=PMID:17893149 +P43614 UniProtKB Natural variant 84 84 . . . Note=In strain: KA31a. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17893149;Dbxref=PMID:17893149 +P43614 UniProtKB Mutagenesis 124 124 . . . Note=In KEG1-1%3B temperature-sensitive. Increased sensitivity to chitin-binding dye Calcofluor white and zymolyase. Shows K1 killer toxin resistance%2C and reduced content of the cell wall beta-1%2C6-glucan. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17893149;Dbxref=PMID:17893149 +##sequence-region P35844 1 434 +P35844 UniProtKB Chain 1 434 . . . ID=PRO_0000100386;Note=Oxysterol-binding protein homolog 4 +P35844 UniProtKB Region 24 29 . . . Note=Phosphatidylinositol 4-phosphate binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3SPW,ECO:0000269|PubMed:22162133;Dbxref=PMID:22162133 +P35844 UniProtKB Region 109 112 . . . Note=Phosphatidylinositol 4-phosphate binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3SPW,ECO:0000269|PubMed:22162133;Dbxref=PMID:22162133 +P35844 UniProtKB Region 143 144 . . . Note=Phosphatidylinositol 4-phosphate binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3SPW,ECO:0000269|PubMed:22162133;Dbxref=PMID:22162133 +P35844 UniProtKB Binding site 96 96 . . . Note=Sterol;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1ZHT,ECO:0000244|PDB:1ZHW,ECO:0000244|PDB:1ZHX,ECO:0000244|PDB:1ZHY,ECO:0000244|PDB:1ZHZ,ECO:0000244|PDB:4FES,ECO:0000269|PubMed:16136145,ECO:0000269|PubMed:23756172;Dbxref=PMID:16136145,PMID:23756172 +P35844 UniProtKB Binding site 336 336 . . . Note=Phosphatidylinositol 4-phosphate;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3SPW,ECO:0000269|PubMed:22162133;Dbxref=PMID:22162133 +P35844 UniProtKB Binding site 340 340 . . . Note=Phosphatidylinositol 4-phosphate;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3SPW,ECO:0000269|PubMed:22162133;Dbxref=PMID:22162133 +P35844 UniProtKB Binding site 344 344 . . . Note=Phosphatidylinositol 4-phosphate;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:3SPW,ECO:0000269|PubMed:22162133;Dbxref=PMID:22162133 +P35844 UniProtKB Modified residue 370 370 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35844 UniProtKB Modified residue 389 389 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P35844 UniProtKB Mutagenesis 97 97 . . . Note=Abolishes both cholesterol binding and biological function. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16136145;Dbxref=PMID:16136145 +P35844 UniProtKB Mutagenesis 109 109 . . . Note=Strong reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16136145,ECO:0000269|PubMed:22162133;Dbxref=PMID:16136145,PMID:22162133 +P35844 UniProtKB Mutagenesis 111 111 . . . Note=Abolishes both cholesterol binding and biological function. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16136145;Dbxref=PMID:16136145 +P35844 UniProtKB Mutagenesis 112 112 . . . Note=Abolishes binding to phosphatidylinositol 4-phosphate. N->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22162133;Dbxref=PMID:22162133 +P35844 UniProtKB Mutagenesis 117 117 . . . Note=Abolishes both cholesterol binding and biological function. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16136145;Dbxref=PMID:16136145 +P35844 UniProtKB Mutagenesis 143 144 . . . Note=Reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. HH->AA;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16136145,ECO:0000269|PubMed:22162133,ECO:0000269|PubMed:26206936;Dbxref=PMID:16136145,PMID:22162133,PMID:26206936 +P35844 UniProtKB Mutagenesis 168 168 . . . Note=Slight reduction in cholesterol transport. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16136145;Dbxref=PMID:16136145 +P35844 UniProtKB Mutagenesis 168 168 . . . Note=Strong reduction in cholesterol transport. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16136145;Dbxref=PMID:16136145 +P35844 UniProtKB Mutagenesis 202 204 . . . Note=Strong reduction in cholesterol binding without affecting phosphatidylinositol 4-phosphate binding. HIE->AIA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22162133;Dbxref=PMID:22162133 +P35844 UniProtKB Mutagenesis 336 336 . . . Note=Strong reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16136145,ECO:0000269|PubMed:22162133;Dbxref=PMID:16136145,PMID:22162133 +P35844 UniProtKB Mutagenesis 340 340 . . . Note=Abolishes binding to phosphatidylinositol 4-phosphate. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22162133;Dbxref=PMID:22162133 +P35844 UniProtKB Mutagenesis 344 344 . . . Note=Slight reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16136145,ECO:0000269|PubMed:22162133;Dbxref=PMID:16136145,PMID:22162133 +P35844 UniProtKB Sequence conflict 355 355 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35844 UniProtKB Turn 4 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Helix 8 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Turn 16 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Helix 24 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Helix 31 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 34 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Helix 39 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZI7 +P35844 UniProtKB Helix 50 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Helix 55 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Turn 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Helix 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Helix 77 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 118 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Turn 129 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 134 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Turn 143 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 147 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Turn 155 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 159 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 173 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZI7 +P35844 UniProtKB Beta strand 177 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 185 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 192 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 201 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Turn 206 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 212 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 217 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 228 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 236 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 241 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Helix 256 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Helix 260 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 264 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 273 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Helix 283 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 287 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Turn 292 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Helix 305 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Helix 313 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Helix 318 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Helix 329 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Helix 357 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZI7 +P35844 UniProtKB Beta strand 360 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 368 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Helix 383 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 396 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Helix 407 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Beta strand 417 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +P35844 UniProtKB Helix 423 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZHX +##sequence-region P13134 1 814 +P13134 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13134 UniProtKB Propeptide 20 109 . . . ID=PRO_0000027043 +P13134 UniProtKB Propeptide 110 113 . . . ID=PRO_0000027044;Note=Removed by dipeptidylpeptidase STE13 +P13134 UniProtKB Chain 114 814 . . . ID=PRO_0000027045;Note=Kexin +P13134 UniProtKB Topological domain 114 678 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13134 UniProtKB Transmembrane 679 699 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13134 UniProtKB Topological domain 700 814 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13134 UniProtKB Domain 171 453 . . . Note=Peptidase S8 +P13134 UniProtKB Domain 462 596 . . . Note=P/Homo B;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01173 +P13134 UniProtKB Compositional bias 625 642 . . . Note=Ser/Thr-rich +P13134 UniProtKB Active site 175 175 . . . Note=Charge relay system +P13134 UniProtKB Active site 213 213 . . . Note=Charge relay system +P13134 UniProtKB Active site 385 385 . . . Note=Charge relay system +P13134 UniProtKB Metal binding 135 135 . . . Note=Calcium 1 +P13134 UniProtKB Metal binding 184 184 . . . Note=Calcium 1 +P13134 UniProtKB Metal binding 227 227 . . . Note=Calcium 1 +P13134 UniProtKB Metal binding 277 277 . . . Note=Calcium 2 +P13134 UniProtKB Metal binding 320 320 . . . Note=Calcium 2 +P13134 UniProtKB Metal binding 350 350 . . . Note=Calcium 2 +P13134 UniProtKB Glycosylation 42 42 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13134 UniProtKB Glycosylation 163 163 . . . Note=N-linked (GlcNAc...) asparagine +P13134 UniProtKB Glycosylation 404 404 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13134 UniProtKB Glycosylation 480 480 . . . Note=N-linked (GlcNAc...) asparagine +P13134 UniProtKB Disulfide bond 230 377 . . . . +P13134 UniProtKB Disulfide bond 322 352 . . . . +P13134 UniProtKB Helix 123 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Helix 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Turn 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 147 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Helix 157 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 170 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Turn 183 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Helix 191 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Turn 197 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Turn 209 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Helix 213 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 225 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Turn 234 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 238 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R64 +P13134 UniProtKB Helix 252 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Turn 259 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 267 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 278 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Helix 287 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 307 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Helix 316 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Helix 322 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Turn 326 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 333 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 355 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 368 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 377 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Helix 384 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Helix 407 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Helix 425 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 433 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Turn 440 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Helix 449 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 465 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 477 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 486 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Helix 494 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 502 518 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Helix 519 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 522 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 533 537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 549 557 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Turn 558 561 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 566 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Beta strand 581 595 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +P13134 UniProtKB Helix 597 599 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ID4 +##sequence-region P38692 1 1080 +P38692 UniProtKB Chain 1 1080 . . . ID=PRO_0000086127;Note=Serine/threonine-protein kinase KIC1 +P38692 UniProtKB Domain 23 276 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38692 UniProtKB Nucleotide binding 29 37 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38692 UniProtKB Active site 144 144 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P38692 UniProtKB Binding site 52 52 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38692 UniProtKB Modified residue 735 735 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38991 1 367 +P38991 UniProtKB Chain 1 367 . . . ID=PRO_0000086029;Note=Spindle assembly checkpoint kinase +P38991 UniProtKB Domain 104 355 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38991 UniProtKB Nucleotide binding 110 118 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38991 UniProtKB Active site 227 227 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P38991 UniProtKB Binding site 133 133 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38991 UniProtKB Modified residue 5 5 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12408861;Dbxref=PMID:12408861 +P38991 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12408861;Dbxref=PMID:12408861 +P38991 UniProtKB Modified residue 260 260 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12408861;Dbxref=PMID:12408861 +P38991 UniProtKB Mutagenesis 260 260 . . . Note=In IPL1-4%3B causes missegregation of chromosomes at 37 degrees Celsius. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8007975;Dbxref=PMID:8007975 +P38991 UniProtKB Mutagenesis 340 340 . . . Note=In IPL1-1%3B causes missegregation of chromosomes at 37 degrees Celsius. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8007975;Dbxref=PMID:8007975 +P38991 UniProtKB Mutagenesis 352 352 . . . Note=In IPL1-2%3B causes missegregation of chromosomes at 37 degrees Celsius. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8007975;Dbxref=PMID:8007975 +##sequence-region P38250 1 946 +P38250 UniProtKB Chain 1 946 . . . ID=PRO_0000084261;Note=Increased sodium tolerance protein 2 +P38250 UniProtKB Topological domain 1 121 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38250 UniProtKB Transmembrane 122 142 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38250 UniProtKB Topological domain 143 153 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38250 UniProtKB Transmembrane 154 174 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38250 UniProtKB Topological domain 175 217 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38250 UniProtKB Transmembrane 218 238 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38250 UniProtKB Topological domain 239 253 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38250 UniProtKB Transmembrane 254 274 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38250 UniProtKB Topological domain 275 302 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38250 UniProtKB Transmembrane 303 323 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38250 UniProtKB Topological domain 324 447 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38250 UniProtKB Transmembrane 448 468 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38250 UniProtKB Topological domain 469 505 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38250 UniProtKB Transmembrane 506 526 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38250 UniProtKB Topological domain 527 563 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38250 UniProtKB Transmembrane 564 584 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38250 UniProtKB Topological domain 585 946 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38250 UniProtKB Modified residue 638 638 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38250 UniProtKB Modified residue 701 701 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38250 UniProtKB Modified residue 704 704 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38250 UniProtKB Modified residue 720 720 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38250 UniProtKB Modified residue 726 726 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38250 UniProtKB Modified residue 729 729 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38250 UniProtKB Modified residue 730 730 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38250 UniProtKB Modified residue 757 757 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956 +P38250 UniProtKB Modified residue 793 793 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38250 UniProtKB Modified residue 844 844 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38250 UniProtKB Modified residue 847 847 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38250 UniProtKB Modified residue 850 850 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38250 UniProtKB Sequence conflict 243 243 . . . Note=I->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38250 UniProtKB Sequence conflict 243 243 . . . Note=I->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38250 UniProtKB Sequence conflict 243 243 . . . Note=I->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25389 1 1037 +P25389 UniProtKB Chain 1 1037 . . . ID=PRO_0000086109;Note=Probable serine/threonine-protein kinase KCC4 +P25389 UniProtKB Domain 21 285 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P25389 UniProtKB Nucleotide binding 27 35 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P25389 UniProtKB Compositional bias 388 499 . . . Note=Ser-rich +P25389 UniProtKB Active site 152 152 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P25389 UniProtKB Binding site 50 50 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P25389 UniProtKB Modified residue 396 396 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25389 UniProtKB Modified residue 675 675 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25389 UniProtKB Modified residue 707 707 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25389 UniProtKB Modified residue 777 777 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25389 UniProtKB Modified residue 822 822 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25389 UniProtKB Modified residue 825 825 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25389 UniProtKB Modified residue 871 871 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25389 UniProtKB Helix 921 924 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST +P25389 UniProtKB Helix 925 927 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST +P25389 UniProtKB Beta strand 930 933 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST +P25389 UniProtKB Beta strand 938 942 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST +P25389 UniProtKB Helix 944 956 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST +P25389 UniProtKB Helix 959 961 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST +P25389 UniProtKB Beta strand 963 969 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST +P25389 UniProtKB Turn 970 973 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST +P25389 UniProtKB Beta strand 974 979 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST +P25389 UniProtKB Beta strand 984 986 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST +P25389 UniProtKB Beta strand 990 998 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST +P25389 UniProtKB Beta strand 1004 1013 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST +P25389 UniProtKB Helix 1015 1031 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OST +##sequence-region P17423 1 357 +P17423 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2165904;Dbxref=PMID:2165904 +P17423 UniProtKB Chain 2 357 . . . ID=PRO_0000156656;Note=Homoserine kinase +P17423 UniProtKB Nucleotide binding 104 114 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17423 UniProtKB Cross-link 133 133 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P17423 UniProtKB Sequence conflict 87 87 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P07277 1 443 +P07277 UniProtKB Chain 1 443 . . . ID=PRO_0000156662;Note=Mevalonate kinase +P07277 UniProtKB Nucleotide binding 141 151 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07277 UniProtKB Active site 202 202 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07277 UniProtKB Binding site 138 138 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P13185 1 1064 +P13185 UniProtKB Chain 1 1064 . . . ID=PRO_0000086131;Note=Serine/threonine protein kinase KIN1 +P13185 UniProtKB Domain 120 398 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P13185 UniProtKB Domain 1015 1064 . . . Note=KA1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00565 +P13185 UniProtKB Nucleotide binding 126 134 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P13185 UniProtKB Active site 269 269 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P13185 UniProtKB Binding site 149 149 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P13185 UniProtKB Modified residue 534 534 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P13185 UniProtKB Modified residue 593 593 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P13185 UniProtKB Modified residue 646 646 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P13185 UniProtKB Modified residue 764 764 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P13185 UniProtKB Modified residue 986 986 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P13185 UniProtKB Sequence conflict 25 25 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13185 UniProtKB Sequence conflict 453 453 . . . Note=T->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13185 UniProtKB Sequence conflict 455 455 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13185 UniProtKB Sequence conflict 718 718 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13185 UniProtKB Sequence conflict 920 921 . . . Note=NI->IN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13185 UniProtKB Sequence conflict 976 976 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13185 UniProtKB Sequence conflict 979 980 . . . Note=SI->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13185 UniProtKB Sequence conflict 984 985 . . . Note=KT->NS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P06242 1 306 +P06242 UniProtKB Chain 1 306 . . . ID=PRO_0000086132;Note=Serine/threonine-protein kinase KIN28 +P06242 UniProtKB Domain 7 290 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P06242 UniProtKB Nucleotide binding 13 21 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P06242 UniProtKB Active site 129 129 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P06242 UniProtKB Binding site 36 36 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P06242 UniProtKB Modified residue 162 162 . . . Note=Phosphothreonine%3B by CAK;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10373527,ECO:0000269|PubMed:11839796,ECO:0000269|PubMed:9774652;Dbxref=PMID:10373527,PMID:11839796,PMID:9774652 +P06242 UniProtKB Mutagenesis 17 18 . . . Note=No effect on phosphorylation%3B no effect on kinase activity. TY->AF;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10373527;Dbxref=PMID:10373527 +P06242 UniProtKB Mutagenesis 17 17 . . . Note=Slow growth. T->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11839796;Dbxref=PMID:11839796 +P06242 UniProtKB Mutagenesis 17 17 . . . Note=Normal growth. T->E%2CQ%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11839796;Dbxref=PMID:11839796 +P06242 UniProtKB Mutagenesis 36 36 . . . Note=Slow growth. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11839796;Dbxref=PMID:11839796 +P06242 UniProtKB Mutagenesis 54 54 . . . Note=Non-viable. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11839796;Dbxref=PMID:11839796 +P06242 UniProtKB Mutagenesis 147 147 . . . Note=Abolishes kinase activity. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10373527,ECO:0000269|PubMed:11839796;Dbxref=PMID:10373527,PMID:11839796 +P06242 UniProtKB Mutagenesis 162 162 . . . Note=Diminishes phosphorylation%3B 75-80%25 loss in kinase activity%3B no effect on survival. T->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10373527,ECO:0000269|PubMed:11839796,ECO:0000269|PubMed:9774652;Dbxref=PMID:10373527,PMID:11839796,PMID:9774652 +P06242 UniProtKB Mutagenesis 162 162 . . . Note=No effect on kinase activity. T->S%2CD%2CE;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10373527,ECO:0000269|PubMed:11839796,ECO:0000269|PubMed:9774652;Dbxref=PMID:10373527,PMID:11839796,PMID:9774652 +P06242 UniProtKB Mutagenesis 163 163 . . . Note=Normal growth. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11839796;Dbxref=PMID:11839796 +##sequence-region P24583 1 1151 +P24583 UniProtKB Chain 1 1151 . . . ID=PRO_0000055738;Note=Protein kinase C-like 1 +P24583 UniProtKB Repeat 5 77 . . . Note=REM 1 +P24583 UniProtKB Repeat 118 193 . . . Note=REM 2 +P24583 UniProtKB Domain 196 288 . . . Note=C2 +P24583 UniProtKB Domain 824 1083 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P24583 UniProtKB Domain 1084 1151 . . . Note=AGC-kinase C-terminal +P24583 UniProtKB Zinc finger 414 461 . . . Note=Phorbol-ester/DAG-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226 +P24583 UniProtKB Zinc finger 481 531 . . . Note=Phorbol-ester/DAG-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226 +P24583 UniProtKB Nucleotide binding 830 838 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P24583 UniProtKB Active site 949 949 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P24583 UniProtKB Binding site 853 853 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P24583 UniProtKB Modified residue 226 226 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P24583 UniProtKB Modified residue 761 761 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P24583 UniProtKB Natural variant 958 958 . . . Note=In cly5%3B temperature-sensitive mutation that cause cell lysis at high temperature. T->I +P24583 UniProtKB Natural variant 1023 1023 . . . Note=In cly7%3B temperature-sensitive mutation that cause cell lysis at high temperature. P->S +P24583 UniProtKB Sequence conflict 81 81 . . . Note=C->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24583 UniProtKB Sequence conflict 81 81 . . . Note=C->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24583 UniProtKB Sequence conflict 244 244 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24583 UniProtKB Sequence conflict 606 606 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24583 UniProtKB Sequence conflict 621 621 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24583 UniProtKB Sequence conflict 621 621 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24583 UniProtKB Sequence conflict 621 621 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24583 UniProtKB Sequence conflict 623 623 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24583 UniProtKB Sequence conflict 789 789 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P24583 UniProtKB Sequence conflict 789 789 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40565 1 148 +P40565 UniProtKB Chain 1 148 . . . ID=PRO_0000081621;Note=U2 snRNP component IST3 +P40565 UniProtKB Domain 31 109 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P40565 UniProtKB Beta strand 27 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UQT +P40565 UniProtKB Beta strand 32 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC +P40565 UniProtKB Helix 44 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC +P40565 UniProtKB Helix 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC +P40565 UniProtKB Beta strand 57 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC +P40565 UniProtKB Beta strand 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC +P40565 UniProtKB Beta strand 71 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC +P40565 UniProtKB Helix 82 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC +P40565 UniProtKB Beta strand 103 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC +P40565 UniProtKB Helix 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MY3 +P40565 UniProtKB Helix 116 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC +##sequence-region Q06505 1 410 +Q06505 UniProtKB Chain 1 410 . . . ID=PRO_0000083366;Note=Transcription factor SPN1 +Q06505 UniProtKB Domain 219 296 . . . Note=TFIIS N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00649 +Q06505 UniProtKB Modified residue 15 15 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06505 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q06505 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06505 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06505 UniProtKB Modified residue 86 86 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06505 UniProtKB Modified residue 89 89 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:12242279;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198,PMID:12242279 +Q06505 UniProtKB Mutagenesis 192 192 . . . Note=Suppresses postrecruitment-defective SPT15/TBP alleles. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12524336;Dbxref=PMID:12524336 +Q06505 UniProtKB Helix 150 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFQ +Q06505 UniProtKB Helix 191 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFQ +Q06505 UniProtKB Helix 206 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFQ +Q06505 UniProtKB Helix 209 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFQ +Q06505 UniProtKB Helix 217 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFQ +Q06505 UniProtKB Helix 236 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFQ +Q06505 UniProtKB Helix 253 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFQ +Q06505 UniProtKB Helix 261 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFQ +Q06505 UniProtKB Beta strand 272 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OAK +Q06505 UniProtKB Helix 276 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NFQ +##sequence-region Q12350 1 301 +Q12350 UniProtKB Chain 1 301 . . . ID=PRO_0000240378;Note=J domain-containing protein 1 +Q12350 UniProtKB Transmembrane 208 228 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12350 UniProtKB Domain 58 150 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +##sequence-region Q03361 1 876 +Q03361 UniProtKB Chain 1 876 . . . ID=PRO_0000253825;Note=Uncharacterized protein JIP4 +Q03361 UniProtKB Compositional bias 685 854 . . . Note=Ser-rich +Q03361 UniProtKB Modified residue 48 48 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03361 UniProtKB Modified residue 51 51 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03361 UniProtKB Modified residue 360 360 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03361 UniProtKB Modified residue 510 510 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03361 UniProtKB Modified residue 552 552 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03361 UniProtKB Modified residue 577 577 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q03361 UniProtKB Modified residue 775 775 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03361 UniProtKB Sequence conflict 708 708 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02196 1 202 +Q02196 UniProtKB Chain 1 202 . . . ID=PRO_0000105936;Note=Adenylyl-sulfate kinase +Q02196 UniProtKB Nucleotide binding 31 38 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02196 UniProtKB Active site 105 105 . . . Note=Phosphoserine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P25583 1 335 +P25583 UniProtKB Chain 1 335 . . . ID=PRO_0000207635;Note=Karyogamy protein KAR4 +##sequence-region P00549 1 500 +P00549 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P00549 UniProtKB Chain 2 500 . . . ID=PRO_0000112121;Note=Pyruvate kinase 1 +P00549 UniProtKB Region 402 407 . . . Note=Allosteric activator binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410 +P00549 UniProtKB Metal binding 51 51 . . . Note=Potassium;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410 +P00549 UniProtKB Metal binding 53 53 . . . Note=Potassium;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410 +P00549 UniProtKB Metal binding 84 84 . . . Note=Potassium;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410 +P00549 UniProtKB Metal binding 85 85 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410 +P00549 UniProtKB Metal binding 242 242 . . . Note=Manganese;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410 +P00549 UniProtKB Metal binding 266 266 . . . Note=Manganese;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410 +P00549 UniProtKB Binding site 49 49 . . . Note=Substrate;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410 +P00549 UniProtKB Binding site 240 240 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410 +P00549 UniProtKB Binding site 265 265 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410 +P00549 UniProtKB Binding site 266 266 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410 +P00549 UniProtKB Binding site 298 298 . . . Note=Substrate;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410 +P00549 UniProtKB Binding site 337 337 . . . Note=ADP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00549 UniProtKB Binding site 452 452 . . . Note=Allosteric activator;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410 +P00549 UniProtKB Binding site 459 459 . . . Note=Allosteric activator;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410 +P00549 UniProtKB Binding site 484 484 . . . Note=Allosteric activator%3B via amide nitrogen;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1A3W,ECO:0000244|PDB:1A3X,ECO:0000269|PubMed:9519410;Dbxref=PMID:9519410 +P00549 UniProtKB Site 240 240 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10413488;Dbxref=PMID:10413488 +P00549 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P00549 UniProtKB Modified residue 9 9 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P00549 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P00549 UniProtKB Modified residue 31 31 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00549 UniProtKB Modified residue 70 70 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00549 UniProtKB Modified residue 184 184 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00549 UniProtKB Modified residue 213 213 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P00549 UniProtKB Modified residue 316 316 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00549 UniProtKB Modified residue 450 450 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00549 UniProtKB Modified residue 478 478 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P00549 UniProtKB Cross-link 204 204 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00549 UniProtKB Cross-link 255 255 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00549 UniProtKB Cross-link 446 446 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00549 UniProtKB Mutagenesis 240 240 . . . Note=Reduces activity 1000-fold. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10413488;Dbxref=PMID:10413488 +P00549 UniProtKB Sequence conflict 382 386 . . . Note=VAASA->SLPR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00549 UniProtKB Helix 3 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 21 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3X +P00549 UniProtKB Helix 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Helix 34 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Helix 57 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 96 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 108 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Turn 116 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 126 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Helix 133 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 142 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Turn 146 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 150 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Turn 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3X +P00549 UniProtKB Beta strand 163 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Helix 193 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 208 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Helix 218 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 235 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Helix 245 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Helix 250 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 260 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Helix 264 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Helix 273 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Helix 276 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 294 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Helix 302 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Helix 312 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 327 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Turn 333 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Helix 341 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 357 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3X +P00549 UniProtKB Helix 361 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Helix 378 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 398 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 403 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Helix 406 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 420 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Helix 429 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Helix 433 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 439 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Turn 452 454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Helix 455 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 478 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Turn 487 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +P00549 UniProtKB Beta strand 494 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A3W +##sequence-region P14681 1 368 +P14681 UniProtKB Chain 1 368 . . . ID=PRO_0000186333;Note=Mitogen-activated protein kinase KSS1 +P14681 UniProtKB Domain 13 313 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P14681 UniProtKB Nucleotide binding 19 27 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P14681 UniProtKB Motif 183 185 . . . Note=TXY +P14681 UniProtKB Compositional bias 345 349 . . . Note=Poly-Glu +P14681 UniProtKB Active site 143 143 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P14681 UniProtKB Binding site 42 42 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P14681 UniProtKB Modified residue 183 183 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P14681 UniProtKB Modified residue 185 185 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region P50090 1 882 +P50090 UniProtKB Chain 1 882 . . . ID=PRO_0000119097;Note=Kelch repeat-containing protein 2 +P50090 UniProtKB Repeat 99 143 . . . Note=Kelch 1 +P50090 UniProtKB Repeat 153 207 . . . Note=Kelch 2 +P50090 UniProtKB Repeat 213 267 . . . Note=Kelch 3 +P50090 UniProtKB Repeat 268 317 . . . Note=Kelch 4 +P50090 UniProtKB Repeat 319 369 . . . Note=Kelch 5 +P50090 UniProtKB Repeat 371 417 . . . Note=Kelch 6 +P50090 UniProtKB Coiled coil 550 685 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50090 UniProtKB Coiled coil 728 881 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50090 UniProtKB Modified residue 455 455 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P50090 UniProtKB Modified residue 509 509 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P13186 1 1147 +P13186 UniProtKB Chain 1 1147 . . . ID=PRO_0000086133;Note=Serine/threonine-protein kinase KIN2 +P13186 UniProtKB Domain 99 377 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P13186 UniProtKB Domain 1098 1147 . . . Note=KA1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00565 +P13186 UniProtKB Nucleotide binding 105 113 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P13186 UniProtKB Compositional bias 527 536 . . . Note=Poly-Gln +P13186 UniProtKB Active site 248 248 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P13186 UniProtKB Binding site 128 128 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P13186 UniProtKB Modified residue 22 22 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13186 UniProtKB Modified residue 146 146 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P13186 UniProtKB Modified residue 549 549 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P13186 UniProtKB Modified residue 609 609 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P13186 UniProtKB Modified residue 888 888 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P13186 UniProtKB Sequence conflict 216 217 . . . Note=QH->HD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13186 UniProtKB Sequence conflict 675 707 . . . Note=QEPLPEREPPTYMSKSNEISIKVPKSHSRTISD->SGTYSSKENLQHICQNQMKFPSKYRKAIVVLYQT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13186 UniProtKB Sequence conflict 756 758 . . . Note=NAE->KRQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13186 UniProtKB Sequence conflict 805 805 . . . Note=P->PLSVP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13186 UniProtKB Sequence conflict 1034 1037 . . . Note=ATNT->TTNSI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13186 UniProtKB Sequence conflict 1041 1042 . . . Note=NS->KT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q01919 1 800 +Q01919 UniProtKB Chain 1 800 . . . ID=PRO_0000086135;Note=Serine/threonine-protein kinase KIN4 +Q01919 UniProtKB Domain 46 313 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q01919 UniProtKB Nucleotide binding 52 60 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q01919 UniProtKB Active site 175 175 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q01919 UniProtKB Binding site 80 80 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q01919 UniProtKB Modified residue 365 365 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q01919 UniProtKB Modified residue 388 388 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q01919 UniProtKB Modified residue 521 521 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q01919 UniProtKB Modified residue 748 748 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P28743 1 706 +P28743 UniProtKB Chain 1 706 . . . ID=PRO_0000125453;Note=Kinesin-like protein KIP2 +P28743 UniProtKB Domain 102 493 . . . Note=Kinesin motor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283 +P28743 UniProtKB Nucleotide binding 202 209 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283 +P28743 UniProtKB Coiled coil 507 541 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28743 UniProtKB Coiled coil 569 589 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28743 UniProtKB Coiled coil 612 689 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38063 1 326 +P38063 UniProtKB Chain 1 326 . . . ID=PRO_0000141089;Note=Ribose-phosphate pyrophosphokinase 4 +P38063 UniProtKB Metal binding 140 140 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38063 UniProtKB Metal binding 142 142 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38063 UniProtKB Metal binding 151 151 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38063 UniProtKB Metal binding 155 155 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38063 UniProtKB Sequence conflict 90 90 . . . Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38063 UniProtKB Sequence conflict 169 169 . . . Note=T->AR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P52489 1 506 +P52489 UniProtKB Chain 1 506 . . . ID=PRO_0000112122;Note=Pyruvate kinase 2 +P52489 UniProtKB Metal binding 53 53 . . . Note=Potassium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52489 UniProtKB Metal binding 55 55 . . . Note=Potassium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52489 UniProtKB Metal binding 86 86 . . . Note=Potassium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52489 UniProtKB Metal binding 87 87 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52489 UniProtKB Metal binding 244 244 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52489 UniProtKB Metal binding 268 268 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52489 UniProtKB Binding site 51 51 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52489 UniProtKB Binding site 267 267 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52489 UniProtKB Binding site 268 268 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52489 UniProtKB Binding site 300 300 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52489 UniProtKB Binding site 339 339 . . . Note=ADP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52489 UniProtKB Site 242 242 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52489 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P42846 1 591 +P42846 UniProtKB Chain 1 591 . . . ID=PRO_0000203368;Note=Protein KRI1 +P42846 UniProtKB Compositional bias 53 475 . . . Note=Glu-rich +P42846 UniProtKB Modified residue 177 177 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P42846 UniProtKB Modified residue 184 184 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P42846 UniProtKB Modified residue 185 185 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P42846 UniProtKB Modified residue 486 486 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P54070 1 446 +P54070 UniProtKB Chain 1 446 . . . ID=PRO_0000208247;Note=Mannosyltransferase KTR6 +P54070 UniProtKB Topological domain 1 8 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54070 UniProtKB Transmembrane 9 29 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54070 UniProtKB Topological domain 30 446 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54070 UniProtKB Region 30 114 . . . Note=Stem region;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P54070 UniProtKB Region 115 446 . . . Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P54070 UniProtKB Active site 334 334 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54070 UniProtKB Glycosylation 82 82 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54070 UniProtKB Glycosylation 98 98 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q02733 1 499 +Q02733 UniProtKB Chain 1 499 . . . ID=PRO_0000268179;Note=Increased recombination centers protein 15 +Q02733 UniProtKB Nucleotide binding 47 56 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q06554 1 1556 +Q06554 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q06554 UniProtKB Chain 2 1556 . . . ID=PRO_0000268181;Note=Uncharacterized ATP-dependent helicase IRC20 +Q06554 UniProtKB Domain 378 583 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q06554 UniProtKB Domain 1363 1531 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q06554 UniProtKB Nucleotide binding 391 398 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q06554 UniProtKB Zinc finger 1239 1277 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +Q06554 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q06554 UniProtKB Modified residue 810 810 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region A0A023PXB5 1 102 +A0A023PXB5 UniProtKB Chain 1 102 . . . ID=PRO_0000430978;Note=Putative uncharacterized membrane protein IRC2 +A0A023PXB5 UniProtKB Transmembrane 21 43 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PXB5 UniProtKB Transmembrane 58 80 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03036 1 179 +Q03036 UniProtKB Chain 1 179 . . . ID=PRO_0000253886;Note=Uncharacterized protein IRC4 +Q03036 UniProtKB Helix 7 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG +Q03036 UniProtKB Helix 24 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG +Q03036 UniProtKB Helix 30 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG +Q03036 UniProtKB Helix 44 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG +Q03036 UniProtKB Beta strand 73 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG +Q03036 UniProtKB Helix 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG +Q03036 UniProtKB Helix 83 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG +Q03036 UniProtKB Helix 99 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG +Q03036 UniProtKB Helix 122 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG +Q03036 UniProtKB Beta strand 127 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG +Q03036 UniProtKB Helix 133 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG +Q03036 UniProtKB Helix 142 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG +Q03036 UniProtKB Helix 151 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5COG +##sequence-region P47010 1 130 +P47010 UniProtKB Chain 1 130 . . . ID=PRO_0000203035;Note=Putative uncharacterized protein IRC9 +P47010 UniProtKB Transmembrane 25 45 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47010 UniProtKB Transmembrane 50 70 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47010 UniProtKB Transmembrane 83 103 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32361 1 1115 +P32361 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32361 UniProtKB Chain 19 1115 . . . ID=PRO_0000024338;Note=Serine/threonine-protein kinase/endoribonuclease IRE1 +P32361 UniProtKB Topological domain 19 526 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32361 UniProtKB Transmembrane 527 555 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32361 UniProtKB Topological domain 556 1115 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32361 UniProtKB Domain 674 980 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32361 UniProtKB Domain 983 1115 . . . Note=KEN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00725 +P32361 UniProtKB Nucleotide binding 680 688 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32361 UniProtKB Active site 797 797 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P32361 UniProtKB Binding site 702 702 . . . Note=ATP +P32361 UniProtKB Modified residue 840 840 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8670804;Dbxref=PMID:8670804 +P32361 UniProtKB Modified residue 841 841 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8670804;Dbxref=PMID:8670804 +P32361 UniProtKB Glycosylation 111 111 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32361 UniProtKB Glycosylation 213 213 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32361 UniProtKB Glycosylation 298 298 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32361 UniProtKB Glycosylation 397 397 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32361 UniProtKB Mutagenesis 702 702 . . . Note=Loss of autophosphorylation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8663458;Dbxref=PMID:8663458 +P32361 UniProtKB Sequence conflict 368 368 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32361 UniProtKB Sequence conflict 625 626 . . . Note=ND->KH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32361 UniProtKB Beta strand 116 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 132 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Turn 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 142 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Helix 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 154 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Turn 162 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 165 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Turn 175 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 178 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Turn 184 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 187 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Helix 195 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 203 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 222 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 228 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Turn 238 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 243 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 277 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 300 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Turn 308 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Helix 311 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 321 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 326 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Turn 330 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 333 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 344 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 355 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Turn 365 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 369 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 390 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 400 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Turn 405 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Helix 409 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Helix 419 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Helix 424 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Helix 429 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Helix 435 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Beta strand 444 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BE1 +P32361 UniProtKB Turn 666 669 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LJ2 +P32361 UniProtKB Beta strand 674 682 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Turn 684 686 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBV +P32361 UniProtKB Beta strand 688 705 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 706 708 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 709 722 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Beta strand 731 736 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Beta strand 738 745 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Beta strand 749 751 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 752 757 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 765 769 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBV +P32361 UniProtKB Helix 774 790 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 800 802 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Beta strand 803 806 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 809 812 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Beta strand 823 826 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Turn 836 838 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBV +P32361 UniProtKB Helix 851 855 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBV +P32361 UniProtKB Helix 858 861 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 900 914 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Turn 924 926 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 927 933 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 947 960 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 965 967 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 971 975 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 978 980 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 983 998 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Turn 1002 1005 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 1007 1013 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 1016 1019 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 1025 1028 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 1031 1035 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBV +P32361 UniProtKB Beta strand 1038 1041 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBV +P32361 UniProtKB Helix 1048 1060 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 1062 1064 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 1067 1072 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 1078 1087 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 1091 1102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Turn 1107 1109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +P32361 UniProtKB Helix 1110 1114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RIO +##sequence-region P30606 1 609 +P30606 UniProtKB Chain 1 609 . . . ID=PRO_0000050458;Note=Myo-inositol transporter 2 +P30606 UniProtKB Topological domain 1 104 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Transmembrane 105 125 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Topological domain 126 152 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Transmembrane 153 173 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Topological domain 174 179 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Transmembrane 180 200 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Topological domain 201 209 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Transmembrane 210 230 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Topological domain 231 240 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Transmembrane 241 261 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Topological domain 262 269 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Transmembrane 270 290 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Topological domain 291 359 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Transmembrane 360 380 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Topological domain 381 396 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Transmembrane 397 417 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Topological domain 418 423 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Transmembrane 424 444 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Topological domain 445 465 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Transmembrane 466 486 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Topological domain 487 506 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Transmembrane 507 527 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Topological domain 528 533 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Transmembrane 534 554 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Topological domain 555 609 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30606 UniProtKB Glycosylation 394 394 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04934 1 453 +Q04934 UniProtKB Chain 1 453 . . . ID=PRO_0000084277;Note=Protein IVY1 +Q04934 UniProtKB Coiled coil 102 122 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04934 UniProtKB Coiled coil 230 257 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04934 UniProtKB Modified residue 59 59 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q04934 UniProtKB Modified residue 84 84 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04934 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04934 UniProtKB Modified residue 335 335 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P36035 1 616 +P36035 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:12872131;Dbxref=PMID:17761666,PMID:22814378,PMID:12872131 +P36035 UniProtKB Chain 2 616 . . . ID=PRO_0000050460;Note=Carboxylic acid transporter protein homolog +P36035 UniProtKB Topological domain 2 140 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Transmembrane 141 161 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Topological domain 162 176 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Transmembrane 177 197 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Topological domain 198 205 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Transmembrane 206 226 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Topological domain 227 230 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Transmembrane 231 251 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Topological domain 252 263 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Transmembrane 264 284 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Topological domain 285 296 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Transmembrane 297 317 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Topological domain 318 363 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Transmembrane 364 384 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Topological domain 385 402 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Transmembrane 403 423 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Topological domain 424 432 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Transmembrane 433 453 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Topological domain 454 457 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Transmembrane 458 478 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Topological domain 479 489 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Transmembrane 490 510 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Topological domain 511 535 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Transmembrane 536 556 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Topological domain 557 616 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36035 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:22814378;Dbxref=PMID:17761666,PMID:22814378 +P36035 UniProtKB Modified residue 4 4 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P36035 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P36035 UniProtKB Modified residue 61 61 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36035 UniProtKB Modified residue 66 66 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36035 UniProtKB Modified residue 70 70 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36035 UniProtKB Modified residue 584 584 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P36035 UniProtKB Modified residue 603 603 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36035 UniProtKB Modified residue 606 606 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:19779198;Dbxref=PMID:17761666,PMID:19779198 +P36035 UniProtKB Cross-link 9 9 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P36035 UniProtKB Cross-link 338 338 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region P46997 1 583 +P46997 UniProtKB Chain 1 583 . . . ID=PRO_0000071142;Note=J protein JJJ2 +P46997 UniProtKB Domain 11 79 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +P46997 UniProtKB Compositional bias 232 236 . . . Note=Poly-Glu +P46997 UniProtKB Compositional bias 240 252 . . . Note=Poly-Gln +P46997 UniProtKB Modified residue 229 229 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P26364 1 225 +P26364 UniProtKB Chain 1 225 . . . ID=PRO_0000158907;Note=GTP:AMP phosphotransferase%2C mitochondrial +P26364 UniProtKB Nucleotide binding 24 29 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169 +P26364 UniProtKB Nucleotide binding 72 74 . . . Note=AMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169 +P26364 UniProtKB Nucleotide binding 103 106 . . . Note=AMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169 +P26364 UniProtKB Nucleotide binding 154 155 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169 +P26364 UniProtKB Region 45 74 . . . Note=NMPbind;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169 +P26364 UniProtKB Region 144 181 . . . Note=LID;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169 +P26364 UniProtKB Binding site 46 46 . . . Note=AMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169 +P26364 UniProtKB Binding site 51 51 . . . Note=AMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169 +P26364 UniProtKB Binding site 110 110 . . . Note=AMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169 +P26364 UniProtKB Binding site 145 145 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169 +P26364 UniProtKB Binding site 178 178 . . . Note=AMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169 +P26364 UniProtKB Binding site 189 189 . . . Note=AMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169 +P26364 UniProtKB Binding site 218 218 . . . Note=GTP%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03169 +##sequence-region P06244 1 397 +P06244 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P06244 UniProtKB Chain 2 397 . . . ID=PRO_0000086046;Note=cAMP-dependent protein kinase type 1 +P06244 UniProtKB Domain 87 341 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P06244 UniProtKB Domain 342 397 . . . Note=AGC-kinase C-terminal +P06244 UniProtKB Nucleotide binding 93 101 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P06244 UniProtKB Active site 210 210 . . . Note=Proton acceptor +P06244 UniProtKB Binding site 116 116 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P06244 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P06244 UniProtKB Sequence conflict 79 86 . . . Note=SGKYSLQD->VGSIVYKN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06244 UniProtKB Sequence conflict 79 86 . . . Note=SGKYSLQD->VGSIVYKN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06244 UniProtKB Sequence conflict 164 171 . . . Note=MDYIEGGE->ILKVER;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06244 UniProtKB Sequence conflict 180 181 . . . Note=QR->KD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06244 UniProtKB Sequence conflict 188 190 . . . Note=KFY->QIF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06244 UniProtKB Helix 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Beta strand 87 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Beta strand 100 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Turn 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Beta strand 112 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Helix 120 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Helix 129 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Beta strand 150 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Beta strand 157 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Helix 172 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Helix 184 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Turn 203 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Helix 213 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Beta strand 216 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Beta strand 224 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Turn 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Helix 251 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Helix 263 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Helix 287 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Helix 307 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Turn 321 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Turn 329 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Helix 333 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Helix 339 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Helix 346 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +P06244 UniProtKB Helix 391 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FOT +##sequence-region Q07551 1 312 +Q07551 UniProtKB Chain 1 312 . . . ID=PRO_0000262755;Note=NADPH-dependent alpha-keto amide reductase +Q07551 UniProtKB Nucleotide binding 208 268 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07551 UniProtKB Active site 64 64 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07551 UniProtKB Binding site 122 122 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07551 UniProtKB Site 89 89 . . . Note=Lowers pKa of active site Tyr;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07551 UniProtKB Modified residue 123 123 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q08979 1 651 +Q08979 UniProtKB Chain 1 651 . . . ID=PRO_0000119098;Note=Kelch repeat-containing protein 3 +Q08979 UniProtKB Repeat 94 148 . . . Note=Kelch 1 +Q08979 UniProtKB Repeat 150 199 . . . Note=Kelch 2 +Q08979 UniProtKB Repeat 208 259 . . . Note=Kelch 3 +Q08979 UniProtKB Repeat 262 310 . . . Note=Kelch 4 +Q08979 UniProtKB Repeat 334 383 . . . Note=Kelch 5 +Q08979 UniProtKB Modified residue 47 47 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region Q04066 1 261 +Q04066 UniProtKB Chain 1 261 . . . ID=PRO_0000234660;Note=Kynurenine formamidase +Q04066 UniProtKB Motif 36 40 . . . Note=HGGXW +Q04066 UniProtKB Active site 110 110 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03014 +Q04066 UniProtKB Active site 211 211 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03014 +Q04066 UniProtKB Active site 243 243 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03014 +Q04066 UniProtKB Modified residue 9 9 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +Q04066 UniProtKB Helix 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Beta strand 19 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Beta strand 30 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Turn 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Helix 47 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Helix 51 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Beta strand 66 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Turn 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Helix 83 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Beta strand 104 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Helix 111 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Helix 121 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Turn 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Helix 132 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Beta strand 144 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Helix 156 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Helix 164 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Helix 167 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Helix 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Helix 185 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Beta strand 202 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Helix 217 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Beta strand 233 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Helix 243 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +Q04066 UniProtKB Helix 250 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VKH +##sequence-region P36005 1 433 +P36005 UniProtKB Chain 1 433 . . . ID=PRO_0000086150;Note=Serine/threonine-protein kinase KDX1 +P36005 UniProtKB Domain 23 318 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P36005 UniProtKB Nucleotide binding 29 37 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P36005 UniProtKB Active site 153 153 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P36005 UniProtKB Binding site 55 55 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +##sequence-region P38853 1 1164 +P38853 UniProtKB Chain 1 1164 . . . ID=PRO_0000119096;Note=Kelch repeat-containing protein 1 +P38853 UniProtKB Repeat 139 186 . . . Note=Kelch 1 +P38853 UniProtKB Repeat 253 307 . . . Note=Kelch 2 +P38853 UniProtKB Repeat 308 357 . . . Note=Kelch 3 +P38853 UniProtKB Repeat 359 409 . . . Note=Kelch 4 +P38853 UniProtKB Repeat 411 460 . . . Note=Kelch 5 +P38853 UniProtKB Coiled coil 777 931 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38853 UniProtKB Coiled coil 974 1163 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38853 UniProtKB Modified residue 20 20 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38853 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38853 UniProtKB Modified residue 25 25 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38853 UniProtKB Modified residue 94 94 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P38853 UniProtKB Modified residue 467 467 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38853 UniProtKB Modified residue 477 477 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38853 UniProtKB Modified residue 503 503 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38853 UniProtKB Modified residue 604 604 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38853 UniProtKB Modified residue 613 613 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +P38853 UniProtKB Modified residue 626 626 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38853 UniProtKB Modified residue 689 689 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38853 UniProtKB Modified residue 691 691 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38853 UniProtKB Modified residue 717 717 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38853 UniProtKB Modified residue 748 748 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38853 UniProtKB Modified residue 837 837 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38853 UniProtKB Modified residue 848 848 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38853 UniProtKB Modified residue 958 958 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38853 UniProtKB Modified residue 997 997 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38853 UniProtKB Modified residue 1003 1003 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38853 UniProtKB Modified residue 1022 1022 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38853 UniProtKB Sequence conflict 447 447 . . . Note=D->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40309 1 873 +P40309 UniProtKB Chain 1 873 . . . ID=PRO_0000196618;Note=K(+)/H(+) antiporter 1 +P40309 UniProtKB Topological domain 1 23 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Transmembrane 24 44 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Topological domain 45 51 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Transmembrane 52 72 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Topological domain 73 82 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Transmembrane 83 103 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Topological domain 104 116 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Transmembrane 117 137 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Topological domain 138 154 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Transmembrane 155 175 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Topological domain 176 188 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Transmembrane 189 209 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Topological domain 210 220 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Transmembrane 221 241 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Topological domain 242 267 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Transmembrane 268 288 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Topological domain 289 316 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Transmembrane 317 337 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Topological domain 338 341 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Transmembrane 342 362 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Topological domain 363 375 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Transmembrane 376 396 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Topological domain 397 404 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Transmembrane 405 425 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Topological domain 426 726 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Transmembrane 727 747 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Topological domain 748 873 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40309 UniProtKB Modified residue 557 557 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P40309 UniProtKB Cross-link 562 562 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P22209 1 435 +P22209 UniProtKB Chain 1 435 . . . ID=PRO_0000086134;Note=Serine/threonine-protein kinase KIN3 +P22209 UniProtKB Domain 25 343 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P22209 UniProtKB Nucleotide binding 31 39 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P22209 UniProtKB Active site 174 174 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P22209 UniProtKB Binding site 54 54 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P22209 UniProtKB Sequence conflict 92 92 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22209 UniProtKB Sequence conflict 98 98 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22209 UniProtKB Sequence conflict 121 121 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22209 UniProtKB Sequence conflict 130 130 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22209 UniProtKB Sequence conflict 235 238 . . . Note=AKSL->SQIS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22209 UniProtKB Sequence conflict 358 358 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25341 1 720 +P25341 UniProtKB Chain 1 720 . . . ID=PRO_0000086136;Note=Serine/threonine-protein kinase KIN82 +P25341 UniProtKB Domain 324 602 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P25341 UniProtKB Nucleotide binding 330 338 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P25341 UniProtKB Active site 449 449 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P25341 UniProtKB Binding site 353 353 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P25341 UniProtKB Modified residue 203 203 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25341 UniProtKB Sequence conflict 341 341 . . . Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25341 UniProtKB Sequence conflict 341 341 . . . Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53086 1 805 +P53086 UniProtKB Chain 1 805 . . . ID=PRO_0000125404;Note=Kinesin-like protein KIP3 +P53086 UniProtKB Domain 10 438 . . . Note=Kinesin motor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283 +P53086 UniProtKB Nucleotide binding 192 199 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283 +P53086 UniProtKB Coiled coil 449 481 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGJ3 1 72 +Q8TGJ3 UniProtKB Signal peptide 1 26 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q8TGJ3 UniProtKB Chain 27 72 . . . ID=PRO_0000247775;Note=Protein kish +Q8TGJ3 UniProtKB Topological domain 27 53 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q8TGJ3 UniProtKB Transmembrane 54 72 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P50112 1 268 +P50112 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50112 UniProtKB Chain 21 268 . . . ID=PRO_0000016851;Note=Cell wall synthesis protein KNH1 +P50112 UniProtKB Sequence conflict 238 238 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38873 1 1557 +P38873 UniProtKB Chain 1 1557 . . . ID=PRO_0000051476;Note=Target of rapamycin complex 1 subunit KOG1 +P38873 UniProtKB Repeat 548 586 . . . Note=HEAT 1 +P38873 UniProtKB Repeat 588 625 . . . Note=HEAT 2 +P38873 UniProtKB Repeat 777 814 . . . Note=HEAT 3 +P38873 UniProtKB Repeat 888 925 . . . Note=HEAT 4 +P38873 UniProtKB Repeat 1207 1248 . . . Note=WD 1 +P38873 UniProtKB Repeat 1252 1293 . . . Note=WD 2 +P38873 UniProtKB Repeat 1296 1346 . . . Note=WD 3 +P38873 UniProtKB Repeat 1350 1390 . . . Note=WD 4 +P38873 UniProtKB Repeat 1400 1440 . . . Note=WD 5 +P38873 UniProtKB Repeat 1452 1492 . . . Note=WD 6 +P38873 UniProtKB Repeat 1517 1557 . . . Note=WD 7 +P38873 UniProtKB Compositional bias 513 525 . . . Note=Poly-Gln +P38873 UniProtKB Compositional bias 846 855 . . . Note=Poly-Gln +##sequence-region P40504 1 517 +P40504 UniProtKB Chain 1 517 . . . ID=PRO_0000208248;Note=Probable mannosyltransferase KTR7 +P40504 UniProtKB Topological domain 1 23 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40504 UniProtKB Transmembrane 24 44 . . . Note=Helical%3B Signal-anchor for type II membrane protein +P40504 UniProtKB Topological domain 45 517 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40504 UniProtKB Region 45 85 . . . Note=Stem region;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40504 UniProtKB Region 86 517 . . . Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40504 UniProtKB Active site 367 367 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40504 UniProtKB Glycosylation 89 89 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40504 UniProtKB Glycosylation 144 144 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36146 1 502 +P36146 UniProtKB Chain 1 502 . . . ID=PRO_0000211561;Note=Protein LAS1 +P36146 UniProtKB Sequence conflict 97 97 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39518 1 744 +P39518 UniProtKB Chain 1 744 . . . ID=PRO_0000193120;Note=Long-chain-fatty-acid--CoA ligase 2 +P39518 UniProtKB Mutagenesis 1 1 . . . Note=In FAM1-1. M->MWKNAGYKKRIRTNLFRNM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7988550;Dbxref=PMID:7988550 +##sequence-region P09620 1 729 +P09620 UniProtKB Signal peptide 1 22 . . . . +P09620 UniProtKB Chain 23 729 . . . ID=PRO_0000004287;Note=Pheromone-processing carboxypeptidase KEX1 +P09620 UniProtKB Topological domain 23 616 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P09620 UniProtKB Transmembrane 617 637 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P09620 UniProtKB Topological domain 638 729 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P09620 UniProtKB Compositional bias 526 531 . . . Note=Poly-Glu +P09620 UniProtKB Compositional bias 545 561 . . . Note=Poly-Asp +P09620 UniProtKB Compositional bias 567 578 . . . Note=Poly-Asp +P09620 UniProtKB Compositional bias 597 607 . . . Note=Poly-Glu +P09620 UniProtKB Compositional bias 703 711 . . . Note=Poly-Lys +P09620 UniProtKB Active site 198 198 . . . . +P09620 UniProtKB Active site 405 405 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09620 UniProtKB Active site 470 470 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09620 UniProtKB Modified residue 660 660 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P09620 UniProtKB Glycosylation 81 81 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P09620 UniProtKB Glycosylation 459 459 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1469044;Dbxref=PMID:1469044 +P09620 UniProtKB Glycosylation 467 467 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1469044;Dbxref=PMID:1469044 +P09620 UniProtKB Mutagenesis 198 198 . . . Note=Inactivates enzyme. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3301004;Dbxref=PMID:3301004 +P09620 UniProtKB Helix 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 50 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 72 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 91 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Turn 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 104 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 110 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 129 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 133 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 154 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 166 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 190 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 200 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 226 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 239 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 246 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 263 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 283 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 287 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 291 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 296 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 314 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 320 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Turn 327 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 337 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 350 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Turn 358 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 369 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 383 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 387 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 396 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 410 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 425 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 433 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 452 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 460 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 472 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Helix 477 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 492 496 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +P09620 UniProtKB Beta strand 499 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AC5 +##sequence-region P15454 1 187 +P15454 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2551688;Dbxref=PMID:2551688 +P15454 UniProtKB Chain 2 187 . . . ID=PRO_0000170655;Note=Guanylate kinase +P15454 UniProtKB Domain 2 184 . . . Note=Guanylate kinase-like +P15454 UniProtKB Nucleotide binding 9 16 . . . Note=ATP +P15454 UniProtKB Nucleotide binding 35 82 . . . Note=GMP +P15454 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1314905,ECO:0000269|PubMed:2551688;Dbxref=PMID:1314905,PMID:2551688 +P15454 UniProtKB Modified residue 149 149 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P15454 UniProtKB Modified residue 157 157 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P15454 UniProtKB Beta strand 5 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7 +P15454 UniProtKB Helix 15 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7 +P15454 UniProtKB Turn 27 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7 +P15454 UniProtKB Beta strand 30 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7 +P15454 UniProtKB Beta strand 35 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GKY +P15454 UniProtKB Turn 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7 +P15454 UniProtKB Beta strand 50 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GKY +P15454 UniProtKB Helix 56 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7 +P15454 UniProtKB Beta strand 68 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7 +P15454 UniProtKB Beta strand 77 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7 +P15454 UniProtKB Helix 83 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7 +P15454 UniProtKB Beta strand 94 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7 +P15454 UniProtKB Helix 102 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7 +P15454 UniProtKB Helix 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7 +P15454 UniProtKB Beta strand 117 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7 +P15454 UniProtKB Helix 126 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7 +P15454 UniProtKB Helix 141 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7 +P15454 UniProtKB Turn 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7 +P15454 UniProtKB Beta strand 163 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7 +P15454 UniProtKB Helix 172 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EX7 +##sequence-region P17260 1 313 +P17260 UniProtKB Signal peptide 1 26 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17260 UniProtKB Chain 27 288 . . . ID=PRO_0000021561;Note=Protein KRE1 +P17260 UniProtKB Propeptide 289 313 . . . ID=PRO_0000021562;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17260 UniProtKB Repeat 72 86 . . . Note=1 +P17260 UniProtKB Repeat 127 141 . . . Note=2 +P17260 UniProtKB Region 72 141 . . . Note=2 X approximate repeats +P17260 UniProtKB Compositional bias 52 58 . . . Note=Poly-Ala +P17260 UniProtKB Compositional bias 95 100 . . . Note=Poly-Thr +P17260 UniProtKB Compositional bias 106 109 . . . Note=Poly-Thr +P17260 UniProtKB Compositional bias 158 169 . . . Note=Poly-Ser +P17260 UniProtKB Lipidation 288 288 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38691 1 1029 +P38691 UniProtKB Chain 1 1029 . . . ID=PRO_0000086228;Note=Serine/threonine-protein kinase KSP1 +P38691 UniProtKB Domain 18 351 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38691 UniProtKB Nucleotide binding 27 35 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38691 UniProtKB Active site 207 207 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P38691 UniProtKB Binding site 47 47 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38691 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38691 UniProtKB Modified residue 419 419 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38691 UniProtKB Modified residue 501 501 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38691 UniProtKB Modified residue 504 504 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38691 UniProtKB Modified residue 526 526 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P38691 UniProtKB Modified residue 529 529 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38691 UniProtKB Modified residue 646 646 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38691 UniProtKB Modified residue 845 845 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38691 UniProtKB Modified residue 884 884 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38691 UniProtKB Modified residue 1005 1005 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38691 UniProtKB Modified residue 1014 1014 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P38130 1 404 +P38130 UniProtKB Chain 1 404 . . . ID=PRO_0000208244;Note=Probable mannosyltransferase KTR3 +P38130 UniProtKB Topological domain 1 27 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38130 UniProtKB Transmembrane 28 44 . . . Note=Helical%3B Signal-anchor for type II membrane protein +P38130 UniProtKB Topological domain 45 404 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38130 UniProtKB Region 45 83 . . . Note=Stem region;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38130 UniProtKB Region 84 404 . . . Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38130 UniProtKB Active site 295 295 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38130 UniProtKB Sequence conflict 100 100 . . . Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38800 1 1345 +P38800 UniProtKB Chain 1 1345 . . . ID=PRO_0000202901;Note=Membrane-anchored lipid-binding protein LAM4 +P38800 UniProtKB Topological domain 1 1197 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38800 UniProtKB Transmembrane 1198 1218 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38800 UniProtKB Topological domain 1219 1345 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38800 UniProtKB Domain 549 616 . . . Note=GRAM;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38800 UniProtKB Domain 758 930 . . . Note=VASt 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01114 +P38800 UniProtKB Domain 967 1139 . . . Note=VASt 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01114 +P38800 UniProtKB Compositional bias 679 711 . . . Note=Asp-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00004 +P38800 UniProtKB Modified residue 66 66 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38800 UniProtKB Modified residue 747 747 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P38800 UniProtKB Mutagenesis 1119 1119 . . . Note=Abolishes the ability to bind sterol. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26001273;Dbxref=PMID:26001273 +##sequence-region P38210 1 180 +P38210 UniProtKB Chain 1 180 . . . ID=PRO_0000076230;Note=Chromatin structure-remodeling complex protein RSC14 +##sequence-region P20485 1 582 +P20485 UniProtKB Chain 1 582 . . . ID=PRO_0000206226;Note=Choline kinase +P20485 UniProtKB Modified residue 30 30 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12105205;Dbxref=PMID:12105205 +P20485 UniProtKB Modified residue 48 48 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P20485 UniProtKB Modified residue 51 51 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P20485 UniProtKB Modified residue 54 54 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P20485 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12105205;Dbxref=PMID:12105205 +P20485 UniProtKB Mutagenesis 30 30 . . . Note=Decrease in activity and in phosphorylation by PKA. No phosphorylation by PKA%2C and strong decrease in activity%3B when associated with A-85. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12105205;Dbxref=PMID:12105205 +P20485 UniProtKB Mutagenesis 85 85 . . . Note=No phosphorylation by PKA%2C and strong decrease in activity%3B when associated with A-30. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12105205;Dbxref=PMID:12105205 +##sequence-region P38689 1 320 +P38689 UniProtKB Chain 1 320 . . . ID=PRO_0000141088;Note=Ribose-phosphate pyrophosphokinase 3 +P38689 UniProtKB Metal binding 131 131 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38689 UniProtKB Metal binding 133 133 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38689 UniProtKB Metal binding 142 142 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38689 UniProtKB Metal binding 146 146 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04431 1 385 +Q04431 UniProtKB Chain 1 385 . . . ID=PRO_0000253889;Note=Spindle pole body component KRE28 +Q04431 UniProtKB Coiled coil 128 167 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04431 UniProtKB Coiled coil 229 258 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04431 UniProtKB Sequence conflict 263 263 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P22023 1 1365 +P22023 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22023 UniProtKB Chain 18 1365 . . . ID=PRO_0000021563;Note=Killer toxin-resistance protein 5 +P22023 UniProtKB Motif 1362 1365 . . . Note=Prevents secretion from ER +P22023 UniProtKB Glycosylation 115 115 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22023 UniProtKB Glycosylation 228 228 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22023 UniProtKB Glycosylation 293 293 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22023 UniProtKB Glycosylation 457 457 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22023 UniProtKB Glycosylation 519 519 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22023 UniProtKB Glycosylation 523 523 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22023 UniProtKB Glycosylation 644 644 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22023 UniProtKB Glycosylation 870 870 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22023 UniProtKB Glycosylation 1091 1091 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22023 UniProtKB Glycosylation 1150 1150 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22023 UniProtKB Glycosylation 1195 1195 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22023 UniProtKB Sequence conflict 582 582 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22023 UniProtKB Sequence conflict 780 794 . . . Note=HLDQNEVPETEHFEA->ILIKMKCQKQNISKAK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P33550 1 425 +P33550 UniProtKB Chain 1 425 . . . ID=PRO_0000208243;Note=Probable mannosyltransferase KTR2 +P33550 UniProtKB Topological domain 1 13 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33550 UniProtKB Transmembrane 14 33 . . . Note=Helical%3B Signal-anchor for type II membrane protein +P33550 UniProtKB Topological domain 34 425 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33550 UniProtKB Region 34 89 . . . Note=Stem region;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33550 UniProtKB Region 90 425 . . . Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33550 UniProtKB Active site 313 313 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33550 UniProtKB Glycosylation 65 65 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33550 UniProtKB Glycosylation 81 81 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33550 UniProtKB Glycosylation 92 92 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33550 UniProtKB Glycosylation 167 167 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43560 1 674 +P43560 UniProtKB Chain 1 674 . . . ID=PRO_0000202673;Note=Membrane-anchored lipid-binding protein LAM5 +P43560 UniProtKB Topological domain 1 633 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43560 UniProtKB Transmembrane 634 654 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43560 UniProtKB Topological domain 655 674 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43560 UniProtKB Domain 198 264 . . . Note=GRAM;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43560 UniProtKB Domain 409 582 . . . Note=VASt;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01114 +P43560 UniProtKB Compositional bias 81 140 . . . Note=Ser-rich +P43560 UniProtKB Modified residue 110 110 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P43560 UniProtKB Modified residue 113 113 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P43560 UniProtKB Modified residue 140 140 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P43560 UniProtKB Modified residue 143 143 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P43560 UniProtKB Modified residue 149 149 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region Q06346 1 221 +Q06346 UniProtKB Chain 1 221 . . . ID=PRO_0000253846;Note=Inositol phosphorylceramide synthase regulatory subunit KEI1 +Q06346 UniProtKB Chain 1 135 . . . ID=PRO_0000409445;Note=KEI1N +Q06346 UniProtKB Chain 136 221 . . . ID=PRO_0000409446;Note=KEI1C +Q06346 UniProtKB Transmembrane 11 31 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06346 UniProtKB Transmembrane 54 74 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06346 UniProtKB Transmembrane 79 99 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06346 UniProtKB Transmembrane 154 174 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06346 UniProtKB Region 176 221 . . . Note=COPI vesicle-binding +Q06346 UniProtKB Mutagenesis 103 103 . . . Note=Decreases ICP synthase activity. F->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19726565;Dbxref=PMID:19726565 +Q06346 UniProtKB Mutagenesis 135 135 . . . Note=Impairs cleavage by KEX2. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19726565;Dbxref=PMID:19726565 +##sequence-region P36004 1 724 +P36004 UniProtKB Chain 1 724 . . . ID=PRO_0000086151;Note=Probable serine/threonine-protein kinase KKQ8 +P36004 UniProtKB Domain 412 712 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P36004 UniProtKB Nucleotide binding 418 426 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P36004 UniProtKB Active site 563 563 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P36004 UniProtKB Binding site 455 455 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P36004 UniProtKB Modified residue 19 19 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P36004 UniProtKB Modified residue 232 232 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P36004 UniProtKB Modified residue 238 238 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P36004 UniProtKB Modified residue 241 241 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region P32350 1 737 +P32350 UniProtKB Chain 1 737 . . . ID=PRO_0000086155;Note=Dual specificity protein kinase KNS1 +P32350 UniProtKB Domain 313 720 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32350 UniProtKB Nucleotide binding 319 327 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32350 UniProtKB Compositional bias 143 146 . . . Note=Poly-Ser +P32350 UniProtKB Compositional bias 148 152 . . . Note=Poly-Asn +P32350 UniProtKB Compositional bias 673 679 . . . Note=Ser/Thr-rich +P32350 UniProtKB Active site 440 440 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P32350 UniProtKB Binding site 343 343 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32350 UniProtKB Modified residue 562 562 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32350 UniProtKB Sequence conflict 411 421 . . . Note=RFPGSHIQAIA->GSPALISGHC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32895 1 427 +P32895 UniProtKB Chain 1 427 . . . ID=PRO_0000141086;Note=Ribose-phosphate pyrophosphokinase 1 +P32895 UniProtKB Metal binding 128 128 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32895 UniProtKB Metal binding 130 130 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32895 UniProtKB Metal binding 143 143 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32895 UniProtKB Modified residue 199 199 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P32895 UniProtKB Modified residue 218 218 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32895 UniProtKB Modified residue 271 271 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32895 UniProtKB Modified residue 295 295 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P53158 1 218 +P53158 UniProtKB Chain 1 218 . . . ID=PRO_0000202759;Note=Biogenesis of lysosome-related organelles complex 1 subunit KXD1 +P53158 UniProtKB Coiled coil 142 192 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53158 UniProtKB Motif 175 179 . . . Note=KxDL +P53158 UniProtKB Compositional bias 16 64 . . . Note=Ser-rich +##sequence-region P40970 1 561 +P40970 UniProtKB Chain 1 561 . . . ID=PRO_0000163862;Note=Serine palmitoyltransferase 2 +P40970 UniProtKB Transmembrane 57 77 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40970 UniProtKB Transmembrane 443 463 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40970 UniProtKB Modified residue 366 366 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40970 UniProtKB Mutagenesis 334 334 . . . Note=Loss of activity. No effect on interaction with LCB1. H->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11781309;Dbxref=PMID:11781309 +P40970 UniProtKB Mutagenesis 366 366 . . . Note=Loss of activity. No effect on interaction with LCB1. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11781309;Dbxref=PMID:11781309 +P40970 UniProtKB Sequence conflict 5 6 . . . Note=AN->PH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40970 UniProtKB Sequence conflict 23 23 . . . Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40970 UniProtKB Sequence conflict 236 236 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40970 UniProtKB Sequence conflict 441 441 . . . Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39002 1 694 +P39002 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P39002 UniProtKB Chain 2 694 . . . ID=PRO_0000193121;Note=Long-chain-fatty-acid--CoA ligase 3 +P39002 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P40079 1 357 +P40079 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40079 UniProtKB Chain 2 357 . . . ID=PRO_0000084370;Note=U3 small nucleolar ribonucleoprotein protein LCP5 +P40079 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P25587 1 256 +P25587 UniProtKB Chain 1 256 . . . ID=PRO_0000202538;Note=Protein LDB16 +P25587 UniProtKB Transmembrane 1 21 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25587 UniProtKB Transmembrane 22 42 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25587 UniProtKB Topological domain 43 75 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25587 UniProtKB Transmembrane 76 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25587 UniProtKB Topological domain 97 256 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25587 UniProtKB Modified residue 180 180 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25587 UniProtKB Modified residue 184 184 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25587 UniProtKB Modified residue 241 241 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +##sequence-region Q02799 1 301 +Q02799 UniProtKB Chain 1 301 . . . ID=PRO_0000213909;Note=Zinc finger protein LEE1 +Q02799 UniProtKB Zinc finger 87 114 . . . Note=C3H1-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 +Q02799 UniProtKB Zinc finger 123 145 . . . Note=C3H1-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 +Q02799 UniProtKB Modified residue 21 21 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02799 UniProtKB Modified residue 30 30 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02799 UniProtKB Modified residue 282 282 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02799 UniProtKB Sequence conflict 198 198 . . . Note=Y->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12166 1 604 +Q12166 UniProtKB Transit peptide 1 50 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12166 UniProtKB Chain 51 604 . . . ID=PRO_0000255958;Note=2-isopropylmalate synthase 2%2C mitochondrial +Q12166 UniProtKB Domain 60 335 . . . Note=Pyruvate carboxyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01151 +##sequence-region P50107 1 326 +P50107 UniProtKB Chain 1 326 . . . ID=PRO_0000168087;Note=Lactoylglutathione lyase +P50107 UniProtKB Domain 22 167 . . . Note=VOC 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01163 +P50107 UniProtKB Domain 182 322 . . . Note=VOC 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01163 +P50107 UniProtKB Active site 163 163 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50107 UniProtKB Metal binding 25 25 . . . Note=Zinc%3B via tele nitrogen%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50107 UniProtKB Metal binding 89 89 . . . Note=Zinc%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50107 UniProtKB Metal binding 117 117 . . . Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50107 UniProtKB Metal binding 163 163 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50107 UniProtKB Binding site 29 29 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50107 UniProtKB Binding site 93 93 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50107 UniProtKB Binding site 113 113 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50107 UniProtKB Binding site 117 117 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P50107 UniProtKB Sequence conflict 36 36 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P50107 UniProtKB Sequence conflict 156 156 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P50107 UniProtKB Sequence conflict 156 156 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P50107 UniProtKB Sequence conflict 322 322 . . . Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06005 1 328 +Q06005 UniProtKB Domain 108 312 . . . Note=BPL/LPL catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01067 +Q06005 UniProtKB Region 162 169 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06005 UniProtKB Region 241 243 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06005 UniProtKB Region 254 256 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06005 UniProtKB Active site 272 272 . . . Note=Acyl-thioester intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06005 UniProtKB Site 238 238 . . . Note=Lowers pKa of active site Cys;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38878 1 278 +P38878 UniProtKB Chain 1 278 . . . ID=PRO_0000202936;Note=Protein lunapark +P38878 UniProtKB Topological domain 1 45 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38878 UniProtKB Transmembrane 46 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38878 UniProtKB Topological domain 67 77 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38878 UniProtKB Transmembrane 78 98 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38878 UniProtKB Topological domain 99 278 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38878 UniProtKB Zinc finger 223 247 . . . Note=C4-type%3B plays a role in ER morphology +P38878 UniProtKB Coiled coil 107 183 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38878 UniProtKB Mutagenesis 223 223 . . . Note=In lnp1-1%3B causes aberrant ER morphology%3B when associaetd with A-226%2C A-244 and A-247. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22729086;Dbxref=PMID:22729086 +P38878 UniProtKB Mutagenesis 226 226 . . . Note=In lnp1-1%3B causes aberrant ER morphology%3B when associaetd with A-223%2C A-244 and A-247. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22729086;Dbxref=PMID:22729086 +P38878 UniProtKB Mutagenesis 244 244 . . . Note=In lnp1-1%3B causes aberrant ER morphology%3B when associaetd with A-223%2C A-226 and A-247. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22729086;Dbxref=PMID:22729086 +P38878 UniProtKB Mutagenesis 247 247 . . . Note=In lnp1-1%3B causes aberrant ER morphology%3B when associaetd with A-223%2C A-226 and A-244. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22729086;Dbxref=PMID:22729086 +##sequence-region Q04396 1 274 +Q04396 UniProtKB Chain 1 274 . . . ID=PRO_0000220919;Note=Lipid phosphate phosphatase 1 +Q04396 UniProtKB Topological domain 1 15 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04396 UniProtKB Transmembrane 16 33 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04396 UniProtKB Topological domain 34 69 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04396 UniProtKB Transmembrane 70 87 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04396 UniProtKB Topological domain 88 117 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04396 UniProtKB Transmembrane 118 139 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04396 UniProtKB Topological domain 140 189 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04396 UniProtKB Transmembrane 190 203 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04396 UniProtKB Topological domain 204 214 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04396 UniProtKB Transmembrane 215 231 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04396 UniProtKB Topological domain 232 237 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04396 UniProtKB Transmembrane 238 255 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04396 UniProtKB Topological domain 256 274 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04396 UniProtKB Region 136 144 . . . Note=Phosphatase sequence motif I +Q04396 UniProtKB Region 186 189 . . . Note=Phosphatase sequence motif II +Q04396 UniProtKB Region 228 239 . . . Note=Phosphatase sequence motif III +##sequence-region P53281 1 241 +P53281 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53281 UniProtKB Chain 2 241 . . . ID=PRO_0000202825;Note=LAS seventeen-binding protein 1 +P53281 UniProtKB Domain 53 112 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P53281 UniProtKB Motif 135 138 . . . Note=PY motif +P53281 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53281 UniProtKB Modified residue 48 48 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53281 UniProtKB Modified residue 114 114 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P53281 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P53281 UniProtKB Cross-link 41 41 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P53281 UniProtKB Cross-link 79 79 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P53281 UniProtKB Cross-link 118 118 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P53281 UniProtKB Cross-link 219 219 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P53281 UniProtKB Mutagenesis 90 90 . . . Note=Abolishes interaction with LAS17%2C but not with SUP35. Blocks colocalization with actin. W->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21777813;Dbxref=PMID:21777813 +##sequence-region P42838 1 414 +P42838 UniProtKB Chain 1 414 . . . ID=PRO_0000207671;Note=Alkylphosphocholine resistance protein LEM3 +P42838 UniProtKB Transmembrane 75 95 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42838 UniProtKB Transmembrane 373 393 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42838 UniProtKB Modified residue 36 36 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P42838 UniProtKB Glycosylation 113 113 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42838 UniProtKB Glycosylation 240 240 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42838 UniProtKB Glycosylation 256 256 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42838 UniProtKB Glycosylation 279 279 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42838 UniProtKB Glycosylation 298 298 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42838 UniProtKB Glycosylation 332 332 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P06208 1 619 +P06208 UniProtKB Chain 1 619 . . . ID=PRO_0000001046;Note=2-isopropylmalate synthase +P06208 UniProtKB Domain 61 336 . . . Note=Pyruvate carboxyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01151 +P06208 UniProtKB Alternative sequence 1 30 . . . ID=VSP_018640;Note=In isoform Cytoplasmic. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32875 1 414 +P32875 UniProtKB Transit peptide 1 18 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03123 +P32875 UniProtKB Chain 19 414 . . . ID=PRO_0000017726;Note=Lipoyl synthase%2C mitochondrial +P32875 UniProtKB Metal binding 150 150 . . . Note=Iron-sulfur 1 (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03123 +P32875 UniProtKB Metal binding 155 155 . . . Note=Iron-sulfur 1 (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03123 +P32875 UniProtKB Metal binding 161 161 . . . Note=Iron-sulfur 1 (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03123 +P32875 UniProtKB Metal binding 181 181 . . . Note=Iron-sulfur 2 (4Fe-4S-S-AdoMet);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03123 +P32875 UniProtKB Metal binding 185 185 . . . Note=Iron-sulfur 2 (4Fe-4S-S-AdoMet);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03123 +P32875 UniProtKB Metal binding 188 188 . . . Note=Iron-sulfur 2 (4Fe-4S-S-AdoMet);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03123 +##sequence-region P36775 1 1133 +P36775 UniProtKB Transit peptide 1 37 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03120 +P36775 UniProtKB Propeptide 38 98 . . . ID=PRO_0000395761;Note=Removed in mature form%3B by autocatalysis;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03120,ECO:0000269|PubMed:9405361,ECO:0000269|PubMed:9724747;Dbxref=PMID:9405361,PMID:9724747 +P36775 UniProtKB Chain 99 1133 . . . ID=PRO_0000026733;Note=Lon protease homolog%2C mitochondrial +P36775 UniProtKB Domain 182 478 . . . Note=Lon N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01123 +P36775 UniProtKB Domain 923 1109 . . . Note=Lon proteolytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01122 +P36775 UniProtKB Nucleotide binding 632 639 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03120 +P36775 UniProtKB Active site 1015 1015 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03120 +P36775 UniProtKB Active site 1058 1058 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03120 +P36775 UniProtKB Mutagenesis 638 638 . . . Note=Abolishes ATP-binding. K->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8810243,ECO:0000269|PubMed:9405361;Dbxref=PMID:8810243,PMID:9405361 +P36775 UniProtKB Mutagenesis 1015 1015 . . . Note=Abolishes peptidase activity. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8810243,ECO:0000269|PubMed:9405361;Dbxref=PMID:8810243,PMID:9405361 +P36775 UniProtKB Sequence conflict 509 509 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38131 1 464 +P38131 UniProtKB Chain 1 464 . . . ID=PRO_0000208245;Note=Probable mannosyltransferase KTR4 +P38131 UniProtKB Topological domain 1 11 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38131 UniProtKB Transmembrane 12 32 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38131 UniProtKB Topological domain 33 464 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38131 UniProtKB Region 33 130 . . . Note=Stem region;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38131 UniProtKB Region 131 464 . . . Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38131 UniProtKB Active site 352 352 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38131 UniProtKB Helix 71 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 95 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Turn 128 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Beta strand 133 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 146 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Beta strand 168 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 178 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Beta strand 194 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 201 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 212 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Turn 228 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 233 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 250 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Beta strand 256 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 275 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Beta strand 286 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Beta strand 291 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 296 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 302 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 314 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 323 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 333 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Beta strand 345 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Beta strand 351 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 356 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 362 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 376 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 384 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 398 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Beta strand 401 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Beta strand 409 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Beta strand 414 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Beta strand 429 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 440 445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 448 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +P38131 UniProtKB Helix 458 461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A07 +##sequence-region Q08218 1 356 +Q08218 UniProtKB Chain 1 356 . . . ID=PRO_0000235923;Note=Outer spore wall protein LDS2 +Q08218 UniProtKB Topological domain 1 92 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31379 +Q08218 UniProtKB Transmembrane 93 113 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08218 UniProtKB Topological domain 114 115 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31379 +Q08218 UniProtKB Transmembrane 116 136 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08218 UniProtKB Topological domain 137 213 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31379 +Q08218 UniProtKB Transmembrane 214 234 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08218 UniProtKB Topological domain 235 294 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31379 +Q08218 UniProtKB Transmembrane 295 315 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08218 UniProtKB Topological domain 316 356 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31379 +##sequence-region P28742 1 1111 +P28742 UniProtKB Chain 1 1111 . . . ID=PRO_0000125369;Note=Kinesin-like protein KIP1 +P28742 UniProtKB Domain 52 410 . . . Note=Kinesin motor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283 +P28742 UniProtKB Nucleotide binding 141 148 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283 +P28742 UniProtKB Coiled coil 424 510 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28742 UniProtKB Coiled coil 648 670 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28742 UniProtKB Coiled coil 710 780 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28742 UniProtKB Coiled coil 808 828 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38169 1 460 +P38169 UniProtKB Chain 1 460 . . . ID=PRO_0000020823;Note=Kynurenine 3-monooxygenase +P38169 UniProtKB Beta strand 4 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Helix 12 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 27 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 50 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Helix 56 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Helix 67 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Turn 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 82 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 92 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 99 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J34 +P38169 UniProtKB Beta strand 104 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Helix 109 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Turn 121 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 126 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 131 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 143 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Turn 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 156 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Helix 173 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 185 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 194 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Turn 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 211 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 220 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 230 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 241 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Helix 249 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Helix 259 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Helix 271 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Turn 274 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Helix 279 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 295 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 302 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J36 +P38169 UniProtKB Turn 305 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Beta strand 309 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Helix 314 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Turn 321 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Helix 326 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Turn 344 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Helix 348 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +P38169 UniProtKB Turn 384 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J33 +##sequence-region P38620 1 318 +P38620 UniProtKB Chain 1 318 . . . ID=PRO_0000141087;Note=Ribose-phosphate pyrophosphokinase 2 +P38620 UniProtKB Metal binding 132 132 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38620 UniProtKB Metal binding 134 134 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38620 UniProtKB Metal binding 143 143 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38620 UniProtKB Metal binding 147 147 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12265 1 496 +Q12265 UniProtKB Chain 1 496 . . . ID=PRO_0000141090;Note=Ribose-phosphate pyrophosphokinase 5 +Q12265 UniProtKB Metal binding 242 242 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12265 UniProtKB Metal binding 244 244 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12265 UniProtKB Metal binding 253 253 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12265 UniProtKB Metal binding 257 257 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12265 UniProtKB Modified residue 119 119 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12265 UniProtKB Modified residue 120 120 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12265 UniProtKB Modified residue 123 123 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q12265 UniProtKB Modified residue 127 127 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +Q12265 UniProtKB Modified residue 183 183 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358;Dbxref=PMID:15665377,PMID:17287358 +Q12265 UniProtKB Modified residue 332 332 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P34253 1 313 +P34253 UniProtKB Chain 1 313 . . . ID=PRO_0000084335;Note=Protein KTI12 +P34253 UniProtKB Nucleotide binding 8 15 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34253 UniProtKB Sequence conflict 103 103 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P34253 UniProtKB Sequence conflict 150 150 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P27810 1 393 +P27810 UniProtKB Chain 1 393 . . . ID=PRO_0000208242;Note=Alpha-1%2C2 mannosyltransferase KTR1 +P27810 UniProtKB Topological domain 1 16 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27810 UniProtKB Transmembrane 17 34 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27810 UniProtKB Topological domain 35 393 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27810 UniProtKB Region 35 68 . . . Note=Stem region;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P27810 UniProtKB Region 69 393 . . . Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P27810 UniProtKB Active site 280 280 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27810 UniProtKB Glycosylation 120 120 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q92325 1 660 +Q92325 UniProtKB Chain 1 660 . . . ID=PRO_0000084352;Note=Cullin-associated NEDD8-dissociated protein 1 homolog +Q92325 UniProtKB Compositional bias 344 393 . . . Note=Asp-rich +Q92325 UniProtKB Cross-link 16 16 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) +Q92325 UniProtKB Mutagenesis 16 16 . . . Note=Does not affect interaction with CDC53. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19942853;Dbxref=PMID:19942853 +Q92325 UniProtKB Mutagenesis 17 23 . . . Note=Decreased interaction with CDC53. DNDLKYM->ANALKAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19942853;Dbxref=PMID:19942853 +Q92325 UniProtKB Mutagenesis 551 552 . . . Note=Decreased interaction with CDC53. GN->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19942853;Dbxref=PMID:19942853 +Q92325 UniProtKB Sequence conflict 13 13 . . . Note=R->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q92325 UniProtKB Sequence conflict 156 157 . . . Note=QL->HV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q92325 UniProtKB Sequence conflict 486 491 . . . Note=CTLAHT->VSYAI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12446 1 633 +Q12446 UniProtKB Chain 1 633 . . . ID=PRO_0000084361;Note=Proline-rich protein LAS17 +Q12446 UniProtKB Domain 16 127 . . . Note=WH1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00410 +Q12446 UniProtKB Domain 547 567 . . . Note=WH2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00406 +Q12446 UniProtKB Compositional bias 185 529 . . . Note=Pro-rich +Q12446 UniProtKB Compositional bias 185 190 . . . Note=Poly-Pro +Q12446 UniProtKB Compositional bias 323 329 . . . Note=Poly-Pro +Q12446 UniProtKB Compositional bias 342 348 . . . Note=Poly-Pro +Q12446 UniProtKB Compositional bias 352 358 . . . Note=Poly-Pro +Q12446 UniProtKB Compositional bias 385 391 . . . Note=Poly-Pro +Q12446 UniProtKB Compositional bias 427 431 . . . Note=Poly-Pro +Q12446 UniProtKB Compositional bias 470 474 . . . Note=Poly-Pro +Q12446 UniProtKB Compositional bias 503 507 . . . Note=Poly-Pro +Q12446 UniProtKB Compositional bias 520 526 . . . Note=Poly-Pro +Q12446 UniProtKB Modified residue 334 334 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12446 UniProtKB Modified residue 337 337 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12446 UniProtKB Modified residue 588 588 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P00572 1 216 +P00572 UniProtKB Chain 1 216 . . . ID=PRO_0000155214;Note=Thymidylate kinase +P00572 UniProtKB Nucleotide binding 12 19 . . . Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00572 UniProtKB Sequence conflict 57 57 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00572 UniProtKB Sequence conflict 188 188 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00572 UniProtKB Beta strand 7 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK +P00572 UniProtKB Beta strand 14 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK +P00572 UniProtKB Helix 18 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK +P00572 UniProtKB Beta strand 31 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK +P00572 UniProtKB Helix 44 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK +P00572 UniProtKB Helix 62 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK +P00572 UniProtKB Helix 77 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK +P00572 UniProtKB Beta strand 89 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK +P00572 UniProtKB Helix 96 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK +P00572 UniProtKB Helix 113 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK +P00572 UniProtKB Helix 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK +P00572 UniProtKB Beta strand 123 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2TMK +P00572 UniProtKB Beta strand 127 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK +P00572 UniProtKB Helix 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK +P00572 UniProtKB Beta strand 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK +P00572 UniProtKB Helix 154 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK +P00572 UniProtKB Beta strand 178 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK +P00572 UniProtKB Helix 189 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TMK +##sequence-region P31379 1 325 +P31379 UniProtKB Chain 1 325 . . . ID=PRO_0000202413;Note=Outer spore wall protein LDS1 +P31379 UniProtKB Topological domain 1 91 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P31379 UniProtKB Transmembrane 92 112 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31379 UniProtKB Topological domain 113 118 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P31379 UniProtKB Transmembrane 119 139 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31379 UniProtKB Topological domain 140 208 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P31379 UniProtKB Transmembrane 209 229 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31379 UniProtKB Topological domain 230 263 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P31379 UniProtKB Transmembrane 264 284 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31379 UniProtKB Topological domain 285 325 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +##sequence-region P04173 1 364 +P04173 UniProtKB Chain 1 364 . . . ID=PRO_0000083623;Note=3-isopropylmalate dehydrogenase +P04173 UniProtKB Nucleotide binding 79 90 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04173 UniProtKB Nucleotide binding 289 300 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04173 UniProtKB Metal binding 225 225 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04173 UniProtKB Metal binding 250 250 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04173 UniProtKB Metal binding 254 254 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04173 UniProtKB Binding site 97 97 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04173 UniProtKB Binding site 107 107 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04173 UniProtKB Binding site 136 136 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04173 UniProtKB Binding site 225 225 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04173 UniProtKB Site 143 143 . . . Note=Important for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04173 UniProtKB Site 192 192 . . . Note=Important for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04173 UniProtKB Sequence conflict 69 69 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04173 UniProtKB Sequence conflict 69 69 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04173 UniProtKB Sequence conflict 69 69 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04173 UniProtKB Sequence conflict 300 300 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04173 UniProtKB Sequence conflict 300 300 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38702 1 357 +P38702 UniProtKB Chain 1 357 . . . ID=PRO_0000090683;Note=Mitochondrial carrier protein LEU5 +P38702 UniProtKB Transmembrane 31 47 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38702 UniProtKB Transmembrane 103 119 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38702 UniProtKB Transmembrane 136 153 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38702 UniProtKB Transmembrane 208 228 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38702 UniProtKB Transmembrane 269 285 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38702 UniProtKB Transmembrane 325 347 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38702 UniProtKB Repeat 31 122 . . . Note=Solcar 1 +P38702 UniProtKB Repeat 130 231 . . . Note=Solcar 2 +P38702 UniProtKB Repeat 262 354 . . . Note=Solcar 3 +##sequence-region P07264 1 779 +P07264 UniProtKB Chain 1 779 . . . ID=PRO_0000076894;Note=3-isopropylmalate dehydratase +P07264 UniProtKB Metal binding 360 360 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07264 UniProtKB Metal binding 421 421 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07264 UniProtKB Metal binding 424 424 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07264 UniProtKB Modified residue 488 488 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P07264 UniProtKB Modified residue 494 494 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07264 UniProtKB Modified residue 495 495 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07264 UniProtKB Sequence conflict 291 291 . . . Note=N->TLKH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07264 UniProtKB Sequence conflict 423 423 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07264 UniProtKB Sequence conflict 459 459 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07264 UniProtKB Sequence conflict 744 744 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07264 UniProtKB Sequence conflict 744 744 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02796 1 332 +Q02796 UniProtKB Chain 1 332 . . . ID=PRO_0000076234;Note=Transcriptional regulatory protein LGE1 +Q02796 UniProtKB Coiled coil 284 328 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02796 UniProtKB Sequence conflict 28 28 . . . Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53966 1 522 +P53966 UniProtKB Chain 1 522 . . . ID=PRO_0000208246;Note=Probable mannosyltransferase KTR5 +P53966 UniProtKB Topological domain 1 16 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53966 UniProtKB Transmembrane 17 37 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53966 UniProtKB Topological domain 38 522 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53966 UniProtKB Region 38 82 . . . Note=Stem region;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53966 UniProtKB Region 83 522 . . . Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53966 UniProtKB Active site 363 363 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53966 UniProtKB Glycosylation 86 86 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32807 1 602 +P32807 UniProtKB Chain 1 602 . . . ID=PRO_0000210184;Note=ATP-dependent DNA helicase II subunit 1 +P32807 UniProtKB Domain 268 483 . . . Note=Ku +P32807 UniProtKB Modified residue 370 370 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32807 UniProtKB Modified residue 371 371 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32807 UniProtKB Modified residue 372 372 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32807 UniProtKB Natural variant 21 21 . . . Note=In strain: ABYS 60 and SK1. T->K +P32807 UniProtKB Natural variant 50 50 . . . Note=In strain: ABYS 60%2C DBVPG6044%2C SK1 and YPS128. E->D +P32807 UniProtKB Natural variant 230 230 . . . Note=In strain: DBVPG6044. T->A +P32807 UniProtKB Natural variant 368 368 . . . Note=In strain: YPS128. F->I +P32807 UniProtKB Natural variant 562 562 . . . Note=In strain: ABYS 60%2C DBVPG6044%2C SK1 and YPS128. I->T +P32807 UniProtKB Sequence conflict 3 3 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32807 UniProtKB Sequence conflict 87 87 . . . Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25045 1 558 +P25045 UniProtKB Chain 1 558 . . . ID=PRO_0000163856;Note=Serine palmitoyltransferase 1 +P25045 UniProtKB Topological domain 1 49 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854 +P25045 UniProtKB Transmembrane 50 84 . . . Note=Helical +P25045 UniProtKB Topological domain 85 341 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854 +P25045 UniProtKB Transmembrane 342 371 . . . Note=Helical +P25045 UniProtKB Topological domain 372 424 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854 +P25045 UniProtKB Transmembrane 425 457 . . . Note=Helical +P25045 UniProtKB Topological domain 458 558 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854 +P25045 UniProtKB Modified residue 121 121 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P25045 UniProtKB Mutagenesis 24 26 . . . Note=No effect on stability. No effect on LCB2 stabilization. YLW->DRS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854 +P25045 UniProtKB Mutagenesis 50 85 . . . Note=No effect on stability. No effect on LCB2 stabilization. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854 +P25045 UniProtKB Mutagenesis 66 68 . . . Note=No effect on stability. No effect on LCB2 stabilization. YGI->DVK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854 +P25045 UniProtKB Mutagenesis 180 180 . . . Note=Loss of activity. No effect on interaction with LCB2. C->W%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11781309;Dbxref=PMID:11781309 +P25045 UniProtKB Mutagenesis 191 191 . . . Note=Loss of activity. No effect on interaction with LCB2. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11781309;Dbxref=PMID:11781309 +P25045 UniProtKB Mutagenesis 342 371 . . . Note=Unstable. Destabilizes LCB2. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854 +P25045 UniProtKB Mutagenesis 371 386 . . . Note=No effect on stability. Destabilizes LCB2. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854 +P25045 UniProtKB Mutagenesis 386 416 . . . Note=Unstable. Destabilizes LCB2. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854 +P25045 UniProtKB Mutagenesis 416 425 . . . Note=No effect on stability. Destabilizes LCB2. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854 +P25045 UniProtKB Mutagenesis 433 458 . . . Note=Unstable. Destabilizes LCB2. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854 +P25045 UniProtKB Mutagenesis 549 550 . . . Note=No effect on stability. Partially stabilizes LCB2. IL->AS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854 +P25045 UniProtKB Mutagenesis 549 550 . . . Note=No effect on stability. Partially stabilizes LCB2. IL->PR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15485854;Dbxref=PMID:15485854 +P25045 UniProtKB Sequence conflict 443 443 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06147 1 687 +Q06147 UniProtKB Chain 1 687 . . . ID=PRO_0000255957;Note=Sphingoid long chain base kinase 5 +Q06147 UniProtKB Domain 266 405 . . . Note=DAGKc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 +Q06147 UniProtKB Nucleotide binding 276 278 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 +Q06147 UniProtKB Nucleotide binding 366 368 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 +Q06147 UniProtKB Nucleotide binding 652 654 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 +Q06147 UniProtKB Region 333 336 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06147 UniProtKB Active site 335 335 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06147 UniProtKB Binding site 308 308 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 +Q06147 UniProtKB Binding site 340 340 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 +Q06147 UniProtKB Binding site 434 434 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 +Q06147 UniProtKB Binding site 440 440 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 +Q06147 UniProtKB Lipidation 91 91 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06147 UniProtKB Lipidation 94 94 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53153 1 274 +P53153 UniProtKB Chain 1 274 . . . ID=PRO_0000215285;Note=Probable endonuclease LCL3 +P53153 UniProtKB Transmembrane 15 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53153 UniProtKB Domain 53 261 . . . Note=TNase-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00272 +P53153 UniProtKB Active site 151 151 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00272 +P53153 UniProtKB Active site 159 159 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00272 +P53153 UniProtKB Active site 199 199 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00272 +P53153 UniProtKB Metal binding 156 156 . . . Note=Calcium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00272 +##sequence-region Q04081 1 328 +Q04081 UniProtKB Chain 1 328 . . . ID=PRO_0000226135;Note=Leucine carboxyl methyltransferase 1 +Q04081 UniProtKB Region 175 177 . . . Note=S-adenosyl-L-methionine binding +Q04081 UniProtKB Binding site 81 81 . . . Note=S-adenosyl-L-methionine +Q04081 UniProtKB Binding site 105 105 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen +Q04081 UniProtKB Binding site 128 128 . . . Note=S-adenosyl-L-methionine +Q04081 UniProtKB Binding site 201 201 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen +Q04081 UniProtKB Helix 3 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Helix 8 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Turn 28 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Helix 35 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Helix 57 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Helix 72 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Beta strand 97 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Helix 112 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Beta strand 122 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Helix 130 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Helix 144 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Beta strand 162 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Beta strand 167 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Beta strand 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJG +Q04081 UniProtKB Helix 179 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Beta strand 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJE +Q04081 UniProtKB Beta strand 196 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Helix 204 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Helix 209 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Beta strand 224 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Helix 243 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Turn 260 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Helix 268 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Helix 273 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Beta strand 278 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Helix 286 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Helix 296 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Helix 311 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +Q04081 UniProtKB Beta strand 321 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJD +##sequence-region P08638 1 886 +P08638 UniProtKB Chain 1 886 . . . ID=PRO_0000114954;Note=Regulatory protein LEU3 +P08638 UniProtKB DNA binding 37 67 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P08638 UniProtKB Motif 874 882 . . . Note=9aaTAD +P08638 UniProtKB Compositional bias 678 697 . . . Note=Asp/Glu-rich (acidic) +P08638 UniProtKB Sequence conflict 504 504 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08638 UniProtKB Helix 38 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ER8 +P08638 UniProtKB Helix 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ER8 +P08638 UniProtKB Helix 58 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ER8 +P08638 UniProtKB Helix 78 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ER8 +##sequence-region P36016 1 881 +P36016 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36016 UniProtKB Chain 21 881 . . . ID=PRO_0000013556;Note=Heat shock protein 70 homolog LHS1 +P36016 UniProtKB Motif 878 881 . . . Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10138 +P36016 UniProtKB Glycosylation 128 128 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36016 UniProtKB Glycosylation 458 458 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36016 UniProtKB Glycosylation 474 474 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36016 UniProtKB Glycosylation 481 481 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36016 UniProtKB Glycosylation 489 489 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36016 UniProtKB Glycosylation 527 527 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36016 UniProtKB Glycosylation 844 844 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36016 UniProtKB Mutagenesis 239 239 . . . Note=In allele LHS1-1%3B constitutive ATPase activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14704430;Dbxref=PMID:14704430 +##sequence-region Q04005 1 294 +Q04005 UniProtKB Chain 1 294 . . . ID=PRO_0000076239;Note=Protein ATC1/LIC4 +Q04005 UniProtKB Sequence conflict 204 204 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39946 1 494 +P39946 UniProtKB Chain 1 494 . . . ID=PRO_0000051113;Note=Nuclear distribution protein PAC1 +P39946 UniProtKB Domain 14 46 . . . Note=LisH;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03141 +P39946 UniProtKB Repeat 153 192 . . . Note=WD 1 +P39946 UniProtKB Repeat 196 244 . . . Note=WD 2 +P39946 UniProtKB Repeat 251 292 . . . Note=WD 3 +P39946 UniProtKB Repeat 295 334 . . . Note=WD 4 +P39946 UniProtKB Repeat 347 395 . . . Note=WD 5 +P39946 UniProtKB Repeat 415 454 . . . Note=WD 6 +P39946 UniProtKB Repeat 457 492 . . . Note=WD 7 +P39946 UniProtKB Coiled coil 90 123 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03141 +##sequence-region Q10740 1 671 +Q10740 UniProtKB Chain 1 671 . . . ID=PRO_0000095129;Note=Leukotriene A-4 hydrolase homolog +Q10740 UniProtKB Region 184 186 . . . Note=Substrate binding +Q10740 UniProtKB Region 311 316 . . . Note=Substrate binding +Q10740 UniProtKB Active site 341 341 . . . Note=Proton acceptor +Q10740 UniProtKB Active site 429 429 . . . Note=Proton donor +Q10740 UniProtKB Metal binding 340 340 . . . Note=Zinc%3B catalytic +Q10740 UniProtKB Metal binding 344 344 . . . Note=Zinc%3B catalytic +Q10740 UniProtKB Metal binding 363 363 . . . Note=Zinc%3B catalytic +Q10740 UniProtKB Mutagenesis 244 244 . . . Note=Reduces strongly the substrate affinity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16597475;Dbxref=PMID:16597475 +Q10740 UniProtKB Mutagenesis 316 316 . . . Note=Abolishes the aminopeptidase activity. E->A%2CQ%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16024909;Dbxref=PMID:16024909 +Q10740 UniProtKB Mutagenesis 340 340 . . . Note=Abolishes the epoxide hydrolase and aminopeptidase activities. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11601994;Dbxref=PMID:11601994 +Q10740 UniProtKB Mutagenesis 341 341 . . . Note=Abolishes aminopeptidase activity. No effect on the epoxide hydrolase activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11601994;Dbxref=PMID:11601994 +Q10740 UniProtKB Mutagenesis 344 344 . . . Note=Abolishes the epoxide hydrolase and aminopeptidase activities. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11601994;Dbxref=PMID:11601994 +Q10740 UniProtKB Mutagenesis 363 363 . . . Note=Abolishes the epoxide hydrolase activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11601994;Dbxref=PMID:11601994 +Q10740 UniProtKB Mutagenesis 424 424 . . . Note=Increases the aminopeptidase activity and decreases the epoxide hydrolase activity. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11601994;Dbxref=PMID:11601994 +Q10740 UniProtKB Mutagenesis 429 429 . . . Note=Abolishes the aminopeptidase activity and decreases the epoxide hydrolase activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11601994;Dbxref=PMID:11601994 +Q10740 UniProtKB Mutagenesis 627 627 . . . Note=Abolishes the aminopeptidase activity. R->K%2CA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16024909;Dbxref=PMID:16024909 +Q10740 UniProtKB Helix 43 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 51 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 67 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Turn 80 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 84 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 99 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XPY +Q10740 UniProtKB Beta strand 105 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 111 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Turn 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 140 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 147 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 164 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Turn 171 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 175 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XPY +Q10740 UniProtKB Beta strand 180 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Turn 186 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 190 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 204 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 216 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 232 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 243 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 248 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 254 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 262 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 268 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Turn 279 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 282 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 297 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XPZ +Q10740 UniProtKB Beta strand 303 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 312 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 321 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 325 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 330 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 336 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Turn 348 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 351 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 356 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 360 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 380 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 401 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XPZ +Q10740 UniProtKB Helix 404 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 409 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 416 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 420 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 427 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 446 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Turn 460 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 463 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 467 477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 479 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 482 486 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 490 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 508 523 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Turn 524 526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 530 536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 539 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 547 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Beta strand 562 565 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XPZ +Q10740 UniProtKB Helix 572 574 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 576 585 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 587 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 596 608 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 612 614 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 615 621 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Turn 622 624 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 628 639 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 643 653 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 654 656 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +Q10740 UniProtKB Helix 659 668 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XQ0 +##sequence-region P40026 1 464 +P40026 UniProtKB Chain 1 464 . . . ID=PRO_0000084329;Note=DNA repair protein KRE29 +P40026 UniProtKB Modified residue 81 81 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40026 UniProtKB Modified residue 101 101 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P27809 1 442 +P27809 UniProtKB Chain 1 442 . . . ID=PRO_0000208241;Note=Glycolipid 2-alpha-mannosyltransferase +P27809 UniProtKB Topological domain 1 11 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27809 UniProtKB Transmembrane 12 30 . . . Note=Helical%3B Signal-anchor for type II membrane protein +P27809 UniProtKB Topological domain 31 442 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27809 UniProtKB Region 31 118 . . . Note=Stem region +P27809 UniProtKB Region 119 442 . . . Note=Catalytic +P27809 UniProtKB Active site 329 329 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27809 UniProtKB Glycosylation 197 197 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1550992;Dbxref=PMID:1550992 +P27809 UniProtKB Helix 106 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Beta strand 123 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 134 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Turn 148 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Beta strand 156 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 166 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Beta strand 180 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 198 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Turn 209 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Turn 213 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 218 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 231 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 235 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Beta strand 241 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 260 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Beta strand 271 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Beta strand 276 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 281 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 287 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 299 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 308 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Beta strand 322 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Beta strand 328 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 333 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 339 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 353 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 361 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 375 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Beta strand 378 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Beta strand 386 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Beta strand 391 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 398 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 410 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 422 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +P27809 UniProtKB Helix 437 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1S4N +##sequence-region P39005 1 276 +P39005 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39005 UniProtKB Chain 22 276 . . . ID=PRO_0000016849;Note=Cell wall synthesis protein KRE9 +##sequence-region P25586 1 316 +P25586 UniProtKB Chain 1 316 . . . ID=PRO_0000202553;Note=KRR1 small subunit processome component +P25586 UniProtKB Domain 122 192 . . . Note=KH +P25586 UniProtKB Mutagenesis 20 20 . . . Note=In temperature-sensitive mutant KRR1-17%3B grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius%3B when associated with N-66%3B R-162 and A-261. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11027267;Dbxref=PMID:11027267 +P25586 UniProtKB Mutagenesis 45 45 . . . Note=In temperature-sensitive mutant KRR1-18%3B grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius%3B when associated with S-95 and G-207. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11027267;Dbxref=PMID:11027267 +P25586 UniProtKB Mutagenesis 66 66 . . . Note=In temperature-sensitive mutant KRR1-17%3B grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius%3B when associated with E-20%3B R-162 and A-261. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11027267;Dbxref=PMID:11027267 +P25586 UniProtKB Mutagenesis 95 95 . . . Note=In temperature-sensitive mutant KRR1-18%3B grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius%3B when associated with L-45 and G-207. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11027267;Dbxref=PMID:11027267 +P25586 UniProtKB Mutagenesis 162 162 . . . Note=In temperature-sensitive mutant KRR1-17%3B grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius%3B when associated with E-20%3B N-66 and A-261. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11027267;Dbxref=PMID:11027267 +P25586 UniProtKB Mutagenesis 207 207 . . . Note=In temperature-sensitive mutant KRR1-18%3B grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius%3B when associated with L-45 and S-95. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11027267;Dbxref=PMID:11027267 +P25586 UniProtKB Mutagenesis 261 261 . . . Note=In temperature-sensitive mutant KRR1-17%3B grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius%3B when associated with E-20%3B N-66 and R-162. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11027267;Dbxref=PMID:11027267 +P25586 UniProtKB Beta strand 40 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Helix 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Helix 50 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Turn 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Beta strand 70 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Turn 75 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Beta strand 79 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Helix 93 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Helix 110 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Helix 114 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Beta strand 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Beta strand 122 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Beta strand 133 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Helix 136 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Helix 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Helix 151 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Beta strand 163 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Beta strand 170 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Helix 177 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +P25586 UniProtKB Helix 197 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QMF +##sequence-region P30624 1 700 +P30624 UniProtKB Chain 1 700 . . . ID=PRO_0000193119;Note=Long-chain-fatty-acid--CoA ligase 1 +P30624 UniProtKB Cross-link 189 189 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P32486 1 720 +P32486 UniProtKB Chain 1 720 . . . ID=PRO_0000084331;Note=Beta-glucan synthesis-associated protein KRE6 +P32486 UniProtKB Topological domain 1 252 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32486 UniProtKB Transmembrane 253 273 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32486 UniProtKB Topological domain 274 720 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32486 UniProtKB Domain 289 664 . . . Note=GH16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01098 +P32486 UniProtKB Modified residue 81 81 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32486 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32486 UniProtKB Modified residue 133 133 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32486 UniProtKB Modified residue 134 134 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32486 UniProtKB Modified residue 136 136 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32486 UniProtKB Modified residue 139 139 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32486 UniProtKB Glycosylation 374 374 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32486 UniProtKB Glycosylation 461 461 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32486 UniProtKB Glycosylation 538 538 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32486 UniProtKB Glycosylation 563 563 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32486 UniProtKB Glycosylation 691 691 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32486 UniProtKB Sequence conflict 310 310 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32486 UniProtKB Sequence conflict 310 310 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32486 UniProtKB Sequence conflict 483 483 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32486 UniProtKB Sequence conflict 483 483 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39526 1 2014 +P39526 UniProtKB Chain 1 2014 . . . ID=PRO_0000203015;Note=AP-1 accessory protein LAA1 +##sequence-region P47912 1 694 +P47912 UniProtKB Chain 1 694 . . . ID=PRO_0000193122;Note=Long-chain-fatty-acid--CoA ligase 4 +P47912 UniProtKB Sequence conflict 552 552 . . . Note=N->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47912 UniProtKB Sequence conflict 631 631 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P33399 1 275 +P33399 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P33399 UniProtKB Chain 2 275 . . . ID=PRO_0000207608;Note=La protein homolog +P33399 UniProtKB Domain 23 112 . . . Note=HTH La-type RNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00332 +P33399 UniProtKB Domain 123 216 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P33399 UniProtKB Motif 240 256 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33399 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P33399 UniProtKB Modified residue 15 15 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:11720288;Dbxref=PMID:17287358,PMID:18407956,PMID:11720288 +P33399 UniProtKB Modified residue 19 19 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:11720288;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198,PMID:11720288 +P33399 UniProtKB Modified residue 104 104 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23865587;Dbxref=PMID:23865587 +P33399 UniProtKB Modified residue 230 230 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P33399 UniProtKB Modified residue 233 233 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P33399 UniProtKB Modified residue 235 235 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000269|PubMed:11720288;Dbxref=PMID:17287358,PMID:11720288 +P33399 UniProtKB Mutagenesis 15 15 . . . Note=Prevents phosphorylation%3B when associated with A-19 and A-235. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11720288;Dbxref=PMID:11720288 +P33399 UniProtKB Mutagenesis 19 19 . . . Note=Prevents phosphorylation%3B when associated with A-15 and A-235. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11720288;Dbxref=PMID:11720288 +P33399 UniProtKB Mutagenesis 235 235 . . . Note=Prevents phosphorylation%3B when associated with A-15 and A-19. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11720288;Dbxref=PMID:11720288 +##sequence-region Q03579 1 150 +Q03579 UniProtKB Chain 1 150 . . . ID=PRO_0000203352;Note=Ceramide synthase subunit LIP1 +Q03579 UniProtKB Topological domain 1 20 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15692566;Dbxref=PMID:15692566 +Q03579 UniProtKB Transmembrane 21 40 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03579 UniProtKB Topological domain 41 150 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15692566;Dbxref=PMID:15692566 +##sequence-region Q05979 1 453 +Q05979 UniProtKB Chain 1 453 . . . ID=PRO_0000218665;Note=Kynureninase +Q05979 UniProtKB Region 139 142 . . . Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017 +Q05979 UniProtKB Binding site 111 111 . . . Note=Pyridoxal phosphate%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017 +Q05979 UniProtKB Binding site 112 112 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017 +Q05979 UniProtKB Binding site 196 196 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017 +Q05979 UniProtKB Binding site 226 226 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017 +Q05979 UniProtKB Binding site 229 229 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017 +Q05979 UniProtKB Binding site 251 251 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017 +Q05979 UniProtKB Binding site 286 286 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017 +Q05979 UniProtKB Binding site 314 314 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017 +Q05979 UniProtKB Modified residue 252 252 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03017 +##sequence-region P28496 1 418 +P28496 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P28496 UniProtKB Chain 2 418 . . . ID=PRO_0000185535;Note=Sphingosine N-acyltransferase LAC1 +P28496 UniProtKB Topological domain 2 81 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28496 UniProtKB Transmembrane 82 102 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28496 UniProtKB Topological domain 103 134 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28496 UniProtKB Transmembrane 135 155 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28496 UniProtKB Topological domain 156 172 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28496 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28496 UniProtKB Topological domain 194 221 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28496 UniProtKB Transmembrane 222 242 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28496 UniProtKB Topological domain 243 259 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28496 UniProtKB Transmembrane 260 280 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28496 UniProtKB Topological domain 281 296 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28496 UniProtKB Transmembrane 297 317 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28496 UniProtKB Topological domain 318 355 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28496 UniProtKB Transmembrane 356 376 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28496 UniProtKB Topological domain 377 418 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28496 UniProtKB Domain 168 384 . . . Note=TLC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00205 +P28496 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P28496 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38703 +P28496 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38703 +P28496 UniProtKB Glycosylation 103 103 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38703 1 411 +P38703 UniProtKB Chain 1 411 . . . ID=PRO_0000185527;Note=Sphingosine N-acyltransferase LAG1 +P38703 UniProtKB Topological domain 1 81 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38703 UniProtKB Transmembrane 82 102 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38703 UniProtKB Topological domain 103 134 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38703 UniProtKB Transmembrane 135 155 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38703 UniProtKB Topological domain 156 176 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38703 UniProtKB Transmembrane 177 197 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38703 UniProtKB Topological domain 198 211 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38703 UniProtKB Transmembrane 212 232 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38703 UniProtKB Topological domain 233 251 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38703 UniProtKB Transmembrane 252 272 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38703 UniProtKB Topological domain 273 296 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38703 UniProtKB Transmembrane 297 317 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38703 UniProtKB Topological domain 318 355 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38703 UniProtKB Transmembrane 356 376 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38703 UniProtKB Topological domain 377 411 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38703 UniProtKB Domain 168 384 . . . Note=TLC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00205 +P38703 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38703 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38703 UniProtKB Glycosylation 103 103 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38851 1 1228 +P38851 UniProtKB Chain 1 1228 . . . ID=PRO_0000202927;Note=Membrane-anchored lipid-binding protein LAM1 +P38851 UniProtKB Topological domain 1 1062 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26001273;Dbxref=PMID:26001273 +P38851 UniProtKB Transmembrane 1063 1083 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38851 UniProtKB Topological domain 1084 1228 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P38717 +P38851 UniProtKB Domain 308 421 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +P38851 UniProtKB Domain 773 978 . . . Note=VASt;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01114 +P38851 UniProtKB Glycosylation 1205 1205 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +##sequence-region Q08001 1 693 +Q08001 UniProtKB Chain 1 693 . . . ID=PRO_0000247247;Note=Membrane-anchored lipid-binding protein LAM6 +Q08001 UniProtKB Topological domain 1 630 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08001 UniProtKB Transmembrane 631 651 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08001 UniProtKB Topological domain 652 693 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08001 UniProtKB Domain 164 230 . . . Note=GRAM;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08001 UniProtKB Domain 403 576 . . . Note=VASt;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01114 +Q08001 UniProtKB Compositional bias 347 360 . . . Note=Poly-Ser +Q08001 UniProtKB Modified residue 343 343 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q08001 UniProtKB Modified residue 591 591 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q08001 UniProtKB Modified residue 593 593 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08001 UniProtKB Modified residue 594 594 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q08001 UniProtKB Modified residue 597 597 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region Q04377 1 747 +Q04377 UniProtKB Chain 1 747 . . . ID=PRO_0000227715;Note=DNA damage checkpoint protein LCD1 +Q04377 UniProtKB Coiled coil 62 139 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04377 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04377 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04377 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04377 UniProtKB Mutagenesis 177 177 . . . Note=Impairs dsDNA and ssDNA binding of the MEC1-LCD1 complex. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983176;Dbxref=PMID:11983176 +Q04377 UniProtKB Mutagenesis 179 179 . . . Note=Impairs dsDNA and ssDNA binding of the MEC1-LCD1 complex. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983176;Dbxref=PMID:11983176 +##sequence-region Q02786 1 101 +Q02786 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02786 UniProtKB Chain 18 81 . . . ID=PRO_0000238639;Note=Long chronological lifespan protein 1 +Q02786 UniProtKB Propeptide 82 101 . . . ID=PRO_0000238640;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02786 UniProtKB Lipidation 81 81 . . . Note=GPI-anchor amidated serine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08045 1 131 +Q08045 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08045 UniProtKB Chain 25 131 . . . ID=PRO_0000247350;Note=Long chronological lifespan protein 2 +Q08045 UniProtKB Compositional bias 32 40 . . . Note=Poly-Gln +##sequence-region Q07887 1 179 +Q07887 UniProtKB Chain 1 179 . . . ID=PRO_0000240386;Note=Protein LDB18 +##sequence-region P38139 1 375 +P38139 UniProtKB Chain 1 375 . . . ID=PRO_0000090373;Note=Lipid droplet hydrolase 1 +P38139 UniProtKB Domain 88 358 . . . Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38139 UniProtKB Motif 373 375 . . . Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38139 UniProtKB Active site 177 177 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38139 UniProtKB Active site 351 351 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38139 UniProtKB Mutagenesis 177 177 . . . Note=Abolishes serine hydrolase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21478434;Dbxref=PMID:21478434 +P38139 UniProtKB Sequence conflict 63 63 . . . Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38139 UniProtKB Sequence conflict 63 63 . . . Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38439 1 464 +P38439 UniProtKB Chain 1 464 . . . ID=PRO_0000084406;Note=RNA polymerase-associated protein LEO1 +P38439 UniProtKB Compositional bias 68 74 . . . Note=Poly-Asp +P38439 UniProtKB Compositional bias 383 464 . . . Note=Asp/Glu-rich (highly acidic) +P38439 UniProtKB Modified residue 105 105 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38439 UniProtKB Modified residue 132 132 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38439 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38439 UniProtKB Modified residue 358 358 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38439 UniProtKB Modified residue 372 372 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38439 UniProtKB Sequence conflict 134 134 . . . Note=Q->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38439 UniProtKB Sequence conflict 320 320 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38852 1 340 +P38852 UniProtKB Chain 1 340 . . . ID=PRO_0000195038;Note=Protein LIN1 +P38852 UniProtKB Domain 282 340 . . . Note=GYF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00101 +##sequence-region Q12342 1 491 +Q12342 UniProtKB Chain 1 491 . . . ID=PRO_0000240385;Note=Protein LDB17 +Q12342 UniProtKB Compositional bias 475 483 . . . Note=Poly-Pro +Q12342 UniProtKB Modified residue 7 7 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12342 UniProtKB Modified residue 463 463 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q12342 UniProtKB Modified residue 466 466 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P53150 1 421 +P53150 UniProtKB Chain 1 421 . . . ID=PRO_0000084419;Note=Ligase-interacting factor 1 +P53150 UniProtKB Sequence conflict 44 44 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47055 1 219 +P47055 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47055 UniProtKB Chain 20 219 . . . ID=PRO_0000203068;Note=Outer spore wall protein 4 +P47055 UniProtKB Topological domain 20 170 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P47055 UniProtKB Transmembrane 171 191 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47055 UniProtKB Topological domain 192 193 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P47055 UniProtKB Transmembrane 194 214 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47055 UniProtKB Topological domain 215 219 . . . Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +P47055 UniProtKB Glycosylation 42 42 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P47055 UniProtKB Glycosylation 62 62 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P47055 UniProtKB Glycosylation 136 136 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +##sequence-region P25579 1 583 +P25579 UniProtKB Chain 1 583 . . . ID=PRO_0000084482;Note=Laminarase-resistance protein LRE1 +P25579 UniProtKB Modified residue 393 393 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25579 UniProtKB Modified residue 398 398 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25579 UniProtKB Modified residue 516 516 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25579 UniProtKB Modified residue 552 552 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P53237 1 242 +P53237 UniProtKB Chain 1 242 . . . ID=PRO_0000202801;Note=Protein LST7 +P53237 UniProtKB Domain 48 212 . . . Note=uDENN FLCN/SMCR8-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01178 +P53237 UniProtKB Natural variant 4 4 . . . Note=In strain: SK1. T->I +##sequence-region Q06508 1 300 +Q06508 UniProtKB Chain 1 300 . . . ID=PRO_0000065908;Note=Lysophosphatidic acid:oleoyl-CoA acyltransferase 1 +Q06508 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06508 UniProtKB Motif 101 106 . . . Note=HXXXXD motif +##sequence-region P43586 1 204 +P43586 UniProtKB Chain 1 204 . . . ID=PRO_0000202680;Note=60S ribosomal subunit assembly/export protein LOC1 +P43586 UniProtKB Coiled coil 120 166 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43586 UniProtKB Compositional bias 39 199 . . . Note=Lys-rich +P43586 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P34234 1 306 +P34234 UniProtKB Chain 1 306 . . . ID=PRO_0000203137;Note=Protein LOT5 +##sequence-region Q12405 1 387 +Q12405 UniProtKB Chain 1 387 . . . ID=PRO_0000270570;Note=Peroxisomal membrane protein LPX1 +Q12405 UniProtKB Region 385 387 . . . Note=Peroxisomal targeting signal type 1 +Q12405 UniProtKB Beta strand 5 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Beta strand 23 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Beta strand 32 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Turn 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Beta strand 51 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Helix 65 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Turn 80 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Beta strand 84 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Helix 98 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Turn 104 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Helix 114 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Helix 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6V +Q12405 UniProtKB Beta strand 136 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Helix 146 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Beta strand 163 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Helix 194 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Beta strand 207 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Helix 211 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Turn 223 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Helix 229 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Beta strand 253 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Helix 259 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Helix 269 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Helix 273 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Helix 280 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Beta strand 285 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Helix 300 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Beta strand 311 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Helix 325 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Helix 330 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Helix 360 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6U +Q12405 UniProtKB Helix 383 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y6V +##sequence-region P35688 1 1017 +P35688 UniProtKB Chain 1 1017 . . . ID=PRO_0000075838;Note=Rho-GTPase-activating protein LRG1 +P35688 UniProtKB Domain 28 88 . . . Note=LIM zinc-binding 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125 +P35688 UniProtKB Domain 98 148 . . . Note=LIM zinc-binding 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125 +P35688 UniProtKB Domain 155 184 . . . Note=LIM zinc-binding 3%3B truncated;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125 +P35688 UniProtKB Domain 419 474 . . . Note=LIM zinc-binding 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125 +P35688 UniProtKB Domain 730 953 . . . Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172 +P35688 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P35688 UniProtKB Modified residue 562 562 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35688 UniProtKB Sequence conflict 531 531 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35688 UniProtKB Sequence conflict 766 766 . . . Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35688 UniProtKB Sequence conflict 791 791 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35688 UniProtKB Sequence conflict 821 821 . . . Note=L->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35688 UniProtKB Sequence conflict 838 838 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35688 UniProtKB Sequence conflict 849 849 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35688 UniProtKB Sequence conflict 895 895 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35688 UniProtKB Sequence conflict 928 928 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35688 UniProtKB Sequence conflict 935 935 . . . Note=Y->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35688 UniProtKB Sequence conflict 977 1017 . . . Note=INHFISTVMQSKTIDYSECDIKTPVTVKDSTTTVIQGEINK->TILFPPLCKVKQSIIPNVT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47093 1 109 +P47093 UniProtKB Chain 1 109 . . . ID=PRO_0000203088;Note=U6 snRNA-associated Sm-like protein LSm8 +P47093 UniProtKB Mutagenesis 57 57 . . . Note=Reduces affinity for poly-U RNA ends. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24240276;Dbxref=PMID:24240276 +P47093 UniProtKB Helix 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D +P47093 UniProtKB Beta strand 11 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D +P47093 UniProtKB Beta strand 22 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D +P47093 UniProtKB Beta strand 36 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D +P47093 UniProtKB Turn 44 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D +P47093 UniProtKB Beta strand 48 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D +P47093 UniProtKB Helix 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D +P47093 UniProtKB Beta strand 61 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D +P47093 UniProtKB Helix 96 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M77 +##sequence-region P40495 1 371 +P40495 UniProtKB Transit peptide 1 22 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40495 UniProtKB Chain 23 371 . . . ID=PRO_0000043097;Note=Homoisocitrate dehydrogenase%2C mitochondrial +P40495 UniProtKB Metal binding 243 243 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40495 UniProtKB Metal binding 267 267 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40495 UniProtKB Metal binding 271 271 . . . Note=Magnesium or manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40495 UniProtKB Binding site 114 114 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40495 UniProtKB Binding site 124 124 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40495 UniProtKB Binding site 143 143 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40495 UniProtKB Binding site 243 243 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40495 UniProtKB Site 150 150 . . . Note=Critical for catalysis +P40495 UniProtKB Site 206 206 . . . Note=Critical for catalysis +P40495 UniProtKB Modified residue 98 98 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40495 UniProtKB Mutagenesis 150 150 . . . Note=Strongly reduced enzyme activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19530703;Dbxref=PMID:19530703 +P40495 UniProtKB Mutagenesis 206 206 . . . Note=Strongly reduced enzyme activity. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19530703;Dbxref=PMID:19530703 +##sequence-region P47051 1 409 +P47051 UniProtKB Chain 1 409 . . . ID=PRO_0000203066;Note=Putative lipoate-protein ligase A +P47051 UniProtKB Domain 146 330 . . . Note=BPL/LPL catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01067 +P47051 UniProtKB Nucleotide binding 193 196 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47051 UniProtKB Binding site 188 188 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47051 UniProtKB Binding site 249 249 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47051 UniProtKB Binding site 249 249 . . . Note=Lipoate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q04087 1 347 +Q04087 UniProtKB Chain 1 347 . . . ID=PRO_0000257808;Note=Monopolin complex subunit LRS4 +Q04087 UniProtKB Coiled coil 46 118 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04087 UniProtKB Modified residue 168 168 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04087 UniProtKB Modified residue 230 230 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P43603 1 459 +P43603 UniProtKB Chain 1 459 . . . ID=PRO_0000202691;Note=LAS seventeen-binding protein 3 +P43603 UniProtKB Domain 400 459 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P43603 UniProtKB Compositional bias 229 284 . . . Note=Asp-rich +P43603 UniProtKB Modified residue 227 227 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43603 UniProtKB Modified residue 298 298 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43603 UniProtKB Modified residue 300 300 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P43603 UniProtKB Modified residue 303 303 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +P43603 UniProtKB Modified residue 393 393 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P43603 UniProtKB Modified residue 397 397 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43603 UniProtKB Modified residue 402 402 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P43603 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P43603 UniProtKB Beta strand 404 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OOT +P43603 UniProtKB Beta strand 426 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OOT +P43603 UniProtKB Beta strand 438 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OOT +P43603 UniProtKB Beta strand 447 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OOT +P43603 UniProtKB Helix 453 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OOT +P43603 UniProtKB Beta strand 456 458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OOT +##sequence-region P47017 1 172 +P47017 UniProtKB Chain 1 172 . . . ID=PRO_0000125553;Note=Sm-like protein LSm1 +P47017 UniProtKB Mutagenesis 105 105 . . . Note=Slightly reduces affinity for poly-U RNA ends. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24513854;Dbxref=PMID:24513854 +P47017 UniProtKB Helix 42 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M75 +P47017 UniProtKB Beta strand 48 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P47017 UniProtKB Beta strand 63 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P47017 UniProtKB Beta strand 77 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P47017 UniProtKB Turn 89 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P47017 UniProtKB Beta strand 93 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P47017 UniProtKB Helix 106 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P47017 UniProtKB Beta strand 109 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P47017 UniProtKB Helix 117 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P47017 UniProtKB Beta strand 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P47017 UniProtKB Helix 132 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P47017 UniProtKB Turn 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +##sequence-region Q12230 1 341 +Q12230 UniProtKB Chain 1 341 . . . ID=PRO_0000084505;Note=Sphingolipid long chain base-responsive protein LSP1 +Q12230 UniProtKB Compositional bias 21 25 . . . Note=Poly-Pro +Q12230 UniProtKB Compositional bias 283 324 . . . Note=Glu-rich +Q12230 UniProtKB Modified residue 233 233 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +Q12230 UniProtKB Turn 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLT +Q12230 UniProtKB Helix 56 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLT +Q12230 UniProtKB Helix 95 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLT +Q12230 UniProtKB Helix 165 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLT +Q12230 UniProtKB Beta strand 234 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLT +Q12230 UniProtKB Helix 244 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLT +##sequence-region Q04781 1 1562 +Q04781 UniProtKB Chain 1 1562 . . . ID=PRO_0000056341;Note=E3 ubiquitin-protein ligase listerin +Q04781 UniProtKB Repeat 41 78 . . . Note=HEAT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04781 UniProtKB Repeat 127 164 . . . Note=HEAT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04781 UniProtKB Repeat 175 217 . . . Note=HEAT 3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04781 UniProtKB Repeat 262 301 . . . Note=HEAT 4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04781 UniProtKB Repeat 304 348 . . . Note=HEAT 5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04781 UniProtKB Repeat 495 532 . . . Note=HEAT 6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04781 UniProtKB Repeat 555 592 . . . Note=HEAT 7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04781 UniProtKB Repeat 813 850 . . . Note=HEAT 8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04781 UniProtKB Repeat 908 945 . . . Note=HEAT 9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04781 UniProtKB Repeat 997 1037 . . . Note=HEAT 10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04781 UniProtKB Repeat 1047 1085 . . . Note=HEAT 11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04781 UniProtKB Repeat 1188 1226 . . . Note=HEAT 12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04781 UniProtKB Repeat 1263 1298 . . . Note=HEAT 13;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04781 UniProtKB Repeat 1299 1339 . . . Note=HEAT 14;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04781 UniProtKB Zinc finger 1508 1555 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +Q04781 UniProtKB Mutagenesis 1542 1542 . . . Note=Abolishes ability to control levels of proteins with 'non-stop'. W->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20835226;Dbxref=PMID:20835226 +Q04781 UniProtKB Beta strand 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Beta strand 27 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 36 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 45 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 59 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Turn 75 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG1 +Q04781 UniProtKB Helix 85 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 104 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Turn 122 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 126 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 129 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 145 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Turn 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 163 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 174 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 190 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Turn 196 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 201 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 229 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 234 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Beta strand 243 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG1 +Q04781 UniProtKB Helix 247 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Beta strand 253 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 259 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 276 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 281 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 295 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Turn 300 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 303 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 307 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 310 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Turn 321 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 327 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 335 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 354 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 366 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Turn 373 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 377 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Helix 398 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +Q04781 UniProtKB Turn 414 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FG0 +##sequence-region P22134 1 296 +P22134 UniProtKB Chain 1 296 . . . ID=PRO_0000194883;Note=DNA-3-methyladenine glycosylase +P22134 UniProtKB Active site 209 209 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22134 UniProtKB Site 189 189 . . . Note=Determinant for substrate specificity and/or activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22134 UniProtKB Modified residue 110 110 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q12176 1 1025 +Q12176 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12176 UniProtKB Chain 2 1025 . . . ID=PRO_0000173472;Note=Ribosome biogenesis protein MAK21 +Q12176 UniProtKB Compositional bias 74 77 . . . Note=Poly-Asp +Q12176 UniProtKB Compositional bias 117 122 . . . Note=Poly-Asp +Q12176 UniProtKB Compositional bias 979 986 . . . Note=Poly-Glu +Q12176 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12176 UniProtKB Modified residue 62 62 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +Q12176 UniProtKB Modified residue 73 73 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12176 UniProtKB Modified residue 80 80 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12176 UniProtKB Modified residue 275 275 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12176 UniProtKB Modified residue 708 708 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12176 UniProtKB Modified residue 710 710 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12176 UniProtKB Modified residue 874 874 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12176 UniProtKB Modified residue 878 878 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12176 UniProtKB Modified residue 977 977 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12176 UniProtKB Modified residue 978 978 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12176 UniProtKB Modified residue 1024 1024 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P53341 1 584 +P53341 UniProtKB Chain 1 584 . . . ID=PRO_0000054328;Note=Alpha-glucosidase MAL12 +P53341 UniProtKB Active site 214 214 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53341 UniProtKB Active site 276 276 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53341 UniProtKB Site 349 349 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q12246 1 624 +Q12246 UniProtKB Chain 1 624 . . . ID=PRO_0000255956;Note=Sphingoid long chain base kinase 4 +Q12246 UniProtKB Domain 224 363 . . . Note=DAGKc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 +Q12246 UniProtKB Nucleotide binding 234 236 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 +Q12246 UniProtKB Nucleotide binding 324 326 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 +Q12246 UniProtKB Nucleotide binding 589 591 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 +Q12246 UniProtKB Region 291 294 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12246 UniProtKB Active site 293 293 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12246 UniProtKB Binding site 266 266 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 +Q12246 UniProtKB Binding site 298 298 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 +Q12246 UniProtKB Binding site 392 392 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 +Q12246 UniProtKB Binding site 398 398 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 +Q12246 UniProtKB Modified residue 111 111 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12246 UniProtKB Modified residue 120 120 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12246 UniProtKB Modified residue 154 154 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12246 UniProtKB Modified residue 160 160 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12246 UniProtKB Modified residue 451 451 . . . Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:15598647;Dbxref=PMID:17330950,PMID:19779198,PMID:15598647 +Q12246 UniProtKB Modified residue 454 454 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q12246 UniProtKB Modified residue 455 455 . . . Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:15598647;Dbxref=PMID:17330950,PMID:19779198,PMID:15598647 +Q12246 UniProtKB Modified residue 460 460 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12246 UniProtKB Lipidation 43 43 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16227572;Dbxref=PMID:16227572 +Q12246 UniProtKB Lipidation 46 46 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16227572;Dbxref=PMID:16227572 +Q12246 UniProtKB Cross-link 148 148 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q12502 1 818 +Q12502 UniProtKB Chain 1 818 . . . ID=PRO_0000240388;Note=Protein LDB19 +Q12502 UniProtKB Compositional bias 67 124 . . . Note=Ser-rich +Q12502 UniProtKB Modified residue 93 93 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12502 UniProtKB Modified residue 384 384 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12502 UniProtKB Modified residue 619 619 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12502 UniProtKB Modified residue 808 808 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12502 UniProtKB Cross-link 486 486 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14557538;Dbxref=PMID:14557538 +##sequence-region Q02783 1 413 +Q02783 UniProtKB Transit peptide 1 35 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02783 UniProtKB Chain 36 413 . . . ID=PRO_0000042816;Note=Mitochondrial inner membrane magnesium transporter MFM1 +Q02783 UniProtKB Transmembrane 329 349 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02783 UniProtKB Transmembrane 367 387 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02783 UniProtKB Motif 353 356 . . . Note=YGMN +Q02783 UniProtKB Glycosylation 202 202 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02783 UniProtKB Sequence conflict 267 267 . . . Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40070 1 187 +P40070 UniProtKB Chain 1 187 . . . ID=PRO_0000125571;Note=U6 snRNA-associated Sm-like protein LSm4 +P40070 UniProtKB Mutagenesis 72 72 . . . Note=Slightly reduces affinity for poly-U RNA ends. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24240276,ECO:0000269|PubMed:24513854;Dbxref=PMID:24240276,PMID:24513854 +P40070 UniProtKB Sequence conflict 155 155 . . . Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40070 UniProtKB Helix 2 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P40070 UniProtKB Turn 9 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M78 +P40070 UniProtKB Beta strand 14 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P40070 UniProtKB Beta strand 22 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P40070 UniProtKB Beta strand 38 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P40070 UniProtKB Helix 48 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P40070 UniProtKB Beta strand 64 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P40070 UniProtKB Helix 73 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P40070 UniProtKB Beta strand 76 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P40070 UniProtKB Helix 83 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D +##sequence-region P40089 1 93 +P40089 UniProtKB Chain 1 93 . . . ID=PRO_0000125574;Note=U6 snRNA-associated Sm-like protein LSm5 +P40089 UniProtKB Mutagenesis 74 74 . . . Note=Slightly increases affinity for poly-U RNA ends. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24240276,ECO:0000269|PubMed:24513854;Dbxref=PMID:24240276,PMID:24513854 +P40089 UniProtKB Helix 8 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P40089 UniProtKB Turn 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D +P40089 UniProtKB Beta strand 18 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P40089 UniProtKB Beta strand 43 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P40089 UniProtKB Beta strand 62 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P40089 UniProtKB Beta strand 69 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P40089 UniProtKB Beta strand 77 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +##sequence-region P53905 1 115 +P53905 UniProtKB Chain 1 115 . . . ID=PRO_0000125581;Note=U6 snRNA-associated Sm-like protein LSm7 +P53905 UniProtKB Mutagenesis 95 95 . . . Note=Slightly reduces affinity for poly-U RNA ends. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24240276,ECO:0000269|PubMed:24513854;Dbxref=PMID:24240276,PMID:24513854 +P53905 UniProtKB Helix 30 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P53905 UniProtKB Beta strand 36 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P53905 UniProtKB Turn 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7A +P53905 UniProtKB Beta strand 47 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P53905 UniProtKB Beta strand 61 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P53905 UniProtKB Beta strand 86 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P53905 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P53905 UniProtKB Beta strand 99 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +##sequence-region P32487 1 611 +P32487 UniProtKB Chain 1 611 . . . ID=PRO_0000054156;Note=Lysine-specific permease +P32487 UniProtKB Topological domain 1 115 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Transmembrane 116 136 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Topological domain 137 141 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Transmembrane 142 162 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Topological domain 163 185 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Transmembrane 186 205 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Topological domain 206 223 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Transmembrane 224 243 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Topological domain 244 256 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Transmembrane 257 274 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Topological domain 275 303 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Transmembrane 304 321 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Topological domain 322 344 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Transmembrane 345 365 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Topological domain 366 398 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Transmembrane 399 418 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Topological domain 419 445 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Transmembrane 446 464 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Topological domain 465 473 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Transmembrane 474 494 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Topological domain 495 513 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Transmembrane 514 532 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Topological domain 533 547 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Transmembrane 548 566 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Topological domain 567 611 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32487 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32487 UniProtKB Modified residue 75 75 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32487 UniProtKB Modified residue 77 77 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32487 UniProtKB Modified residue 79 79 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198 +P32487 UniProtKB Modified residue 87 87 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32487 UniProtKB Modified residue 90 90 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32487 UniProtKB Cross-link 54 54 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32487 UniProtKB Sequence conflict 90 90 . . . Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32487 UniProtKB Sequence conflict 93 93 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32487 UniProtKB Sequence conflict 561 561 . . . Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40971 1 790 +P40971 UniProtKB Chain 1 790 . . . ID=PRO_0000114955;Note=Lysine biosynthesis regulatory protein LYS14 +P40971 UniProtKB DNA binding 159 186 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P40971 UniProtKB Sequence conflict 121 121 . . . Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40971 UniProtKB Sequence conflict 760 760 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38828 1 187 +P38828 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38828 UniProtKB Chain 2 187 . . . ID=PRO_0000202913;Note=Protein LSM12 +P38828 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P10962 1 306 +P10962 UniProtKB Chain 1 306 . . . ID=PRO_0000203793;Note=Protein MAK16 +P10962 UniProtKB Repeat 213 220 . . . Note=1 +P10962 UniProtKB Repeat 222 229 . . . Note=2 +P10962 UniProtKB Region 213 229 . . . Note=2 X 8 AA repeats +P10962 UniProtKB Region 251 264 . . . Note=7 X 2 AA repeats of S-[DE] +P10962 UniProtKB Motif 139 144 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10962 UniProtKB Motif 282 287 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10962 UniProtKB Compositional bias 195 235 . . . Note=Asp/Glu-rich (acidic) +P10962 UniProtKB Sequence conflict 250 250 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10962 UniProtKB Sequence conflict 250 250 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P23060 1 363 +P23060 UniProtKB Chain 1 363 . . . ID=PRO_0000084555;Note=Protein MAK32 +P23060 UniProtKB Sequence conflict 15 15 . . . Note=I->II;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23060 UniProtKB Sequence conflict 82 82 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53048 1 616 +P53048 UniProtKB Chain 1 616 . . . ID=PRO_0000050425;Note=General alpha-glucoside permease +P53048 UniProtKB Topological domain 1 115 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Transmembrane 116 136 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Topological domain 137 150 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Transmembrane 151 171 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Topological domain 172 186 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Transmembrane 187 207 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Topological domain 208 208 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Transmembrane 209 229 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Topological domain 230 242 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Transmembrane 243 263 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Topological domain 264 278 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Transmembrane 279 299 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Topological domain 300 370 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Transmembrane 371 391 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Topological domain 392 404 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Transmembrane 405 425 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Topological domain 426 433 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Transmembrane 434 454 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Topological domain 455 466 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Transmembrane 467 487 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Topological domain 488 499 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Transmembrane 500 520 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Topological domain 521 532 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Transmembrane 533 553 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Topological domain 554 616 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Glycosylation 523 523 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53048 UniProtKB Sequence conflict 396 398 . . . Note=RAG->KKQV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38157 1 468 +P38157 UniProtKB Chain 1 468 . . . ID=PRO_0000114957;Note=Maltose fermentation regulatory protein MAL33 +P38157 UniProtKB DNA binding 8 34 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P38157 UniProtKB Motif 41 49 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CW40 1 589 +P0CW40 UniProtKB Chain 1 589 . . . ID=PRO_0000054332;Note=Oligo-1%2C6-glucosidase IMA3 +P0CW40 UniProtKB Active site 215 215 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CW40 UniProtKB Active site 277 277 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CW40 UniProtKB Site 352 352 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53051 1 589 +P53051 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15291818;Dbxref=PMID:15291818 +P53051 UniProtKB Chain 2 589 . . . ID=PRO_0000054333;Note=Oligo-1%2C6-glucosidase IMA1 +P53051 UniProtKB Active site 215 215 . . . Note=Nucleophile +P53051 UniProtKB Active site 277 277 . . . Note=Proton donor +P53051 UniProtKB Site 352 352 . . . Note=Transition state stabilizer +P53051 UniProtKB Mutagenesis 215 215 . . . Note=Abolishes catalytic activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15291818;Dbxref=PMID:15291818 +P53051 UniProtKB Mutagenesis 216 216 . . . Note=Can also hydrolyze maltose. V->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15291818;Dbxref=PMID:15291818 +P53051 UniProtKB Mutagenesis 217 217 . . . Note=Does not alter substrate specificity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15291818;Dbxref=PMID:15291818 +P53051 UniProtKB Mutagenesis 218 218 . . . Note=Does not alter substrate specificity. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15291818;Dbxref=PMID:15291818 +P53051 UniProtKB Sequence conflict 428 428 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53051 UniProtKB Helix 8 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 14 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 20 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 31 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 39 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 46 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 55 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Turn 68 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 75 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Turn 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 87 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 103 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 118 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 141 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 160 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Turn 168 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 172 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 177 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 190 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 202 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 211 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 217 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 237 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 242 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 251 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 273 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 283 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 292 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 298 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 304 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 314 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 323 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Turn 332 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 335 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 356 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Turn 365 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 368 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 382 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 392 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 404 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 410 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 425 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 428 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 442 445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Turn 455 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 473 477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 481 486 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 491 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Helix 506 509 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 513 519 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 523 532 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 535 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 544 546 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 559 566 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Turn 568 570 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +P53051 UniProtKB Beta strand 583 588 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AJ7 +##sequence-region P40065 1 302 +P40065 UniProtKB Chain 1 302 . . . ID=PRO_0000202645;Note=Monopolin complex subunit MAM1 +P40065 UniProtKB Sequence conflict 202 202 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40065 UniProtKB Helix 94 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P40065 UniProtKB Helix 101 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P40065 UniProtKB Turn 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P40065 UniProtKB Helix 121 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P40065 UniProtKB Helix 130 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P40065 UniProtKB Helix 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P40065 UniProtKB Beta strand 141 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P40065 UniProtKB Helix 148 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P40065 UniProtKB Helix 158 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P40065 UniProtKB Helix 170 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P40065 UniProtKB Beta strand 177 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CZO +P40065 UniProtKB Helix 184 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYZ +P40065 UniProtKB Helix 231 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KTB +P40065 UniProtKB Helix 234 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KTB +P40065 UniProtKB Helix 240 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KTB +P40065 UniProtKB Helix 247 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5KTB +##sequence-region Q01662 1 387 +Q01662 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q01662 UniProtKB Propeptide 2 10 . . . ID=PRO_0000018596;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1569059;Dbxref=PMID:1569059 +Q01662 UniProtKB Chain 11 387 . . . ID=PRO_0000018597;Note=Methionine aminopeptidase 1 +Q01662 UniProtKB Region 22 66 . . . Note=Zinc finger-like%3B important for proper ribosome association +Q01662 UniProtKB Metal binding 219 219 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03174 +Q01662 UniProtKB Metal binding 230 230 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03174 +Q01662 UniProtKB Metal binding 230 230 . . . Note=Divalent metal cation 2%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03174 +Q01662 UniProtKB Metal binding 294 294 . . . Note=Divalent metal cation 2%3B catalytic%3B via tele nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03174 +Q01662 UniProtKB Metal binding 327 327 . . . Note=Divalent metal cation 2%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03174 +Q01662 UniProtKB Metal binding 358 358 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03174 +Q01662 UniProtKB Metal binding 358 358 . . . Note=Divalent metal cation 2%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03174 +Q01662 UniProtKB Binding site 202 202 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03174 +Q01662 UniProtKB Binding site 301 301 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03174 +Q01662 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q01662 UniProtKB Mutagenesis 22 22 . . . Note=Changes the ribosome profile distribution of the protein and also increases its occurrence in the cytosolic fraction. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11968008;Dbxref=PMID:11968008 +Q01662 UniProtKB Mutagenesis 62 62 . . . Note=Changes the ribosome profile distribution of the protein. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11968008;Dbxref=PMID:11968008 +Q01662 UniProtKB Mutagenesis 219 219 . . . Note=Reduces activity 1000-fold. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9367524;Dbxref=PMID:9367524 +##sequence-region P38174 1 421 +P38174 UniProtKB Chain 1 421 . . . ID=PRO_0000148988;Note=Methionine aminopeptidase 2 +P38174 UniProtKB Compositional bias 41 57 . . . Note=Lys-rich +P38174 UniProtKB Metal binding 194 194 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03175 +P38174 UniProtKB Metal binding 205 205 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03175 +P38174 UniProtKB Metal binding 205 205 . . . Note=Divalent metal cation 2%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03175 +P38174 UniProtKB Metal binding 274 274 . . . Note=Divalent metal cation 2%3B catalytic%3B via tele nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03175 +P38174 UniProtKB Metal binding 307 307 . . . Note=Divalent metal cation 2%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03175 +P38174 UniProtKB Metal binding 402 402 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03175 +P38174 UniProtKB Metal binding 402 402 . . . Note=Divalent metal cation 2%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03175 +P38174 UniProtKB Binding site 174 174 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03175 +P38174 UniProtKB Binding site 282 282 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03175 +P38174 UniProtKB Modified residue 35 35 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38174 UniProtKB Mutagenesis 174 174 . . . Note=Abolishes catalytic activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15547949;Dbxref=PMID:15547949 +P38174 UniProtKB Sequence conflict 86 86 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38174 UniProtKB Sequence conflict 86 86 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q9ZZW7 1 517 +Q9ZZW7 UniProtKB Chain 1 517 . . . ID=PRO_0000061915;Note=Cytochrome b mRNA maturase bI3 +Q9ZZW7 UniProtKB Topological domain 1 31 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q9ZZW7 UniProtKB Transmembrane 32 52 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968 +Q9ZZW7 UniProtKB Topological domain 53 84 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q9ZZW7 UniProtKB Transmembrane 85 105 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968 +Q9ZZW7 UniProtKB Topological domain 106 115 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q9ZZW7 UniProtKB Transmembrane 116 136 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968 +Q9ZZW7 UniProtKB Topological domain 137 145 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q9ZZW7 UniProtKB Transmembrane 146 166 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968 +Q9ZZW7 UniProtKB Topological domain 167 184 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q9ZZW7 UniProtKB Transmembrane 185 205 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968 +Q9ZZW7 UniProtKB Topological domain 206 224 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q9ZZW7 UniProtKB Transmembrane 225 242 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968 +Q9ZZW7 UniProtKB Topological domain 243 517 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q9ZZW7 UniProtKB Region 1 169 . . . Note=Cytochrome b +Q9ZZW7 UniProtKB Region 170 517 . . . Note=Maturase +Q9ZZW7 UniProtKB Natural variant 269 269 . . . Note=In strain: 777-3A. G->V +Q9ZZW7 UniProtKB Natural variant 350 350 . . . Note=In strain: 777-3A. D->N +Q9ZZW7 UniProtKB Natural variant 412 412 . . . Note=In strain: 777-3A. E->K +Q9ZZW7 UniProtKB Natural variant 434 434 . . . Note=In strain: 777-3A. Q->M +Q9ZZW7 UniProtKB Natural variant 437 437 . . . Note=In strain: 777-3A. S->N +Q9ZZW7 UniProtKB Natural variant 451 452 . . . Note=In strain: 777-3A. TQ->NN +Q9ZZW7 UniProtKB Natural variant 456 458 . . . Note=In strain: 777-3A. TDK->MNE +Q9ZZW7 UniProtKB Natural variant 463 463 . . . Note=In strain: 777-3A. R->K +Q9ZZW7 UniProtKB Natural variant 471 471 . . . Note=In strain: 777-3A. G->D +Q9ZZW7 UniProtKB Natural variant 515 515 . . . Note=In strain: 777-3A. P->S +Q9ZZW7 UniProtKB Mutagenesis 151 151 . . . Note=In M2011%3B leads to absence of functional cytochrome b%2C but does not affect splicing. F->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2538624;Dbxref=PMID:2538624 +Q9ZZW7 UniProtKB Mutagenesis 407 407 . . . Note=In G5037%3B blocks formation of mature cytochrome b mRNA. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2538624;Dbxref=PMID:2538624 +Q9ZZW7 UniProtKB Helix 264 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Beta strand 276 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Beta strand 286 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Helix 297 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Helix 300 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Beta strand 314 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Beta strand 327 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Helix 338 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Helix 345 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Helix 359 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Helix 376 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Helix 392 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Helix 401 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Beta strand 413 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Beta strand 423 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Beta strand 427 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Helix 438 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Beta strand 454 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Beta strand 462 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Helix 469 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Helix 489 501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +Q9ZZW7 UniProtKB Helix 505 508 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AB5 +##sequence-region P42951 1 607 +P42951 UniProtKB Chain 1 607 . . . ID=PRO_0000088850;Note=Phosphatidylinositol 4-kinase LSB6 +P42951 UniProtKB Domain 170 507 . . . Note=PI3K/PI4K +##sequence-region P38203 1 95 +P38203 UniProtKB Chain 1 95 . . . ID=PRO_0000125559;Note=U6 snRNA-associated Sm-like protein LSm2 +P38203 UniProtKB Mutagenesis 35 35 . . . Note=Strongly reduces affinity for poly-U RNA ends. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24240276;Dbxref=PMID:24240276 +P38203 UniProtKB Mutagenesis 37 37 . . . Note=Strongly reduces affinity for poly-U RNA ends. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24240276;Dbxref=PMID:24240276 +P38203 UniProtKB Mutagenesis 63 63 . . . Note=Strongly reduces affinity for poly-U RNA ends. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24240276,ECO:0000269|PubMed:24513854;Dbxref=PMID:24240276,PMID:24513854 +P38203 UniProtKB Helix 2 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P38203 UniProtKB Turn 9 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P38203 UniProtKB Beta strand 13 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P38203 UniProtKB Turn 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7D +P38203 UniProtKB Beta strand 24 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P38203 UniProtKB Beta strand 38 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P38203 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P38203 UniProtKB Beta strand 54 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M75 +P38203 UniProtKB Beta strand 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P38203 UniProtKB Helix 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P38203 UniProtKB Beta strand 67 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P38203 UniProtKB Helix 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P38203 UniProtKB Helix 79 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +##sequence-region P34239 1 828 +P34239 UniProtKB Chain 1 828 . . . ID=PRO_0000203139;Note=Protein LST4 +P34239 UniProtKB Domain 114 302 . . . Note=uDENN FNIP1/2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01180 +P34239 UniProtKB Domain 310 712 . . . Note=cDENN FNIP1/2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01180 +P34239 UniProtKB Domain 718 825 . . . Note=dDENN FNIP1/2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01180 +P34239 UniProtKB Compositional bias 437 570 . . . Note=Ser-rich +P34239 UniProtKB Modified residue 401 401 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P41318 1 303 +P41318 UniProtKB Chain 1 303 . . . ID=PRO_0000051483;Note=Target of rapamycin complex subunit LST8 +P41318 UniProtKB Repeat 1 27 . . . Note=WD 1 +P41318 UniProtKB Repeat 30 68 . . . Note=WD 2 +P41318 UniProtKB Repeat 73 112 . . . Note=WD 3 +P41318 UniProtKB Repeat 114 153 . . . Note=WD 4 +P41318 UniProtKB Repeat 157 196 . . . Note=WD 5 +P41318 UniProtKB Repeat 205 244 . . . Note=WD 6 +P41318 UniProtKB Repeat 248 287 . . . Note=WD 7 +P41318 UniProtKB Mutagenesis 138 138 . . . Note=In LST8-3%3B abolishes repression of RTG1-RTG3-dependent gene expression. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11742997;Dbxref=PMID:11742997 +P41318 UniProtKB Mutagenesis 146 146 . . . Note=In LST8-2%3B abolishes repression of RTG1-RTG3-dependent gene expression. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11742997;Dbxref=PMID:11742997 +P41318 UniProtKB Mutagenesis 171 171 . . . Note=In LST8-5%3B abolishes repression of RTG1-RTG3-dependent gene expression. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11742997;Dbxref=PMID:11742997 +P41318 UniProtKB Mutagenesis 181 181 . . . Note=In LST8-4%3B abolishes repression of RTG1-RTG3-dependent gene expression. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11742997;Dbxref=PMID:11742997 +P41318 UniProtKB Mutagenesis 300 300 . . . Note=In LST8-1%3B abolishes repression of RTG2- and RTG1-RTG3-dependent gene expression. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9409822;Dbxref=PMID:9409822 +##sequence-region P07866 1 1435 +P07866 UniProtKB Chain 1 1435 . . . ID=PRO_0000068884;Note=Guanine nucleotide exchange factor LTE1 +P07866 UniProtKB Domain 25 157 . . . Note=N-terminal Ras-GEF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00135 +P07866 UniProtKB Domain 1194 1434 . . . Note=Ras-GEF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00168 +P07866 UniProtKB Modified residue 271 271 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P07866 UniProtKB Modified residue 559 559 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07866 UniProtKB Modified residue 689 689 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07866 UniProtKB Modified residue 691 691 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07866 UniProtKB Modified residue 808 808 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07866 UniProtKB Modified residue 810 810 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07866 UniProtKB Modified residue 1028 1028 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P07866 UniProtKB Modified residue 1109 1109 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07866 UniProtKB Sequence conflict 998 1009 . . . Note=TNSNISGSVLTM->LIVHIRKCIDN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07866 UniProtKB Sequence conflict 1161 1163 . . . Note=AAQ->GE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07508 1 261 +Q07508 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q07508 UniProtKB Chain 2 261 . . . ID=PRO_0000255959;Note=Protein LUC7 +Q07508 UniProtKB Coiled coil 123 190 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07508 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P35192 1 417 +P35192 UniProtKB Chain 1 417 . . . ID=PRO_0000194928;Note=Metal-binding activator 1 +P35192 UniProtKB Repeat 264 279 . . . Note=1 +P35192 UniProtKB Repeat 322 337 . . . Note=2 +P35192 UniProtKB DNA binding 1 40 . . . Note=Copper-fist;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055 +P35192 UniProtKB Region 264 337 . . . Note=2 X 16 AA repeat of C-X-C-X(4)-C-X-C-X-X-C-X-X-H +P35192 UniProtKB Metal binding 11 11 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055 +P35192 UniProtKB Metal binding 14 14 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055 +P35192 UniProtKB Metal binding 23 23 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055 +P35192 UniProtKB Metal binding 25 25 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00055 +P35192 UniProtKB Modified residue 143 143 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P35192 UniProtKB Mutagenesis 279 279 . . . Note=Gain of function. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8262047;Dbxref=PMID:8262047 +P35192 UniProtKB Sequence conflict 198 198 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35192 UniProtKB Sequence conflict 380 380 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06436 1 670 +Q06436 UniProtKB Chain 1 670 . . . ID=PRO_0000257809;Note=RING-finger protein MAG2 +Q06436 UniProtKB Zinc finger 195 250 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +##sequence-region P0CW41 1 589 +P0CW41 UniProtKB Chain 1 589 . . . ID=PRO_0000408197;Note=Oligo-1%2C6-glucosidase IMA4 +P0CW41 UniProtKB Active site 215 215 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CW41 UniProtKB Active site 277 277 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CW41 UniProtKB Site 352 352 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P30952 1 554 +P30952 UniProtKB Chain 1 554 . . . ID=PRO_0000166864;Note=Malate synthase 1%2C glyoxysomal +P30952 UniProtKB Motif 552 554 . . . Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30952 UniProtKB Active site 177 177 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P30952 UniProtKB Active site 457 457 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P30952 UniProtKB Natural variant 118 118 . . . Note=In strain: Awamori-1%2C AKU-4011%2C K1%2C K5%2C NRIC 23%2C NRIC 1413 and NRIC 1685. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16103919;Dbxref=PMID:16103919 +P30952 UniProtKB Natural variant 199 199 . . . Note=In strain: Pasteur Red. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16103919;Dbxref=PMID:16103919 +P30952 UniProtKB Natural variant 217 217 . . . Note=In strain: YJM326. G->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P30952 UniProtKB Natural variant 253 253 . . . Note=In strain: Levuline ALS%2C Lalvin CY-3079%2C Cote des Blancs%2C I14%2C M1%2C M11%2C M12%2C M13%2C M15%2C M2%2C M20%2C M21%2C M22%2C M24%2C M29%2C M3%2C M30%2C M31%2C M32%2C M33%2C M34%2C M4%2C M5%2C M6%2C M7%2C M8%2C M9%2C NRRL Y-1438%2C NRRL YB-1952%2C NRRL Y-2411%2C Pasteur Red%2C UCD 51%2C UCD 2120%2C UCD 175%2C UCD 529%2C UCD 765%2C UCD 781%2C UCD 820%2C UCD 762%2C YJM269%2C YJM270%2C YJM308%2C YJM326%2C YJM434 and YJM1129. T->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16103919,ECO:0000269|PubMed:18780730;Dbxref=PMID:16103919,PMID:18780730 +P30952 UniProtKB Natural variant 310 310 . . . Note=In strain: SK1%2C V1-09%2C YJM269%2C YJM270%2C YJM280%2C YJM320%2C YJM326%2C YJM339%2C YJM627 and YJM1129. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P30952 UniProtKB Natural variant 541 541 . . . Note=In strain: YJM269 and YJM270. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +##sequence-region P21826 1 554 +P21826 UniProtKB Chain 1 554 . . . ID=PRO_0000166865;Note=Malate synthase 2%2C glyoxysomal +P21826 UniProtKB Motif 552 554 . . . Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21826 UniProtKB Active site 177 177 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21826 UniProtKB Active site 457 457 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21826 UniProtKB Sequence conflict 115 115 . . . Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21826 UniProtKB Sequence conflict 115 115 . . . Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21826 UniProtKB Sequence conflict 166 166 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21826 UniProtKB Sequence conflict 166 166 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21826 UniProtKB Sequence conflict 302 302 . . . Note=P->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21826 UniProtKB Sequence conflict 302 302 . . . Note=P->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P50113 1 272 +P50113 UniProtKB Chain 1 272 . . . ID=PRO_0000175742;Note=L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase +##sequence-region P47074 1 515 +P47074 UniProtKB Chain 1 515 . . . ID=PRO_0000084549;Note=Spindle assembly checkpoint component MAD3 +P47074 UniProtKB Domain 67 228 . . . Note=BUB1 N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00822 +P47074 UniProtKB Modified residue 268 268 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47074 UniProtKB Mutagenesis 156 159 . . . Note=Abolishes interaction with CDC20. Benomyl-sensitive phenotype. GIGS->AAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10704439;Dbxref=PMID:10704439 +P47074 UniProtKB Mutagenesis 382 382 . . . Note=Abolishes interaction with BUB3. Benomyl-sensitive phenotype. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10704439;Dbxref=PMID:10704439 +P47074 UniProtKB Beta strand 356 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3T +P47074 UniProtKB Helix 362 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3T +P47074 UniProtKB Helix 381 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3T +P47074 UniProtKB Turn 388 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2I3T +##sequence-region P41910 1 395 +P41910 UniProtKB Chain 1 395 . . . ID=PRO_0000213972;Note=Repressor of RNA polymerase III transcription MAF1 +P41910 UniProtKB Modified residue 90 90 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P41910 UniProtKB Modified residue 209 209 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P41910 UniProtKB Modified residue 210 210 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P41910 UniProtKB Modified residue 347 347 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P39534 1 108 +P39534 UniProtKB Chain 1 108 . . . ID=PRO_0000203017;Note=Uncharacterized protein MBB1 +##sequence-region Q07376 1 486 +Q07376 UniProtKB Chain 1 486 . . . ID=PRO_0000084877;Note=Probable transporter MCH1 +Q07376 UniProtKB Topological domain 1 29 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Transmembrane 30 50 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Topological domain 51 67 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Transmembrane 68 88 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Topological domain 89 93 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Transmembrane 94 114 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Topological domain 115 133 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Transmembrane 134 154 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Topological domain 155 163 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Transmembrane 164 184 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Topological domain 185 212 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Transmembrane 213 233 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Topological domain 234 279 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Transmembrane 280 300 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Topological domain 301 320 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Transmembrane 321 343 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Topological domain 344 347 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Transmembrane 348 368 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Topological domain 369 385 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Transmembrane 386 406 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Topological domain 407 413 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Transmembrane 414 434 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Topological domain 435 456 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Transmembrane 457 477 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Topological domain 478 486 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Modified residue 255 255 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q07376 UniProtKB Glycosylation 60 60 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Glycosylation 131 131 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07376 UniProtKB Glycosylation 194 194 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36032 1 473 +P36032 UniProtKB Chain 1 473 . . . ID=PRO_0000211403;Note=Probable transporter MCH2 +P36032 UniProtKB Topological domain 1 37 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Transmembrane 38 58 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Topological domain 59 83 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Transmembrane 84 105 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Topological domain 106 111 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Transmembrane 112 135 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Topological domain 136 141 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Transmembrane 142 163 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Topological domain 164 169 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Transmembrane 170 186 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Topological domain 187 200 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Transmembrane 201 220 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Topological domain 221 243 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Transmembrane 244 268 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Topological domain 269 286 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Transmembrane 287 304 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Topological domain 305 312 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Transmembrane 313 332 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Topological domain 333 342 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Transmembrane 343 362 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Topological domain 363 370 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Transmembrane 371 394 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Topological domain 395 408 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Transmembrane 409 433 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Topological domain 434 473 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Glycosylation 72 72 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36032 UniProtKB Sequence conflict 342 342 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36032 UniProtKB Sequence conflict 342 342 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08777 1 521 +Q08777 UniProtKB Chain 1 521 . . . ID=PRO_0000257810;Note=Riboflavin transporter MCH5 +Q08777 UniProtKB Topological domain 1 103 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Transmembrane 104 124 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Topological domain 125 143 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Transmembrane 144 164 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Topological domain 165 172 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Topological domain 194 200 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Transmembrane 201 221 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Topological domain 222 233 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Transmembrane 234 254 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Topological domain 255 269 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Transmembrane 270 290 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Topological domain 291 325 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Transmembrane 326 346 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Topological domain 347 367 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Transmembrane 368 388 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Topological domain 389 396 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Transmembrane 397 417 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Topological domain 418 422 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Transmembrane 423 443 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Topological domain 444 461 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Transmembrane 462 482 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Topological domain 483 487 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Transmembrane 488 508 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Topological domain 509 521 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Glycosylation 125 125 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Glycosylation 194 194 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Glycosylation 419 419 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08777 UniProtKB Sequence conflict 495 495 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08777 UniProtKB Sequence conflict 495 495 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12262 1 181 +Q12262 UniProtKB Chain 1 181 . . . ID=PRO_0000096281;Note=Central kinetochore subunit MCM16 +Q12262 UniProtKB Coiled coil 112 171 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06675 1 368 +Q06675 UniProtKB Chain 1 368 . . . ID=PRO_0000096282;Note=Central kinetochore subunit MCM21 +Q06675 UniProtKB Coiled coil 1 43 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06675 UniProtKB Modified residue 88 88 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P11746 1 286 +P11746 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P11746 UniProtKB Chain 2 286 . . . ID=PRO_0000199439;Note=Pheromone receptor transcription factor +P11746 UniProtKB Domain 18 72 . . . Note=MADS-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00251 +P11746 UniProtKB Compositional bias 98 120 . . . Note=Asp/Glu-rich (acidic) +P11746 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P11746 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P11746 UniProtKB Modified residue 144 144 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P11746 UniProtKB Sequence conflict 9 9 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11746 UniProtKB Sequence conflict 37 37 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11746 UniProtKB Sequence conflict 156 157 . . . Note=GA->AR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11746 UniProtKB Sequence conflict 158 286 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11746 UniProtKB Helix 29 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNM +P11746 UniProtKB Beta strand 57 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNM +P11746 UniProtKB Beta strand 69 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNM +P11746 UniProtKB Turn 75 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNM +P11746 UniProtKB Helix 79 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNM +P11746 UniProtKB Helix 84 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNM +##sequence-region P17505 1 334 +P17505 UniProtKB Transit peptide 1 17 . . . Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:3072021,ECO:0000269|PubMed:3552052;Dbxref=PMID:3072021,PMID:3552052 +P17505 UniProtKB Chain 18 334 . . . ID=PRO_0000018633;Note=Malate dehydrogenase%2C mitochondrial +P17505 UniProtKB Nucleotide binding 24 30 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P17505 UniProtKB Nucleotide binding 135 137 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P17505 UniProtKB Active site 195 195 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P17505 UniProtKB Binding site 50 50 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P17505 UniProtKB Binding site 99 99 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004 +P17505 UniProtKB Binding site 105 105 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004 +P17505 UniProtKB Binding site 112 112 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P17505 UniProtKB Binding site 137 137 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004 +P17505 UniProtKB Binding site 171 171 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004 +P17505 UniProtKB Binding site 245 245 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P17505 UniProtKB Modified residue 177 177 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P17505 UniProtKB Modified residue 199 199 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P17505 UniProtKB Sequence conflict 68 68 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17505 UniProtKB Sequence conflict 306 306 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07923 1 191 +Q07923 UniProtKB Chain 1 191 . . . ID=PRO_0000234661;Note=NAD(P)H-dependent FMN reductase LOT6 +Q07923 UniProtKB Region 94 97 . . . Note=FMN binding +Q07923 UniProtKB Binding site 11 11 . . . Note=FMN +Q07923 UniProtKB Binding site 124 124 . . . Note=FMN +Q07923 UniProtKB Beta strand 2 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I +Q07923 UniProtKB Helix 16 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I +Q07923 UniProtKB Turn 31 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I +Q07923 UniProtKB Beta strand 39 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I +Q07923 UniProtKB Helix 45 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I +Q07923 UniProtKB Helix 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I +Q07923 UniProtKB Helix 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I +Q07923 UniProtKB Helix 73 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I +Q07923 UniProtKB Beta strand 86 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I +Q07923 UniProtKB Helix 101 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I +Q07923 UniProtKB Turn 112 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I +Q07923 UniProtKB Beta strand 118 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I +Q07923 UniProtKB Turn 126 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I +Q07923 UniProtKB Helix 130 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I +Q07923 UniProtKB Beta strand 146 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I +Q07923 UniProtKB Turn 164 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I +Q07923 UniProtKB Helix 168 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I +Q07923 UniProtKB Helix 174 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T0I +##sequence-region P25369 1 354 +P25369 UniProtKB Chain 1 354 . . . ID=PRO_0000084502;Note=LAS seventeen-binding protein 5 +P25369 UniProtKB Domain 15 161 . . . Note=VHS +##sequence-region P53145 1 640 +P53145 UniProtKB Chain 1 640 . . . ID=PRO_0000122454;Note=Large subunit GTPase 1 +P53145 UniProtKB Domain 188 394 . . . Note=CP-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01058 +P53145 UniProtKB Nucleotide binding 236 239 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53145 UniProtKB Nucleotide binding 343 350 . . . Note=GTP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53145 UniProtKB Nucleotide binding 387 390 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53145 UniProtKB Modified residue 103 103 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53145 UniProtKB Mutagenesis 204 204 . . . Note=Impairs the nuclear export of 60S ribosomal subunit in cytoplasm. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15660131;Dbxref=PMID:15660131 +P53145 UniProtKB Mutagenesis 349 349 . . . Note=Dominant negative mutant%3B prevents the nuclear export of 60S ribosomal subunit in cytoplasm. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15660131;Dbxref=PMID:15660131 +##sequence-region P34078 1 463 +P34078 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P34078 UniProtKB Chain 2 463 . . . ID=PRO_0000084522;Note=Protein LTV1 +P34078 UniProtKB Coiled coil 355 462 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34078 UniProtKB Motif 168 179 . . . Note=Nuclear export signal +P34078 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P34078 UniProtKB Modified residue 288 288 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34078 UniProtKB Modified residue 293 293 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34078 UniProtKB Modified residue 299 299 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34078 UniProtKB Modified residue 303 303 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P40957 1 749 +P40957 UniProtKB Chain 1 749 . . . ID=PRO_0000213798;Note=Spindle assembly checkpoint component MAD1 +P40957 UniProtKB Coiled coil 57 324 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40957 UniProtKB Coiled coil 390 656 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40957 UniProtKB Compositional bias 323 329 . . . Note=Poly-Asp +P40957 UniProtKB Compositional bias 330 347 . . . Note=Poly-Asn +P40957 UniProtKB Compositional bias 355 363 . . . Note=Poly-Asn +P40957 UniProtKB Compositional bias 601 604 . . . Note=Poly-Leu +P40957 UniProtKB Modified residue 502 502 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40957 UniProtKB Mutagenesis 653 655 . . . Note=Abolishes interaction with BUB1 and BUB3 and spindle checkpoint function. RLK->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10837255;Dbxref=PMID:10837255 +##sequence-region P40958 1 196 +P40958 UniProtKB Chain 1 196 . . . ID=PRO_0000126115;Note=Mitotic spindle checkpoint component MAD2 +P40958 UniProtKB Domain 8 192 . . . Note=HORMA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00109 +##sequence-region P20484 1 414 +P20484 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P20484 UniProtKB Chain 2 414 . . . ID=PRO_0000051079;Note=Protein MAK11 +P20484 UniProtKB Repeat 50 78 . . . Note=WD 1 +P20484 UniProtKB Repeat 90 135 . . . Note=WD 2 +P20484 UniProtKB Repeat 147 177 . . . Note=WD 3 +P20484 UniProtKB Repeat 189 221 . . . Note=WD 4 +P20484 UniProtKB Repeat 238 267 . . . Note=WD 5 +P20484 UniProtKB Repeat 298 330 . . . Note=WD 6 +P20484 UniProtKB Compositional bias 386 408 . . . Note=Lys-rich (basic) +P20484 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P20484 UniProtKB Modified residue 376 376 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P20484 UniProtKB Modified residue 380 380 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P20484 UniProtKB Modified residue 382 382 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P38112 1 773 +P38112 UniProtKB Chain 1 773 . . . ID=PRO_0000055048;Note=ATP-dependent RNA helicase MAK5 +P38112 UniProtKB Domain 202 399 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P38112 UniProtKB Domain 452 615 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P38112 UniProtKB Nucleotide binding 215 222 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P38112 UniProtKB Motif 171 199 . . . Note=Q motif +P38112 UniProtKB Motif 333 336 . . . Note=DEAD box +P38112 UniProtKB Modified residue 135 135 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38112 UniProtKB Modified residue 138 138 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38112 UniProtKB Modified residue 678 678 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38112 UniProtKB Mutagenesis 218 218 . . . Note=Delays the appearance and decreases the level of 25S rRNA. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:13680366;Dbxref=PMID:13680366 +##sequence-region P57743 1 89 +P57743 UniProtKB Chain 1 89 . . . ID=PRO_0000125563;Note=U6 snRNA-associated Sm-like protein LSm3 +P57743 UniProtKB Mutagenesis 36 36 . . . Note=Strongly reduces affinity for poly-U RNA ends. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24240276;Dbxref=PMID:24240276 +P57743 UniProtKB Mutagenesis 38 38 . . . Note=Strongly reduces affinity for poly-U RNA ends. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24240276;Dbxref=PMID:24240276 +P57743 UniProtKB Mutagenesis 69 69 . . . Note=Strongly reduces affinity for poly-U RNA ends. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24240276,ECO:0000269|PubMed:24513854;Dbxref=PMID:24240276,PMID:24513854 +P57743 UniProtKB Helix 4 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P57743 UniProtKB Turn 10 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P57743 UniProtKB Beta strand 14 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P57743 UniProtKB Turn 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P57743 UniProtKB Beta strand 24 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P57743 UniProtKB Beta strand 39 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P57743 UniProtKB Beta strand 55 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P57743 UniProtKB Helix 70 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +P57743 UniProtKB Beta strand 73 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +##sequence-region Q06406 1 86 +Q06406 UniProtKB Chain 1 86 . . . ID=PRO_0000125578;Note=U6 snRNA-associated Sm-like protein LSm6 +Q06406 UniProtKB Mutagenesis 74 74 . . . Note=Reduces affinity for poly-U RNA ends. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24240276,ECO:0000269|PubMed:24513854;Dbxref=PMID:24240276,PMID:24513854 +Q06406 UniProtKB Helix 11 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +Q06406 UniProtKB Turn 18 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +Q06406 UniProtKB Beta strand 22 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +Q06406 UniProtKB Beta strand 31 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +Q06406 UniProtKB Beta strand 47 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +Q06406 UniProtKB Turn 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M75 +Q06406 UniProtKB Beta strand 65 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M7A +Q06406 UniProtKB Beta strand 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +Q06406 UniProtKB Helix 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +Q06406 UniProtKB Beta strand 78 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C92 +##sequence-region P36007 1 326 +P36007 UniProtKB Chain 1 326 . . . ID=PRO_0000185589;Note=L-threo-3-hydroxyaspartate ammonia-lyase +P36007 UniProtKB Region 179 183 . . . Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04968 +P36007 UniProtKB Binding site 80 80 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04968 +P36007 UniProtKB Binding site 304 304 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04968 +P36007 UniProtKB Modified residue 53 53 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04968 +##sequence-region P38156 1 614 +P38156 UniProtKB Chain 1 614 . . . ID=PRO_0000050422;Note=Maltose permease MAL31 +P38156 UniProtKB Topological domain 1 108 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Transmembrane 109 129 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Topological domain 130 144 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Transmembrane 145 165 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Topological domain 166 180 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Transmembrane 181 201 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Topological domain 202 202 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Transmembrane 203 223 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Topological domain 224 236 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Transmembrane 237 257 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Topological domain 258 272 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Transmembrane 273 293 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Topological domain 294 364 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Transmembrane 365 385 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Topological domain 386 398 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Transmembrane 399 419 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Topological domain 420 427 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Transmembrane 428 448 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Topological domain 449 460 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Transmembrane 461 481 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Topological domain 482 493 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Transmembrane 494 514 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Topological domain 515 526 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Transmembrane 527 547 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38156 UniProtKB Topological domain 548 614 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P22855 1 1083 +P22855 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P22855 UniProtKB Chain 2 1083 . . . ID=PRO_0000206910;Note=Alpha-mannosidase +P22855 UniProtKB Active site 411 411 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22855 UniProtKB Metal binding 298 298 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22855 UniProtKB Metal binding 300 300 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22855 UniProtKB Metal binding 411 411 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22855 UniProtKB Metal binding 626 626 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22855 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P22855 UniProtKB Sequence conflict 786 786 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22855 UniProtKB Sequence conflict 798 798 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q92328 1 271 +Q92328 UniProtKB Chain 1 271 . . . ID=PRO_0000096329;Note=Mitochondrial distribution and morphology protein 12 +Q92328 UniProtKB Cross-link 49 49 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q92328 UniProtKB Sequence conflict 91 91 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q92328 UniProtKB Sequence conflict 269 269 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q92328 UniProtKB Beta strand 1 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD +Q92328 UniProtKB Helix 8 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD +Q92328 UniProtKB Helix 16 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD +Q92328 UniProtKB Beta strand 37 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD +Q92328 UniProtKB Beta strand 49 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD +Q92328 UniProtKB Helix 64 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD +Q92328 UniProtKB Beta strand 119 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD +Q92328 UniProtKB Beta strand 132 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD +Q92328 UniProtKB Beta strand 143 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD +Q92328 UniProtKB Beta strand 149 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD +Q92328 UniProtKB Beta strand 174 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD +Q92328 UniProtKB Helix 186 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD +Q92328 UniProtKB Helix 200 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD +Q92328 UniProtKB Helix 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD +Q92328 UniProtKB Beta strand 213 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD +Q92328 UniProtKB Helix 225 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD +Q92328 UniProtKB Helix 231 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD +Q92328 UniProtKB Beta strand 262 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GYD +##sequence-region P38295 1 451 +P38295 UniProtKB Chain 1 451 . . . ID=PRO_0000212454;Note=Medium-chain fatty acid ethyl ester synthase/esterase 2 +P38295 UniProtKB Domain 166 430 . . . Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38295 UniProtKB Active site 247 247 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38295 UniProtKB Active site 395 395 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38295 UniProtKB Active site 423 423 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38295 UniProtKB Cross-link 114 114 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P47167 1 239 +P47167 UniProtKB Chain 1 239 . . . ID=PRO_0000096283;Note=Central kinetochore subunit MCM22 +##sequence-region P29469 1 868 +P29469 UniProtKB Chain 1 868 . . . ID=PRO_0000194091;Note=DNA replication licensing factor MCM2 +P29469 UniProtKB Domain 493 700 . . . Note=MCM +P29469 UniProtKB Zinc finger 341 367 . . . Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P29469 UniProtKB Nucleotide binding 543 550 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P29469 UniProtKB Motif 675 678 . . . Note=Arginine finger +P29469 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P29469 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P29469 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P29469 UniProtKB Modified residue 164 164 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P29469 UniProtKB Modified residue 170 170 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P29469 UniProtKB Natural variant 392 392 . . . Note=In allele MCM2-1. E->K +P29469 UniProtKB Mutagenesis 364 364 . . . Note=Loss of activity. C->Y%2CF%2CS%2CH;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2044961;Dbxref=PMID:2044961 +P29469 UniProtKB Mutagenesis 367 367 . . . Note=Loss of activity. C->Y%2CF%2CS%2CH;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2044961;Dbxref=PMID:2044961 +P29469 UniProtKB Mutagenesis 549 549 . . . Note=Reduces MCM2-7 complex helicase activity. Abolishes MCM2-7 complex helicase activity%3B when associated with MCM5 A-422. Reduces MCM2-7 complex helicase activity%3B when associated with MCM3 A-415. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657510;Dbxref=PMID:18657510 +P29469 UniProtKB Mutagenesis 676 676 . . . Note=Loss of MCM2-7 complex helicase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657510;Dbxref=PMID:18657510 +P29469 UniProtKB Sequence conflict 164 164 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29469 UniProtKB Sequence conflict 172 173 . . . Note=MD->IH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29469 UniProtKB Sequence conflict 529 529 . . . Note=G->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29469 UniProtKB Sequence conflict 578 578 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29469 UniProtKB Sequence conflict 583 583 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29469 UniProtKB Sequence conflict 712 712 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29469 UniProtKB Sequence conflict 733 747 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29469 UniProtKB Sequence conflict 859 868 . . . Note=RSFAIYTLGH->SLSQFIPWVTKTLLFLRISGYEDKKFSVSIHVLAILFSIYKFPLFFV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P30665 1 933 +P30665 UniProtKB Chain 1 933 . . . ID=PRO_0000194105;Note=DNA replication licensing factor MCM4 +P30665 UniProtKB Domain 518 725 . . . Note=MCM +P30665 UniProtKB Nucleotide binding 568 575 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P30665 UniProtKB Motif 700 703 . . . Note=Arginine finger +P30665 UniProtKB Modified residue 52 52 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P30665 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P30665 UniProtKB Modified residue 69 69 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P30665 UniProtKB Mutagenesis 574 574 . . . Note=Loss of MCM2-7 complex helicase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657510;Dbxref=PMID:18657510 +##sequence-region P53091 1 1017 +P53091 UniProtKB Chain 1 1017 . . . ID=PRO_0000194117;Note=DNA replication licensing factor MCM6 +P53091 UniProtKB Domain 525 732 . . . Note=MCM +P53091 UniProtKB Nucleotide binding 575 582 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53091 UniProtKB Motif 707 710 . . . Note=Arginine finger +P53091 UniProtKB Modified residue 78 78 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53091 UniProtKB Modified residue 249 249 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53091 UniProtKB Modified residue 372 372 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53091 UniProtKB Modified residue 766 766 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P53091 UniProtKB Mutagenesis 581 581 . . . Note=Loss of MCM2-7 complex helicase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657510;Dbxref=PMID:18657510 +P53091 UniProtKB Sequence conflict 179 179 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38132 1 845 +P38132 UniProtKB Chain 1 845 . . . ID=PRO_0000194124;Note=DNA replication licensing factor MCM7 +P38132 UniProtKB Domain 410 617 . . . Note=MCM +P38132 UniProtKB Nucleotide binding 460 467 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38132 UniProtKB Motif 592 595 . . . Note=Arginine finger +P38132 UniProtKB Modified residue 811 811 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P38132 UniProtKB Modified residue 819 819 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38132 UniProtKB Modified residue 838 838 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38132 UniProtKB Mutagenesis 466 466 . . . Note=Loss of MCM2-7 complex helicase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657510;Dbxref=PMID:18657510 +P38132 UniProtKB Sequence conflict 552 552 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38132 UniProtKB Sequence conflict 552 552 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38132 UniProtKB Sequence conflict 556 558 . . . Note=TLN->NPG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38132 UniProtKB Sequence conflict 556 558 . . . Note=TLN->NPG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38132 UniProtKB Sequence conflict 574 574 . . . Note=Y->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38132 UniProtKB Sequence conflict 574 574 . . . Note=Y->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32419 1 343 +P32419 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1447211;Dbxref=PMID:1447211 +P32419 UniProtKB Chain 2 343 . . . ID=PRO_0000113342;Note=Malate dehydrogenase%2C peroxisomal +P32419 UniProtKB Nucleotide binding 8 14 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32419 UniProtKB Nucleotide binding 116 118 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32419 UniProtKB Active site 187 187 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32419 UniProtKB Binding site 34 34 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32419 UniProtKB Binding site 80 80 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004 +P32419 UniProtKB Binding site 86 86 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004 +P32419 UniProtKB Binding site 93 93 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32419 UniProtKB Binding site 118 118 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004 +P32419 UniProtKB Binding site 152 152 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004 +P32419 UniProtKB Binding site 237 237 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32419 UniProtKB Sequence conflict 240 240 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q05930 1 598 +Q05930 UniProtKB Chain 1 598 . . . ID=PRO_0000119969;Note=Mitochondrial distribution and morphology protein 30 +Q05930 UniProtKB Domain 13 59 . . . Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080 +##sequence-region Q12285 1 212 +Q12285 UniProtKB Chain 1 212 . . . ID=PRO_0000235917;Note=Ubiquitin-like protein MDY2 +Q12285 UniProtKB Domain 74 152 . . . Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 +Q12285 UniProtKB Helix 4 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LKU +Q12285 UniProtKB Helix 8 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +Q12285 UniProtKB Helix 35 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WPV +Q12285 UniProtKB Beta strand 74 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A20 +Q12285 UniProtKB Beta strand 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A20 +Q12285 UniProtKB Beta strand 86 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A20 +Q12285 UniProtKB Helix 98 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A20 +Q12285 UniProtKB Helix 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A20 +Q12285 UniProtKB Beta strand 117 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A20 +Q12285 UniProtKB Beta strand 124 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A20 +Q12285 UniProtKB Helix 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A20 +Q12285 UniProtKB Beta strand 139 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZDM +Q12285 UniProtKB Beta strand 143 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A20 +Q12285 UniProtKB Helix 179 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VEJ +Q12285 UniProtKB Turn 190 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VEJ +Q12285 UniProtKB Helix 194 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VEJ +##sequence-region P32259 1 974 +P32259 UniProtKB Chain 1 974 . . . ID=PRO_0000096364;Note=Mediator of RNA polymerase II transcription subunit 16 +P32259 UniProtKB Motif 889 893 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32259 UniProtKB Compositional bias 63 81 . . . Note=Ser/Thr-rich +##sequence-region Q08278 1 222 +Q08278 UniProtKB Chain 1 222 . . . ID=PRO_0000096393;Note=Mediator of RNA polymerase II transcription subunit 7 +Q08278 UniProtKB Helix 18 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI +Q08278 UniProtKB Helix 25 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI +Q08278 UniProtKB Helix 61 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI +Q08278 UniProtKB Helix 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI +Q08278 UniProtKB Helix 112 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKH +Q08278 UniProtKB Beta strand 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKH +Q08278 UniProtKB Helix 141 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKH +Q08278 UniProtKB Helix 144 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKH +Q08278 UniProtKB Helix 166 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKH +##sequence-region P38304 1 223 +P38304 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9918841;Dbxref=PMID:9918841 +P38304 UniProtKB Chain 2 223 . . . ID=PRO_0000096397;Note=Mediator of RNA polymerase II transcription subunit 8 +P38304 UniProtKB Region 2 138 . . . Note=Interaction with TBP1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16964259;Dbxref=PMID:16964259 +P38304 UniProtKB Coiled coil 33 59 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38304 UniProtKB Helix 198 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZS +##sequence-region P24719 1 497 +P24719 UniProtKB Chain 1 497 . . . ID=PRO_0000086321;Note=Meiosis-specific serine/threonine-protein kinase MEK1 +P24719 UniProtKB Domain 47 102 . . . Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 +P24719 UniProtKB Domain 162 444 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P24719 UniProtKB Nucleotide binding 168 176 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P24719 UniProtKB Active site 290 290 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P24719 UniProtKB Binding site 199 199 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +##sequence-region Q12198 1 575 +Q12198 UniProtKB Chain 1 575 . . . ID=PRO_0000114782;Note=Putative cystathionine gamma-synthase YLL058W +Q12198 UniProtKB Modified residue 376 376 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q99257 1 599 +Q99257 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q99257 UniProtKB Chain 2 599 . . . ID=PRO_0000220542;Note=mRNA export factor MEX67 +Q99257 UniProtKB Repeat 163 184 . . . Note=LRR 1 +Q99257 UniProtKB Repeat 189 210 . . . Note=LRR 2 +Q99257 UniProtKB Domain 224 262 . . . Note=LRRCT +Q99257 UniProtKB Domain 280 467 . . . Note=NTF2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00137 +Q99257 UniProtKB Domain 546 599 . . . Note=TAP-C;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00611 +Q99257 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q99257 UniProtKB Mutagenesis 400 400 . . . Note=Impairs association with the nuclear pores and interaction with MTR2. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10952996;Dbxref=PMID:10952996 +Q99257 UniProtKB Beta strand 24 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Helix 35 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Beta strand 51 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Beta strand 59 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Helix 67 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Beta strand 82 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Beta strand 87 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Helix 102 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Turn 117 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Beta strand 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Helix 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Helix 131 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Beta strand 140 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Helix 148 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Beta strand 165 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Helix 177 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Helix 183 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Beta strand 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Helix 205 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Beta strand 218 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Helix 225 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Helix 232 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Helix 254 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Beta strand 269 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Helix 279 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +Q99257 UniProtKB Helix 296 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +Q99257 UniProtKB Beta strand 303 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +Q99257 UniProtKB Turn 332 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Turn 341 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Helix 347 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +Q99257 UniProtKB Helix 357 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +Q99257 UniProtKB Beta strand 371 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +Q99257 UniProtKB Turn 375 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +Q99257 UniProtKB Helix 379 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +Q99257 UniProtKB Beta strand 383 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +Q99257 UniProtKB Helix 390 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +Q99257 UniProtKB Beta strand 394 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +Q99257 UniProtKB Beta strand 441 454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +Q99257 UniProtKB Beta strand 457 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +Q99257 UniProtKB Helix 546 559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JP7 +Q99257 UniProtKB Helix 563 572 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JP7 +Q99257 UniProtKB Turn 573 575 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JP7 +Q99257 UniProtKB Helix 578 586 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JP7 +Q99257 UniProtKB Turn 588 590 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JP7 +Q99257 UniProtKB Helix 593 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JP7 +##sequence-region P34166 1 38 +P34166 UniProtKB Propeptide 1 23 . . . ID=PRO_0000021693;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3542988;Dbxref=PMID:3542988 +P34166 UniProtKB Peptide 24 35 . . . ID=PRO_0000021694;Note=Mating hormone A-factor 2 +P34166 UniProtKB Propeptide 36 38 . . . ID=PRO_0000021695;Note=Removed in mature form +P34166 UniProtKB Modified residue 35 35 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3056940;Dbxref=PMID:3056940 +P34166 UniProtKB Lipidation 35 35 . . . Note=S-farnesyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3056940;Dbxref=PMID:3056940 +##sequence-region P40578 1 1113 +P40578 UniProtKB Chain 1 1113 . . . ID=PRO_0000067074;Note=Protein MGA2 +P40578 UniProtKB Transmembrane 1037 1054 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40578 UniProtKB Domain 530 610 . . . Note=IPT/TIG +P40578 UniProtKB Repeat 719 748 . . . Note=ANK 1 +P40578 UniProtKB Repeat 752 781 . . . Note=ANK 2 +P40578 UniProtKB Modified residue 255 255 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40578 UniProtKB Modified residue 467 467 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +##sequence-region P43638 1 1398 +P43638 UniProtKB Chain 1 1398 . . . ID=PRO_0000072754;Note=MAP-homologous protein 1 +P43638 UniProtKB Region 1227 1258 . . . Note=Tau/MAP repeat-like;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8947554;Dbxref=PMID:8947554 +P43638 UniProtKB Compositional bias 66 69 . . . Note=Poly-Ser +P43638 UniProtKB Compositional bias 128 137 . . . Note=Poly-His +P43638 UniProtKB Compositional bias 396 400 . . . Note=Poly-Asn +P43638 UniProtKB Compositional bias 423 426 . . . Note=Poly-Ser +P43638 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P43638 UniProtKB Modified residue 81 81 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43638 UniProtKB Modified residue 222 222 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P43638 UniProtKB Modified residue 309 309 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P43638 UniProtKB Modified residue 311 311 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P43638 UniProtKB Modified residue 354 354 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43638 UniProtKB Modified residue 357 357 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43638 UniProtKB Modified residue 577 577 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P43638 UniProtKB Cross-link 221 221 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P43638 UniProtKB Sequence conflict 108 108 . . . Note=R->RV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43638 UniProtKB Sequence conflict 112 184 . . . Note=KSVVETNLSNVEADSGHHHHHRHHHHTEDAPAPKKVGFFKSLFGHRKKDQEQQEKERERKERSPSPTHVDRGA->QWWRLTCLTLRLTPDIITTTATTITRKMLLHLRRSDSLRVCLAIGRRIRNNRRRNEKGKSAHPLRLTWTVAR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43638 UniProtKB Sequence conflict 331 331 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43638 UniProtKB Sequence conflict 419 419 . . . Note=T->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43638 UniProtKB Sequence conflict 594 595 . . . Note=ID->MH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43638 UniProtKB Sequence conflict 619 619 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43638 UniProtKB Sequence conflict 659 660 . . . Note=KQ->NE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43638 UniProtKB Sequence conflict 1175 1176 . . . Note=LL->FI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43638 UniProtKB Sequence conflict 1309 1320 . . . Note=KQGNQEETAFRT->NRETKKRPRSEP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43638 UniProtKB Sequence conflict 1339 1339 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43638 UniProtKB Sequence conflict 1356 1356 . . . Note=A->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12525 1 324 +Q12525 UniProtKB Chain 1 324 . . . ID=PRO_0000114618;Note=Homocysteine S-methyltransferase 1 +Q12525 UniProtKB Domain 6 320 . . . Note=Hcy-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00333 +Q12525 UniProtKB Metal binding 238 238 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00333 +Q12525 UniProtKB Metal binding 305 305 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00333 +Q12525 UniProtKB Metal binding 306 306 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00333 +##sequence-region P38880 1 579 +P38880 UniProtKB Transit peptide 1 47 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38880 UniProtKB Chain 48 579 . . . ID=PRO_0000021664;Note=Mitochondrial distribution and morphology protein 31 +P38880 UniProtKB Topological domain 48 114 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38880 UniProtKB Transmembrane 115 135 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38880 UniProtKB Topological domain 136 558 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38880 UniProtKB Transmembrane 559 578 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38880 UniProtKB Topological domain 579 579 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53083 1 459 +P53083 UniProtKB Chain 1 459 . . . ID=PRO_0000096331;Note=Mitochondrial distribution and morphology protein 34 +##sequence-region Q12019 1 4910 +Q12019 UniProtKB Chain 1 4910 . . . ID=PRO_0000096337;Note=Midasin +Q12019 UniProtKB Domain 4704 4899 . . . Note=VWFA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00219 +Q12019 UniProtKB Nucleotide binding 315 322 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12019 UniProtKB Nucleotide binding 653 660 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12019 UniProtKB Nucleotide binding 1083 1090 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12019 UniProtKB Nucleotide binding 1368 1375 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12019 UniProtKB Nucleotide binding 1747 1754 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12019 UniProtKB Nucleotide binding 2054 2061 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12019 UniProtKB Compositional bias 768 771 . . . Note=Poly-Lys +Q12019 UniProtKB Compositional bias 2904 2907 . . . Note=Poly-Leu +Q12019 UniProtKB Compositional bias 4136 4139 . . . Note=Poly-Glu +Q12019 UniProtKB Modified residue 1026 1026 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12019 UniProtKB Modified residue 2971 2971 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12019 UniProtKB Modified residue 4353 4353 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12019 UniProtKB Modified residue 4388 4388 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12019 UniProtKB Modified residue 4555 4555 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q06213 1 157 +Q06213 UniProtKB Chain 1 157 . . . ID=PRO_0000096357;Note=Mediator of RNA polymerase II transcription subunit 10 +##sequence-region P32585 1 307 +P32585 UniProtKB Chain 1 307 . . . ID=PRO_0000096368;Note=Mediator of RNA polymerase II transcription subunit 18 +P32585 UniProtKB Mutagenesis 22 22 . . . Note=In SRB5-1%3B suppresses the phenotypic defects of an RNA polymerase II CTD truncation. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8324825;Dbxref=PMID:8324825 +P32585 UniProtKB Sequence conflict 225 225 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32585 UniProtKB Beta strand 3 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Helix 13 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Helix 16 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Beta strand 32 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Helix 45 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Beta strand 64 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Helix 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Helix 75 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZS +P32585 UniProtKB Turn 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZS +P32585 UniProtKB Helix 87 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Beta strand 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Beta strand 164 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Helix 173 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Beta strand 180 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Helix 200 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Beta strand 209 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Helix 225 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Beta strand 229 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Beta strand 242 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Turn 246 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Beta strand 250 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Helix 265 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Turn 282 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Helix 293 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P32585 UniProtKB Helix 299 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +##sequence-region P25046 1 220 +P25046 UniProtKB Chain 1 220 . . . ID=PRO_0000096370;Note=Mediator of RNA polymerase II transcription subunit 19 +P25046 UniProtKB Sequence conflict 18 18 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P34162 1 210 +P34162 UniProtKB Chain 1 210 . . . ID=PRO_0000096374;Note=Mediator of RNA polymerase II transcription subunit 20 +P34162 UniProtKB Compositional bias 1 210 . . . Note=Ser/Thr/Tyr-rich +P34162 UniProtKB Mutagenesis 14 14 . . . Note=In SRB2-1%3B suppresses the phenotypic defects of an RNA polymerase II CTD truncation. P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1591782;Dbxref=PMID:1591782 +P34162 UniProtKB Beta strand 4 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P34162 UniProtKB Helix 16 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P34162 UniProtKB Helix 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P34162 UniProtKB Beta strand 30 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZS +P34162 UniProtKB Beta strand 35 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P34162 UniProtKB Beta strand 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZS +P34162 UniProtKB Beta strand 56 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P34162 UniProtKB Beta strand 76 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P34162 UniProtKB Helix 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P34162 UniProtKB Helix 89 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P34162 UniProtKB Helix 104 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P34162 UniProtKB Turn 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P34162 UniProtKB Beta strand 116 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P34162 UniProtKB Beta strand 135 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P34162 UniProtKB Beta strand 147 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P34162 UniProtKB Helix 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P34162 UniProtKB Helix 163 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P34162 UniProtKB Beta strand 183 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +P34162 UniProtKB Helix 196 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HZM +##sequence-region P40469 1 1032 +P40469 UniProtKB Chain 1 1032 . . . ID=PRO_0000096445;Note=DNA repair/transcription protein MET18/MMS19 +P40469 UniProtKB Repeat 40 77 . . . Note=HEAT 1 +P40469 UniProtKB Repeat 121 160 . . . Note=HEAT 2 +P40469 UniProtKB Repeat 256 293 . . . Note=HEAT 3 +P40469 UniProtKB Repeat 463 500 . . . Note=HEAT 4 +P40469 UniProtKB Repeat 504 542 . . . Note=HEAT 5 +P40469 UniProtKB Repeat 550 587 . . . Note=HEAT 6 +P40469 UniProtKB Repeat 614 651 . . . Note=HEAT 7 +P40469 UniProtKB Repeat 759 796 . . . Note=HEAT 8 +P40469 UniProtKB Repeat 808 850 . . . Note=HEAT 9 +P40469 UniProtKB Repeat 863 901 . . . Note=HEAT 10 +P40469 UniProtKB Repeat 906 943 . . . Note=HEAT 11 +P40469 UniProtKB Repeat 947 987 . . . Note=HEAT 12 +P40469 UniProtKB Repeat 992 1029 . . . Note=HEAT 13 +P40469 UniProtKB Compositional bias 628 635 . . . Note=Poly-Asn +P40469 UniProtKB Natural variant 111 112 . . . Note=In strain: SK1. AL->SF +P40469 UniProtKB Natural variant 329 329 . . . Note=In strain: SK1. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P40469 UniProtKB Natural variant 335 335 . . . Note=In strain: SK1. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P40469 UniProtKB Natural variant 444 444 . . . Note=In strain: SK1. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P40469 UniProtKB Natural variant 697 697 . . . Note=In strain: SK1. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P40469 UniProtKB Natural variant 814 814 . . . Note=In strain: SK1. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P40469 UniProtKB Natural variant 816 816 . . . Note=In strain: SK1. K->M +P40469 UniProtKB Natural variant 930 930 . . . Note=In strain: SK1. A->T +P40469 UniProtKB Natural variant 963 963 . . . Note=In strain: SK1. H->Q +P40469 UniProtKB Natural variant 969 969 . . . Note=In strain: SK1. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P40469 UniProtKB Sequence conflict 230 230 . . . Note=P->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40469 UniProtKB Sequence conflict 329 329 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40469 UniProtKB Sequence conflict 335 335 . . . Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40469 UniProtKB Sequence conflict 361 361 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32179 1 357 +P32179 UniProtKB Chain 1 357 . . . ID=PRO_0000142537;Note=3'(2')%2C5'-bisphosphate nucleotidase +P32179 UniProtKB Region 144 147 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32179 UniProtKB Metal binding 72 72 . . . Note=Magnesium 1 +P32179 UniProtKB Metal binding 142 142 . . . Note=Magnesium 1 +P32179 UniProtKB Metal binding 142 142 . . . Note=Magnesium 2 +P32179 UniProtKB Metal binding 144 144 . . . Note=Magnesium 1%3B via carbonyl oxygen +P32179 UniProtKB Metal binding 145 145 . . . Note=Magnesium 2 +P32179 UniProtKB Metal binding 294 294 . . . Note=Magnesium 2 +P32179 UniProtKB Binding site 72 72 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32179 UniProtKB Binding site 294 294 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32179 UniProtKB Natural variant 40 40 . . . Note=In strain: Montrache. N->S +P32179 UniProtKB Natural variant 61 61 . . . Note=In strain: Montrache. K->M +P32179 UniProtKB Natural variant 63 63 . . . Note=In strain: Montrache. N->S +P32179 UniProtKB Natural variant 308 308 . . . Note=In strain: Montrache. I->V +P32179 UniProtKB Helix 4 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Turn 31 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Beta strand 35 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Beta strand 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Helix 47 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Beta strand 69 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Helix 80 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Beta strand 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Helix 118 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Beta strand 134 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Helix 147 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Beta strand 157 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Beta strand 167 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Helix 180 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Turn 189 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Beta strand 196 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Turn 202 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K9Z +P32179 UniProtKB Beta strand 206 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Turn 211 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Beta strand 218 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K9Z +P32179 UniProtKB Helix 228 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Beta strand 232 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Turn 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Helix 244 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Beta strand 258 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Helix 266 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Beta strand 277 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Helix 292 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Helix 296 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Beta strand 308 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Beta strand 312 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Beta strand 322 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Beta strand 327 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Beta strand 331 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +P32179 UniProtKB Helix 338 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KA1 +##sequence-region P34165 1 36 +P34165 UniProtKB Propeptide 1 21 . . . ID=PRO_0000021690;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3542988;Dbxref=PMID:3542988 +P34165 UniProtKB Peptide 22 33 . . . ID=PRO_0000021691;Note=Mating hormone A-factor 1 +P34165 UniProtKB Propeptide 34 36 . . . ID=PRO_0000021692;Note=Removed in mature form +P34165 UniProtKB Modified residue 33 33 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3056940;Dbxref=PMID:3056940 +P34165 UniProtKB Lipidation 33 33 . . . Note=S-farnesyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3056940;Dbxref=PMID:3056940 +##sequence-region P32435 1 120 +P32435 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32435 UniProtKB Propeptide 22 86 . . . ID=PRO_0000419677 +P32435 UniProtKB Peptide 87 99 . . . ID=PRO_0000021702;Note=Mating factor alpha-like +P32435 UniProtKB Propeptide 102 107 . . . ID=PRO_0000419678 +P32435 UniProtKB Peptide 108 120 . . . ID=PRO_0000021703;Note=Mating factor alpha +##sequence-region P40002 1 666 +P40002 UniProtKB Chain 1 666 . . . ID=PRO_0000202617;Note=Transcriptional regulator MIT1 +P40002 UniProtKB Compositional bias 334 382 . . . Note=Asn-rich +P40002 UniProtKB Modified residue 152 152 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38286 1 347 +P38286 UniProtKB Chain 1 347 . . . ID=PRO_0000054868;Note=Very-long-chain 3-oxoacyl-CoA reductase +P38286 UniProtKB Transmembrane 20 40 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03107 +P38286 UniProtKB Active site 223 223 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03107 +P38286 UniProtKB Binding site 210 210 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03107 +##sequence-region P32490 1 508 +P32490 UniProtKB Chain 1 508 . . . ID=PRO_0000086332;Note=MAP kinase kinase MKK1/SSP32 +P32490 UniProtKB Domain 221 488 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32490 UniProtKB Nucleotide binding 227 235 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32490 UniProtKB Active site 349 349 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P32490 UniProtKB Binding site 250 250 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32490 UniProtKB Modified residue 192 192 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P53141 1 149 +P53141 UniProtKB Chain 1 149 . . . ID=PRO_0000198765;Note=Myosin light chain 1 +P53141 UniProtKB Domain 2 37 . . . Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P53141 UniProtKB Domain 81 116 . . . Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P53141 UniProtKB Domain 117 149 . . . Note=EF-hand 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P53141 UniProtKB Calcium binding 15 26 . . . Note=1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P53141 UniProtKB Calcium binding 94 105 . . . Note=2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P53141 UniProtKB Calcium binding 121 132 . . . Note=3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P53141 UniProtKB Cross-link 116 116 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P53141 UniProtKB Mutagenesis 93 93 . . . Note=In MLC1-1%3B causes a defect in septum formation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12456647;Dbxref=PMID:12456647 +P53141 UniProtKB Mutagenesis 114 114 . . . Note=In MLC1-11%3B abolishes interaction with MYO2 and IQG1 and reduces interaction with MYO1. Leads to mislocalization of IQG1 and a severe defect in cytokinesis. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15210731;Dbxref=PMID:15210731 +P53141 UniProtKB Mutagenesis 135 135 . . . Note=In MLC1-93%3B reduces interaction with MYO1%2C but does not cause any defect in cytokinesis. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15210731;Dbxref=PMID:15210731 +P53141 UniProtKB Mutagenesis 142 142 . . . Note=In MLC1-5%3B causes a defect in septum formation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12456647;Dbxref=PMID:12456647 +P53141 UniProtKB Helix 11 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45 +P53141 UniProtKB Beta strand 20 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45 +P53141 UniProtKB Helix 24 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45 +P53141 UniProtKB Helix 27 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45 +P53141 UniProtKB Helix 40 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45 +P53141 UniProtKB Helix 51 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N2D +P53141 UniProtKB Beta strand 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45 +P53141 UniProtKB Helix 61 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45 +P53141 UniProtKB Helix 72 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45 +P53141 UniProtKB Helix 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45 +P53141 UniProtKB Helix 84 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45 +P53141 UniProtKB Beta strand 95 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45 +P53141 UniProtKB Helix 103 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45 +P53141 UniProtKB Beta strand 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N2D +P53141 UniProtKB Helix 119 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45 +P53141 UniProtKB Beta strand 135 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45 +P53141 UniProtKB Helix 139 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45 +##sequence-region Q12083 1 715 +Q12083 UniProtKB Chain 1 715 . . . ID=PRO_0000245570;Note=DNA mismatch repair protein MLH3 +##sequence-region P38998 1 373 +P38998 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:418069,ECO:0000269|Ref.4;Dbxref=PMID:418069 +P38998 UniProtKB Chain 2 373 . . . ID=PRO_0000199016;Note=Saccharopine dehydrogenase [NAD(+)%2C L-lysine-forming] +P38998 UniProtKB Active site 205 205 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:378997;Dbxref=PMID:378997 +P38998 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4 +P38998 UniProtKB Sequence conflict 209 209 . . . Note=A->AL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38998 UniProtKB Sequence conflict 309 309 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38998 UniProtKB Beta strand 5 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Helix 23 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Beta strand 35 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Beta strand 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRL +P38998 UniProtKB Helix 48 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Beta strand 57 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Helix 63 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Beta strand 71 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Beta strand 89 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Helix 104 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Beta strand 117 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Helix 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Beta strand 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UHA +P38998 UniProtKB Helix 136 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Helix 172 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Turn 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Beta strand 196 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Helix 204 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Helix 220 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Beta strand 223 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Helix 228 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Helix 239 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Beta strand 243 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Helix 262 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Beta strand 274 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Beta strand 303 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Beta strand 308 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Beta strand 313 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Helix 321 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Helix 326 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Turn 345 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Helix 351 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRJ +P38998 UniProtKB Helix 370 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QRL +##sequence-region P07702 1 1392 +P07702 UniProtKB Chain 1 1392 . . . ID=PRO_0000193153;Note=L-2-aminoadipate reductase +P07702 UniProtKB Domain 843 920 . . . Note=Carrier;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00258 +P07702 UniProtKB Modified residue 880 880 . . . Note=O-(pantetheine 4'-phosphoryl)serine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00258,ECO:0000269|PubMed:10320345;Dbxref=PMID:10320345 +P07702 UniProtKB Cross-link 541 541 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P07702 UniProtKB Cross-link 1276 1276 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P49367 1 693 +P49367 UniProtKB Transit peptide 1 20 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P49367 UniProtKB Chain 21 693 . . . ID=PRO_0000000551;Note=Homoaconitase%2C mitochondrial +P49367 UniProtKB Metal binding 340 340 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49367 UniProtKB Metal binding 407 407 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49367 UniProtKB Metal binding 410 410 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49367 UniProtKB Sequence conflict 581 581 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38999 1 446 +P38999 UniProtKB Chain 1 446 . . . ID=PRO_0000212839;Note=Saccharopine dehydrogenase [NADP(+)%2C L-glutamate-forming] +P38999 UniProtKB Sequence conflict 393 393 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38999 UniProtKB Beta strand 3 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 14 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Beta strand 27 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 36 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Turn 44 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Beta strand 49 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 58 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Beta strand 68 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 80 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Beta strand 93 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 102 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Beta strand 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Turn 124 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 128 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Beta strand 146 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Beta strand 171 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 176 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Beta strand 186 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Beta strand 193 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Turn 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 202 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Beta strand 217 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 228 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Beta strand 238 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 250 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Turn 260 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 269 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 277 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Beta strand 288 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 292 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 308 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Turn 321 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 335 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Beta strand 355 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Beta strand 372 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 390 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Beta strand 414 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Helix 422 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +P38999 UniProtKB Beta strand 441 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AXQ +##sequence-region O14467 1 151 +O14467 UniProtKB Chain 1 151 . . . ID=PRO_0000149814;Note=Multiprotein-bridging factor 1 +O14467 UniProtKB Domain 85 139 . . . Note=HTH cro/C1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00257 +O14467 UniProtKB DNA binding 96 115 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00257 +O14467 UniProtKB Region 41 119 . . . Note=Essential for TBP-binding +O14467 UniProtKB Modified residue 143 143 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +O14467 UniProtKB Mutagenesis 112 112 . . . Note=Reduces interaction to TBP. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9710580;Dbxref=PMID:9710580 +##sequence-region Q08601 1 432 +Q08601 UniProtKB Region 29 131 . . . Note=Prion domain (PrD) +Q08601 UniProtKB Active site 220 220 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08601 UniProtKB Active site 276 276 . . . . +Q08601 UniProtKB Mutagenesis 276 276 . . . Note=Blocks the processing and reduces caspase activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983181;Dbxref=PMID:11983181 +Q08601 UniProtKB Turn 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6O +Q08601 UniProtKB Beta strand 102 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6O +Q08601 UniProtKB Beta strand 136 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Helix 155 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Helix 174 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Beta strand 177 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Helix 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Helix 193 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Beta strand 212 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Beta strand 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Beta strand 237 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Helix 244 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Helix 252 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Turn 260 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Beta strand 268 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Beta strand 275 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Turn 279 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Beta strand 285 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Beta strand 292 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Beta strand 354 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Helix 380 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Helix 397 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Turn 409 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +Q08601 UniProtKB Beta strand 415 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6P +##sequence-region Q12106 1 302 +Q12106 UniProtKB Chain 1 302 . . . ID=PRO_0000245281;Note=MDM10-complementing protein 1 +Q12106 UniProtKB Topological domain 1 61 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23781023;Dbxref=PMID:23781023 +Q12106 UniProtKB Transmembrane 62 82 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12106 UniProtKB Topological domain 83 100 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23781023;Dbxref=PMID:23781023 +Q12106 UniProtKB Transmembrane 101 121 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12106 UniProtKB Topological domain 122 173 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23781023;Dbxref=PMID:23781023 +Q12106 UniProtKB Transmembrane 174 194 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12106 UniProtKB Topological domain 195 219 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23781023;Dbxref=PMID:23781023 +Q12106 UniProtKB Transmembrane 220 240 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12106 UniProtKB Topological domain 241 258 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23781023;Dbxref=PMID:23781023 +Q12106 UniProtKB Transmembrane 259 276 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12106 UniProtKB Topological domain 277 302 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23781023;Dbxref=PMID:23781023 +##sequence-region P35191 1 511 +P35191 UniProtKB Transit peptide 1 55 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35191 UniProtKB Chain 56 511 . . . ID=PRO_0000007268;Note=DnaJ homolog 1%2C mitochondrial +P35191 UniProtKB Domain 59 127 . . . Note=J +P35191 UniProtKB Repeat 230 237 . . . Note=CXXCXGXG motif +P35191 UniProtKB Repeat 247 254 . . . Note=CXXCXGXG motif +P35191 UniProtKB Repeat 269 276 . . . Note=CXXCXGXG motif +P35191 UniProtKB Repeat 285 292 . . . Note=CXXCXGXG motif +P35191 UniProtKB Zinc finger 217 297 . . . Note=CR-type +P35191 UniProtKB Compositional bias 130 186 . . . Note=Gly-rich +##sequence-region P19659 1 1081 +P19659 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P19659 UniProtKB Chain 2 1081 . . . ID=PRO_0000096363;Note=Mediator of RNA polymerase II transcription subunit 15 +P19659 UniProtKB Repeat 422 423 . . . Note=1 +P19659 UniProtKB Repeat 424 425 . . . Note=2 +P19659 UniProtKB Repeat 426 427 . . . Note=3 +P19659 UniProtKB Repeat 428 429 . . . Note=4 +P19659 UniProtKB Repeat 430 431 . . . Note=5 +P19659 UniProtKB Repeat 432 433 . . . Note=6 +P19659 UniProtKB Repeat 434 435 . . . Note=7 +P19659 UniProtKB Repeat 436 437 . . . Note=8 +P19659 UniProtKB Repeat 438 439 . . . Note=9 +P19659 UniProtKB Repeat 440 441 . . . Note=10 +P19659 UniProtKB Repeat 442 443 . . . Note=11 +P19659 UniProtKB Repeat 444 445 . . . Note=12%3B approximate +P19659 UniProtKB Repeat 446 447 . . . Note=13%3B approximate +P19659 UniProtKB Repeat 448 449 . . . Note=14 +P19659 UniProtKB Repeat 450 451 . . . Note=15 +P19659 UniProtKB Repeat 452 453 . . . Note=16 +P19659 UniProtKB Repeat 454 455 . . . Note=17 +P19659 UniProtKB Repeat 456 457 . . . Note=18 +P19659 UniProtKB Repeat 458 459 . . . Note=19 +P19659 UniProtKB Repeat 460 461 . . . Note=20 +P19659 UniProtKB Repeat 462 463 . . . Note=21 +P19659 UniProtKB Repeat 464 465 . . . Note=22 +P19659 UniProtKB Repeat 466 467 . . . Note=23 +P19659 UniProtKB Repeat 468 469 . . . Note=24 +P19659 UniProtKB Repeat 470 471 . . . Note=25 +P19659 UniProtKB Repeat 472 473 . . . Note=26 +P19659 UniProtKB Repeat 474 475 . . . Note=27 +P19659 UniProtKB Repeat 476 477 . . . Note=28 +P19659 UniProtKB Repeat 478 479 . . . Note=29 +P19659 UniProtKB Repeat 480 481 . . . Note=30 +P19659 UniProtKB Region 422 481 . . . Note=30 X 2 AA approximate tandem repeats of Q-A +P19659 UniProtKB Compositional bias 147 158 . . . Note=Poly-Gln +P19659 UniProtKB Compositional bias 674 696 . . . Note=Poly-Gln +P19659 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P19659 UniProtKB Modified residue 335 335 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P19659 UniProtKB Modified residue 736 736 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P19659 UniProtKB Modified residue 752 752 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P19659 UniProtKB Modified residue 783 783 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198 +P19659 UniProtKB Modified residue 785 785 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P19659 UniProtKB Modified residue 789 789 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P19659 UniProtKB Modified residue 793 793 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P19659 UniProtKB Modified residue 831 831 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P19659 UniProtKB Modified residue 1003 1003 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P19659 UniProtKB Modified residue 1008 1008 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P19659 UniProtKB Modified residue 1018 1018 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P19659 UniProtKB Modified residue 1034 1034 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P19659 UniProtKB Sequence conflict 171 171 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19659 UniProtKB Sequence conflict 302 302 . . . Note=P->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19659 UniProtKB Sequence conflict 499 499 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19659 UniProtKB Sequence conflict 751 751 . . . Note=P->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19659 UniProtKB Beta strand 8 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0N +P19659 UniProtKB Helix 14 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0N +P19659 UniProtKB Helix 41 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0N +P19659 UniProtKB Helix 63 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0N +P19659 UniProtKB Helix 164 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LPB +P19659 UniProtKB Helix 172 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LPB +P19659 UniProtKB Helix 180 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LPB +P19659 UniProtKB Helix 196 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LPB +P19659 UniProtKB Helix 201 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LPB +P19659 UniProtKB Helix 210 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LPB +##sequence-region P47822 1 140 +P47822 UniProtKB Chain 1 140 . . . ID=PRO_0000096377;Note=Mediator of RNA polymerase II transcription subunit 21 +P47822 UniProtKB Coiled coil 85 125 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47822 UniProtKB Mutagenesis 21 21 . . . Note=In SRB7-1%3B suppresses the phenotypic defects of an RNA polymerase II CTD truncation. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7774808;Dbxref=PMID:7774808 +P47822 UniProtKB Helix 3 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKH +P47822 UniProtKB Helix 31 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKE +P47822 UniProtKB Helix 52 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKH +P47822 UniProtKB Turn 81 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKH +P47822 UniProtKB Helix 87 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YKH +##sequence-region Q02205 1 184 +Q02205 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q02205 UniProtKB Chain 2 184 . . . ID=PRO_0000203193;Note=Protein MEH1 +Q02205 UniProtKB Coiled coil 30 71 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02205 UniProtKB Modified residue 146 146 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q02205 UniProtKB Modified residue 149 149 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q02205 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16732272;Dbxref=PMID:16732272 +Q02205 UniProtKB Lipidation 7 7 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107 +Q02205 UniProtKB Lipidation 8 8 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107 +Q02205 UniProtKB Beta strand 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM +Q02205 UniProtKB Helix 154 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM +Q02205 UniProtKB Beta strand 180 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XPM +##sequence-region P33441 1 392 +P33441 UniProtKB Chain 1 392 . . . ID=PRO_0000096463;Note=THO complex subunit MFT1 +P33441 UniProtKB Modified residue 266 266 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P25573 1 417 +P25573 UniProtKB Chain 1 417 . . . ID=PRO_0000202546;Note=Mitochondrial inner membrane i-AAA protease supercomplex subunit MGR1 +P25573 UniProtKB Topological domain 1 56 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16267274;Dbxref=PMID:16267274 +P25573 UniProtKB Transmembrane 57 73 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25573 UniProtKB Topological domain 74 151 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16267274;Dbxref=PMID:16267274 +P25573 UniProtKB Transmembrane 152 169 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25573 UniProtKB Topological domain 170 417 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16267274;Dbxref=PMID:16267274 +##sequence-region Q96VH5 1 97 +Q96VH5 UniProtKB Chain 1 97 . . . ID=PRO_0000221640;Note=MICOS complex subunit MIC10 +Q96VH5 UniProtKB Topological domain 1 35 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q96VH5 UniProtKB Transmembrane 36 58 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q96VH5 UniProtKB Topological domain 59 97 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P50087 1 233 +P50087 UniProtKB Chain 1 233 . . . ID=PRO_0000202852;Note=MICOS subunit MIC26 +P50087 UniProtKB Topological domain 1 119 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50087 UniProtKB Transmembrane 120 137 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50087 UniProtKB Topological domain 138 141 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50087 UniProtKB Transmembrane 142 164 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50087 UniProtKB Topological domain 165 233 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P35201 1 549 +P35201 UniProtKB Chain 1 549 . . . ID=PRO_0000096486;Note=Protein MIF2 +P35201 UniProtKB DNA binding 356 364 . . . Note=A.T hook +P35201 UniProtKB Compositional bias 178 263 . . . Note=Asp/Glu-rich (acidic) +P35201 UniProtKB Modified residue 325 325 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P35201 UniProtKB Turn 447 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV +P35201 UniProtKB Beta strand 453 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV +P35201 UniProtKB Helix 463 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV +P35201 UniProtKB Beta strand 467 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV +P35201 UniProtKB Beta strand 473 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV +P35201 UniProtKB Beta strand 492 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV +P35201 UniProtKB Beta strand 501 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV +P35201 UniProtKB Beta strand 509 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV +P35201 UniProtKB Beta strand 516 518 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV +P35201 UniProtKB Beta strand 520 528 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VPV +##sequence-region P27705 1 504 +P27705 UniProtKB Chain 1 504 . . . ID=PRO_0000046881;Note=Regulatory protein MIG1 +P27705 UniProtKB Zinc finger 38 60 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P27705 UniProtKB Zinc finger 66 90 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P27705 UniProtKB Compositional bias 253 260 . . . Note=Gln-rich +P27705 UniProtKB Compositional bias 411 444 . . . Note=Asn/Gln-rich +P27705 UniProtKB Modified residue 278 278 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P27705 UniProtKB Modified residue 302 302 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P27705 UniProtKB Modified residue 310 310 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P27705 UniProtKB Modified residue 311 311 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P27705 UniProtKB Modified residue 314 314 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P27705 UniProtKB Modified residue 377 377 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q06820 1 579 +Q06820 UniProtKB Chain 1 579 . . . ID=PRO_0000096332;Note=Mitochondrial distribution and morphology protein 36 +Q06820 UniProtKB Compositional bias 143 147 . . . Note=Poly-Asp +Q06820 UniProtKB Modified residue 42 42 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q08179 1 573 +Q08179 UniProtKB Transit peptide 1 56 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08179 UniProtKB Chain 57 573 . . . ID=PRO_0000017697;Note=Mitochondrial distribution and morphology protein 38 +Q08179 UniProtKB Topological domain 57 138 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08179 UniProtKB Transmembrane 139 159 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08179 UniProtKB Topological domain 160 573 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08179 UniProtKB Domain 182 404 . . . Note=Letm1 RBD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01094 +Q08179 UniProtKB Coiled coil 408 440 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08179 UniProtKB Coiled coil 503 541 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08179 UniProtKB Compositional bias 423 552 . . . Note=Glu-rich +Q08179 UniProtKB Helix 183 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +Q08179 UniProtKB Helix 206 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +Q08179 UniProtKB Helix 212 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +Q08179 UniProtKB Beta strand 234 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +Q08179 UniProtKB Helix 238 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +Q08179 UniProtKB Helix 250 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +Q08179 UniProtKB Helix 259 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +Q08179 UniProtKB Helix 277 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +Q08179 UniProtKB Helix 303 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +Q08179 UniProtKB Helix 308 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +Q08179 UniProtKB Helix 327 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +Q08179 UniProtKB Helix 348 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +Q08179 UniProtKB Helix 356 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +Q08179 UniProtKB Beta strand 359 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +Q08179 UniProtKB Beta strand 368 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +Q08179 UniProtKB Helix 373 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +Q08179 UniProtKB Beta strand 378 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +Q08179 UniProtKB Helix 383 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +Q08179 UniProtKB Turn 405 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SKQ +##sequence-region Q02574 1 474 +Q02574 UniProtKB Chain 1 474 . . . ID=PRO_0000096344;Note=DNA damage checkpoint control protein MEC3 +Q02574 UniProtKB Modified residue 452 452 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q02574 UniProtKB Sequence conflict 120 120 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q02574 UniProtKB Sequence conflict 176 176 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q02574 UniProtKB Sequence conflict 454 454 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12321 1 566 +Q12321 UniProtKB Chain 1 566 . . . ID=PRO_0000096372;Note=Mediator of RNA polymerase II transcription subunit 1 +Q12321 UniProtKB Modified residue 155 155 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12321 UniProtKB Modified residue 423 423 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P32570 1 121 +P32570 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32570 UniProtKB Chain 2 121 . . . ID=PRO_0000096379;Note=Mediator of RNA polymerase II transcription subunit 22 +P32570 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32570 UniProtKB Mutagenesis 86 86 . . . Note=In SRB6-1%3B suppresses the phenotypic defects of an RNA polymerase II CTD truncation. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8324825;Dbxref=PMID:8324825 +P32570 UniProtKB Helix 4 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R84 +P32570 UniProtKB Helix 42 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R84 +P32570 UniProtKB Helix 50 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R84 +P32570 UniProtKB Helix 101 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +##sequence-region Q12041 1 191 +Q12041 UniProtKB Chain 1 191 . . . ID=PRO_0000046809;Note=Transcriptional regulator MET32 +Q12041 UniProtKB Zinc finger 98 120 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q12041 UniProtKB Zinc finger 126 150 . . . Note=C2H2-type 2%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +##sequence-region P43623 1 340 +P43623 UniProtKB Chain 1 340 . . . ID=PRO_0000114774;Note=Putative cystathionine beta-lyase +P43623 UniProtKB Modified residue 208 208 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q04533 1 649 +Q04533 UniProtKB Chain 1 649 . . . ID=PRO_0000114783;Note=Putative cystathionine gamma-synthase YML082W +Q04533 UniProtKB Modified residue 287 287 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04533 UniProtKB Modified residue 451 451 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P01149 1 165 +P01149 UniProtKB Signal peptide 1 19 . . . Note=Or 20;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:340452,ECO:0000305|Ref.7;Dbxref=PMID:340452 +P01149 UniProtKB Propeptide 20 89 . . . ID=PRO_0000419673 +P01149 UniProtKB Peptide 90 102 . . . ID=PRO_0000021697;Note=Mating factor alpha +P01149 UniProtKB Propeptide 105 110 . . . ID=PRO_0000419674 +P01149 UniProtKB Peptide 111 123 . . . ID=PRO_0000021698;Note=Mating factor alpha +P01149 UniProtKB Propeptide 126 131 . . . ID=PRO_0000419675 +P01149 UniProtKB Peptide 132 144 . . . ID=PRO_0000021699;Note=Mating factor alpha +P01149 UniProtKB Propeptide 147 152 . . . ID=PRO_0000419676 +P01149 UniProtKB Peptide 153 165 . . . ID=PRO_0000021700;Note=Mating factor alpha +P01149 UniProtKB Natural variant 165 165 . . . Note=In strain: Italicus / IFO 0253. Y->YKREADAEAWHWLQLKPGQPMY +P01149 UniProtKB Sequence conflict 42 42 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P01149 UniProtKB Sequence conflict 107 107 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53050 1 456 +P53050 UniProtKB Chain 1 456 . . . ID=PRO_0000124593;Note=Protein MGA1 +P53050 UniProtKB DNA binding 3 118 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53050 UniProtKB Compositional bias 182 185 . . . Note=Poly-Gln +P53050 UniProtKB Compositional bias 283 290 . . . Note=Poly-Gln +##sequence-region P40081 1 178 +P40081 UniProtKB Chain 1 178 . . . ID=PRO_0000202650;Note=Putative magnesium-dependent phosphatase YER134C +P40081 UniProtKB Active site 11 11 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40081 UniProtKB Active site 13 13 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40081 UniProtKB Metal binding 11 11 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40081 UniProtKB Metal binding 13 13 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40081 UniProtKB Metal binding 141 141 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40081 UniProtKB Binding site 12 12 . . . Note=Phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40081 UniProtKB Binding site 13 13 . . . Note=Phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40081 UniProtKB Binding site 74 74 . . . Note=Phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40081 UniProtKB Binding site 75 75 . . . Note=Phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40081 UniProtKB Binding site 75 75 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q06630 1 226 +Q06630 UniProtKB Chain 1 226 . . . ID=PRO_0000255967;Note=Mitochondrial homologous recombination protein 1 +Q06630 UniProtKB Mutagenesis 172 172 . . . Note=In MHR1-1%3B causes a defect in the partitioning of nascent mtDNA into buds and delays generation of homoplasmic cells. G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12198175,ECO:0000269|PubMed:14565971;Dbxref=PMID:12198175,PMID:14565971 +##sequence-region P43594 1 170 +P43594 UniProtKB Chain 1 170 . . . ID=PRO_0000202684;Note=MICOS complex subunit MIC19 +##sequence-region P36027 1 376 +P36027 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36027 UniProtKB Chain 26 376 . . . ID=PRO_0000096485;Note=Cell wall integrity sensor MID2 +P36027 UniProtKB Topological domain 26 224 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36027 UniProtKB Transmembrane 225 245 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36027 UniProtKB Topological domain 246 376 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36027 UniProtKB Compositional bias 31 219 . . . Note=Ser-rich +P36027 UniProtKB Modified residue 260 260 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36027 UniProtKB Modified residue 327 327 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36027 UniProtKB Modified residue 329 329 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36027 UniProtKB Modified residue 355 355 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36027 UniProtKB Glycosylation 35 35 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36027 UniProtKB Glycosylation 211 211 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36027 UniProtKB Sequence conflict 303 304 . . . Note=GG->VV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38760 1 659 +P38760 UniProtKB Chain 1 659 . . . ID=PRO_0000082032;Note=RNA-binding protein MIP6 +P38760 UniProtKB Domain 111 189 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P38760 UniProtKB Domain 199 267 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P38760 UniProtKB Domain 313 389 . . . Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P38760 UniProtKB Beta strand 314 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5D78 +P38760 UniProtKB Helix 326 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5D78 +P38760 UniProtKB Turn 334 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5D78 +P38760 UniProtKB Beta strand 339 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5D78 +P38760 UniProtKB Beta strand 354 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5D78 +P38760 UniProtKB Helix 362 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5D78 +P38760 UniProtKB Beta strand 375 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5D78 +P38760 UniProtKB Beta strand 380 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5D78 +##sequence-region Q02455 1 1875 +Q02455 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q02455 UniProtKB Chain 2 1875 . . . ID=PRO_0000096501;Note=Protein MLP1 +Q02455 UniProtKB Coiled coil 69 487 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02455 UniProtKB Coiled coil 531 1678 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02455 UniProtKB Coiled coil 1834 1866 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02455 UniProtKB Motif 1496 1565 . . . Note=Required for nuclear localization +Q02455 UniProtKB Compositional bias 1804 1865 . . . Note=Glu-rich +Q02455 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q02455 UniProtKB Modified residue 337 337 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q02455 UniProtKB Modified residue 379 379 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q02455 UniProtKB Modified residue 1670 1670 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q02455 UniProtKB Modified residue 1710 1710 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q02455 UniProtKB Modified residue 1733 1733 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02455 UniProtKB Modified residue 1803 1803 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q02455 UniProtKB Sequence conflict 301 301 . . . Note=R->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38300 1 278 +P38300 UniProtKB Transit peptide 1 33 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38300 UniProtKB Chain 34 278 . . . ID=PRO_0000021656;Note=Inner membrane mitoribosome receptor MBA1%2C mitochondrial +##sequence-region P32354 1 571 +P32354 UniProtKB Chain 1 571 . . . ID=PRO_0000079949;Note=Minichromosome maintenance protein 10 +P32354 UniProtKB Region 309 335 . . . Note=Zinc finger-like +P32354 UniProtKB Region 435 512 . . . Note=Sufficient for nuclear localization +P32354 UniProtKB Region 453 553 . . . Note=Sufficient for nuclear localization +P32354 UniProtKB Motif 435 451 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32354 UniProtKB Motif 512 527 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32354 UniProtKB Modified residue 17 17 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32354 UniProtKB Modified residue 18 18 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32354 UniProtKB Modified residue 453 453 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32354 UniProtKB Modified residue 454 454 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32354 UniProtKB Mutagenesis 245 245 . . . Note=Inhibits interaction with POL30/PCNA and abolishes cell proliferation. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16782870;Dbxref=PMID:16782870 +P32354 UniProtKB Mutagenesis 261 261 . . . Note=Temperature sensitive%3B loss of CDC17 stabilization. G->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16675460;Dbxref=PMID:16675460 +P32354 UniProtKB Mutagenesis 268 268 . . . Note=Temperature sensitive%3B loss of CDC17 stabilization. N->D%2CI;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16675460;Dbxref=PMID:16675460 +P32354 UniProtKB Mutagenesis 269 269 . . . Note=In mcm10-1%3B diminishes interaction with MCM7. P->L +P32354 UniProtKB Mutagenesis 320 320 . . . Note=In mcm10-43%3B abolishes self-association and diminishes interaction with MCM7. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12844493;Dbxref=PMID:12844493 +P32354 UniProtKB Mutagenesis 332 332 . . . Note=Abolishes self-association%3B when associated with L-335. C->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12844493;Dbxref=PMID:12844493 +P32354 UniProtKB Mutagenesis 335 335 . . . Note=Abolishes self-association%3B when associated with G-332. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12844493;Dbxref=PMID:12844493 +P32354 UniProtKB Mutagenesis 449 451 . . . Note=No effect on nuclear localization. RRR->GGG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:13680157;Dbxref=PMID:13680157 +P32354 UniProtKB Sequence conflict 38 38 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32354 UniProtKB Sequence conflict 458 458 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32354 UniProtKB Sequence conflict 492 571 . . . Note=ISQVLKSSVSGSEPKNNLLGKKKTVINDLLHYKKEKVILAPSKNEWFKKRSHREEVWQKHFGSKETKETSDGSASDLEII->NFPKYSSLLYQGANLRTTYSVKKKLL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P22133 1 377 +P22133 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1986231,ECO:0000269|PubMed:3552052;Dbxref=PMID:1986231,PMID:3552052 +P22133 UniProtKB Chain 2 377 . . . ID=PRO_0000113338;Note=Malate dehydrogenase%2C cytoplasmic +P22133 UniProtKB Nucleotide binding 20 26 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22133 UniProtKB Nucleotide binding 144 146 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22133 UniProtKB Active site 215 215 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22133 UniProtKB Binding site 57 57 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22133 UniProtKB Binding site 106 106 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004 +P22133 UniProtKB Binding site 112 112 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004 +P22133 UniProtKB Binding site 119 119 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22133 UniProtKB Binding site 146 146 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004 +P22133 UniProtKB Binding site 185 185 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10004 +P22133 UniProtKB Binding site 266 266 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22133 UniProtKB Modified residue 6 6 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region O60200 1 86 +O60200 UniProtKB Chain 1 86 . . . ID=PRO_0000220526;Note=Mitochondrial distribution and morphology protein 35 +O60200 UniProtKB Domain 10 60 . . . Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +O60200 UniProtKB Motif 13 23 . . . Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +O60200 UniProtKB Motif 42 52 . . . Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +O60200 UniProtKB Disulfide bond 13 52 . . . Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4XHR,ECO:0000244|PDB:4XIZ,ECO:0000244|PDB:4YTV,ECO:0000244|PDB:4YTW,ECO:0000244|PDB:4YTX,ECO:0000255|PROSITE-ProRule:PRU01150,ECO:0000269|PubMed:26071601,ECO:0000269|PubMed:26235513;Dbxref=PMID:26071601,PMID:26235513 +O60200 UniProtKB Disulfide bond 23 42 . . . Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4XHR,ECO:0000244|PDB:4XIZ,ECO:0000244|PDB:4YTV,ECO:0000244|PDB:4YTW,ECO:0000244|PDB:4YTX,ECO:0000255|PROSITE-ProRule:PRU01150,ECO:0000269|PubMed:26071601,ECO:0000269|PubMed:26235513;Dbxref=PMID:26071601,PMID:26235513 +O60200 UniProtKB Mutagenesis 24 24 . . . Note=Impairs interaction with UPS1 and UPS2%3B when associated with A-27 and A-28. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513 +O60200 UniProtKB Mutagenesis 27 27 . . . Note=Impairs interaction with UPS1 and UPS2%3B when associated with A-24 and A-28. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513 +O60200 UniProtKB Mutagenesis 28 28 . . . Note=Impairs interaction with UPS1 and UPS2%3B when associated with A-24 and A-27. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513 +O60200 UniProtKB Mutagenesis 32 32 . . . Note=Impairs interaction with UPS1 and UPS2. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235513;Dbxref=PMID:26235513 +O60200 UniProtKB Helix 4 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTV +O60200 UniProtKB Helix 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +O60200 UniProtKB Helix 14 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +O60200 UniProtKB Turn 31 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +O60200 UniProtKB Helix 43 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +O60200 UniProtKB Helix 63 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTW +##sequence-region P53094 1 1487 +P53094 UniProtKB Chain 1 1487 . . . ID=PRO_0000119137;Note=Negative regulator of sporulation MDS3 +P53094 UniProtKB Repeat 171 226 . . . Note=Kelch 1 +P53094 UniProtKB Repeat 234 287 . . . Note=Kelch 2 +P53094 UniProtKB Repeat 371 419 . . . Note=Kelch 3 +P53094 UniProtKB Modified residue 472 472 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53094 UniProtKB Modified residue 475 475 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53094 UniProtKB Modified residue 621 621 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53094 UniProtKB Modified residue 639 639 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P53094 UniProtKB Modified residue 693 693 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53094 UniProtKB Modified residue 698 698 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53094 UniProtKB Modified residue 744 744 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53094 UniProtKB Modified residue 747 747 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53094 UniProtKB Modified residue 756 756 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53094 UniProtKB Modified residue 757 757 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53094 UniProtKB Modified residue 781 781 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53094 UniProtKB Modified residue 785 785 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53094 UniProtKB Modified residue 787 787 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53094 UniProtKB Modified residue 900 900 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53094 UniProtKB Modified residue 904 904 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53094 UniProtKB Modified residue 930 930 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53094 UniProtKB Modified residue 1187 1187 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53094 UniProtKB Sequence conflict 262 264 . . . Note=QSE->HPK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53094 UniProtKB Sequence conflict 262 264 . . . Note=QSE->HPK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53094 UniProtKB Sequence conflict 403 403 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53094 UniProtKB Sequence conflict 403 403 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47025 1 714 +P47025 UniProtKB Chain 1 714 . . . ID=PRO_0000051477;Note=Mitochondrial division protein 1 +P47025 UniProtKB Repeat 396 436 . . . Note=WD 1 +P47025 UniProtKB Repeat 439 478 . . . Note=WD 2 +P47025 UniProtKB Repeat 500 539 . . . Note=WD 3 +P47025 UniProtKB Repeat 561 603 . . . Note=WD 4 +P47025 UniProtKB Repeat 604 642 . . . Note=WD 5 +P47025 UniProtKB Repeat 644 681 . . . Note=WD 6 +P47025 UniProtKB Repeat 685 714 . . . Note=WD 7 +P47025 UniProtKB Coiled coil 240 298 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47025 UniProtKB Modified residue 376 376 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P47025 UniProtKB Mutagenesis 148 148 . . . Note=Abolishes interaction with FIS1. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16272155;Dbxref=PMID:16272155 +P47025 UniProtKB Mutagenesis 250 250 . . . Note=Suppresses the mitochondrial fission defect of a FIS1-3 mutant by affecting interaction with FIS1. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16247028;Dbxref=PMID:16247028 +P47025 UniProtKB Mutagenesis 400 400 . . . Note=No interaction with FIS1%3B slight decrease in interaction with DNM1. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14517324;Dbxref=PMID:14517324 +P47025 UniProtKB Mutagenesis 440 440 . . . Note=Abolishes interaction with DNM1. H->E%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16272155;Dbxref=PMID:16272155 +P47025 UniProtKB Mutagenesis 461 461 . . . Note=Slight decrease in interaction with FIS1%3B 20-fold decrease in interaction with DNM1%3B even distribution along mitochondria not punctate. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14517324;Dbxref=PMID:14517324 +P47025 UniProtKB Mutagenesis 544 544 . . . Note=Results in mitrochondrial division defect%2C but has no effect on the interaction with DNM1. N->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16272155;Dbxref=PMID:16272155 +P47025 UniProtKB Mutagenesis 605 605 . . . Note=Abolishes interaction with DNM1. H->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16272155;Dbxref=PMID:16272155 +P47025 UniProtKB Mutagenesis 664 664 . . . Note=Slight decrease in interaction with DNM1. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14517324;Dbxref=PMID:14517324 +P47025 UniProtKB Mutagenesis 689 689 . . . Note=Slight decrease in interaction with DNM1. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14517324;Dbxref=PMID:14517324 +P47025 UniProtKB Helix 148 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PQN +P47025 UniProtKB Helix 231 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XU6 +##sequence-region P19263 1 1082 +P19263 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P19263 UniProtKB Chain 2 1082 . . . ID=PRO_0000096362;Note=Mediator of RNA polymerase II transcription subunit 14 +P19263 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P19263 UniProtKB Modified residue 7 7 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:18407956 +P19263 UniProtKB Modified residue 1036 1036 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P19263 UniProtKB Sequence conflict 46 46 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19263 UniProtKB Sequence conflict 51 51 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19263 UniProtKB Sequence conflict 56 56 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19263 UniProtKB Sequence conflict 285 285 . . . Note=E->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19263 UniProtKB Sequence conflict 746 746 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P29467 1 408 +P29467 UniProtKB Chain 1 408 . . . ID=PRO_0000096402;Note=Meiosis-specific protein MEI4 +P29467 UniProtKB Sequence conflict 329 329 . . . Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39692 1 1035 +P39692 UniProtKB Chain 1 1035 . . . ID=PRO_0000199947;Note=Sulfite reductase [NADPH] flavoprotein component +P39692 UniProtKB Domain 648 879 . . . Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716 +P39692 UniProtKB Nucleotide binding 684 695 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39692 UniProtKB Nucleotide binding 814 824 . . . Note=FAD (flavin part);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39692 UniProtKB Sequence conflict 172 172 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39692 UniProtKB Sequence conflict 420 420 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39692 UniProtKB Sequence conflict 977 977 . . . Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39014 1 640 +P39014 UniProtKB Chain 1 640 . . . ID=PRO_0000051087;Note=F-box protein MET30 +P39014 UniProtKB Domain 181 227 . . . Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080 +P39014 UniProtKB Repeat 300 328 . . . Note=WD 1 +P39014 UniProtKB Repeat 340 368 . . . Note=WD 2 +P39014 UniProtKB Repeat 380 408 . . . Note=WD 3 +P39014 UniProtKB Repeat 419 449 . . . Note=WD 4 +P39014 UniProtKB Repeat 461 499 . . . Note=WD 5 +P39014 UniProtKB Repeat 509 538 . . . Note=WD 6 +P39014 UniProtKB Repeat 550 578 . . . Note=WD 7 +P39014 UniProtKB Repeat 607 635 . . . Note=WD 8 +P39014 UniProtKB Region 1 299 . . . Note=Necessary to mediate nuclear localization +P39014 UniProtKB Region 180 277 . . . Note=Important for mediating homomultimerization +P39014 UniProtKB Region 180 225 . . . Note=Interaction with SKP1/CBF3D +P39014 UniProtKB Region 277 640 . . . Note=Interaction with MET4 +P39014 UniProtKB Modified residue 67 67 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39014 UniProtKB Mutagenesis 187 187 . . . Note=Strongly reduces nuclear localization%3B inhibits interaction with SKP1/CBF3D. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14660673;Dbxref=PMID:14660673 +P39014 UniProtKB Mutagenesis 190 190 . . . Note=Strongly reduces nuclear localization%3B inhibits interaction with SKP1/CBF3D. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14660673;Dbxref=PMID:14660673 +P39014 UniProtKB Mutagenesis 386 386 . . . Note=Inactivates MET30 and prevents MET4 interaction%3B when associated with A-425 and A-467. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15883825;Dbxref=PMID:15883825 +P39014 UniProtKB Mutagenesis 425 425 . . . Note=Inactivates MET30 and prevents MET4 interaction%3B when associated with D-530 or D-386 and A-467. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15883825;Dbxref=PMID:15883825 +P39014 UniProtKB Mutagenesis 467 467 . . . Note=Inactivates MET30 and prevents MET4 interaction%3B when associated with D-386 and A-425. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15883825;Dbxref=PMID:15883825 +P39014 UniProtKB Mutagenesis 530 530 . . . Note=Inactivates MET30 and prevents MET4 interaction%3B when associated with A-425. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15883825;Dbxref=PMID:15883825 +P39014 UniProtKB Sequence conflict 61 61 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P08536 1 511 +P08536 UniProtKB Chain 1 511 . . . ID=PRO_0000105954;Note=Sulfate adenylyltransferase +P08536 UniProtKB Nucleotide binding 194 198 . . . Note=ATP +P08536 UniProtKB Nucleotide binding 289 293 . . . Note=ATP +P08536 UniProtKB Region 1 167 . . . Note=N-terminal +P08536 UniProtKB Region 168 393 . . . Note=Catalytic +P08536 UniProtKB Region 394 511 . . . Note=Required for oligomerization%3B adenylyl-sulfate kinase-like +P08536 UniProtKB Active site 196 196 . . . . +P08536 UniProtKB Active site 197 197 . . . . +P08536 UniProtKB Active site 198 198 . . . . +P08536 UniProtKB Binding site 204 204 . . . Note=Substrate +P08536 UniProtKB Binding site 331 331 . . . Note=ATP%3B via amide nitrogen +P08536 UniProtKB Binding site 355 355 . . . Note=Substrate +P08536 UniProtKB Binding site 356 356 . . . Note=Substrate%3B via carbonyl oxygen +P08536 UniProtKB Site 201 201 . . . Note=Transition state stabilizer +P08536 UniProtKB Site 204 204 . . . Note=Transition state stabilizer +P08536 UniProtKB Site 328 328 . . . Note=Induces change in substrate recognition on ATP binding +P08536 UniProtKB Sequence conflict 221 221 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08536 UniProtKB Helix 12 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Helix 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Helix 20 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Beta strand 32 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Helix 39 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Turn 51 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Helix 62 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Beta strand 86 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Helix 90 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Beta strand 101 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Turn 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Beta strand 110 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Helix 125 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Helix 140 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Beta strand 151 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Turn 170 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F +P08536 UniProtKB Helix 176 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Beta strand 191 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Helix 202 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Beta strand 218 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Helix 235 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Helix 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Beta strand 254 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Helix 267 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Beta strand 284 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Turn 290 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Beta strand 303 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Helix 309 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Beta strand 324 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Beta strand 331 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Helix 335 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Beta strand 339 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Turn 343 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Beta strand 348 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Helix 358 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Turn 373 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Helix 378 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R6X +P08536 UniProtKB Helix 391 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F +P08536 UniProtKB Beta strand 396 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F +P08536 UniProtKB Helix 408 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F +P08536 UniProtKB Beta strand 428 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F +P08536 UniProtKB Helix 437 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F +P08536 UniProtKB Helix 443 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F +P08536 UniProtKB Beta strand 452 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F +P08536 UniProtKB Helix 461 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F +P08536 UniProtKB Beta strand 472 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F +P08536 UniProtKB Beta strand 482 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F +P08536 UniProtKB Helix 492 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G8F +##sequence-region P47164 1 639 +P47164 UniProtKB Chain 1 639 . . . ID=PRO_0000114781;Note=Cystathionine gamma-synthase +P47164 UniProtKB Modified residue 443 443 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P19358 1 384 +P19358 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P19358 UniProtKB Chain 2 384 . . . ID=PRO_0000174452;Note=S-adenosylmethionine synthase 2 +P19358 UniProtKB Nucleotide binding 168 170 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00266 +P19358 UniProtKB Nucleotide binding 236 239 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00266 +P19358 UniProtKB Nucleotide binding 253 254 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817 +P19358 UniProtKB Metal binding 12 12 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13444 +P19358 UniProtKB Metal binding 46 46 . . . Note=Potassium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817 +P19358 UniProtKB Binding site 18 18 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00266 +P19358 UniProtKB Binding site 59 59 . . . Note=Methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817 +P19358 UniProtKB Binding site 102 102 . . . Note=Methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817 +P19358 UniProtKB Binding site 247 247 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q00266 +P19358 UniProtKB Binding site 247 247 . . . Note=Methionine%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817 +P19358 UniProtKB Binding site 270 270 . . . Note=ATP%3B via amide nitrogen%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817 +P19358 UniProtKB Binding site 274 274 . . . Note=ATP%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817 +P19358 UniProtKB Binding site 278 278 . . . Note=ATP%3B shared with neighboring subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13444 +P19358 UniProtKB Binding site 278 278 . . . Note=Methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A817 +P19358 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P19358 UniProtKB Sequence conflict 130 130 . . . Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02889 1 113 +Q02889 UniProtKB Chain 1 113 . . . ID=PRO_0000252278;Note=Protein MGR2 +Q02889 UniProtKB Topological domain 1 22 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02889 UniProtKB Transmembrane 23 43 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02889 UniProtKB Topological domain 44 56 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02889 UniProtKB Transmembrane 57 77 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02889 UniProtKB Topological domain 78 113 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E835 1 90 +Q3E835 UniProtKB Chain 1 90 . . . ID=PRO_0000235928;Note=MHF histone-fold complex subunit 1 +Q3E835 UniProtKB Mutagenesis 55 55 . . . Note=Disrupts the heterotetrameric state and becomes hypersensitive to MMS%3B when associated with A-62. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22325783;Dbxref=PMID:22325783 +Q3E835 UniProtKB Mutagenesis 62 62 . . . Note=Disrupts the heterotetrameric state and becomes hypersensitive to MMS%3B when associated with A-55 or 78-AA-79. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22325783;Dbxref=PMID:22325783 +Q3E835 UniProtKB Mutagenesis 78 79 . . . Note=Disrupts the heterotetrameric state and becomes hypersensitive to MMS%3B when associated with A-62. RK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22325783;Dbxref=PMID:22325783 +Q3E835 UniProtKB Helix 3 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R +Q3E835 UniProtKB Helix 35 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R +Q3E835 UniProtKB Beta strand 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R +Q3E835 UniProtKB Helix 70 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R +Q3E835 UniProtKB Turn 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R +Q3E835 UniProtKB Helix 81 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V9R +##sequence-region P36051 1 919 +P36051 UniProtKB Chain 1 919 . . . ID=PRO_0000211412;Note=GPI ethanolamine phosphate transferase 1 +P36051 UniProtKB Topological domain 1 9 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Transmembrane 10 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Topological domain 31 457 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Transmembrane 458 478 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Topological domain 479 488 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Transmembrane 489 509 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Topological domain 510 512 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Transmembrane 513 533 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Topological domain 534 553 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Transmembrane 554 574 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Topological domain 575 576 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Transmembrane 577 597 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Topological domain 598 598 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Transmembrane 599 619 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Topological domain 620 626 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Transmembrane 627 647 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Topological domain 648 655 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Transmembrane 656 676 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Topological domain 677 687 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Transmembrane 688 708 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Topological domain 709 720 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Transmembrane 721 741 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Topological domain 742 776 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Transmembrane 777 797 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Topological domain 798 807 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Transmembrane 808 828 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Topological domain 829 848 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Transmembrane 849 869 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Topological domain 870 885 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Transmembrane 886 906 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Topological domain 907 919 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Glycosylation 90 90 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Glycosylation 138 138 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Glycosylation 198 198 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Glycosylation 202 202 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Glycosylation 286 286 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Glycosylation 312 312 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36051 UniProtKB Mutagenesis 227 227 . . . Note=In mcd4-174%3B defective in endoplasmic reticulum-to-Golgi transport of GPI-anchored proteins. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10069808;Dbxref=PMID:10069808 +P36051 UniProtKB Mutagenesis 302 302 . . . Note=Induces auxotrophy for ethanolamine. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11470244;Dbxref=PMID:11470244 +P36051 UniProtKB Mutagenesis 916 917 . . . Note=No effect on subcellular location. KK->SS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10069808;Dbxref=PMID:10069808 +##sequence-region P21965 1 375 +P21965 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P21965 UniProtKB Chain 2 375 . . . ID=PRO_0000086317;Note=Protein kinase MCK1 +P21965 UniProtKB Domain 35 327 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P21965 UniProtKB Nucleotide binding 41 49 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P21965 UniProtKB Active site 164 164 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P21965 UniProtKB Binding site 68 68 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P21965 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P21965 UniProtKB Modified residue 198 198 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P21965 UniProtKB Modified residue 199 199 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P21965 UniProtKB Modified residue 202 202 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P24279 1 971 +P24279 UniProtKB Chain 1 971 . . . ID=PRO_0000194099;Note=DNA replication licensing factor MCM3 +P24279 UniProtKB Domain 359 566 . . . Note=MCM +P24279 UniProtKB Nucleotide binding 409 416 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P24279 UniProtKB Motif 541 544 . . . Note=Arginine finger +P24279 UniProtKB Modified residue 761 761 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P24279 UniProtKB Modified residue 777 777 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P24279 UniProtKB Modified residue 781 781 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P24279 UniProtKB Modified residue 868 868 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P24279 UniProtKB Mutagenesis 415 415 . . . Note=No effect on MCM2-7 complex helicase activity. Loss of MCM2-7 complex helicase activity%3B when associated with MCM5 A-422. Reduces MCM2-7 complex helicase activity%3B when associated with MCM2 A-549. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657510;Dbxref=PMID:18657510 +##sequence-region Q12171 1 622 +Q12171 UniProtKB Transit peptide 1 70 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12171 UniProtKB Chain 71 622 . . . ID=PRO_0000021665;Note=Mitochondrial distribution and morphology protein 32 +Q12171 UniProtKB Topological domain 71 123 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12171 UniProtKB Transmembrane 124 144 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12171 UniProtKB Topological domain 145 601 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12171 UniProtKB Transmembrane 602 622 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q99278 1 115 +Q99278 UniProtKB Chain 1 115 . . . ID=PRO_0000096358;Note=Mediator of RNA polymerase II transcription subunit 11 +Q99278 UniProtKB Coiled coil 56 107 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99278 UniProtKB Mutagenesis 17 17 . . . Note=Results in a decrease of TFIIK and RNA polymerase II occupancies at active promoters%3B when associated with K-24. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21498544;Dbxref=PMID:21498544 +Q99278 UniProtKB Mutagenesis 24 24 . . . Note=Results in a decrease of TFIIK and RNA polymerase II occupancies at active promoters%3B when associated with K-17. L->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21498544;Dbxref=PMID:21498544 +Q99278 UniProtKB Mutagenesis 31 31 . . . Note=Impairs interaction with RAD3%2C reducing the interaction of TFIIH with the head module and consequently resulting in a reduction of RNA polymerase II CTD 'Ser-5' phosphorylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18691966;Dbxref=PMID:18691966 +Q99278 UniProtKB Mutagenesis 66 66 . . . Note=Impairs interaction with SRB4/MED17%2C SRB6/MED22 and RAD3. L->P +Q99278 UniProtKB Mutagenesis 92 92 . . . Note=Impairs interaction with SRB4/MED17. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18691966;Dbxref=PMID:18691966 +Q99278 UniProtKB Helix 5 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R84 +Q99278 UniProtKB Helix 42 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R84 +Q99278 UniProtKB Helix 45 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R84 +Q99278 UniProtKB Turn 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R84 +Q99278 UniProtKB Helix 94 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +##sequence-region Q12343 1 284 +Q12343 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12343 UniProtKB Chain 2 284 . . . ID=PRO_0000096386;Note=Mediator of RNA polymerase II transcription subunit 4 +Q12343 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12343 UniProtKB Modified residue 237 237 . . . Note=Phosphothreonine%3B by KIN28;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:15126497;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198,PMID:15126497 +Q12343 UniProtKB Modified residue 242 242 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +##sequence-region P33308 1 149 +P33308 UniProtKB Chain 1 149 . . . ID=PRO_0000076529;Note=Mediator of RNA polymerase II transcription subunit 9 +P33308 UniProtKB Motif 77 99 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33308 UniProtKB Motif 136 149 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P08465 1 486 +P08465 UniProtKB Chain 1 486 . . . ID=PRO_0000155758;Note=Homoserine O-acetyltransferase +P08465 UniProtKB Domain 66 436 . . . Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08465 UniProtKB Active site 162 162 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P45131 +P08465 UniProtKB Active site 401 401 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P45131 +P08465 UniProtKB Active site 430 430 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P45131 +P08465 UniProtKB Sequence conflict 429 486 . . . Note=GHDAFLLEFKLINKLIVQFLKTNCKAITDAAPRAWGGDVGNDETKTSVFGEAEEVTNW->ATMPSYWSLS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08465 UniProtKB Sequence conflict 429 486 . . . Note=GHDAFLLEFKLINKLIVQFLKTNCKAITDAAPRAWGGDVGNDETKTSVFGEAEEVTNW->ATMPSYWSLS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53338 1 473 +P53338 UniProtKB Chain 1 473 . . . ID=PRO_0000114956;Note=Maltose fermentation regulatory protein MAL13 +P53338 UniProtKB DNA binding 13 39 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P53338 UniProtKB Motif 46 54 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38158 1 584 +P38158 UniProtKB Chain 1 584 . . . ID=PRO_0000054329;Note=Alpha-glucosidase MAL32 +P38158 UniProtKB Active site 214 214 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38158 UniProtKB Active site 276 276 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38158 UniProtKB Site 349 349 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P40513 1 266 +P40513 UniProtKB Transit peptide 1 47 . . . Note=Mitochondrion +P40513 UniProtKB Chain 48 266 . . . ID=PRO_0000018589;Note=Mitochondrial acidic protein MAM33 +P40513 UniProtKB Modified residue 91 91 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40513 UniProtKB Sequence conflict 129 129 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40513 UniProtKB Helix 50 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0 +P40513 UniProtKB Helix 74 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0 +P40513 UniProtKB Beta strand 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0 +P40513 UniProtKB Beta strand 95 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0 +P40513 UniProtKB Beta strand 108 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0 +P40513 UniProtKB Helix 115 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0 +P40513 UniProtKB Beta strand 151 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0 +P40513 UniProtKB Beta strand 166 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0 +P40513 UniProtKB Turn 175 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0 +P40513 UniProtKB Beta strand 179 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0 +P40513 UniProtKB Helix 191 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0 +P40513 UniProtKB Helix 199 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0 +P40513 UniProtKB Helix 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0 +P40513 UniProtKB Helix 219 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0 +P40513 UniProtKB Helix 236 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QV0 +##sequence-region Q12296 1 706 +Q12296 UniProtKB Chain 1 706 . . . ID=PRO_0000255960;Note=Protein MAM3 +Q12296 UniProtKB Topological domain 1 16 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12296 UniProtKB Transmembrane 17 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12296 UniProtKB Topological domain 38 65 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12296 UniProtKB Transmembrane 66 86 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12296 UniProtKB Topological domain 87 120 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12296 UniProtKB Transmembrane 121 141 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12296 UniProtKB Topological domain 142 145 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12296 UniProtKB Transmembrane 146 166 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12296 UniProtKB Topological domain 167 177 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12296 UniProtKB Transmembrane 178 198 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12296 UniProtKB Topological domain 199 706 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12296 UniProtKB Domain 65 233 . . . Note=DUF21 +Q12296 UniProtKB Domain 259 320 . . . Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +Q12296 UniProtKB Domain 321 386 . . . Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +Q12296 UniProtKB Modified residue 439 439 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12296 UniProtKB Modified residue 447 447 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12296 UniProtKB Modified residue 527 527 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q12296 UniProtKB Modified residue 603 603 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12296 UniProtKB Modified residue 604 604 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12296 UniProtKB Modified residue 607 607 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12296 UniProtKB Modified residue 614 614 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P03879 1 638 +P03879 UniProtKB Region 1 253 . . . Note=COB exons 1 to 4 encoded +P03879 UniProtKB Region 253 638 . . . Note=COB intron 4 encoded +P03879 UniProtKB Sequence conflict 370 370 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03879 UniProtKB Sequence conflict 390 390 . . . Note=T->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03879 UniProtKB Sequence conflict 433 433 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03879 UniProtKB Sequence conflict 459 459 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03879 UniProtKB Sequence conflict 465 465 . . . Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03879 UniProtKB Sequence conflict 586 586 . . . Note=T->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39678 1 833 +P39678 UniProtKB Chain 1 833 . . . ID=PRO_0000067062;Note=Transcription factor MBP1 +P39678 UniProtKB Domain 5 111 . . . Note=HTH APSES-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630 +P39678 UniProtKB Repeat 394 423 . . . Note=ANK 1 +P39678 UniProtKB Repeat 512 541 . . . Note=ANK 2 +P39678 UniProtKB DNA binding 36 57 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630 +P39678 UniProtKB Modified residue 110 110 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P39678 UniProtKB Modified residue 325 325 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39678 UniProtKB Modified residue 326 326 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39678 UniProtKB Modified residue 330 330 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39678 UniProtKB Modified residue 827 827 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39678 UniProtKB Beta strand 5 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8 +P39678 UniProtKB Beta strand 13 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8 +P39678 UniProtKB Beta strand 24 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8 +P39678 UniProtKB Turn 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8 +P39678 UniProtKB Beta strand 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1L3G +P39678 UniProtKB Helix 36 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8 +P39678 UniProtKB Helix 47 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8 +P39678 UniProtKB Turn 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8 +P39678 UniProtKB Beta strand 64 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8 +P39678 UniProtKB Turn 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MB1 +P39678 UniProtKB Beta strand 75 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8 +P39678 UniProtKB Helix 80 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8 +P39678 UniProtKB Helix 93 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BM8 +##sequence-region P23493 1 339 +P23493 UniProtKB Chain 1 339 . . . ID=PRO_0000096271;Note=Mitochondrial biogenesis regulation protein 1 +P23493 UniProtKB Modified residue 159 159 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P23493 UniProtKB Modified residue 177 177 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P23493 UniProtKB Modified residue 224 224 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P23493 UniProtKB Modified residue 227 227 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P23493 UniProtKB Sequence conflict 88 88 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23493 UniProtKB Sequence conflict 168 168 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23493 UniProtKB Sequence conflict 206 206 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23493 UniProtKB Sequence conflict 245 245 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q01159 1 459 +Q01159 UniProtKB Chain 1 459 . . . ID=PRO_0000210106;Note=mRNA-capping enzyme subunit alpha +Q01159 UniProtKB Active site 70 70 . . . Note=N6-GMP-lysine intermediate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8022828;Dbxref=PMID:8022828 +Q01159 UniProtKB Mutagenesis 57 57 . . . Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 58 58 . . . Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 59 59 . . . Note=No effect. K->A%2CT%2CS%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8022828;Dbxref=PMID:8022828 +Q01159 UniProtKB Mutagenesis 66 66 . . . Note=Temperature-sensitive. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 70 70 . . . Note=Lethal. K->A%2CR%2CM%2CI%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8022828;Dbxref=PMID:8022828 +Q01159 UniProtKB Mutagenesis 71 71 . . . Note=No effect. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 72 72 . . . Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 73 73 . . . Note=Lethal. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 95 95 . . . Note=Temperature-sensitive. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 96 96 . . . Note=Temperature-sensitive. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 97 97 . . . Note=Temperature-sensitive. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 107 109 . . . Note=Reduced growth at 25 degrees and lethal at 37 degrees. RFP->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 114 114 . . . Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 115 115 . . . Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 116 116 . . . Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 117 117 . . . Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 118 118 . . . Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 129 129 . . . Note=No effect. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 130 130 . . . Note=Lethal. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 131 131 . . . Note=Temperature-sensitive. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 132 132 . . . Note=Lethal. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 134 134 . . . Note=No effect. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 218 218 . . . Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 219 219 . . . Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 225 225 . . . Note=Lethal. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 226 226 . . . Note=Lethal. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 241 241 . . . Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 242 242 . . . Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 249 249 . . . Note=Lethal. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 253 253 . . . Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 254 254 . . . Note=No effect. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 255 255 . . . Note=Temperature-sensitive. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 257 257 . . . Note=Lethal. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 274 274 . . . Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 275 275 . . . Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 276 276 . . . Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 395 395 . . . Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Mutagenesis 396 396 . . . Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7991582;Dbxref=PMID:7991582 +Q01159 UniProtKB Sequence conflict 45 45 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01159 UniProtKB Sequence conflict 300 300 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01159 UniProtKB Helix 21 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Helix 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 47 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Helix 53 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 65 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 73 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Turn 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 89 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 100 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Helix 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 126 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Turn 139 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 144 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 162 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Helix 166 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Helix 178 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 197 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Helix 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Helix 210 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 224 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 238 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Turn 251 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 257 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 291 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Helix 300 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Turn 313 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Helix 317 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Turn 321 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 324 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Turn 334 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Helix 337 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 350 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Turn 358 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 365 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Beta strand 372 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Helix 378 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Helix 395 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Helix 399 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +Q01159 UniProtKB Helix 402 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KYH +##sequence-region P32783 1 436 +P32783 UniProtKB Chain 1 436 . . . ID=PRO_0000210134;Note=mRNA cap guanine-N7 methyltransferase +P32783 UniProtKB Domain 101 430 . . . Note=mRNA cap 0 methyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895 +P32783 UniProtKB Region 150 151 . . . Note=mRNA cap binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895 +P32783 UniProtKB Binding site 154 154 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895 +P32783 UniProtKB Binding site 172 172 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895 +P32783 UniProtKB Binding site 194 194 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895 +P32783 UniProtKB Binding site 223 223 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43148 +P32783 UniProtKB Binding site 249 249 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43148 +P32783 UniProtKB Binding site 253 253 . . . Note=mRNA cap;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895 +P32783 UniProtKB Binding site 254 254 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43148 +P32783 UniProtKB Binding site 347 347 . . . Note=mRNA cap;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895 +P32783 UniProtKB Binding site 416 416 . . . Note=mRNA cap;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895 +P32783 UniProtKB Site 175 175 . . . Note=mRNA cap binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895 +P32783 UniProtKB Site 181 181 . . . Note=mRNA cap binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895 +P32783 UniProtKB Site 206 206 . . . Note=mRNA cap binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00895 +P32783 UniProtKB Mutagenesis 168 168 . . . Note=Still viable%3B normal growth. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431 +P32783 UniProtKB Mutagenesis 170 170 . . . Note=Non-viable%3B reduced enzyme activity to 8%25 of wild-type. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11472630,ECO:0000269|PubMed:9169431;Dbxref=PMID:11472630,PMID:9169431 +P32783 UniProtKB Mutagenesis 170 170 . . . Note=Still viable%3B increase in activity. E->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11472630,ECO:0000269|PubMed:9169431;Dbxref=PMID:11472630,PMID:9169431 +P32783 UniProtKB Mutagenesis 170 170 . . . Note=Non-viable%3B reduced enzyme activity to 8%25 of wild-type. E->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11472630,ECO:0000269|PubMed:9169431;Dbxref=PMID:11472630,PMID:9169431 +P32783 UniProtKB Mutagenesis 172 172 . . . Note=Still viable%3B normal growth. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431 +P32783 UniProtKB Mutagenesis 174 174 . . . Note=Non viable%3B no growth. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8552073;Dbxref=PMID:8552073 +P32783 UniProtKB Mutagenesis 176 176 . . . Note=Still viable%3B normal growth. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431 +P32783 UniProtKB Mutagenesis 178 178 . . . Note=Microcolony formation. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8552073;Dbxref=PMID:8552073 +P32783 UniProtKB Mutagenesis 181 181 . . . Note=Still viable%3B normal growth. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431 +P32783 UniProtKB Mutagenesis 182 182 . . . Note=Still viable%3B normal growth. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431 +P32783 UniProtKB Mutagenesis 194 194 . . . Note=Lethal%3B no enzyme activity. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11472630,ECO:0000269|PubMed:9169431;Dbxref=PMID:11472630,PMID:9169431 +P32783 UniProtKB Mutagenesis 194 194 . . . Note=Still viable%3B activity near to wild-type. D->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11472630,ECO:0000269|PubMed:9169431;Dbxref=PMID:11472630,PMID:9169431 +P32783 UniProtKB Mutagenesis 194 194 . . . Note=Lethal%3B no enzyme activity. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11472630,ECO:0000269|PubMed:9169431;Dbxref=PMID:11472630,PMID:9169431 +P32783 UniProtKB Mutagenesis 206 206 . . . Note=Lethal. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11472630,ECO:0000269|PubMed:9169431;Dbxref=PMID:11472630,PMID:9169431 +P32783 UniProtKB Mutagenesis 206 206 . . . Note=Still viable%3B little change in enzyme activity. R->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11472630,ECO:0000269|PubMed:9169431;Dbxref=PMID:11472630,PMID:9169431 +P32783 UniProtKB Mutagenesis 253 253 . . . Note=Still viable%3B normal growth. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8552073;Dbxref=PMID:8552073 +P32783 UniProtKB Mutagenesis 254 254 . . . Note=Non viable%3B no growth. Y->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8552073,ECO:0000269|PubMed:9169431;Dbxref=PMID:8552073,PMID:9169431 +P32783 UniProtKB Mutagenesis 254 254 . . . Note=Still viable%3B slow growth%3B near to wild-type enzyme activity. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8552073,ECO:0000269|PubMed:9169431;Dbxref=PMID:8552073,PMID:9169431 +P32783 UniProtKB Mutagenesis 254 254 . . . Note=Lethal%3B Enzyme activity 10%25 of wild-type. Y->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8552073,ECO:0000269|PubMed:9169431;Dbxref=PMID:8552073,PMID:9169431 +P32783 UniProtKB Mutagenesis 276 276 . . . Note=Still viable%3B normal growth. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431 +P32783 UniProtKB Mutagenesis 277 277 . . . Note=Still viable%3B normal growth. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431 +P32783 UniProtKB Mutagenesis 282 282 . . . Note=Still viable%3B normal growth. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8552073;Dbxref=PMID:8552073 +P32783 UniProtKB Mutagenesis 287 287 . . . Note=Still viable%3B normal growth. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8552073;Dbxref=PMID:8552073 +P32783 UniProtKB Mutagenesis 347 347 . . . Note=Still viable%3B normal growth. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431 +P32783 UniProtKB Mutagenesis 348 348 . . . Note=Still viable%3B normal growth. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431 +P32783 UniProtKB Mutagenesis 349 349 . . . Note=Still viable%3B normal growth. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431 +P32783 UniProtKB Mutagenesis 350 350 . . . Note=Still viable%3B normal growth. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431 +P32783 UniProtKB Mutagenesis 361 361 . . . Note=Still viable%3B normal growth. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8552073;Dbxref=PMID:8552073 +P32783 UniProtKB Mutagenesis 362 362 . . . Note=Still viable%3B normal growth. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8552073;Dbxref=PMID:8552073 +P32783 UniProtKB Mutagenesis 363 363 . . . Note=Still viable%3B normal growth. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431 +P32783 UniProtKB Mutagenesis 366 366 . . . Note=Still viable%3B normal growth. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431 +P32783 UniProtKB Mutagenesis 367 367 . . . Note=Still viable%3B normal growth. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431 +P32783 UniProtKB Mutagenesis 372 372 . . . Note=Still viable%3B normal growth. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9169431;Dbxref=PMID:9169431 +P32783 UniProtKB Sequence conflict 126 126 . . . Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02891 1 456 +Q02891 UniProtKB Chain 1 456 . . . ID=PRO_0000212456;Note=Medium-chain fatty acid ethyl ester synthase/esterase 1 +Q02891 UniProtKB Domain 168 434 . . . Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02891 UniProtKB Active site 251 251 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02891 UniProtKB Active site 399 399 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02891 UniProtKB Active site 428 428 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P42834 1 146 +P42834 UniProtKB Chain 1 146 . . . ID=PRO_0000071094;Note=Mitochondrial DnaJ homolog 2 +P42834 UniProtKB Domain 85 146 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +##sequence-region P33310 1 695 +P33310 UniProtKB Transit peptide 1 100 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33310 UniProtKB Chain 101 695 . . . ID=PRO_0000045330;Note=ATP-dependent permease MDL1%2C mitochondrial +P33310 UniProtKB Transmembrane 103 123 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P33310 UniProtKB Transmembrane 156 176 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P33310 UniProtKB Transmembrane 242 262 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P33310 UniProtKB Transmembrane 337 357 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P33310 UniProtKB Transmembrane 372 392 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P33310 UniProtKB Domain 103 398 . . . Note=ABC transmembrane type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P33310 UniProtKB Domain 432 673 . . . Note=ABC transporter;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P33310 UniProtKB Nucleotide binding 467 474 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P33310 UniProtKB Mutagenesis 467 467 . . . Note=Decreased release of long peptides from mitochondria. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11251115;Dbxref=PMID:11251115 +P33310 UniProtKB Mutagenesis 575 575 . . . Note=Decreased release of long peptides from mitochondria. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11251115;Dbxref=PMID:11251115 +P33310 UniProtKB Mutagenesis 598 598 . . . Note=Decreased release of long peptides from mitochondria. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11251115;Dbxref=PMID:11251115 +P33310 UniProtKB Sequence conflict 22 22 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33310 UniProtKB Sequence conflict 150 150 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33310 UniProtKB Sequence conflict 267 268 . . . Note=GA->WP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33310 UniProtKB Sequence conflict 313 314 . . . Note=NE->KQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P33311 1 773 +P33311 UniProtKB Transit peptide 1 90 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33311 UniProtKB Chain 91 773 . . . ID=PRO_0000045331;Note=ATP-dependent permease MDL2%2C mitochondrial +P33311 UniProtKB Transmembrane 123 143 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P33311 UniProtKB Transmembrane 170 192 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P33311 UniProtKB Transmembrane 257 277 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P33311 UniProtKB Domain 119 413 . . . Note=ABC transmembrane type-1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P33311 UniProtKB Domain 493 733 . . . Note=ABC transporter;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P33311 UniProtKB Nucleotide binding 481 488 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P33311 UniProtKB Sequence conflict 56 56 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33311 UniProtKB Sequence conflict 265 265 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33311 UniProtKB Sequence conflict 752 752 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32489 1 222 +P32489 UniProtKB Chain 1 222 . . . ID=PRO_0000096403;Note=Meiosis protein 5 +P32489 UniProtKB Sequence conflict 155 156 . . . Note=SD->VT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32489 UniProtKB Sequence conflict 160 162 . . . Note=QLS->RTFR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32489 UniProtKB Sequence conflict 168 168 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32489 UniProtKB Sequence conflict 217 217 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P29496 1 775 +P29496 UniProtKB Chain 1 775 . . . ID=PRO_0000194111;Note=Minichromosome maintenance protein 5 +P29496 UniProtKB Domain 366 573 . . . Note=MCM +P29496 UniProtKB Nucleotide binding 416 423 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P29496 UniProtKB Motif 548 551 . . . Note=Arginine finger +P29496 UniProtKB Compositional bias 351 356 . . . Note=Poly-Glu +P29496 UniProtKB Mutagenesis 422 422 . . . Note=Loss of MCM2-7 complex helicase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18657510;Dbxref=PMID:18657510 +##sequence-region Q06567 1 569 +Q06567 UniProtKB Transit peptide 1 18 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06567 UniProtKB Chain 19 569 . . . ID=PRO_0000200737;Note=ABC1 family protein MCP2 +Q06567 UniProtKB Topological domain 19 34 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23781023;Dbxref=PMID:23781023 +Q06567 UniProtKB Transmembrane 35 51 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06567 UniProtKB Topological domain 52 569 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23781023;Dbxref=PMID:23781023 +##sequence-region P36060 1 302 +P36060 UniProtKB Chain 1 302 . . . ID=PRO_0000019404;Note=NADH-cytochrome b5 reductase p34 form +P36060 UniProtKB Propeptide 1 41 . . . ID=PRO_0000019405;Note=Removed in p32 form;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8001120,ECO:0000269|PubMed:9866716;Dbxref=PMID:8001120,PMID:9866716 +P36060 UniProtKB Chain 42 302 . . . ID=PRO_0000019406;Note=NADH-cytochrome b5 reductase p32 form +P36060 UniProtKB Transmembrane 12 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36060 UniProtKB Domain 51 155 . . . Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716 +P36060 UniProtKB Nucleotide binding 158 193 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36060 UniProtKB Site 41 42 . . . Note=Cleavage%3B by IMP1 +P36060 UniProtKB Modified residue 278 278 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P36060 UniProtKB Mutagenesis 23 24 . . . Note=Prevents insertion into the outer membrane and increases the efficiency of import into the intermembrane space. AA->QQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9199337;Dbxref=PMID:9199337 +P36060 UniProtKB Sequence conflict 2 2 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36060 UniProtKB Sequence conflict 101 101 . . . Note=N->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53885 1 366 +P53885 UniProtKB Chain 1 366 . . . ID=PRO_0000096326;Note=Signal transduction protein MDG1 +P53885 UniProtKB Modified residue 160 160 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53885 UniProtKB Modified residue 216 216 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53885 UniProtKB Modified residue 288 288 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53885 UniProtKB Cross-link 314 314 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P32569 1 687 +P32569 UniProtKB Chain 1 687 . . . ID=PRO_0000096366;Note=Mediator of RNA polymerase II transcription subunit 17 +P32569 UniProtKB Mutagenesis 353 353 . . . Note=In SRB4-1%3B suppresses the phenotypic defects of an RNA polymerase II CTD truncation. G->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8324825;Dbxref=PMID:8324825 +P32569 UniProtKB Sequence conflict 430 431 . . . Note=QL->PI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32569 UniProtKB Sequence conflict 647 647 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32569 UniProtKB Beta strand 388 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Beta strand 403 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Helix 425 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Helix 450 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Beta strand 457 461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Beta strand 464 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Beta strand 470 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Helix 498 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Turn 525 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Helix 535 538 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Helix 542 565 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Turn 566 569 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Beta strand 574 579 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Helix 597 604 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Helix 607 610 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Beta strand 614 620 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Beta strand 630 636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Beta strand 640 642 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Beta strand 644 650 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Turn 654 656 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Beta strand 660 665 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +P32569 UniProtKB Helix 667 680 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H62 +##sequence-region Q12124 1 431 +Q12124 UniProtKB Chain 1 431 . . . ID=PRO_0000096381;Note=Mediator of RNA polymerase II transcription subunit 2 +Q12124 UniProtKB Compositional bias 107 142 . . . Note=Glu-rich +Q12124 UniProtKB Compositional bias 264 412 . . . Note=Asn-rich +Q12124 UniProtKB Modified residue 6 6 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12124 UniProtKB Modified residue 208 208 . . . Note=Phosphoserine%3B by CDK8;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14988503,ECO:0000269|PubMed:16109375;Dbxref=PMID:14988503,PMID:16109375 +Q12124 UniProtKB Mutagenesis 208 208 . . . Note=Reduces expression of several genes from the endogenous 2-micron plasmid and augments expression of numerous iron-response genes. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14988503,ECO:0000269|PubMed:16109375;Dbxref=PMID:14988503,PMID:16109375 +##sequence-region P38633 1 127 +P38633 UniProtKB Chain 1 127 . . . ID=PRO_0000212534;Note=Mediator of RNA polymerase II transcription subunit 31 +P38633 UniProtKB Helix 22 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI +P38633 UniProtKB Helix 36 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI +P38633 UniProtKB Helix 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI +P38633 UniProtKB Helix 53 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI +P38633 UniProtKB Helix 61 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI +P38633 UniProtKB Helix 69 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI +P38633 UniProtKB Helix 77 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI +P38633 UniProtKB Beta strand 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI +P38633 UniProtKB Helix 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FBI +##sequence-region P40260 1 492 +P40260 UniProtKB Chain 1 492 . . . ID=PRO_0000139754;Note=Ammonium transporter MEP1 +P40260 UniProtKB Topological domain 1 18 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Transmembrane 19 39 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Topological domain 40 49 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Transmembrane 50 70 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Topological domain 71 109 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Transmembrane 110 130 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Topological domain 131 140 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Transmembrane 141 161 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Topological domain 162 174 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Transmembrane 175 195 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Topological domain 196 210 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Transmembrane 211 231 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Topological domain 232 240 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Transmembrane 241 261 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Topological domain 262 268 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Transmembrane 269 289 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Topological domain 290 290 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Transmembrane 291 311 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Topological domain 312 331 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Transmembrane 332 352 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Topological domain 353 373 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Transmembrane 374 394 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Topological domain 395 492 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40260 UniProtKB Modified residue 442 442 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40260 UniProtKB Modified residue 445 445 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P16523 1 270 +P16523 UniProtKB Chain 1 270 . . . ID=PRO_0000050120;Note=Meiotic recombination 1 protein +P16523 UniProtKB Domain 191 225 . . . Note=KH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117 +##sequence-region P32389 1 672 +P32389 UniProtKB Chain 1 672 . . . ID=PRO_0000076519;Note=Transcriptional activator of sulfur metabolism MET4 +P32389 UniProtKB Domain 586 649 . . . Note=bZIP +P32389 UniProtKB Region 95 144 . . . Note=Transcriptional activation +P32389 UniProtKB Region 188 235 . . . Note=Inhibitory region%3B AdoMet responsiveness%3B required for interaction with MET30 +P32389 UniProtKB Region 312 375 . . . Note=Auxiliary%3B required for high transcriptional activity under nonrepressive growth conditions +P32389 UniProtKB Region 375 403 . . . Note=Required for interaction with MET31 and MET32 +P32389 UniProtKB Region 601 612 . . . Note=Basic motif;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32389 UniProtKB Region 614 642 . . . Note=Leucine-zipper;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32389 UniProtKB Coiled coil 609 648 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32389 UniProtKB Compositional bias 53 57 . . . Note=Poly-Ser +P32389 UniProtKB Compositional bias 106 242 . . . Note=Asn-rich +P32389 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32389 UniProtKB Modified residue 564 564 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32389 UniProtKB Sequence conflict 441 442 . . . Note=RG->AA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32389 UniProtKB Sequence conflict 441 442 . . . Note=RG->AA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P15807 1 274 +P15807 UniProtKB Chain 1 274 . . . ID=PRO_0000096446;Note=Siroheme biosynthesis protein MET8 +P15807 UniProtKB Nucleotide binding 23 24 . . . Note=NAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11980703;Dbxref=PMID:11980703 +P15807 UniProtKB Nucleotide binding 43 45 . . . Note=NAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11980703;Dbxref=PMID:11980703 +P15807 UniProtKB Active site 141 141 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15807 UniProtKB Binding site 93 93 . . . Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11980703;Dbxref=PMID:11980703 +P15807 UniProtKB Mutagenesis 22 22 . . . Note=Loss of dehydrogenase activity. No effect on chelatase activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11980703;Dbxref=PMID:11980703 +P15807 UniProtKB Mutagenesis 141 141 . . . Note=Loss of chelatase and dehydrogenase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11980703;Dbxref=PMID:11980703 +P15807 UniProtKB Mutagenesis 237 237 . . . Note=No effect on dehydrogenase or chelatase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11980703;Dbxref=PMID:11980703 +P15807 UniProtKB Sequence conflict 15 15 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15807 UniProtKB Sequence conflict 33 33 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15807 UniProtKB Sequence conflict 61 61 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15807 UniProtKB Sequence conflict 102 102 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15807 UniProtKB Beta strand 5 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Beta strand 15 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Helix 23 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Helix 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Beta strand 38 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Helix 50 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Helix 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Turn 68 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Beta strand 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Beta strand 86 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Helix 95 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Beta strand 107 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Helix 117 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Beta strand 135 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Helix 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Beta strand 146 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Beta strand 152 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Turn 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Beta strand 160 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Helix 171 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Helix 193 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Helix 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Helix 217 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Helix 236 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Helix 241 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Turn 253 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +P15807 UniProtKB Helix 264 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KYQ +##sequence-region P36013 1 669 +P36013 UniProtKB Active site 187 187 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36013 UniProtKB Active site 259 259 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36013 UniProtKB Metal binding 330 330 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36013 UniProtKB Metal binding 331 331 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36013 UniProtKB Metal binding 354 354 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36013 UniProtKB Binding site 354 354 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36013 UniProtKB Binding site 499 499 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36013 UniProtKB Site 354 354 . . . Note=Important for activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P03873 1 423 +P03873 UniProtKB Chain 1 423 . . . ID=PRO_0000061914;Note=Cytochrome b mRNA maturase bI2 +P03873 UniProtKB Topological domain 1 31 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P03873 UniProtKB Transmembrane 32 52 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968 +P03873 UniProtKB Topological domain 53 84 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P03873 UniProtKB Transmembrane 85 105 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968 +P03873 UniProtKB Topological domain 106 115 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P03873 UniProtKB Transmembrane 116 136 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968 +P03873 UniProtKB Topological domain 137 153 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P03873 UniProtKB Transmembrane 154 174 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00968 +P03873 UniProtKB Topological domain 175 423 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P03873 UniProtKB Region 1 143 . . . Note=Cytochrome b +P03873 UniProtKB Region 144 423 . . . Note=Maturase +P03873 UniProtKB Natural variant 122 122 . . . Note=In strain: 777-3A. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7004642;Dbxref=PMID:7004642 +P03873 UniProtKB Natural variant 221 221 . . . Note=In strain: Capensis / YB4237. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8670880;Dbxref=PMID:8670880 +P03873 UniProtKB Natural variant 315 315 . . . Note=In strain: Capensis / YB4237. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8670880;Dbxref=PMID:8670880 +P03873 UniProtKB Natural variant 324 324 . . . Note=In strain: 777-3A. I->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7004642;Dbxref=PMID:7004642 +P03873 UniProtKB Natural variant 355 355 . . . Note=In strain: Capensis / YB4237. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8670880;Dbxref=PMID:8670880 +P03873 UniProtKB Natural variant 382 382 . . . Note=In strain: Capensis / YB4237. T->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8670880;Dbxref=PMID:8670880 +P03873 UniProtKB Mutagenesis 228 228 . . . Note=In M1282 / M4111%3B abolishes maturase and endonuclease activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11016843;Dbxref=PMID:11016843 +P03873 UniProtKB Mutagenesis 233 233 . . . Note=Abolishes endonuclease activity. D->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11016843;Dbxref=PMID:11016843 +P03873 UniProtKB Mutagenesis 235 235 . . . Note=In M4962%3B abolishes maturase and endonuclease activity. H->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11016843;Dbxref=PMID:11016843 +P03873 UniProtKB Mutagenesis 339 339 . . . Note=Abolishes maturase and endonuclease activity. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11016843;Dbxref=PMID:11016843 +P03873 UniProtKB Mutagenesis 343 343 . . . Note=Abolishes endonuclease activity. D->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11016843;Dbxref=PMID:11016843 +P03873 UniProtKB Mutagenesis 344 344 . . . Note=Abolishes endonuclease activity. D->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11016843;Dbxref=PMID:11016843 +P03873 UniProtKB Mutagenesis 364 364 . . . Note=Abolishes endonuclease activity. In box3-2 / G1909%3B abolishes maturase and endonuclease activity%3B when associated with N-393. V->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7004642,ECO:0000269|PubMed:8670880;Dbxref=PMID:7004642,PMID:8670880 +P03873 UniProtKB Mutagenesis 379 379 . . . Note=In W404-3%3B abolishes maturase and endonuclease activity%3B when associated with M-395. S->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11016843;Dbxref=PMID:11016843 +P03873 UniProtKB Mutagenesis 393 393 . . . Note=Abolishes endonuclease activity. In box3-2 / G1909%3B abolishes maturase and endonuclease activity%3B when associated with F-364. I->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7004642,ECO:0000269|PubMed:8670880;Dbxref=PMID:7004642,PMID:8670880 +P03873 UniProtKB Mutagenesis 395 395 . . . Note=In W404-4%3B abolishes maturase and endonuclease activity%3B when associated with Y-379. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11016843;Dbxref=PMID:11016843 +##sequence-region Q08268 1 501 +Q08268 UniProtKB Chain 1 501 . . . ID=PRO_0000211404;Note=Probable transporter MCH4 +Q08268 UniProtKB Topological domain 1 97 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Transmembrane 98 120 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Topological domain 121 134 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Transmembrane 135 157 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Topological domain 158 163 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Transmembrane 164 183 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Topological domain 184 187 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Transmembrane 188 210 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Topological domain 211 222 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Transmembrane 223 245 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Topological domain 246 254 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Transmembrane 255 274 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Topological domain 275 310 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Transmembrane 311 333 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Topological domain 334 342 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Transmembrane 343 365 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Topological domain 366 371 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Transmembrane 372 394 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Topological domain 395 403 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Transmembrane 404 426 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Topological domain 427 438 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Transmembrane 439 461 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Topological domain 462 470 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Transmembrane 471 493 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Topological domain 494 501 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Glycosylation 131 131 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08268 UniProtKB Cross-link 54 54 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P18409 1 493 +P18409 UniProtKB Chain 1 493 . . . ID=PRO_0000096327;Note=Mitochondrial distribution and morphology protein 10 +P18409 UniProtKB Sequence conflict 272 272 . . . Note=N->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18409 UniProtKB Sequence conflict 272 272 . . . Note=N->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18409 UniProtKB Sequence conflict 272 272 . . . Note=N->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q01846 1 1127 +Q01846 UniProtKB Chain 1 1127 . . . ID=PRO_0000096330;Note=Structural protein MDM1 +Q01846 UniProtKB Domain 85 273 . . . Note=PXA;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147,ECO:0000255|PROSITE-ProRule:PRU00553 +Q01846 UniProtKB Domain 782 905 . . . Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147 +Q01846 UniProtKB Coiled coil 705 762 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01846 UniProtKB Modified residue 670 670 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q01846 UniProtKB Modified residue 673 673 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q01846 UniProtKB Modified residue 692 692 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q01846 UniProtKB Sequence conflict 635 635 . . . Note=H->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01846 UniProtKB Sequence conflict 772 772 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01846 UniProtKB Sequence conflict 899 899 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01846 UniProtKB Sequence conflict 1063 1063 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01846 UniProtKB Sequence conflict 1081 1081 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01846 UniProtKB Sequence conflict 1096 1096 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40356 1 397 +P40356 UniProtKB Chain 1 397 . . . ID=PRO_0000096382;Note=Mediator of RNA polymerase II transcription subunit 3 +P40356 UniProtKB Compositional bias 347 362 . . . Note=Gln-rich +P40356 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40356 UniProtKB Sequence conflict 158 158 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53114 1 1132 +P53114 UniProtKB Chain 1 1132 . . . ID=PRO_0000096387;Note=Mediator of RNA polymerase II transcription subunit 5 +##sequence-region P38782 1 295 +P38782 UniProtKB Chain 1 295 . . . ID=PRO_0000096391;Note=Mediator of RNA polymerase II transcription subunit 6 +P38782 UniProtKB Modified residue 225 225 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P41948 1 499 +P41948 UniProtKB Chain 1 499 . . . ID=PRO_0000139755;Note=Ammonium transporter MEP2 +P41948 UniProtKB Topological domain 1 31 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Transmembrane 32 52 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Topological domain 53 62 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Transmembrane 63 83 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Topological domain 84 122 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Transmembrane 123 143 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Topological domain 144 152 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Transmembrane 153 173 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Topological domain 174 187 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Transmembrane 188 208 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Topological domain 209 230 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Transmembrane 231 251 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Topological domain 252 257 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Transmembrane 258 278 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Topological domain 279 300 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Transmembrane 301 321 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Topological domain 322 346 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Transmembrane 347 367 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Topological domain 368 393 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Transmembrane 394 414 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Topological domain 415 499 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41948 UniProtKB Glycosylation 4 4 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11069679;Dbxref=PMID:11069679 +P41948 UniProtKB Mutagenesis 4 4 . . . Note=Molecular weight equal to non-glycosylated form. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11069679;Dbxref=PMID:11069679 +P41948 UniProtKB Mutagenesis 252 252 . . . Note=Molecular weight similar to wild-type glycosylated form. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11069679;Dbxref=PMID:11069679 +P41948 UniProtKB Mutagenesis 368 368 . . . Note=Molecular weight similar to wild-type glycosylated form. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11069679;Dbxref=PMID:11069679 +P41948 UniProtKB Mutagenesis 483 483 . . . Note=Molecular weight similar to wild-type glycosylated form. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11069679;Dbxref=PMID:11069679 +P41948 UniProtKB Helix 23 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 29 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 45 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 65 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 84 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Beta strand 91 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Beta strand 111 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 122 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 150 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 165 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Turn 178 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Turn 190 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 194 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 228 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 248 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Beta strand 251 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 255 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 291 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Turn 303 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 314 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 333 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 342 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 365 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 369 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 382 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 389 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Turn 419 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Turn 427 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Helix 436 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +P41948 UniProtKB Beta strand 441 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AEX +##sequence-region P53390 1 489 +P53390 UniProtKB Chain 1 489 . . . ID=PRO_0000139756;Note=Ammonium transporter MEP3 +P53390 UniProtKB Topological domain 1 17 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Transmembrane 18 38 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Topological domain 39 48 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Transmembrane 49 69 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Topological domain 70 108 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Transmembrane 109 129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Topological domain 130 139 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Transmembrane 140 160 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Topological domain 161 173 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Transmembrane 174 194 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Topological domain 195 209 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Transmembrane 210 230 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Topological domain 231 239 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Transmembrane 240 260 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Topological domain 261 267 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Transmembrane 268 288 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Topological domain 289 289 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Transmembrane 290 310 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Topological domain 311 330 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Transmembrane 331 351 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Topological domain 352 372 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Transmembrane 373 393 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Topological domain 394 489 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53390 UniProtKB Sequence conflict 7 7 . . . Note=H->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32559 1 526 +P32559 UniProtKB Transit peptide 1 19 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32559 UniProtKB Chain 20 526 . . . ID=PRO_0000035781;Note=tRNA modification GTPase MSS1%2C mitochondrial +P32559 UniProtKB Domain 274 444 . . . Note=TrmE-type G +P32559 UniProtKB Nucleotide binding 281 288 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32559 UniProtKB Nucleotide binding 328 332 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32559 UniProtKB Nucleotide binding 394 397 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32559 UniProtKB Sequence conflict 53 53 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CY06 1 175 +P0CY06 UniProtKB Chain 1 175 . . . ID=PRO_0000096610;Note=Mating-type protein ALPHA1 +P0CY06 UniProtKB DNA binding 88 144 . . . Note=Alpha box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00655 +##sequence-region P38849 1 526 +P38849 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38849 UniProtKB Chain 21 526 . . . ID=PRO_0000202926;Note=Maintenance of telomere capping protein 6 +P38849 UniProtKB Topological domain 21 477 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38849 UniProtKB Transmembrane 478 498 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38849 UniProtKB Topological domain 499 526 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38849 UniProtKB Glycosylation 32 32 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38849 UniProtKB Glycosylation 60 60 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38849 UniProtKB Glycosylation 80 80 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38849 UniProtKB Glycosylation 89 89 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38849 UniProtKB Glycosylation 156 156 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38849 UniProtKB Glycosylation 171 171 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38849 UniProtKB Glycosylation 175 175 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38849 UniProtKB Glycosylation 202 202 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38849 UniProtKB Glycosylation 240 240 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38849 UniProtKB Glycosylation 259 259 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38849 UniProtKB Glycosylation 311 311 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38849 UniProtKB Glycosylation 362 362 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38849 UniProtKB Glycosylation 433 433 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CX81 1 61 +P0CX81 UniProtKB Propeptide 1 8 . . . ID=PRO_0000410444 +P0CX81 UniProtKB Chain 9 61 . . . ID=PRO_0000410445;Note=Copper metallothionein 1-2 +P0CX81 UniProtKB Metal binding 15 15 . . . Note=Copper 1 +P0CX81 UniProtKB Metal binding 15 15 . . . Note=Copper 2 +P0CX81 UniProtKB Metal binding 17 17 . . . Note=Copper 1 +P0CX81 UniProtKB Metal binding 17 17 . . . Note=Copper 3 +P0CX81 UniProtKB Metal binding 19 19 . . . Note=Copper 4 +P0CX81 UniProtKB Metal binding 19 19 . . . Note=Copper 5 +P0CX81 UniProtKB Metal binding 22 22 . . . Note=Copper 3 +P0CX81 UniProtKB Metal binding 22 22 . . . Note=Copper 4 +P0CX81 UniProtKB Metal binding 22 22 . . . Note=Copper 6 +P0CX81 UniProtKB Metal binding 28 28 . . . Note=Copper 2 +P0CX81 UniProtKB Metal binding 28 28 . . . Note=Copper 6 +P0CX81 UniProtKB Metal binding 32 32 . . . Note=Copper 1 +P0CX81 UniProtKB Metal binding 32 32 . . . Note=Copper 7 +P0CX81 UniProtKB Metal binding 34 34 . . . Note=Copper 3 +P0CX81 UniProtKB Metal binding 34 34 . . . Note=Copper 7 +P0CX81 UniProtKB Metal binding 34 34 . . . Note=Copper 8 +P0CX81 UniProtKB Metal binding 38 38 . . . Note=Copper 5 +P0CX81 UniProtKB Metal binding 38 38 . . . Note=Copper 8 +P0CX81 UniProtKB Metal binding 44 44 . . . Note=Copper 4 +P0CX81 UniProtKB Metal binding 44 44 . . . Note=Copper 8 +P0CX81 UniProtKB Metal binding 46 46 . . . Note=Copper 6 +P0CX81 UniProtKB Metal binding 46 46 . . . Note=Copper 7 +P0CX81 UniProtKB Cross-link 30 30 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q02046 1 320 +Q02046 UniProtKB Chain 1 320 . . . ID=PRO_0000199319;Note=Methylenetetrahydrofolate dehydrogenase [NAD(+)] +Q02046 UniProtKB Nucleotide binding 185 186 . . . Note=NAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10933503;Dbxref=PMID:10933503 +Q02046 UniProtKB Nucleotide binding 208 209 . . . Note=NAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10933503;Dbxref=PMID:10933503 +Q02046 UniProtKB Nucleotide binding 274 276 . . . Note=NAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10933503;Dbxref=PMID:10933503 +Q02046 UniProtKB Active site 150 150 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q02046 UniProtKB Helix 10 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Turn 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Beta strand 38 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Helix 48 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Beta strand 67 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Helix 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Helix 79 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Beta strand 94 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Beta strand 101 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Helix 105 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Turn 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Turn 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Beta strand 119 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EE9 +Q02046 UniProtKB Helix 125 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Beta strand 137 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Helix 150 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Turn 174 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Beta strand 179 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Turn 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Helix 190 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Beta strand 203 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Beta strand 209 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Beta strand 227 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Helix 236 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Beta strand 247 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Turn 262 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Beta strand 269 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Beta strand 275 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Helix 282 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Beta strand 288 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +Q02046 UniProtKB Helix 296 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EDZ +##sequence-region Q03151 1 367 +Q03151 UniProtKB Domain 36 228 . . . Note=CP-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01058 +Q03151 UniProtKB Nucleotide binding 89 92 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03151 UniProtKB Nucleotide binding 160 165 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03151 UniProtKB Binding site 224 224 . . . Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P47095 1 244 +P47095 UniProtKB Chain 1 244 . . . ID=PRO_0000162938;Note=Methylthioribulose-1-phosphate dehydratase +P47095 UniProtKB Active site 130 130 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03116 +P47095 UniProtKB Metal binding 107 107 . . . Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03116 +P47095 UniProtKB Metal binding 109 109 . . . Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03116 +P47095 UniProtKB Metal binding 192 192 . . . Note=Zinc%3B via tele nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03116 +P47095 UniProtKB Binding site 89 89 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03116 +##sequence-region Q04149 1 632 +Q04149 UniProtKB Chain 1 632 . . . ID=PRO_0000198861;Note=Crossover junction endonuclease MUS81 +Q04149 UniProtKB Domain 351 448 . . . Note=ERCC4 +Q04149 UniProtKB Region 527 632 . . . Note=Interaction with MMS4 +Q04149 UniProtKB Active site 415 415 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q04149 UniProtKB Mutagenesis 414 415 . . . Note=In allele MUS81-DD%3B abrogates endonuclease activity. DD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12750322;Dbxref=PMID:12750322 +##sequence-region P40959 1 511 +P40959 UniProtKB Chain 1 511 . . . ID=PRO_0000213802;Note=Sorting nexin MVP1 +P40959 UniProtKB Domain 128 247 . . . Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147 +P40959 UniProtKB Binding site 172 172 . . . Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40959 UniProtKB Binding site 174 174 . . . Note=Phosphatidylinositol 3-phosphate%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40959 UniProtKB Binding site 198 198 . . . Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40959 UniProtKB Binding site 213 213 . . . Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40959 UniProtKB Sequence conflict 85 85 . . . Note=Q->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36006 1 1272 +P36006 UniProtKB Chain 1 1272 . . . ID=PRO_0000123490;Note=Myosin-3 +P36006 UniProtKB Domain 36 715 . . . Note=Myosin motor +P36006 UniProtKB Domain 719 739 . . . Note=IQ 1 +P36006 UniProtKB Domain 740 765 . . . Note=IQ 2 +P36006 UniProtKB Domain 771 961 . . . Note=TH1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01093 +P36006 UniProtKB Domain 1120 1182 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P36006 UniProtKB Nucleotide binding 129 136 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36006 UniProtKB Region 404 486 . . . Note=Actin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36006 UniProtKB Compositional bias 1003 1123 . . . Note=Ala/Pro-rich +P36006 UniProtKB Compositional bias 1109 1116 . . . Note=Poly-Pro +P36006 UniProtKB Compositional bias 1259 1271 . . . Note=Asp-rich (acidic) +P36006 UniProtKB Modified residue 357 357 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:9388196;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:9388196 +P36006 UniProtKB Mutagenesis 132 132 . . . Note=Loss of function. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10648569;Dbxref=PMID:10648569 +P36006 UniProtKB Mutagenesis 357 357 . . . Note=Loss of function. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10648569,ECO:0000269|PubMed:9388196;Dbxref=PMID:10648569,PMID:9388196 +P36006 UniProtKB Mutagenesis 357 357 . . . Note=Has a constitutive higher activity in actin assembly. S->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10648569,ECO:0000269|PubMed:9388196;Dbxref=PMID:10648569,PMID:9388196 +P36006 UniProtKB Mutagenesis 1158 1158 . . . Note=Abolishes interaction with LAS17 and causes severe mislocalization of the protein. W->S +P36006 UniProtKB Mutagenesis 1272 1272 . . . Note=Abolishes interaction with ARC40. Missing +P36006 UniProtKB Sequence conflict 95 95 . . . Note=G->RK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36006 UniProtKB Sequence conflict 168 169 . . . Note=NP->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36006 UniProtKB Sequence conflict 263 270 . . . Note=TADTIDDV->SADQLMR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36006 UniProtKB Sequence conflict 917 918 . . . Note=VG->RLV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36006 UniProtKB Sequence conflict 1021 1021 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36006 UniProtKB Beta strand 1123 1129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RUW +P36006 UniProtKB Beta strand 1137 1139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BTT +P36006 UniProtKB Beta strand 1147 1153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RUW +P36006 UniProtKB Beta strand 1157 1163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RUW +P36006 UniProtKB Beta strand 1169 1173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RUW +P36006 UniProtKB Helix 1174 1176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RUW +P36006 UniProtKB Beta strand 1177 1179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RUW +##sequence-region P47018 1 478 +P47018 UniProtKB Chain 1 478 . . . ID=PRO_0000203040;Note=Maintenance of telomere capping protein 1 +P47018 UniProtKB Compositional bias 124 141 . . . Note=Poly-Glu +P47018 UniProtKB Modified residue 273 273 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P47018 UniProtKB Modified residue 436 436 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P53077 1 123 +P53077 UniProtKB Transit peptide 1 37 . . . Note=Mitochondrion +P53077 UniProtKB Chain 38 123 . . . ID=PRO_0000202714;Note=Maintenance of telomere capping protein 3%2C mitochondrial +##sequence-region P53320 1 366 +P53320 UniProtKB Chain 1 366 . . . ID=PRO_0000090697;Note=Mitochondrial carrier protein MTM1 +P53320 UniProtKB Transmembrane 17 36 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53320 UniProtKB Transmembrane 126 146 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53320 UniProtKB Transmembrane 162 182 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53320 UniProtKB Transmembrane 229 249 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53320 UniProtKB Transmembrane 268 286 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53320 UniProtKB Transmembrane 331 352 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53320 UniProtKB Repeat 14 149 . . . Note=Solcar 1 +P53320 UniProtKB Repeat 156 250 . . . Note=Solcar 2 +P53320 UniProtKB Repeat 266 359 . . . Note=Solcar 3 +##sequence-region P32377 1 396 +P32377 UniProtKB Chain 1 396 . . . ID=PRO_0000087015;Note=Diphosphomevalonate decarboxylase +P32377 UniProtKB Sequence conflict 160 160 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32377 UniProtKB Beta strand 4 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Beta strand 13 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Beta strand 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Turn 25 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Beta strand 29 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Beta strand 34 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Turn 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Beta strand 46 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Turn 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Beta strand 67 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Helix 75 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Helix 99 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Beta strand 104 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Helix 120 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Helix 142 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Helix 154 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Beta strand 161 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Beta strand 179 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Helix 186 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Beta strand 192 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Helix 208 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Helix 221 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Helix 229 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Helix 246 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Beta strand 267 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Helix 276 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Beta strand 297 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Beta strand 303 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Beta strand 307 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Helix 313 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Helix 316 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Turn 334 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Helix 339 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Helix 363 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Beta strand 367 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +P32377 UniProtKB Beta strand 389 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FI4 +##sequence-region P23059 1 88 +P23059 UniProtKB Chain 1 88 . . . ID=PRO_0000084554;Note=N-alpha-acetyltransferase 38%2C NatC auxiliary subunit +##sequence-region P32505 1 525 +P32505 UniProtKB Chain 1 525 . . . ID=PRO_0000096687;Note=Nuclear polyadenylated RNA-binding protein NAB2 +P32505 UniProtKB Repeat 121 124 . . . Note=1 +P32505 UniProtKB Repeat 125 128 . . . Note=2 +P32505 UniProtKB Repeat 129 132 . . . Note=3 +P32505 UniProtKB Repeat 133 136 . . . Note=4 +P32505 UniProtKB Repeat 137 140 . . . Note=5 +P32505 UniProtKB Repeat 141 144 . . . Note=6 +P32505 UniProtKB Repeat 145 148 . . . Note=7 +P32505 UniProtKB Repeat 149 152 . . . Note=8 +P32505 UniProtKB Repeat 153 156 . . . Note=9 +P32505 UniProtKB Repeat 157 160 . . . Note=10%3B approximate +P32505 UniProtKB Zinc finger 262 278 . . . Note=C3H1-type 1 +P32505 UniProtKB Zinc finger 283 300 . . . Note=C3H1-type 2 +P32505 UniProtKB Zinc finger 340 355 . . . Note=C3H1-type 3 +P32505 UniProtKB Zinc finger 371 386 . . . Note=C3H1-type 4 +P32505 UniProtKB Zinc finger 415 430 . . . Note=C3H1-type 5 +P32505 UniProtKB Zinc finger 437 452 . . . Note=C3H1-type 6 +P32505 UniProtKB Zinc finger 458 473 . . . Note=C3H1-type 7 +P32505 UniProtKB Region 121 156 . . . Note=10 X 4 AA tandem repeats of Q-Q-Q-P +P32505 UniProtKB Region 209 228 . . . Note=RNA-binding RGG-box;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32505 UniProtKB Compositional bias 97 172 . . . Note=Gln-rich +P32505 UniProtKB Compositional bias 106 116 . . . Note=Poly-Gln +P32505 UniProtKB Natural variant 130 157 . . . Note=In YJA512. Missing +P32505 UniProtKB Helix 7 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V75 +P32505 UniProtKB Helix 28 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V75 +P32505 UniProtKB Helix 45 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V75 +P32505 UniProtKB Helix 61 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V75 +P32505 UniProtKB Helix 84 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V75 +P32505 UniProtKB Turn 269 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ1 +P32505 UniProtKB Turn 293 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ1 +P32505 UniProtKB Beta strand 297 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ1 +P32505 UniProtKB Beta strand 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ1 +P32505 UniProtKB Helix 305 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ1 +P32505 UniProtKB Beta strand 328 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ1 +P32505 UniProtKB Helix 343 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ2 +P32505 UniProtKB Beta strand 353 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ2 +P32505 UniProtKB Helix 374 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ2 +P32505 UniProtKB Beta strand 384 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ2 +P32505 UniProtKB Helix 390 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZJ2 +P32505 UniProtKB Beta strand 412 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5L2L +P32505 UniProtKB Helix 418 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5L2L +P32505 UniProtKB Beta strand 427 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LHN +P32505 UniProtKB Beta strand 433 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5L2L +P32505 UniProtKB Helix 440 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5L2L +P32505 UniProtKB Beta strand 455 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5L2L +P32505 UniProtKB Helix 461 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5L2L +P32505 UniProtKB Beta strand 470 472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LHN +##sequence-region P40314 1 149 +P40314 UniProtKB Chain 1 149 . . . ID=PRO_0000213551;Note=Nascent polypeptide-associated complex subunit beta-2 +P40314 UniProtKB Domain 38 103 . . . Note=NAC-A/B;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00507 +##sequence-region P43619 1 295 +P43619 UniProtKB Chain 1 295 . . . ID=PRO_0000155956;Note=Nicotinate-nucleotide pyrophosphorylase [carboxylating] +P43619 UniProtKB Region 142 144 . . . Note=Substrate binding +P43619 UniProtKB Region 256 258 . . . Note=Substrate binding +P43619 UniProtKB Binding site 107 107 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18321072;Dbxref=PMID:18321072 +P43619 UniProtKB Binding site 166 166 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18321072;Dbxref=PMID:18321072 +P43619 UniProtKB Binding site 176 176 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18321072;Dbxref=PMID:18321072 +P43619 UniProtKB Binding site 206 206 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P43619 UniProtKB Binding site 227 227 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18321072;Dbxref=PMID:18321072 +P43619 UniProtKB Helix 4 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Beta strand 10 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Helix 13 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Helix 31 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Beta strand 40 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Beta strand 49 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Helix 56 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Beta strand 69 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Helix 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Beta strand 85 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Beta strand 90 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Helix 99 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Beta strand 137 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Turn 147 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2V +P43619 UniProtKB Helix 150 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Turn 169 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Beta strand 172 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Helix 177 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Helix 186 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Beta strand 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2O +P43619 UniProtKB Beta strand 203 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Beta strand 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Helix 211 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Beta strand 222 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Beta strand 252 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Beta strand 273 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Helix 278 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +P43619 UniProtKB Turn 281 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2V +P43619 UniProtKB Beta strand 289 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C2E +##sequence-region Q03455 1 724 +Q03455 UniProtKB Chain 1 724 . . . ID=PRO_0000206115;Note=Probable zinc transporter MSC2 +Q03455 UniProtKB Topological domain 1 6 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Topological domain 28 58 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Transmembrane 59 79 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Topological domain 80 90 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Transmembrane 91 111 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Topological domain 112 134 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Transmembrane 135 155 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Topological domain 156 174 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Transmembrane 175 195 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Topological domain 196 219 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Transmembrane 220 240 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Topological domain 241 244 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Transmembrane 245 265 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Topological domain 266 298 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Transmembrane 299 319 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Topological domain 320 386 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Transmembrane 387 407 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Topological domain 408 417 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Transmembrane 418 438 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Topological domain 439 453 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Transmembrane 454 474 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Topological domain 475 491 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Transmembrane 492 512 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Topological domain 513 528 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Transmembrane 529 549 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Topological domain 550 563 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Transmembrane 564 584 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Topological domain 585 724 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03455 UniProtKB Compositional bias 369 379 . . . Note=His-rich +Q03455 UniProtKB Compositional bias 643 661 . . . Note=His-rich +##sequence-region P25847 1 964 +P25847 UniProtKB Chain 1 964 . . . ID=PRO_0000115191;Note=DNA mismatch repair protein MSH2 +P25847 UniProtKB Nucleotide binding 688 695 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25847 UniProtKB Region 851 964 . . . Note=Interaction with MSH6 +P25847 UniProtKB Mutagenesis 42 42 . . . Note=Moderately reduced activity in a mismatch repair assay. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390 +P25847 UniProtKB Mutagenesis 65 65 . . . Note=Defective in a mismatch repair assay. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390 +P25847 UniProtKB Mutagenesis 317 317 . . . Note=Partially defective in a mismatch repair assay. G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10469597,ECO:0000269|PubMed:11555625;Dbxref=PMID:10469597,PMID:11555625 +P25847 UniProtKB Mutagenesis 402 402 . . . Note=Partially defective in a mismatch repair assay. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10469597;Dbxref=PMID:10469597 +P25847 UniProtKB Mutagenesis 430 430 . . . Note=Partially defective in a mismatch repair assay. Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10469597;Dbxref=PMID:10469597 +P25847 UniProtKB Mutagenesis 518 518 . . . Note=Defective in MMR%2C but not in NHTR. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644 +P25847 UniProtKB Mutagenesis 524 524 . . . Note=Partially defective in a mismatch repair assay. D->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10469597;Dbxref=PMID:10469597 +P25847 UniProtKB Mutagenesis 542 542 . . . Note=Defective in a mismatch repair assay. R->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10469597;Dbxref=PMID:10469597 +P25847 UniProtKB Mutagenesis 561 561 . . . Note=Causes strong defects in MutS alpha mismatch binding. Defective in MMR%2C but not in NHTR. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12875840;Dbxref=PMID:12875840 +P25847 UniProtKB Mutagenesis 564 564 . . . Note=Causes strong defects in MutS alpha mismatch binding. Defective in MMR%2C but not in NHTR. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12875840;Dbxref=PMID:12875840 +P25847 UniProtKB Mutagenesis 566 566 . . . Note=Defective in MMR%2C but not in NHTR. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12875840;Dbxref=PMID:12875840 +P25847 UniProtKB Mutagenesis 574 574 . . . Note=Defective in MMR and in NHTR. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644 +P25847 UniProtKB Mutagenesis 584 584 . . . Note=Defective in MMR and in NHTR. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644 +P25847 UniProtKB Mutagenesis 640 640 . . . Note=Defective in a mismatch repair assay. P->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10469597,ECO:0000269|PubMed:11555625;Dbxref=PMID:10469597,PMID:11555625 +P25847 UniProtKB Mutagenesis 656 656 . . . Note=Causes defects in ATP-dependent dissociation of MutS alpha from mismatch DNA and in interactions between MutS alpha and MutL alpha. Defective in MMR%2C but not in NHTR. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12875840;Dbxref=PMID:12875840 +P25847 UniProtKB Mutagenesis 658 658 . . . Note=Fully functional in a mismatch repair assay. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11555625;Dbxref=PMID:11555625 +P25847 UniProtKB Mutagenesis 688 688 . . . Note=Moderately reduced activity in a mismatch repair assay. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10077621;Dbxref=PMID:10077621 +P25847 UniProtKB Mutagenesis 693 693 . . . Note=Has a dominant negative mutator effect. G->A%2CS;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10077621,ECO:0000269|PubMed:9819445;Dbxref=PMID:10077621,PMID:9819445 +P25847 UniProtKB Mutagenesis 693 693 . . . Note=Has no defect in mismatch DNA binding%2C but lacks ATP-induced conformational change. Defective in MMR and in NHTR. G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10077621,ECO:0000269|PubMed:9819445;Dbxref=PMID:10077621,PMID:9819445 +P25847 UniProtKB Mutagenesis 694 694 . . . Note=Impairs ATP binding%3B reduces catalytic activity 1.6-fold for ATP hydrolysis. Has a dominant negative mutator effect. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10077621,ECO:0000269|PubMed:16214425,ECO:0000269|PubMed:16600868;Dbxref=PMID:10077621,PMID:16214425,PMID:16600868 +P25847 UniProtKB Mutagenesis 694 694 . . . Note=Defective in MMR and in NHTR. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10077621,ECO:0000269|PubMed:16214425,ECO:0000269|PubMed:16600868;Dbxref=PMID:10077621,PMID:16214425,PMID:16600868 +P25847 UniProtKB Mutagenesis 695 695 . . . Note=Has a dominant negative mutator effect. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10077621;Dbxref=PMID:10077621 +P25847 UniProtKB Mutagenesis 716 716 . . . Note=Defective in a mismatch repair assay. C->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10469597;Dbxref=PMID:10469597 +P25847 UniProtKB Mutagenesis 730 730 . . . Note=Disruptes MutS alpha ATPase activity%2C but does not affect ATP binding or interactions with MutL alpha. Defective in MMR%2C but not in NHTR. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12875840;Dbxref=PMID:12875840 +P25847 UniProtKB Mutagenesis 742 742 . . . Note=Defective in MMR%2C but not in NHTR. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644 +P25847 UniProtKB Mutagenesis 742 742 . . . Note=Defective in MMR and in NHTR. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644 +P25847 UniProtKB Mutagenesis 768 768 . . . Note=Reduces catalytic activity 50-fold for ATP hydrolysis. E->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12509278,ECO:0000269|PubMed:15513922,ECO:0000269|PubMed:16214425;Dbxref=PMID:12509278,PMID:15513922,PMID:16214425 +P25847 UniProtKB Mutagenesis 773 773 . . . Note=Defective in MMR and in NHTR. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644 +P25847 UniProtKB Mutagenesis 855 855 . . . Note=Defective in MMR%2C but not in NHTR. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644 +P25847 UniProtKB Mutagenesis 859 859 . . . Note=Defective in MMR%2C but not in NHTR. A->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644 +P25847 UniProtKB Mutagenesis 862 862 . . . Note=Defective in MMR%2C but not in NHTR. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644 +P25847 UniProtKB Mutagenesis 863 868 . . . Note=Defective in MMR and in NHTR. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523644;Dbxref=PMID:10523644 +P25847 UniProtKB Sequence conflict 957 964 . . . Note=KYIKALLL->EIYKSPCCYN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P28737 1 362 +P28737 UniProtKB Chain 1 362 . . . ID=PRO_0000084757;Note=Protein MSP1 +P28737 UniProtKB Topological domain 1 12 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28737 UniProtKB Transmembrane 13 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28737 UniProtKB Topological domain 29 362 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28737 UniProtKB Nucleotide binding 133 140 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53176 1 234 +P53176 UniProtKB Chain 1 234 . . . ID=PRO_0000207525;Note=Multicopy suppressor of SEC21 protein 27 +P53176 UniProtKB Topological domain 1 47 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53176 UniProtKB Transmembrane 48 68 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53176 UniProtKB Topological domain 69 72 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53176 UniProtKB Transmembrane 73 93 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53176 UniProtKB Topological domain 94 234 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53176 UniProtKB Region 231 234 . . . Note=COPI binding +P53176 UniProtKB Modified residue 3 3 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P39552 +P53176 UniProtKB Mutagenesis 231 232 . . . Note=Abolishes binding to COPI coatomer complex. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12925749;Dbxref=PMID:12925749 +##sequence-region Q03920 1 221 +Q03920 UniProtKB Chain 1 221 . . . ID=PRO_0000245840;Note=eRF1 methyltransferase catalytic subunit MTQ2 +Q03920 UniProtKB Region 50 54 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03920 UniProtKB Region 122 125 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03920 UniProtKB Binding site 77 77 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03920 UniProtKB Binding site 122 122 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P48240 1 250 +P48240 UniProtKB Chain 1 250 . . . ID=PRO_0000139979;Note=Exosome complex component MTR3 +P48240 UniProtKB Compositional bias 216 222 . . . Note=Asp/Glu-rich (acidic) +P48240 UniProtKB Beta strand 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +P48240 UniProtKB Beta strand 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36 +P48240 UniProtKB Beta strand 45 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P48240 UniProtKB Beta strand 56 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P48240 UniProtKB Beta strand 69 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P48240 UniProtKB Beta strand 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P48240 UniProtKB Beta strand 89 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P48240 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36 +P48240 UniProtKB Helix 107 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P48240 UniProtKB Helix 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P48240 UniProtKB Beta strand 133 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P48240 UniProtKB Helix 165 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P48240 UniProtKB Beta strand 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P48240 UniProtKB Beta strand 192 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P48240 UniProtKB Beta strand 199 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P48240 UniProtKB Helix 205 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P48240 UniProtKB Beta strand 209 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P48240 UniProtKB Helix 223 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +##sequence-region Q12093 1 417 +Q12093 UniProtKB Chain 1 417 . . . ID=PRO_0000121711;Note=Mitochondrial tRNA-specific 2-thiouridylase 1 +Q12093 UniProtKB Nucleotide binding 32 39 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12093 UniProtKB Region 122 124 . . . Note=Interaction with target base in tRNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12093 UniProtKB Region 179 181 . . . Note=Interaction with tRNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12093 UniProtKB Region 354 355 . . . Note=Interaction with tRNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12093 UniProtKB Active site 127 127 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12093 UniProtKB Active site 229 229 . . . Note=Cysteine persulfide intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12093 UniProtKB Binding site 58 58 . . . Note=ATP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12093 UniProtKB Binding site 154 154 . . . Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12093 UniProtKB Site 155 155 . . . Note=Interaction with tRNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12093 UniProtKB Site 281 281 . . . Note=Interaction with tRNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12093 UniProtKB Site 391 391 . . . Note=Interaction with tRNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12093 UniProtKB Disulfide bond 127 229 . . . Note=Alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12093 UniProtKB Mutagenesis 38 38 . . . Note=Loss of activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15509579;Dbxref=PMID:15509579 +##sequence-region P36084 1 527 +P36084 UniProtKB Chain 1 527 . . . ID=PRO_0000081654;Note=Splicing factor MUD2 +P36084 UniProtKB Domain 424 511 . . . Note=RRM +P36084 UniProtKB Modified residue 49 49 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P36084 UniProtKB Sequence conflict 98 98 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32335 1 436 +P32335 UniProtKB Transit peptide 1 26 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32335 UniProtKB Chain 27 436 . . . ID=PRO_0000096603;Note=Protein MSS51%2C mitochondrial +P32335 UniProtKB Mutagenesis 167 167 . . . Note=Partially suppresses the respiratory defect of SHY1 mutants by increasing COX1 translation. T->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11782424;Dbxref=PMID:11782424 +P32335 UniProtKB Mutagenesis 199 199 . . . Note=Partially suppresses the respiratory defect of SHY1 mutants by increasing COX1 translation. F->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11782424;Dbxref=PMID:11782424 +P32335 UniProtKB Sequence conflict 210 210 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32335 UniProtKB Sequence conflict 210 210 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39552 1 234 +P39552 UniProtKB Chain 1 234 . . . ID=PRO_0000207526;Note=Multicopy suppressor of SEC21 protein 28 +P39552 UniProtKB Topological domain 1 47 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39552 UniProtKB Transmembrane 48 68 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39552 UniProtKB Topological domain 69 72 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39552 UniProtKB Transmembrane 73 93 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39552 UniProtKB Topological domain 94 234 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39552 UniProtKB Region 231 234 . . . Note=COPI binding +P39552 UniProtKB Modified residue 3 3 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P0CY08 1 210 +P0CY08 UniProtKB Chain 1 210 . . . ID=PRO_0000049186;Note=Mating-type protein ALPHA2 +P0CY08 UniProtKB DNA binding 129 191 . . . Note=Homeobox%3B TALE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00108 +P0CY08 UniProtKB Region 1 102 . . . Note=N-terminal domain +P0CY08 UniProtKB Region 103 128 . . . Note=Flexible linker +P0CY08 UniProtKB Region 190 210 . . . Note=C-terminal tail +P0CY08 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20110468;Dbxref=PMID:20110468 +P0CY08 UniProtKB Mutagenesis 4 4 . . . Note=Reduces the ability of ALPHA2 to repress transcription%2C but binds normally to DNA and MCM1. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7995523;Dbxref=PMID:7995523 +P0CY08 UniProtKB Mutagenesis 9 9 . . . Note=Reduces the ability of ALPHA2 to repress transcription%2C but binds normally to DNA and MCM1. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7995523;Dbxref=PMID:7995523 +P0CY08 UniProtKB Mutagenesis 10 10 . . . Note=Reduces the ability of ALPHA2 to repress transcription%2C but binds normally to DNA and MCM1. Disrupts interaction with TUP1. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7995523;Dbxref=PMID:7995523 +P0CY08 UniProtKB Mutagenesis 71 71 . . . Note=Reduces the ability of alpha2 to repress transcription%2C but binds normally to DNA and MCM1. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7995523;Dbxref=PMID:7995523 +P0CY08 UniProtKB Mutagenesis 114 114 . . . Note=Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2887035;Dbxref=PMID:2887035 +P0CY08 UniProtKB Mutagenesis 115 115 . . . Note=Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2887035;Dbxref=PMID:2887035 +P0CY08 UniProtKB Mutagenesis 116 116 . . . Note=Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2887035;Dbxref=PMID:2887035 +P0CY08 UniProtKB Mutagenesis 117 117 . . . Note=Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2887035;Dbxref=PMID:2887035 +P0CY08 UniProtKB Mutagenesis 118 118 . . . Note=Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2887035;Dbxref=PMID:2887035 +P0CY08 UniProtKB Mutagenesis 119 119 . . . Note=Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2887035;Dbxref=PMID:2887035 +P0CY08 UniProtKB Mutagenesis 120 120 . . . Note=Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2887035;Dbxref=PMID:2887035 +P0CY08 UniProtKB Mutagenesis 173 173 . . . Note=Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. Disrupts interaction with SSN6. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10759558;Dbxref=PMID:10759558 +P0CY08 UniProtKB Mutagenesis 181 181 . . . Note=In ALPHA2-3A%3B defective in binding DNA alone or in complex with MCM1%2C but binds DNA normally in complex with A1%3B when associated with A-182 and A-185. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12121651;Dbxref=PMID:12121651 +P0CY08 UniProtKB Mutagenesis 182 182 . . . Note=In ALPHA2-3A%3B defective in binding DNA alone or in complex with MCM1%2C but binds DNA normally in complex with A1%3B when associated with A-181 and A-185. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12121651;Dbxref=PMID:12121651 +P0CY08 UniProtKB Mutagenesis 185 185 . . . Note=In ALPHA2-3A%3B defective in binding DNA alone or in complex with MCM1%2C but binds DNA normally in complex with A1%3B when associated with A-181 and A-182. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12121651;Dbxref=PMID:12121651 +P0CY08 UniProtKB Mutagenesis 192 192 . . . Note=Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7569974;Dbxref=PMID:7569974 +P0CY08 UniProtKB Mutagenesis 196 196 . . . Note=Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. L->A%2CS;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2851482,ECO:0000269|PubMed:7569974;Dbxref=PMID:2851482,PMID:7569974 +P0CY08 UniProtKB Mutagenesis 199 199 . . . Note=Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7569974;Dbxref=PMID:7569974 +P0CY08 UniProtKB Mutagenesis 200 200 . . . Note=Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7569974;Dbxref=PMID:7569974 +P0CY08 UniProtKB Sequence conflict 56 56 . . . Note=G->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0CY08 UniProtKB Sequence conflict 150 150 . . . Note=K->KK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0CY08 UniProtKB Sequence conflict 154 154 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0CY08 UniProtKB Beta strand 116 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNM +P0CY08 UniProtKB Beta strand 125 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNM +P0CY08 UniProtKB Helix 138 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K61 +P0CY08 UniProtKB Turn 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K61 +P0CY08 UniProtKB Helix 159 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K61 +P0CY08 UniProtKB Helix 173 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K61 +P0CY08 UniProtKB Helix 194 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LE8 +P0CY08 UniProtKB Beta strand 200 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1LE8 +##sequence-region P34246 1 357 +P34246 UniProtKB Chain 1 357 . . . ID=PRO_0000203161;Note=Maintenance of telomere capping protein 2 +##sequence-region P38335 1 694 +P38335 UniProtKB Chain 1 694 . . . ID=PRO_0000202525;Note=Maintenance of telomere capping protein 4 +P38335 UniProtKB Transmembrane 655 675 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38335 UniProtKB Compositional bias 226 240 . . . Note=His-rich +P38335 UniProtKB Compositional bias 268 275 . . . Note=Poly-Asn +P38335 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38335 UniProtKB Modified residue 263 263 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38335 UniProtKB Modified residue 481 481 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38335 UniProtKB Modified residue 491 491 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38335 UniProtKB Modified residue 493 493 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P32633 1 139 +P32633 UniProtKB Chain 1 139 . . . ID=PRO_0000202608;Note=Maintenance of telomere capping protein 7 +P32633 UniProtKB Transmembrane 13 33 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32633 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P46151 1 657 +P46151 UniProtKB Chain 1 657 . . . ID=PRO_0000190255;Note=Methylenetetrahydrofolate reductase 1 +P46151 UniProtKB Nucleotide binding 18 23 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46151 UniProtKB Nucleotide binding 49 50 . . . Note=NAD and FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46151 UniProtKB Nucleotide binding 108 110 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46151 UniProtKB Nucleotide binding 129 130 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46151 UniProtKB Active site 18 18 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46151 UniProtKB Binding site 78 78 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46151 UniProtKB Binding site 110 110 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46151 UniProtKB Binding site 152 152 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46151 UniProtKB Binding site 171 171 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46151 UniProtKB Binding site 178 178 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46151 UniProtKB Binding site 189 189 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46151 UniProtKB Binding site 286 286 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46151 UniProtKB Modified residue 120 120 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P46151 UniProtKB Modified residue 301 301 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P46151 UniProtKB Modified residue 358 358 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46151 UniProtKB Sequence conflict 110 111 . . . Note=DP->NL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46151 UniProtKB Sequence conflict 115 116 . . . Note=ED->VV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46151 UniProtKB Sequence conflict 119 119 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46151 UniProtKB Sequence conflict 124 131 . . . Note=ESPFKYAV->RLLNMRLF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53128 1 600 +P53128 UniProtKB Chain 1 600 . . . ID=PRO_0000190256;Note=Methylenetetrahydrofolate reductase 2 +P53128 UniProtKB Nucleotide binding 22 27 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53128 UniProtKB Nucleotide binding 54 55 . . . Note=NAD and FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53128 UniProtKB Nucleotide binding 114 116 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53128 UniProtKB Nucleotide binding 133 134 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53128 UniProtKB Active site 22 22 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53128 UniProtKB Binding site 84 84 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53128 UniProtKB Binding site 116 116 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53128 UniProtKB Binding site 156 156 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53128 UniProtKB Binding site 171 171 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53128 UniProtKB Binding site 178 178 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53128 UniProtKB Binding site 189 189 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53128 UniProtKB Binding site 282 282 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53128 UniProtKB Sequence conflict 41 42 . . . Note=RM->LA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53128 UniProtKB Sequence conflict 48 48 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53128 UniProtKB Sequence conflict 73 73 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53128 UniProtKB Sequence conflict 152 154 . . . Note=GVA->RC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53128 UniProtKB Sequence conflict 183 183 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53128 UniProtKB Sequence conflict 211 211 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53128 UniProtKB Sequence conflict 233 243 . . . Note=GQISIPQHFSS->ANLHPSTFLV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53128 UniProtKB Sequence conflict 266 276 . . . Note=MCQKLLDSGYV->CVKIARQWLR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06489 1 411 +Q06489 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q06489 UniProtKB Chain 2 411 . . . ID=PRO_0000156110;Note=Methylthioribose-1-phosphate isomerase +Q06489 UniProtKB Active site 280 280 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03119 +Q06489 UniProtKB Site 181 181 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03119 +Q06489 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q06489 UniProtKB Modified residue 351 351 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06489 UniProtKB Beta strand 5 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Beta strand 17 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Turn 23 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Beta strand 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Helix 38 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Helix 53 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Helix 79 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Helix 88 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Helix 111 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Helix 129 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Beta strand 173 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Helix 185 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Beta strand 188 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Helix 194 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Beta strand 223 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Turn 233 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Helix 237 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Helix 242 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Beta strand 253 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Helix 258 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Helix 261 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Beta strand 272 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Beta strand 280 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Beta strand 288 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Helix 294 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Beta strand 307 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Helix 314 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Helix 324 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Helix 335 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Beta strand 339 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Turn 347 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Beta strand 362 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Beta strand 377 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Helix 384 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Beta strand 388 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Beta strand 395 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +Q06489 UniProtKB Helix 408 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W2W +##sequence-region Q06106 1 887 +Q06106 UniProtKB Chain 1 887 . . . ID=PRO_0000081647;Note=Multiple RNA-binding domain-containing protein 1 +Q06106 UniProtKB Domain 2 94 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q06106 UniProtKB Domain 345 423 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q06106 UniProtKB Domain 532 604 . . . Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q06106 UniProtKB Domain 663 746 . . . Note=RRM 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q06106 UniProtKB Domain 763 840 . . . Note=RRM 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q06106 UniProtKB Modified residue 220 220 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06106 UniProtKB Modified residue 264 264 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +##sequence-region Q12117 1 320 +Q12117 UniProtKB Chain 1 320 . . . ID=PRO_0000196285;Note=Protein MRH1 +Q12117 UniProtKB Topological domain 1 34 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12117 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12117 UniProtKB Topological domain 56 62 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12117 UniProtKB Transmembrane 63 83 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12117 UniProtKB Topological domain 84 116 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12117 UniProtKB Transmembrane 117 137 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12117 UniProtKB Topological domain 138 141 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12117 UniProtKB Transmembrane 142 162 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12117 UniProtKB Topological domain 163 167 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12117 UniProtKB Transmembrane 168 188 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12117 UniProtKB Topological domain 189 204 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12117 UniProtKB Transmembrane 205 225 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12117 UniProtKB Topological domain 226 238 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12117 UniProtKB Transmembrane 239 259 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12117 UniProtKB Topological domain 260 320 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12117 UniProtKB Compositional bias 300 318 . . . Note=Lys-rich +Q12117 UniProtKB Modified residue 289 289 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:17761666,PMID:18407956,PMID:19779198 +Q12117 UniProtKB Modified residue 295 295 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:17761666,PMID:18407956,PMID:19779198 +Q12117 UniProtKB Modified residue 299 299 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +##sequence-region P50873 1 501 +P50873 UniProtKB Chain 1 501 . . . ID=PRO_0000086399;Note=Serine/threonine-protein kinase MRK1 +P50873 UniProtKB Domain 164 447 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P50873 UniProtKB Nucleotide binding 170 178 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P50873 UniProtKB Active site 289 289 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P50873 UniProtKB Binding site 193 193 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P50873 UniProtKB Modified residue 13 13 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P35719 1 219 +P35719 UniProtKB Chain 1 219 . . . ID=PRO_0000087699;Note=Uncharacterized protein MRP8 +P35719 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35719 UniProtKB Cross-link 137 137 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15166219;Dbxref=PMID:15166219 +##sequence-region P47007 1 382 +P47007 UniProtKB Transit peptide 1 12 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47007 UniProtKB Chain 13 382 . . . ID=PRO_0000203032;Note=MIOREX complex component 5 +##sequence-region Q07349 1 420 +Q07349 UniProtKB Chain 1 420 . . . ID=PRO_0000202592;Note=MIOREX complex component 9 +Q07349 UniProtKB Transmembrane 125 145 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07349 UniProtKB Transmembrane 149 169 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P13712 1 422 +P13712 UniProtKB Chain 1 422 . . . ID=PRO_0000051086;Note=Chromatin assembly factor 1 subunit p50 +P13712 UniProtKB Repeat 127 158 . . . Note=WD 1 +P13712 UniProtKB Repeat 198 238 . . . Note=WD 2 +P13712 UniProtKB Repeat 249 289 . . . Note=WD 3 +P13712 UniProtKB Repeat 294 334 . . . Note=WD 4 +P13712 UniProtKB Repeat 338 379 . . . Note=WD 5 +P13712 UniProtKB Repeat 382 421 . . . Note=WD 6 +##sequence-region Q03162 1 620 +Q03162 UniProtKB Chain 1 620 . . . ID=PRO_0000218323;Note=MYND-type zinc finger protein MUB1 +Q03162 UniProtKB Zinc finger 514 555 . . . Note=MYND-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00134 +##sequence-region P50276 1 574 +P50276 UniProtKB Chain 1 574 . . . ID=PRO_0000096648;Note=High-affinity methionine permease +P50276 UniProtKB Topological domain 1 61 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Transmembrane 62 82 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Topological domain 83 92 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Transmembrane 93 113 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Topological domain 114 140 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Transmembrane 141 161 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Topological domain 162 182 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Transmembrane 183 203 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Topological domain 204 207 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Transmembrane 208 228 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Topological domain 229 293 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Transmembrane 294 314 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Topological domain 315 340 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Transmembrane 341 361 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Topological domain 362 418 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Transmembrane 419 439 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Topological domain 440 455 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Transmembrane 456 476 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Topological domain 477 490 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Transmembrane 491 511 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Topological domain 512 574 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50276 UniProtKB Modified residue 552 552 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P50276 UniProtKB Modified residue 573 573 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P50276 UniProtKB Cross-link 28 28 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P38994 1 779 +P38994 UniProtKB Chain 1 779 . . . ID=PRO_0000185455;Note=Probable phosphatidylinositol 4-phosphate 5-kinase MSS4 +P38994 UniProtKB Domain 376 756 . . . Note=PIPK;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00781 +P38994 UniProtKB Modified residue 207 207 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38994 UniProtKB Modified residue 222 222 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38994 UniProtKB Modified residue 225 225 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38994 UniProtKB Modified residue 659 659 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38994 UniProtKB Modified residue 661 661 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38994 UniProtKB Sequence conflict 610 610 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03429 1 123 +Q03429 UniProtKB Transit peptide 1 24 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03429 UniProtKB Chain 25 123 . . . ID=PRO_0000253826;Note=Mitochondrial zinc maintenance protein 1%2C mitochondrial +##sequence-region Q02642 1 157 +Q02642 UniProtKB Chain 1 157 . . . ID=PRO_0000213552;Note=Nascent polypeptide-associated complex subunit beta-1 +Q02642 UniProtKB Domain 38 103 . . . Note=NAC-A/B;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00507 +Q02642 UniProtKB Modified residue 151 151 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region Q99316 1 277 +Q99316 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99316 UniProtKB Chain 23 277 . . . ID=PRO_0000034182;Note=Protein disulfide isomerase MPD2 +Q99316 UniProtKB Domain 27 172 . . . Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +Q99316 UniProtKB Motif 274 277 . . . Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10138 +Q99316 UniProtKB Disulfide bond 56 59 . . . Note=Redox-active;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +Q99316 UniProtKB Mutagenesis 56 56 . . . Note=Loss of function%3B when associated with S-59. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9367834;Dbxref=PMID:9367834 +Q99316 UniProtKB Mutagenesis 59 59 . . . Note=Loss of function%3B when associated with S-56. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9367834;Dbxref=PMID:9367834 +##sequence-region Q06390 1 306 +Q06390 UniProtKB Chain 1 306 . . . ID=PRO_0000253821;Note=Methylated RNA-binding protein 1 +Q06390 UniProtKB Domain 155 290 . . . Note=YTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00225 +Q06390 UniProtKB Region 161 163 . . . Note=N6-methyladenosine binding;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:4RCM,ECO:0000269|PubMed:26318451;Dbxref=PMID:26318451 +Q06390 UniProtKB Binding site 207 207 . . . Note=N6-methyladenosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y5A9 +Q06390 UniProtKB Binding site 231 231 . . . Note=N6-methyladenosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9BYJ9 +Q06390 UniProtKB Mutagenesis 177 177 . . . Note=Abolishes binding to N6-methyladenosine (m6A)-containing RNAs. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26318451;Dbxref=PMID:26318451 +Q06390 UniProtKB Mutagenesis 231 231 . . . Note=Abolishes binding to N6-methyladenosine (m6A)-containing RNAs. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26318451;Dbxref=PMID:26318451 +Q06390 UniProtKB Mutagenesis 273 273 . . . Note=Abolishes binding to N6-methyladenosine (m6A)-containing RNAs. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26318451;Dbxref=PMID:26318451 +Q06390 UniProtKB Beta strand 156 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM +Q06390 UniProtKB Helix 165 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM +Q06390 UniProtKB Helix 181 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM +Q06390 UniProtKB Beta strand 200 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM +Q06390 UniProtKB Turn 207 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM +Q06390 UniProtKB Beta strand 211 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM +Q06390 UniProtKB Beta strand 223 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM +Q06390 UniProtKB Helix 228 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM +Q06390 UniProtKB Helix 234 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM +Q06390 UniProtKB Beta strand 240 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM +Q06390 UniProtKB Helix 253 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM +Q06390 UniProtKB Turn 262 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM +Q06390 UniProtKB Helix 269 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM +Q06390 UniProtKB Helix 280 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RCM +##sequence-region P25588 1 1096 +P25588 UniProtKB Chain 1 1096 . . . ID=PRO_0000096574;Note=Mediator of replication checkpoint protein 1 +P25588 UniProtKB Coiled coil 488 542 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25588 UniProtKB Coiled coil 652 716 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25588 UniProtKB Modified residue 144 144 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25588 UniProtKB Modified residue 409 409 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25588 UniProtKB Modified residue 411 411 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25588 UniProtKB Modified residue 434 434 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25588 UniProtKB Modified residue 605 605 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198 +P25588 UniProtKB Modified residue 607 607 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P25588 UniProtKB Modified residue 609 609 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P25588 UniProtKB Modified residue 801 801 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25588 UniProtKB Modified residue 807 807 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25588 UniProtKB Modified residue 911 911 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25588 UniProtKB Sequence conflict 748 748 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25588 UniProtKB Sequence conflict 808 808 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06815 1 381 +Q06815 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06815 UniProtKB Chain 24 381 . . . ID=PRO_0000042715;Note=Mannose 6-phosphate receptor-like protein 1 +Q06815 UniProtKB Topological domain 24 236 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06815 UniProtKB Transmembrane 237 257 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06815 UniProtKB Topological domain 258 381 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06815 UniProtKB Modified residue 335 335 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q06815 UniProtKB Modified residue 339 339 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q06815 UniProtKB Modified residue 342 342 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q06815 UniProtKB Modified residue 371 371 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06815 UniProtKB Modified residue 380 380 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06815 UniProtKB Glycosylation 116 116 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06815 UniProtKB Glycosylation 136 136 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06815 UniProtKB Glycosylation 178 178 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06815 UniProtKB Glycosylation 215 215 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P25270 1 412 +P25270 UniProtKB Transit peptide 1 20 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25270 UniProtKB Chain 21 412 . . . ID=PRO_0000058321;Note=rRNA methyltransferase 1%2C mitochondrial +##sequence-region P53123 1 320 +P53123 UniProtKB Transit peptide 1 18 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53123 UniProtKB Chain 19 320 . . . ID=PRO_0000155588;Note=rRNA methyltransferase 2%2C mitochondrial +P53123 UniProtKB Region 83 86 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UI43 +P53123 UniProtKB Region 178 179 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UI43 +P53123 UniProtKB Active site 264 264 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0C0R7 +P53123 UniProtKB Binding site 104 104 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UI43 +P53123 UniProtKB Binding site 203 203 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UI43 +##sequence-region O75012 1 95 +O75012 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9151978;Dbxref=PMID:9151978 +O75012 UniProtKB Chain 2 95 . . . ID=PRO_0000042818;Note=37S ribosomal protein MRP10%2C mitochondrial +O75012 UniProtKB Domain 27 69 . . . Note=CHCH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +O75012 UniProtKB Motif 30 40 . . . Note=Cx9C motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +O75012 UniProtKB Motif 51 61 . . . Note=Cx9C motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +O75012 UniProtKB Disulfide bond 30 61 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +O75012 UniProtKB Disulfide bond 40 51 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01150 +##sequence-region P10566 1 314 +P10566 UniProtKB Chain 1 314 . . . ID=PRO_0000090691;Note=Mitochondrial RNA-splicing protein MRS3 +P10566 UniProtKB Transmembrane 33 52 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10566 UniProtKB Transmembrane 93 112 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10566 UniProtKB Transmembrane 130 149 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10566 UniProtKB Transmembrane 185 204 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10566 UniProtKB Transmembrane 219 238 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10566 UniProtKB Transmembrane 285 298 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10566 UniProtKB Repeat 31 118 . . . Note=Solcar 1 +P10566 UniProtKB Repeat 128 210 . . . Note=Solcar 2 +P10566 UniProtKB Repeat 217 310 . . . Note=Solcar 3 +##sequence-region Q03079 1 207 +Q03079 UniProtKB Transit peptide 1 46 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03079 UniProtKB Chain 47 207 . . . ID=PRO_0000238638;Note=MIOREX complex component 11 +Q03079 UniProtKB Topological domain 47 98 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q03079 UniProtKB Transmembrane 99 119 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03079 UniProtKB Topological domain 120 177 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q03079 UniProtKB Transmembrane 178 198 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03079 UniProtKB Topological domain 199 207 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +Q03079 UniProtKB Sequence conflict 108 112 . . . Note=ILPLF->NTTTV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38172 1 270 +P38172 UniProtKB Transit peptide 1 12 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38172 UniProtKB Chain 13 270 . . . ID=PRO_0000202441;Note=MIOREX complex component 3 +##sequence-region P36157 1 363 +P36157 UniProtKB Chain 1 363 . . . ID=PRO_0000203223;Note=Putative transcriptional activator MSA2 +P36157 UniProtKB Modified residue 157 157 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36157 UniProtKB Modified residue 292 292 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36157 UniProtKB Sequence conflict 122 122 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32334 1 1306 +P32334 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32334 UniProtKB Chain 22 1306 . . . ID=PRO_0000096589;Note=Signaling mucin MSB2 +P32334 UniProtKB Topological domain 22 1185 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32334 UniProtKB Transmembrane 1186 1206 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32334 UniProtKB Topological domain 1207 1306 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32334 UniProtKB Repeat 698 714 . . . Note=1 +P32334 UniProtKB Repeat 715 731 . . . Note=2 +P32334 UniProtKB Repeat 732 748 . . . Note=3 +P32334 UniProtKB Repeat 749 765 . . . Note=4 +P32334 UniProtKB Repeat 766 782 . . . Note=5 +P32334 UniProtKB Repeat 783 799 . . . Note=6 +P32334 UniProtKB Repeat 800 816 . . . Note=7 +P32334 UniProtKB Region 698 816 . . . Note=7 X 17 AA tandem repeats +P32334 UniProtKB Compositional bias 37 956 . . . Note=Ser-rich +P32334 UniProtKB Compositional bias 1132 1150 . . . Note=Poly-Ser +P32334 UniProtKB Modified residue 1300 1300 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32334 UniProtKB Glycosylation 30 30 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32334 UniProtKB Glycosylation 859 859 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32334 UniProtKB Glycosylation 885 885 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32334 UniProtKB Glycosylation 945 945 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32334 UniProtKB Glycosylation 1049 1049 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32334 UniProtKB Glycosylation 1088 1088 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32334 UniProtKB Glycosylation 1175 1175 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38694 1 644 +P38694 UniProtKB Chain 1 644 . . . ID=PRO_0000056596;Note=Putative aldehyde dehydrogenase-like protein YHR039C +P38694 UniProtKB Active site 354 354 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008 +P38694 UniProtKB Active site 389 389 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008 +P38694 UniProtKB Site 248 248 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38694 UniProtKB Glycosylation 15 15 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38694 UniProtKB Glycosylation 565 565 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38694 UniProtKB Glycosylation 627 627 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P10849 1 440 +P10849 UniProtKB Transit peptide 1 15 . . . Note=Mitochondrion +P10849 UniProtKB Chain 16 440 . . . ID=PRO_0000021790;Note=Mitochondrial transcription factor 2 +##sequence-region P38860 1 518 +P38860 UniProtKB Transit peptide 1 23 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38860 UniProtKB Chain 24 518 . . . ID=PRO_0000122468;Note=GTPase MTG2%2C mitochondrial +P38860 UniProtKB Domain 340 512 . . . Note=OBG-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +P38860 UniProtKB Nucleotide binding 346 353 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +P38860 UniProtKB Nucleotide binding 394 398 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +P38860 UniProtKB Nucleotide binding 460 463 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +##sequence-region P35198 1 433 +P35198 UniProtKB Chain 1 433 . . . ID=PRO_0000096625;Note=Protein MTH1 +##sequence-region Q03677 1 179 +Q03677 UniProtKB Chain 1 179 . . . ID=PRO_0000162946;Note=1%2C2-dihydroxy-3-keto-5-methylthiopentene dioxygenase +Q03677 UniProtKB Metal binding 85 85 . . . Note=Iron or nickel;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03154 +Q03677 UniProtKB Metal binding 87 87 . . . Note=Iron or nickel;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03154 +Q03677 UniProtKB Metal binding 91 91 . . . Note=Iron or nickel;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03154 +Q03677 UniProtKB Metal binding 132 132 . . . Note=Iron or nickel;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03154 +Q03677 UniProtKB Mutagenesis 24 24 . . . Note=No loss of acireductone dioxygenase activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15938715;Dbxref=PMID:15938715 +Q03677 UniProtKB Mutagenesis 45 45 . . . Note=No loss of acireductone dioxygenase activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15938715;Dbxref=PMID:15938715 +Q03677 UniProtKB Mutagenesis 91 91 . . . Note=Loss of acireductone dioxygenase activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15938715;Dbxref=PMID:15938715 +Q03677 UniProtKB Mutagenesis 151 151 . . . Note=No loss of acireductone dioxygenase activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15938715;Dbxref=PMID:15938715 +##sequence-region P53070 1 669 +P53070 UniProtKB Transit peptide 1 59 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53070 UniProtKB Chain 60 669 . . . ID=PRO_0000042687;Note=Mitochondrial translation optimization protein 1 +P53070 UniProtKB Mutagenesis 431 431 . . . Note=Does not completely restore mitochondrial DNA-dependent respiratory chain activities in respiration-defective mutant cells. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22608499;Dbxref=PMID:22608499 +##sequence-region P53944 1 314 +P53944 UniProtKB Chain 1 314 . . . ID=PRO_0000203448;Note=Mitochondrial N(5)-glutamine methyltransferase MTQ1 +P53944 UniProtKB Region 118 122 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53944 UniProtKB Region 188 191 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53944 UniProtKB Binding site 141 141 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53944 UniProtKB Binding site 188 188 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P34232 1 184 +P34232 UniProtKB Chain 1 184 . . . ID=PRO_0000096634;Note=mRNA transport regulator MTR2 +P34232 UniProtKB Modified residue 125 125 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P34232 UniProtKB Helix 15 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +P34232 UniProtKB Helix 39 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +P34232 UniProtKB Beta strand 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +P34232 UniProtKB Beta strand 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +P34232 UniProtKB Beta strand 57 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +P34232 UniProtKB Helix 62 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +P34232 UniProtKB Beta strand 77 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +P34232 UniProtKB Turn 89 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +P34232 UniProtKB Beta strand 93 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +P34232 UniProtKB Beta strand 115 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WWU +P34232 UniProtKB Beta strand 145 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +P34232 UniProtKB Helix 155 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +P34232 UniProtKB Beta strand 166 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OF5 +##sequence-region P48563 1 1636 +P48563 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P48563 UniProtKB Chain 2 1636 . . . ID=PRO_0000203372;Note=Protein MON2 +P48563 UniProtKB Region 60 410 . . . Note=Golgi membrane targeting and interaction with ARL1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12052896;Dbxref=PMID:12052896 +P48563 UniProtKB Region 1501 1636 . . . Note=Required for function in membrane trafficking +P48563 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P48563 UniProtKB Modified residue 564 564 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48563 UniProtKB Modified residue 567 567 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48563 UniProtKB Modified residue 571 571 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q05812 1 728 +Q05812 UniProtKB Chain 1 728 . . . ID=PRO_0000096595;Note=Meiotic sister-chromatid recombination protein 3 +Q05812 UniProtKB Modified residue 57 57 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05812 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05812 UniProtKB Modified residue 127 127 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05812 UniProtKB Modified residue 151 151 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q05812 UniProtKB Modified residue 155 155 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q05812 UniProtKB Modified residue 363 363 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q05812 UniProtKB Modified residue 646 646 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05812 UniProtKB Modified residue 660 660 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P53214 1 551 +P53214 UniProtKB Signal peptide 1 35 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53214 UniProtKB Chain 36 551 . . . ID=PRO_0000202787;Note=Protein MTL1 +P53214 UniProtKB Topological domain 36 361 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53214 UniProtKB Transmembrane 362 382 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53214 UniProtKB Topological domain 383 551 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53214 UniProtKB Compositional bias 11 356 . . . Note=Ser-rich +P53214 UniProtKB Compositional bias 468 474 . . . Note=Poly-Asp +P53214 UniProtKB Modified residue 481 481 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53214 UniProtKB Modified residue 482 482 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53214 UniProtKB Natural variant 264 264 . . . Note=In strain: ATCC 204278. S->SSSSSSSSSSISLSSSSSSSSSSSSSSSS +P53214 UniProtKB Natural variant 427 427 . . . Note=In strain: SK1. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +##sequence-region Q08550 1 464 +Q08550 UniProtKB Chain 1 464 . . . ID=PRO_0000096555;Note=Meiotic plaque component protein 54 +Q08550 UniProtKB Coiled coil 99 119 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08550 UniProtKB Coiled coil 156 193 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08550 UniProtKB Coiled coil 231 365 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P29952 1 429 +P29952 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1377774;Dbxref=PMID:1377774 +P29952 UniProtKB Chain 2 429 . . . ID=PRO_0000194247;Note=Mannose-6-phosphate isomerase +P29952 UniProtKB Active site 300 300 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P29952 UniProtKB Metal binding 109 109 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P29952 UniProtKB Metal binding 111 111 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P29952 UniProtKB Metal binding 136 136 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P29952 UniProtKB Metal binding 281 281 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P29952 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1377774;Dbxref=PMID:1377774 +P29952 UniProtKB Modified residue 107 107 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P29952 UniProtKB Sequence conflict 25 25 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P11914 1 482 +P11914 UniProtKB Transit peptide 1 13 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2007593;Dbxref=PMID:2007593 +P11914 UniProtKB Chain 14 482 . . . ID=PRO_0000026773;Note=Mitochondrial-processing peptidase subunit alpha +P11914 UniProtKB Sequence conflict 235 235 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11914 UniProtKB Turn 15 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR8 +P11914 UniProtKB Beta strand 20 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Beta strand 29 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Beta strand 38 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Turn 54 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 60 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Turn 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Beta strand 72 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR7 +P11914 UniProtKB Helix 77 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Beta strand 91 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Beta strand 100 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 108 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 111 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 129 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 150 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Turn 163 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 167 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 176 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 184 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 197 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Beta strand 200 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 209 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Beta strand 240 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Beta strand 251 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Beta strand 257 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 273 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Beta strand 285 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 301 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Turn 306 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Beta strand 311 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Beta strand 327 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 337 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 343 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Turn 353 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 364 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 385 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 405 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 417 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Beta strand 443 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 450 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P11914 UniProtKB Helix 456 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +##sequence-region P10507 1 462 +P10507 UniProtKB Transit peptide 1 20 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2007593;Dbxref=PMID:2007593 +P10507 UniProtKB Chain 21 462 . . . ID=PRO_0000026784;Note=Mitochondrial-processing peptidase subunit beta +P10507 UniProtKB Active site 73 73 . . . Note=Proton acceptor +P10507 UniProtKB Metal binding 70 70 . . . Note=Zinc;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10096,ECO:0000269|PubMed:11470436;Dbxref=PMID:11470436 +P10507 UniProtKB Metal binding 74 74 . . . Note=Zinc;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10096,ECO:0000269|PubMed:11470436;Dbxref=PMID:11470436 +P10507 UniProtKB Metal binding 150 150 . . . Note=Zinc;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10096,ECO:0000269|PubMed:11470436;Dbxref=PMID:11470436 +P10507 UniProtKB Modified residue 243 243 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P10507 UniProtKB Mutagenesis 73 73 . . . Note=Loss of activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11470436;Dbxref=PMID:11470436 +P10507 UniProtKB Beta strand 27 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Beta strand 36 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Beta strand 46 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Turn 63 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 68 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Beta strand 78 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 85 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Beta strand 98 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Beta strand 105 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 119 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 137 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 158 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Turn 171 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 175 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 184 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 192 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 205 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Beta strand 208 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 218 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Beta strand 254 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Beta strand 264 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 282 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Beta strand 294 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Turn 297 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Beta strand 302 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 308 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Beta strand 321 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Beta strand 334 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Turn 344 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 349 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 370 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 391 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 411 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 423 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Beta strand 434 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Beta strand 439 445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 447 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +P10507 UniProtKB Helix 453 461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HR6 +##sequence-region P07266 1 363 +P07266 UniProtKB Chain 1 363 . . . ID=PRO_0000096580;Note=Mitochondrial RNA-splicing protein MRS1 +P07266 UniProtKB Sequence conflict 182 182 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07266 UniProtKB Sequence conflict 318 318 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P23500 1 304 +P23500 UniProtKB Chain 1 304 . . . ID=PRO_0000090692;Note=Mitochondrial RNA-splicing protein MRS4 +P23500 UniProtKB Transmembrane 23 41 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23500 UniProtKB Transmembrane 83 102 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23500 UniProtKB Transmembrane 120 139 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23500 UniProtKB Transmembrane 175 194 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23500 UniProtKB Transmembrane 209 228 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23500 UniProtKB Transmembrane 275 288 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23500 UniProtKB Repeat 21 108 . . . Note=Solcar 1 +P23500 UniProtKB Repeat 118 200 . . . Note=Solcar 2 +P23500 UniProtKB Repeat 207 300 . . . Note=Solcar 3 +##sequence-region Q12467 1 430 +Q12467 UniProtKB Transit peptide 1 27 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12467 UniProtKB Chain 28 430 . . . ID=PRO_0000238656;Note=MIOREX complex component 4 +Q12467 UniProtKB Transmembrane 403 420 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q05473 1 314 +Q05473 UniProtKB Chain 1 314 . . . ID=PRO_0000253817;Note=MIOREX complex component 8 +Q05473 UniProtKB Domain 132 312 . . . Note=EngB-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01043 +Q05473 UniProtKB Nucleotide binding 140 147 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01043 +Q05473 UniProtKB Nucleotide binding 173 177 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01043 +Q05473 UniProtKB Nucleotide binding 191 194 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01043 +Q05473 UniProtKB Nucleotide binding 253 256 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01043 +Q05473 UniProtKB Nucleotide binding 290 292 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01043 +Q05473 UniProtKB Metal binding 147 147 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01043 +Q05473 UniProtKB Metal binding 175 175 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01043 +##sequence-region P21339 1 1137 +P21339 UniProtKB Chain 1 1137 . . . ID=PRO_0000096588;Note=Morphogenesis-related protein MSB1 +P21339 UniProtKB Modified residue 538 538 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P21339 UniProtKB Modified residue 776 776 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P21339 UniProtKB Modified residue 816 816 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region Q12317 1 492 +Q12317 UniProtKB Chain 1 492 . . . ID=PRO_0000208020;Note=GTPase-activating protein MSB4 +Q12317 UniProtKB Domain 147 367 . . . Note=Rab-GAP TBC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00163 +Q12317 UniProtKB Mutagenesis 200 200 . . . Note=Reduced GAP activity. R->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12913108;Dbxref=PMID:12913108 +Q12317 UniProtKB Mutagenesis 200 200 . . . Note=Reduced GAP activity. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12913108;Dbxref=PMID:12913108 +##sequence-region Q03104 1 513 +Q03104 UniProtKB Chain 1 513 . . . ID=PRO_0000096591;Note=Meiotic sister chromatid recombination protein 1 +Q03104 UniProtKB Modified residue 237 237 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +Q03104 UniProtKB Modified residue 243 243 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +Q03104 UniProtKB Sequence conflict 52 52 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38590 1 489 +P38590 UniProtKB Chain 1 489 . . . ID=PRO_0000094916;Note=Tyrosine-protein phosphatase MSG5 +P38590 UniProtKB Active site 319 319 . . . Note=Phosphocysteine intermediate +P38590 UniProtKB Modified residue 22 22 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38590 UniProtKB Modified residue 98 98 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38590 UniProtKB Modified residue 151 151 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38590 UniProtKB Modified residue 178 178 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38590 UniProtKB Mutagenesis 319 319 . . . Note=Loss of activity. C->A +P38590 UniProtKB Sequence conflict 347 348 . . . Note=NK->DE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03834 1 1242 +Q03834 UniProtKB Chain 1 1242 . . . ID=PRO_0000115213;Note=DNA mismatch repair protein MSH6 +Q03834 UniProtKB DNA binding 228 299 . . . . +Q03834 UniProtKB Nucleotide binding 982 989 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03834 UniProtKB Region 305 421 . . . Note=Mispair-binding domain +Q03834 UniProtKB Motif 27 34 . . . Note=PIP box +Q03834 UniProtKB Modified residue 102 102 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03834 UniProtKB Modified residue 145 145 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q03834 UniProtKB Modified residue 150 150 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q03834 UniProtKB Modified residue 201 201 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03834 UniProtKB Modified residue 451 451 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03834 UniProtKB Mutagenesis 26 27 . . . Note=Partially functional in a mismatch repair assay%3B when associated with 33-AA-34. KQ->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11005803;Dbxref=PMID:11005803 +Q03834 UniProtKB Mutagenesis 33 34 . . . Note=Abolishes interaction with PCNA (POL30)%2C but only causes a moderate mismatch repair defect. Partially functional in a mismatch repair assay%3B when associated with 26-AA-27. FF->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11005803,ECO:0000269|PubMed:11062484;Dbxref=PMID:11005803,PMID:11062484 +Q03834 UniProtKB Mutagenesis 301 301 . . . Note=Fully functional in a mismatch repair assay. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10537275;Dbxref=PMID:10537275 +Q03834 UniProtKB Mutagenesis 313 313 . . . Note=Fully functional in a mismatch repair assay. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390 +Q03834 UniProtKB Mutagenesis 337 337 . . . Note=Shows defects in both homoduplex and mispair DNA binding and is only partially functional in a mismatch repair assay. F->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10347163,ECO:0000269|PubMed:10970737,ECO:0000269|PubMed:11641390;Dbxref=PMID:10347163,PMID:10970737,PMID:11641390 +Q03834 UniProtKB Mutagenesis 337 337 . . . Note=Partially functional in a mismatch repair assay. F->H%2CI%2CY;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10347163,ECO:0000269|PubMed:10970737,ECO:0000269|PubMed:11641390;Dbxref=PMID:10347163,PMID:10970737,PMID:11641390 +Q03834 UniProtKB Mutagenesis 337 337 . . . Note=Completely abolishes mismatch repair. F->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10347163,ECO:0000269|PubMed:10970737,ECO:0000269|PubMed:11641390;Dbxref=PMID:10347163,PMID:10970737,PMID:11641390 +Q03834 UniProtKB Mutagenesis 337 337 . . . Note=In MSH6-6%3B partially functional in a mismatch repair assay. F->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10347163,ECO:0000269|PubMed:10970737,ECO:0000269|PubMed:11641390;Dbxref=PMID:10347163,PMID:10970737,PMID:11641390 +Q03834 UniProtKB Mutagenesis 339 339 . . . Note=Defective in repairing 8-oxo-G-A mismatches. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11641390,ECO:0000269|PubMed:17141577;Dbxref=PMID:11641390,PMID:17141577 +Q03834 UniProtKB Mutagenesis 340 343 . . . Note=In MSH6-340%3B shows defects in mispair DNA binding%2C but not in homoduplex DNA binding. LYEK->CFAE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10615127;Dbxref=PMID:10615127 +Q03834 UniProtKB Mutagenesis 368 368 . . . Note=Moderately reduced activity in a mismatch repair assay. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390 +Q03834 UniProtKB Mutagenesis 370 370 . . . Note=Partially functional in a mismatch repair assay. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390 +Q03834 UniProtKB Mutagenesis 393 393 . . . Note=Moderately reduced activity in a mismatch repair assay. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390 +Q03834 UniProtKB Mutagenesis 393 393 . . . Note=In MSH6-5%3B partially functional in a mismatch repair assay. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390 +Q03834 UniProtKB Mutagenesis 412 412 . . . Note=Completely abolishes mismatch repair. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390 +Q03834 UniProtKB Mutagenesis 412 412 . . . Note=In MSH6-7%3B partially functional in a mismatch repair assay. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390 +Q03834 UniProtKB Mutagenesis 421 421 . . . Note=In PMS3-1%3B completely abolishes mismatch repair. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8600025;Dbxref=PMID:8600025 +Q03834 UniProtKB Mutagenesis 477 477 . . . Note=Partially functional in a mismatch repair assay. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10537275;Dbxref=PMID:10537275 +Q03834 UniProtKB Mutagenesis 848 848 . . . Note=Fully functional in a mismatch repair assay. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390 +Q03834 UniProtKB Mutagenesis 852 852 . . . Note=Moderately reduced activity in a mismatch repair assay. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11641390;Dbxref=PMID:11641390 +Q03834 UniProtKB Mutagenesis 987 987 . . . Note=Has no defect in mismatch DNA binding%2C but lacks ATP-induced conformational change. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9819445;Dbxref=PMID:9819445 +Q03834 UniProtKB Mutagenesis 988 988 . . . Note=Impairs ATP binding%3B reduces catalytic activity 13-fold for ATP hydrolysis. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16214425,ECO:0000269|PubMed:16600868;Dbxref=PMID:16214425,PMID:16600868 +Q03834 UniProtKB Mutagenesis 1036 1036 . . . Note=In MSH6-4%3B defective for ATP-induced sliding clamp formation and assembly of ternary complexes with MutL alpha. S->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11986324,ECO:0000269|PubMed:16407100;Dbxref=PMID:11986324,PMID:16407100 +Q03834 UniProtKB Mutagenesis 1062 1062 . . . Note=Reduces catalytic activity 13-fold for ATP hydrolysis. E->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12509278,ECO:0000269|PubMed:15513922,ECO:0000269|PubMed:16214425;Dbxref=PMID:12509278,PMID:15513922,PMID:16214425 +Q03834 UniProtKB Mutagenesis 1067 1067 . . . Note=In MSH6-3%3B defective for ATP-induced sliding clamp formation and assembly of ternary complexes with MutL alpha. G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11986324,ECO:0000269|PubMed:16407100;Dbxref=PMID:11986324,PMID:16407100 +Q03834 UniProtKB Mutagenesis 1096 1096 . . . Note=In MSH6-9%3B shows normal mispair binding and dissociation%2C but fails to show complete mispair activation of the ATPase. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11986324;Dbxref=PMID:11986324 +Q03834 UniProtKB Mutagenesis 1142 1142 . . . Note=In MSH6-2%3B defective for ATP-induced sliding clamp formation%2C but assembles ternary complexes with MutL alpha. G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11986324,ECO:0000269|PubMed:16407100;Dbxref=PMID:11986324,PMID:16407100 +##sequence-region P33749 1 630 +P33749 UniProtKB Chain 1 630 . . . ID=PRO_0000046811;Note=Zinc finger protein MSN4 +P33749 UniProtKB Zinc finger 573 596 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P33749 UniProtKB Zinc finger 602 624 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P33749 UniProtKB Motif 237 245 . . . Note=9aaTAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27618436;Dbxref=PMID:27618436 +P33749 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P33749 UniProtKB Modified residue 178 178 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33749 UniProtKB Modified residue 263 263 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P33749 UniProtKB Modified residue 316 316 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33749 UniProtKB Modified residue 319 319 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P33749 UniProtKB Modified residue 479 479 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P33749 UniProtKB Modified residue 558 558 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:19779198 +##sequence-region Q99189 1 972 +Q99189 UniProtKB Chain 1 972 . . . ID=PRO_0000096632;Note=mRNA transport regulator MTR10 +Q99189 UniProtKB Compositional bias 196 201 . . . Note=Poly-Ser +##sequence-region P47047 1 1073 +P47047 UniProtKB Chain 1 1073 . . . ID=PRO_0000102092;Note=ATP-dependent RNA helicase DOB1 +P47047 UniProtKB Domain 158 314 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P47047 UniProtKB Domain 393 597 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P47047 UniProtKB Nucleotide binding 171 178 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P47047 UniProtKB Motif 262 265 . . . Note=DEVH box +P47047 UniProtKB Modified residue 34 34 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P47047 UniProtKB Modified residue 84 84 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P47047 UniProtKB Modified residue 843 843 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47047 UniProtKB Helix 8 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFD +P47047 UniProtKB Beta strand 81 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XGJ +P47047 UniProtKB Beta strand 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XGJ +P47047 UniProtKB Beta strand 119 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 152 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 166 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 173 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 177 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 194 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 202 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 219 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 233 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 239 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 252 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 256 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 264 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Turn 270 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 273 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 288 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 299 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 314 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 326 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 336 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 350 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 393 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 408 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 413 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QU4 +P47047 UniProtKB Helix 416 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 427 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QU4 +P47047 UniProtKB Helix 434 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 453 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 459 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 465 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 472 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 477 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QU4 +P47047 UniProtKB Helix 481 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 497 501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 503 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 513 519 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 521 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 526 531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 534 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Turn 547 549 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 553 559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 565 572 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 587 595 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 596 598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XGJ +P47047 UniProtKB Helix 601 607 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 609 635 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 642 664 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 667 670 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 671 673 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 678 684 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Turn 685 687 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 688 700 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 713 715 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 716 727 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 732 734 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 755 763 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 764 766 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 767 774 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 786 800 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 801 803 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XGJ +P47047 UniProtKB Turn 810 814 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 819 837 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 839 841 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 843 845 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XGJ +P47047 UniProtKB Helix 847 871 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 876 891 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 903 909 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 916 925 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Turn 926 930 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 933 944 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Beta strand 950 952 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 957 979 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 986 992 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 998 1006 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 1010 1015 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 1021 1043 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Turn 1044 1046 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 1048 1061 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +P47047 UniProtKB Helix 1064 1067 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4C +##sequence-region P39731 1 289 +P39731 UniProtKB Chain 1 289 . . . ID=PRO_0000096641;Note=Kinetochore-associated protein MTW1 +P39731 UniProtKB Coiled coil 105 147 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08750 1 479 +Q08750 UniProtKB Chain 1 479 . . . ID=PRO_0000255970;Note=Protein MUM3 +Q08750 UniProtKB Transmembrane 33 49 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08750 UniProtKB Glycosylation 285 285 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P19524 1 1574 +P19524 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P19524 UniProtKB Chain 2 1574 . . . ID=PRO_0000123489;Note=Myosin-2 +P19524 UniProtKB Domain 70 781 . . . Note=Myosin motor +P19524 UniProtKB Domain 784 806 . . . Note=IQ 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116 +P19524 UniProtKB Domain 807 831 . . . Note=IQ 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116 +P19524 UniProtKB Domain 832 855 . . . Note=IQ 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116 +P19524 UniProtKB Domain 856 879 . . . Note=IQ 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116 +P19524 UniProtKB Domain 880 902 . . . Note=IQ 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116 +P19524 UniProtKB Domain 903 932 . . . Note=IQ 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116 +P19524 UniProtKB Domain 1226 1501 . . . Note=Dilute;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00503 +P19524 UniProtKB Nucleotide binding 164 171 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19524 UniProtKB Region 443 523 . . . Note=Actin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19524 UniProtKB Region 1087 1574 . . . Note=Non alpha-helical%2C tail domain +P19524 UniProtKB Coiled coil 933 1088 . . . . +P19524 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P19524 UniProtKB Modified residue 1097 1097 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P19524 UniProtKB Modified residue 1121 1121 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P19524 UniProtKB Mutagenesis 511 511 . . . Note=In MYO2-66%3B disrupts actin binding. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8188749;Dbxref=PMID:8188749 +P19524 UniProtKB Mutagenesis 1189 1189 . . . Note=In MYO2-573%3B causes a mitochondria inheritance defect%3B when associated with G-1288%3B M-1500%3B S-1529%3B G-1546 and R-1559. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144 +P19524 UniProtKB Mutagenesis 1247 1247 . . . Note=Intragenic suppressor of MYO2-2. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12642614;Dbxref=PMID:12642614 +P19524 UniProtKB Mutagenesis 1248 1248 . . . Note=In MYO2-2%3B causes a vacuole inheritance defect. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9843969;Dbxref=PMID:9843969 +P19524 UniProtKB Mutagenesis 1262 1262 . . . Note=Intragenic suppressor of MYO2-2. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12642614;Dbxref=PMID:12642614 +P19524 UniProtKB Mutagenesis 1264 1264 . . . Note=Intragenic suppressor of MYO2-2. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12642614;Dbxref=PMID:12642614 +P19524 UniProtKB Mutagenesis 1268 1268 . . . Note=Intragenic suppressor of MYO2-2. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12642614;Dbxref=PMID:12642614 +P19524 UniProtKB Mutagenesis 1274 1274 . . . Note=Intragenic suppressor of MYO2-2. T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12642614;Dbxref=PMID:12642614 +P19524 UniProtKB Mutagenesis 1275 1275 . . . Note=Intragenic suppressor of MYO2-2. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12642614;Dbxref=PMID:12642614 +P19524 UniProtKB Mutagenesis 1288 1288 . . . Note=Intragenic suppressor of MYO2-2. V->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12391144,ECO:0000269|PubMed:12642614;Dbxref=PMID:12391144,PMID:12642614 +P19524 UniProtKB Mutagenesis 1288 1288 . . . Note=In MYO2-573%3B causes a mitochondria inheritance defect%3B when associated with A-1189%3B M-1500%3B S-1529%3B G-1546 and R-1559. V->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12391144,ECO:0000269|PubMed:12642614;Dbxref=PMID:12391144,PMID:12642614 +P19524 UniProtKB Mutagenesis 1297 1297 . . . Note=Causes a vacuole inheritance defect. D->G%2CN%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10931864;Dbxref=PMID:10931864 +P19524 UniProtKB Mutagenesis 1301 1301 . . . Note=Causes a vacuole inheritance defect. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10931864;Dbxref=PMID:10931864 +P19524 UniProtKB Mutagenesis 1304 1304 . . . Note=Causes a vacuole inheritance defect. N->D%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10931864;Dbxref=PMID:10931864 +P19524 UniProtKB Mutagenesis 1307 1307 . . . Note=Causes a vacuole inheritance defect. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10931864;Dbxref=PMID:10931864 +P19524 UniProtKB Mutagenesis 1474 1474 . . . Note=In MYO2-338%3B abolishes interaction with YPT11%3B when associated with G-1484 and G-1511. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144 +P19524 UniProtKB Mutagenesis 1484 1484 . . . Note=In MYO2-338%3B abolishes interaction with YPT11%3B when associated with S-1474 and G-1511. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144 +P19524 UniProtKB Mutagenesis 1500 1500 . . . Note=In MYO2-573%3B causes a mitochondria inheritance defect%3B when associated with A-1189%3B G-1288%3B S-1529%3B G-1546 and R-1559. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144 +P19524 UniProtKB Mutagenesis 1511 1511 . . . Note=In MYO2-338%3B abolishes interaction with YPT11%3B when associated with S-1474 and G-1484. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144 +P19524 UniProtKB Mutagenesis 1529 1529 . . . Note=In MYO2-573%3B causes a mitochondria inheritance defect%3B when associated with A-1189%3B G-1288%3B M-1500%3B G-1546 and R-1559. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144 +P19524 UniProtKB Mutagenesis 1546 1546 . . . Note=In MYO2-573%3B causes a mitochondria inheritance defect%3B when associated with A-1189%3B G-1288%3B M-1500%3B S-1529 and R-1559. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144 +P19524 UniProtKB Mutagenesis 1559 1559 . . . Note=In MYO2-573%3B causes a mitochondria inheritance defect%3B when associated with A-1189%3B G-1288%3B M-1500%3B S-1529 and G-1546. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12391144;Dbxref=PMID:12391144 +P19524 UniProtKB Helix 807 829 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M45 +P19524 UniProtKB Helix 855 877 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M46 +P19524 UniProtKB Helix 1153 1165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Helix 1167 1176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Turn 1177 1181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Helix 1195 1198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Helix 1200 1214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Helix 1218 1237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Helix 1241 1243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Helix 1244 1271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Helix 1281 1325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Turn 1332 1335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Helix 1355 1371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Helix 1376 1399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Helix 1407 1426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Helix 1432 1435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Helix 1437 1445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Helix 1453 1462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Turn 1463 1465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Helix 1468 1477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Helix 1489 1504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Helix 1505 1507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Helix 1533 1536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +P19524 UniProtKB Helix 1556 1567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6H +##sequence-region P32492 1 1471 +P32492 UniProtKB Chain 1 1471 . . . ID=PRO_0000123491;Note=Myosin-4 +P32492 UniProtKB Domain 71 777 . . . Note=Myosin motor +P32492 UniProtKB Domain 781 801 . . . Note=IQ 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116 +P32492 UniProtKB Domain 804 824 . . . Note=IQ 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116 +P32492 UniProtKB Domain 829 849 . . . Note=IQ 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116 +P32492 UniProtKB Domain 876 898 . . . Note=IQ 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116 +P32492 UniProtKB Domain 899 928 . . . Note=IQ 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116 +P32492 UniProtKB Domain 1164 1419 . . . Note=Dilute;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00503 +P32492 UniProtKB Nucleotide binding 165 172 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32492 UniProtKB Coiled coil 938 1063 . . . . +P32492 UniProtKB Helix 1104 1109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Helix 1111 1121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Helix 1128 1130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LL6 +P32492 UniProtKB Helix 1138 1152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Helix 1156 1176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Turn 1179 1181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Helix 1182 1193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Helix 1196 1204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Helix 1205 1207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LL6 +P32492 UniProtKB Helix 1217 1253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Helix 1255 1259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Helix 1262 1264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Beta strand 1265 1267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Helix 1270 1289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Helix 1294 1319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Helix 1325 1342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Turn 1343 1345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Helix 1350 1353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Helix 1354 1364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Helix 1370 1377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Helix 1385 1393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Beta strand 1398 1401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LL6 +P32492 UniProtKB Helix 1407 1423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Helix 1440 1442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +P32492 UniProtKB Helix 1460 1467 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MMI +##sequence-region P37293 1 288 +P37293 UniProtKB Chain 1 288 . . . ID=PRO_0000096740;Note=Putative N-terminal acetyltransferase 2 +P37293 UniProtKB Sequence conflict 61 61 . . . Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37293 UniProtKB Sequence conflict 63 63 . . . Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37293 UniProtKB Sequence conflict 218 218 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06504 1 195 +Q06504 UniProtKB Chain 1 195 . . . ID=PRO_0000074635;Note=N-terminal acetyltransferase B complex catalytic subunit NAT3 +Q06504 UniProtKB Domain 2 172 . . . Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532 +##sequence-region Q08689 1 176 +Q08689 UniProtKB Chain 1 176 . . . ID=PRO_0000240642;Note=N-alpha-acetyltransferase NAT5 +Q08689 UniProtKB Domain 14 176 . . . Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532 +Q08689 UniProtKB Beta strand 5 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +Q08689 UniProtKB Helix 13 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +Q08689 UniProtKB Helix 16 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +Q08689 UniProtKB Helix 33 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +Q08689 UniProtKB Beta strand 59 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +Q08689 UniProtKB Beta strand 69 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +Q08689 UniProtKB Beta strand 90 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +Q08689 UniProtKB Helix 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +Q08689 UniProtKB Beta strand 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +Q08689 UniProtKB Helix 107 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +Q08689 UniProtKB Beta strand 126 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +Q08689 UniProtKB Helix 136 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +Q08689 UniProtKB Beta strand 148 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +Q08689 UniProtKB Beta strand 165 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +##sequence-region Q08920 1 208 +Q08920 UniProtKB Chain 1 208 . . . ID=PRO_0000232990;Note=Nuclear cap-binding protein subunit 2 +Q08920 UniProtKB Domain 46 124 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q08920 UniProtKB Region 118 122 . . . Note=mRNA cap-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08920 UniProtKB Region 129 133 . . . Note=mRNA cap-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08920 UniProtKB Region 139 140 . . . Note=mRNA cap-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08920 UniProtKB Binding site 24 24 . . . Note=mRNA cap;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08920 UniProtKB Binding site 49 49 . . . Note=mRNA cap;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P16603 1 691 +P16603 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3139648;Dbxref=PMID:3139648 +P16603 UniProtKB Chain 2 691 . . . ID=PRO_0000167608;Note=NADPH--cytochrome P450 reductase +P16603 UniProtKB Topological domain 2 7 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16603 UniProtKB Transmembrane 8 24 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16603 UniProtKB Topological domain 25 691 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16603 UniProtKB Domain 61 204 . . . Note=Flavodoxin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212 +P16603 UniProtKB Domain 266 529 . . . Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212 +P16603 UniProtKB Nucleotide binding 67 72 . . . Note=FMN;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065,ECO:0000269|PubMed:19483672;Dbxref=PMID:16407065,PMID:19483672 +P16603 UniProtKB Nucleotide binding 116 119 . . . Note=FMN;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065,ECO:0000269|PubMed:19483672;Dbxref=PMID:16407065,PMID:19483672 +P16603 UniProtKB Nucleotide binding 152 161 . . . Note=FMN;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065,ECO:0000269|PubMed:19483672;Dbxref=PMID:16407065,PMID:19483672 +P16603 UniProtKB Nucleotide binding 439 442 . . . Note=FAD;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065 +P16603 UniProtKB Nucleotide binding 457 459 . . . Note=FAD;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065 +P16603 UniProtKB Nucleotide binding 476 479 . . . Note=FAD;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065 +P16603 UniProtKB Nucleotide binding 610 611 . . . Note=NADP;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065 +P16603 UniProtKB Nucleotide binding 617 621 . . . Note=NADP;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065 +P16603 UniProtKB Binding site 78 78 . . . Note=FMN%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065 +P16603 UniProtKB Binding site 187 187 . . . Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03212 +P16603 UniProtKB Binding site 187 187 . . . Note=FMN%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065 +P16603 UniProtKB Binding site 285 285 . . . Note=NADP;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065 +P16603 UniProtKB Binding site 543 543 . . . Note=NADP;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065 +P16603 UniProtKB Binding site 646 646 . . . Note=NADP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065 +P16603 UniProtKB Binding site 691 691 . . . Note=FAD;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03212,ECO:0000269|PubMed:16407065;Dbxref=PMID:16407065 +P16603 UniProtKB Cross-link 666 666 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P16603 UniProtKB Natural variant 474 474 . . . Note=V->G +P16603 UniProtKB Sequence conflict 423 423 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16603 UniProtKB Helix 50 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO +P16603 UniProtKB Beta strand 60 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO +P16603 UniProtKB Beta strand 68 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO +P16603 UniProtKB Helix 71 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO +P16603 UniProtKB Beta strand 91 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO +P16603 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO +P16603 UniProtKB Helix 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO +P16603 UniProtKB Beta strand 109 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO +P16603 UniProtKB Beta strand 119 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO +P16603 UniProtKB Helix 125 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO +P16603 UniProtKB Helix 128 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO +P16603 UniProtKB Turn 139 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO +P16603 UniProtKB Beta strand 146 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO +P16603 UniProtKB Beta strand 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO +P16603 UniProtKB Helix 162 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO +P16603 UniProtKB Beta strand 183 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO +P16603 UniProtKB Turn 187 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO +P16603 UniProtKB Helix 192 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FJO +P16603 UniProtKB Beta strand 223 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BN4 +P16603 UniProtKB Beta strand 234 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BN4 +P16603 UniProtKB Helix 243 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Beta strand 271 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Beta strand 287 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Beta strand 306 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Helix 315 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Beta strand 332 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Beta strand 337 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Beta strand 348 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Helix 352 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Helix 368 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Helix 375 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BN4 +P16603 UniProtKB Helix 381 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Helix 394 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Helix 402 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Helix 408 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Helix 426 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Beta strand 439 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Turn 447 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Beta strand 453 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Beta strand 469 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BF4 +P16603 UniProtKB Helix 477 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Turn 494 496 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Helix 508 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Turn 511 515 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Beta strand 519 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Beta strand 536 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Helix 542 545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Helix 546 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Turn 564 566 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BN4 +P16603 UniProtKB Beta strand 574 585 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Turn 587 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Helix 592 599 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Helix 600 602 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Beta strand 603 610 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Helix 620 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Helix 628 635 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Turn 636 638 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Beta strand 640 645 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Helix 650 665 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Helix 670 682 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +P16603 UniProtKB Beta strand 685 690 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BPO +##sequence-region Q06389 1 190 +Q06389 UniProtKB Initiator methionine 1 1 . . . Note=Removed +Q06389 UniProtKB Chain 2 190 . . . ID=PRO_0000073795;Note=Calcium-binding protein NCS-1 +Q06389 UniProtKB Domain 24 59 . . . Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +Q06389 UniProtKB Domain 60 95 . . . Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +Q06389 UniProtKB Domain 96 131 . . . Note=EF-hand 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +Q06389 UniProtKB Domain 144 179 . . . Note=EF-hand 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +Q06389 UniProtKB Calcium binding 73 84 . . . Note=1 +Q06389 UniProtKB Calcium binding 109 120 . . . Note=2 +Q06389 UniProtKB Calcium binding 157 168 . . . Note=3 +Q06389 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10559922;Dbxref=PMID:10559922 +Q06389 UniProtKB Mutagenesis 2 2 . . . Note=Abolishes N-myristoylation. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10559922;Dbxref=PMID:10559922 +Q06389 UniProtKB Beta strand 7 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JU0 +Q06389 UniProtKB Helix 11 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW +Q06389 UniProtKB Turn 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW +Q06389 UniProtKB Helix 24 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW +Q06389 UniProtKB Helix 45 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW +Q06389 UniProtKB Helix 63 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW +Q06389 UniProtKB Beta strand 77 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW +Q06389 UniProtKB Helix 82 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW +Q06389 UniProtKB Helix 99 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW +Q06389 UniProtKB Beta strand 113 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW +Q06389 UniProtKB Helix 118 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW +Q06389 UniProtKB Beta strand 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW +Q06389 UniProtKB Helix 145 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW +Q06389 UniProtKB Turn 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW +Q06389 UniProtKB Beta strand 161 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW +Q06389 UniProtKB Helix 166 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW +Q06389 UniProtKB Helix 179 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FPW +##sequence-region Q12366 1 352 +Q12366 UniProtKB Chain 1 352 . . . ID=PRO_0000268688;Note=Non-disjunction protein 1 +##sequence-region P38757 1 446 +P38757 UniProtKB Chain 1 446 . . . ID=PRO_0000212579;Note=Nuclear envelope morphology protein 1 +P38757 UniProtKB Transmembrane 87 103 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38757 UniProtKB Domain 247 424 . . . Note=FCP1 homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00336 +P38757 UniProtKB Mutagenesis 257 257 . . . Note=Abolishes phosphatase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15889145;Dbxref=PMID:15889145 +##sequence-region Q03264 1 515 +Q03264 UniProtKB Chain 1 515 . . . ID=PRO_0000218579;Note=RNA exonuclease NGL2 +##sequence-region P0CX80 1 61 +P0CX80 UniProtKB Propeptide 1 8 . . . ID=PRO_0000018675 +P0CX80 UniProtKB Chain 9 61 . . . ID=PRO_0000018676;Note=Copper metallothionein 1-1 +P0CX80 UniProtKB Metal binding 15 15 . . . Note=Copper 1 +P0CX80 UniProtKB Metal binding 15 15 . . . Note=Copper 2 +P0CX80 UniProtKB Metal binding 17 17 . . . Note=Copper 1 +P0CX80 UniProtKB Metal binding 17 17 . . . Note=Copper 3 +P0CX80 UniProtKB Metal binding 19 19 . . . Note=Copper 4 +P0CX80 UniProtKB Metal binding 19 19 . . . Note=Copper 5 +P0CX80 UniProtKB Metal binding 22 22 . . . Note=Copper 3 +P0CX80 UniProtKB Metal binding 22 22 . . . Note=Copper 4 +P0CX80 UniProtKB Metal binding 22 22 . . . Note=Copper 6 +P0CX80 UniProtKB Metal binding 28 28 . . . Note=Copper 2 +P0CX80 UniProtKB Metal binding 28 28 . . . Note=Copper 6 +P0CX80 UniProtKB Metal binding 32 32 . . . Note=Copper 1 +P0CX80 UniProtKB Metal binding 32 32 . . . Note=Copper 7 +P0CX80 UniProtKB Metal binding 34 34 . . . Note=Copper 3 +P0CX80 UniProtKB Metal binding 34 34 . . . Note=Copper 7 +P0CX80 UniProtKB Metal binding 34 34 . . . Note=Copper 8 +P0CX80 UniProtKB Metal binding 38 38 . . . Note=Copper 5 +P0CX80 UniProtKB Metal binding 38 38 . . . Note=Copper 8 +P0CX80 UniProtKB Metal binding 44 44 . . . Note=Copper 4 +P0CX80 UniProtKB Metal binding 44 44 . . . Note=Copper 8 +P0CX80 UniProtKB Metal binding 46 46 . . . Note=Copper 6 +P0CX80 UniProtKB Metal binding 46 46 . . . Note=Copper 7 +P0CX80 UniProtKB Cross-link 30 30 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX80 UniProtKB Turn 20 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJU +P0CX80 UniProtKB Helix 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJU +P0CX80 UniProtKB Turn 36 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AQR +P0CX80 UniProtKB Helix 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RJU +##sequence-region P14908 1 341 +P14908 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1939277;Dbxref=PMID:1939277 +P14908 UniProtKB Chain 2 341 . . . ID=PRO_0000096621;Note=Mitochondrial transcription factor 1 +P14908 UniProtKB Compositional bias 157 196 . . . Note=Arg/Lys-rich (basic) +P14908 UniProtKB Compositional bias 209 233 . . . Note=Asp/Glu-rich (acidic) +P14908 UniProtKB Compositional bias 246 260 . . . Note=Asp/Glu-rich (acidic) +P14908 UniProtKB Binding site 23 23 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026 +P14908 UniProtKB Binding site 77 77 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026 +P14908 UniProtKB Binding site 101 101 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026 +P14908 UniProtKB Binding site 137 137 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01026 +P14908 UniProtKB Sequence conflict 79 79 . . . Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14908 UniProtKB Sequence conflict 287 288 . . . Note=QY->PI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14908 UniProtKB Helix 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Helix 26 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Helix 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Turn 45 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Beta strand 49 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Helix 59 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Beta strand 71 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Helix 80 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Turn 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Beta strand 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Helix 105 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Turn 112 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Beta strand 127 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Helix 143 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Helix 159 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Beta strand 164 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Helix 174 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Helix 191 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Beta strand 200 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Helix 210 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Helix 218 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Helix 231 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Beta strand 234 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Beta strand 242 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Helix 256 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Turn 268 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Turn 274 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Helix 277 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Helix 285 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Turn 290 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Turn 297 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Helix 303 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +P14908 UniProtKB Helix 308 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I4W +##sequence-region P08964 1 1928 +P08964 UniProtKB Chain 1 1928 . . . ID=PRO_0000123484;Note=Myosin-1 +P08964 UniProtKB Domain 75 791 . . . Note=Myosin motor +P08964 UniProtKB Domain 794 823 . . . Note=IQ;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00116 +P08964 UniProtKB Nucleotide binding 180 187 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08964 UniProtKB Region 460 529 . . . Note=Actin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08964 UniProtKB Coiled coil 856 1911 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08964 UniProtKB Sequence conflict 36 36 . . . Note=K->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 46 46 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 46 46 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 59 59 . . . Note=V->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 59 59 . . . Note=V->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 86 86 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 330 330 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 330 330 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 343 343 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 343 343 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 421 426 . . . Note=QQAKFI->TKLSSL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 515 515 . . . Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 529 535 . . . Note=SKGPPTG->ARGHDR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 529 535 . . . Note=SKGPPTG->ARGHDR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 541 541 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 541 541 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 550 551 . . . Note=TD->LM;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 573 573 . . . Note=R->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 582 582 . . . Note=H->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 588 599 . . . Note=EYTVEGWLSKNK->NTLWKAGYPKT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 599 599 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 627 632 . . . Note=EKSSSA->GKNLLVC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 627 632 . . . Note=EKSSSA->GKNLLVC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 695 695 . . . Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 695 695 . . . Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 736 742 . . . Note=ENSTTTT->RKFNHHD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 756 756 . . . Note=E->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 756 756 . . . Note=E->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 773 784 . . . Note=NTKLFFKAGVLA->ILTVFQKLEYWS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 793 794 . . . Note=KL->NV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 896 896 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 900 900 . . . Note=N->NSQITKINTNITETPQSTYIGERPKRVICGN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 906 906 . . . Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 911 911 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 915 930 . . . Note=NESLLNRVKTSSETLQ->RIAIKILKPAINIT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 934 939 . . . Note=DDLVSE->MTLFL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 951 958 . . . Note=AQNLEEAH->RKILKKLD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1002 1002 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1049 1049 . . . Note=L->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1056 1056 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1060 1060 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1085 1085 . . . Note=A->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1123 1123 . . . Note=V->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1133 1133 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1144 1146 . . . Note=KSN->NLI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1159 1168 . . . Note=RETKEQEQKK->TRKKEEQDKE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1179 1204 . . . Note=SKIKELEARLSQEISLNQYLNKRISG->ELKVKEWKARCHRKYLKSILKQKNIR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1224 1224 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1228 1228 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1253 1253 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1311 1323 . . . Note=PDKESDINKLMLE->LTKSLILTNGNAS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1400 1400 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1454 1554 . . . Note=SEQLDRLQKDLESTERQKELLSSTIKQQKQQFENCMDDLQGNELRLREHIHALKQAEEDVKNMASIIEKLKTQNKQKEKLIWEREMERNDSDMQLQETLLE->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1568 1568 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1630 1646 . . . Note=DLLKQLDHYTKVVEMLN->SEAARSLYKSGGNVD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1699 1705 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1725 1737 . . . Note=TLQLQMEQNSRNG->NTTANGTKFKEW;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1754 1757 . . . Note=FDDE->LMM;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1777 1777 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1788 1788 . . . Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1825 1825 . . . Note=S->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1882 1882 . . . Note=S->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08964 UniProtKB Sequence conflict 1902 1904 . . . Note=FWK->NSGKRLDADDL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04439 1 1219 +Q04439 UniProtKB Chain 1 1219 . . . ID=PRO_0000123492;Note=Myosin-5 +Q04439 UniProtKB Domain 36 715 . . . Note=Myosin motor +Q04439 UniProtKB Domain 719 739 . . . Note=IQ 1 +Q04439 UniProtKB Domain 740 765 . . . Note=IQ 2 +Q04439 UniProtKB Domain 771 961 . . . Note=TH1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01093 +Q04439 UniProtKB Domain 1085 1147 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +Q04439 UniProtKB Nucleotide binding 129 136 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04439 UniProtKB Region 404 486 . . . Note=Actin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04439 UniProtKB Compositional bias 1000 1088 . . . Note=Ala/Pro-rich +Q04439 UniProtKB Compositional bias 1011 1016 . . . Note=Poly-Pro +Q04439 UniProtKB Compositional bias 1060 1063 . . . Note=Poly-Ala +Q04439 UniProtKB Compositional bias 1073 1081 . . . Note=Poly-Pro +Q04439 UniProtKB Compositional bias 1204 1218 . . . Note=Asp/Glu-rich (acidic) +Q04439 UniProtKB Modified residue 357 357 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:16478726;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:16478726 +Q04439 UniProtKB Modified residue 359 359 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q04439 UniProtKB Modified residue 777 777 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16478726;Dbxref=PMID:16478726 +Q04439 UniProtKB Modified residue 992 992 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q04439 UniProtKB Modified residue 1205 1205 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q04439 UniProtKB Mutagenesis 164 164 . . . Note=Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12808026;Dbxref=PMID:12808026 +Q04439 UniProtKB Mutagenesis 168 168 . . . Note=Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12808026;Dbxref=PMID:12808026 +Q04439 UniProtKB Mutagenesis 209 209 . . . Note=Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12808026;Dbxref=PMID:12808026 +Q04439 UniProtKB Mutagenesis 357 357 . . . Note=Leads to a depolarized actin cytoskeleton and a strong defect in the capacity to internalize STE2. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16478726;Dbxref=PMID:16478726 +Q04439 UniProtKB Mutagenesis 357 357 . . . Note=No growth defect%2C but leads to a partially depolarized actin cytoskeleton. Accelerates the constitutive internalization of STE2. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16478726;Dbxref=PMID:16478726 +Q04439 UniProtKB Mutagenesis 377 377 . . . Note=Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12808026;Dbxref=PMID:12808026 +Q04439 UniProtKB Mutagenesis 472 472 . . . Note=In MYO5-1%3B temperature sensitive loss of function. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8614799;Dbxref=PMID:8614799 +Q04439 UniProtKB Mutagenesis 1123 1123 . . . Note=Abolishes interaction with BBC1 and VRP1. W->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10944111,ECO:0000269|PubMed:11901111;Dbxref=PMID:10944111,PMID:11901111 +Q04439 UniProtKB Beta strand 1089 1094 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUY +Q04439 UniProtKB Beta strand 1112 1118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUY +Q04439 UniProtKB Beta strand 1122 1130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUY +Q04439 UniProtKB Beta strand 1134 1138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUY +Q04439 UniProtKB Helix 1139 1141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZUY +Q04439 UniProtKB Beta strand 1142 1144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YP5 +##sequence-region Q12387 1 796 +Q12387 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12387 UniProtKB Chain 2 796 . . . ID=PRO_0000079850;Note=N-terminal acetyltransferase B complex subunit MDM20 +Q12387 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P38795 1 714 +P38795 UniProtKB Chain 1 714 . . . ID=PRO_0000152248;Note=Glutamine-dependent NAD(+) synthetase +P38795 UniProtKB Domain 5 275 . . . Note=CN hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054 +P38795 UniProtKB Nucleotide binding 359 366 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38795 UniProtKB Region 329 714 . . . Note=Ligase +P38795 UniProtKB Active site 45 45 . . . Note=Proton acceptor%3B for glutaminase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WJJ3 +P38795 UniProtKB Active site 114 114 . . . Note=For glutaminase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WJJ3 +P38795 UniProtKB Active site 175 175 . . . Note=Nucleophile%3B for glutaminase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P9WJJ3 +P38795 UniProtKB Active site 361 361 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P12945 1 854 +P12945 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12945 UniProtKB Chain 2 854 . . . ID=PRO_0000096739;Note=N-terminal acetyltransferase A complex subunit NAT1 +P12945 UniProtKB Repeat 20 53 . . . Note=TPR 1 +P12945 UniProtKB Repeat 54 87 . . . Note=TPR 2 +P12945 UniProtKB Repeat 91 124 . . . Note=TPR 3 +P12945 UniProtKB Repeat 126 162 . . . Note=TPR 4 +P12945 UniProtKB Repeat 241 274 . . . Note=TPR 5 +P12945 UniProtKB Repeat 384 417 . . . Note=TPR 6 +P12945 UniProtKB Repeat 452 485 . . . Note=TPR 7 +P12945 UniProtKB Repeat 728 761 . . . Note=TPR 8 +P12945 UniProtKB Coiled coil 623 667 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12945 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12945 UniProtKB Modified residue 674 674 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P12945 UniProtKB Helix 24 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 36 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 54 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 70 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 91 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 107 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 126 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 141 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 159 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 175 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 198 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 220 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 234 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 240 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 257 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 275 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 291 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 309 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 314 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 322 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 344 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 356 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Turn 376 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 380 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 400 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 418 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 434 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 452 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 468 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Turn 478 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY +P12945 UniProtKB Beta strand 484 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 488 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 497 523 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 536 570 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 571 574 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 575 582 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 585 595 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 596 600 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 602 621 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Turn 629 631 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY +P12945 UniProtKB Helix 662 669 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Turn 674 676 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 683 686 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 691 698 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 700 706 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Turn 709 711 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 714 721 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Turn 722 725 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 727 741 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Beta strand 743 745 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY +P12945 UniProtKB Helix 746 758 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Beta strand 763 765 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 767 781 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Turn 782 784 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 787 791 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 797 805 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 810 818 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Turn 819 822 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Helix 827 837 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +P12945 UniProtKB Turn 838 840 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNY +P12945 UniProtKB Helix 843 852 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XNH +##sequence-region P52919 1 319 +P52919 UniProtKB Chain 1 319 . . . ID=PRO_0000096745;Note=NAP1-binding protein +P52919 UniProtKB Modified residue 251 251 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P52919 UniProtKB Modified residue 260 260 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q12163 1 236 +Q12163 UniProtKB Chain 1 236 . . . ID=PRO_0000257822;Note=NAP1-binding protein 2 +Q12163 UniProtKB Domain 110 171 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +Q12163 UniProtKB Modified residue 102 102 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12163 UniProtKB Modified residue 196 196 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +Q12163 UniProtKB Modified residue 235 235 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12163 UniProtKB Beta strand 113 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YN8 +Q12163 UniProtKB Beta strand 136 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YN8 +Q12163 UniProtKB Beta strand 147 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YN8 +Q12163 UniProtKB Beta strand 158 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YN8 +Q12163 UniProtKB Helix 163 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YN8 +Q12163 UniProtKB Beta strand 166 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YN8 +##sequence-region Q12374 1 616 +Q12374 UniProtKB Chain 1 616 . . . ID=PRO_0000096754;Note=Nuclear control of ATPase protein 2 +Q12374 UniProtKB Transmembrane 321 341 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12374 UniProtKB Transmembrane 488 508 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12374 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q02866 1 612 +Q02866 UniProtKB Chain 1 612 . . . ID=PRO_0000255969;Note=Protein MUK1 +Q02866 UniProtKB Domain 273 414 . . . Note=VPS9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00550 +Q02866 UniProtKB Compositional bias 115 195 . . . Note=Ser-rich +Q02866 UniProtKB Compositional bias 512 554 . . . Note=Ser-rich +Q02866 UniProtKB Modified residue 67 67 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02866 UniProtKB Modified residue 163 163 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q02866 UniProtKB Modified residue 185 185 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q02866 UniProtKB Modified residue 245 245 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q02197 1 733 +Q02197 UniProtKB Chain 1 733 . . . ID=PRO_0000084553;Note=N-alpha-acetyltransferase%2C 35 NatC auxiliary subunit +##sequence-region Q8TGN9 1 163 +Q8TGN9 UniProtKB Chain 1 163 . . . ID=PRO_0000299922;Note=Protein NAG1 +Q8TGN9 UniProtKB Transmembrane 76 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P27929 1 486 +P27929 UniProtKB Chain 1 486 . . . ID=PRO_0000030639;Note=37S ribosomal protein NAM9%2C mitochondrial +P27929 UniProtKB Domain 103 172 . . . Note=S4 RNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00182 +P27929 UniProtKB Mutagenesis 82 82 . . . Note=In NAM9-1%3B suppressor for ocher mutations in mitochondrial DNA%2C possibly through decreasing the fidelity of translation. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7557422;Dbxref=PMID:7557422 +P27929 UniProtKB Mutagenesis 109 109 . . . Note=In MNA6-3%3B causes temperature-dependent loss of the 15S rRNA. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10529174;Dbxref=PMID:10529174 +P27929 UniProtKB Mutagenesis 111 111 . . . Note=In MNA6-1%3B causes temperature-dependent loss of the 15S rRNA. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10529174;Dbxref=PMID:10529174 +P27929 UniProtKB Mutagenesis 424 424 . . . Note=In MNA6-4%3B causes temperature-dependent loss of the 15S rRNA. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10529174;Dbxref=PMID:10529174 +P27929 UniProtKB Mutagenesis 438 438 . . . Note=In MNA6-2%3B causes temperature-dependent loss of the 15S rRNA. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10529174;Dbxref=PMID:10529174 +##sequence-region P25293 1 417 +P25293 UniProtKB Chain 1 417 . . . ID=PRO_0000185659;Note=Nucleosome assembly protein +P25293 UniProtKB DNA binding 330 356 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25293 UniProtKB Region 143 362 . . . Note=Interaction with NBA1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 +P25293 UniProtKB Compositional bias 168 180 . . . Note=Asp/Glu-rich (acidic) +P25293 UniProtKB Compositional bias 324 336 . . . Note=Asp/Glu-rich (acidic) +P25293 UniProtKB Compositional bias 366 403 . . . Note=Asp/Glu-rich (acidic) +P25293 UniProtKB Modified residue 20 20 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P25293 UniProtKB Modified residue 24 24 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P25293 UniProtKB Modified residue 27 27 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P25293 UniProtKB Modified residue 53 53 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25293 UniProtKB Modified residue 69 69 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25293 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +P25293 UniProtKB Modified residue 82 82 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18086883;Dbxref=PMID:19779198,PMID:18086883 +P25293 UniProtKB Modified residue 98 98 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 +P25293 UniProtKB Modified residue 104 104 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 +P25293 UniProtKB Modified residue 140 140 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:18086883;Dbxref=PMID:18407956,PMID:18086883 +P25293 UniProtKB Modified residue 159 159 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 +P25293 UniProtKB Modified residue 177 177 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18086883;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:18086883 +P25293 UniProtKB Modified residue 397 397 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 +P25293 UniProtKB Cross-link 50 50 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25293 UniProtKB Mutagenesis 99 99 . . . Note=Predominantly cytoplasmic%3B when associated with A-159%2C A-177 and S-397. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 +P25293 UniProtKB Mutagenesis 159 159 . . . Note=Significant reduction in phosphorylation%3B when associated with A-397. Complete inhibition of phosphorylation%3B when associated with A-177 and A-397. Leads to a prolonged S phase and a shortened passage through G1%3B when associated with A-177 and A-397. Predominantly cytoplasmic%3B when associated with S-99%2C A-177 and A-397. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 +P25293 UniProtKB Mutagenesis 159 159 . . . Note=Leads to a prolonged S phase and a shortened passage through G1%3B when associated with A-177 and A-397. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 +P25293 UniProtKB Mutagenesis 177 177 . . . Note=Significant reduction in phosphorylation%3B when associated with A-397. Complete inhibition of phosphorylation%3B when associated with A-159 and A-397. Leads to a prolonged S phase and a shortened passage through G1%3B when associated with A-159 and A-397. Predominantly cytoplasmic%3B when associated with S-99%2C A-159 and A-397. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 +P25293 UniProtKB Mutagenesis 177 177 . . . Note=Leads to a prolonged S phase and a shortened passage through G1%3B when associated with A-159 and A-397. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 +P25293 UniProtKB Mutagenesis 397 397 . . . Note=Significant reduction in phosphorylation%3B when associated with either A-159 or A-177. Complete inhibition of phosphorylation%3B when associated with A-159 and A-177. Leads to a prolonged S phase and a shortened passage through G1%3B when associated with A-159 and A-177. Predominantly cytoplasmic%3B when associated with S-99%3B A-159 and A-177. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 +P25293 UniProtKB Mutagenesis 397 397 . . . Note=Leads to a prolonged S phase and a shortened passage through G1%3B when associated with A-159 and A-177. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 +P25293 UniProtKB Sequence conflict 2 2 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25293 UniProtKB Sequence conflict 103 104 . . . Note=QS->LC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25293 UniProtKB Sequence conflict 137 138 . . . Note=RI->TM;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25293 UniProtKB Sequence conflict 384 384 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25293 UniProtKB Turn 73 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Helix 77 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Helix 90 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Beta strand 141 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Helix 147 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Helix 163 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Helix 188 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Helix 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Helix 205 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Helix 210 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Beta strand 214 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Beta strand 224 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Beta strand 228 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Turn 237 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Beta strand 241 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Beta strand 246 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Beta strand 260 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Beta strand 265 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Turn 279 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Beta strand 285 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Turn 295 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z2R +P25293 UniProtKB Beta strand 304 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Helix 312 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Beta strand 327 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Helix 332 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Turn 351 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Helix 356 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +P25293 UniProtKB Helix 363 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AYU +##sequence-region Q02820 1 53 +Q02820 UniProtKB Chain 1 53 . . . ID=PRO_0000096759;Note=Non-classical export protein 1 +Q02820 UniProtKB Transmembrane 7 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06568 1 189 +Q06568 UniProtKB Chain 1 189 . . . ID=PRO_0000240229;Note=Nuclear distribution protein nudE homolog 1 +Q06568 UniProtKB Coiled coil 4 121 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38236 1 366 +P38236 UniProtKB Chain 1 366 . . . ID=PRO_0000096647;Note=Protein MUM2 +##sequence-region P38734 1 546 +P38734 UniProtKB Chain 1 546 . . . ID=PRO_0000096649;Note=Low-affinity methionine permease +P38734 UniProtKB Topological domain 1 70 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Transmembrane 71 91 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Topological domain 92 98 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Transmembrane 99 119 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Topological domain 120 148 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Transmembrane 149 169 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Topological domain 170 188 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Transmembrane 189 209 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Topological domain 210 213 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Transmembrane 214 234 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Topological domain 235 254 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Transmembrane 255 275 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Topological domain 276 297 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Transmembrane 298 318 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Topological domain 319 319 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Transmembrane 320 340 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Topological domain 341 346 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Transmembrane 347 367 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Topological domain 368 393 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Transmembrane 394 414 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Topological domain 415 423 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Transmembrane 424 444 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Topological domain 445 459 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Transmembrane 460 480 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Topological domain 481 494 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Transmembrane 495 515 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38734 UniProtKB Topological domain 516 546 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P42939 1 101 +P42939 UniProtKB Chain 1 101 . . . ID=PRO_0000202845;Note=Multivesicular body sorting factor 12 +P42939 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P42939 UniProtKB Modified residue 94 94 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P42939 UniProtKB Mutagenesis 47 47 . . . Note=Defective in MVB12 incorporation in ESCRT-I complex%3B reduces localization to MVBs%3B abolishes interaction with STP22 and SRN2%3B when associated with D-57. L->D +P42939 UniProtKB Mutagenesis 54 54 . . . Note=Defective in MVB12 incorporation in ESCRT-I complex%3B when associated with D-57. C->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384 +P42939 UniProtKB Mutagenesis 57 57 . . . Note=Defective in MVB12 incorporation in ESCRT-I complex%3B reduces localization to MVBs%3B abolishes interaction with STP22 and SRN2%3B when associated with D-47. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384 +P42939 UniProtKB Mutagenesis 64 64 . . . Note=Defective in MVB12 incorporation in ESCRT-I complex%3B when associated with D-47. H->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384 +P42939 UniProtKB Helix 4 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +P42939 UniProtKB Beta strand 15 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +P42939 UniProtKB Helix 41 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +P42939 UniProtKB Helix 67 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +##sequence-region P25566 1 168 +P25566 UniProtKB Chain 1 168 . . . ID=PRO_0000140326;Note=Peptide methionine sulfoxide reductase 2 +P25566 UniProtKB Domain 40 168 . . . Note=MsrB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01126 +P25566 UniProtKB Active site 157 157 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01126 +P25566 UniProtKB Metal binding 79 79 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01126 +P25566 UniProtKB Metal binding 82 82 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01126 +P25566 UniProtKB Metal binding 128 128 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01126 +P25566 UniProtKB Metal binding 131 131 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01126 +P25566 UniProtKB Disulfide bond 97 157 . . . Note=Redox-active;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q04751 1 285 +Q04751 UniProtKB Chain 1 285 . . . ID=PRO_0000074636;Note=N-alpha-acetyltransferase 40 +Q04751 UniProtKB Domain 88 274 . . . Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532 +Q04751 UniProtKB Region 163 165 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q86UY6 +Q04751 UniProtKB Region 187 189 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q86UY6 +Q04751 UniProtKB Region 195 200 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q86UY6 +Q04751 UniProtKB Binding site 116 116 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q86UY6 +Q04751 UniProtKB Binding site 185 185 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q86UY6 +Q04751 UniProtKB Binding site 228 228 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q86UY6 +Q04751 UniProtKB Binding site 233 233 . . . Note=Acetyl-CoA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q86UY6 +Q04751 UniProtKB Site 186 186 . . . Note=Essential for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q86UY6 +##sequence-region Q03735 1 1134 +Q03735 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q03735 UniProtKB Chain 2 1134 . . . ID=PRO_0000082034;Note=RNA-binding protein NAB6 +Q03735 UniProtKB Domain 653 726 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q03735 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q03735 UniProtKB Modified residue 464 464 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03735 UniProtKB Modified residue 467 467 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P53919 1 492 +P53919 UniProtKB Chain 1 492 . . . ID=PRO_0000203428;Note=H/ACA ribonucleoprotein complex non-core subunit NAF1 +P53919 UniProtKB Region 172 230 . . . Note=RNA-binding +P53919 UniProtKB Compositional bias 55 81 . . . Note=Ser-rich +P53919 UniProtKB Compositional bias 361 456 . . . Note=Pro-rich +P53919 UniProtKB Compositional bias 419 488 . . . Note=Gln-rich +P53919 UniProtKB Modified residue 255 255 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53919 UniProtKB Natural variant 378 378 . . . Note=In strain: YJM269%2C YJM270%2C YJM326 and YJM1129. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53919 UniProtKB Natural variant 423 423 . . . Note=In strain: YJM627. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53919 UniProtKB Natural variant 424 424 . . . Note=In strain: YJM269%2C YJM270%2C YJM326 and YJM1129. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53919 UniProtKB Natural variant 426 426 . . . Note=In strain: SK1%2C V1-09%2C YJM269%2C YJM270%2C YJM280%2C YJM320%2C YJM326%2C YJM339%2C YJM627%2C YJM789 and YJM1129. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53919 UniProtKB Natural variant 480 480 . . . Note=In strain: V1-09 and YJM627. H->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53919 UniProtKB Beta strand 137 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M +P53919 UniProtKB Beta strand 150 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M +P53919 UniProtKB Beta strand 169 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M +P53919 UniProtKB Beta strand 177 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M +P53919 UniProtKB Beta strand 183 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M +P53919 UniProtKB Beta strand 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M +P53919 UniProtKB Beta strand 192 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M +P53919 UniProtKB Helix 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M +P53919 UniProtKB Helix 202 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M +P53919 UniProtKB Turn 210 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M +P53919 UniProtKB Beta strand 214 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3M +##sequence-region P40360 1 574 +P40360 UniProtKB Transit peptide 1 13 . . . Note=Mitochondrion +P40360 UniProtKB Chain 14 574 . . . ID=PRO_0000203054;Note=Amino-acid acetyltransferase%2C mitochondrial +P40360 UniProtKB Domain 392 560 . . . Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532 +##sequence-region P30771 1 971 +P30771 UniProtKB Chain 1 971 . . . ID=PRO_0000080713;Note=ATP-dependent helicase NAM7 +P30771 UniProtKB Zinc finger 61 208 . . . Note=UPF1-type +P30771 UniProtKB Nucleotide binding 430 437 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P30771 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P30771 UniProtKB Modified residue 869 869 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P30771 UniProtKB Turn 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Turn 70 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 73 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Turn 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 88 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 94 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 123 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Turn 130 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 133 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 145 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Turn 149 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 162 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 166 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 171 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Turn 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 186 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 195 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 235 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 267 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 277 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 298 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 305 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 311 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 328 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 345 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 356 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 377 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 411 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 424 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 436 451 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 455 461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 462 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 479 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 485 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 495 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 499 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 510 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 526 545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 548 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 556 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 567 571 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 574 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 579 586 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Turn 587 589 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 590 597 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 609 613 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Turn 614 617 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 620 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 642 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 658 661 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Turn 663 666 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 682 686 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 697 701 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 703 718 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 723 725 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 726 731 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 733 746 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 751 755 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 757 761 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 762 765 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 770 776 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 787 790 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 792 799 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 800 810 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 812 815 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Helix 819 831 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 834 838 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +P30771 UniProtKB Beta strand 841 844 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XZL +##sequence-region Q08229 1 501 +Q08229 UniProtKB Chain 1 501 . . . ID=PRO_0000235925;Note=Protein NBA1 +Q08229 UniProtKB Region 275 501 . . . Note=Necessary for the normal cellular distribution and bud neck targeting +Q08229 UniProtKB Compositional bias 405 424 . . . Note=Lys-rich +Q08229 UniProtKB Modified residue 138 138 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08229 UniProtKB Modified residue 208 208 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08229 UniProtKB Modified residue 403 403 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P52920 1 328 +P52920 UniProtKB Chain 1 328 . . . ID=PRO_0000184947;Note=Cytosolic Fe-S cluster assembly factor NBP35 +P52920 UniProtKB Nucleotide binding 80 87 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03038 +P52920 UniProtKB Metal binding 27 27 . . . Note=Iron-sulfur 1 (4Fe-4S) +P52920 UniProtKB Metal binding 41 41 . . . Note=Iron-sulfur 1 (4Fe-4S) +P52920 UniProtKB Metal binding 44 44 . . . Note=Iron-sulfur 1 (4Fe-4S) +P52920 UniProtKB Metal binding 50 50 . . . Note=Iron-sulfur 1 (4Fe-4S) +P52920 UniProtKB Metal binding 253 253 . . . Note=Iron-sulfur 2 (4Fe-4S)%3B shared with dimeric partner +P52920 UniProtKB Metal binding 256 256 . . . Note=Iron-sulfur 2 (4Fe-4S)%3B shared with dimeric partner +P52920 UniProtKB Mutagenesis 27 27 . . . Note=Supports growth%2C albeit at a lower rate. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766 +P52920 UniProtKB Mutagenesis 41 41 . . . Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766 +P52920 UniProtKB Mutagenesis 44 44 . . . Note=Loss of function. C->A%2CG;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22362766,ECO:0000269|PubMed:9290212;Dbxref=PMID:22362766,PMID:9290212 +P52920 UniProtKB Mutagenesis 50 50 . . . Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766 +P52920 UniProtKB Mutagenesis 86 86 . . . Note=Lethal. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9290212;Dbxref=PMID:9290212 +P52920 UniProtKB Mutagenesis 234 234 . . . Note=Does not impair function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766 +P52920 UniProtKB Mutagenesis 253 253 . . . Note=Loss fo function and disrupts heterotetramer formation. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17401378,ECO:0000269|PubMed:22362766;Dbxref=PMID:17401378,PMID:22362766 +P52920 UniProtKB Mutagenesis 256 256 . . . Note=Loss of function and disrupts heterotetramer formation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766 +P52920 UniProtKB Mutagenesis 295 295 . . . Note=Does not impair function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22362766;Dbxref=PMID:22362766 +P52920 UniProtKB Sequence conflict 58 58 . . . Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P46955 1 337 +P46955 UniProtKB Compositional bias 61 64 . . . Note=Poly-Thr +P46955 UniProtKB Sequence conflict 292 292 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P34160 1 861 +P34160 UniProtKB Chain 1 861 . . . ID=PRO_0000087447;Note=Nuclear cap-binding protein complex subunit 1 +P34160 UniProtKB Domain 36 264 . . . Note=MIF4G +P34160 UniProtKB Motif 22 30 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34160 UniProtKB Compositional bias 774 801 . . . Note=Asp/Glu-rich (acidic) +P34160 UniProtKB Compositional bias 802 825 . . . Note=Arg/Lys-rich (basic) +P34160 UniProtKB Sequence conflict 164 164 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P34160 UniProtKB Sequence conflict 633 633 . . . Note=R->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P34160 UniProtKB Sequence conflict 704 704 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38205 1 684 +P38205 UniProtKB Chain 1 684 . . . ID=PRO_0000211820;Note=Multisite-specific tRNA:(cytosine-C(5))-methyltransferase +P38205 UniProtKB Region 173 179 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023 +P38205 UniProtKB Active site 310 310 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023 +P38205 UniProtKB Binding site 202 202 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023 +P38205 UniProtKB Binding site 229 229 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023 +P38205 UniProtKB Binding site 257 257 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023 +P38205 UniProtKB Modified residue 426 426 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38205 UniProtKB Modified residue 431 431 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38205 UniProtKB Modified residue 667 667 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q07500 1 545 +Q07500 UniProtKB Transit peptide 1 21 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07500 UniProtKB Chain 22 545 . . . ID=PRO_0000268687;Note=External NADH-ubiquinone oxidoreductase 2%2C mitochondrial +Q07500 UniProtKB Nucleotide binding 99 129 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07500 UniProtKB Nucleotide binding 260 296 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q03503 1 176 +Q03503 UniProtKB Chain 1 176 . . . ID=PRO_0000074560;Note=N-alpha-acetyltransferase 30 +Q03503 UniProtKB Domain 3 159 . . . Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532 +##sequence-region P38996 1 802 +P38996 UniProtKB Chain 1 802 . . . ID=PRO_0000081657;Note=Nuclear polyadenylated RNA-binding protein 3 +P38996 UniProtKB Domain 330 401 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P38996 UniProtKB Compositional bias 68 71 . . . Note=Poly-Glu +P38996 UniProtKB Compositional bias 87 93 . . . Note=Poly-Glu +P38996 UniProtKB Compositional bias 101 106 . . . Note=Poly-Asp +P38996 UniProtKB Compositional bias 108 115 . . . Note=Poly-Glu +P38996 UniProtKB Compositional bias 116 127 . . . Note=Poly-Asp +P38996 UniProtKB Compositional bias 128 137 . . . Note=Poly-Glu +P38996 UniProtKB Compositional bias 603 608 . . . Note=Poly-Gln +P38996 UniProtKB Compositional bias 644 648 . . . Note=Poly-Pro +P38996 UniProtKB Compositional bias 698 703 . . . Note=Poly-Gln +P38996 UniProtKB Compositional bias 723 728 . . . Note=Poly-Gln +P38996 UniProtKB Compositional bias 765 768 . . . Note=Poly-Pro +P38996 UniProtKB Compositional bias 769 784 . . . Note=Poly-Gln +P38996 UniProtKB Modified residue 86 86 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38996 UniProtKB Modified residue 451 451 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38996 UniProtKB Sequence conflict 341 341 . . . Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38996 UniProtKB Beta strand 331 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XNQ +P38996 UniProtKB Beta strand 339 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XNR +P38996 UniProtKB Helix 344 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XNQ +P38996 UniProtKB Helix 352 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XNQ +P38996 UniProtKB Beta strand 357 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XNQ +P38996 UniProtKB Beta strand 364 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XNQ +P38996 UniProtKB Helix 374 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XNQ +P38996 UniProtKB Beta strand 387 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XNQ +P38996 UniProtKB Turn 391 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KVI +P38996 UniProtKB Beta strand 395 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XNQ +##sequence-region P38879 1 174 +P38879 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.5;Dbxref=PMID:22814378 +P38879 UniProtKB Chain 2 174 . . . ID=PRO_0000135594;Note=Nascent polypeptide-associated complex subunit alpha +P38879 UniProtKB Domain 15 73 . . . Note=NAC-A/B;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00507 +P38879 UniProtKB Domain 135 174 . . . Note=UBA +P38879 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.5;Dbxref=PMID:22814378 +P38879 UniProtKB Modified residue 93 93 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P23503 1 491 +P23503 UniProtKB Chain 1 491 . . . ID=PRO_0000096718;Note=Cytosolic Fe-S cluster assembly factor NAR1 +P23503 UniProtKB Metal binding 20 20 . . . Note=Iron-sulfur 1 (4Fe-4S);Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23503 UniProtKB Metal binding 59 59 . . . Note=Iron-sulfur 1 (4Fe-4S);Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23503 UniProtKB Metal binding 62 62 . . . Note=Iron-sulfur 1 (4Fe-4S);Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23503 UniProtKB Metal binding 65 65 . . . Note=Iron-sulfur 1 (4Fe-4S);Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23503 UniProtKB Metal binding 177 177 . . . Note=Iron-sulfur 2 (4Fe-4S);Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23503 UniProtKB Metal binding 231 231 . . . Note=Iron-sulfur 2 (4Fe-4S);Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23503 UniProtKB Metal binding 412 412 . . . Note=Iron-sulfur 2 (4Fe-4S);Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23503 UniProtKB Metal binding 416 416 . . . Note=Iron-sulfur 2 (4Fe-4S);Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23503 UniProtKB Mutagenesis 20 20 . . . Note=Weakly reduced iron content and impaired maturation of cytosolic Fe/S proteins. Strongly impaired maturation of cytosolic Fe/S proteins%3B when associated with A-62 or A-65. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19385603;Dbxref=PMID:19385603 +P23503 UniProtKB Mutagenesis 59 59 . . . Note=Reduced iron content and strongly impaired maturation of cytosolic Fe/S proteins. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19385603;Dbxref=PMID:19385603 +P23503 UniProtKB Mutagenesis 62 62 . . . Note=Reduced iron content and strongly impaired maturation of cytosolic Fe/S proteins. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19385603;Dbxref=PMID:19385603 +P23503 UniProtKB Mutagenesis 65 65 . . . Note=Reduced iron content and strongly impaired maturation of cytosolic Fe/S proteins. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19385603;Dbxref=PMID:19385603 +P23503 UniProtKB Mutagenesis 177 177 . . . Note=Impaired maturation of cytosolic Fe/S proteins. Reduced iron content and strongly impaired maturation of cytosolic Fe/S proteins%3B when associated with A-416. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19385603;Dbxref=PMID:19385603 +P23503 UniProtKB Mutagenesis 177 177 . . . Note=Reduced iron content and strongly impaired maturation of cytosolic Fe/S proteins%3B when associated with S-412. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19385603;Dbxref=PMID:19385603 +P23503 UniProtKB Mutagenesis 231 231 . . . Note=Impaired maturation of cytosolic Fe/S proteins. Strongly impaired maturation of cytosolic Fe/S proteins%3B when associated with A-416. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19385603;Dbxref=PMID:19385603 +P23503 UniProtKB Mutagenesis 412 412 . . . Note=Reduced iron content and strongly impaired maturation of cytosolic Fe/S proteins%3B when associated with S-177. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19385603;Dbxref=PMID:19385603 +P23503 UniProtKB Mutagenesis 416 416 . . . Note=Reduced iron content and strongly impaired maturation of cytosolic Fe/S proteins%3B when associated with A-177 or A-231. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19385603;Dbxref=PMID:19385603 +##sequence-region Q3E7Y6 1 73 +Q3E7Y6 UniProtKB Chain 1 73 . . . ID=PRO_0000245397;Note=N-terminal-borealin-like protein +##sequence-region Q12207 1 173 +Q12207 UniProtKB Chain 1 173 . . . ID=PRO_0000096760;Note=Non-classical export protein 2 +Q12207 UniProtKB Topological domain 1 10 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12207 UniProtKB Transmembrane 11 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12207 UniProtKB Topological domain 31 37 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12207 UniProtKB Transmembrane 38 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12207 UniProtKB Topological domain 63 75 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12207 UniProtKB Transmembrane 76 93 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12207 UniProtKB Topological domain 94 137 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12207 UniProtKB Transmembrane 138 157 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12207 UniProtKB Topological domain 158 173 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08887 1 554 +Q08887 UniProtKB Chain 1 554 . . . ID=PRO_0000268686;Note=Nuclear division defective protein 1 +Q08887 UniProtKB Compositional bias 96 113 . . . Note=Gln-rich +Q08887 UniProtKB Compositional bias 493 546 . . . Note=Ser-rich +Q08887 UniProtKB Modified residue 319 319 . . . Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000269|PubMed:12865300;Dbxref=PMID:18407956,PMID:12865300 +Q08887 UniProtKB Mutagenesis 319 319 . . . Note=Growth delay. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12865300;Dbxref=PMID:12865300 +##sequence-region P36010 1 153 +P36010 UniProtKB Chain 1 153 . . . ID=PRO_0000137153;Note=Nucleoside diphosphate kinase +P36010 UniProtKB Active site 119 119 . . . Note=Pros-phosphohistidine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36010 UniProtKB Binding site 13 13 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36010 UniProtKB Binding site 61 61 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36010 UniProtKB Binding site 89 89 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36010 UniProtKB Binding site 95 95 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36010 UniProtKB Binding site 106 106 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36010 UniProtKB Binding site 116 116 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36010 UniProtKB Modified residue 95 95 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36010 UniProtKB Beta strand 7 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54 +P36010 UniProtKB Helix 14 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54 +P36010 UniProtKB Helix 22 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54 +P36010 UniProtKB Beta strand 35 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54 +P36010 UniProtKB Helix 46 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54 +P36010 UniProtKB Helix 63 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54 +P36010 UniProtKB Beta strand 74 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54 +P36010 UniProtKB Helix 84 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54 +P36010 UniProtKB Helix 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54 +P36010 UniProtKB Helix 105 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54 +P36010 UniProtKB Beta strand 117 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54 +P36010 UniProtKB Helix 124 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54 +P36010 UniProtKB Helix 148 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B54 +##sequence-region P25374 1 497 +P25374 UniProtKB Transit peptide 1 33 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25374 UniProtKB Chain 34 497 . . . ID=PRO_0000001304;Note=Cysteine desulfurase%2C mitochondrial +P25374 UniProtKB Region 168 169 . . . Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6B9 +P25374 UniProtKB Region 296 298 . . . Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6B9 +P25374 UniProtKB Active site 421 421 . . . Note=Cysteine persulfide intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6B7 +P25374 UniProtKB Metal binding 421 421 . . . Note=Iron-sulfur (2Fe-2S)%3B via persulfide group;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O29689 +P25374 UniProtKB Binding site 248 248 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O29689 +P25374 UniProtKB Binding site 276 276 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6B9 +P25374 UniProtKB Binding site 336 336 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6B9 +P25374 UniProtKB Modified residue 299 299 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A6B9 +P25374 UniProtKB Mutagenesis 191 191 . . . Note=Exhibits constitutive up-regulation of the genes of the cellular iron uptake system. I->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10551871;Dbxref=PMID:10551871 +P25374 UniProtKB Sequence conflict 150 150 . . . Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q99271 1 985 +Q99271 UniProtKB Chain 1 985 . . . ID=PRO_0000052407;Note=Na(+)/H(+) antiporter +Q99271 UniProtKB Topological domain 1 12 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Transmembrane 13 33 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Topological domain 34 36 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Transmembrane 37 57 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Topological domain 58 70 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Transmembrane 71 91 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Topological domain 92 105 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Transmembrane 106 126 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Topological domain 127 128 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Transmembrane 129 149 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Topological domain 150 176 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Transmembrane 177 197 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Topological domain 198 203 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Transmembrane 204 224 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Topological domain 225 244 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Transmembrane 245 265 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Topological domain 266 294 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Transmembrane 295 315 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Topological domain 316 319 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Transmembrane 320 340 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Topological domain 341 361 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Transmembrane 362 382 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Topological domain 383 410 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Transmembrane 411 431 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Topological domain 432 985 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99271 UniProtKB Modified residue 568 568 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q99271 UniProtKB Modified residue 765 765 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q99271 UniProtKB Modified residue 768 768 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q99271 UniProtKB Modified residue 774 774 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region Q00539 1 523 +Q00539 UniProtKB Chain 1 523 . . . ID=PRO_0000081659;Note=Protein NAM8 +Q00539 UniProtKB Domain 54 145 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q00539 UniProtKB Domain 163 242 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q00539 UniProtKB Domain 313 385 . . . Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q00539 UniProtKB Sequence conflict 180 180 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00539 UniProtKB Sequence conflict 208 209 . . . Note=GF->VL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53914 1 1056 +P53914 UniProtKB Chain 1 1056 . . . ID=PRO_0000215890;Note=RNA cytidine acetyltransferase +P53914 UniProtKB Domain 566 706 . . . Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03211 +P53914 UniProtKB Nucleotide binding 286 295 . . . Note=ATP;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P76562,ECO:0000255|HAMAP-Rule:MF_03211 +P53914 UniProtKB Region 638 640 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P76562,ECO:0000255|HAMAP-Rule:MF_03211 +P53914 UniProtKB Region 645 651 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P76562,ECO:0000255|HAMAP-Rule:MF_03211 +P53914 UniProtKB Binding site 475 475 . . . Note=ATP;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P76562,ECO:0000255|HAMAP-Rule:MF_03211 +P53914 UniProtKB Binding site 739 739 . . . Note=Acetyl-CoA;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P76562,ECO:0000255|HAMAP-Rule:MF_03211 +P53914 UniProtKB Modified residue 1001 1001 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53914 UniProtKB Modified residue 1007 1007 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53914 UniProtKB Modified residue 1010 1010 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53914 UniProtKB Mutagenesis 289 289 . . . Note=Reduces 18S rRNA acetylation by 80%25 and tRNA acetylation by 47%25. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25653167;Dbxref=PMID:25653167 +P53914 UniProtKB Mutagenesis 545 545 . . . Note=Total loss of 18S rRNA acetylation and tRNA acetylation. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25653167;Dbxref=PMID:25653167 +P53914 UniProtKB Mutagenesis 637 637 . . . Note=Total loss of 18S rRNA acetylation and tRNA acetylation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25653167;Dbxref=PMID:25653167 +##sequence-region P40096 1 142 +P40096 UniProtKB Chain 1 142 . . . ID=PRO_0000096755;Note=Negative cofactor 2 complex subunit alpha +P40096 UniProtKB Domain 29 137 . . . Note=Histone-fold +P40096 UniProtKB Compositional bias 35 40 . . . Note=Poly-Asn +P40096 UniProtKB Modified residue 27 27 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40096 UniProtKB Modified residue 141 141 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P32500 1 655 +P32500 UniProtKB Chain 1 655 . . . ID=PRO_0000204862;Note=Nucleoporin NDC1 +P32500 UniProtKB Topological domain 1 33 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P32500 UniProtKB Transmembrane 34 54 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32500 UniProtKB Topological domain 55 58 . . . Note=Perinuclear space;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P32500 UniProtKB Transmembrane 59 79 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32500 UniProtKB Topological domain 80 88 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P32500 UniProtKB Transmembrane 89 108 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32500 UniProtKB Topological domain 109 109 . . . Note=Perinuclear space;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P32500 UniProtKB Transmembrane 110 130 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32500 UniProtKB Topological domain 131 190 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P32500 UniProtKB Transmembrane 191 211 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32500 UniProtKB Topological domain 212 224 . . . Note=Perinuclear space;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P32500 UniProtKB Transmembrane 225 245 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32500 UniProtKB Topological domain 246 655 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +P32500 UniProtKB Modified residue 401 401 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32500 UniProtKB Modified residue 412 412 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40460 1 691 +P40460 UniProtKB Chain 1 691 . . . ID=PRO_0000202958;Note=Kinetochore protein NDC80 +P40460 UniProtKB Coiled coil 376 446 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40460 UniProtKB Coiled coil 522 686 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40460 UniProtKB Modified residue 38 38 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40460 UniProtKB Modified residue 248 248 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40460 UniProtKB Mutagenesis 201 201 . . . Note=Loss of function. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12386167;Dbxref=PMID:12386167 +P40460 UniProtKB Helix 122 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P40460 UniProtKB Helix 141 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P40460 UniProtKB Helix 159 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P40460 UniProtKB Helix 184 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P40460 UniProtKB Helix 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P40460 UniProtKB Helix 204 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P40460 UniProtKB Helix 215 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P40460 UniProtKB Turn 261 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P40460 UniProtKB Helix 267 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P40460 UniProtKB Helix 298 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P40460 UniProtKB Helix 621 679 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +##sequence-region P32831 1 672 +P32831 UniProtKB Chain 1 672 . . . ID=PRO_0000081660;Note=Negative growth regulatory protein NGR1 +P32831 UniProtKB Domain 36 159 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P32831 UniProtKB Domain 192 271 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P32831 UniProtKB Domain 360 432 . . . Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P32831 UniProtKB Compositional bias 278 295 . . . Note=Gln-rich +P32831 UniProtKB Compositional bias 485 495 . . . Note=Poly-Gln +P32831 UniProtKB Compositional bias 566 672 . . . Note=Asn/Met-rich +P32831 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32831 UniProtKB Modified residue 524 524 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198 +P32831 UniProtKB Alternative sequence 1 1 . . . ID=VSP_058122;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32831 UniProtKB Sequence conflict 322 322 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32831 UniProtKB Sequence conflict 568 568 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32831 UniProtKB Sequence conflict 585 585 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32340 1 513 +P32340 UniProtKB Transit peptide 1 26 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1735444;Dbxref=PMID:1735444 +P32340 UniProtKB Chain 27 513 . . . ID=PRO_0000021793;Note=Rotenone-insensitive NADH-ubiquinone oxidoreductase%2C mitochondrial +P32340 UniProtKB Nucleotide binding 55 85 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32340 UniProtKB Nucleotide binding 229 265 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32340 UniProtKB Natural variant 10 10 . . . Note=K->R +P32340 UniProtKB Beta strand 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 50 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6G +P32340 UniProtKB Beta strand 55 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Helix 63 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Turn 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 78 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Helix 91 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Turn 97 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Helix 104 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 108 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Helix 111 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 122 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Helix 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 138 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 165 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 170 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6G +P32340 UniProtKB Helix 188 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 193 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6G +P32340 UniProtKB Helix 198 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Helix 223 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 230 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Helix 238 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Helix 255 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Helix 260 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 267 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 273 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Helix 283 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 299 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 304 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 311 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 321 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G74 +P32340 UniProtKB Beta strand 325 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 333 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 341 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6G +P32340 UniProtKB Helix 345 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Helix 355 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 362 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 370 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 376 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Helix 382 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 385 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Helix 393 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Helix 414 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 422 424 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Helix 427 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 445 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 455 461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Beta strand 464 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Helix 472 485 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +P32340 UniProtKB Helix 489 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G6H +##sequence-region P39744 1 710 +P39744 UniProtKB Chain 1 710 . . . ID=PRO_0000121054;Note=Nucleolar complex protein 2 +P39744 UniProtKB Compositional bias 101 104 . . . Note=Poly-Ser +P39744 UniProtKB Compositional bias 105 108 . . . Note=Poly-Glu +P39744 UniProtKB Modified residue 70 70 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P39744 UniProtKB Modified residue 149 149 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P39744 UniProtKB Modified residue 160 160 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P39744 UniProtKB Modified residue 166 166 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P39744 UniProtKB Modified residue 698 698 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P39744 UniProtKB Modified residue 708 708 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P39744 UniProtKB Sequence conflict 151 179 . . . Note=DEGEDAERNSNIEEKSEQMELEKEKIELS->MKVKMLKETVILKKNLNKWSWKRKKLSFL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39744 UniProtKB Sequence conflict 231 232 . . . Note=FH->LD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39744 UniProtKB Sequence conflict 333 333 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39744 UniProtKB Sequence conflict 360 362 . . . Note=TTY->QRT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39744 UniProtKB Sequence conflict 542 542 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39744 UniProtKB Sequence conflict 707 710 . . . Note=MSDA->NVRRLTTQQDLIFCLEFNSIVYKCVNKRKVFFKAYISLCSHVLTCEHSKLSLVSWIFLYFGRFMDRKHVKRSMDLIKSNDVKQGTKMKEVRFTVIKFSKSFNSLKVPHEIDMIANITENFSTRYMISYCWKISSNLNLGAMFMDNNSWNNSFAAYGIVILIIFSALLQVVHQPL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25353 1 742 +P25353 UniProtKB Chain 1 742 . . . ID=PRO_0000202566;Note=Ectonucleotide pyrophosphatase/phosphodiesterase 1 +P25353 UniProtKB Topological domain 1 113 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25353 UniProtKB Transmembrane 114 134 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25353 UniProtKB Topological domain 135 742 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25353 UniProtKB Region 168 545 . . . Note=Phosphodiesterase +P25353 UniProtKB Compositional bias 692 702 . . . Note=Poly-Ser +P25353 UniProtKB Active site 219 219 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25353 UniProtKB Glycosylation 161 161 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25353 UniProtKB Glycosylation 204 204 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25353 UniProtKB Glycosylation 264 264 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25353 UniProtKB Glycosylation 296 296 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25353 UniProtKB Glycosylation 403 403 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53718 1 249 +P53718 UniProtKB Chain 1 249 . . . ID=PRO_0000203470;Note=Transcription factor NRM1 +P53718 UniProtKB Modified residue 145 145 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q08485 1 598 +Q08485 UniProtKB Chain 1 598 . . . ID=PRO_0000197927;Note=Nicotinamide riboside transporter 1 +Q08485 UniProtKB Transmembrane 48 68 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08485 UniProtKB Transmembrane 71 91 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08485 UniProtKB Transmembrane 112 132 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08485 UniProtKB Transmembrane 174 194 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08485 UniProtKB Transmembrane 197 217 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08485 UniProtKB Transmembrane 241 261 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08485 UniProtKB Transmembrane 273 293 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08485 UniProtKB Transmembrane 372 392 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08485 UniProtKB Transmembrane 395 415 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08485 UniProtKB Transmembrane 447 467 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08485 UniProtKB Transmembrane 484 504 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08485 UniProtKB Modified residue 560 560 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08485 UniProtKB Modified residue 572 572 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38632 1 267 +P38632 UniProtKB Chain 1 267 . . . ID=PRO_0000218991;Note=E3 SUMO-protein ligase MMS21 +P38632 UniProtKB Zinc finger 169 246 . . . Note=SP-RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00452 +P38632 UniProtKB Sequence conflict 124 124 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38632 UniProtKB Helix 16 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +P38632 UniProtKB Helix 19 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +P38632 UniProtKB Helix 31 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +P38632 UniProtKB Helix 60 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +P38632 UniProtKB Helix 108 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +P38632 UniProtKB Beta strand 115 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +P38632 UniProtKB Helix 122 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +P38632 UniProtKB Helix 142 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +P38632 UniProtKB Beta strand 177 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +P38632 UniProtKB Turn 185 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +P38632 UniProtKB Beta strand 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +P38632 UniProtKB Beta strand 192 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +P38632 UniProtKB Beta strand 203 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +P38632 UniProtKB Helix 206 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +P38632 UniProtKB Helix 223 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +P38632 UniProtKB Helix 232 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +P38632 UniProtKB Beta strand 235 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +P38632 UniProtKB Helix 239 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +##sequence-region Q05541 1 303 +Q05541 UniProtKB Chain 1 303 . . . ID=PRO_0000057962;Note=Non-structural maintenance of chromosome element 3 +##sequence-region P53898 1 299 +P53898 UniProtKB Chain 1 299 . . . ID=PRO_0000203417;Note=Protein NSG2 +P53898 UniProtKB Topological domain 1 108 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53898 UniProtKB Transmembrane 109 129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53898 UniProtKB Topological domain 130 161 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53898 UniProtKB Transmembrane 162 182 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53898 UniProtKB Topological domain 183 237 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53898 UniProtKB Transmembrane 238 258 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53898 UniProtKB Topological domain 259 268 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53898 UniProtKB Transmembrane 269 289 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53898 UniProtKB Topological domain 290 299 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53898 UniProtKB Modified residue 90 90 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region Q12457 1 570 +Q12457 UniProtKB Chain 1 570 . . . ID=PRO_0000242620;Note=RNA polymerase I termination factor +Q12457 UniProtKB Domain 273 339 . . . Note=Myb-like 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00133 +Q12457 UniProtKB Domain 340 391 . . . Note=HTH myb-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +Q12457 UniProtKB Domain 392 486 . . . Note=Myb-like 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00133 +Q12457 UniProtKB Domain 493 549 . . . Note=Myb-like 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00133 +Q12457 UniProtKB DNA binding 367 389 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +Q12457 UniProtKB Compositional bias 35 138 . . . Note=Lys-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00012 +Q12457 UniProtKB Modified residue 64 64 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P36052 1 402 +P36052 UniProtKB Chain 1 402 . . . ID=PRO_0000203142;Note=Protein arginine methyltransferase NDUFAF7 homolog%2C mitochondrial +##sequence-region Q06148 1 342 +Q06148 UniProtKB Chain 1 342 . . . ID=PRO_0000268689;Note=Non-homologous end-joining protein 1 +Q06148 UniProtKB Transmembrane 27 47 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06148 UniProtKB Transmembrane 129 149 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06148 UniProtKB Natural variant 17 17 . . . Note=In strain: DBVPG1135%2C DBVPG1373%2C DBVPG1378%2C DBVPG1788%2C DBVPG1794%2C DBVPG1853%2C DBVPG3051%2C DBVPG6044%2C DBVPG6763%2C DBVPG6765%2C SK1%2C Y55 and YPS128. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060 +Q06148 UniProtKB Natural variant 21 21 . . . Note=In strain: DBVPG1135%2C DBVPG1373%2C DBVPG1378%2C DBVPG1788%2C DBVPG1794%2C DBVPG1853%2C DBVPG3051%2C DBVPG6763%2C DBVPG6765 and SK1. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060 +Q06148 UniProtKB Natural variant 65 65 . . . Note=In strain: YPS128. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060 +Q06148 UniProtKB Natural variant 105 105 . . . Note=In strain: YPS128. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060 +Q06148 UniProtKB Natural variant 161 161 . . . Note=In strain: DBVPG1135%2C DBVPG1373%2C DBVPG1378%2C DBVPG1788%2C DBVPG1794%2C DBVPG1853%2C DBVPG3051%2C DBVPG6763%2C DBVPG6765 and SK1. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060 +Q06148 UniProtKB Natural variant 204 204 . . . Note=In strain: DBVPG6044 and Y55. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060 +Q06148 UniProtKB Natural variant 231 231 . . . Note=In strain: DBVPG1135%2C DBVPG1373%2C DBVPG1378%2C DBVPG1788%2C DBVPG1794%2C DBVPG1853%2C DBVPG3051%2C DBVPG6763%2C DBVPG6765 and SK1. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060 +Q06148 UniProtKB Natural variant 249 249 . . . Note=In strain: DBVPG1135%2C DBVPG1373%2C DBVPG1378%2C DBVPG1788%2C DBVPG1794%2C DBVPG1853%2C DBVPG3051%2C DBVPG6763%2C DBVPG6765 and SK1. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060 +Q06148 UniProtKB Natural variant 270 270 . . . Note=In strain: DBVPG1135%2C DBVPG1373%2C DBVPG1378%2C DBVPG1788%2C DBVPG1794%2C DBVPG1853%2C DBVPG3051%2C DBVPG6763%2C DBVPG6765 and SK1. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060 +Q06148 UniProtKB Natural variant 281 281 . . . Note=In strain: DBVPG1135%2C DBVPG1373%2C DBVPG1378%2C DBVPG1788%2C DBVPG1794%2C DBVPG1853%2C DBVPG3051%2C DBVPG6763%2C DBVPG6765 and SK1. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16951060;Dbxref=PMID:16951060 +##sequence-region P25382 1 515 +P25382 UniProtKB Chain 1 515 . . . ID=PRO_0000051471;Note=Ribosome assembly protein 4 +P25382 UniProtKB Repeat 141 181 . . . Note=WD 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25382 UniProtKB Repeat 184 223 . . . Note=WD 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25382 UniProtKB Repeat 227 273 . . . Note=WD 3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25382 UniProtKB Repeat 276 314 . . . Note=WD 4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25382 UniProtKB Repeat 352 396 . . . Note=WD 5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25382 UniProtKB Repeat 400 439 . . . Note=WD 6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25382 UniProtKB Repeat 442 481 . . . Note=WD 7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25382 UniProtKB Repeat 484 515 . . . Note=WD 8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25382 UniProtKB Region 20 128 . . . Note=Interaction with MDN1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19737519;Dbxref=PMID:19737519 +P25382 UniProtKB Mutagenesis 114 114 . . . Note=Impairs interaction with MDN1. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19737519;Dbxref=PMID:19737519 +P25382 UniProtKB Mutagenesis 114 114 . . . Note=Impairs interaction with MDN1. Blocks progression of the nascent pre-60S subunit and subsequent export to the cytoplasm. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19737519;Dbxref=PMID:19737519 +P25382 UniProtKB Beta strand 34 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Helix 57 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 77 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Helix 103 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 117 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 146 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 156 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 168 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Turn 173 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 177 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 189 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 201 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 210 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Turn 215 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 232 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Helix 240 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 251 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 260 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Turn 265 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 269 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 281 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 290 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 301 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Helix 306 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 312 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 323 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Helix 331 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Helix 349 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 365 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 374 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 383 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Turn 388 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 395 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 405 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 414 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 426 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Turn 431 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 436 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 447 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 456 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 466 472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Turn 473 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 477 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 489 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 500 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +P25382 UniProtKB Beta strand 510 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJU +##sequence-region P38798 1 1089 +P38798 UniProtKB Chain 1 1089 . . . ID=PRO_0000096873;Note=Nonsense-mediated mRNA decay protein 2 +P38798 UniProtKB Compositional bias 843 975 . . . Note=Asp/Glu-rich (highly acidic) +P38798 UniProtKB Sequence conflict 2 2 . . . Note=D->YQQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38798 UniProtKB Sequence conflict 2 2 . . . Note=D->YQQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38798 UniProtKB Helix 3 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN +P38798 UniProtKB Helix 34 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN +P38798 UniProtKB Helix 52 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN +P38798 UniProtKB Helix 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN +P38798 UniProtKB Helix 69 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN +P38798 UniProtKB Helix 87 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN +P38798 UniProtKB Helix 106 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN +P38798 UniProtKB Helix 117 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN +P38798 UniProtKB Helix 130 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN +P38798 UniProtKB Helix 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN +P38798 UniProtKB Helix 170 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN +P38798 UniProtKB Helix 182 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN +P38798 UniProtKB Helix 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN +P38798 UniProtKB Helix 201 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN +P38798 UniProtKB Helix 212 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN +P38798 UniProtKB Helix 223 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN +P38798 UniProtKB Helix 231 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN +P38798 UniProtKB Helix 277 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LUN +##sequence-region P47149 1 201 +P47149 UniProtKB Chain 1 201 . . . ID=PRO_0000096885;Note=Kinetochore-associated protein NNF1 +P47149 UniProtKB Sequence conflict 55 55 . . . Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47149 UniProtKB Sequence conflict 89 89 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47149 UniProtKB Sequence conflict 152 152 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47149 UniProtKB Sequence conflict 164 165 . . . Note=NE->KQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47149 UniProtKB Sequence conflict 193 193 . . . Note=M->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36059 1 337 +P36059 UniProtKB Chain 1 337 . . . ID=PRO_0000119053;Note=ATP-dependent (S)-NAD(P)H-hydrate dehydratase +P36059 UniProtKB Domain 11 335 . . . Note=YjeF C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03157 +P36059 UniProtKB Nucleotide binding 218 222 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03157 +P36059 UniProtKB Nucleotide binding 240 249 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03157 +P36059 UniProtKB Region 182 188 . . . Note=NAD(P)HX;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03157 +P36059 UniProtKB Binding site 121 121 . . . Note=NAD(P)HX%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03157 +P36059 UniProtKB Binding site 250 250 . . . Note=NAD(P)HX;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03157 +P36059 UniProtKB Modified residue 6 6 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36059 UniProtKB Sequence conflict 182 182 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40165 1 246 +P40165 UniProtKB Chain 1 246 . . . ID=PRO_0000119061;Note=NAD(P)H-hydrate epimerase +P40165 UniProtKB Domain 12 234 . . . Note=YjeF N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03159 +P40165 UniProtKB Region 69 73 . . . Note=NAD(P)HX;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03159 +P40165 UniProtKB Region 142 148 . . . Note=NAD(P)HX;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03159 +P40165 UniProtKB Metal binding 70 70 . . . Note=Potassium;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03159 +P40165 UniProtKB Metal binding 138 138 . . . Note=Potassium;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03159 +P40165 UniProtKB Metal binding 176 176 . . . Note=Potassium;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03159 +P40165 UniProtKB Binding site 173 173 . . . Note=NAD(P)HX;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03159 +P40165 UniProtKB Helix 9 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Turn 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Helix 28 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Helix 54 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Beta strand 60 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Helix 69 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Beta strand 88 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Helix 100 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Helix 124 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Turn 130 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Beta strand 133 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Helix 153 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Turn 164 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Beta strand 169 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Turn 180 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Beta strand 186 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Beta strand 193 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Helix 203 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Turn 210 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Beta strand 214 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Helix 224 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +P40165 UniProtKB Beta strand 242 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JZT +##sequence-region Q06162 1 153 +Q06162 UniProtKB Chain 1 153 . . . ID=PRO_0000096868;Note=Central kinetochore subunit NKP2 +Q06162 UniProtKB Coiled coil 86 128 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P48234 1 707 +P48234 UniProtKB Chain 1 707 . . . ID=PRO_0000051473;Note=Ribosome biogenesis protein ENP2 +P48234 UniProtKB Repeat 54 94 . . . Note=WD 1 +P48234 UniProtKB Repeat 178 217 . . . Note=WD 2 +P48234 UniProtKB Repeat 226 265 . . . Note=WD 3 +P48234 UniProtKB Repeat 269 310 . . . Note=WD 4 +P48234 UniProtKB Repeat 312 351 . . . Note=WD 5 +P48234 UniProtKB Modified residue 529 529 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P48234 UniProtKB Modified residue 550 550 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P48234 UniProtKB Modified residue 555 555 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P48234 UniProtKB Sequence conflict 678 678 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P48234 UniProtKB Sequence conflict 678 678 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07623 1 225 +Q07623 UniProtKB Chain 1 225 . . . ID=PRO_0000268691;Note=Nucleolar protein 6 +Q07623 UniProtKB Domain 78 155 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q07623 UniProtKB Compositional bias 7 74 . . . Note=Lys-rich +Q07623 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q07623 UniProtKB Modified residue 160 160 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07623 UniProtKB Beta strand 77 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ +Q07623 UniProtKB Helix 91 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ +Q07623 UniProtKB Turn 99 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ +Q07623 UniProtKB Beta strand 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ +Q07623 UniProtKB Helix 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ +Q07623 UniProtKB Beta strand 114 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ +Q07623 UniProtKB Helix 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ +Q07623 UniProtKB Turn 125 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ +Q07623 UniProtKB Helix 128 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ +Q07623 UniProtKB Turn 137 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ +Q07623 UniProtKB Beta strand 149 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MZJ +##sequence-region P38082 1 220 +P38082 UniProtKB Chain 1 220 . . . ID=PRO_0000046813;Note=Probable transcriptional regulator NRG2 +P38082 UniProtKB Zinc finger 153 175 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P38082 UniProtKB Zinc finger 181 205 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +##sequence-region P27476 1 414 +P27476 UniProtKB Chain 1 414 . . . ID=PRO_0000081690;Note=Nuclear localization sequence-binding protein +P27476 UniProtKB Domain 168 246 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P27476 UniProtKB Domain 267 345 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P27476 UniProtKB Region 353 384 . . . Note=RGG-box +P27476 UniProtKB Region 366 384 . . . Note=RNA-binding RGG-box;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P27476 UniProtKB Compositional bias 29 136 . . . Note=Asp/Glu/Ser-rich +P27476 UniProtKB Modified residue 353 353 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P27476 UniProtKB Modified residue 362 362 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P27476 UniProtKB Modified residue 366 366 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P27476 UniProtKB Modified residue 375 375 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P27476 UniProtKB Modified residue 379 379 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +P27476 UniProtKB Modified residue 382 382 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12756332;Dbxref=PMID:12756332 +##sequence-region Q08214 1 380 +Q08214 UniProtKB Chain 1 380 . . . ID=PRO_0000102238;Note=Endonuclease III homolog 2 +Q08214 UniProtKB Domain 228 252 . . . Note=HhH;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183 +Q08214 UniProtKB Region 15 40 . . . Note=Interaction with MLH1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12042306;Dbxref=PMID:12042306 +Q08214 UniProtKB Motif 8 12 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08214 UniProtKB Motif 376 380 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08214 UniProtKB Active site 248 248 . . . Note=Nucleophile%3B for N-glycosylase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183 +Q08214 UniProtKB Metal binding 319 319 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183 +Q08214 UniProtKB Metal binding 326 326 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183 +Q08214 UniProtKB Metal binding 329 329 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183 +Q08214 UniProtKB Metal binding 335 335 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183 +Q08214 UniProtKB Site 267 267 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183 +Q08214 UniProtKB Cross-link 194 194 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08214 UniProtKB Mutagenesis 24 24 . . . Note=Abolishes interaction with MLH1. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12042306;Dbxref=PMID:12042306 +Q08214 UniProtKB Mutagenesis 26 26 . . . Note=Abolishes interaction with MLH1. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12042306;Dbxref=PMID:12042306 +Q08214 UniProtKB Mutagenesis 27 27 . . . Note=Abolishes interaction with MLH1. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12042306;Dbxref=PMID:12042306 +##sequence-region P40215 1 560 +P40215 UniProtKB Transit peptide 1 41 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40215 UniProtKB Chain 42 560 . . . ID=PRO_0000203306;Note=External NADH-ubiquinone oxidoreductase 1%2C mitochondrial +P40215 UniProtKB Nucleotide binding 114 144 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40215 UniProtKB Nucleotide binding 275 311 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q03210 1 505 +Q03210 UniProtKB Chain 1 505 . . . ID=PRO_0000218580;Note=Probable RNA exonuclease NGL3 +Q03210 UniProtKB Modified residue 62 62 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +##sequence-region P32495 1 156 +P32495 UniProtKB Chain 1 156 . . . ID=PRO_0000136776;Note=H/ACA ribonucleoprotein complex subunit 2 +P32495 UniProtKB Mutagenesis 56 56 . . . Note=No effect. V->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11433018;Dbxref=PMID:11433018 +P32495 UniProtKB Mutagenesis 59 59 . . . Note=Significant growth impairment at 30 and 37 degrees Celsius. Impaired association with H/ACA snoRNAs. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11433018;Dbxref=PMID:11433018 +P32495 UniProtKB Mutagenesis 68 68 . . . Note=No effect. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11433018;Dbxref=PMID:11433018 +P32495 UniProtKB Mutagenesis 76 77 . . . Note=Lethal. Impaired association with H/ACA snoRNAs. Accumulation of NHP2 within the nucleolus. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11433018;Dbxref=PMID:11433018 +P32495 UniProtKB Mutagenesis 80 80 . . . Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11433018;Dbxref=PMID:11433018 +P32495 UniProtKB Helix 37 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW +P32495 UniProtKB Turn 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW +P32495 UniProtKB Beta strand 56 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW +P32495 UniProtKB Helix 60 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW +P32495 UniProtKB Beta strand 74 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW +P32495 UniProtKB Helix 86 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW +P32495 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW +P32495 UniProtKB Helix 107 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW +P32495 UniProtKB Beta strand 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBX +P32495 UniProtKB Beta strand 121 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW +P32495 UniProtKB Helix 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW +P32495 UniProtKB Beta strand 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBX +P32495 UniProtKB Helix 139 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LBW +##sequence-region Q04121 1 633 +Q04121 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Chain 22 633 . . . ID=PRO_0000052380;Note=Endosomal/prevacuolar sodium/hydrogen exchanger +Q04121 UniProtKB Topological domain 22 61 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Transmembrane 62 82 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Topological domain 83 85 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Transmembrane 86 106 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Topological domain 107 117 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Transmembrane 118 138 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Topological domain 139 152 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Transmembrane 153 173 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Topological domain 174 189 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Transmembrane 190 211 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Topological domain 212 217 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Transmembrane 218 238 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Topological domain 239 258 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Transmembrane 259 279 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Topological domain 280 288 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Transmembrane 289 308 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Topological domain 309 313 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Transmembrane 314 333 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Topological domain 334 344 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Transmembrane 345 364 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Topological domain 365 376 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Transmembrane 377 397 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Topological domain 398 431 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Transmembrane 432 452 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Topological domain 453 457 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Transmembrane 458 478 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Motif 124 133 . . . Note=Amiloride-binding +Q04121 UniProtKB Compositional bias 23 50 . . . Note=Asp-rich +Q04121 UniProtKB Modified residue 490 490 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04121 UniProtKB Modified residue 494 494 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04121 UniProtKB Modified residue 498 498 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04121 UniProtKB Modified residue 499 499 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04121 UniProtKB Modified residue 569 569 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04121 UniProtKB Glycosylation 420 420 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04121 UniProtKB Glycosylation 515 515 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11036065;Dbxref=PMID:11036065 +Q04121 UniProtKB Glycosylation 550 550 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11036065;Dbxref=PMID:11036065 +Q04121 UniProtKB Glycosylation 563 563 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11036065;Dbxref=PMID:11036065 +Q04121 UniProtKB Mutagenesis 201 201 . . . Note=Impairs protein-trafficking to the vacuole. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11102523;Dbxref=PMID:11102523 +Q04121 UniProtKB Mutagenesis 225 225 . . . Note=Impairs protein-trafficking to the vacuole. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11102523;Dbxref=PMID:11102523 +Q04121 UniProtKB Mutagenesis 230 230 . . . Note=Impairs protein-trafficking to the vacuole. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11102523;Dbxref=PMID:11102523 +Q04121 UniProtKB Mutagenesis 355 355 . . . Note=Impairs partially resistance to osmotic stress and hygromycin. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16671892;Dbxref=PMID:16671892 +Q04121 UniProtKB Mutagenesis 357 357 . . . Note=Impairs resistance to osmotic stress and hygromycin%2C and blocks protein-trafficking to the vacuole. F->A%2CL%2CI;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16671892;Dbxref=PMID:16671892 +Q04121 UniProtKB Mutagenesis 357 357 . . . Note=Impairs partially resistance to osmotic stress and hygromycin. F->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16671892;Dbxref=PMID:16671892 +Q04121 UniProtKB Mutagenesis 361 361 . . . Note=Impairs resistance to osmotic stress and hygromycin%2C and blocks protein-trafficking to the vacuole. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16671892;Dbxref=PMID:16671892 +Q04121 UniProtKB Mutagenesis 365 365 . . . Note=Impairs resistance to osmotic stress and hygromycin%2C and blocks protein-trafficking to the vacuole. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16671892;Dbxref=PMID:16671892 +Q04121 UniProtKB Mutagenesis 369 369 . . . Note=Impairs partially resistance to osmotic stress and hygromycin. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16671892;Dbxref=PMID:16671892 +Q04121 UniProtKB Mutagenesis 376 376 . . . Note=Impairs resistance to osmotic stress and hygromycin. P->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16671892;Dbxref=PMID:16671892 +##sequence-region P34077 1 839 +P34077 UniProtKB Chain 1 839 . . . ID=PRO_0000124787;Note=Nucleoporin NIC96 +P34077 UniProtKB Region 25 60 . . . Note=Leucine zipper-like heptad repeat%2C required for interaction with NSP1 +P34077 UniProtKB Compositional bias 187 236 . . . Note=Asn-rich +P34077 UniProtKB Sequence conflict 59 59 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P34077 UniProtKB Helix 206 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 234 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 248 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Turn 262 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 270 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 301 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Beta strand 312 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Beta strand 316 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Beta strand 320 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 333 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Turn 342 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 346 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 357 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 367 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Turn 375 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RFO +P34077 UniProtKB Beta strand 384 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RFO +P34077 UniProtKB Helix 388 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RFO +P34077 UniProtKB Turn 398 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RFO +P34077 UniProtKB Beta strand 402 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RFO +P34077 UniProtKB Helix 406 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 420 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 426 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 432 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Beta strand 449 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RFO +P34077 UniProtKB Helix 459 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 471 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 478 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 488 496 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 500 512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 534 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Turn 543 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 550 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 559 562 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 566 583 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 586 590 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Beta strand 595 597 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RFO +P34077 UniProtKB Helix 603 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 609 611 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 616 633 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 637 646 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 650 667 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Beta strand 675 679 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RFO +P34077 UniProtKB Turn 681 683 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 685 696 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 700 703 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 708 728 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 732 741 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 750 753 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RFO +P34077 UniProtKB Helix 754 759 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 760 762 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 765 768 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 771 790 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 799 819 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 820 823 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +P34077 UniProtKB Helix 826 833 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QX5 +##sequence-region P32770 1 719 +P32770 UniProtKB Chain 1 719 . . . ID=PRO_0000081689;Note=Asparagine-rich protein +P32770 UniProtKB Domain 226 322 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P32770 UniProtKB Zinc finger 355 384 . . . Note=RanBP2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00322 +P32770 UniProtKB Zinc finger 581 610 . . . Note=RanBP2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00322 +P32770 UniProtKB Compositional bias 490 564 . . . Note=Asn-rich +P32770 UniProtKB Modified residue 345 345 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:18407956 +P32770 UniProtKB Modified residue 455 455 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P32770 UniProtKB Modified residue 630 630 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32770 UniProtKB Sequence conflict 493 493 . . . Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12181 1 623 +Q12181 UniProtKB Chain 1 623 . . . ID=PRO_0000167624;Note=NADPH-dependent diflavin oxidoreductase 1 +Q12181 UniProtKB Domain 7 168 . . . Note=Flavodoxin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178 +Q12181 UniProtKB Domain 224 491 . . . Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178 +Q12181 UniProtKB Nucleotide binding 13 18 . . . Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178 +Q12181 UniProtKB Nucleotide binding 60 63 . . . Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178 +Q12181 UniProtKB Nucleotide binding 106 115 . . . Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178 +Q12181 UniProtKB Nucleotide binding 413 416 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178 +Q12181 UniProtKB Nucleotide binding 445 448 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178 +Q12181 UniProtKB Nucleotide binding 538 539 . . . Note=NADP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178 +Q12181 UniProtKB Binding site 142 142 . . . Note=FMN;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178 +Q12181 UniProtKB Binding site 383 383 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178 +Q12181 UniProtKB Binding site 623 623 . . . Note=FAD;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03178 +##sequence-region P53317 1 196 +P53317 UniProtKB Chain 1 196 . . . ID=PRO_0000202860;Note=Nucleolar protein 19 +##sequence-region P37838 1 685 +P37838 UniProtKB Chain 1 685 . . . ID=PRO_0000081677;Note=Nucleolar protein 4 +P37838 UniProtKB Domain 26 103 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P37838 UniProtKB Domain 147 225 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P37838 UniProtKB Domain 290 383 . . . Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P37838 UniProtKB Domain 462 612 . . . Note=RRM 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P37838 UniProtKB Compositional bias 241 267 . . . Note=Asp/Glu-rich (acidic) +P37838 UniProtKB Modified residue 247 247 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P37838 UniProtKB Modified residue 379 379 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P37838 UniProtKB Natural variant 308 308 . . . Note=P->A +##sequence-region Q12080 1 455 +Q12080 UniProtKB Chain 1 455 . . . ID=PRO_0000218965;Note=Ribosome biogenesis protein NOP53 +Q12080 UniProtKB Compositional bias 273 276 . . . Note=Poly-Glu +Q12080 UniProtKB Compositional bias 281 293 . . . Note=Poly-Glu +Q12080 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P33755 1 580 +P33755 UniProtKB Chain 1 580 . . . ID=PRO_0000057944;Note=Nuclear protein localization protein 4 +P33755 UniProtKB Domain 237 377 . . . Note=MPN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182 +P33755 UniProtKB Mutagenesis 323 323 . . . Note=In npl4-1%3B nuclear-targeted proteins accumulate in the cytoplasm. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11598205;Dbxref=PMID:11598205 +##sequence-region P22211 1 790 +P22211 UniProtKB Chain 1 790 . . . ID=PRO_0000086445;Note=Nitrogen permease reactivator protein +P22211 UniProtKB Domain 438 742 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P22211 UniProtKB Nucleotide binding 444 452 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P22211 UniProtKB Compositional bias 1 339 . . . Note=Ser-rich (may play a regulatory role) +P22211 UniProtKB Compositional bias 51 58 . . . Note=Poly-Ser +P22211 UniProtKB Compositional bias 782 786 . . . Note=Poly-Lys +P22211 UniProtKB Active site 561 561 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P22211 UniProtKB Binding site 467 467 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P22211 UniProtKB Modified residue 47 47 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Modified residue 90 90 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Modified residue 100 100 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Modified residue 111 111 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Modified residue 125 125 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18980262;Dbxref=PMID:17330950,PMID:19779198,PMID:18980262 +P22211 UniProtKB Modified residue 137 137 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18980262;Dbxref=PMID:19779198,PMID:18980262 +P22211 UniProtKB Modified residue 141 141 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:18980262;Dbxref=PMID:19779198,PMID:18980262 +P22211 UniProtKB Modified residue 257 257 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Modified residue 259 259 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Modified residue 260 260 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Modified residue 288 288 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Modified residue 292 292 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Modified residue 317 317 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Modified residue 320 320 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Modified residue 328 328 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Modified residue 334 334 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P22211 UniProtKB Modified residue 336 336 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Modified residue 353 353 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Modified residue 356 356 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Modified residue 357 357 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000269|PubMed:18980262;Dbxref=PMID:17330950,PMID:18980262 +P22211 UniProtKB Modified residue 385 385 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Mutagenesis 47 47 . . . Note=Abolishes autophosphorylation%3B when associated with A-257 and A-357. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Mutagenesis 257 257 . . . Note=Abolishes autophosphorylation%3B when associated with A-47 and A-357. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Mutagenesis 257 257 . . . Note=Abolishes autophosphorylation. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Mutagenesis 357 357 . . . Note=Abolishes autophosphorylation%3B when associated with A-47 and A-257. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 +P22211 UniProtKB Sequence conflict 154 154 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22211 UniProtKB Sequence conflict 277 277 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39683 1 429 +P39683 UniProtKB Chain 1 429 . . . ID=PRO_0000205862;Note=Nicotinate phosphoribosyltransferase +P39683 UniProtKB Sequence conflict 131 137 . . . Note=YEIPLLS->MRSLTV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39683 UniProtKB Sequence conflict 144 158 . . . Note=FKFVDIDWDYENQLE->LIVTSTGLRNHR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39683 UniProtKB Sequence conflict 175 177 . . . Note=SEF->RIH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39683 UniProtKB Sequence conflict 243 243 . . . Note=E->EL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39683 UniProtKB Beta strand 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 14 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Beta strand 31 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 47 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 67 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 82 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 97 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Beta strand 101 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Beta strand 111 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 125 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 132 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 156 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Beta strand 174 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 185 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 203 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Turn 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Beta strand 210 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 216 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 232 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 248 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 262 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Beta strand 267 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 275 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 286 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Beta strand 292 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 300 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Beta strand 321 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 332 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Beta strand 348 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 355 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Beta strand 364 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Beta strand 369 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Beta strand 376 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +P39683 UniProtKB Helix 402 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLP +##sequence-region P53915 1 240 +P53915 UniProtKB Chain 1 240 . . . ID=PRO_0000215898;Note=Nicotinamide riboside kinase +P53915 UniProtKB Nucleotide binding 13 21 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6 +P53915 UniProtKB Nucleotide binding 162 164 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6 +P53915 UniProtKB Nucleotide binding 208 210 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6 +P53915 UniProtKB Region 39 42 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6 +P53915 UniProtKB Region 59 60 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6 +P53915 UniProtKB Region 164 165 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6 +P53915 UniProtKB Active site 39 39 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6 +P53915 UniProtKB Metal binding 20 20 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6 +P53915 UniProtKB Metal binding 39 39 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6 +P53915 UniProtKB Binding site 158 158 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6 +P53915 UniProtKB Binding site 159 159 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NWW6 +##sequence-region P53935 1 1240 +P53935 UniProtKB Chain 1 1240 . . . ID=PRO_0000203442;Note=Stress response protein NST1 +P53935 UniProtKB Coiled coil 616 777 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53935 UniProtKB Compositional bias 506 554 . . . Note=His-rich +P53935 UniProtKB Compositional bias 989 1115 . . . Note=Ser-rich +P53935 UniProtKB Modified residue 266 266 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53935 UniProtKB Natural variant 162 162 . . . Note=In strain: SK1. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P53935 UniProtKB Natural variant 208 208 . . . Note=In strain: SK1. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P53935 UniProtKB Natural variant 354 354 . . . Note=In strain: SK1. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P53935 UniProtKB Natural variant 899 899 . . . Note=In strain: SK1. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +##sequence-region Q12311 1 748 +Q12311 UniProtKB Chain 1 748 . . . ID=PRO_0000268692;Note=NuA3 HAT complex component NTO1 +Q12311 UniProtKB Zinc finger 263 313 . . . Note=PHD-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 +Q12311 UniProtKB Zinc finger 317 350 . . . Note=C2HC pre-PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01146 +Q12311 UniProtKB Zinc finger 374 439 . . . Note=PHD-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01146 +Q12311 UniProtKB Modified residue 728 728 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q02629 1 959 +Q02629 UniProtKB Chain 1 959 . . . ID=PRO_0000204830;Note=Nucleoporin NUP100/NSP100 +Q02629 UniProtKB Repeat 2 3 . . . Note=FG 1 +Q02629 UniProtKB Repeat 9 10 . . . Note=FG 2 +Q02629 UniProtKB Repeat 17 17 . . . Note=FG 3 +Q02629 UniProtKB Repeat 21 24 . . . Note=SLFG 1%3B approximate +Q02629 UniProtKB Repeat 33 36 . . . Note=SLFG 2 +Q02629 UniProtKB Repeat 51 54 . . . Note=SLFG 3%3B approximate +Q02629 UniProtKB Repeat 66 69 . . . Note=SLFG 4 +Q02629 UniProtKB Repeat 77 80 . . . Note=GLFG 1%3B approximate +Q02629 UniProtKB Repeat 89 92 . . . Note=SLFG 5%3B approximate +Q02629 UniProtKB Repeat 105 106 . . . Note=FG 4 +Q02629 UniProtKB Repeat 112 115 . . . Note=GLFG 2%3B approximate +Q02629 UniProtKB Repeat 131 134 . . . Note=SLFG 6%3B approximate +Q02629 UniProtKB Repeat 145 146 . . . Note=FG 5 +Q02629 UniProtKB Repeat 157 160 . . . Note=SLFG 7 +Q02629 UniProtKB Repeat 168 171 . . . Note=GLFG 3%3B approximate +Q02629 UniProtKB Repeat 175 178 . . . Note=SLFG 8%3B approximate +Q02629 UniProtKB Repeat 189 190 . . . Note=FG 6 +Q02629 UniProtKB Repeat 202 205 . . . Note=SLFG 9 +Q02629 UniProtKB Repeat 210 213 . . . Note=SLFG 10%3B approximate +Q02629 UniProtKB Repeat 220 223 . . . Note=SLFG 11 +Q02629 UniProtKB Repeat 233 234 . . . Note=FG 7 +Q02629 UniProtKB Repeat 242 245 . . . Note=SLFG 12%3B approximate +Q02629 UniProtKB Repeat 253 256 . . . Note=SLFG 13 +Q02629 UniProtKB Repeat 271 274 . . . Note=GLFG 4 +Q02629 UniProtKB Repeat 287 290 . . . Note=GLFG 5 +Q02629 UniProtKB Repeat 300 303 . . . Note=GLFG 6%3B approximate +Q02629 UniProtKB Repeat 318 321 . . . Note=SLFG 14 +Q02629 UniProtKB Repeat 333 336 . . . Note=GLFG 7 +Q02629 UniProtKB Repeat 345 348 . . . Note=GLFG 8 +Q02629 UniProtKB Repeat 358 361 . . . Note=GLFG 9 +Q02629 UniProtKB Repeat 379 382 . . . Note=GLFG 10 +Q02629 UniProtKB Repeat 393 396 . . . Note=GLFG 11 +Q02629 UniProtKB Repeat 405 408 . . . Note=SLFG 15 +Q02629 UniProtKB Repeat 417 420 . . . Note=SLFG 16 +Q02629 UniProtKB Repeat 436 439 . . . Note=SLFG 17 +Q02629 UniProtKB Repeat 448 449 . . . Note=FG 8 +Q02629 UniProtKB Repeat 462 465 . . . Note=SLFG 18 +Q02629 UniProtKB Repeat 474 477 . . . Note=SLFG 19%3B approximate +Q02629 UniProtKB Repeat 490 493 . . . Note=GLFG 12 +Q02629 UniProtKB Repeat 506 509 . . . Note=GLFG 13 +Q02629 UniProtKB Repeat 523 526 . . . Note=GLFG 14 +Q02629 UniProtKB Repeat 542 543 . . . Note=FG 9 +Q02629 UniProtKB Repeat 550 553 . . . Note=GLFG 15 +Q02629 UniProtKB Repeat 569 570 . . . Note=FG 10 +Q02629 UniProtKB Domain 814 956 . . . Note=Peptidase S59;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00765 +Q02629 UniProtKB Region 816 955 . . . Note=Nucleoporin RNA-binding motif (NRM) +Q02629 UniProtKB Compositional bias 32 386 . . . Note=Asn-rich +Q02629 UniProtKB Compositional bias 37 43 . . . Note=Poly-Asn +Q02629 UniProtKB Compositional bias 52 570 . . . Note=Gly-rich +Q02629 UniProtKB Compositional bias 312 317 . . . Note=Poly-Asn +Q02629 UniProtKB Compositional bias 337 390 . . . Note=Gln-rich +Q02629 UniProtKB Compositional bias 387 390 . . . Note=Poly-Gln +Q02629 UniProtKB Modified residue 763 763 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q02629 UniProtKB Modified residue 783 783 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q92317 1 146 +Q92317 UniProtKB Chain 1 146 . . . ID=PRO_0000255268;Note=Negative cofactor 2 complex subunit beta +Q92317 UniProtKB Modified residue 135 135 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q92317 UniProtKB Modified residue 137 137 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q92317 UniProtKB Modified residue 142 142 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P38626 1 284 +P38626 UniProtKB Chain 1 284 . . . ID=PRO_0000167627;Note=NADH-cytochrome b5 reductase 1 +P38626 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38626 UniProtKB Domain 38 142 . . . Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716 +P38626 UniProtKB Nucleotide binding 122 137 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38626 UniProtKB Nucleotide binding 148 180 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38830 1 627 +P38830 UniProtKB Chain 1 627 . . . ID=PRO_0000096772;Note=Meiosis-specific transcription factor NDT80 +P38830 UniProtKB DNA binding 28 335 . . . Note=NDT80;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00850 +P38830 UniProtKB Site 58 58 . . . Note=Interaction with DNA +P38830 UniProtKB Site 111 111 . . . Note=Interaction with DNA +P38830 UniProtKB Site 177 177 . . . Note=Interaction with DNA +P38830 UniProtKB Site 208 208 . . . Note=Interaction with DNA +P38830 UniProtKB Site 254 254 . . . Note=Interaction with DNA +P38830 UniProtKB Site 326 326 . . . Note=Interaction with DNA +P38830 UniProtKB Mutagenesis 50 50 . . . Note=Reduces DNA-binding by 70%25. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15161958;Dbxref=PMID:15161958 +P38830 UniProtKB Mutagenesis 54 54 . . . Note=Reduces DNA-binding by 50%25. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15161958;Dbxref=PMID:15161958 +P38830 UniProtKB Mutagenesis 57 57 . . . Note=Reduces DNA-binding by 65%25. P->A +P38830 UniProtKB Mutagenesis 58 58 . . . Note=Reduces DNA-binding by 65%25. R->A +P38830 UniProtKB Mutagenesis 59 59 . . . Note=Reduces DNA-binding by 86%25. S->A +P38830 UniProtKB Mutagenesis 97 97 . . . Note=Reduces DNA-binding by 67%25. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15161958;Dbxref=PMID:15161958 +P38830 UniProtKB Mutagenesis 110 110 . . . Note=No effect on DNA-binding but strongly reduces progress through meiosis and sporulation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12384578;Dbxref=PMID:12384578 +P38830 UniProtKB Mutagenesis 111 111 . . . Note=Reduces DNA-binding by 95%25 and abolishes sporulation. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12384578,ECO:0000269|PubMed:15161958;Dbxref=PMID:12384578,PMID:15161958 +P38830 UniProtKB Mutagenesis 113 113 . . . Note=Reduces DNA-binding by 80%25 and abolishes sporulation. Y->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12384578,ECO:0000269|PubMed:15161958;Dbxref=PMID:12384578,PMID:15161958 +P38830 UniProtKB Mutagenesis 173 173 . . . Note=Reduces DNA-binding by 80%25 and strongly reduces progress through meiosis and sporulation. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12384578;Dbxref=PMID:12384578 +P38830 UniProtKB Mutagenesis 176 176 . . . Note=Reduces DNA-binding by 50%25 but does not abolish sporulation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12384578;Dbxref=PMID:12384578 +P38830 UniProtKB Mutagenesis 177 177 . . . Note=Reduces DNA-binding by 96%25 and abolishes sporulation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12384578;Dbxref=PMID:12384578 +P38830 UniProtKB Mutagenesis 202 202 . . . Note=No effect on DNA-binding but strongly reduces progress through meiosis and sporulation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12384578;Dbxref=PMID:12384578 +P38830 UniProtKB Mutagenesis 208 208 . . . Note=Reduces DNA-binding by 50%25 and abolishes sporulation. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12384578,ECO:0000269|PubMed:15161958;Dbxref=PMID:12384578,PMID:15161958 +P38830 UniProtKB Mutagenesis 254 254 . . . Note=Reduces DNA-binding by 93%25 and abolishes sporulation. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12384578,ECO:0000269|PubMed:15161958;Dbxref=PMID:12384578,PMID:15161958 +P38830 UniProtKB Mutagenesis 326 326 . . . Note=Reduces DNA-binding by 50%25 and abolishes sporulation. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12384578,ECO:0000269|PubMed:15161958;Dbxref=PMID:12384578,PMID:15161958 +P38830 UniProtKB Sequence conflict 200 200 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38830 UniProtKB Sequence conflict 213 213 . . . Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38830 UniProtKB Sequence conflict 225 225 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38830 UniProtKB Sequence conflict 267 267 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38830 UniProtKB Sequence conflict 363 363 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38830 UniProtKB Sequence conflict 493 493 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38830 UniProtKB Sequence conflict 568 568 . . . Note=P->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38830 UniProtKB Beta strand 35 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Beta strand 44 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Turn 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Helix 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Beta strand 70 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Beta strand 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Turn 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Beta strand 90 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Beta strand 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Beta strand 105 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Beta strand 114 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Helix 127 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Beta strand 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Turn 141 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MN4 +P38830 UniProtKB Beta strand 147 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EVG +P38830 UniProtKB Beta strand 152 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Turn 162 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Beta strand 166 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M7U +P38830 UniProtKB Beta strand 170 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Helix 177 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Beta strand 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Helix 198 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Turn 204 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Helix 210 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Beta strand 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Helix 224 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Helix 229 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Helix 237 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Beta strand 241 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Beta strand 273 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Helix 285 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M6U +P38830 UniProtKB Beta strand 288 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M6U +P38830 UniProtKB Beta strand 297 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Beta strand 303 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Beta strand 321 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Helix 328 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +P38830 UniProtKB Helix 332 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MNN +##sequence-region P33420 1 868 +P33420 UniProtKB Chain 1 868 . . . ID=PRO_0000083525;Note=Protein NIP100 +P33420 UniProtKB Domain 34 84 . . . Note=CAP-Gly;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00045 +P33420 UniProtKB Coiled coil 101 175 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33420 UniProtKB Coiled coil 207 375 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33420 UniProtKB Coiled coil 645 776 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40447 1 199 +P40447 UniProtKB Chain 1 199 . . . ID=PRO_0000204049;Note=Putative nitrilase-like protein NIT1 +P40447 UniProtKB Domain 2 199 . . . Note=CN hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054 +P40447 UniProtKB Active site 44 44 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054 +P40447 UniProtKB Active site 135 135 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054 +P40447 UniProtKB Active site 169 169 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054,ECO:0000255|PROSITE-ProRule:PRU10105 +P40447 UniProtKB Sequence conflict 4 4 . . . Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40447 UniProtKB Sequence conflict 106 106 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40447 UniProtKB Sequence conflict 173 173 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P49954 1 291 +P49954 UniProtKB Chain 1 291 . . . ID=PRO_0000213256;Note=Probable hydrolase NIT3 +P49954 UniProtKB Domain 11 264 . . . Note=CN hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054 +P49954 UniProtKB Active site 53 53 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054 +P49954 UniProtKB Active site 128 128 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054 +P49954 UniProtKB Active site 169 169 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054 +P49954 UniProtKB Modified residue 34 34 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P49954 UniProtKB Beta strand 4 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Beta strand 11 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Helix 25 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Beta strand 46 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Turn 53 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Helix 61 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Beta strand 73 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Helix 78 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Beta strand 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Beta strand 99 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Turn 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Beta strand 109 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Beta strand 122 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Helix 143 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Beta strand 155 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Beta strand 162 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Helix 169 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Helix 175 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Beta strand 186 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Helix 199 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Beta strand 217 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Beta strand 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Beta strand 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Beta strand 247 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Beta strand 253 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +P49954 UniProtKB Helix 264 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F89 +##sequence-region Q06178 1 401 +Q06178 UniProtKB Chain 1 401 . . . ID=PRO_0000135018;Note=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 +Q06178 UniProtKB Nucleotide binding 172 174 . . . Note=ATP;Ontology_term=ECO:0000250,ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66,ECO:0000250|UniProtKB:Q9HAN9 +Q06178 UniProtKB Nucleotide binding 288 290 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66 +Q06178 UniProtKB Nucleotide binding 356 359 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66 +Q06178 UniProtKB Region 212 214 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HAN9 +Q06178 UniProtKB Region 250 253 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HAN9 +Q06178 UniProtKB Region 300 301 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HAN9 +Q06178 UniProtKB Compositional bias 61 67 . . . Note=Poly-His +Q06178 UniProtKB Binding site 181 181 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66 +Q06178 UniProtKB Modified residue 91 91 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q06178 UniProtKB Modified residue 95 95 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q06178 UniProtKB Modified residue 96 96 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q06178 UniProtKB Modified residue 111 111 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38861 1 518 +P38861 UniProtKB Chain 1 518 . . . ID=PRO_0000096874;Note=60S ribosomal export protein NMD3 +P38861 UniProtKB Motif 399 415 . . . Note=Nuclear localization signal +P38861 UniProtKB Motif 493 502 . . . Note=Nuclear export signal +P38861 UniProtKB Sequence conflict 94 94 . . . Note=K->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P46970 1 1048 +P46970 UniProtKB Chain 1 1048 . . . ID=PRO_0000096880;Note=Nonsense-mediated mRNA decay protein 5 +P46970 UniProtKB Domain 24 104 . . . Note=Importin N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00115 +P46970 UniProtKB Modified residue 977 977 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P46970 UniProtKB Sequence conflict 258 258 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46970 UniProtKB Sequence conflict 517 517 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08213 1 363 +Q08213 UniProtKB Chain 1 363 . . . ID=PRO_0000218578;Note=RNA exonuclease NGL1 +##sequence-region P53939 1 407 +P53939 UniProtKB Chain 1 407 . . . ID=PRO_0000203447;Note=Protein NIS1 +P53939 UniProtKB Motif 391 398 . . . Note=SUMO-binding +P53939 UniProtKB Modified residue 260 260 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53939 UniProtKB Modified residue 264 264 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53939 UniProtKB Modified residue 300 300 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P53939 UniProtKB Modified residue 302 302 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P34909 1 587 +P34909 UniProtKB Chain 1 587 . . . ID=PRO_0000081681;Note=General negative regulator of transcription subunit 4 +P34909 UniProtKB Domain 137 228 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P34909 UniProtKB Zinc finger 33 78 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +P34909 UniProtKB Zinc finger 229 256 . . . Note=C3H1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 +P34909 UniProtKB Coiled coil 94 128 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34909 UniProtKB Modified residue 310 310 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P34909 UniProtKB Modified residue 312 312 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P34909 UniProtKB Modified residue 326 326 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34909 UniProtKB Modified residue 360 360 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34909 UniProtKB Cross-link 270 270 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P34909 UniProtKB Turn 34 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIE +P34909 UniProtKB Turn 42 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIE +P34909 UniProtKB Helix 58 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIE +P34909 UniProtKB Beta strand 68 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIE +P34909 UniProtKB Turn 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIE +##sequence-region P32494 1 702 +P32494 UniProtKB Chain 1 702 . . . ID=PRO_0000064448;Note=Chromatin-remodeling complexes subunit NGG1 +P32494 UniProtKB Motif 606 618 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32494 UniProtKB Modified residue 134 134 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P32494 UniProtKB Modified residue 407 407 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32494 UniProtKB Modified residue 464 464 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32494 UniProtKB Sequence conflict 520 520 . . . Note=K->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P11633 1 99 +P11633 UniProtKB Chain 1 99 . . . ID=PRO_0000048566;Note=Non-histone chromosomal protein 6B +P11633 UniProtKB DNA binding 27 95 . . . Note=HMG box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267 +P11633 UniProtKB Sequence conflict 30 30 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11633 UniProtKB Sequence conflict 30 30 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47016 1 307 +P47016 UniProtKB Chain 1 307 . . . ID=PRO_0000213255;Note=Probable hydrolase NIT2 +P47016 UniProtKB Domain 6 285 . . . Note=CN hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054 +P47016 UniProtKB Active site 45 45 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054 +P47016 UniProtKB Active site 127 127 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054 +P47016 UniProtKB Active site 169 169 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00054,ECO:0000269|PubMed:23897470;Dbxref=PMID:23897470 +P47016 UniProtKB Binding site 173 173 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23897470;Dbxref=PMID:23897470 +P47016 UniProtKB Binding site 199 199 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23897470;Dbxref=PMID:23897470 +P47016 UniProtKB Mutagenesis 169 169 . . . Note=Abolishes enzyme activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23897470;Dbxref=PMID:23897470 +P47016 UniProtKB Beta strand 5 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Helix 19 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Beta strand 39 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Helix 54 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Helix 64 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Beta strand 87 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Helix 98 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Beta strand 108 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Beta strand 121 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Beta strand 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Beta strand 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Helix 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Beta strand 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Beta strand 162 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Helix 171 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Helix 175 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Beta strand 187 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Helix 197 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Beta strand 218 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Beta strand 223 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Helix 233 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Turn 243 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Beta strand 251 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Beta strand 257 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Beta strand 265 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Beta strand 277 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Helix 285 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Helix 297 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +P47016 UniProtKB Turn 303 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HG5 +##sequence-region Q6Q547 1 58 +Q6Q547 UniProtKB Chain 1 58 . . . ID=PRO_0000149013;Note=H/ACA ribonucleoprotein complex subunit 3 +Q6Q547 UniProtKB Modified residue 36 36 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q6Q547 UniProtKB Cross-link 28 28 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q6Q547 UniProtKB Beta strand 4 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +Q6Q547 UniProtKB Beta strand 8 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y2Y +Q6Q547 UniProtKB Beta strand 13 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +Q6Q547 UniProtKB Beta strand 28 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +Q6Q547 UniProtKB Beta strand 32 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y2Y +Q6Q547 UniProtKB Beta strand 37 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQA +Q6Q547 UniProtKB Helix 42 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3U28 +Q6Q547 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y2Y +##sequence-region Q99207 1 810 +Q99207 UniProtKB Chain 1 810 . . . ID=PRO_0000137163;Note=Nucleolar complex protein 14 +##sequence-region Q01560 1 414 +Q01560 UniProtKB Chain 1 414 . . . ID=PRO_0000081676;Note=Nucleolar protein 3 +Q01560 UniProtKB Domain 125 195 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q01560 UniProtKB Domain 200 275 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q01560 UniProtKB Compositional bias 280 398 . . . Note=Arg/Gly-rich +Q01560 UniProtKB Modified residue 182 182 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q01560 UniProtKB Modified residue 224 224 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q01560 UniProtKB Beta strand 125 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVO +Q01560 UniProtKB Helix 138 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVO +Q01560 UniProtKB Turn 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVO +Q01560 UniProtKB Beta strand 153 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVO +Q01560 UniProtKB Beta strand 160 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVO +Q01560 UniProtKB Helix 168 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVO +Q01560 UniProtKB Beta strand 189 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVO +Q01560 UniProtKB Beta strand 200 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVR +Q01560 UniProtKB Helix 213 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVR +Q01560 UniProtKB Beta strand 228 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVR +Q01560 UniProtKB Beta strand 236 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVR +Q01560 UniProtKB Beta strand 241 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVR +Q01560 UniProtKB Helix 248 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVR +Q01560 UniProtKB Beta strand 261 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVR +Q01560 UniProtKB Beta strand 266 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JVR +##sequence-region Q12499 1 511 +Q12499 UniProtKB Chain 1 511 . . . ID=PRO_0000219029;Note=Nucleolar protein 58 +Q12499 UniProtKB Domain 283 403 . . . Note=Nop;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00690 +Q12499 UniProtKB Coiled coil 435 511 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12499 UniProtKB Compositional bias 441 511 . . . Note=Asp/Glu/Lys-rich +Q12499 UniProtKB Cross-link 281 281 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P47077 1 666 +P47077 UniProtKB Chain 1 666 . . . ID=PRO_0000075939;Note=Nucleolar protein 9 +P47077 UniProtKB Domain 23 435 . . . Note=PUM-HD +P47077 UniProtKB Repeat 92 127 . . . Note=Pumilio 1 +P47077 UniProtKB Repeat 128 163 . . . Note=Pumilio 2 +P47077 UniProtKB Repeat 188 223 . . . Note=Pumilio 3 +P47077 UniProtKB Repeat 286 326 . . . Note=Pumilio 4 +P47077 UniProtKB Repeat 334 368 . . . Note=Pumilio 5 +P47077 UniProtKB Repeat 369 407 . . . Note=Pumilio 6 +P47077 UniProtKB Repeat 511 548 . . . Note=Pumilio 7 +P47077 UniProtKB Repeat 549 587 . . . Note=Pumilio 8 +P47077 UniProtKB Helix 58 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 79 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Turn 94 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 97 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Turn 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 107 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 119 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Turn 128 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 133 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 142 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 178 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 190 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 193 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 202 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 256 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Beta strand 278 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 287 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Turn 298 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 301 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 311 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 319 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Beta strand 328 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 333 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 346 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 361 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 373 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 376 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Turn 383 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 386 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 399 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 410 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 413 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 421 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Turn 434 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WTY +P47077 UniProtKB Helix 439 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Beta strand 455 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WTY +P47077 UniProtKB Helix 460 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 467 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 482 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 499 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 514 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 526 533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 536 538 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 541 551 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 552 554 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 555 559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 564 574 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Turn 575 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 579 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 593 597 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 600 608 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 611 616 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +P47077 UniProtKB Helix 618 632 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SVD +##sequence-region P39923 1 615 +P39923 UniProtKB Chain 1 615 . . . ID=PRO_0000213321;Note=Nitrogen permease regulator 2 +P39923 UniProtKB Compositional bias 354 420 . . . Note=Ser-rich +P39923 UniProtKB Modified residue 362 362 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P39923 UniProtKB Sequence conflict 225 225 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53164 1 384 +P53164 UniProtKB Chain 1 384 . . . ID=PRO_0000056961;Note=NADH pyrophosphatase +P53164 UniProtKB Domain 219 351 . . . Note=Nudix hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00794 +P53164 UniProtKB Motif 257 278 . . . Note=Nudix box +P53164 UniProtKB Metal binding 272 272 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53164 UniProtKB Metal binding 276 276 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53164 UniProtKB Sequence conflict 44 44 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08972 1 1196 +Q08972 UniProtKB Chain 1 1196 . . . ID=PRO_0000268690;Note=[NU+] prion formation protein 1 +Q08972 UniProtKB Domain 570 786 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q08972 UniProtKB Domain 812 1129 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q08972 UniProtKB Domain 942 1003 . . . Note=Chromo;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00053 +Q08972 UniProtKB Nucleotide binding 604 611 . . . Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q08972 UniProtKB Nucleotide binding 846 853 . . . Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q08972 UniProtKB Compositional bias 61 104 . . . Note=Tyr-rich +Q08972 UniProtKB Compositional bias 70 95 . . . Note=Asn-rich +Q08972 UniProtKB Modified residue 443 443 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q08972 UniProtKB Modified residue 1191 1191 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P0CE68 1 1218 +P0CE68 UniProtKB Chain 1 1218 . . . ID=PRO_0000093462;Note=ABC transporter NFT1 +P0CE68 UniProtKB Topological domain 1 29 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE68 UniProtKB Transmembrane 30 50 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P0CE68 UniProtKB Topological domain 51 103 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE68 UniProtKB Transmembrane 104 124 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P0CE68 UniProtKB Topological domain 125 130 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE68 UniProtKB Transmembrane 131 151 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P0CE68 UniProtKB Topological domain 152 169 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE68 UniProtKB Transmembrane 170 190 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P0CE68 UniProtKB Topological domain 191 201 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE68 UniProtKB Transmembrane 202 222 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P0CE68 UniProtKB Topological domain 223 302 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE68 UniProtKB Transmembrane 303 323 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P0CE68 UniProtKB Topological domain 324 351 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE68 UniProtKB Transmembrane 352 374 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P0CE68 UniProtKB Topological domain 375 449 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE68 UniProtKB Transmembrane 450 470 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P0CE68 UniProtKB Topological domain 471 481 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE68 UniProtKB Transmembrane 482 504 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P0CE68 UniProtKB Topological domain 505 558 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE68 UniProtKB Transmembrane 559 579 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P0CE68 UniProtKB Topological domain 580 584 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE68 UniProtKB Transmembrane 585 605 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P0CE68 UniProtKB Topological domain 606 953 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE68 UniProtKB Transmembrane 954 974 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P0CE68 UniProtKB Topological domain 975 1013 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE68 UniProtKB Transmembrane 1014 1034 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P0CE68 UniProtKB Topological domain 1035 1082 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE68 UniProtKB Transmembrane 1083 1105 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P0CE68 UniProtKB Topological domain 1106 1109 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE68 UniProtKB Transmembrane 1110 1132 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P0CE68 UniProtKB Topological domain 1133 1197 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE68 UniProtKB Transmembrane 1198 1218 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P0CE68 UniProtKB Domain 311 621 . . . Note=ABC transmembrane type-1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P0CE68 UniProtKB Domain 651 892 . . . Note=ABC transporter;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P0CE68 UniProtKB Domain 961 1218 . . . Note=ABC transmembrane type-1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P0CE68 UniProtKB Nucleotide binding 686 693 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P0CE68 UniProtKB Glycosylation 4 4 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32860 1 256 +P32860 UniProtKB Motif 196 199 . . . Note=CxxC motif;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:27532773;Dbxref=PMID:27532773 +P32860 UniProtKB Mutagenesis 194 194 . . . Note=Dominant negative mutant%3B cells show a severe synthetic sick phenotype on glycerol/lactate medium. G->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27532773;Dbxref=PMID:27532773 +P32860 UniProtKB Mutagenesis 196 199 . . . Note=Loss of function. Abolished homodimerization. CTSC->ATSA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27532773;Dbxref=PMID:27532773 +P32860 UniProtKB Beta strand 24 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LTL +P32860 UniProtKB Beta strand 32 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LTL +P32860 UniProtKB Beta strand 53 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LTL +P32860 UniProtKB Helix 60 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LTL +P32860 UniProtKB Helix 67 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LTL +P32860 UniProtKB Beta strand 79 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LTL +P32860 UniProtKB Beta strand 86 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LTL +P32860 UniProtKB Helix 99 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LTL +P32860 UniProtKB Beta strand 118 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LTL +##sequence-region Q03435 1 203 +Q03435 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q03435 UniProtKB Chain 2 203 . . . ID=PRO_0000048567;Note=Non-histone protein 10 +Q03435 UniProtKB DNA binding 94 158 . . . Note=HMG box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267 +Q03435 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P53081 1 288 +P53081 UniProtKB Chain 1 288 . . . ID=PRO_0000147356;Note=NGG1-interacting factor 3 +P53081 UniProtKB Sequence conflict 53 53 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53920 1 997 +P53920 UniProtKB Chain 1 997 . . . ID=PRO_0000203429;Note=Pro-apoptotic serine protease NMA111 +P53920 UniProtKB Domain 300 378 . . . Note=PDZ 1 +P53920 UniProtKB Domain 779 854 . . . Note=PDZ 2 +P53920 UniProtKB Region 83 273 . . . Note=Serine protease +P53920 UniProtKB Active site 121 121 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53920 UniProtKB Active site 152 152 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53920 UniProtKB Active site 235 235 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53920 UniProtKB Natural variant 162 162 . . . Note=In strain: YJM269%2C YJM270 and YJM1129. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53920 UniProtKB Natural variant 241 241 . . . Note=In strain: YJM269 and YJM270. V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53920 UniProtKB Natural variant 331 331 . . . Note=In strain: YJM326. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53920 UniProtKB Natural variant 343 343 . . . Note=In strain: YJM269 and YJM270. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53920 UniProtKB Natural variant 386 386 . . . Note=In strain: YJM269%2C YJM270 and YJM1129. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53920 UniProtKB Natural variant 457 457 . . . Note=In strain: YJM269 and YJM270. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53920 UniProtKB Natural variant 530 530 . . . Note=In strain: YJM627. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53920 UniProtKB Natural variant 580 580 . . . Note=In strain: YJM627. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53920 UniProtKB Natural variant 621 621 . . . Note=In strain: YJM269 and YJM270. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53920 UniProtKB Natural variant 942 942 . . . Note=In strain: YJM627. P->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18780730;Dbxref=PMID:18780730 +P53920 UniProtKB Mutagenesis 235 235 . . . Note=Impairs BIR1 degradation and death-promoting activity. S->C;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14657274,ECO:0000269|PubMed:16608876;Dbxref=PMID:14657274,PMID:16608876 +##sequence-region Q12129 1 218 +Q12129 UniProtKB Chain 1 218 . . . ID=PRO_0000096879;Note=Nonsense-mediated decay protein 4 +##sequence-region P53253 1 936 +P53253 UniProtKB Chain 1 936 . . . ID=PRO_0000202809;Note=Protein NNF2 +P53253 UniProtKB Topological domain 1 41 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53253 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53253 UniProtKB Topological domain 63 120 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53253 UniProtKB Transmembrane 121 141 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53253 UniProtKB Topological domain 142 245 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53253 UniProtKB Transmembrane 246 266 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53253 UniProtKB Topological domain 267 936 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53253 UniProtKB Cross-link 10 10 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region Q08444 1 459 +Q08444 UniProtKB Chain 1 459 . . . ID=PRO_0000270554;Note=20S-pre-rRNA D-site endonuclease NOB1 +Q08444 UniProtKB Domain 10 115 . . . Note=PINc +Q08444 UniProtKB Metal binding 304 304 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08444 UniProtKB Metal binding 307 307 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08444 UniProtKB Metal binding 323 323 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08444 UniProtKB Metal binding 326 326 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08444 UniProtKB Mutagenesis 92 92 . . . Note=No 20S cleavage. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15388878;Dbxref=PMID:15388878 +Q08444 UniProtKB Mutagenesis 110 110 . . . Note=No change in activity or growth. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15388878;Dbxref=PMID:15388878 +Q08444 UniProtKB Mutagenesis 279 279 . . . Note=Temperature-sensitive. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12502737;Dbxref=PMID:12502737 +Q08444 UniProtKB Mutagenesis 280 280 . . . Note=Temperature-sensitive. Q->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12502737;Dbxref=PMID:12502737 +Q08444 UniProtKB Mutagenesis 281 281 . . . Note=Temperature-sensitive. M->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12502737;Dbxref=PMID:12502737 +##sequence-region Q06512 1 552 +Q06512 UniProtKB Chain 1 552 . . . ID=PRO_0000173491;Note=Nucleolar complex protein 4 +##sequence-region Q08208 1 459 +Q08208 UniProtKB Chain 1 459 . . . ID=PRO_0000081675;Note=Nucleolar protein 12 +Q08208 UniProtKB Domain 279 371 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q08208 UniProtKB Modified residue 70 70 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q08208 UniProtKB Modified residue 181 181 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08208 UniProtKB Modified residue 184 184 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region Q12460 1 504 +Q12460 UniProtKB Chain 1 504 . . . ID=PRO_0000219030;Note=Nucleolar protein 56 +Q12460 UniProtKB Domain 299 417 . . . Note=Nop;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00690 +Q12460 UniProtKB Compositional bias 443 504 . . . Note=Asp/Glu/Lys-rich +Q12460 UniProtKB Modified residue 321 321 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12460 UniProtKB Mutagenesis 333 333 . . . Note=Reduced growth rate at all temperatures%3B when associated with R-385. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372940;Dbxref=PMID:9372940 +Q12460 UniProtKB Mutagenesis 355 355 . . . Note=At 37 degrees%2C growth slows after 6 to 8 hours and cell division stops after 20 hours. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372940;Dbxref=PMID:9372940 +Q12460 UniProtKB Mutagenesis 385 385 . . . Note=Reduced growth rate at all temperatures%3B when associated with A-333. M->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9372940;Dbxref=PMID:9372940 +##sequence-region Q12408 1 173 +Q12408 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12408 UniProtKB Propeptide 22 34 . . . ID=PRO_0000019897;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12408 UniProtKB Chain 35 173 . . . ID=PRO_0000019898;Note=Phosphatidylglycerol/phosphatidylinositol transfer protein +##sequence-region Q06287 1 252 +Q06287 UniProtKB Chain 1 252 . . . ID=PRO_0000158612;Note=Ribosomal RNA small subunit methyltransferase NEP1 +Q06287 UniProtKB Region 212 214 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18063569,ECO:0000269|PubMed:21087996;Dbxref=PMID:18063569,PMID:21087996 +Q06287 UniProtKB Region 227 232 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18063569,ECO:0000269|PubMed:21087996;Dbxref=PMID:18063569,PMID:21087996 +Q06287 UniProtKB Binding site 180 180 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18063569,ECO:0000269|PubMed:21087996;Dbxref=PMID:18063569,PMID:21087996 +Q06287 UniProtKB Binding site 207 207 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18063569,ECO:0000269|PubMed:21087996;Dbxref=PMID:18063569,PMID:21087996 +Q06287 UniProtKB Site 88 88 . . . Note=Interaction with substrate rRNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21087996;Dbxref=PMID:21087996 +Q06287 UniProtKB Site 90 90 . . . Note=Stabilizes Arg-88;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:21087996;Dbxref=PMID:21087996 +Q06287 UniProtKB Site 129 129 . . . Note=Interaction with substrate rRNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21087996;Dbxref=PMID:21087996 +Q06287 UniProtKB Site 132 132 . . . Note=Interaction with substrate rRNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21087996;Dbxref=PMID:21087996 +Q06287 UniProtKB Site 136 136 . . . Note=Interaction with substrate rRNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21087996;Dbxref=PMID:21087996 +Q06287 UniProtKB Mutagenesis 88 88 . . . Note=Loss of substrate rRNA binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18208838;Dbxref=PMID:18208838 +Q06287 UniProtKB Mutagenesis 88 88 . . . Note=Loss of substrate rRNA binding. No effect on growth. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18063569;Dbxref=PMID:18063569 +Q06287 UniProtKB Mutagenesis 90 90 . . . Note=Loses its exclusive nucleolar localization and mislocalizes to the cytoplasm. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20972225;Dbxref=PMID:20972225 +Q06287 UniProtKB Mutagenesis 129 129 . . . Note=Loss of substrate rRNA binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18208838;Dbxref=PMID:18208838 +Q06287 UniProtKB Mutagenesis 132 132 . . . Note=Loss of substrate rRNA binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18208838;Dbxref=PMID:18208838 +Q06287 UniProtKB Mutagenesis 136 136 . . . Note=Loss of substrate rRNA binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18208838;Dbxref=PMID:18208838 +Q06287 UniProtKB Mutagenesis 214 214 . . . Note=Almost complete loss of SAM binding. No effect on growth and ribosome biogenesis. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18063569;Dbxref=PMID:18063569 +Q06287 UniProtKB Mutagenesis 232 232 . . . Note=Almost complete loss of SAM binding. No effect on growth and ribosome biogenesis. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18063569;Dbxref=PMID:18063569 +Q06287 UniProtKB Mutagenesis 237 237 . . . Note=Almost complete loss of SAM binding. No effect on growth and ribosome biogenesis. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18063569;Dbxref=PMID:18063569 +Q06287 UniProtKB Sequence conflict 114 114 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06287 UniProtKB Beta strand 36 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V3J +Q06287 UniProtKB Beta strand 41 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +Q06287 UniProtKB Beta strand 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIN +Q06287 UniProtKB Beta strand 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OIN +Q06287 UniProtKB Turn 70 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +Q06287 UniProtKB Helix 74 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +Q06287 UniProtKB Helix 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +Q06287 UniProtKB Helix 89 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +Q06287 UniProtKB Helix 103 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +Q06287 UniProtKB Beta strand 110 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +Q06287 UniProtKB Beta strand 121 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +Q06287 UniProtKB Helix 134 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +Q06287 UniProtKB Beta strand 148 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +Q06287 UniProtKB Beta strand 155 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +Q06287 UniProtKB Helix 167 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +Q06287 UniProtKB Beta strand 173 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +Q06287 UniProtKB Helix 189 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +Q06287 UniProtKB Beta strand 201 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +Q06287 UniProtKB Beta strand 209 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +Q06287 UniProtKB Turn 216 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +Q06287 UniProtKB Beta strand 222 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +Q06287 UniProtKB Helix 234 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OII +##sequence-region P47035 1 1189 +P47035 UniProtKB Chain 1 1189 . . . ID=PRO_0000096784;Note=Nucleolar protein NET1 +P47035 UniProtKB Compositional bias 192 199 . . . Note=Poly-Thr +P47035 UniProtKB Compositional bias 328 335 . . . Note=Poly-Ser +P47035 UniProtKB Compositional bias 415 418 . . . Note=Poly-Ser +P47035 UniProtKB Compositional bias 982 988 . . . Note=Poly-Ser +P47035 UniProtKB Compositional bias 993 1000 . . . Note=Poly-Ser +P47035 UniProtKB Compositional bias 1171 1174 . . . Note=Poly-Lys +P47035 UniProtKB Modified residue 60 60 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47035 UniProtKB Modified residue 166 166 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47035 UniProtKB Modified residue 231 231 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P47035 UniProtKB Modified residue 252 252 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47035 UniProtKB Modified residue 437 437 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47035 UniProtKB Modified residue 439 439 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47035 UniProtKB Modified residue 447 447 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47035 UniProtKB Modified residue 452 452 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47035 UniProtKB Modified residue 497 497 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P47035 UniProtKB Modified residue 676 676 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P47035 UniProtKB Modified residue 830 830 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47035 UniProtKB Modified residue 1042 1042 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P47035 UniProtKB Modified residue 1056 1056 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47035 UniProtKB Modified residue 1059 1059 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P11632 1 93 +P11632 UniProtKB Chain 1 93 . . . ID=PRO_0000048565;Note=Non-histone chromosomal protein 6A +P11632 UniProtKB DNA binding 21 89 . . . Note=HMG box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267 +P11632 UniProtKB Mutagenesis 18 18 . . . Note=Does not affect affinity for DNA. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9468494;Dbxref=PMID:9468494 +P11632 UniProtKB Mutagenesis 21 21 . . . Note=Shows a 4-fold reduced affinity for DNA. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9468494;Dbxref=PMID:9468494 +P11632 UniProtKB Mutagenesis 28 28 . . . Note=Shows a strongly reduced affinity for linear and circular DNA. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9468494;Dbxref=PMID:9468494 +P11632 UniProtKB Mutagenesis 29 29 . . . Note=Unable to form 75 bp microcircles. M->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9468494;Dbxref=PMID:9468494 +P11632 UniProtKB Mutagenesis 30 30 . . . Note=Does not affect affinity for DNA. F->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9468494;Dbxref=PMID:9468494 +P11632 UniProtKB Mutagenesis 31 31 . . . Note=Shows a strongly reduced affinity for linear and circular DNA. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9468494;Dbxref=PMID:9468494 +P11632 UniProtKB Beta strand 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1J5N +P11632 UniProtKB Helix 27 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CG7 +P11632 UniProtKB Turn 38 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CG7 +P11632 UniProtKB Helix 48 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CG7 +P11632 UniProtKB Turn 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CG7 +P11632 UniProtKB Helix 55 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CG7 +P11632 UniProtKB Helix 63 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CG7 +P11632 UniProtKB Helix 77 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CG7 +P11632 UniProtKB Helix 83 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CG7 +##sequence-region Q07896 1 663 +Q07896 UniProtKB Chain 1 663 . . . ID=PRO_0000173483;Note=Nucleolar complex-associated protein 3 +Q07896 UniProtKB Coiled coil 363 408 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07896 UniProtKB Modified residue 395 395 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q03790 1 475 +Q03790 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q03790 UniProtKB Chain 2 475 . . . ID=PRO_0000204871;Note=Nucleoporin NUP53 +Q03790 UniProtKB Repeat 124 125 . . . Note=FG 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785 +Q03790 UniProtKB Domain 247 352 . . . Note=RRM Nup35-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00804 +Q03790 UniProtKB Repeat 264 265 . . . Note=FG 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785 +Q03790 UniProtKB Repeat 273 274 . . . Note=FG 3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785 +Q03790 UniProtKB Repeat 470 471 . . . Note=FG 4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785 +Q03790 UniProtKB Region 405 438 . . . Note=PSE1 binding +Q03790 UniProtKB Region 449 475 . . . Note=Required for nuclear membrane association and proliferation +Q03790 UniProtKB Compositional bias 24 41 . . . Note=Gln-rich +Q03790 UniProtKB Compositional bias 115 147 . . . Note=Asn-rich +Q03790 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q03790 UniProtKB Modified residue 101 101 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03790 UniProtKB Modified residue 297 297 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03790 UniProtKB Modified residue 438 438 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P46673 1 744 +P46673 UniProtKB Chain 1 744 . . . ID=PRO_0000204885;Note=Nucleoporin NUP85 +P46673 UniProtKB Compositional bias 646 652 . . . Note=Poly-Leu +P46673 UniProtKB Sequence conflict 101 101 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46673 UniProtKB Sequence conflict 471 471 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46673 UniProtKB Beta strand 41 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3P +P46673 UniProtKB Beta strand 67 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Beta strand 77 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Beta strand 89 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 102 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 119 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 135 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 170 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Beta strand 190 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 197 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 201 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 221 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Beta strand 237 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 243 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 258 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Turn 266 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 272 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 279 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 300 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 326 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 343 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 353 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 368 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 371 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Beta strand 388 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 391 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 403 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 406 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 414 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Beta strand 454 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 461 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Turn 479 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 482 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Beta strand 493 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 497 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 508 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 516 529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 532 543 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P46673 UniProtKB Helix 545 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +##sequence-region P36023 1 863 +P36023 UniProtKB Chain 1 863 . . . ID=PRO_0000115002;Note=Oleate activated transcription factor 3 +P36023 UniProtKB DNA binding 18 47 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +##sequence-region Q03028 1 310 +Q03028 UniProtKB Chain 1 310 . . . ID=PRO_0000090648;Note=Mitochondrial 2-oxodicarboxylate carrier 1 +Q03028 UniProtKB Transmembrane 9 29 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03028 UniProtKB Transmembrane 78 97 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03028 UniProtKB Transmembrane 126 146 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03028 UniProtKB Transmembrane 179 199 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03028 UniProtKB Transmembrane 219 239 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03028 UniProtKB Transmembrane 281 301 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03028 UniProtKB Repeat 9 108 . . . Note=Solcar 1 +Q03028 UniProtKB Repeat 120 204 . . . Note=Solcar 2 +Q03028 UniProtKB Repeat 213 300 . . . Note=Solcar 3 +##sequence-region P32473 1 366 +P32473 UniProtKB Transit peptide 1 33 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8433986;Dbxref=PMID:8433986 +P32473 UniProtKB Chain 34 366 . . . ID=PRO_0000020461;Note=Pyruvate dehydrogenase E1 component subunit beta%2C mitochondrial +P32473 UniProtKB Binding site 95 95 . . . Note=Thiamine pyrophosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32473 UniProtKB Sequence conflict 160 160 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53397 1 376 +P53397 UniProtKB Chain 1 376 . . . ID=PRO_0000058595;Note=N-glycosylase/DNA lyase +P53397 UniProtKB Active site 241 241 . . . Note=Schiff-base intermediate with DNA +P53397 UniProtKB Binding site 134 134 . . . Note=DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53397 UniProtKB Binding site 139 139 . . . Note=DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53397 UniProtKB Binding site 189 189 . . . Note=DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53397 UniProtKB Binding site 258 258 . . . Note=8-oxoguanine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53397 UniProtKB Binding site 260 260 . . . Note=8-oxoguanine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53397 UniProtKB Binding site 262 262 . . . Note=DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53397 UniProtKB Binding site 320 320 . . . Note=8-oxoguanine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53397 UniProtKB Binding site 324 324 . . . Note=8-oxoguanine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53397 UniProtKB Mutagenesis 241 241 . . . Note=Abolishes both DNA glycosylase and AP lyase activity. K->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677220,ECO:0000269|PubMed:9241232;Dbxref=PMID:10677220,PMID:9241232 +P53397 UniProtKB Mutagenesis 241 241 . . . Note=Diminishes both DNA glycosylase and AP lyase activity. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10677220,ECO:0000269|PubMed:9241232;Dbxref=PMID:10677220,PMID:9241232 +##sequence-region Q08962 1 181 +Q08962 UniProtKB Chain 1 181 . . . ID=PRO_0000218776;Note=60S ribosome subunit biogenesis protein NIP7 +Q08962 UniProtKB Domain 94 170 . . . Note=PUA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00161 +Q08962 UniProtKB Mutagenesis 161 164 . . . Note=Reduces RNA-binding ability in vitro. IVAF->AVAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18001138;Dbxref=PMID:18001138 +##sequence-region Q12493 1 238 +Q12493 UniProtKB Chain 1 238 . . . ID=PRO_0000096867;Note=Central kinetochore subunit NKP1 +Q12493 UniProtKB Modified residue 222 222 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P14743 1 455 +P14743 UniProtKB Chain 1 455 . . . ID=PRO_0000064248;Note=Glycylpeptide N-tetradecanoyltransferase +P14743 UniProtKB Region 38 41 . . . Note=Myristoyl CoA-binding +P14743 UniProtKB Region 168 204 . . . Note=Myristoyl CoA-binding +P14743 UniProtKB Active site 455 455 . . . Note=Proton acceptor%3B via carboxylate +P14743 UniProtKB Mutagenesis 99 99 . . . Note=In NMT1-72%3B temperature-sensitive mutant with myristic acid auxotrophy. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8416952;Dbxref=PMID:8416952 +P14743 UniProtKB Mutagenesis 169 169 . . . Note=Reduces the chemical transformation rate%3B when associated with A-205. N->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11478885;Dbxref=PMID:11478885 +P14743 UniProtKB Mutagenesis 170 170 . . . Note=Reduces the chemical transformation rate%3B when associated with A-171. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11478885;Dbxref=PMID:11478885 +P14743 UniProtKB Mutagenesis 171 171 . . . Note=Reduces the chemical transformation rate%3B when associated with A-170. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11478885;Dbxref=PMID:11478885 +P14743 UniProtKB Mutagenesis 202 202 . . . Note=Reduces affinity for both substrate and myristoyl-CoA. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8955162;Dbxref=PMID:8955162 +P14743 UniProtKB Mutagenesis 205 205 . . . Note=Reduces the chemical transformation rate%3B when associated with L-169. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11478885;Dbxref=PMID:11478885 +P14743 UniProtKB Mutagenesis 217 217 . . . Note=Reduces affinity for substrate%2C but not for myristoyl-CoA. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8955162;Dbxref=PMID:8955162 +P14743 UniProtKB Mutagenesis 328 328 . . . Note=Moderately reduces affinity for myristoyl-CoA%2C but not for substrate. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8955162;Dbxref=PMID:8955162 +P14743 UniProtKB Mutagenesis 404 404 . . . Note=Moderately reduces affinity for substrate%2C but not for myristoyl-CoA. N->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8955162;Dbxref=PMID:8955162 +P14743 UniProtKB Mutagenesis 426 426 . . . Note=Reduces affinity for myristoyl-CoA%2C but not for substrate. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8955162;Dbxref=PMID:8955162 +P14743 UniProtKB Mutagenesis 451 451 . . . Note=In NMT1-181%3B temperature-sensitive with myristic acid auxotrophy. Reduces affinity for myristoyl-CoA. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2045414;Dbxref=PMID:2045414 +P14743 UniProtKB Mutagenesis 454 455 . . . Note=Reduces chemical transformation rate 400-fold. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11478885;Dbxref=PMID:11478885 +P14743 UniProtKB Helix 6 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P6E +P14743 UniProtKB Helix 35 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NMT +P14743 UniProtKB Helix 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 57 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Helix 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 79 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 86 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P6G +P14743 UniProtKB Helix 89 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 103 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Helix 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Helix 117 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Helix 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 134 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Turn 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 145 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 161 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Helix 175 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 179 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IID +P14743 UniProtKB Helix 183 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Turn 196 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 202 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 214 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Helix 226 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Helix 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IID +P14743 UniProtKB Helix 243 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 261 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Helix 266 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Helix 269 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 283 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Helix 291 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P6E +P14743 UniProtKB Helix 306 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 311 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 323 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 334 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 343 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 347 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Turn 357 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Helix 367 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 394 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Helix 404 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Turn 407 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 414 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 434 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Beta strand 440 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +P14743 UniProtKB Turn 444 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IIC +##sequence-region P36003 1 928 +P36003 UniProtKB Chain 1 928 . . . ID=PRO_0000086152;Note=Nitrogen network kinase 1 +P36003 UniProtKB Domain 449 912 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P36003 UniProtKB Nucleotide binding 455 463 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P36003 UniProtKB Active site 580 580 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P36003 UniProtKB Binding site 478 478 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P36003 UniProtKB Modified residue 178 178 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36003 UniProtKB Modified residue 179 179 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36003 UniProtKB Modified residue 405 405 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36003 UniProtKB Modified residue 426 426 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36003 UniProtKB Modified residue 737 737 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P36003 UniProtKB Modified residue 739 739 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q02892 1 647 +Q02892 UniProtKB Chain 1 647 . . . ID=PRO_0000195035;Note=Nucleolar GTP-binding protein 1 +Q02892 UniProtKB Domain 168 340 . . . Note=OBG-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +Q02892 UniProtKB Nucleotide binding 174 181 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +Q02892 UniProtKB Nucleotide binding 220 224 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +Q02892 UniProtKB Nucleotide binding 288 291 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +Q02892 UniProtKB Modified residue 563 563 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P06100 1 191 +P06100 UniProtKB Chain 1 191 . . . ID=PRO_0000198336;Note=General negative regulator of transcription subunit 2 +P06100 UniProtKB Beta strand 7 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +P06100 UniProtKB Helix 35 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +P06100 UniProtKB Helix 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +P06100 UniProtKB Beta strand 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +P06100 UniProtKB Helix 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +P06100 UniProtKB Helix 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +P06100 UniProtKB Beta strand 88 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +P06100 UniProtKB Turn 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +P06100 UniProtKB Helix 101 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +P06100 UniProtKB Helix 109 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +P06100 UniProtKB Helix 123 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +P06100 UniProtKB Beta strand 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +P06100 UniProtKB Turn 141 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +P06100 UniProtKB Beta strand 145 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +P06100 UniProtKB Beta strand 161 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +P06100 UniProtKB Turn 173 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +P06100 UniProtKB Beta strand 177 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +P06100 UniProtKB Helix 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +##sequence-region Q12514 1 560 +Q12514 UniProtKB Chain 1 560 . . . ID=PRO_0000198338;Note=General negative regulator of transcription subunit 5 +Q12514 UniProtKB Coiled coil 3 26 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12514 UniProtKB Coiled coil 37 71 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12514 UniProtKB Coiled coil 124 177 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12514 UniProtKB Modified residue 306 306 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q12514 UniProtKB Modified residue 377 377 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12514 UniProtKB Cross-link 338 338 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q12514 UniProtKB Turn 348 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +Q12514 UniProtKB Helix 353 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +Q12514 UniProtKB Helix 356 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +Q12514 UniProtKB Helix 367 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +Q12514 UniProtKB Helix 378 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +Q12514 UniProtKB Helix 394 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +Q12514 UniProtKB Turn 459 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +Q12514 UniProtKB Helix 464 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +Q12514 UniProtKB Helix 474 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +Q12514 UniProtKB Helix 488 501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +Q12514 UniProtKB Beta strand 504 506 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +Q12514 UniProtKB Turn 507 509 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +Q12514 UniProtKB Beta strand 512 515 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +Q12514 UniProtKB Beta strand 532 535 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +Q12514 UniProtKB Turn 537 540 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +Q12514 UniProtKB Beta strand 542 545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +Q12514 UniProtKB Helix 554 556 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY6 +##sequence-region P38742 1 1146 +P38742 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38742 UniProtKB Chain 26 1146 . . . ID=PRO_0000202882;Note=Nitrogen permease regulator 3 +P38742 UniProtKB Compositional bias 149 315 . . . Note=Ser-rich +P38742 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P38742 UniProtKB Modified residue 486 486 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38742 UniProtKB Modified residue 987 987 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region Q03718 1 556 +Q03718 UniProtKB Chain 1 556 . . . ID=PRO_0000057963;Note=Non-structural maintenance of chromosome element 5 +##sequence-region P32499 1 720 +P32499 UniProtKB Chain 1 720 . . . ID=PRO_0000204903;Note=Nucleoporin NUP2 +P32499 UniProtKB Repeat 67 69 . . . Note=FXF 1 +P32499 UniProtKB Repeat 189 192 . . . Note=FXFG 1 +P32499 UniProtKB Repeat 216 218 . . . Note=FXF 2 +P32499 UniProtKB Repeat 247 249 . . . Note=FXF 3 +P32499 UniProtKB Repeat 285 288 . . . Note=FXFG 2 +P32499 UniProtKB Repeat 302 305 . . . Note=FXFG 3 +P32499 UniProtKB Repeat 318 321 . . . Note=FXFG 4 +P32499 UniProtKB Repeat 352 354 . . . Note=FXF 4 +P32499 UniProtKB Repeat 369 372 . . . Note=FXFG 5 +P32499 UniProtKB Repeat 386 389 . . . Note=FXFG 6 +P32499 UniProtKB Repeat 438 441 . . . Note=FXFG 7 +P32499 UniProtKB Repeat 474 477 . . . Note=FXFG 8 +P32499 UniProtKB Repeat 493 496 . . . Note=FXFG 9 +P32499 UniProtKB Repeat 511 514 . . . Note=FXFG 10 +P32499 UniProtKB Repeat 524 527 . . . Note=FXFG 11 +P32499 UniProtKB Repeat 550 552 . . . Note=FXF 5 +P32499 UniProtKB Domain 583 720 . . . Note=RanBD1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00164 +P32499 UniProtKB Region 35 50 . . . Note=Interaction with SRP1 NLS binding site 1 +P32499 UniProtKB Compositional bias 333 377 . . . Note=Ser-rich +P32499 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P32499 UniProtKB Modified residue 20 20 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P32499 UniProtKB Modified residue 137 137 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32499 UniProtKB Modified residue 165 165 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P32499 UniProtKB Modified residue 203 203 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P32499 UniProtKB Modified residue 205 205 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P32499 UniProtKB Modified residue 348 348 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32499 UniProtKB Modified residue 351 351 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32499 UniProtKB Modified residue 361 361 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32499 UniProtKB Modified residue 581 581 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32499 UniProtKB Modified residue 590 590 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32499 UniProtKB Sequence conflict 137 137 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32499 UniProtKB Sequence conflict 370 370 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32499 UniProtKB Sequence conflict 418 418 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32499 UniProtKB Turn 12 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C1T +P32499 UniProtKB Helix 34 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C1T +P32499 UniProtKB Turn 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UN0 +##sequence-region P49686 1 430 +P49686 UniProtKB Chain 1 430 . . . ID=PRO_0000204866;Note=Nucleoporin NUP42 +P49686 UniProtKB Repeat 2 5 . . . Note=SXFG 1 +P49686 UniProtKB Repeat 38 46 . . . Note=SAFGXPXFG 1 +P49686 UniProtKB Repeat 58 66 . . . Note=SAFGXPXFG 2 +P49686 UniProtKB Repeat 78 81 . . . Note=SXFG 2 +P49686 UniProtKB Repeat 90 98 . . . Note=SAFGXPXFG 3 +P49686 UniProtKB Repeat 112 120 . . . Note=SAFGXPXFG 4 +P49686 UniProtKB Repeat 124 125 . . . Note=FG 1 +P49686 UniProtKB Repeat 134 135 . . . Note=FG 2 +P49686 UniProtKB Repeat 143 151 . . . Note=SAFGXPXFG 5 +P49686 UniProtKB Repeat 168 171 . . . Note=SXFG 3 +P49686 UniProtKB Repeat 182 185 . . . Note=SXFG 4 +P49686 UniProtKB Repeat 200 208 . . . Note=SAFGXPXFG 6 +P49686 UniProtKB Repeat 215 218 . . . Note=SXFG 5 +P49686 UniProtKB Repeat 232 235 . . . Note=SXFG 6 +P49686 UniProtKB Repeat 259 262 . . . Note=SXFG 7 +P49686 UniProtKB Repeat 277 280 . . . Note=SXFG 8 +P49686 UniProtKB Repeat 296 297 . . . Note=FG 3 +P49686 UniProtKB Repeat 312 315 . . . Note=SXFG 9 +P49686 UniProtKB Repeat 319 322 . . . Note=FG 4 +P49686 UniProtKB Repeat 339 340 . . . Note=FG 5 +P49686 UniProtKB Repeat 361 364 . . . Note=FG 6 +P49686 UniProtKB Region 121 230 . . . Note=Interactions with CRM1 and GFD1 +P49686 UniProtKB Region 365 430 . . . Note=Interaction with GLE1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10610322;Dbxref=PMID:10610322 +P49686 UniProtKB Compositional bias 269 273 . . . Note=Poly-Asn +P49686 UniProtKB Compositional bias 423 426 . . . Note=Poly-Pro +P49686 UniProtKB Modified residue 137 137 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P49686 UniProtKB Modified residue 298 298 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P49686 UniProtKB Sequence conflict 331 331 . . . Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P49686 UniProtKB Sequence conflict 419 419 . . . Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P48837 1 541 +P48837 UniProtKB Chain 1 541 . . . ID=PRO_0000204877;Note=Nucleoporin NUP57 +P48837 UniProtKB Repeat 2 3 . . . Note=FG 1 +P48837 UniProtKB Repeat 11 12 . . . Note=FG 2 +P48837 UniProtKB Repeat 21 24 . . . Note=FXFG 1 +P48837 UniProtKB Repeat 39 42 . . . Note=FXFG 2 +P48837 UniProtKB Repeat 56 57 . . . Note=FG 3 +P48837 UniProtKB Repeat 65 66 . . . Note=FG 4 +P48837 UniProtKB Repeat 76 79 . . . Note=GLFG 1 +P48837 UniProtKB Repeat 103 106 . . . Note=GLFG 2 +P48837 UniProtKB Repeat 120 123 . . . Note=GLFG 3 +P48837 UniProtKB Repeat 132 135 . . . Note=GLFG 4 +P48837 UniProtKB Repeat 147 150 . . . Note=GLFG 5 +P48837 UniProtKB Repeat 175 178 . . . Note=GLFG 6 +P48837 UniProtKB Repeat 190 193 . . . Note=GLFG 7 +P48837 UniProtKB Repeat 204 207 . . . Note=GLFG 8 +P48837 UniProtKB Repeat 220 223 . . . Note=GLFG 9 +P48837 UniProtKB Coiled coil 398 425 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48837 UniProtKB Compositional bias 3 223 . . . Note=Gly-rich +P48837 UniProtKB Compositional bias 26 31 . . . Note=Poly-Asn +P48837 UniProtKB Compositional bias 127 130 . . . Note=Poly-Thr +P48837 UniProtKB Compositional bias 217 220 . . . Note=Poly-Gly +P48837 UniProtKB Compositional bias 224 291 . . . Note=Gln-rich +P48837 UniProtKB Compositional bias 258 266 . . . Note=Poly-Gln +P48837 UniProtKB Compositional bias 277 280 . . . Note=Poly-Gln +##sequence-region Q05166 1 528 +Q05166 UniProtKB Chain 1 528 . . . ID=PRO_0000204878;Note=Nucleoporin ASM4 +Q05166 UniProtKB Repeat 2 3 . . . Note=FG 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785 +Q05166 UniProtKB Repeat 61 62 . . . Note=FG 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785 +Q05166 UniProtKB Repeat 195 196 . . . Note=FG 3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785 +Q05166 UniProtKB Domain 265 394 . . . Note=RRM Nup35-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00804 +Q05166 UniProtKB Repeat 274 275 . . . Note=FG 4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785 +Q05166 UniProtKB Repeat 291 292 . . . Note=FG 5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785 +Q05166 UniProtKB Repeat 523 524 . . . Note=FG 6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12604785;Dbxref=PMID:12604785 +Q05166 UniProtKB Coiled coil 490 510 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05166 UniProtKB Compositional bias 19 49 . . . Note=Gln-rich +Q05166 UniProtKB Compositional bias 28 46 . . . Note=Poly-Gln +Q05166 UniProtKB Compositional bias 63 178 . . . Note=Asn-rich +Q05166 UniProtKB Compositional bias 84 87 . . . Note=Poly-Asn +Q05166 UniProtKB Modified residue 458 458 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05166 UniProtKB Modified residue 464 464 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05166 UniProtKB Sequence conflict 114 114 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q05166 UniProtKB Sequence conflict 171 171 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q05166 UniProtKB Sequence conflict 446 528 . . . Note=PAGHAGNPTNISSPIVANSPNKRLDVIDGKLPFMQNAGPNSNIPNLLRNLESKMRQQEAKYRNNEPAGFTHKLSNWLFGWNDL->LPVMLVIQQIFQVQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12066 1 484 +Q12066 UniProtKB Chain 1 484 . . . ID=PRO_0000202586;Note=Nuclear rim protein 1 +Q12066 UniProtKB Transmembrane 145 165 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12066 UniProtKB Transmembrane 252 272 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12066 UniProtKB Modified residue 3 3 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12066 UniProtKB Modified residue 417 417 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12066 UniProtKB Modified residue 474 474 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P32332 1 324 +P32332 UniProtKB Chain 1 324 . . . ID=PRO_0000090689;Note=Mitochondrial oxaloacetate transport protein +P32332 UniProtKB Transmembrane 26 46 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32332 UniProtKB Transmembrane 79 99 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32332 UniProtKB Transmembrane 132 152 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32332 UniProtKB Transmembrane 193 213 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32332 UniProtKB Transmembrane 233 253 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32332 UniProtKB Transmembrane 284 305 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32332 UniProtKB Repeat 20 111 . . . Note=Solcar 1 +P32332 UniProtKB Repeat 126 218 . . . Note=Solcar 2 +P32332 UniProtKB Repeat 227 312 . . . Note=Solcar 3 +##sequence-region P39720 1 1047 +P39720 UniProtKB Chain 1 1047 . . . ID=PRO_0000114990;Note=Oleate-activated transcription factor 1 +P39720 UniProtKB DNA binding 66 93 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P39720 UniProtKB Motif 1034 1042 . . . Note=9aaTAD +P39720 UniProtKB Modified residue 155 155 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39720 UniProtKB Sequence conflict 70 70 . . . Note=R->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39720 UniProtKB Sequence conflict 447 447 . . . Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39720 UniProtKB Sequence conflict 588 588 . . . Note=K->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53949 1 197 +P53949 UniProtKB Chain 1 197 . . . ID=PRO_0000203451;Note=Tyrosine-protein phosphatase-like protein OCA2 +P53949 UniProtKB Modified residue 181 181 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53949 UniProtKB Sequence conflict 11 11 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07913 1 336 +Q07913 UniProtKB Chain 1 336 . . . ID=PRO_0000114116;Note=Non-structural maintenance of chromosomes element 1 +Q07913 UniProtKB Zinc finger 268 327 . . . Note=NSE1-type +##sequence-region P38837 1 291 +P38837 UniProtKB Chain 1 291 . . . ID=PRO_0000202918;Note=Protein NSG1 +P38837 UniProtKB Topological domain 1 96 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38837 UniProtKB Transmembrane 97 117 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38837 UniProtKB Topological domain 118 156 . . . Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38837 UniProtKB Transmembrane 157 177 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38837 UniProtKB Topological domain 178 230 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38837 UniProtKB Transmembrane 231 251 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38837 UniProtKB Topological domain 252 261 . . . Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38837 UniProtKB Transmembrane 262 282 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38837 UniProtKB Topological domain 283 291 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38837 UniProtKB Modified residue 39 39 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198 +P38837 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38837 UniProtKB Sequence conflict 8 8 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12143 1 216 +Q12143 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12143 UniProtKB Chain 2 216 . . . ID=PRO_0000057965;Note=Kinetochore-associated protein NSL1 +Q12143 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12143 UniProtKB Sequence conflict 212 212 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P14907 1 823 +P14907 UniProtKB Chain 1 823 . . . ID=PRO_0000204865;Note=Nucleoporin NSP1 +P14907 UniProtKB Repeat 13 16 . . . Note=FSFG 1 +P14907 UniProtKB Repeat 36 37 . . . Note=FG 1 +P14907 UniProtKB Repeat 43 44 . . . Note=FG 2 +P14907 UniProtKB Repeat 64 65 . . . Note=FG 3 +P14907 UniProtKB Repeat 74 75 . . . Note=FG 4 +P14907 UniProtKB Repeat 84 85 . . . Note=FG 5 +P14907 UniProtKB Repeat 94 95 . . . Note=FG 6 +P14907 UniProtKB Repeat 104 105 . . . Note=FG 7 +P14907 UniProtKB Repeat 123 124 . . . Note=FG 8 +P14907 UniProtKB Repeat 142 143 . . . Note=FG 9 +P14907 UniProtKB Repeat 147 148 . . . Note=FG 10 +P14907 UniProtKB Repeat 168 169 . . . Note=FG 11 +P14907 UniProtKB Repeat 179 182 . . . Note=FSFG 2 +P14907 UniProtKB Repeat 217 220 . . . Note=FSFG 3 +P14907 UniProtKB Repeat 239 240 . . . Note=FG 12 +P14907 UniProtKB Repeat 268 269 . . . Note=FG 13 +P14907 UniProtKB Repeat 284 287 . . . Note=FSFG 4 +P14907 UniProtKB Repeat 303 306 . . . Note=FSFG 5 +P14907 UniProtKB Repeat 322 325 . . . Note=FSFG 6 +P14907 UniProtKB Repeat 341 344 . . . Note=FSFG 7 +P14907 UniProtKB Repeat 360 363 . . . Note=FSFG 8 +P14907 UniProtKB Repeat 379 382 . . . Note=FSFG 9 +P14907 UniProtKB Repeat 398 401 . . . Note=FSFG 10 +P14907 UniProtKB Repeat 417 420 . . . Note=FSFG 11 +P14907 UniProtKB Repeat 436 439 . . . Note=FSFG 12 +P14907 UniProtKB Repeat 455 458 . . . Note=FSFG 13 +P14907 UniProtKB Repeat 474 477 . . . Note=FSFG 14 +P14907 UniProtKB Repeat 493 496 . . . Note=FSFG 15 +P14907 UniProtKB Repeat 512 515 . . . Note=FSFG 16 +P14907 UniProtKB Repeat 531 534 . . . Note=FSFG 17 +P14907 UniProtKB Repeat 550 553 . . . Note=FSFG 18 +P14907 UniProtKB Repeat 571 572 . . . Note=FG 14 +P14907 UniProtKB Repeat 588 591 . . . Note=FSFG 19%3B approximate +P14907 UniProtKB Region 673 738 . . . Note=Competitive binding site of NUP57 and NUP82 +P14907 UniProtKB Region 740 823 . . . Note=Required for association with NUP57 subcomplex +P14907 UniProtKB Coiled coil 630 823 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14907 UniProtKB Compositional bias 2 175 . . . Note=Asn-rich +P14907 UniProtKB Compositional bias 308 628 . . . Note=Lys-rich +P14907 UniProtKB Modified residue 238 238 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14907 UniProtKB Modified residue 361 361 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14907 UniProtKB Modified residue 456 456 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14907 UniProtKB Modified residue 631 631 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P35729 1 1037 +P35729 UniProtKB Chain 1 1037 . . . ID=PRO_0000204836;Note=Nucleoporin NUP120 +P35729 UniProtKB Region 131 152 . . . Note=Leucine-zipper 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35729 UniProtKB Region 290 311 . . . Note=Leucine-zipper 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35729 UniProtKB Modified residue 417 417 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P35729 UniProtKB Beta strand 2 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Turn 11 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 16 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 23 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 55 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HXR +P35729 UniProtKB Beta strand 67 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 78 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Helix 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Turn 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 92 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H7N +P35729 UniProtKB Helix 104 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 108 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 114 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 128 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Helix 135 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Turn 158 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 163 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 170 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 179 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HXR +P35729 UniProtKB Beta strand 183 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HXR +P35729 UniProtKB Beta strand 187 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Helix 203 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 216 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H7N +P35729 UniProtKB Beta strand 223 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Turn 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 233 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 242 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Turn 248 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 252 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Turn 259 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 280 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 293 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 297 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 307 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H7N +P35729 UniProtKB Beta strand 312 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 318 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Turn 325 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 330 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 343 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HXR +P35729 UniProtKB Beta strand 348 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 360 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 370 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 375 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 383 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HXR +P35729 UniProtKB Helix 386 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Helix 406 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Helix 417 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Turn 429 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Helix 440 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 460 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Turn 467 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 470 477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 480 486 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Helix 489 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Turn 495 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Helix 505 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Helix 522 537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 538 540 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 542 544 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H7N +P35729 UniProtKB Helix 546 557 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Turn 558 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Helix 564 574 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Helix 579 588 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Turn 589 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Helix 609 639 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Turn 644 647 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Helix 648 670 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Helix 672 680 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 681 684 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Beta strand 685 688 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HXR +P35729 UniProtKB Helix 695 711 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +P35729 UniProtKB Helix 719 728 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F7F +##sequence-region P40064 1 1391 +P40064 UniProtKB Chain 1 1391 . . . ID=PRO_0000204848;Note=Nucleoporin NUP157 +P40064 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40064 UniProtKB Modified residue 1034 1034 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40064 UniProtKB Helix 90 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 122 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Turn 129 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 133 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 138 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 148 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Turn 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 161 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Turn 167 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 171 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 179 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Turn 185 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 191 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 201 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Turn 214 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 218 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 244 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Turn 256 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 260 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Turn 267 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 271 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 284 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 303 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 341 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Turn 349 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 353 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 363 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 372 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 381 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 397 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Turn 401 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 406 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Turn 414 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 418 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 431 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 447 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 483 486 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 500 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Turn 503 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 506 512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 536 543 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 545 551 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 555 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 567 574 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 581 583 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Turn 584 587 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 589 592 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Turn 593 595 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 600 614 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 617 623 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Turn 624 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 629 635 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 637 649 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 655 667 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Turn 670 672 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 707 719 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Turn 720 725 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 726 729 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Beta strand 745 747 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 749 768 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 770 772 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 787 815 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 816 818 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 819 829 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 838 845 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 849 853 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 857 872 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +P40064 UniProtKB Helix 879 890 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MHC +##sequence-region P40477 1 1460 +P40477 UniProtKB Chain 1 1460 . . . ID=PRO_0000204849;Note=Nucleoporin NUP159 +P40477 UniProtKB Repeat 228 231 . . . Note=FG 1 +P40477 UniProtKB Repeat 267 270 . . . Note=PXFG 1 +P40477 UniProtKB Repeat 462 470 . . . Note=SXFGXPXFG 1 +P40477 UniProtKB Repeat 503 511 . . . Note=SXFGXPXFG 2%3B approximate +P40477 UniProtKB Repeat 522 530 . . . Note=SXFGXPXFG 3%3B approximate +P40477 UniProtKB Repeat 532 535 . . . Note=PXFG 2 +P40477 UniProtKB Repeat 548 556 . . . Note=SXFGXPXFG 4 +P40477 UniProtKB Repeat 558 561 . . . Note=PXFG 3 +P40477 UniProtKB Repeat 574 582 . . . Note=SXFGXPXFG 5 +P40477 UniProtKB Repeat 584 587 . . . Note=PXFG 4 +P40477 UniProtKB Repeat 600 608 . . . Note=SXFGXPXFG 6 +P40477 UniProtKB Repeat 610 613 . . . Note=SXFG 1 +P40477 UniProtKB Repeat 624 632 . . . Note=SXFGXPXFG 7%3B approximate +P40477 UniProtKB Repeat 642 645 . . . Note=FG 2 +P40477 UniProtKB Repeat 687 690 . . . Note=FG 3 +P40477 UniProtKB Repeat 704 707 . . . Note=FXFG 1 +P40477 UniProtKB Repeat 709 712 . . . Note=SXFG 2 +P40477 UniProtKB Repeat 728 731 . . . Note=FXFG 2 +P40477 UniProtKB Repeat 842 845 . . . Note=PXFG 5 +P40477 UniProtKB Repeat 873 876 . . . Note=FXFG 3 +P40477 UniProtKB Region 1 500 . . . Note=Interaction with DBP5 +P40477 UniProtKB Region 497 701 . . . Note=Interactions with CRM1 and GLE1 +P40477 UniProtKB Region 1223 1460 . . . Note=Interaction with NUP82;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9736720;Dbxref=PMID:9736720 +P40477 UniProtKB Coiled coil 1279 1320 . . . . +P40477 UniProtKB Coiled coil 1383 1418 . . . . +P40477 UniProtKB Compositional bias 455 766 . . . Note=Ser-rich +P40477 UniProtKB Modified residue 404 404 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P40477 UniProtKB Modified residue 657 657 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40477 UniProtKB Modified residue 724 724 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40477 UniProtKB Modified residue 735 735 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40477 UniProtKB Modified residue 745 745 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40477 UniProtKB Modified residue 803 803 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P40477 UniProtKB Modified residue 805 805 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40477 UniProtKB Modified residue 819 819 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40477 UniProtKB Modified residue 889 889 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40477 UniProtKB Modified residue 940 940 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40477 UniProtKB Beta strand 10 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 17 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 42 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Turn 46 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 50 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 58 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Helix 64 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 73 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 81 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 89 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 98 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 118 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 128 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 135 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 145 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Turn 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 157 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 171 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 183 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 192 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Helix 203 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Turn 210 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 213 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 245 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 256 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 278 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 286 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 292 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 305 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 309 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Helix 318 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Turn 328 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 336 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 364 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 372 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XIP +P40477 UniProtKB Beta strand 1118 1123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DS1 +P40477 UniProtKB Helix 1436 1454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +##sequence-region P08466 1 329 +P08466 UniProtKB Chain 1 329 . . . ID=PRO_0000178670;Note=Mitochondrial nuclease +P08466 UniProtKB Active site 138 138 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10047 +P08466 UniProtKB Metal binding 170 170 . . . Note=Magnesium or manganese%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P40010 1 520 +P40010 UniProtKB Chain 1 520 . . . ID=PRO_0000122452;Note=Nuclear GTP-binding protein NUG1 +P40010 UniProtKB Domain 165 343 . . . Note=CP-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01058 +P40010 UniProtKB Nucleotide binding 213 216 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40010 UniProtKB Nucleotide binding 287 294 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40010 UniProtKB Nucleotide binding 336 339 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40010 UniProtKB Modified residue 337 337 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q00402 1 2748 +Q00402 UniProtKB Chain 1 2748 . . . ID=PRO_0000057997;Note=Nuclear migration protein NUM1 +Q00402 UniProtKB Repeat 593 656 . . . Note=1 +Q00402 UniProtKB Repeat 657 727 . . . Note=2 +Q00402 UniProtKB Repeat 728 798 . . . Note=3 +Q00402 UniProtKB Repeat 799 862 . . . Note=4 +Q00402 UniProtKB Repeat 863 926 . . . Note=5 +Q00402 UniProtKB Repeat 927 990 . . . Note=6 +Q00402 UniProtKB Repeat 991 1054 . . . Note=7 +Q00402 UniProtKB Repeat 1055 1118 . . . Note=8 +Q00402 UniProtKB Repeat 1119 1182 . . . Note=9 +Q00402 UniProtKB Repeat 1183 1246 . . . Note=10 +Q00402 UniProtKB Repeat 1247 1310 . . . Note=11 +Q00402 UniProtKB Repeat 1311 1374 . . . Note=12 +Q00402 UniProtKB Repeat 1375 1384 . . . Note=13%3B truncated +Q00402 UniProtKB Domain 2573 2683 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +Q00402 UniProtKB Region 593 1384 . . . Note=13 X tandem repeats +Q00402 UniProtKB Modified residue 611 611 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q00402 UniProtKB Modified residue 675 675 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q00402 UniProtKB Modified residue 746 746 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q00402 UniProtKB Modified residue 881 881 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q00402 UniProtKB Modified residue 945 945 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q00402 UniProtKB Modified residue 1009 1009 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q00402 UniProtKB Modified residue 1201 1201 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q00402 UniProtKB Modified residue 1265 1265 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q00402 UniProtKB Modified residue 1329 1329 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q00402 UniProtKB Modified residue 2162 2162 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00402 UniProtKB Modified residue 2164 2164 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00402 UniProtKB Modified residue 2197 2197 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +Q00402 UniProtKB Modified residue 2217 2217 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00402 UniProtKB Modified residue 2220 2220 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q00402 UniProtKB Modified residue 2221 2221 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q00402 UniProtKB Modified residue 2360 2360 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00402 UniProtKB Modified residue 2424 2424 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00402 UniProtKB Modified residue 2494 2494 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00402 UniProtKB Modified residue 2545 2545 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00402 UniProtKB Sequence conflict 1570 1570 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00402 UniProtKB Sequence conflict 1822 1822 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00402 UniProtKB Sequence conflict 1960 1962 . . . Note=KAS->RHL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00402 UniProtKB Sequence conflict 1971 1972 . . . Note=KD->RN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00402 UniProtKB Sequence conflict 2049 2049 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00402 UniProtKB Sequence conflict 2637 2637 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39705 1 539 +P39705 UniProtKB Chain 1 539 . . . ID=PRO_0000204879;Note=Nucleoporin NUP60 +P39705 UniProtKB Repeat 399 401 . . . Note=FXF 1 +P39705 UniProtKB Repeat 427 429 . . . Note=FXF 2 +P39705 UniProtKB Repeat 469 471 . . . Note=FXF 3 +P39705 UniProtKB Repeat 509 511 . . . Note=FXF 4 +P39705 UniProtKB Coiled coil 91 118 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39705 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P39705 UniProtKB Modified residue 49 49 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P39705 UniProtKB Modified residue 81 81 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P39705 UniProtKB Modified residue 89 89 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39705 UniProtKB Modified residue 162 162 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39705 UniProtKB Modified residue 171 171 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39705 UniProtKB Modified residue 214 214 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39705 UniProtKB Modified residue 222 222 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39705 UniProtKB Modified residue 352 352 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P39705 UniProtKB Modified residue 360 360 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P39705 UniProtKB Modified residue 374 374 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P39705 UniProtKB Modified residue 382 382 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39705 UniProtKB Modified residue 460 460 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39705 UniProtKB Modified residue 480 480 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P39705 UniProtKB Modified residue 483 483 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region P40368 1 713 +P40368 UniProtKB Chain 1 713 . . . ID=PRO_0000204883;Note=Nucleoporin NUP82 +P40368 UniProtKB Region 1 409 . . . Note=Interaction with NUP116;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10891509;Dbxref=PMID:10891509 +P40368 UniProtKB Region 463 713 . . . Note=Interaction with NSP1 and NUP159;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9843582;Dbxref=PMID:9843582 +P40368 UniProtKB Coiled coil 582 713 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40368 UniProtKB Motif 607 623 . . . Note=Bipartite nuclear localization signal +P40368 UniProtKB Beta strand 5 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TKN +P40368 UniProtKB Turn 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TKN +P40368 UniProtKB Beta strand 24 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Turn 30 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 34 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 42 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Turn 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 55 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Turn 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 70 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 77 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 85 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Helix 103 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 110 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Helix 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 119 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TKN +P40368 UniProtKB Beta strand 127 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Helix 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 141 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 151 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 164 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 171 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 182 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 194 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 204 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 214 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Helix 220 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Helix 243 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Turn 265 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 269 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Helix 274 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 286 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Helix 293 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 299 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 308 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 313 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Turn 320 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 323 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 347 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 362 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 372 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 378 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Helix 387 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Helix 403 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 413 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 425 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 434 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +P40368 UniProtKB Beta strand 445 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBP +##sequence-region P38881 1 321 +P38881 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38881 UniProtKB Chain 23 321 . . . ID=PRO_0000202937;Note=Nucleus-vacuole junction protein 1 +P38881 UniProtKB Transmembrane 94 114 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38881 UniProtKB Region 73 125 . . . Note=TSC13-binding +P38881 UniProtKB Region 139 195 . . . Note=OSH1-binding +P38881 UniProtKB Region 233 321 . . . Note=VAC8-binding +P38881 UniProtKB Compositional bias 235 303 . . . Note=Ser-rich +P38881 UniProtKB Modified residue 156 156 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P38881 UniProtKB Modified residue 199 199 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38881 UniProtKB Modified residue 285 285 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38881 UniProtKB Modified residue 298 298 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40354 1 457 +P40354 UniProtKB Chain 1 457 . . . ID=PRO_0000204068;Note=Protein N-terminal amidase +P40354 UniProtKB Domain 19 453 . . . Note=CN hydrolase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054 +P40354 UniProtKB Active site 63 63 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054 +P40354 UniProtKB Active site 136 136 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054 +P40354 UniProtKB Active site 187 187 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00054 +##sequence-region P38302 1 140 +P38302 UniProtKB Chain 1 140 . . . ID=PRO_0000057974;Note=Pre-mRNA-splicing factor NTC20 +P38302 UniProtKB Modified residue 139 139 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P31378 1 399 +P31378 UniProtKB Transit peptide 1 26 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183 +P31378 UniProtKB Chain 27 399 . . . ID=PRO_0000001744;Note=Endonuclease III homolog 1 +P31378 UniProtKB Domain 223 247 . . . Note=HhH;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183 +P31378 UniProtKB Motif 14 37 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31378 UniProtKB Active site 243 243 . . . Note=Nucleophile%3B for N-glycosylase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183 +P31378 UniProtKB Site 262 262 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03183 +P31378 UniProtKB Cross-link 194 194 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31378 UniProtKB Mutagenesis 3 6 . . . Note=In NTG1(mts)%3B reduces mitochondrial localization by 40%25. KISK->EISE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20194111;Dbxref=PMID:20194111 +P31378 UniProtKB Mutagenesis 15 16 . . . Note=In NTG1(nls1)%3B reduces nuclear localization by 60%25. KR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20194111;Dbxref=PMID:20194111 +P31378 UniProtKB Mutagenesis 33 34 . . . Note=In NTG1(nls2)%3B reduces nuclear localization by 60%25. KR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20194111;Dbxref=PMID:20194111 +P31378 UniProtKB Mutagenesis 243 243 . . . Note=Abolishes cleavage of substrate oligonucleotides. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20194111;Dbxref=PMID:20194111 +P31378 UniProtKB Mutagenesis 364 364 . . . Note=Cannot properly relocalize in response to oxidative stress. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19029246;Dbxref=PMID:19029246 +##sequence-region P49687 1 1317 +P49687 UniProtKB Chain 1 605 . . . ID=PRO_0000019927;Note=Nucleoporin NUP145N +P49687 UniProtKB Chain 606 1317 . . . ID=PRO_0000019928;Note=Nucleoporin NUP145C +P49687 UniProtKB Repeat 12 13 . . . Note=FG 1 +P49687 UniProtKB Repeat 39 42 . . . Note=GLFG 1 +P49687 UniProtKB Repeat 79 80 . . . Note=FG 2 +P49687 UniProtKB Repeat 89 92 . . . Note=GLFG 2 +P49687 UniProtKB Repeat 106 107 . . . Note=FG 3 +P49687 UniProtKB Repeat 136 139 . . . Note=GLFG 3 +P49687 UniProtKB Repeat 154 157 . . . Note=GLFG 4 +P49687 UniProtKB Repeat 168 171 . . . Note=GLFG 5 +P49687 UniProtKB Repeat 181 184 . . . Note=GLFG 6 +P49687 UniProtKB Repeat 193 196 . . . Note=GLFG 7%3B approximate +P49687 UniProtKB Repeat 206 209 . . . Note=GLFG 8 +P49687 UniProtKB Domain 458 605 . . . Note=Peptidase S59;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00765 +P49687 UniProtKB Region 398 523 . . . Note=Required for autocatalytic cleavage +P49687 UniProtKB Region 460 604 . . . Note=Nucleoporin RNA-binding motif (NRM) +P49687 UniProtKB Motif 369 385 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P49687 UniProtKB Compositional bias 43 145 . . . Note=Asn-rich +P49687 UniProtKB Compositional bias 140 145 . . . Note=Poly-Asn +P49687 UniProtKB Modified residue 273 273 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P49687 UniProtKB Modified residue 403 403 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P49687 UniProtKB Modified residue 404 404 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P49687 UniProtKB Modified residue 414 414 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P49687 UniProtKB Modified residue 667 667 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P49687 UniProtKB Modified residue 679 679 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P49687 UniProtKB Modified residue 689 689 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P49687 UniProtKB Modified residue 751 751 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P49687 UniProtKB Mutagenesis 604 604 . . . Note=Loss of autocatalytic cleavage%3B when associated with L-608. H->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9305650;Dbxref=PMID:9305650 +P49687 UniProtKB Mutagenesis 605 605 . . . Note=Loss of autocatalytic cleavage%3B when associated with R-608. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9305650;Dbxref=PMID:9305650 +P49687 UniProtKB Mutagenesis 606 606 . . . Note=Loss of autocatalytic cleavage. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10542288;Dbxref=PMID:10542288 +P49687 UniProtKB Mutagenesis 608 608 . . . Note=Loss of autocatalytic cleavage%3B when associated with P-604. W->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9305650;Dbxref=PMID:9305650 +P49687 UniProtKB Mutagenesis 608 608 . . . Note=Loss of autocatalytic cleavage%3B when associated with F-605. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9305650;Dbxref=PMID:9305650 +P49687 UniProtKB Sequence conflict 281 282 . . . Note=NA->QR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P49687 UniProtKB Sequence conflict 1142 1142 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P49687 UniProtKB Sequence conflict 1310 1316 . . . Note=LMKCTYK->FEVYI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P49687 UniProtKB Helix 454 458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KES +P49687 UniProtKB Beta strand 461 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Helix 467 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Helix 477 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Beta strand 480 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Beta strand 485 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Turn 489 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Beta strand 492 498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Helix 503 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Helix 509 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Turn 515 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Beta strand 518 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Turn 522 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Beta strand 525 528 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Turn 532 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Beta strand 546 552 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Turn 558 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Helix 570 582 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Beta strand 584 592 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Turn 593 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Beta strand 597 603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEP +P49687 UniProtKB Turn 731 733 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P49687 UniProtKB Helix 738 746 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Turn 747 749 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Beta strand 757 759 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P49687 UniProtKB Turn 761 763 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG0 +P49687 UniProtKB Beta strand 765 769 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P49687 UniProtKB Beta strand 772 775 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG0 +P49687 UniProtKB Helix 788 791 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 793 801 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Beta strand 803 807 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Beta strand 809 812 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P49687 UniProtKB Beta strand 814 819 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 823 827 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 835 846 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 859 881 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 883 891 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 896 904 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Turn 905 907 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 909 918 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 922 931 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 936 948 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Turn 950 952 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P49687 UniProtKB Helix 958 968 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Beta strand 971 974 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG0 +P49687 UniProtKB Helix 979 983 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 987 996 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Turn 997 1002 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P49687 UniProtKB Helix 1005 1015 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 1023 1032 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 1034 1036 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +P49687 UniProtKB Helix 1037 1045 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 1053 1064 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 1073 1089 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 1093 1100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 1106 1119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 1122 1124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Turn 1126 1129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 1132 1135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +P49687 UniProtKB Helix 1140 1157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BG1 +##sequence-region P38219 1 394 +P38219 UniProtKB Chain 1 394 . . . ID=PRO_0000122462;Note=Obg-like ATPase 1 +P38219 UniProtKB Domain 21 285 . . . Note=OBG-type G +P38219 UniProtKB Nucleotide binding 30 35 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03167 +P38219 UniProtKB Metal binding 34 34 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38219 UniProtKB Metal binding 55 55 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38219 UniProtKB Binding site 233 233 . . . Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03167 +P38219 UniProtKB Modified residue 89 89 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38219 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38219 UniProtKB Modified residue 119 119 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38219 UniProtKB Cross-link 98 98 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P53204 1 395 +P53204 UniProtKB Chain 1 395 . . . ID=PRO_0000135019;Note=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 +P53204 UniProtKB Nucleotide binding 166 168 . . . Note=ATP;Ontology_term=ECO:0000250,ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66,ECO:0000250|UniProtKB:Q9HAN9 +P53204 UniProtKB Nucleotide binding 282 284 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66 +P53204 UniProtKB Nucleotide binding 350 353 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66 +P53204 UniProtKB Region 206 208 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HAN9 +P53204 UniProtKB Region 244 247 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HAN9 +P53204 UniProtKB Region 294 295 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HAN9 +P53204 UniProtKB Binding site 175 175 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66 +P53204 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53204 UniProtKB Modified residue 89 89 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53204 UniProtKB Modified residue 90 90 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P53883 1 403 +P53883 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P53883 UniProtKB Chain 2 403 . . . ID=PRO_0000082036;Note=Nucleolar protein 13 +P53883 UniProtKB Domain 125 219 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P53883 UniProtKB Domain 239 317 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P53883 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P53883 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:18407956 +P53883 UniProtKB Modified residue 105 105 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53883 UniProtKB Modified residue 335 335 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53883 UniProtKB Sequence conflict 296 296 . . . Note=A->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53927 1 220 +P53927 UniProtKB Chain 1 220 . . . ID=PRO_0000082035;Note=Ribosome biogenesis protein 15 +P53927 UniProtKB Domain 91 169 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P53927 UniProtKB Beta strand 89 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P +P53927 UniProtKB Helix 104 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P +P53927 UniProtKB Helix 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P +P53927 UniProtKB Beta strand 117 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P +P53927 UniProtKB Turn 126 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P +P53927 UniProtKB Beta strand 131 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P +P53927 UniProtKB Helix 142 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P +P53927 UniProtKB Beta strand 163 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P +P53927 UniProtKB Helix 173 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P +P53927 UniProtKB Helix 181 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P +P53927 UniProtKB Turn 187 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T9P +##sequence-region P25655 1 2108 +P25655 UniProtKB Chain 1 2108 . . . ID=PRO_0000096955;Note=General negative regulator of transcription subunit 1 +P25655 UniProtKB Coiled coil 795 813 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25655 UniProtKB Coiled coil 1021 1046 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25655 UniProtKB Compositional bias 1009 1046 . . . Note=Gln-rich +P25655 UniProtKB Compositional bias 1300 1329 . . . Note=Gln-rich +P25655 UniProtKB Modified residue 2102 2102 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:18407956 +P25655 UniProtKB Sequence conflict 526 526 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25655 UniProtKB Sequence conflict 569 569 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25655 UniProtKB Helix 194 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 198 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 201 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 234 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 249 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 254 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 275 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 288 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 301 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Turn 316 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 323 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Beta strand 334 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 343 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 347 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Turn 359 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 367 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 384 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 395 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 405 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 424 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 427 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 437 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 457 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 468 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 479 482 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 484 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 495 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Turn 505 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 508 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Turn 530 532 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 536 547 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 553 569 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 571 573 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Turn 574 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 581 585 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Beta strand 589 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 595 609 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 615 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 631 647 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 648 653 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 656 671 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 677 691 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 698 709 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 710 716 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 718 727 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 729 733 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Helix 735 743 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8B +P25655 UniProtKB Beta strand 765 767 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P25655 UniProtKB Helix 783 795 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Turn 798 800 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Helix 801 811 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Helix 814 816 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Helix 817 827 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Turn 828 831 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Helix 833 835 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Helix 836 846 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Helix 849 867 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Helix 872 874 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Helix 877 890 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Helix 892 894 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Turn 900 902 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Helix 905 914 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Helix 918 929 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Helix 930 932 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Beta strand 936 939 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Helix 943 958 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Helix 963 975 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +P25655 UniProtKB Helix 980 982 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B89 +##sequence-region P06102 1 836 +P06102 UniProtKB Chain 1 836 . . . ID=PRO_0000198337;Note=General negative regulator of transcription subunit 3 +P06102 UniProtKB Coiled coil 36 68 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06102 UniProtKB Coiled coil 119 195 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06102 UniProtKB Coiled coil 255 292 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06102 UniProtKB Coiled coil 803 831 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06102 UniProtKB Modified residue 303 303 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06102 UniProtKB Modified residue 307 307 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06102 UniProtKB Modified residue 322 322 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P06102 UniProtKB Modified residue 446 446 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06102 UniProtKB Modified residue 450 450 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P06102 UniProtKB Modified residue 565 565 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P06102 UniProtKB Modified residue 569 569 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06102 UniProtKB Modified residue 571 571 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06102 UniProtKB Modified residue 657 657 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P06102 UniProtKB Cross-link 535 535 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P06102 UniProtKB Sequence conflict 106 106 . . . Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06102 UniProtKB Sequence conflict 593 593 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06102 UniProtKB Sequence conflict 725 725 . . . Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06102 UniProtKB Sequence conflict 827 836 . . . Note=KQLKQGKISV->ETIETGKN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39997 1 493 +P39997 UniProtKB Chain 1 493 . . . ID=PRO_0000202612;Note=Ectonucleotide pyrophosphatase/phosphodiesterase 2 +P39997 UniProtKB Topological domain 1 28 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39997 UniProtKB Transmembrane 29 45 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39997 UniProtKB Topological domain 46 493 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39997 UniProtKB Region 76 438 . . . Note=Phosphodiesterase +P39997 UniProtKB Active site 127 127 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39997 UniProtKB Glycosylation 62 62 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39997 UniProtKB Glycosylation 69 69 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39997 UniProtKB Glycosylation 112 112 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39997 UniProtKB Glycosylation 153 153 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39997 UniProtKB Glycosylation 441 441 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39997 UniProtKB Sequence conflict 125 125 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53617 1 575 +P53617 UniProtKB Chain 1 575 . . . ID=PRO_0000081688;Note=Protein NRD1 +P53617 UniProtKB Domain 1 153 . . . Note=CID;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00724 +P53617 UniProtKB Domain 339 409 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P53617 UniProtKB Compositional bias 541 544 . . . Note=Poly-Ala +P53617 UniProtKB Compositional bias 567 574 . . . Note=Poly-Gln +P53617 UniProtKB Modified residue 263 263 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53617 UniProtKB Modified residue 265 265 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53617 UniProtKB Modified residue 271 271 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53617 UniProtKB Helix 3 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LO6 +P53617 UniProtKB Helix 7 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ +P53617 UniProtKB Helix 16 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ +P53617 UniProtKB Beta strand 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ +P53617 UniProtKB Helix 26 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ +P53617 UniProtKB Helix 39 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ +P53617 UniProtKB Helix 43 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ +P53617 UniProtKB Helix 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ +P53617 UniProtKB Helix 62 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ +P53617 UniProtKB Helix 94 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ +P53617 UniProtKB Helix 118 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ +P53617 UniProtKB Turn 135 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ +P53617 UniProtKB Turn 143 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ +P53617 UniProtKB Helix 148 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CLJ +P53617 UniProtKB Beta strand 331 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88 +P53617 UniProtKB Beta strand 340 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88 +P53617 UniProtKB Beta strand 347 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88 +P53617 UniProtKB Helix 352 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88 +P53617 UniProtKB Beta strand 356 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88 +P53617 UniProtKB Beta strand 365 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88 +P53617 UniProtKB Turn 372 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88 +P53617 UniProtKB Beta strand 376 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88 +P53617 UniProtKB Helix 384 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88 +P53617 UniProtKB Beta strand 397 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88 +P53617 UniProtKB Beta strand 401 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88 +P53617 UniProtKB Helix 418 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88 +P53617 UniProtKB Helix 426 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88 +P53617 UniProtKB Helix 429 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88 +P53617 UniProtKB Beta strand 440 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88 +P53617 UniProtKB Beta strand 445 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88 +P53617 UniProtKB Helix 450 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M88 +##sequence-region P40007 1 231 +P40007 UniProtKB Chain 1 231 . . . ID=PRO_0000202619;Note=Nucleolar protein 16 +P40007 UniProtKB Modified residue 176 176 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P40007 UniProtKB Modified residue 178 178 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region P40991 1 618 +P40991 UniProtKB Chain 1 618 . . . ID=PRO_0000211819;Note=25S rRNA (cytosine(2870)-C(5))-methyltransferase +P40991 UniProtKB Region 353 359 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023 +P40991 UniProtKB Active site 478 478 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023 +P40991 UniProtKB Binding site 377 377 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023 +P40991 UniProtKB Binding site 404 404 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023 +P40991 UniProtKB Binding site 421 421 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023 +P40991 UniProtKB Modified residue 580 580 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40991 UniProtKB Mutagenesis 424 424 . . . Note=Cannot complement loss of wild type NOP2. C->A%2CS;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23913415,ECO:0000269|PubMed:9854021;Dbxref=PMID:23913415,PMID:9854021 +P40991 UniProtKB Mutagenesis 478 478 . . . Note=Fails to ctalyze the C-5 methylation of the C2870 residue and strongly affects 60S biogenesis. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23913415,ECO:0000269|PubMed:9854021;Dbxref=PMID:23913415,PMID:9854021 +P40991 UniProtKB Sequence conflict 216 216 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40991 UniProtKB Sequence conflict 577 577 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08287 1 484 +Q08287 UniProtKB Chain 1 484 . . . ID=PRO_0000081678;Note=60S ribosome subunit biogenesis protein NOP8 +Q08287 UniProtKB Domain 7 83 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q08287 UniProtKB Compositional bias 280 290 . . . Note=Poly-Glu +Q08287 UniProtKB Modified residue 234 234 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08287 UniProtKB Modified residue 239 239 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08287 UniProtKB Modified residue 268 268 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q08287 UniProtKB Modified residue 370 370 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P40078 1 261 +P40078 UniProtKB Chain 1 261 . . . ID=PRO_0000202648;Note=Ribosome biogenesis protein NSA2 +P40078 UniProtKB Turn 89 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WJV +##sequence-region P43124 1 402 +P43124 UniProtKB Chain 1 402 . . . ID=PRO_0000214100;Note=Non-structural maintenance of chromosome element 4 +##sequence-region Q04958 1 1679 +Q04958 UniProtKB Chain 1 1679 . . . ID=PRO_0000172528;Note=Lysophospholipase NTE1 +Q04958 UniProtKB Topological domain 1 49 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04958 UniProtKB Transmembrane 50 70 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04958 UniProtKB Topological domain 71 103 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04958 UniProtKB Transmembrane 104 124 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04958 UniProtKB Topological domain 125 1679 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04958 UniProtKB Domain 1373 1537 . . . Note=PNPLA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161 +Q04958 UniProtKB Nucleotide binding 803 947 . . . Note=cNMP 1 +Q04958 UniProtKB Nucleotide binding 943 1074 . . . Note=cNMP 2 +Q04958 UniProtKB Motif 1377 1382 . . . Note=GXGXXG;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161 +Q04958 UniProtKB Motif 1404 1408 . . . Note=GXSXG;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161 +Q04958 UniProtKB Motif 1524 1526 . . . Note=DGA/G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161 +Q04958 UniProtKB Compositional bias 259 297 . . . Note=Asp-rich +Q04958 UniProtKB Compositional bias 713 718 . . . Note=Poly-Ser +Q04958 UniProtKB Active site 1406 1406 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161 +Q04958 UniProtKB Active site 1524 1524 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161 +Q04958 UniProtKB Modified residue 300 300 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04958 UniProtKB Modified residue 312 312 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04958 UniProtKB Modified residue 632 632 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04958 UniProtKB Modified residue 634 634 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q04958 UniProtKB Modified residue 653 653 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04958 UniProtKB Modified residue 661 661 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04958 UniProtKB Modified residue 670 670 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04958 UniProtKB Modified residue 680 680 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04958 UniProtKB Modified residue 739 739 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04958 UniProtKB Modified residue 803 803 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04958 UniProtKB Mutagenesis 1406 1406 . . . Note=Loss of esterase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15044461;Dbxref=PMID:15044461 +##sequence-region P33331 1 125 +P33331 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P33331 UniProtKB Chain 2 125 . . . ID=PRO_0000194792;Note=Nuclear transport factor 2 +P33331 UniProtKB Domain 8 121 . . . Note=NTF2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00137 +P33331 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P33331 UniProtKB Cross-link 53 53 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P33331 UniProtKB Helix 5 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GY7 +P33331 UniProtKB Helix 24 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GY7 +P33331 UniProtKB Beta strand 31 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GY7 +P33331 UniProtKB Beta strand 42 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GY7 +P33331 UniProtKB Helix 47 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GY7 +P33331 UniProtKB Beta strand 62 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GY7 +P33331 UniProtKB Beta strand 80 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GY7 +P33331 UniProtKB Beta strand 97 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GY7 +P33331 UniProtKB Beta strand 111 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1GY7 +##sequence-region P36118 1 322 +P36118 UniProtKB Chain 1 322 . . . ID=PRO_0000203201;Note=Pre-mRNA-splicing factor NTR2 +P36118 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P36118 UniProtKB Modified residue 153 153 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36118 UniProtKB Modified residue 197 197 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P36161 1 1157 +P36161 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P36161 UniProtKB Chain 2 1157 . . . ID=PRO_0000204841;Note=Nucleoporin NUP133 +P36161 UniProtKB Region 44 236 . . . Note=Required for normal NPC distribution +P36161 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P36161 UniProtKB Helix 951 965 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Helix 973 975 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Helix 978 992 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Beta strand 993 995 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Helix 999 1006 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Helix 1012 1025 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Helix 1026 1028 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Helix 1031 1049 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Helix 1056 1067 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Helix 1070 1073 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Helix 1081 1084 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Helix 1087 1089 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Helix 1092 1099 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Beta strand 1102 1104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Helix 1106 1123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Helix 1124 1127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Helix 1128 1141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Beta strand 1144 1149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Turn 1150 1153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +P36161 UniProtKB Beta strand 1154 1157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KFO +##sequence-region P38181 1 1502 +P38181 UniProtKB Chain 1 1502 . . . ID=PRO_0000204854;Note=Nucleoporin NUP170 +P38181 UniProtKB Region 233 261 . . . Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38181 UniProtKB Modified residue 1247 1247 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38181 UniProtKB Helix 1001 1015 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P +P38181 UniProtKB Helix 1022 1032 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P +P38181 UniProtKB Helix 1045 1056 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P +P38181 UniProtKB Helix 1060 1075 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P +P38181 UniProtKB Helix 1079 1086 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P +P38181 UniProtKB Beta strand 1089 1093 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P +P38181 UniProtKB Helix 1095 1114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P +P38181 UniProtKB Helix 1146 1149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P +P38181 UniProtKB Beta strand 1150 1152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P +P38181 UniProtKB Helix 1155 1167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P +P38181 UniProtKB Helix 1171 1176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P +P38181 UniProtKB Helix 1182 1188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P +P38181 UniProtKB Helix 1196 1201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P +P38181 UniProtKB Helix 1203 1206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P +P38181 UniProtKB Helix 1210 1221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P +P38181 UniProtKB Beta strand 1222 1225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P +P38181 UniProtKB Helix 1229 1242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P +P38181 UniProtKB Helix 1262 1264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +P38181 UniProtKB Helix 1265 1281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +P38181 UniProtKB Beta strand 1283 1285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5P +P38181 UniProtKB Helix 1287 1299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +P38181 UniProtKB Helix 1304 1310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +P38181 UniProtKB Turn 1311 1316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +P38181 UniProtKB Helix 1318 1327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +P38181 UniProtKB Helix 1333 1350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +P38181 UniProtKB Helix 1357 1378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +P38181 UniProtKB Turn 1382 1384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +P38181 UniProtKB Helix 1387 1401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +P38181 UniProtKB Helix 1404 1406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +P38181 UniProtKB Turn 1409 1412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +P38181 UniProtKB Helix 1413 1419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +P38181 UniProtKB Helix 1423 1435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +P38181 UniProtKB Helix 1442 1458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +P38181 UniProtKB Helix 1460 1463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +P38181 UniProtKB Helix 1469 1472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +P38181 UniProtKB Turn 1479 1481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +P38181 UniProtKB Helix 1483 1491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I5Q +##sequence-region P47054 1 1683 +P47054 UniProtKB Chain 1 1683 . . . ID=PRO_0000204858;Note=Nucleoporin NUP192 +P47054 UniProtKB Coiled coil 31 58 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47054 UniProtKB Helix 6 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 22 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Turn 34 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 48 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Beta strand 54 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Beta strand 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Beta strand 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 68 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 87 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 102 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 129 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 139 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 173 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Beta strand 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 211 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 228 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 234 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 242 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 249 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 266 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 272 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Turn 293 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 302 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 307 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 318 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 332 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 344 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 358 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 425 445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 447 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Beta strand 463 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 469 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 477 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 493 496 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 498 501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Beta strand 503 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 506 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 520 533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 537 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Beta strand 549 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 555 572 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 603 622 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 625 642 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 650 660 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 665 668 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 669 680 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 689 699 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 703 716 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Turn 738 744 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Beta strand 745 749 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 750 758 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 761 766 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 770 789 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 794 797 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 815 821 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 824 831 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 834 845 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 861 884 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 886 893 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 909 916 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 921 929 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +P47054 UniProtKB Helix 935 949 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFQ +##sequence-region P53742 1 486 +P53742 UniProtKB Chain 1 486 . . . ID=PRO_0000215817;Note=Nucleolar GTP-binding protein 2 +P53742 UniProtKB Domain 212 373 . . . Note=CP-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01058 +P53742 UniProtKB Nucleotide binding 322 329 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53742 UniProtKB Nucleotide binding 366 370 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53742 UniProtKB Modified residue 60 60 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53742 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53742 UniProtKB Modified residue 155 155 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q12200 1 1170 +Q12200 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Chain 20 1170 . . . ID=PRO_0000268685;Note=Niemann-Pick type C-related protein 1 +Q12200 UniProtKB Transmembrane 260 280 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Transmembrane 341 361 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Transmembrane 556 576 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Transmembrane 585 605 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Transmembrane 616 636 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Transmembrane 667 687 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Transmembrane 698 718 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Transmembrane 752 772 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Transmembrane 1000 1020 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Transmembrane 1027 1047 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Transmembrane 1054 1074 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Transmembrane 1099 1119 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Transmembrane 1133 1153 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Domain 557 717 . . . Note=SSD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00199 +Q12200 UniProtKB Glycosylation 123 123 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Glycosylation 145 145 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Glycosylation 178 178 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Glycosylation 314 314 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Glycosylation 401 401 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Glycosylation 513 513 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Glycosylation 900 900 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Glycosylation 940 940 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12200 UniProtKB Mutagenesis 718 718 . . . Note=Sphingolipids mislocalization and no growth at 38 degrees Celsius. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14970192;Dbxref=PMID:14970192 +##sequence-region Q03125 1 231 +Q03125 UniProtKB Chain 1 231 . . . ID=PRO_0000046812;Note=Transcriptional regulator NRG1 +Q03125 UniProtKB Zinc finger 174 196 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q03125 UniProtKB Zinc finger 202 226 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q03125 UniProtKB Modified residue 163 163 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P39081 1 626 +P39081 UniProtKB Chain 1 626 . . . ID=PRO_0000058247;Note=Protein PCF11 +P39081 UniProtKB Domain 4 139 . . . Note=CID;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00724 +P39081 UniProtKB Region 1 130 . . . Note=Interaction with RBP1 CTD (CID) +P39081 UniProtKB Compositional bias 234 253 . . . Note=Poly-Gln +P39081 UniProtKB Compositional bias 470 473 . . . Note=Poly-Thr +P39081 UniProtKB Mutagenesis 66 66 . . . Note=Loss of interaction with RBP1 CTD. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12727883;Dbxref=PMID:12727883 +P39081 UniProtKB Mutagenesis 68 70 . . . Note=Loss of interaction with RBP1 CTD. DSI->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12727883;Dbxref=PMID:12727883 +P39081 UniProtKB Sequence conflict 286 288 . . . Note=NSL->ILS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39081 UniProtKB Sequence conflict 515 515 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39081 UniProtKB Helix 3 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9 +P39081 UniProtKB Helix 24 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9 +P39081 UniProtKB Helix 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9 +P39081 UniProtKB Helix 41 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9 +P39081 UniProtKB Helix 57 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9 +P39081 UniProtKB Helix 78 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9 +P39081 UniProtKB Helix 86 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9 +P39081 UniProtKB Helix 99 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9 +P39081 UniProtKB Helix 115 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9 +P39081 UniProtKB Helix 125 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SZ9 +P39081 UniProtKB Helix 486 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +P39081 UniProtKB Helix 495 498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OI4 +P39081 UniProtKB Helix 543 547 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX +P39081 UniProtKB Beta strand 550 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX +P39081 UniProtKB Beta strand 561 564 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX +P39081 UniProtKB Turn 565 568 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX +P39081 UniProtKB Beta strand 569 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX +P39081 UniProtKB Turn 577 580 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX +P39081 UniProtKB Beta strand 581 585 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX +P39081 UniProtKB Beta strand 587 590 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX +P39081 UniProtKB Beta strand 593 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX +P39081 UniProtKB Helix 597 603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NAX +##sequence-region P51533 1 1564 +P51533 UniProtKB Chain 1 1564 . . . ID=PRO_0000093443;Note=ATP-dependent permease PDR10 +P51533 UniProtKB Topological domain 1 587 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P51533 UniProtKB Transmembrane 588 608 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P51533 UniProtKB Transmembrane 624 644 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P51533 UniProtKB Transmembrane 674 694 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P51533 UniProtKB Transmembrane 699 719 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P51533 UniProtKB Transmembrane 732 752 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P51533 UniProtKB Transmembrane 841 861 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P51533 UniProtKB Topological domain 862 1304 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P51533 UniProtKB Transmembrane 1305 1325 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P51533 UniProtKB Transmembrane 1340 1360 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P51533 UniProtKB Transmembrane 1390 1410 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P51533 UniProtKB Transmembrane 1426 1446 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P51533 UniProtKB Transmembrane 1459 1479 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P51533 UniProtKB Transmembrane 1491 1511 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P51533 UniProtKB Topological domain 1512 1564 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P51533 UniProtKB Domain 174 430 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P51533 UniProtKB Domain 923 1166 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P51533 UniProtKB Nucleotide binding 959 966 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P51533 UniProtKB Compositional bias 73 80 . . . Note=Poly-Ser +P51533 UniProtKB Compositional bias 568 572 . . . Note=Poly-Thr +P51533 UniProtKB Compositional bias 845 848 . . . Note=Poly-Lys +P51533 UniProtKB Glycosylation 754 754 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q02785 1 1511 +Q02785 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q02785 UniProtKB Chain 2 1511 . . . ID=PRO_0000093445;Note=ATP-dependent permease PDR12 +Q02785 UniProtKB Topological domain 2 508 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Transmembrane 509 529 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Topological domain 530 548 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Transmembrane 549 569 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Topological domain 570 597 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Transmembrane 598 618 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Topological domain 619 622 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Transmembrane 623 643 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Topological domain 644 657 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Transmembrane 658 678 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Topological domain 679 765 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Transmembrane 766 786 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Topological domain 787 1182 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Transmembrane 1183 1203 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Topological domain 1204 1204 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Transmembrane 1205 1225 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Topological domain 1226 1254 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Transmembrane 1255 1275 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Topological domain 1276 1291 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Transmembrane 1292 1312 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Topological domain 1313 1318 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Transmembrane 1319 1339 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Topological domain 1340 1444 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Transmembrane 1445 1465 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Topological domain 1466 1511 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Domain 144 397 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q02785 UniProtKB Domain 836 1084 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q02785 UniProtKB Nucleotide binding 878 885 . . . Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q02785 UniProtKB Nucleotide binding 972 979 . . . Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +Q02785 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q02785 UniProtKB Modified residue 32 32 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q02785 UniProtKB Modified residue 52 52 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +Q02785 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +Q02785 UniProtKB Glycosylation 1405 1405 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02785 UniProtKB Cross-link 426 426 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region P38855 1 283 +P38855 UniProtKB Chain 1 283 . . . ID=PRO_0000202929;Note=Peroxisomal membrane protein PEX18 +##sequence-region Q07418 1 342 +Q07418 UniProtKB Chain 1 339 . . . ID=PRO_0000218763;Note=Peroxisomal membrane protein import receptor PEX19 +Q07418 UniProtKB Propeptide 340 342 . . . ID=PRO_0000396705;Note=Removed in mature form;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q07418 UniProtKB Compositional bias 311 314 . . . Note=Poly-Glu +Q07418 UniProtKB Modified residue 62 62 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q07418 UniProtKB Modified residue 304 304 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +Q07418 UniProtKB Modified residue 339 339 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q07418 UniProtKB Lipidation 339 339 . . . Note=S-farnesyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9418908;Dbxref=PMID:9418908 +Q07418 UniProtKB Mutagenesis 339 339 . . . Note=Prevents farnesylation. C->S%2CR;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16791427,ECO:0000269|PubMed:9418908;Dbxref=PMID:16791427,PMID:9418908 +##sequence-region Q06169 1 523 +Q06169 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q06169 UniProtKB Chain 2 523 . . . ID=PRO_0000252270;Note=Peroxisomal membrane protein PEX30 +Q06169 UniProtKB Transmembrane 91 111 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06169 UniProtKB Transmembrane 118 138 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06169 UniProtKB Transmembrane 184 204 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06169 UniProtKB Transmembrane 207 227 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06169 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q06169 UniProtKB Modified residue 52 52 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06169 UniProtKB Modified residue 420 420 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06169 UniProtKB Modified residue 424 424 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06169 UniProtKB Sequence conflict 257 257 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40005 1 111 +P40005 UniProtKB Chain 1 111 . . . ID=PRO_0000124841;Note=Prefoldin subunit 2 +P40005 UniProtKB Coiled coil 1 36 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40005 UniProtKB Coiled coil 72 92 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40005 UniProtKB Sequence conflict 59 59 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08959 1 321 +Q08959 UniProtKB Chain 1 321 . . . ID=PRO_0000234365;Note=Phosphatidylglycerol phospholipase C +Q08959 UniProtKB Transmembrane 297 315 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08959 UniProtKB Domain 2 251 . . . Note=GP-PDE +##sequence-region Q05637 1 104 +Q05637 UniProtKB Chain 1 104 . . . ID=PRO_0000262734;Note=Phosphate metabolism protein 6 +Q05637 UniProtKB Transmembrane 76 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P07269 1 559 +P07269 UniProtKB Chain 1 559 . . . ID=PRO_0000049247;Note=Regulatory protein PHO2 +P07269 UniProtKB DNA binding 77 136 . . . Note=Homeobox;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00108 +P07269 UniProtKB Compositional bias 23 52 . . . Note=Gln-rich (involved in transcriptional activation) +P07269 UniProtKB Modified residue 542 542 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P17442 1 1178 +P17442 UniProtKB Chain 1 1178 . . . ID=PRO_0000067075;Note=Phosphate system positive regulatory protein PHO81 +P17442 UniProtKB Domain 1 169 . . . Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714 +P17442 UniProtKB Repeat 423 452 . . . Note=ANK 1 +P17442 UniProtKB Repeat 458 487 . . . Note=ANK 2 +P17442 UniProtKB Repeat 506 535 . . . Note=ANK 3 +P17442 UniProtKB Repeat 556 586 . . . Note=ANK 4 +P17442 UniProtKB Repeat 591 620 . . . Note=ANK 5 +P17442 UniProtKB Repeat 624 653 . . . Note=ANK 6 +P17442 UniProtKB Domain 871 1178 . . . Note=GP-PDE +P17442 UniProtKB Compositional bias 198 253 . . . Note=Asn/Asp-rich +P17442 UniProtKB Compositional bias 231 248 . . . Note=Poly-Asn +P17442 UniProtKB Modified residue 956 956 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P17442 UniProtKB Sequence conflict 248 248 . . . Note=N->NN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17442 UniProtKB Sequence conflict 728 728 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17442 UniProtKB Sequence conflict 762 762 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17442 UniProtKB Sequence conflict 845 845 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17442 UniProtKB Sequence conflict 873 873 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17442 UniProtKB Sequence conflict 920 920 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17442 UniProtKB Sequence conflict 984 984 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25360 1 923 +P25360 UniProtKB Chain 1 923 . . . ID=PRO_0000172517;Note=Inorganic phosphate transporter PHO87 +P25360 UniProtKB Topological domain 1 461 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Transmembrane 462 482 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Topological domain 483 493 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Transmembrane 494 514 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Topological domain 515 537 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Transmembrane 538 558 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Topological domain 559 583 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Transmembrane 584 604 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Topological domain 605 627 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Transmembrane 628 648 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Topological domain 649 667 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Transmembrane 668 688 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Topological domain 689 707 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Transmembrane 708 728 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Topological domain 729 735 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Transmembrane 736 756 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Topological domain 757 767 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Transmembrane 768 788 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Topological domain 789 802 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Transmembrane 803 823 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Topological domain 824 849 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Transmembrane 850 870 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Topological domain 871 898 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Transmembrane 899 919 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Topological domain 920 923 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Domain 1 334 . . . Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714 +P25360 UniProtKB Glycosylation 162 162 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Glycosylation 202 202 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Glycosylation 274 274 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25360 UniProtKB Cross-link 102 102 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25360 UniProtKB Sequence conflict 72 72 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06216 1 648 +Q06216 UniProtKB Chain 1 648 . . . ID=PRO_0000071519;Note=Serine/threonine-protein phosphatase 1 regulatory subunit PIG1 +Q06216 UniProtKB Domain 201 331 . . . Note=CBM21;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00491 +Q06216 UniProtKB Compositional bias 41 51 . . . Note=Poly-Ser +Q06216 UniProtKB Sequence conflict 228 228 . . . Note=I->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38768 1 344 +P38768 UniProtKB Chain 1 344 . . . ID=PRO_0000058440;Note=Protein interacting with Hsp90 1 +P38768 UniProtKB Beta strand 29 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH +P38768 UniProtKB Beta strand 35 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH +P38768 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH +P38768 UniProtKB Beta strand 58 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH +P38768 UniProtKB Helix 78 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH +P38768 UniProtKB Beta strand 100 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH +P38768 UniProtKB Beta strand 109 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH +P38768 UniProtKB Helix 119 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH +P38768 UniProtKB Helix 129 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH +P38768 UniProtKB Beta strand 149 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH +P38768 UniProtKB Beta strand 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH +P38768 UniProtKB Beta strand 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH +P38768 UniProtKB Beta strand 164 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH +P38768 UniProtKB Beta strand 171 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH +P38768 UniProtKB Helix 175 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH +P38768 UniProtKB Helix 180 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CHH +P38768 UniProtKB Beta strand 262 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MNJ +P38768 UniProtKB Beta strand 267 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU +P38768 UniProtKB Beta strand 275 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU +P38768 UniProtKB Beta strand 280 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU +P38768 UniProtKB Beta strand 289 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MNJ +P38768 UniProtKB Beta strand 300 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU +P38768 UniProtKB Turn 303 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU +P38768 UniProtKB Beta strand 307 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU +P38768 UniProtKB Beta strand 311 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU +P38768 UniProtKB Beta strand 315 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU +P38768 UniProtKB Turn 326 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU +P38768 UniProtKB Beta strand 330 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU +P38768 UniProtKB Turn 335 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU +P38768 UniProtKB Beta strand 339 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU +##sequence-region Q12057 1 282 +Q12057 UniProtKB Chain 1 282 . . . ID=PRO_0000058442;Note=[PSI+] induction protein 2 +Q12057 UniProtKB Transmembrane 43 63 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12057 UniProtKB Modified residue 141 141 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12057 UniProtKB Glycosylation 91 91 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12057 UniProtKB Glycosylation 132 132 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12057 UniProtKB Glycosylation 276 276 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P46999 1 287 +P46999 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46999 UniProtKB Propeptide 22 62 . . . ID=PRO_0000377623;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46999 UniProtKB Chain 63 287 . . . ID=PRO_0000014333;Note=Cell wall protein PIR5 +P46999 UniProtKB Repeat 62 80 . . . Note=PIR1/2/3 1 +P46999 UniProtKB Repeat 81 99 . . . Note=PIR1/2/3 2 +P46999 UniProtKB Repeat 104 122 . . . Note=PIR1/2/3 3 +P46999 UniProtKB Repeat 144 162 . . . Note=PIR1/2/3 4 +P46999 UniProtKB Site 62 63 . . . Note=Cleavage%3B by KEX2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46999 UniProtKB Site 72 72 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46999 UniProtKB Site 91 91 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46999 UniProtKB Site 114 114 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46999 UniProtKB Site 154 154 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q03407 1 766 +Q03407 UniProtKB Chain 1 766 . . . ID=PRO_0000086552;Note=Serine/threonine-protein kinase PKH1 +Q03407 UniProtKB Domain 125 391 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03407 UniProtKB Nucleotide binding 135 137 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530 +Q03407 UniProtKB Nucleotide binding 204 206 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530 +Q03407 UniProtKB Region 156 201 . . . Note=PIF-pocket;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530 +Q03407 UniProtKB Active site 249 249 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q03407 UniProtKB Binding site 154 154 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530 +Q03407 UniProtKB Binding site 210 210 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530 +Q03407 UniProtKB Binding site 253 253 . . . Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530 +Q03407 UniProtKB Binding site 267 267 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530 +Q03407 UniProtKB Modified residue 294 294 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03407 UniProtKB Modified residue 296 296 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198 +##sequence-region P39105 1 664 +P39105 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Chain 23 634 . . . ID=PRO_0000024646;Note=Lysophospholipase 1 +P39105 UniProtKB Propeptide 635 664 . . . ID=PRO_0000372442;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Domain 35 586 . . . Note=PLA2c;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00555 +P39105 UniProtKB Compositional bias 587 629 . . . Note=Ala/Ser-rich +P39105 UniProtKB Lipidation 634 634 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 26 26 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 33 33 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 52 52 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 78 78 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 92 92 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 123 123 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 160 160 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 170 170 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 215 215 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 277 277 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 307 307 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 345 345 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 388 388 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 459 459 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 489 489 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 513 513 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 541 541 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 565 565 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Glycosylation 582 582 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39105 UniProtKB Sequence conflict 32 32 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39105 UniProtKB Sequence conflict 93 93 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39105 UniProtKB Sequence conflict 494 494 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03674 1 706 +Q03674 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Chain 20 680 . . . ID=PRO_0000024647;Note=Lysophospholipase 2 +Q03674 UniProtKB Propeptide 681 706 . . . ID=PRO_0000372443;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Domain 36 588 . . . Note=PLA2c;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00555 +Q03674 UniProtKB Compositional bias 369 372 . . . Note=Poly-Asp +Q03674 UniProtKB Compositional bias 657 667 . . . Note=Poly-Ser +Q03674 UniProtKB Compositional bias 671 674 . . . Note=Poly-Ser +Q03674 UniProtKB Lipidation 680 680 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 47 47 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 80 80 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 94 94 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 125 125 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 162 162 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 181 181 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 193 193 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 217 217 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 279 279 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 309 309 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 365 365 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 390 390 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 491 491 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 515 515 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 524 524 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 543 543 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 567 567 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 584 584 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 598 598 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 630 630 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 634 634 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 642 642 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 648 648 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 652 652 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03674 UniProtKB Glycosylation 658 658 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32383 1 869 +P32383 UniProtKB Chain 1 869 . . . ID=PRO_0000088514;Note=1-phosphatidylinositol 4%2C5-bisphosphate phosphodiesterase 1 +P32383 UniProtKB Domain 269 304 . . . Note=EF-hand;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P32383 UniProtKB Domain 382 520 . . . Note=PI-PLC X-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00270 +P32383 UniProtKB Domain 590 709 . . . Note=PI-PLC Y-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00271 +P32383 UniProtKB Domain 734 846 . . . Note=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 +P32383 UniProtKB Calcium binding 282 293 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P32383 UniProtKB Active site 395 395 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00270 +P32383 UniProtKB Active site 439 439 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00270 +P32383 UniProtKB Binding site 518 518 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32383 UniProtKB Binding site 520 520 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32383 UniProtKB Binding site 614 614 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32383 UniProtKB Binding site 643 643 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32383 UniProtKB Sequence conflict 159 159 . . . Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32383 UniProtKB Sequence conflict 181 181 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32383 UniProtKB Sequence conflict 581 581 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12511 1 572 +Q12511 UniProtKB Domain 153 543 . . . Note=PPM-type phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01082 +Q12511 UniProtKB Metal binding 197 197 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12511 UniProtKB Metal binding 197 197 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12511 UniProtKB Metal binding 198 198 . . . Note=Manganese 1%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12511 UniProtKB Metal binding 424 424 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12511 UniProtKB Metal binding 480 480 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P25646 1 442 +P25646 UniProtKB Transit peptide 1 34 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25646 UniProtKB Chain 35 442 . . . ID=PRO_0000057788;Note=[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2%2C mitochondrial +P25646 UniProtKB Domain 35 411 . . . Note=PPM-type phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01082 +##sequence-region P53844 1 350 +P53844 UniProtKB Chain 1 350 . . . ID=PRO_0000210746;Note=Phosphatidylinositol transfer protein PDR17 +P53844 UniProtKB Domain 139 297 . . . Note=CRAL-TRIO;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00056 +##sequence-region P27801 1 918 +P27801 UniProtKB Chain 1 918 . . . ID=PRO_0000055993;Note=Vacuolar membrane protein PEP3 +P27801 UniProtKB Repeat 585 741 . . . Note=CHCR +P27801 UniProtKB Zinc finger 826 851 . . . Note=RING-type%3B atypical +P27801 UniProtKB Modified residue 907 907 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P27801 UniProtKB Beta strand 3 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Turn 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 22 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 29 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 35 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 49 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 63 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 75 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 84 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 91 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 103 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 123 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 134 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 149 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 158 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 166 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 184 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 199 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 206 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Turn 237 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 242 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Helix 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 260 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 267 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 277 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Turn 283 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 288 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 310 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Turn 317 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 321 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Beta strand 330 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +P27801 UniProtKB Helix 338 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UUY +##sequence-region P40335 1 379 +P40335 UniProtKB Chain 1 379 . . . ID=PRO_0000073015;Note=Carboxypeptidase Y-deficient protein 8 +P40335 UniProtKB Modified residue 216 216 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40335 UniProtKB Sequence conflict 189 189 . . . Note=A->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40335 UniProtKB Sequence conflict 286 286 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q99373 1 253 +Q99373 UniProtKB Transit peptide 1 36 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99373 UniProtKB Chain 37 253 . . . ID=PRO_0000240390;Note=Protein PET20%2C mitochondrial +##sequence-region Q04370 1 399 +Q04370 UniProtKB Chain 1 399 . . . ID=PRO_0000218617;Note=Peroxisome assembly protein 12 +Q04370 UniProtKB Transmembrane 270 286 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04370 UniProtKB Zinc finger 334 373 . . . Note=RING-type%3B degenerate +Q04370 UniProtKB Sequence conflict 37 37 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08215 1 383 +Q08215 UniProtKB Chain 1 383 . . . ID=PRO_0000270567;Note=Peroxisomal membrane protein PEX15 +Q08215 UniProtKB Topological domain 1 331 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08215 UniProtKB Transmembrane 332 349 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08215 UniProtKB Topological domain 350 383 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08215 UniProtKB Mutagenesis 22 22 . . . Note=No interaction with PEX6. L->F%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12808025;Dbxref=PMID:12808025 +Q08215 UniProtKB Mutagenesis 47 47 . . . Note=No interaction with PEX6. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12808025;Dbxref=PMID:12808025 +Q08215 UniProtKB Mutagenesis 50 50 . . . Note=No interaction with PEX6. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12808025;Dbxref=PMID:12808025 +##sequence-region P53203 1 462 +P53203 UniProtKB Chain 1 462 . . . ID=PRO_0000202779;Note=Peroxisomal membrane protein PEX31 +P53203 UniProtKB Topological domain 1 90 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53203 UniProtKB Transmembrane 91 111 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53203 UniProtKB Topological domain 112 175 . . . Note=Peroxisomal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53203 UniProtKB Transmembrane 176 196 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53203 UniProtKB Topological domain 197 462 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53203 UniProtKB Modified residue 432 432 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198 +P53203 UniProtKB Modified residue 435 435 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P33760 1 1030 +P33760 UniProtKB Chain 1 1030 . . . ID=PRO_0000084621;Note=Peroxisomal ATPase PEX6 +P33760 UniProtKB Nucleotide binding 772 779 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33760 UniProtKB Region 478 683 . . . Note=AAA-cassette D1 +P33760 UniProtKB Region 767 956 . . . Note=AAA-cassette D2 +P33760 UniProtKB Mutagenesis 489 489 . . . Note=In PEX6pA1%3B decreased binding to PEX15. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12808025,ECO:0000269|PubMed:15634331,ECO:0000269|PubMed:16007078;Dbxref=PMID:12808025,PMID:15634331,PMID:16007078 +P33760 UniProtKB Mutagenesis 778 778 . . . Note=In PEX6pA2%3B increased amount of peroxisome-bound PEX6. Results in accumulation of PEX5 on peroxisomal membranes. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12808025,ECO:0000269|PubMed:15634331,ECO:0000269|PubMed:16007078;Dbxref=PMID:12808025,PMID:15634331,PMID:16007078 +P33760 UniProtKB Mutagenesis 831 831 . . . Note=In PEX6pB2%3B increased amount of peroxisome-bound PEX6. Results in accumulation of PEX5 on peroxisomal membranes. D->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12808025,ECO:0000269|PubMed:15634331,ECO:0000269|PubMed:16007078;Dbxref=PMID:12808025,PMID:15634331,PMID:16007078 +##sequence-region P42836 1 336 +P42836 UniProtKB Chain 1 336 . . . ID=PRO_0000212959;Note=Palmitoyltransferase PFA3 +P42836 UniProtKB Topological domain 1 6 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42836 UniProtKB Transmembrane 7 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42836 UniProtKB Topological domain 30 37 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42836 UniProtKB Transmembrane 38 58 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42836 UniProtKB Topological domain 59 147 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42836 UniProtKB Transmembrane 148 168 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42836 UniProtKB Topological domain 169 188 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42836 UniProtKB Transmembrane 189 209 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42836 UniProtKB Topological domain 210 336 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42836 UniProtKB Domain 104 154 . . . Note=DHHC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00067 +P42836 UniProtKB Mutagenesis 134 134 . . . Note=Abolishes autopalmitoylation and VAC8 palmitoylation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16186255;Dbxref=PMID:16186255 +##sequence-region Q12006 1 378 +Q12006 UniProtKB Chain 1 378 . . . ID=PRO_0000212972;Note=Palmitoyltransferase PFA4 +Q12006 UniProtKB Topological domain 1 9 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03199,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q12006 UniProtKB Transmembrane 10 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03199 +Q12006 UniProtKB Topological domain 31 40 . . . Note=Lumenal;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03199,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q12006 UniProtKB Transmembrane 41 61 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03199 +Q12006 UniProtKB Topological domain 62 119 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03199,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q12006 UniProtKB Transmembrane 120 140 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03199 +Q12006 UniProtKB Topological domain 141 164 . . . Note=Lumenal;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03199,ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q12006 UniProtKB Transmembrane 165 185 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03199 +Q12006 UniProtKB Topological domain 186 378 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03199,ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +Q12006 UniProtKB Domain 78 128 . . . Note=DHHC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00067 +Q12006 UniProtKB Active site 108 108 . . . Note=S-palmitoyl cysteine intermediate;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03199,ECO:0000305|PubMed:26224664;Dbxref=PMID:26224664 +Q12006 UniProtKB Mutagenesis 108 108 . . . Note=Causes mislocalization of chitin synthase CHS3 (PubMed:16818716). Reduces%2C but does not abolish catalytic activity. Lacks autopalmitoylation (PubMed:26224664). C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16818716,ECO:0000269|PubMed:26224664;Dbxref=PMID:16818716,PMID:26224664 +Q12006 UniProtKB Mutagenesis 108 108 . . . Note=Reduces%2C but does not abolish catalytic activity. Lacks autopalmitoylation. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26224664;Dbxref=PMID:26224664 +##sequence-region Q03289 1 374 +Q03289 UniProtKB Chain 1 374 . . . ID=PRO_0000212983;Note=Palmitoyltransferase PFA5 +Q03289 UniProtKB Topological domain 1 13 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03289 UniProtKB Transmembrane 14 34 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03289 UniProtKB Topological domain 35 55 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03289 UniProtKB Transmembrane 56 76 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03289 UniProtKB Topological domain 77 173 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03289 UniProtKB Transmembrane 174 194 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03289 UniProtKB Topological domain 195 217 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03289 UniProtKB Transmembrane 218 238 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03289 UniProtKB Topological domain 239 374 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03289 UniProtKB Domain 129 179 . . . Note=DHHC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00067 +##sequence-region P46988 1 109 +P46988 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P46988 UniProtKB Chain 2 109 . . . ID=PRO_0000124834;Note=Prefoldin subunit 1 +P46988 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P46988 UniProtKB Sequence conflict 74 74 . . . Note=D->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P52553 1 114 +P52553 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P52553 UniProtKB Chain 2 114 . . . ID=PRO_0000124855;Note=Prefoldin subunit 6 +P52553 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P32452 1 334 +P32452 UniProtKB Chain 1 334 . . . ID=PRO_0000119206;Note=Putative prephenate dehydratase +P32452 UniProtKB Domain 7 224 . . . Note=Prephenate dehydratase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00517 +P32452 UniProtKB Domain 244 322 . . . Note=ACT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01007 +##sequence-region P07270 1 312 +P07270 UniProtKB Chain 1 312 . . . ID=PRO_0000127422;Note=Phosphate system positive regulatory protein PHO4 +P07270 UniProtKB Domain 250 306 . . . Note=bHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981 +P07270 UniProtKB Region 1 31 . . . Note=Interaction with PHO80 +P07270 UniProtKB Region 75 99 . . . Note=Transcription activation domain +P07270 UniProtKB Region 156 200 . . . Note=Interaction with PHO80 +P07270 UniProtKB Region 201 218 . . . Note=Interaction with PHO2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7957107;Dbxref=PMID:7957107 +P07270 UniProtKB Region 203 227 . . . Note=Involved in oligomerization +P07270 UniProtKB Motif 75 83 . . . Note=9aaTAD +P07270 UniProtKB Motif 140 166 . . . Note=Nuclear localization signal +P07270 UniProtKB Modified residue 100 100 . . . Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10320381,ECO:0000269|PubMed:8539622;Dbxref=PMID:10320381,PMID:8539622 +P07270 UniProtKB Modified residue 114 114 . . . Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10320381,ECO:0000269|PubMed:8539622;Dbxref=PMID:10320381,PMID:8539622 +P07270 UniProtKB Modified residue 128 128 . . . Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10320381,ECO:0000269|PubMed:8539622;Dbxref=PMID:10320381,PMID:8539622 +P07270 UniProtKB Modified residue 152 152 . . . Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10320381,ECO:0000269|PubMed:8539622;Dbxref=PMID:10320381,PMID:8539622 +P07270 UniProtKB Modified residue 204 204 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P07270 UniProtKB Modified residue 223 223 . . . Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:10320381,ECO:0000269|PubMed:8539622;Dbxref=PMID:17330950,PMID:19779198,PMID:10320381,PMID:8539622 +P07270 UniProtKB Modified residue 242 242 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P07270 UniProtKB Modified residue 243 243 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P07270 UniProtKB Sequence conflict 269 269 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07270 UniProtKB Sequence conflict 269 269 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07270 UniProtKB Sequence conflict 310 310 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07270 UniProtKB Helix 254 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A0A +P07270 UniProtKB Helix 260 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A0A +P07270 UniProtKB Helix 279 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A0A +P07270 UniProtKB Helix 294 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1A0A +##sequence-region P20052 1 293 +P20052 UniProtKB Chain 1 293 . . . ID=PRO_0000080502;Note=PHO85 cyclin PHO80 +P20052 UniProtKB Modified residue 234 234 . . . Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15057567;Dbxref=PMID:15057567 +P20052 UniProtKB Modified residue 267 267 . . . Note=Phosphoserine%3B by PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15057567;Dbxref=PMID:15057567 +P20052 UniProtKB Mutagenesis 163 163 . . . Note=Temperature-sensitive allele. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3283704;Dbxref=PMID:3283704 +P20052 UniProtKB Mutagenesis 229 229 . . . Note=In PHO80-1. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2269431;Dbxref=PMID:2269431 +P20052 UniProtKB Sequence conflict 65 65 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20052 UniProtKB Sequence conflict 247 247 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20052 UniProtKB Sequence conflict 247 247 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20052 UniProtKB Sequence conflict 254 254 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20052 UniProtKB Sequence conflict 254 254 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20052 UniProtKB Sequence conflict 292 292 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20052 UniProtKB Sequence conflict 292 292 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20052 UniProtKB Beta strand 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PK9 +P20052 UniProtKB Helix 27 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI +P20052 UniProtKB Helix 32 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI +P20052 UniProtKB Helix 77 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI +P20052 UniProtKB Turn 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI +P20052 UniProtKB Helix 92 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI +P20052 UniProtKB Turn 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PK9 +P20052 UniProtKB Helix 119 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI +P20052 UniProtKB Helix 141 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI +P20052 UniProtKB Helix 152 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI +P20052 UniProtKB Turn 165 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI +P20052 UniProtKB Helix 176 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI +P20052 UniProtKB Helix 210 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI +P20052 UniProtKB Helix 216 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI +P20052 UniProtKB Helix 235 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI +P20052 UniProtKB Beta strand 242 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PK9 +##sequence-region P38361 1 574 +P38361 UniProtKB Chain 1 574 . . . ID=PRO_0000080781;Note=Phosphate permease PHO89 +P38361 UniProtKB Transmembrane 6 26 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38361 UniProtKB Transmembrane 44 64 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38361 UniProtKB Transmembrane 85 105 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38361 UniProtKB Transmembrane 118 138 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38361 UniProtKB Transmembrane 146 166 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38361 UniProtKB Transmembrane 185 205 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38361 UniProtKB Transmembrane 223 243 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38361 UniProtKB Transmembrane 355 375 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38361 UniProtKB Transmembrane 399 419 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38361 UniProtKB Transmembrane 448 468 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38361 UniProtKB Transmembrane 504 524 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38361 UniProtKB Transmembrane 542 562 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P06738 1 902 +P06738 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1613787;Dbxref=PMID:1613787 +P06738 UniProtKB Chain 2 902 . . . ID=PRO_0000188545;Note=Glycogen phosphorylase +P06738 UniProtKB Modified residue 31 31 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:1092346,ECO:0000269|PubMed:1613787;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198,PMID:1092346,PMID:1613787 +P06738 UniProtKB Modified residue 333 333 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P06738 UniProtKB Modified residue 751 751 . . . Note=N6-(pyridoxal phosphate)lysine +P06738 UniProtKB Sequence conflict 167 168 . . . Note=DL->EG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06738 UniProtKB Sequence conflict 167 168 . . . Note=DL->EG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06738 UniProtKB Sequence conflict 326 326 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06738 UniProtKB Sequence conflict 326 326 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06738 UniProtKB Sequence conflict 440 441 . . . Note=VG->RR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06738 UniProtKB Sequence conflict 440 441 . . . Note=VG->RR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06738 UniProtKB Sequence conflict 508 508 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06738 UniProtKB Sequence conflict 508 508 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06738 UniProtKB Sequence conflict 524 524 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06738 UniProtKB Sequence conflict 524 524 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06738 UniProtKB Sequence conflict 578 578 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06738 UniProtKB Sequence conflict 578 578 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06738 UniProtKB Sequence conflict 876 876 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06738 UniProtKB Sequence conflict 876 876 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06738 UniProtKB Helix 35 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 47 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 64 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 88 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 121 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 134 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 158 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 172 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 188 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 207 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 220 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 227 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Turn 235 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 244 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 258 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 273 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 277 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 297 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 313 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 321 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 326 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 337 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 345 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 377 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 380 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 384 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Turn 392 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 395 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 412 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 423 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 432 434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 437 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 440 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 448 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 474 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 481 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 486 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 490 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 493 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 501 508 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 509 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Turn 518 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 521 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 529 531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 532 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 541 544 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Turn 545 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 550 559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 566 568 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 571 582 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 585 607 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Turn 608 611 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 620 622 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 624 630 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 634 636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 638 657 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 662 668 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 672 677 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 685 701 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 705 707 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 710 716 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 721 727 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 728 730 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 732 736 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 747 753 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Turn 754 756 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 758 763 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 766 774 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 776 778 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Beta strand 779 783 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 786 798 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 805 813 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Turn 824 827 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 828 836 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Turn 838 841 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 843 863 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 865 879 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 880 882 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +P06738 UniProtKB Helix 884 894 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YGP +##sequence-region P40187 1 538 +P40187 UniProtKB Chain 1 538 . . . ID=PRO_0000071522;Note=GSY2-interacting protein PIG2 +P40187 UniProtKB Domain 384 508 . . . Note=CBM21;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00491 +P40187 UniProtKB Modified residue 162 162 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950 +P40187 UniProtKB Modified residue 196 196 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P40187 UniProtKB Modified residue 296 296 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40187 UniProtKB Modified residue 304 304 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40187 UniProtKB Sequence conflict 537 537 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06149 1 701 +Q06149 UniProtKB Chain 1 701 . . . ID=PRO_0000114963;Note=Transcription factor PDR8 +Q06149 UniProtKB DNA binding 31 59 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +Q06149 UniProtKB Compositional bias 272 278 . . . Note=Poly-Ser +##sequence-region Q06608 1 200 +Q06608 UniProtKB Chain 1 200 . . . ID=PRO_0000257818;Note=Pyridoxamine 5'-phosphate oxidase homolog +Q06608 UniProtKB Binding site 60 60 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06608 UniProtKB Binding site 68 68 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06608 UniProtKB Binding site 125 125 . . . Note=FMN;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P12868 1 1029 +P12868 UniProtKB Chain 1 1029 . . . ID=PRO_0000055995;Note=E3 ubiquitin-protein ligase PEP5 +P12868 UniProtKB Repeat 406 583 . . . Note=CHCR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01006 +P12868 UniProtKB Zinc finger 928 973 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +P12868 UniProtKB Sequence conflict 37 37 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12868 UniProtKB Sequence conflict 619 625 . . . Note=VFYSYKT->MFFTVTKH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12868 UniProtKB Sequence conflict 769 770 . . . Note=TK->KQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39684 1 611 +P39684 UniProtKB Chain 1 611 . . . ID=PRO_0000081724;Note=Protein PES4 +P39684 UniProtKB Domain 91 169 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P39684 UniProtKB Domain 179 247 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P39684 UniProtKB Domain 303 379 . . . Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P39684 UniProtKB Domain 393 471 . . . Note=RRM 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P39684 UniProtKB Compositional bias 54 64 . . . Note=Poly-Ser +P39684 UniProtKB Sequence conflict 124 124 . . . Note=L->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39684 UniProtKB Sequence conflict 541 611 . . . Note=QVRRGIDFMRFPSATRDENVHGIAEYIFDTYWNRDVLILDKFLSLLNSSPYHEGVLQKQIEEAASSLGFKR->ASKKRYRFHEISKCH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12252 1 991 +Q12252 UniProtKB Chain 1 991 . . . ID=PRO_0000262735;Note=Phosphate metabolism protein 7 +Q12252 UniProtKB Topological domain 1 9 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Transmembrane 10 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Topological domain 31 91 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Transmembrane 92 112 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Topological domain 113 138 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Transmembrane 139 159 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Topological domain 160 388 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Transmembrane 389 409 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Topological domain 410 437 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Transmembrane 438 458 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Topological domain 459 471 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Transmembrane 472 492 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Topological domain 493 523 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Transmembrane 524 544 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Topological domain 545 582 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Transmembrane 583 603 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Topological domain 604 604 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Transmembrane 605 625 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Topological domain 626 637 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Transmembrane 638 658 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Topological domain 659 661 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Transmembrane 662 682 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Topological domain 683 991 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Glycosylation 115 115 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12252 UniProtKB Glycosylation 132 132 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53297 1 722 +P53297 UniProtKB Chain 1 722 . . . ID=PRO_0000058244;Note=PAB1-binding protein 1 +P53297 UniProtKB Modified residue 106 106 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53297 UniProtKB Modified residue 193 193 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53297 UniProtKB Modified residue 215 215 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53297 UniProtKB Modified residue 436 436 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P53297 UniProtKB Cross-link 344 344 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P38151 1 413 +P38151 UniProtKB Chain 1 413 . . . ID=PRO_0000050122;Note=PAB1-binding protein 2 +P38151 UniProtKB Domain 66 130 . . . Note=KH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117 +P38151 UniProtKB Domain 148 213 . . . Note=KH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117 +P38151 UniProtKB Domain 330 394 . . . Note=KH 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117 +##sequence-region P06169 1 563 +P06169 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10545125,ECO:0000269|PubMed:9298649;Dbxref=PMID:10545125,PMID:9298649 +P06169 UniProtKB Chain 2 563 . . . ID=PRO_0000090770;Note=Pyruvate decarboxylase isozyme 1 +P06169 UniProtKB Region 390 476 . . . Note=Thiamine pyrophosphate binding +P06169 UniProtKB Metal binding 444 444 . . . Note=Magnesium +P06169 UniProtKB Metal binding 471 471 . . . Note=Magnesium +P06169 UniProtKB Metal binding 473 473 . . . Note=Magnesium%3B via carbonyl oxygen +P06169 UniProtKB Binding site 28 28 . . . Note=Substrate +P06169 UniProtKB Binding site 115 115 . . . Note=Substrate +P06169 UniProtKB Binding site 157 157 . . . Note=Substrate%3B allosteric site +P06169 UniProtKB Binding site 477 477 . . . Note=Substrate +P06169 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10545125,ECO:0000269|PubMed:9298649;Dbxref=PMID:10545125,PMID:9298649 +P06169 UniProtKB Modified residue 223 223 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P06169 UniProtKB Modified residue 266 266 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P06169 UniProtKB Modified residue 336 336 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06169 UniProtKB Modified residue 353 353 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P06169 UniProtKB Modified residue 522 522 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06169 UniProtKB Modified residue 526 526 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P06169 UniProtKB Cross-link 212 212 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P06169 UniProtKB Cross-link 233 233 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P06169 UniProtKB Cross-link 269 269 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P06169 UniProtKB Cross-link 332 332 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P06169 UniProtKB Cross-link 484 484 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P06169 UniProtKB Cross-link 505 505 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P06169 UniProtKB Cross-link 520 520 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P06169 UniProtKB Mutagenesis 291 291 . . . Note=In PDC1-8%3B reduces catalytic activity to 10%25 but retains autoregulatory activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7050079;Dbxref=PMID:7050079 +P06169 UniProtKB Sequence conflict 55 55 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 106 106 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 106 106 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 106 106 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 106 106 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 115 115 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 143 143 . . . Note=A->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 143 143 . . . Note=A->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 143 143 . . . Note=A->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 145 146 . . . Note=AP->PQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 206 206 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 208 208 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 253 253 . . . Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 253 253 . . . Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 253 253 . . . Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 253 253 . . . Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 336 336 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 336 336 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 336 336 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 336 336 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 538 538 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 538 538 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 538 538 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 538 538 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Sequence conflict 545 563 . . . Note=APQNLVEQAKLTAATNAKQ->CSTKLG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06169 UniProtKB Beta strand 3 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 6 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 21 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 28 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 31 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 36 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 51 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 68 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 76 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 95 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 104 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QPB +P06169 UniProtKB Beta strand 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QPB +P06169 UniProtKB Beta strand 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 124 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 134 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Turn 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 145 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 163 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 171 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 174 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 178 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 194 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 212 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 220 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 228 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 242 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Turn 246 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 259 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 265 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 270 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 280 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Turn 291 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 306 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 311 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 319 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 326 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Turn 341 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 367 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Turn 375 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 383 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 390 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 395 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 405 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Turn 410 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 417 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 438 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 444 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 451 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 454 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 465 473 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 475 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 486 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 495 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 498 501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 505 512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 515 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Turn 525 528 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Beta strand 531 539 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +P06169 UniProtKB Helix 547 561 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VK8 +##sequence-region P38848 1 579 +P38848 UniProtKB Chain 1 579 . . . ID=PRO_0000202925;Note=Peroxisomal membrane protein PEX28 +P38848 UniProtKB Topological domain 1 243 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38848 UniProtKB Transmembrane 244 264 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38848 UniProtKB Topological domain 265 392 . . . Note=Peroxisomal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38848 UniProtKB Transmembrane 393 413 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38848 UniProtKB Topological domain 414 579 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38848 UniProtKB Compositional bias 2 114 . . . Note=Ser-rich +P38848 UniProtKB Glycosylation 361 361 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32800 1 271 +P32800 UniProtKB Chain 1 271 . . . ID=PRO_0000030724;Note=Peroxisomal biogenesis factor 2 +P32800 UniProtKB Zinc finger 222 259 . . . Note=RING-type +P32800 UniProtKB Alternative sequence 1 46 . . . ID=VSP_018874;Note=In isoform Short. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38292 1 413 +P38292 UniProtKB Chain 1 413 . . . ID=PRO_0000202502;Note=Peroxisomal membrane protein PEX32 +P38292 UniProtKB Topological domain 1 66 . . . Note=Peroxisomal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38292 UniProtKB Transmembrane 67 87 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38292 UniProtKB Topological domain 88 103 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38292 UniProtKB Transmembrane 104 124 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38292 UniProtKB Topological domain 125 181 . . . Note=Peroxisomal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38292 UniProtKB Transmembrane 182 202 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38292 UniProtKB Topological domain 203 413 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38292 UniProtKB Sequence conflict 165 165 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P28795 1 441 +P28795 UniProtKB Chain 1 441 . . . ID=PRO_0000208747;Note=Peroxisomal biogenesis factor 3 +P28795 UniProtKB Topological domain 1 17 . . . Note=Peroxisomal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28795 UniProtKB Transmembrane 18 39 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28795 UniProtKB Topological domain 40 441 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P35056 1 612 +P35056 UniProtKB Chain 1 612 . . . ID=PRO_0000106316;Note=Peroxisomal targeting signal receptor +P35056 UniProtKB Repeat 64 97 . . . Note=TPR 1 +P35056 UniProtKB Repeat 313 346 . . . Note=TPR 2 +P35056 UniProtKB Repeat 347 380 . . . Note=TPR 3 +P35056 UniProtKB Repeat 381 418 . . . Note=TPR 4 +P35056 UniProtKB Repeat 419 456 . . . Note=TPR 5 +P35056 UniProtKB Repeat 457 490 . . . Note=TPR 6 +P35056 UniProtKB Repeat 491 524 . . . Note=TPR 7 +P35056 UniProtKB Repeat 525 558 . . . Note=TPR 8 +P35056 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17550898;Dbxref=PMID:17550898 +P35056 UniProtKB Modified residue 61 61 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P35056 UniProtKB Cross-link 6 6 . . . Note=Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17550898;Dbxref=PMID:17550898 +P35056 UniProtKB Cross-link 18 18 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17550898;Dbxref=PMID:17550898 +P35056 UniProtKB Cross-link 24 24 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17550898;Dbxref=PMID:17550898 +P35056 UniProtKB Mutagenesis 6 6 . . . Note=Loss of UBE2D2-independent ubiquitination. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17550898;Dbxref=PMID:17550898 +P35056 UniProtKB Mutagenesis 18 18 . . . Note=Loss of UBE2D2-dependent ubiquitination. No effect on its function. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17550898;Dbxref=PMID:17550898 +P35056 UniProtKB Mutagenesis 24 24 . . . Note=Loss of UBE2D2-dependent ubiquitination. No effect on its function. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17550898;Dbxref=PMID:17550898 +##sequence-region P53900 1 129 +P53900 UniProtKB Chain 1 129 . . . ID=PRO_0000124848;Note=Prefoldin subunit 4 +P53900 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P53872 1 204 +P53872 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53872 UniProtKB Chain 21 174 . . . ID=PRO_0000203402;Note=Hydrophilin YNL190W +P53872 UniProtKB Propeptide 175 204 . . . ID=PRO_0000424804;Note=Removed in mature form +P53872 UniProtKB Compositional bias 7 163 . . . Note=Thr-rich +P53872 UniProtKB Lipidation 174 174 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10383953;Dbxref=PMID:10383953 +P53872 UniProtKB Glycosylation 55 55 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53872 UniProtKB Glycosylation 64 64 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53872 UniProtKB Glycosylation 75 75 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53872 UniProtKB Glycosylation 84 84 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53872 UniProtKB Glycosylation 95 95 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53872 UniProtKB Glycosylation 104 104 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53872 UniProtKB Glycosylation 115 115 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53872 UniProtKB Glycosylation 124 124 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53872 UniProtKB Glycosylation 135 135 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53872 UniProtKB Glycosylation 144 144 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53872 UniProtKB Glycosylation 155 155 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53896 1 198 +P53896 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53896 UniProtKB Chain 24 198 . . . ID=PRO_0000203415;Note=GPI mannosyltransferase 2 subunit PGA1 +P53896 UniProtKB Topological domain 24 163 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53896 UniProtKB Transmembrane 164 184 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53896 UniProtKB Topological domain 185 198 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53896 UniProtKB Glycosylation 72 72 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53896 UniProtKB Glycosylation 80 80 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12746 1 312 +Q12746 UniProtKB Chain 1 312 . . . ID=PRO_0000167628;Note=Plasma membrane-associated coenzyme Q6 reductase PGA3 +Q12746 UniProtKB Topological domain 1 15 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12746 UniProtKB Transmembrane 16 36 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12746 UniProtKB Topological domain 37 39 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12746 UniProtKB Transmembrane 40 60 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12746 UniProtKB Topological domain 61 179 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12746 UniProtKB Transmembrane 180 200 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12746 UniProtKB Topological domain 201 312 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12746 UniProtKB Domain 70 173 . . . Note=FAD-binding FR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00716 +Q12746 UniProtKB Nucleotide binding 153 168 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12746 UniProtKB Nucleotide binding 179 211 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P25578 1 521 +P25578 UniProtKB Chain 1 521 . . . ID=PRO_0000056827;Note=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase +P25578 UniProtKB Domain 177 203 . . . Note=PLD phosphodiesterase 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153 +P25578 UniProtKB Domain 419 457 . . . Note=PLD phosphodiesterase 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153 +P25578 UniProtKB Nucleotide binding 91 98 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25578 UniProtKB Active site 182 182 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153 +P25578 UniProtKB Active site 184 184 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153 +P25578 UniProtKB Active site 189 189 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153 +P25578 UniProtKB Sequence conflict 498 498 . . . Note=F->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P18898 1 376 +P18898 UniProtKB Chain 1 376 . . . ID=PRO_0000119775;Note=Geranylgeranyl transferase type-1 subunit beta +P18898 UniProtKB Repeat 128 179 . . . Note=PFTB 1 +P18898 UniProtKB Repeat 192 231 . . . Note=PFTB 2 +P18898 UniProtKB Repeat 259 301 . . . Note=PFTB 3 +P18898 UniProtKB Repeat 310 353 . . . Note=PFTB 4 +P18898 UniProtKB Region 216 218 . . . Note=Geranylgeranyl diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18898 UniProtKB Region 280 283 . . . Note=Geranylgeranyl diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18898 UniProtKB Region 289 292 . . . Note=Geranylgeranyl diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18898 UniProtKB Compositional bias 138 180 . . . Note=Cys-rich +P18898 UniProtKB Metal binding 286 286 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18898 UniProtKB Metal binding 288 288 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18898 UniProtKB Metal binding 341 341 . . . Note=Zinc%3B via tele nitrogen%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P18898 UniProtKB Mutagenesis 328 328 . . . Note=Defect in nuclear division and bud formation. G->S +##sequence-region P39535 1 881 +P39535 UniProtKB Chain 1 881 . . . ID=PRO_0000172518;Note=Low-affinity phosphate transporter PHO90 +P39535 UniProtKB Transmembrane 417 437 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39535 UniProtKB Transmembrane 456 476 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39535 UniProtKB Transmembrane 493 513 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39535 UniProtKB Transmembrane 514 534 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39535 UniProtKB Transmembrane 539 559 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39535 UniProtKB Transmembrane 581 601 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39535 UniProtKB Transmembrane 663 683 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39535 UniProtKB Transmembrane 691 711 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39535 UniProtKB Transmembrane 718 738 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39535 UniProtKB Transmembrane 758 778 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39535 UniProtKB Transmembrane 805 825 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39535 UniProtKB Transmembrane 854 874 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39535 UniProtKB Domain 1 288 . . . Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714 +##sequence-region P05066 1 565 +P05066 UniProtKB Domain 75 226 . . . Note=Photolyase/cryptochrome alpha/beta +P05066 UniProtKB Nucleotide binding 338 342 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05066 UniProtKB Nucleotide binding 482 484 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05066 UniProtKB Region 384 391 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05066 UniProtKB Region 451 452 . . . Note=Interaction with DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05066 UniProtKB Binding site 326 326 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05066 UniProtKB Binding site 514 514 . . . Note=DNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05066 UniProtKB Site 416 416 . . . Note=Electron transfer via tryptophanyl radical;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05066 UniProtKB Site 469 469 . . . Note=Electron transfer via tryptophanyl radical;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05066 UniProtKB Site 492 492 . . . Note=Electron transfer via tryptophanyl radical;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05066 UniProtKB Mutagenesis 387 387 . . . Note=Reduces substrate binding 100-fold. Reduces quantum yield for dimer photolysis 3-fold. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8344951;Dbxref=PMID:8344951 +P05066 UniProtKB Mutagenesis 463 463 . . . Note=Reduces substrate binding 100-fold. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8344951;Dbxref=PMID:8344951 +P05066 UniProtKB Mutagenesis 507 507 . . . Note=Reduces substrate binding 100-fold. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8344951;Dbxref=PMID:8344951 +P05066 UniProtKB Mutagenesis 517 517 . . . Note=Reduces substrate binding 10-fold. K->A +P05066 UniProtKB Sequence conflict 77 77 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05066 UniProtKB Sequence conflict 165 165 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05066 UniProtKB Sequence conflict 169 169 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05066 UniProtKB Sequence conflict 200 200 . . . Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05066 UniProtKB Sequence conflict 351 351 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05066 UniProtKB Sequence conflict 365 365 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05066 UniProtKB Sequence conflict 473 473 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32854 1 288 +P32854 UniProtKB Chain 1 288 . . . ID=PRO_0000210271;Note=Syntaxin PEP12 +P32854 UniProtKB Topological domain 1 268 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32854 UniProtKB Transmembrane 269 288 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32854 UniProtKB Domain 195 257 . . . Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202 +P32854 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P32854 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32854 UniProtKB Mutagenesis 271 271 . . . Note=Increases ubiquitination by TUL1. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11788821;Dbxref=PMID:11788821 +P32854 UniProtKB Sequence conflict 13 13 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32854 UniProtKB Sequence conflict 89 89 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38921 1 284 +P38921 UniProtKB Chain 1 284 . . . ID=PRO_0000090686;Note=Putative mitochondrial carrier protein PET8 +P38921 UniProtKB Transmembrane 5 25 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38921 UniProtKB Transmembrane 50 70 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38921 UniProtKB Transmembrane 98 118 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38921 UniProtKB Transmembrane 153 169 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38921 UniProtKB Transmembrane 194 214 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38921 UniProtKB Transmembrane 252 272 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38921 UniProtKB Repeat 2 75 . . . Note=Solcar 1 +P38921 UniProtKB Repeat 92 178 . . . Note=Solcar 2 +P38921 UniProtKB Repeat 192 271 . . . Note=Solcar 3 +##sequence-region P40155 1 199 +P40155 UniProtKB Chain 1 199 . . . ID=PRO_0000058333;Note=Peroxisomal membrane protein PEX17 +##sequence-region Q02969 1 394 +Q02969 UniProtKB Chain 1 394 . . . ID=PRO_0000270568;Note=Peroxisomal membrane protein PEX25 +Q02969 UniProtKB Topological domain 1 366 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02969 UniProtKB Transmembrane 367 383 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02969 UniProtKB Topological domain 384 394 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02969 UniProtKB Modified residue 58 58 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q02969 UniProtKB Modified residue 63 63 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q02969 UniProtKB Modified residue 289 289 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +Q02969 UniProtKB Sequence conflict 8 8 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08580 1 376 +Q08580 UniProtKB Chain 1 376 . . . ID=PRO_0000270569;Note=Peroxisomal membrane protein PEX27 +Q08580 UniProtKB Compositional bias 130 138 . . . Note=Poly-Leu +##sequence-region P53248 1 589 +P53248 UniProtKB Chain 1 589 . . . ID=PRO_0000058343;Note=Peroxisomal biogenesis factor 8 +P53248 UniProtKB Motif 587 589 . . . Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53903 1 129 +P53903 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.5 +P53903 UniProtKB Chain 2 129 . . . ID=PRO_0000203421;Note=Processing of GAS1 and ALP protein 2 +P53903 UniProtKB Transmembrane 23 42 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53903 UniProtKB Coiled coil 43 116 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53903 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.5 +P53903 UniProtKB Modified residue 119 119 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P40025 1 321 +P40025 UniProtKB Chain 1 321 . . . ID=PRO_0000202627;Note=Phosphate metabolism protein 8 +##sequence-region Q06651 1 286 +Q06651 UniProtKB Chain 1 286 . . . ID=PRO_0000245839;Note=E3 ubiquitin-protein ligase PIB1 +Q06651 UniProtKB Zinc finger 17 88 . . . Note=FYVE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091 +Q06651 UniProtKB Zinc finger 225 283 . . . Note=RING-type%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +Q06651 UniProtKB Mutagenesis 23 23 . . . Note=Abolishes endosomal targeting. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11526110;Dbxref=PMID:11526110 +Q06651 UniProtKB Mutagenesis 225 225 . . . Note=Abolishes E3 activity%2C strongly reduces zinc binding and destabilizes the protein%2C but no effect on subcellular location. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11526110;Dbxref=PMID:11526110 +Q06651 UniProtKB Sequence conflict 166 166 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P07271 1 859 +P07271 UniProtKB Transit peptide 1 45 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8253734;Dbxref=PMID:8253734 +P07271 UniProtKB Chain 46 859 . . . ID=PRO_0000013269;Note=ATP-dependent DNA helicase PIF1 +P07271 UniProtKB Nucleotide binding 258 265 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03176 +P07271 UniProtKB DNA binding 727 746 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03176 +P07271 UniProtKB Modified residue 70 70 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07271 UniProtKB Modified residue 72 72 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07271 UniProtKB Modified residue 169 169 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07271 UniProtKB Modified residue 584 584 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P07271 UniProtKB Alternative sequence 1 39 . . . ID=VSP_034601;Note=In isoform Nuclear. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07271 UniProtKB Mutagenesis 1 1 . . . Note=In PIF1-m1%3B loss of mitochondrial function. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8287473;Dbxref=PMID:8287473 +P07271 UniProtKB Mutagenesis 40 40 . . . Note=In PIF1-m2%3B loss of nuclear function. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8287473;Dbxref=PMID:8287473 +P07271 UniProtKB Mutagenesis 264 264 . . . Note=Abolishes helicase activity resulting in elongated telomeres%3B binds normally to DNA substrates. K->A%2CR;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10926538,ECO:0000269|PubMed:16121131,ECO:0000269|PubMed:16816432;Dbxref=PMID:10926538,PMID:16121131,PMID:16816432 +P07271 UniProtKB Sequence conflict 309 309 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07271 UniProtKB Sequence conflict 322 322 . . . Note=V->VG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07271 UniProtKB Sequence conflict 426 426 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07271 UniProtKB Sequence conflict 800 801 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P19657 1 947 +P19657 UniProtKB Chain 1 947 . . . ID=PRO_0000046272;Note=Plasma membrane ATPase 2 +P19657 UniProtKB Topological domain 1 144 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19657 UniProtKB Transmembrane 145 165 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19657 UniProtKB Topological domain 166 169 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19657 UniProtKB Transmembrane 170 189 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19657 UniProtKB Topological domain 190 320 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19657 UniProtKB Transmembrane 321 342 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19657 UniProtKB Topological domain 343 353 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19657 UniProtKB Transmembrane 354 376 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19657 UniProtKB Topological domain 377 748 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19657 UniProtKB Transmembrane 749 767 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19657 UniProtKB Topological domain 768 783 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19657 UniProtKB Transmembrane 784 803 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19657 UniProtKB Topological domain 804 853 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19657 UniProtKB Transmembrane 854 874 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19657 UniProtKB Topological domain 875 886 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19657 UniProtKB Transmembrane 887 903 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19657 UniProtKB Topological domain 904 947 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P19657 UniProtKB Compositional bias 33 47 . . . Note=Poly-Ser +P19657 UniProtKB Compositional bias 62 91 . . . Note=Asp/Glu-rich (acidic) +P19657 UniProtKB Active site 407 407 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19657 UniProtKB Metal binding 663 663 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19657 UniProtKB Metal binding 667 667 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P19657 UniProtKB Sequence conflict 944 944 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P87284 1 55 +P87284 UniProtKB Chain 1 55 . . . ID=PRO_0000193987;Note=Plasma membrane proteolipid 3 +P87284 UniProtKB Transmembrane 3 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P87284 UniProtKB Transmembrane 31 51 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P14242 1 873 +P14242 UniProtKB Chain 1 873 . . . ID=PRO_0000245571;Note=DNA mismatch repair protein PMS1 +P14242 UniProtKB Region 1 357 . . . Note=DNA- and ATP-binding +P14242 UniProtKB Region 661 873 . . . Note=Interaction with MLH1 +P14242 UniProtKB Modified residue 393 393 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14242 UniProtKB Modified residue 566 566 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14242 UniProtKB Natural variant 41 41 . . . Note=In strain: SK1 and YJM421. N->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11907579,ECO:0000269|PubMed:16273108;Dbxref=PMID:11907579,PMID:16273108 +P14242 UniProtKB Natural variant 112 112 . . . Note=In strain: SK1 and YJM421. I->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11907579,ECO:0000269|PubMed:16273108;Dbxref=PMID:11907579,PMID:16273108 +P14242 UniProtKB Natural variant 384 384 . . . Note=In strain: SK1%2C YJM320%2C YJM339 and YJM421. F->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11907579,ECO:0000269|PubMed:16273108;Dbxref=PMID:11907579,PMID:16273108 +P14242 UniProtKB Natural variant 392 392 . . . Note=In strain: YJM320. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11907579;Dbxref=PMID:11907579 +P14242 UniProtKB Natural variant 400 400 . . . Note=In strain: SK1%2C YJM320%2C YJM339 and YJM421. T->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11907579,ECO:0000269|PubMed:16273108;Dbxref=PMID:11907579,PMID:16273108 +P14242 UniProtKB Natural variant 401 401 . . . Note=In strain: YJM320 and YJM421. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11907579;Dbxref=PMID:11907579 +P14242 UniProtKB Natural variant 416 416 . . . Note=In strain: SK1%2C YJM320%2C YJM339 and YJM421. T->TCEGT +P14242 UniProtKB Natural variant 458 458 . . . Note=In strain: EAY1068. D->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492773;Dbxref=PMID:16492773 +P14242 UniProtKB Natural variant 475 475 . . . Note=In strain: YJM339. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11907579;Dbxref=PMID:11907579 +P14242 UniProtKB Natural variant 513 513 . . . Note=In strain: SK1. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P14242 UniProtKB Natural variant 564 564 . . . Note=In strain: YJM320. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11907579;Dbxref=PMID:11907579 +P14242 UniProtKB Natural variant 768 768 . . . Note=In strain: YJM320. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11907579;Dbxref=PMID:11907579 +P14242 UniProtKB Natural variant 818 818 . . . Note=In strain: SK1 and YJM320%3B forms a non-functional heterodimer with MHL1 from strain S288c%2C resulting in an accumulation of mutations in spore progeny of crosses between these strains. R->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11907579,ECO:0000269|PubMed:16273108;Dbxref=PMID:11907579,PMID:16273108 +P14242 UniProtKB Mutagenesis 30 30 . . . Note=Reduces ATPase activity by 62%25. Displays 60-fold increase in spontaneous mutation accumulation. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10938116,ECO:0000269|PubMed:11717305;Dbxref=PMID:10938116,PMID:11717305 +P14242 UniProtKB Mutagenesis 34 34 . . . Note=Reduces ATPase activity by 84%25. Displays 11000-fold increase in spontaneous mutation accumulation. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11717305;Dbxref=PMID:11717305 +P14242 UniProtKB Mutagenesis 95 95 . . . Note=Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9234704;Dbxref=PMID:9234704 +P14242 UniProtKB Mutagenesis 97 97 . . . Note=Displays an increase in spontaneous mutation accumulation. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10938116;Dbxref=PMID:10938116 +P14242 UniProtKB Mutagenesis 297 297 . . . Note=Displays a 60-fold increase in spontaneous mutation accumulation. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12682353;Dbxref=PMID:12682353 +P14242 UniProtKB Mutagenesis 851 851 . . . Note=Confers a strong defect in the repair of primer strand-specific 1-bp loops during DNA replication%2C but not during meoitic recombination. Does not impair heterodimer formation. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16227575;Dbxref=PMID:16227575 +P14242 UniProtKB Mutagenesis 857 857 . . . Note=Confers a strong defect in the repair of primer strand-specific 1-bp loops during DNA replication%2C but not during meoitic recombination. Does not impair heterodimer formation. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16227575;Dbxref=PMID:16227575 +P14242 UniProtKB Sequence conflict 695 695 . . . Note=Y->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14242 UniProtKB Sequence conflict 861 861 . . . Note=L->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14242 UniProtKB Helix 13 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Helix 24 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Beta strand 41 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Turn 49 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Beta strand 53 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Helix 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Turn 69 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Beta strand 92 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Helix 98 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Beta strand 106 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Beta strand 120 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Beta strand 131 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Beta strand 140 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Turn 150 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Helix 155 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Helix 165 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Beta strand 187 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Beta strand 199 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Helix 211 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Turn 221 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Beta strand 227 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Helix 237 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Beta strand 259 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Beta strand 274 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Beta strand 288 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Helix 293 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Beta strand 314 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Helix 322 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Beta strand 330 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Helix 341 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3H4L +P14242 UniProtKB Helix 650 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P14242 UniProtKB Helix 653 665 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P14242 UniProtKB Helix 668 672 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P14242 UniProtKB Beta strand 675 680 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P14242 UniProtKB Turn 681 683 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P14242 UniProtKB Beta strand 684 690 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P14242 UniProtKB Beta strand 695 701 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P14242 UniProtKB Helix 702 717 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P14242 UniProtKB Beta strand 722 731 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P14242 UniProtKB Helix 739 742 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P14242 UniProtKB Helix 747 750 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P14242 UniProtKB Beta strand 767 773 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P14242 UniProtKB Helix 782 794 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P14242 UniProtKB Helix 806 819 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P14242 UniProtKB Helix 829 838 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P14242 UniProtKB Helix 839 841 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P14242 UniProtKB Beta strand 842 844 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P14242 UniProtKB Beta strand 853 860 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +P14242 UniProtKB Helix 869 871 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4E4W +##sequence-region P47190 1 753 +P47190 UniProtKB Chain 1 753 . . . ID=PRO_0000121493;Note=Dolichyl-phosphate-mannose--protein mannosyltransferase 3 +P47190 UniProtKB Topological domain 1 50 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Transmembrane 51 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Topological domain 72 148 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Transmembrane 149 169 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Topological domain 170 174 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Transmembrane 175 195 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Topological domain 196 235 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Transmembrane 236 256 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Topological domain 257 282 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Transmembrane 283 303 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Topological domain 304 602 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Transmembrane 603 623 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Topological domain 624 639 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Transmembrane 640 660 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Topological domain 661 665 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Transmembrane 666 686 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Topological domain 687 703 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Transmembrane 704 724 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Topological domain 725 753 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Domain 332 387 . . . Note=MIR 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +P47190 UniProtKB Domain 401 457 . . . Note=MIR 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +P47190 UniProtKB Domain 465 523 . . . Note=MIR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +P47190 UniProtKB Glycosylation 124 124 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Glycosylation 324 324 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Glycosylation 398 398 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47190 UniProtKB Sequence conflict 397 397 . . . Note=E->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47190 UniProtKB Sequence conflict 567 567 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P52867 1 743 +P52867 UniProtKB Chain 1 743 . . . ID=PRO_0000121495;Note=Dolichyl-phosphate-mannose--protein mannosyltransferase 5 +P52867 UniProtKB Topological domain 1 46 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Transmembrane 47 67 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Topological domain 68 129 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Transmembrane 130 150 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Topological domain 151 158 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Transmembrane 159 179 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Topological domain 180 180 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Transmembrane 181 201 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Topological domain 202 231 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Transmembrane 232 252 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Topological domain 253 264 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Transmembrane 265 285 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Topological domain 286 583 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Transmembrane 584 604 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Topological domain 605 623 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Transmembrane 624 644 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Topological domain 645 646 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Transmembrane 647 667 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Topological domain 668 683 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Transmembrane 684 704 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Topological domain 705 743 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Domain 320 374 . . . Note=MIR 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +P52867 UniProtKB Domain 384 444 . . . Note=MIR 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +P52867 UniProtKB Domain 454 510 . . . Note=MIR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +P52867 UniProtKB Glycosylation 33 33 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Glycosylation 213 213 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Glycosylation 380 380 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52867 UniProtKB Glycosylation 386 386 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P42934 1 759 +P42934 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P42934 UniProtKB Chain 2 759 . . . ID=PRO_0000121496;Note=Dolichyl-phosphate-mannose--protein mannosyltransferase 6 +P42934 UniProtKB Topological domain 2 58 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Transmembrane 59 79 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Topological domain 80 164 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Transmembrane 165 185 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Topological domain 186 194 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Transmembrane 195 215 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Topological domain 216 251 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Transmembrane 252 272 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Topological domain 273 293 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Transmembrane 294 314 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Topological domain 315 618 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Transmembrane 619 639 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Topological domain 640 656 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Transmembrane 657 677 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Topological domain 678 686 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Transmembrane 687 707 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Topological domain 708 715 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Transmembrane 716 736 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Topological domain 737 759 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Domain 340 394 . . . Note=MIR 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +P42934 UniProtKB Domain 409 467 . . . Note=MIR 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +P42934 UniProtKB Domain 482 540 . . . Note=MIR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +P42934 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P42934 UniProtKB Glycosylation 156 156 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Glycosylation 404 404 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42934 UniProtKB Glycosylation 481 481 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q05788 1 311 +Q05788 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q05788 UniProtKB Chain 2 311 . . . ID=PRO_0000184538;Note=Purine nucleoside phosphorylase +Q05788 UniProtKB Region 101 103 . . . Note=Phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55859 +Q05788 UniProtKB Binding site 46 46 . . . Note=Phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55859 +Q05788 UniProtKB Binding site 81 81 . . . Note=Phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55859 +Q05788 UniProtKB Binding site 134 134 . . . Note=Phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55859 +Q05788 UniProtKB Binding site 219 219 . . . Note=Purine nucleoside;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55859 +Q05788 UniProtKB Binding site 238 238 . . . Note=Phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55859 +Q05788 UniProtKB Binding site 261 261 . . . Note=Purine nucleoside;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55859 +Q05788 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q05788 UniProtKB Modified residue 275 275 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P47180 1 361 +P47180 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47180 UniProtKB Chain 19 361 . . . ID=PRO_0000024797;Note=Polygalacturonase +P47180 UniProtKB Repeat 155 185 . . . Note=PbH1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47180 UniProtKB Repeat 186 207 . . . Note=PbH1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47180 UniProtKB Repeat 208 228 . . . Note=PbH1 3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47180 UniProtKB Repeat 237 258 . . . Note=PbH1 4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47180 UniProtKB Repeat 266 288 . . . Note=PbH1 5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47180 UniProtKB Active site 200 200 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74213 +P47180 UniProtKB Active site 222 222 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10052 +P47180 UniProtKB Glycosylation 318 318 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P47180 UniProtKB Glycosylation 330 330 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P47180 UniProtKB Disulfide bond 27 43 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74213 +P47180 UniProtKB Disulfide bond 202 218 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74213 +P47180 UniProtKB Disulfide bond 350 361 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O74213 +P47180 UniProtKB Sequence conflict 23 23 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P37012 1 569 +P37012 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P37012 UniProtKB Chain 2 569 . . . ID=PRO_0000147797;Note=Phosphoglucomutase 2 +P37012 UniProtKB Region 119 120 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P37012 UniProtKB Region 294 295 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P37012 UniProtKB Region 378 380 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P37012 UniProtKB Active site 119 119 . . . Note=Phosphoserine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P37012 UniProtKB Metal binding 119 119 . . . Note=Magnesium%3B via phosphate group;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P37012 UniProtKB Metal binding 290 290 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P37012 UniProtKB Metal binding 292 292 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P37012 UniProtKB Metal binding 294 294 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P37012 UniProtKB Binding site 20 20 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P37012 UniProtKB Binding site 24 24 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P37012 UniProtKB Binding site 132 132 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P37012 UniProtKB Binding site 359 359 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P37012 UniProtKB Binding site 391 391 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P37012 UniProtKB Binding site 522 522 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P37012 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P37012 UniProtKB Modified residue 111 111 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P37012 UniProtKB Modified residue 117 117 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P37012 UniProtKB Modified residue 119 119 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P37012 UniProtKB Sequence conflict 27 27 . . . Note=T->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37012 UniProtKB Sequence conflict 32 32 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P37012 UniProtKB Sequence conflict 272 272 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03262 1 622 +Q03262 UniProtKB Chain 1 622 . . . ID=PRO_0000148022;Note=Phosphoribomutase +Q03262 UniProtKB Region 158 159 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +Q03262 UniProtKB Region 329 330 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +Q03262 UniProtKB Region 428 430 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +Q03262 UniProtKB Active site 158 158 . . . Note=Phosphoserine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +Q03262 UniProtKB Metal binding 158 158 . . . Note=Magnesium%3B via phosphate group;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +Q03262 UniProtKB Metal binding 325 325 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +Q03262 UniProtKB Metal binding 327 327 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +Q03262 UniProtKB Metal binding 329 329 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +Q03262 UniProtKB Binding site 57 57 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +Q03262 UniProtKB Binding site 61 61 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +Q03262 UniProtKB Binding site 168 168 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +Q03262 UniProtKB Binding site 404 404 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +Q03262 UniProtKB Binding site 442 442 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +Q03262 UniProtKB Modified residue 158 158 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q03262 UniProtKB Mutagenesis 158 158 . . . Note=Loss of function. S->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18042468;Dbxref=PMID:18042468 +Q03262 UniProtKB Mutagenesis 326 326 . . . Note=No effect. P->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18042468;Dbxref=PMID:18042468 +##sequence-region P40961 1 287 +P40961 UniProtKB Chain 1 287 . . . ID=PRO_0000213883;Note=Prohibitin-1 +P40961 UniProtKB Coiled coil 180 224 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15525670;Dbxref=PMID:15525670 +P40961 UniProtKB Sequence conflict 43 43 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40961 UniProtKB Sequence conflict 222 222 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40961 UniProtKB Sequence conflict 225 225 . . . Note=F->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P50085 1 310 +P50085 UniProtKB Chain 1 310 . . . ID=PRO_0000213888;Note=Prohibitin-2 +P50085 UniProtKB Transmembrane 38 58 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50085 UniProtKB Coiled coil 212 253 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15525670;Dbxref=PMID:15525670 +##sequence-region P36093 1 366 +P36093 UniProtKB Chain 1 366 . . . ID=PRO_0000058377;Note=Putative transcription factor PHD1 +P36093 UniProtKB Domain 186 292 . . . Note=HTH APSES-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630 +P36093 UniProtKB DNA binding 220 241 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630 +##sequence-region P50947 1 330 +P50947 UniProtKB Chain 1 330 . . . ID=PRO_0000203440;Note=Transcriptional regulatory protein PHO23 +P50947 UniProtKB Zinc finger 280 329 . . . Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 +P50947 UniProtKB Metal binding 283 283 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P50947 UniProtKB Metal binding 285 285 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P50947 UniProtKB Metal binding 296 296 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P50947 UniProtKB Metal binding 301 301 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P50947 UniProtKB Metal binding 307 307 . . . Note=Zinc 1%3B via pros nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P50947 UniProtKB Metal binding 310 310 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P50947 UniProtKB Metal binding 323 323 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P50947 UniProtKB Metal binding 326 326 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P50947 UniProtKB Binding site 282 282 . . . Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P50947 UniProtKB Binding site 293 293 . . . Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P50947 UniProtKB Binding site 297 297 . . . Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P50947 UniProtKB Binding site 305 305 . . . Note=Histone H3K4me3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 +P50947 UniProtKB Natural variant 8 8 . . . Note=In strain: SK1. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P50947 UniProtKB Natural variant 35 35 . . . Note=In strain: SK1. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +##sequence-region P25297 1 587 +P25297 UniProtKB Chain 1 587 . . . ID=PRO_0000050477;Note=Inorganic phosphate transporter PHO84 +P25297 UniProtKB Topological domain 1 67 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Transmembrane 68 88 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Topological domain 89 108 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Transmembrane 109 129 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Topological domain 130 133 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Transmembrane 134 154 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Topological domain 155 156 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Transmembrane 157 177 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Topological domain 178 201 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Transmembrane 202 222 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Topological domain 223 250 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Transmembrane 251 271 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Topological domain 272 345 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Transmembrane 346 366 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Topological domain 367 395 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Transmembrane 396 416 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Topological domain 417 419 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Transmembrane 420 440 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Topological domain 441 442 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Transmembrane 443 463 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Topological domain 464 485 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Transmembrane 486 506 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Topological domain 507 522 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Transmembrane 523 543 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Topological domain 544 587 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25297 UniProtKB Modified residue 302 302 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P25297 UniProtKB Modified residue 303 303 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P25297 UniProtKB Modified residue 316 316 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P25297 UniProtKB Modified residue 317 317 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P25297 UniProtKB Modified residue 321 321 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P25297 UniProtKB Modified residue 577 577 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P25297 UniProtKB Modified residue 579 579 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P25297 UniProtKB Modified residue 581 581 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P25297 UniProtKB Cross-link 6 6 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P25297 UniProtKB Cross-link 298 298 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P25297 UniProtKB Sequence conflict 162 162 . . . Note=A->AHSPAINFVA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25297 UniProtKB Sequence conflict 353 353 . . . Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P46956 1 311 +P46956 UniProtKB Chain 1 311 . . . ID=PRO_0000058404;Note=Inorganic phosphate transporter PHO86 +P46956 UniProtKB Topological domain 1 70 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46956 UniProtKB Transmembrane 71 91 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46956 UniProtKB Topological domain 92 117 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46956 UniProtKB Transmembrane 118 138 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46956 UniProtKB Topological domain 139 311 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46956 UniProtKB Sequence conflict 8 8 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38264 1 188 +P38264 UniProtKB Chain 1 188 . . . ID=PRO_0000058405;Note=SRP-independent targeting protein 3 +P38264 UniProtKB Transmembrane 27 47 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38264 UniProtKB Modified residue 157 157 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P27514 1 894 +P27514 UniProtKB Chain 1 894 . . . ID=PRO_0000172519;Note=Low-affinity phosphate transporter PHO91 +P27514 UniProtKB Transmembrane 430 450 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27514 UniProtKB Transmembrane 474 494 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27514 UniProtKB Transmembrane 511 531 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27514 UniProtKB Transmembrane 557 577 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27514 UniProtKB Transmembrane 602 622 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27514 UniProtKB Transmembrane 642 662 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27514 UniProtKB Transmembrane 682 702 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27514 UniProtKB Transmembrane 706 726 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27514 UniProtKB Transmembrane 738 758 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27514 UniProtKB Transmembrane 777 797 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27514 UniProtKB Transmembrane 799 819 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27514 UniProtKB Transmembrane 824 844 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27514 UniProtKB Transmembrane 874 894 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P27514 UniProtKB Domain 1 256 . . . Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714 +P27514 UniProtKB Modified residue 295 295 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P27514 UniProtKB Modified residue 311 311 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P27514 UniProtKB Modified residue 312 312 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q03306 1 898 +Q03306 UniProtKB Chain 1 898 . . . ID=PRO_0000086554;Note=Serine/threonine-protein kinase PKH3 +Q03306 UniProtKB Domain 11 293 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03306 UniProtKB Nucleotide binding 17 25 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03306 UniProtKB Active site 138 138 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q03306 UniProtKB Binding site 41 41 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03306 UniProtKB Modified residue 696 696 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03306 UniProtKB Modified residue 753 753 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03306 UniProtKB Modified residue 871 871 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P33333 1 303 +P33333 UniProtKB Chain 1 303 . . . ID=PRO_0000208189;Note=Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase +P33333 UniProtKB Transmembrane 16 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33333 UniProtKB Motif 82 87 . . . Note=HXXXXD motif +P33333 UniProtKB Natural variant 44 44 . . . Note=In allele suppressor SLC1-1. Q->L +P33333 UniProtKB Sequence conflict 115 115 . . . Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P05030 1 918 +P05030 UniProtKB Chain 1 918 . . . ID=PRO_0000046271;Note=Plasma membrane ATPase 1 +P05030 UniProtKB Topological domain 1 115 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05030 UniProtKB Transmembrane 116 136 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05030 UniProtKB Topological domain 137 140 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05030 UniProtKB Transmembrane 141 160 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05030 UniProtKB Topological domain 161 291 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05030 UniProtKB Transmembrane 292 313 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05030 UniProtKB Topological domain 314 325 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05030 UniProtKB Transmembrane 326 347 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05030 UniProtKB Topological domain 348 719 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05030 UniProtKB Transmembrane 720 738 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05030 UniProtKB Topological domain 739 754 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05030 UniProtKB Transmembrane 755 774 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05030 UniProtKB Topological domain 775 824 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05030 UniProtKB Transmembrane 825 845 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05030 UniProtKB Topological domain 846 857 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05030 UniProtKB Transmembrane 858 874 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05030 UniProtKB Topological domain 875 918 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P05030 UniProtKB Compositional bias 5 17 . . . Note=Poly-Ser +P05030 UniProtKB Compositional bias 31 78 . . . Note=Asp/Glu-rich (acidic) +P05030 UniProtKB Compositional bias 39 44 . . . Note=Poly-Asp +P05030 UniProtKB Compositional bias 585 590 . . . Note=Poly-Gly +P05030 UniProtKB Active site 378 378 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05030 UniProtKB Metal binding 634 634 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05030 UniProtKB Metal binding 638 638 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P05030 UniProtKB Modified residue 61 61 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P05030 UniProtKB Modified residue 175 175 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P05030 UniProtKB Modified residue 911 911 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P05030 UniProtKB Modified residue 912 912 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P05030 UniProtKB Modified residue 918 918 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P05030 UniProtKB Cross-link 252 252 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P05030 UniProtKB Cross-link 555 555 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14557538;Dbxref=PMID:14557538 +P05030 UniProtKB Mutagenesis 129 129 . . . Note=Normal activity. E->L%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955 +P05030 UniProtKB Mutagenesis 200 200 . . . Note=Activity reduced to 23%25. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955 +P05030 UniProtKB Mutagenesis 233 233 . . . Note=Activity reduced to 33%25. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955 +P05030 UniProtKB Mutagenesis 271 271 . . . Note=Normal activity. R->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955 +P05030 UniProtKB Mutagenesis 335 335 . . . Note=Activity reduced to 53%25. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955 +P05030 UniProtKB Mutagenesis 378 378 . . . Note=Activity reduced to 67%25. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955 +P05030 UniProtKB Mutagenesis 378 378 . . . Note=Activity reduced to 73%25. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955 +P05030 UniProtKB Mutagenesis 378 378 . . . Note=Activity reduced to 49%25. D->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955 +P05030 UniProtKB Mutagenesis 474 474 . . . Note=Activity reduced to 19%25. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955 +P05030 UniProtKB Mutagenesis 534 534 . . . Note=Activity reduced to 37%25. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955 +P05030 UniProtKB Mutagenesis 560 560 . . . Note=Activity reduced to 24%25. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955 +P05030 UniProtKB Mutagenesis 638 638 . . . Note=Activity reduced to 24%25. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955 +P05030 UniProtKB Mutagenesis 848 848 . . . Note=Normal activity. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2901955;Dbxref=PMID:2901955 +##sequence-region P53238 1 335 +P53238 UniProtKB Chain 1 335 . . . ID=PRO_0000073720;Note=Peflin +P53238 UniProtKB Domain 144 192 . . . Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P53238 UniProtKB Domain 198 223 . . . Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P53238 UniProtKB Domain 224 259 . . . Note=EF-hand 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P53238 UniProtKB Domain 260 300 . . . Note=EF-hand 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P53238 UniProtKB Domain 301 332 . . . Note=EF-hand 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P53238 UniProtKB Calcium binding 170 181 . . . Note=1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P53238 UniProtKB Calcium binding 237 248 . . . Note=2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P53238 UniProtKB Mutagenesis 218 218 . . . Note=Induces EGTA and SDS sensitivity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17640275;Dbxref=PMID:17640275 +P53238 UniProtKB Sequence conflict 324 324 . . . Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32609 1 515 +P32609 UniProtKB Chain 1 515 . . . ID=PRO_0000046858;Note=Vacuolar segregation protein PEP7 +P32609 UniProtKB Zinc finger 6 29 . . . Note=C2H2-type +P32609 UniProtKB Zinc finger 72 137 . . . Note=FYVE-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091 +P32609 UniProtKB Zinc finger 215 297 . . . Note=FYVE-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091 +P32609 UniProtKB Sequence conflict 366 366 . . . Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53261 1 605 +P53261 UniProtKB Chain 1 605 . . . ID=PRO_0000186192;Note=Pescadillo homolog +P53261 UniProtKB Domain 355 449 . . . Note=BRCT;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03028 +P53261 UniProtKB Region 51 484 . . . Note=Sufficient for interaction with ERB1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18448671;Dbxref=PMID:18448671 +P53261 UniProtKB Coiled coil 294 342 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03028 +P53261 UniProtKB Coiled coil 530 605 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03028 +P53261 UniProtKB Modified residue 288 288 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53261 UniProtKB Modified residue 308 308 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53261 UniProtKB Mutagenesis 380 380 . . . Note=Temperature sensitive mutant. I->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110181;Dbxref=PMID:12110181 +P53261 UniProtKB Mutagenesis 431 431 . . . Note=Temperature sensitive mutant. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110181;Dbxref=PMID:12110181 +##sequence-region P39718 1 180 +P39718 UniProtKB Chain 1 180 . . . ID=PRO_0000058339;Note=Peroxisome assembly protein 22 +P39718 UniProtKB Transmembrane 15 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39718 UniProtKB Beta strand 62 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P39718 UniProtKB Helix 68 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P39718 UniProtKB Helix 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P39718 UniProtKB Turn 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P39718 UniProtKB Beta strand 83 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P39718 UniProtKB Turn 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P39718 UniProtKB Beta strand 94 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P39718 UniProtKB Helix 100 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P39718 UniProtKB Turn 108 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P39718 UniProtKB Helix 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P39718 UniProtKB Beta strand 115 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P39718 UniProtKB Helix 121 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P39718 UniProtKB Beta strand 134 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P39718 UniProtKB Helix 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P39718 UniProtKB Beta strand 145 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9P +P39718 UniProtKB Helix 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9P +P39718 UniProtKB Helix 158 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P39718 UniProtKB Beta strand 163 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +P39718 UniProtKB Helix 171 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Y9M +##sequence-region P16861 1 987 +P16861 UniProtKB Chain 1 987 . . . ID=PRO_0000112045;Note=ATP-dependent 6-phosphofructokinase subunit alpha +P16861 UniProtKB Nucleotide binding 278 279 . . . Note=ATP;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P0A796,ECO:0000255|HAMAP-Rule:MF_03184 +P16861 UniProtKB Nucleotide binding 308 311 . . . Note=ATP;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P0A796,ECO:0000255|HAMAP-Rule:MF_03184 +P16861 UniProtKB Region 1 580 . . . Note=N-terminal catalytic PFK domain 1;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000305|PubMed:21241708;Dbxref=PMID:21241708 +P16861 UniProtKB Region 354 356 . . . Note=Substrate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16861 UniProtKB Region 398 400 . . . Note=Substrate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16861 UniProtKB Region 488 491 . . . Note=Substrate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16861 UniProtKB Region 581 594 . . . Note=Interdomain linker;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000305|PubMed:21241708;Dbxref=PMID:21241708 +P16861 UniProtKB Region 595 987 . . . Note=C-terminal regulatory PFK domain 2;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000305|PubMed:21241708;Dbxref=PMID:21241708 +P16861 UniProtKB Region 722 726 . . . Note=Allosteric activator fructose 2%2C6-bisphosphate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16861 UniProtKB Region 767 769 . . . Note=Allosteric activator fructose 2%2C6-bisphosphate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16861 UniProtKB Region 859 862 . . . Note=Allosteric activator fructose 2%2C6-bisphosphate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16861 UniProtKB Active site 356 356 . . . Note=Proton acceptor;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P0A796,ECO:0000255|HAMAP-Rule:MF_03184 +P16861 UniProtKB Metal binding 309 309 . . . Note=Magnesium%3B catalytic;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P0A796,ECO:0000255|HAMAP-Rule:MF_03184 +P16861 UniProtKB Binding site 215 215 . . . Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P0A796,ECO:0000255|HAMAP-Rule:MF_03184 +P16861 UniProtKB Binding site 391 391 . . . Note=Substrate%3B shared with subunit beta;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16861 UniProtKB Binding site 455 455 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16861 UniProtKB Binding site 482 482 . . . Note=Substrate%3B shared with subunit beta;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16861 UniProtKB Binding site 665 665 . . . Note=Allosteric activator fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16861 UniProtKB Binding site 760 760 . . . Note=Allosteric activator fructose 2%2C6-bisphosphate%3B shared with subunit beta;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16861 UniProtKB Binding site 827 827 . . . Note=Allosteric activator fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16861 UniProtKB Binding site 853 853 . . . Note=Allosteric activator fructose 2%2C6-bisphosphate%3B shared with subunit beta;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16861 UniProtKB Binding site 952 952 . . . Note=Allosteric activator fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16861 UniProtKB Modified residue 3 3 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P16861 UniProtKB Modified residue 166 166 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P16861 UniProtKB Modified residue 179 179 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P16861 UniProtKB Modified residue 185 185 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P16861 UniProtKB Modified residue 189 189 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P16861 UniProtKB Modified residue 192 192 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P16861 UniProtKB Modified residue 217 217 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P16861 UniProtKB Modified residue 450 450 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P16861 UniProtKB Cross-link 89 89 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P16861 UniProtKB Cross-link 625 625 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P16861 UniProtKB Mutagenesis 309 309 . . . Note=Reduces maximal activity of the holoenzyme by 50%25. Completely abolishes catalytic activity%3B when associated with 'S-348' in subunit beta. D->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8132627;Dbxref=PMID:8132627 +P16861 UniProtKB Mutagenesis 356 356 . . . Note=Reduces maximal activity of the holoenzyme by 50%25. Completely abolishes catalytic activity%3B when associated with 'S-348' in subunit beta. D->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8132627;Dbxref=PMID:8132627 +P16861 UniProtKB Mutagenesis 447 447 . . . Note=Reduces maximal activity of the holoenzyme by less than 25%25. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8132627;Dbxref=PMID:8132627 +P16861 UniProtKB Mutagenesis 488 488 . . . Note=Increases the KM for fructose 6-phosphate 20 fold. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8132627;Dbxref=PMID:8132627 +P16861 UniProtKB Mutagenesis 724 724 . . . Note=Abolishes sensitivity of the holoenzyme to fructose 2%2C6-bisphosphate activation%3B when associated with 'D-718' in subunit beta. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8663166;Dbxref=PMID:8663166 +P16861 UniProtKB Mutagenesis 728 728 . . . Note=Drastically reduces sensitivity of the holoenzyme to ATP inhibition. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11221662;Dbxref=PMID:11221662 +P16861 UniProtKB Mutagenesis 859 859 . . . Note=Reduces sensitivity of the holoenzyme to fructose 2%2C6-bisphosphate activation%3B when associated with 'S-853' in subunit beta. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8663166;Dbxref=PMID:8663166 +P16861 UniProtKB Beta strand 207 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 220 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 237 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 244 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 254 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 260 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 266 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 281 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 285 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 300 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 309 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 322 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 331 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Turn 337 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 347 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 368 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 392 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 404 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 416 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 421 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Turn 427 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 430 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 449 454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 467 477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 481 485 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 487 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 497 515 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 524 537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 538 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 557 562 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 568 579 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 595 603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 608 622 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 625 629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 632 639 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 642 644 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Turn 647 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 653 655 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 668 670 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 672 681 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 685 692 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 693 705 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Turn 706 708 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 710 713 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 716 721 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 736 757 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 758 766 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 773 780 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Turn 781 783 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 785 788 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 790 792 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 796 812 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 821 826 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 831 833 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 835 846 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 849 856 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 858 862 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 868 890 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 921 923 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 924 930 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 933 938 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 939 942 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Turn 948 951 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Beta strand 953 955 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 960 969 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16861 UniProtKB Helix 972 978 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +##sequence-region P16862 1 959 +P16862 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8223596;Dbxref=PMID:8223596 +P16862 UniProtKB Chain 2 959 . . . ID=PRO_0000112046;Note=ATP-dependent 6-phosphofructokinase subunit beta +P16862 UniProtKB Nucleotide binding 270 271 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03184 +P16862 UniProtKB Nucleotide binding 300 303 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03184 +P16862 UniProtKB Region 2 573 . . . Note=N-terminal catalytic PFK domain 1;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000305|PubMed:21241708;Dbxref=PMID:21241708 +P16862 UniProtKB Region 346 348 . . . Note=Substrate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16862 UniProtKB Region 390 392 . . . Note=Substrate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16862 UniProtKB Region 481 484 . . . Note=Substrate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16862 UniProtKB Region 574 587 . . . Note=Interdomain linker;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000305|PubMed:21241708;Dbxref=PMID:21241708 +P16862 UniProtKB Region 588 959 . . . Note=C-terminal regulatory PFK domain 2;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000305|PubMed:21241708;Dbxref=PMID:21241708 +P16862 UniProtKB Region 716 720 . . . Note=Allosteric activator fructose 2%2C6-bisphosphate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16862 UniProtKB Region 761 763 . . . Note=Allosteric activator fructose 2%2C6-bisphosphate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16862 UniProtKB Region 853 856 . . . Note=Allosteric activator fructose 2%2C6-bisphosphate binding;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16862 UniProtKB Active site 348 348 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03184 +P16862 UniProtKB Metal binding 301 301 . . . Note=Magnesium%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03184 +P16862 UniProtKB Binding site 206 206 . . . Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03184 +P16862 UniProtKB Binding site 383 383 . . . Note=Substrate%3B shared with subunit alpha;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16862 UniProtKB Binding site 447 447 . . . Note=Substrate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16862 UniProtKB Binding site 475 475 . . . Note=Substrate%3B shared with subunit alpha;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16862 UniProtKB Binding site 658 658 . . . Note=Allosteric activator fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16862 UniProtKB Binding site 754 754 . . . Note=Allosteric activator fructose 2%2C6-bisphosphate%3B shared with subunit alpha;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03184 +P16862 UniProtKB Binding site 847 847 . . . Note=Allosteric activator fructose 2%2C6-bisphosphate%3B shared with subunit alpha;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03184 +P16862 UniProtKB Binding site 935 935 . . . Note=Allosteric activator fructose 2%2C6-bisphosphate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03184,ECO:0000269|PubMed:21241708;Dbxref=PMID:21241708 +P16862 UniProtKB Modified residue 152 152 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P16862 UniProtKB Modified residue 163 163 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P16862 UniProtKB Modified residue 171 171 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P16862 UniProtKB Modified residue 803 803 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P16862 UniProtKB Mutagenesis 301 301 . . . Note=Reduces maximal activity of the holoenzyme by 30%25. D->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8132627;Dbxref=PMID:8132627 +P16862 UniProtKB Mutagenesis 348 348 . . . Note=Reduces maximal activity of the holoenzyme by 50%25. Completely abolishes catalytic activity%3B when associated with 'T-309' or 'S-356' in subunit alpha. D->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8132627;Dbxref=PMID:8132627 +P16862 UniProtKB Mutagenesis 439 439 . . . Note=Reduces maximal activity of the holoenzyme by less than 25%25. R->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8132627;Dbxref=PMID:8132627 +P16862 UniProtKB Mutagenesis 481 481 . . . Note=Increases the KM for fructose 6-phosphate 50 fold. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8132627;Dbxref=PMID:8132627 +P16862 UniProtKB Mutagenesis 718 718 . . . Note=Abolishes sensitivity of the holoenzyme to fructose 2%2C6-bisphosphate activation%3B when associated with 'D-724' in subunit alpha. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8663166;Dbxref=PMID:8663166 +P16862 UniProtKB Mutagenesis 722 722 . . . Note=Drastically reduces sensitivity of the holoenzyme to ATP inhibition. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11221662;Dbxref=PMID:11221662 +P16862 UniProtKB Mutagenesis 853 853 . . . Note=Reduces sensitivity of the holoenzyme to fructose 2%2C6-bisphosphate activation%3B when associated with 'S-859' in subunit alpha. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8663166;Dbxref=PMID:8663166 +P16862 UniProtKB Sequence conflict 137 137 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16862 UniProtKB Sequence conflict 880 880 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16862 UniProtKB Beta strand 198 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 211 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 228 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 235 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Turn 244 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 247 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 252 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 258 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 273 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 277 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 294 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 301 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 325 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 329 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 339 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 360 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 384 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 396 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 408 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 421 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 441 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 459 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 474 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 480 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 490 509 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 517 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 526 530 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 531 546 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 550 556 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 561 573 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 581 584 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 588 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 601 615 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 618 622 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 625 632 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 635 637 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 640 643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 646 648 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 661 664 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 666 676 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 679 686 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 687 697 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Turn 698 702 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 704 706 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 712 715 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 730 751 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 752 760 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 767 776 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 779 782 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Turn 784 786 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 790 807 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 815 820 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 821 823 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 829 840 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 845 850 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 852 856 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 862 881 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 884 889 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 890 894 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 901 904 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 907 911 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 913 915 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 918 921 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 922 928 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 932 934 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Beta strand 935 939 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +P16862 UniProtKB Helix 943 952 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O8O +##sequence-region P00560 1 416 +P00560 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +P00560 UniProtKB Chain 2 416 . . . ID=PRO_0000145893;Note=Phosphoglycerate kinase +P00560 UniProtKB Nucleotide binding 371 374 . . . Note=ATP +P00560 UniProtKB Region 24 26 . . . Note=Substrate binding +P00560 UniProtKB Region 63 66 . . . Note=Substrate binding +P00560 UniProtKB Binding site 39 39 . . . Note=Substrate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:6765200,ECO:0000269|PubMed:8672447;Dbxref=PMID:6765200,PMID:8672447 +P00560 UniProtKB Binding site 122 122 . . . Note=Substrate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:6765200,ECO:0000269|PubMed:8672447;Dbxref=PMID:6765200,PMID:8672447 +P00560 UniProtKB Binding site 169 169 . . . Note=Substrate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:6765200,ECO:0000269|PubMed:8672447;Dbxref=PMID:6765200,PMID:8672447 +P00560 UniProtKB Binding site 218 218 . . . Note=ATP +P00560 UniProtKB Binding site 311 311 . . . Note=ATP%3B via carbonyl oxygen +P00560 UniProtKB Binding site 335 335 . . . Note=ATP +P00560 UniProtKB Binding site 342 342 . . . Note=ATP +P00560 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +P00560 UniProtKB Modified residue 93 93 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P00560 UniProtKB Modified residue 110 110 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00560 UniProtKB Modified residue 130 130 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P00560 UniProtKB Modified residue 154 154 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P00560 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00560 UniProtKB Modified residue 203 203 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P00560 UniProtKB Modified residue 241 241 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P00560 UniProtKB Modified residue 298 298 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00560 UniProtKB Modified residue 318 318 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00560 UniProtKB Modified residue 331 331 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P00560 UniProtKB Modified residue 392 392 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P00560 UniProtKB Cross-link 82 82 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00560 UniProtKB Cross-link 197 197 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00560 UniProtKB Cross-link 258 258 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00560 UniProtKB Cross-link 274 274 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00560 UniProtKB Cross-link 302 302 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00560 UniProtKB Mutagenesis 22 22 . . . Note=2-fold reduction of Vmax. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1628654;Dbxref=PMID:1628654 +P00560 UniProtKB Mutagenesis 22 22 . . . Note=7-fold reduction of Vmax. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1628654;Dbxref=PMID:1628654 +P00560 UniProtKB Sequence conflict 185 185 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00560 UniProtKB Sequence conflict 191 191 . . . Note=E->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00560 UniProtKB Helix 9 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QPG +P00560 UniProtKB Beta strand 18 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QPG +P00560 UniProtKB Beta strand 29 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QPG +P00560 UniProtKB Helix 38 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QPG +P00560 UniProtKB Beta strand 56 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QPG +P00560 UniProtKB Beta strand 69 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PGK +P00560 UniProtKB Helix 73 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QPG +P00560 UniProtKB Helix 78 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Beta strand 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Beta strand 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Helix 101 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Beta strand 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PGK +P00560 UniProtKB Beta strand 114 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Helix 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Turn 125 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Beta strand 129 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Beta strand 136 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Helix 142 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Beta strand 157 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Helix 164 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Helix 172 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Beta strand 182 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Helix 186 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Beta strand 204 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Turn 216 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Helix 219 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Beta strand 230 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Helix 236 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Helix 239 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Helix 247 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PGK +P00560 UniProtKB Helix 258 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Beta strand 277 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Beta strand 282 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Beta strand 296 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Turn 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Beta strand 304 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PGK +P00560 UniProtKB Beta strand 310 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Helix 316 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Beta strand 330 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Helix 344 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Helix 348 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Beta strand 366 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Helix 373 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Helix 384 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Beta strand 387 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Helix 395 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +P00560 UniProtKB Helix 407 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FW8 +##sequence-region P33401 1 570 +P33401 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P33401 UniProtKB Chain 2 570 . . . ID=PRO_0000147796;Note=Phosphoglucomutase 1 +P33401 UniProtKB Region 120 121 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P33401 UniProtKB Region 295 296 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P33401 UniProtKB Region 379 381 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P33401 UniProtKB Active site 120 120 . . . Note=Phosphoserine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P33401 UniProtKB Metal binding 120 120 . . . Note=Magnesium%3B via phosphate group;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P33401 UniProtKB Metal binding 291 291 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P33401 UniProtKB Metal binding 293 293 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P33401 UniProtKB Metal binding 295 295 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P33401 UniProtKB Binding site 20 20 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P33401 UniProtKB Binding site 24 24 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P33401 UniProtKB Binding site 133 133 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P33401 UniProtKB Binding site 360 360 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P33401 UniProtKB Binding site 392 392 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P33401 UniProtKB Binding site 523 523 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00949 +P33401 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P33401 UniProtKB Modified residue 120 120 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P0CE93 1 120 +P0CE93 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE93 UniProtKB Chain 21 120 . . . ID=PRO_0000392928;Note=Seripauperin-11 +##sequence-region P40585 1 124 +P40585 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40585 UniProtKB Chain 21 124 . . . ID=PRO_0000033246;Note=Seripauperin-15 +##sequence-region P0CE85 1 124 +P0CE85 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CE85 UniProtKB Chain 21 124 . . . ID=PRO_0000033249;Note=Seripauperin-19 +P0CE85 UniProtKB Sequence conflict 18 18 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CE86 1 164 +P0CE86 UniProtKB Chain 1 164 . . . ID=PRO_0000392931;Note=Seripauperin-21 +P0CE86 UniProtKB Alternative sequence 1 40 . . . ID=VSP_038855;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0CE86 UniProtKB Sequence conflict 24 26 . . . Note=HFF->PSL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32612 1 120 +P32612 UniProtKB Chain 1 120 . . . ID=PRO_0000203779;Note=Seripauperin-2 +P32612 UniProtKB Transmembrane 7 24 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43575 1 122 +P43575 UniProtKB Chain 1 122 . . . ID=PRO_0000203782;Note=Seripauperin-5 +P43575 UniProtKB Transmembrane 7 24 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E770 1 120 +Q3E770 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E770 UniProtKB Chain 21 120 . . . ID=PRO_0000248410;Note=Seripauperin-9 +##sequence-region Q3E833 1 88 +Q3E833 UniProtKB Chain 1 88 . . . ID=PRO_0000245368;Note=EKC/KEOPS complex subunit PCC1 +Q3E833 UniProtKB Beta strand 11 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA +Q3E833 UniProtKB Helix 22 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA +Q3E833 UniProtKB Turn 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA +Q3E833 UniProtKB Beta strand 43 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA +Q3E833 UniProtKB Beta strand 53 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA +Q3E833 UniProtKB Helix 63 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WXA +##sequence-region P16467 1 563 +P16467 UniProtKB Chain 1 563 . . . ID=PRO_0000090771;Note=Pyruvate decarboxylase isozyme 2 +P16467 UniProtKB Region 390 476 . . . Note=Thiamine pyrophosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P16467 UniProtKB Metal binding 444 444 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P16467 UniProtKB Metal binding 471 471 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P16467 UniProtKB Metal binding 473 473 . . . Note=Magnesium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P16467 UniProtKB Binding site 28 28 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P16467 UniProtKB Binding site 115 115 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P16467 UniProtKB Binding site 157 157 . . . Note=Substrate%3B allosteric site;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P16467 UniProtKB Binding site 477 477 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P16467 UniProtKB Sequence conflict 35 35 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16467 UniProtKB Sequence conflict 143 143 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16467 UniProtKB Sequence conflict 207 207 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16467 UniProtKB Sequence conflict 222 222 . . . Note=A->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16467 UniProtKB Sequence conflict 341 341 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16467 UniProtKB Sequence conflict 373 373 . . . Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P10834 1 293 +P10834 UniProtKB Chain 1 293 . . . ID=PRO_0000058319;Note=Protein PET54 +##sequence-region Q05568 1 337 +Q05568 UniProtKB Chain 1 337 . . . ID=PRO_0000056381;Note=Peroxisome biogenesis factor 10 +Q05568 UniProtKB Zinc finger 286 327 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +Q05568 UniProtKB Sequence conflict 183 183 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38244 1 976 +P38244 UniProtKB Chain 1 976 . . . ID=PRO_0000174140;Note=Vacuolar membrane protease +P38244 UniProtKB Topological domain 1 15 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23679341;Dbxref=PMID:23679341 +P38244 UniProtKB Transmembrane 16 36 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38244 UniProtKB Topological domain 37 359 . . . Note=Vacuolar;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23679341;Dbxref=PMID:23679341 +P38244 UniProtKB Transmembrane 360 380 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38244 UniProtKB Topological domain 381 392 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23679341;Dbxref=PMID:23679341 +P38244 UniProtKB Transmembrane 393 412 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38244 UniProtKB Topological domain 413 428 . . . Note=Vacuolar;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23679341;Dbxref=PMID:23679341 +P38244 UniProtKB Transmembrane 429 449 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38244 UniProtKB Topological domain 450 461 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23679341;Dbxref=PMID:23679341 +P38244 UniProtKB Transmembrane 462 482 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38244 UniProtKB Topological domain 483 496 . . . Note=Vacuolar;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23679341;Dbxref=PMID:23679341 +P38244 UniProtKB Transmembrane 497 517 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38244 UniProtKB Topological domain 518 627 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23679341;Dbxref=PMID:23679341 +P38244 UniProtKB Transmembrane 628 648 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38244 UniProtKB Topological domain 649 668 . . . Note=Vacuolar;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23679341;Dbxref=PMID:23679341 +P38244 UniProtKB Transmembrane 669 689 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38244 UniProtKB Topological domain 690 692 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23679341;Dbxref=PMID:23679341 +P38244 UniProtKB Transmembrane 693 713 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38244 UniProtKB Topological domain 714 976 . . . Note=Vacuolar;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23679341;Dbxref=PMID:23679341 +P38244 UniProtKB Active site 200 200 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561 +P38244 UniProtKB Metal binding 156 156 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561 +P38244 UniProtKB Metal binding 168 168 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561 +P38244 UniProtKB Metal binding 168 168 . . . Note=Zinc 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561 +P38244 UniProtKB Metal binding 201 201 . . . Note=Zinc 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561 +P38244 UniProtKB Metal binding 226 226 . . . Note=Zinc 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561 +P38244 UniProtKB Metal binding 300 300 . . . Note=Zinc 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561 +P38244 UniProtKB Site 299 299 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80561 +P38244 UniProtKB Glycosylation 96 96 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P38244 UniProtKB Glycosylation 121 121 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P38244 UniProtKB Glycosylation 189 189 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P38244 UniProtKB Glycosylation 217 217 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P38244 UniProtKB Glycosylation 656 656 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P38244 UniProtKB Glycosylation 768 768 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P38244 UniProtKB Glycosylation 796 796 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P38244 UniProtKB Glycosylation 811 811 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P38244 UniProtKB Glycosylation 866 866 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P38244 UniProtKB Glycosylation 937 937 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +P38244 UniProtKB Sequence conflict 832 832 . . . Note=N->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38244 UniProtKB Sequence conflict 832 832 . . . Note=N->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P42841 1 465 +P42841 UniProtKB Chain 1 465 . . . ID=PRO_0000051122;Note=Polyadenylation factor subunit 2 +P42841 UniProtKB Repeat 133 163 . . . Note=WD 1 +P42841 UniProtKB Repeat 175 205 . . . Note=WD 2 +P42841 UniProtKB Repeat 217 247 . . . Note=WD 3 +P42841 UniProtKB Repeat 259 290 . . . Note=WD 4 +P42841 UniProtKB Repeat 348 378 . . . Note=WD 5 +P42841 UniProtKB Sequence conflict 2 2 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q00618 1 327 +Q00618 UniProtKB Chain 1 327 . . . ID=PRO_0000119756;Note=Geranylgeranyl transferase type-2 subunit alpha +Q00618 UniProtKB Repeat 44 78 . . . Note=PFTA 1 +Q00618 UniProtKB Repeat 84 118 . . . Note=PFTA 2 +Q00618 UniProtKB Repeat 123 157 . . . Note=PFTA 3 +Q00618 UniProtKB Repeat 163 197 . . . Note=PFTA 4 +Q00618 UniProtKB Repeat 207 241 . . . Note=PFTA 5 +##sequence-region P20133 1 325 +P20133 UniProtKB Chain 1 325 . . . ID=PRO_0000119777;Note=Geranylgeranyl transferase type-2 subunit beta +P20133 UniProtKB Repeat 9 50 . . . Note=PFTB 1 +P20133 UniProtKB Repeat 57 99 . . . Note=PFTB 2 +P20133 UniProtKB Repeat 109 150 . . . Note=PFTB 3 +P20133 UniProtKB Repeat 157 198 . . . Note=PFTB 4 +P20133 UniProtKB Repeat 208 249 . . . Note=PFTB 5 +P20133 UniProtKB Repeat 256 298 . . . Note=PFTB 6 +P20133 UniProtKB Region 183 185 . . . Note=Geranylgeranyl diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20133 UniProtKB Region 228 240 . . . Note=Geranylgeranyl diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20133 UniProtKB Metal binding 234 234 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20133 UniProtKB Metal binding 234 234 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20133 UniProtKB Metal binding 236 236 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20133 UniProtKB Metal binding 236 236 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20133 UniProtKB Metal binding 286 286 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20133 UniProtKB Metal binding 286 286 . . . Note=Zinc%3B via tele nitrogen%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20133 UniProtKB Sequence conflict 22 22 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20133 UniProtKB Sequence conflict 22 22 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38744 1 120 +P38744 UniProtKB Chain 1 120 . . . ID=PRO_0000063064;Note=Putative pterin-4-alpha-carbinolamine dehydratase +##sequence-region P39104 1 1066 +P39104 UniProtKB Chain 1 1066 . . . ID=PRO_0000088834;Note=Phosphatidylinositol 4-kinase PIK1 +P39104 UniProtKB Domain 1 133 . . . Note=PIK helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00878 +P39104 UniProtKB Domain 793 1041 . . . Note=PI3K/PI4K;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00269 +P39104 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +P39104 UniProtKB Modified residue 236 236 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P39104 UniProtKB Modified residue 384 384 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39104 UniProtKB Modified residue 394 394 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P39104 UniProtKB Modified residue 396 396 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P39104 UniProtKB Modified residue 592 592 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39104 UniProtKB Helix 126 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JU0 +P39104 UniProtKB Helix 156 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JU0 +##sequence-region P53252 1 339 +P53252 UniProtKB Chain 1 339 . . . ID=PRO_0000058441;Note=Sphingolipid long chain base-responsive protein PIL1 +P53252 UniProtKB Compositional bias 21 25 . . . Note=Poly-Pro +P53252 UniProtKB Compositional bias 279 323 . . . Note=Glu-rich +P53252 UniProtKB Modified residue 14 14 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53252 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53252 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53252 UniProtKB Modified residue 98 98 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53252 UniProtKB Modified residue 163 163 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53252 UniProtKB Modified residue 230 230 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53252 UniProtKB Modified residue 233 233 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:17761666,PMID:18407956,PMID:19779198 +P53252 UniProtKB Modified residue 299 299 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53252 UniProtKB Cross-link 29 29 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q03178 1 341 +Q03178 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9301021;Dbxref=PMID:9301021 +Q03178 UniProtKB Propeptide 19 63 . . . ID=PRO_0000033254;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9301021;Dbxref=PMID:9301021 +Q03178 UniProtKB Chain 64 341 . . . ID=PRO_0000033255;Note=Cell wall mannoprotein PIR1 +Q03178 UniProtKB Repeat 64 82 . . . Note=PIR1/2/3 1;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q03178 UniProtKB Repeat 83 101 . . . Note=PIR1/2/3 2;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q03178 UniProtKB Repeat 102 125 . . . Note=PIR1/2/3 3;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q03178 UniProtKB Repeat 126 144 . . . Note=PIR1/2/3 4;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q03178 UniProtKB Repeat 145 163 . . . Note=PIR1/2/3 5;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q03178 UniProtKB Repeat 164 182 . . . Note=PIR1/2/3 6;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q03178 UniProtKB Repeat 183 201 . . . Note=PIR1/2/3 7;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q03178 UniProtKB Repeat 202 220 . . . Note=PIR1/2/3 8;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q03178 UniProtKB Site 63 64 . . . Note=Cleavage%3B by KEX2 +Q03178 UniProtKB Site 74 74 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03178 UniProtKB Site 93 93 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03178 UniProtKB Site 112 112 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03178 UniProtKB Site 136 136 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03178 UniProtKB Site 155 155 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03178 UniProtKB Site 174 174 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03178 UniProtKB Site 193 193 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03178 UniProtKB Site 212 212 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q03180 1 325 +Q03180 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9301021;Dbxref=PMID:9301021 +Q03180 UniProtKB Propeptide 19 67 . . . ID=PRO_0000033256;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8314797;Dbxref=PMID:8314797 +Q03180 UniProtKB Chain 68 325 . . . ID=PRO_0000033257;Note=Cell wall mannoprotein PIR3 +Q03180 UniProtKB Repeat 68 91 . . . Note=PIR1/2/3 1;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q03180 UniProtKB Repeat 92 109 . . . Note=PIR1/2/3 2;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q03180 UniProtKB Repeat 110 127 . . . Note=PIR1/2/3 3;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q03180 UniProtKB Repeat 128 145 . . . Note=PIR1/2/3 4;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q03180 UniProtKB Repeat 146 163 . . . Note=PIR1/2/3 5;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q03180 UniProtKB Repeat 164 181 . . . Note=PIR1/2/3 6;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q03180 UniProtKB Repeat 182 199 . . . Note=PIR1/2/3 7;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q03180 UniProtKB Repeat 200 217 . . . Note=PIR1/2/3 8;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00149,ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q03180 UniProtKB Site 67 68 . . . Note=Cleavage%3B by KEX2 +Q03180 UniProtKB Site 76 76 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03180 UniProtKB Site 102 102 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03180 UniProtKB Site 120 120 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03180 UniProtKB Site 138 138 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03180 UniProtKB Site 156 156 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03180 UniProtKB Site 174 174 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03180 UniProtKB Site 192 192 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03180 UniProtKB Site 209 209 . . . Note=Covalent attachment to cell wall glycan;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03180 UniProtKB Natural variant 113 113 . . . Note=In strain: RAY-3AD. V->A +Q03180 UniProtKB Natural variant 117 117 . . . Note=In strain: RAY-3AD. T->S +Q03180 UniProtKB Natural variant 144 144 . . . Note=In strain: RAY-3AD. S->STAAAVSQITDGQVQAAKSTAAAASQISDGQVQAAKS +##sequence-region P06197 1 220 +P06197 UniProtKB Chain 1 220 . . . ID=PRO_0000056807;Note=CDP-diacylglycerol--inositol 3-phosphatidyltransferase +P06197 UniProtKB Topological domain 1 20 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P06197 UniProtKB Transmembrane 21 41 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06197 UniProtKB Topological domain 42 45 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P06197 UniProtKB Transmembrane 46 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06197 UniProtKB Topological domain 67 75 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P06197 UniProtKB Transmembrane 76 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06197 UniProtKB Topological domain 97 98 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P06197 UniProtKB Transmembrane 99 119 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06197 UniProtKB Topological domain 120 145 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P06197 UniProtKB Transmembrane 146 166 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06197 UniProtKB Topological domain 167 170 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P06197 UniProtKB Transmembrane 171 191 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06197 UniProtKB Topological domain 192 220 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +##sequence-region Q12236 1 1081 +Q12236 UniProtKB Chain 1 1081 . . . ID=PRO_0000086158;Note=Serine/threonine-protein kinase PKH2 +Q12236 UniProtKB Domain 179 443 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12236 UniProtKB Nucleotide binding 189 191 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530 +Q12236 UniProtKB Nucleotide binding 258 260 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530 +Q12236 UniProtKB Region 210 255 . . . Note=PIF-pocket;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530 +Q12236 UniProtKB Active site 303 303 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q12236 UniProtKB Binding site 208 208 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530 +Q12236 UniProtKB Binding site 264 264 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530 +Q12236 UniProtKB Binding site 307 307 . . . Note=ATP%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530 +Q12236 UniProtKB Binding site 321 321 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15530 +Q12236 UniProtKB Modified residue 138 138 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12236 UniProtKB Modified residue 619 619 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12236 UniProtKB Modified residue 1009 1009 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region Q03880 1 122 +Q03880 UniProtKB Chain 1 122 . . . ID=PRO_0000203297;Note=V-type ATPase assembly factor PKR1 +Q03880 UniProtKB Topological domain 1 20 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03880 UniProtKB Transmembrane 21 41 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03880 UniProtKB Topological domain 42 46 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03880 UniProtKB Transmembrane 47 67 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03880 UniProtKB Topological domain 68 122 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P52960 1 996 +P52960 UniProtKB Chain 1 996 . . . ID=PRO_0000114964;Note=Peroxisome proliferation transcriptional regulator +P52960 UniProtKB DNA binding 25 52 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P52960 UniProtKB Motif 985 993 . . . Note=9aaTAD +##sequence-region Q04383 1 521 +Q04383 UniProtKB Chain 1 521 . . . ID=PRO_0000262747;Note=Protein PLM2 +Q04383 UniProtKB Domain 102 156 . . . Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 +Q04383 UniProtKB Modified residue 281 281 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04383 UniProtKB Modified residue 295 295 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +Q04383 UniProtKB Modified residue 302 302 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04383 UniProtKB Modified residue 384 384 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P38197 1 257 +P38197 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38197 UniProtKB Chain 2 257 . . . ID=PRO_0000163213;Note=Pyridoxal phosphate homeostasis protein +P38197 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38197 UniProtKB Modified residue 49 49 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03225,ECO:0000269|PubMed:12499548;Dbxref=PMID:12499548 +P38197 UniProtKB Sequence conflict 8 8 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38197 UniProtKB Helix 9 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Beta strand 43 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Helix 53 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Beta strand 66 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Helix 72 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Beta strand 87 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Helix 99 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Beta strand 108 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Helix 117 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Beta strand 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1B54 +P38197 UniProtKB Beta strand 137 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Beta strand 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Beta strand 151 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Helix 157 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Beta strand 174 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Helix 197 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Beta strand 218 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Turn 224 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Helix 227 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Beta strand 236 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +P38197 UniProtKB Helix 242 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CT5 +##sequence-region Q07930 1 204 +Q07930 UniProtKB Chain 1 204 . . . ID=PRO_0000058466;Note=Pre-mRNA leakage protein 1 +Q07930 UniProtKB Domain 104 172 . . . Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 +Q07930 UniProtKB Sequence conflict 15 15 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q07930 UniProtKB Helix 38 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MKC +Q07930 UniProtKB Helix 61 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS +Q07930 UniProtKB Helix 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS +Q07930 UniProtKB Beta strand 78 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS +Q07930 UniProtKB Helix 85 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS +Q07930 UniProtKB Beta strand 93 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS +Q07930 UniProtKB Beta strand 102 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS +Q07930 UniProtKB Beta strand 128 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS +Q07930 UniProtKB Beta strand 141 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS +Q07930 UniProtKB Beta strand 151 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS +Q07930 UniProtKB Beta strand 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JKD +Q07930 UniProtKB Beta strand 184 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS +Q07930 UniProtKB Helix 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS +Q07930 UniProtKB Beta strand 197 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ELS +##sequence-region Q12412 1 539 +Q12412 UniProtKB Chain 1 539 . . . ID=PRO_0000191740;Note=Protein PNS1 +Q12412 UniProtKB Topological domain 1 81 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Transmembrane 82 102 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Topological domain 103 129 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Transmembrane 130 150 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Topological domain 151 157 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Transmembrane 158 178 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Topological domain 179 182 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Transmembrane 183 203 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Topological domain 204 226 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Transmembrane 227 247 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Topological domain 248 274 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Transmembrane 275 295 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Topological domain 296 332 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Transmembrane 333 353 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Topological domain 354 371 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Transmembrane 372 392 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Topological domain 393 436 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Transmembrane 437 457 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Topological domain 458 473 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Transmembrane 474 494 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Topological domain 495 539 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Glycosylation 259 259 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12412 UniProtKB Sequence conflict 181 181 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07951 1 179 +Q07951 UniProtKB Chain 1 179 . . . ID=PRO_0000247202;Note=Proteasome chaperone 3 +Q07951 UniProtKB Beta strand 3 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +Q07951 UniProtKB Beta strand 26 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +Q07951 UniProtKB Beta strand 38 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +Q07951 UniProtKB Beta strand 50 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +Q07951 UniProtKB Helix 84 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +Q07951 UniProtKB Beta strand 95 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +Q07951 UniProtKB Helix 109 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +Q07951 UniProtKB Beta strand 140 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +Q07951 UniProtKB Helix 147 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +Q07951 UniProtKB Helix 162 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +##sequence-region P25576 1 258 +P25576 UniProtKB Chain 1 258 . . . ID=PRO_0000202549;Note=Nicotinamide mononucleotide adenylyltransferase +P25576 UniProtKB Nucleotide binding 34 36 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66 +P25576 UniProtKB Nucleotide binding 138 140 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66 +P25576 UniProtKB Nucleotide binding 224 227 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66 +P25576 UniProtKB Binding site 43 43 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96T66 +##sequence-region Q04049 1 632 +Q04049 UniProtKB Chain 1 632 . . . ID=PRO_0000268698;Note=DNA polymerase eta +Q04049 UniProtKB Domain 26 309 . . . Note=UmuC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00216 +Q04049 UniProtKB Region 625 632 . . . Note=POL30-binding +Q04049 UniProtKB Metal binding 30 30 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00216 +Q04049 UniProtKB Metal binding 155 155 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00216 +Q04049 UniProtKB Mutagenesis 30 30 . . . Note=Abolishes DNA polymerase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238937;Dbxref=PMID:11238937 +Q04049 UniProtKB Mutagenesis 34 34 . . . Note=Alters translesion activity. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15024063;Dbxref=PMID:15024063 +Q04049 UniProtKB Mutagenesis 39 39 . . . Note=Abolishes DNA polymerase activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238937;Dbxref=PMID:11238937 +Q04049 UniProtKB Mutagenesis 64 64 . . . Note=Decreases efficiency of nucleotide incorporation. Y->F%2CA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665597;Dbxref=PMID:12665597 +Q04049 UniProtKB Mutagenesis 67 67 . . . Note=Decreases efficiency of nucleotide incorporation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665597;Dbxref=PMID:12665597 +Q04049 UniProtKB Mutagenesis 155 155 . . . Note=Abolishes DNA polymerase activity and increases UV-induced mutations. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238937;Dbxref=PMID:11238937 +Q04049 UniProtKB Mutagenesis 156 156 . . . Note=Decreases efficiency of nucleotide incorporation. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238937;Dbxref=PMID:11238937 +Q04049 UniProtKB Mutagenesis 279 279 . . . Note=Decreases efficiency of nucleotide incorporation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665597;Dbxref=PMID:12665597 +Q04049 UniProtKB Mutagenesis 627 627 . . . Note=Abolishes POL30-binding%3B when associated with A-628. F->A +Q04049 UniProtKB Mutagenesis 628 628 . . . Note=Abolishes POL30-binding%3B when associated with A-627. F->A +Q04049 UniProtKB Beta strand 1 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 6 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Turn 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 18 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R8K +Q04049 UniProtKB Beta strand 26 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 34 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 51 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 58 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 64 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Turn 68 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 77 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 88 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 93 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 100 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OHB +Q04049 UniProtKB Helix 115 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OHA +Q04049 UniProtKB Beta strand 123 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 129 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 149 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 156 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 162 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 183 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 188 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 203 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 210 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 219 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 233 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 260 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 268 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Turn 276 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JIH +Q04049 UniProtKB Beta strand 280 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 288 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 291 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 297 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 302 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 306 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JIH +Q04049 UniProtKB Helix 311 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 324 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 327 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 339 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 352 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WTF +Q04049 UniProtKB Turn 357 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OHA +Q04049 UniProtKB Helix 364 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFH +Q04049 UniProtKB Helix 367 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Turn 378 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 395 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Turn 403 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 409 434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 436 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 454 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 466 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Helix 469 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Turn 488 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +Q04049 UniProtKB Beta strand 497 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MFI +##sequence-region Q12445 1 299 +Q12445 UniProtKB Chain 1 299 . . . ID=PRO_0000204911;Note=Nucleoporin POM34 +Q12445 UniProtKB Transmembrane 64 84 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12445 UniProtKB Transmembrane 133 153 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12445 UniProtKB Modified residue 270 270 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12445 UniProtKB Modified residue 273 273 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12445 UniProtKB Modified residue 292 292 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12445 UniProtKB Modified residue 294 294 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:18407956,PMID:19779198 +Q12445 UniProtKB Sequence conflict 191 191 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P28005 1 173 +P28005 UniProtKB Chain 1 173 . . . ID=PRO_0000140015;Note=Ribonuclease P/MRP protein subunit POP5 +##sequence-region P23287 1 553 +P23287 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P23287 UniProtKB Chain 2 553 . . . ID=PRO_0000058836;Note=Serine/threonine-protein phosphatase 2B catalytic subunit A1 +P23287 UniProtKB Active site 180 180 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23287 UniProtKB Metal binding 119 119 . . . Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23287 UniProtKB Metal binding 121 121 . . . Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23287 UniProtKB Metal binding 147 147 . . . Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23287 UniProtKB Metal binding 147 147 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23287 UniProtKB Metal binding 179 179 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23287 UniProtKB Metal binding 228 228 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23287 UniProtKB Metal binding 317 317 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23287 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P23287 UniProtKB Natural variant 45 46 . . . Note=In strain: S288c / GRF88. PI->SY +P23287 UniProtKB Helix 455 458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LHI +P23287 UniProtKB Helix 460 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LHI +##sequence-region P39966 1 464 +P39966 UniProtKB Chain 1 464 . . . ID=PRO_0000057775;Note=Protein phosphatase 2C homolog 2 +P39966 UniProtKB Domain 23 292 . . . Note=PPM-type phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01082 +P39966 UniProtKB Metal binding 62 62 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39966 UniProtKB Metal binding 62 62 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39966 UniProtKB Metal binding 63 63 . . . Note=Manganese 1%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39966 UniProtKB Metal binding 234 234 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39966 UniProtKB Metal binding 283 283 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39966 UniProtKB Modified residue 376 376 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39966 UniProtKB Modified residue 380 380 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P53691 1 371 +P53691 UniProtKB Chain 1 371 . . . ID=PRO_0000064173;Note=Peptidyl-prolyl cis-trans isomerase CPR6 +P53691 UniProtKB Domain 7 174 . . . Note=PPIase cyclophilin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00156 +P53691 UniProtKB Repeat 219 252 . . . Note=TPR 1 +P53691 UniProtKB Repeat 270 303 . . . Note=TPR 2 +P53691 UniProtKB Repeat 308 341 . . . Note=TPR 3 +P53691 UniProtKB Sequence conflict 12 12 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12326 1 303 +Q12326 UniProtKB Chain 1 303 . . . ID=PRO_0000179841;Note=Phosphoglycerate mutase 3 +Q12326 UniProtKB Region 13 20 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +Q12326 UniProtKB Region 26 27 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +Q12326 UniProtKB Region 120 123 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +Q12326 UniProtKB Region 147 148 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +Q12326 UniProtKB Region 236 237 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +Q12326 UniProtKB Active site 14 14 . . . Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +Q12326 UniProtKB Active site 120 120 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +Q12326 UniProtKB Binding site 70 70 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +Q12326 UniProtKB Binding site 131 131 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +Q12326 UniProtKB Site 235 235 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +##sequence-region Q02890 1 363 +Q02890 UniProtKB Chain 1 363 . . . ID=PRO_0000248996;Note=Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase +Q02890 UniProtKB Active site 191 191 . . . Note=Nucleophile +Q02890 UniProtKB Active site 218 218 . . . . +Q02890 UniProtKB Active site 235 235 . . . . +Q02890 UniProtKB Metal binding 129 129 . . . Note=Zinc +Q02890 UniProtKB Metal binding 132 132 . . . Note=Zinc +Q02890 UniProtKB Metal binding 165 165 . . . Note=Zinc +Q02890 UniProtKB Metal binding 168 168 . . . Note=Zinc +Q02890 UniProtKB Binding site 238 238 . . . Note=Substrate +Q02890 UniProtKB Mutagenesis 123 123 . . . Note=No effect. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 129 129 . . . Note=Abolishes enzyme activity. C->A%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 132 132 . . . Note=Abolishes enzyme activity. C->A%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 165 165 . . . Note=Abolishes enzyme activity. C->A%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 168 168 . . . Note=Abolishes enzyme activity. C->A%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 174 174 . . . Note=No effect. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 177 177 . . . Note=No effect. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 187 187 . . . Note=No effect. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 189 189 . . . Note=No effect. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 191 191 . . . Note=Abolishes enzyme activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 194 194 . . . Note=No effect. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 198 198 . . . Note=No effect. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 199 199 . . . Note=No effect. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 203 203 . . . Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 206 206 . . . Note=No effect. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 210 210 . . . Note=Abolishes enzyme activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 212 212 . . . Note=No effect. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 218 218 . . . Note=Abolishes enzyme activity. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10831608,ECO:0000269|PubMed:11812789;Dbxref=PMID:10831608,PMID:11812789 +Q02890 UniProtKB Mutagenesis 218 218 . . . Note=In png1-1%3B abolishes enzyme activity. H->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10831608,ECO:0000269|PubMed:11812789;Dbxref=PMID:10831608,PMID:11812789 +Q02890 UniProtKB Mutagenesis 220 220 . . . Note=Abolishes enzyme activity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 220 220 . . . Note=No effect. W->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 222 222 . . . Note=Abolishes enzyme activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 224 224 . . . Note=No effect. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 230 230 . . . Note=No effect. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 231 231 . . . Note=Abolishes enzyme activity. W->A +Q02890 UniProtKB Mutagenesis 231 231 . . . Note=No effect. W->F +Q02890 UniProtKB Mutagenesis 234 234 . . . Note=No effect. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 235 235 . . . Note=Abolishes enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 242 242 . . . Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 251 251 . . . Note=No effect. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 253 253 . . . Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 257 257 . . . Note=Abolishes enzyme activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 261 261 . . . Note=Abolishes enzyme activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 264 264 . . . Note=No effect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 266 266 . . . Note=No effect. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 268 268 . . . Note=Abolishes enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 273 273 . . . Note=Abolishes enzyme activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 281 281 . . . Note=No effect. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 347 347 . . . Note=No effect. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 354 354 . . . Note=No effect. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Mutagenesis 358 358 . . . Note=No effect. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812789;Dbxref=PMID:11812789 +Q02890 UniProtKB Helix 13 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Beta strand 31 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3W +Q02890 UniProtKB Helix 36 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Helix 50 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Helix 69 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Helix 81 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Beta strand 97 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Helix 103 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Beta strand 130 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Beta strand 138 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Helix 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Beta strand 154 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Turn 166 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Beta strand 171 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Helix 180 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Helix 191 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Turn 204 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Beta strand 209 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Turn 215 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Beta strand 218 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Turn 226 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Beta strand 230 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Turn 236 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Beta strand 240 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Helix 246 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Beta strand 258 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Beta strand 265 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Helix 270 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Beta strand 275 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Helix 286 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Helix 306 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X3Z +Q02890 UniProtKB Beta strand 325 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ESW +##sequence-region P53833 1 195 +P53833 UniProtKB Chain 1 195 . . . ID=PRO_0000058516;Note=Ribonucleases P/MRP protein subunit POP3 +##sequence-region P38208 1 133 +P38208 UniProtKB Chain 1 133 . . . ID=PRO_0000058521;Note=Ribonucleases P/MRP protein subunit POP8 +##sequence-region P20604 1 311 +P20604 UniProtKB Chain 1 311 . . . ID=PRO_0000058881;Note=Serine/threonine-protein phosphatase PP1-1 +P20604 UniProtKB Active site 115 115 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20604 UniProtKB Metal binding 53 53 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20604 UniProtKB Metal binding 55 55 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20604 UniProtKB Metal binding 82 82 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20604 UniProtKB Metal binding 82 82 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20604 UniProtKB Metal binding 114 114 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20604 UniProtKB Metal binding 164 164 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20604 UniProtKB Metal binding 238 238 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20604 UniProtKB Mutagenesis 35 35 . . . Note=Reduced interaction with TAP42. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14551259;Dbxref=PMID:14551259 +P20604 UniProtKB Mutagenesis 37 38 . . . Note=Nearly no interaction with TAP42. EE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14551259;Dbxref=PMID:14551259 +P20604 UniProtKB Mutagenesis 38 38 . . . Note=Normal interaction with TAP42. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14551259;Dbxref=PMID:14551259 +P20604 UniProtKB Mutagenesis 40 40 . . . Note=Normal interaction with TAP42. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14551259;Dbxref=PMID:14551259 +##sequence-region P32345 1 308 +P32345 UniProtKB Chain 1 308 . . . ID=PRO_0000058875;Note=Serine/threonine-protein phosphatase 4 catalytic subunit +P32345 UniProtKB Active site 112 112 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32345 UniProtKB Metal binding 51 51 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32345 UniProtKB Metal binding 53 53 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32345 UniProtKB Metal binding 79 79 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32345 UniProtKB Metal binding 79 79 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32345 UniProtKB Metal binding 111 111 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32345 UniProtKB Metal binding 161 161 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32345 UniProtKB Metal binding 235 235 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32345 UniProtKB Sequence conflict 245 245 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P11491 1 566 +P11491 UniProtKB Topological domain 1 33 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2676517;Dbxref=PMID:2676517 +P11491 UniProtKB Transmembrane 34 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P11491 UniProtKB Active site 123 123 . . . Note=Phosphoserine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10042 +P11491 UniProtKB Metal binding 75 75 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11491 UniProtKB Metal binding 75 75 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11491 UniProtKB Metal binding 174 174 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11491 UniProtKB Metal binding 176 176 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11491 UniProtKB Metal binding 325 325 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11491 UniProtKB Metal binding 330 330 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11491 UniProtKB Metal binding 334 334 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11491 UniProtKB Metal binding 373 373 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11491 UniProtKB Metal binding 374 374 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11491 UniProtKB Metal binding 484 484 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P11491 UniProtKB Modified residue 123 123 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P11491 UniProtKB Glycosylation 268 268 . . . Note=N-linked (GlcNAc...) asparagine +P11491 UniProtKB Glycosylation 401 401 . . . Note=N-linked (GlcNAc...) asparagine +P11491 UniProtKB Sequence conflict 5 5 . . . Note=T->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11491 UniProtKB Sequence conflict 55 55 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11491 UniProtKB Sequence conflict 59 59 . . . Note=L->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11491 UniProtKB Sequence conflict 132 132 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11491 UniProtKB Sequence conflict 271 271 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11491 UniProtKB Sequence conflict 328 328 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11491 UniProtKB Sequence conflict 447 447 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04004 1 230 +Q04004 UniProtKB Chain 1 230 . . . ID=PRO_0000120172;Note=Phosducin-like protein 1 +Q04004 UniProtKB Region 81 230 . . . Note=Thioredoxin fold;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04004 UniProtKB Coiled coil 25 79 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04004 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P32634 1 1753 +P32634 UniProtKB Chain 1 1753 . . . ID=PRO_0000119141;Note=Negative regulator of sporulation PMD1 +P32634 UniProtKB Repeat 143 198 . . . Note=Kelch 1 +P32634 UniProtKB Repeat 206 253 . . . Note=Kelch 2 +P32634 UniProtKB Modified residue 298 298 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32634 UniProtKB Modified residue 838 838 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32634 UniProtKB Modified residue 1289 1289 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32634 UniProtKB Modified residue 1307 1307 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32634 UniProtKB Modified residue 1356 1356 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P32634 UniProtKB Modified residue 1664 1664 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198 +##sequence-region P35999 1 772 +P35999 UniProtKB Transit peptide 1 37 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35999 UniProtKB Chain 38 772 . . . ID=PRO_0000028583;Note=Mitochondrial intermediate peptidase +P35999 UniProtKB Active site 559 559 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P35999 UniProtKB Metal binding 558 558 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P35999 UniProtKB Metal binding 562 562 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P35999 UniProtKB Metal binding 587 587 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35999 UniProtKB Mutagenesis 131 131 . . . Note=Affects protein stability%2C but has no effect on peptidase activity. C->S%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696 +P35999 UniProtKB Mutagenesis 557 557 . . . Note=Affects protein stability. F->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696 +P35999 UniProtKB Mutagenesis 558 558 . . . Note=Abolishes proteolytic activity. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696 +P35999 UniProtKB Mutagenesis 559 559 . . . Note=Abolishes proteolytic activity. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696 +P35999 UniProtKB Mutagenesis 561 561 . . . Note=Affects protein stability. G->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696 +P35999 UniProtKB Mutagenesis 562 562 . . . Note=Abolishes proteolytic activity. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696 +P35999 UniProtKB Mutagenesis 565 565 . . . Note=Temperature sensitive%3B abolishes proteolytic activity for RIP1%2C but not for COX4. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696 +P35999 UniProtKB Mutagenesis 578 578 . . . Note=Temperature sensitive%3B abolishes proteolytic activity for RIP1%2C but not for COX4. G->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696 +P35999 UniProtKB Mutagenesis 581 581 . . . Note=Affects protein stability%2C but has no effect on peptidase activity. C->S%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696 +P35999 UniProtKB Mutagenesis 584 584 . . . Note=No effect. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696 +P35999 UniProtKB Mutagenesis 587 587 . . . Note=Abolishes proteolytic activity. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696 +P35999 UniProtKB Mutagenesis 589 589 . . . Note=No effect. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696 +P35999 UniProtKB Mutagenesis 590 590 . . . Note=Affects protein stability. S->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696 +P35999 UniProtKB Mutagenesis 594 594 . . . Note=No effect. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831696;Dbxref=PMID:8831696 +P35999 UniProtKB Sequence conflict 343 350 . . . Note=MAKNPKDV->WQDRRC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35999 UniProtKB Sequence conflict 694 702 . . . Note=YGATYYSYL->SGQLITATY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32903 1 40 +P32903 UniProtKB Propeptide 1 2 . . . ID=PRO_0000022071;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1532582;Dbxref=PMID:1532582 +P32903 UniProtKB Chain 3 40 . . . ID=PRO_0000022072;Note=Plasma membrane ATPase proteolipid 1 +P32903 UniProtKB Transmembrane 3 26 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32903 UniProtKB Topological domain 27 40 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q06644 1 662 +Q06644 UniProtKB Chain 1 662 . . . ID=PRO_0000121497;Note=Probable dolichyl-phosphate-mannose--protein mannosyltransferase 7 +Q06644 UniProtKB Topological domain 1 26 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06644 UniProtKB Transmembrane 27 47 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06644 UniProtKB Topological domain 48 159 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06644 UniProtKB Transmembrane 160 180 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06644 UniProtKB Topological domain 181 195 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06644 UniProtKB Transmembrane 196 216 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06644 UniProtKB Topological domain 217 235 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06644 UniProtKB Transmembrane 236 256 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06644 UniProtKB Topological domain 257 482 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06644 UniProtKB Transmembrane 483 503 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06644 UniProtKB Topological domain 504 565 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06644 UniProtKB Transmembrane 566 586 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06644 UniProtKB Topological domain 587 617 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06644 UniProtKB Transmembrane 618 638 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06644 UniProtKB Topological domain 639 662 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06644 UniProtKB Domain 289 344 . . . Note=MIR 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +Q06644 UniProtKB Domain 359 418 . . . Note=MIR 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +Q06644 UniProtKB Domain 432 488 . . . Note=MIR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +Q06644 UniProtKB Glycosylation 347 347 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53184 1 216 +P53184 UniProtKB Chain 1 216 . . . ID=PRO_0000206558;Note=Nicotinamidase +P53184 UniProtKB Active site 8 8 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53184 UniProtKB Active site 122 122 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53184 UniProtKB Active site 167 167 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53184 UniProtKB Metal binding 51 51 . . . Note=Zinc;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2H0R,ECO:0000269|PubMed:17382284;Dbxref=PMID:17382284 +P53184 UniProtKB Metal binding 53 53 . . . Note=Zinc;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2H0R,ECO:0000269|PubMed:17382284;Dbxref=PMID:17382284 +P53184 UniProtKB Metal binding 94 94 . . . Note=Zinc;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:2H0R,ECO:0000269|PubMed:17382284;Dbxref=PMID:17382284 +P53184 UniProtKB Beta strand 2 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Helix 11 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Helix 25 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Helix 29 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Helix 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Beta strand 43 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Helix 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Beta strand 72 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Beta strand 85 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Helix 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Helix 106 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Beta strand 118 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Beta strand 132 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Helix 145 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Beta strand 156 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Turn 164 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Helix 167 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Beta strand 181 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Helix 196 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +P53184 UniProtKB Beta strand 212 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V8E +##sequence-region Q99216 1 274 +Q99216 UniProtKB Chain 1 274 . . . ID=PRO_0000270553;Note=Pre-rRNA-processing protein PNO1 +Q99216 UniProtKB Domain 195 247 . . . Note=KH +Q99216 UniProtKB Compositional bias 35 41 . . . Note=Poly-Asp +Q99216 UniProtKB Modified residue 47 47 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q99216 UniProtKB Modified residue 51 51 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q99216 UniProtKB Mutagenesis 203 203 . . . Note=Temperature-sensitive. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12502737;Dbxref=PMID:12502737 +Q99216 UniProtKB Mutagenesis 235 235 . . . Note=Accumulation of aberrant 22S and 23S rRNA intermediates. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12736301;Dbxref=PMID:12736301 +##sequence-region P19881 1 312 +P19881 UniProtKB Chain 1 312 . . . ID=PRO_0000058481;Note=4-nitrophenylphosphatase +P19881 UniProtKB Sequence conflict 50 50 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19881 UniProtKB Sequence conflict 96 96 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19881 UniProtKB Sequence conflict 284 284 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P19881 UniProtKB Sequence conflict 306 306 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36040 1 267 +P36040 UniProtKB Chain 1 267 . . . ID=PRO_0000203132;Note=Proteasome assembly chaperone 2 +P36040 UniProtKB Beta strand 3 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +P36040 UniProtKB Helix 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +P36040 UniProtKB Helix 14 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +P36040 UniProtKB Beta strand 28 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +P36040 UniProtKB Beta strand 51 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +P36040 UniProtKB Beta strand 67 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +P36040 UniProtKB Turn 76 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +P36040 UniProtKB Beta strand 80 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +P36040 UniProtKB Helix 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +P36040 UniProtKB Helix 95 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +P36040 UniProtKB Helix 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +P36040 UniProtKB Beta strand 113 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +P36040 UniProtKB Helix 183 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +P36040 UniProtKB Helix 220 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +P36040 UniProtKB Helix 247 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +P36040 UniProtKB Helix 258 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +##sequence-region Q12164 1 279 +Q12164 UniProtKB Chain 1 279 . . . ID=PRO_0000247116;Note=Pore membrane protein of 33 kDa +Q12164 UniProtKB Topological domain 1 31 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12164 UniProtKB Transmembrane 32 52 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12164 UniProtKB Topological domain 53 56 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12164 UniProtKB Transmembrane 57 79 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12164 UniProtKB Topological domain 80 124 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12164 UniProtKB Transmembrane 125 145 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12164 UniProtKB Topological domain 146 180 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12164 UniProtKB Transmembrane 181 201 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12164 UniProtKB Topological domain 202 203 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12164 UniProtKB Transmembrane 204 221 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12164 UniProtKB Topological domain 222 279 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32838 1 368 +P32838 UniProtKB Chain 1 368 . . . ID=PRO_0000058876;Note=Serine/threonine-protein phosphatase PP2A-like PPG1 +P32838 UniProtKB Active site 111 111 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32838 UniProtKB Metal binding 50 50 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32838 UniProtKB Metal binding 52 52 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32838 UniProtKB Metal binding 78 78 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32838 UniProtKB Metal binding 78 78 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32838 UniProtKB Metal binding 110 110 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32838 UniProtKB Metal binding 161 161 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32838 UniProtKB Metal binding 247 247 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32838 UniProtKB Sequence conflict 126 126 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32838 UniProtKB Sequence conflict 154 154 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38693 1 467 +P38693 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38693 UniProtKB Chain 18 467 . . . ID=PRO_0000023957;Note=Acid phosphatase PHO12 +P38693 UniProtKB Active site 75 75 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38693 UniProtKB Active site 338 338 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38693 UniProtKB Glycosylation 97 97 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38693 UniProtKB Glycosylation 162 162 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38693 UniProtKB Glycosylation 192 192 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38693 UniProtKB Glycosylation 250 250 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38693 UniProtKB Glycosylation 315 315 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38693 UniProtKB Glycosylation 356 356 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38693 UniProtKB Glycosylation 390 390 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38693 UniProtKB Glycosylation 439 439 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38693 UniProtKB Glycosylation 445 445 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38693 UniProtKB Glycosylation 461 461 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08108 1 686 +Q08108 UniProtKB Signal peptide 1 26 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08108 UniProtKB Chain 27 659 . . . ID=PRO_0000024648;Note=Lysophospholipase 3 +Q08108 UniProtKB Propeptide 660 686 . . . ID=PRO_0000372444;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08108 UniProtKB Domain 39 592 . . . Note=PLA2c;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00555 +Q08108 UniProtKB Compositional bias 627 643 . . . Note=Poly-Ser +Q08108 UniProtKB Lipidation 659 659 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08108 UniProtKB Glycosylation 56 56 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08108 UniProtKB Glycosylation 82 82 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08108 UniProtKB Glycosylation 129 129 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08108 UniProtKB Glycosylation 166 166 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08108 UniProtKB Glycosylation 221 221 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08108 UniProtKB Glycosylation 283 283 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08108 UniProtKB Glycosylation 313 313 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08108 UniProtKB Glycosylation 351 351 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08108 UniProtKB Glycosylation 495 495 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08108 UniProtKB Glycosylation 519 519 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08108 UniProtKB Glycosylation 547 547 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08108 UniProtKB Glycosylation 571 571 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08108 UniProtKB Glycosylation 588 588 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08108 UniProtKB Glycosylation 614 614 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P05375 1 206 +P05375 UniProtKB Chain 1 206 . . . ID=PRO_0000193924;Note=Phosphatidyl-N-methylethanolamine N-methyltransferase +P05375 UniProtKB Topological domain 1 20 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216 +P05375 UniProtKB Intramembrane 21 41 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216 +P05375 UniProtKB Topological domain 42 53 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216 +P05375 UniProtKB Transmembrane 54 74 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216 +P05375 UniProtKB Topological domain 75 101 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216 +P05375 UniProtKB Transmembrane 102 122 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216 +P05375 UniProtKB Topological domain 123 165 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216 +P05375 UniProtKB Transmembrane 166 186 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216 +P05375 UniProtKB Topological domain 187 206 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216 +P05375 UniProtKB Region 106 108 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216 +P05375 UniProtKB Region 188 189 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03216 +##sequence-region P41812 1 875 +P41812 UniProtKB Chain 1 875 . . . ID=PRO_0000058514;Note=Ribonucleases P/MRP protein subunit POP1 +P41812 UniProtKB Modified residue 524 524 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q06494 1 345 +Q06494 UniProtKB Chain 1 345 . . . ID=PRO_0000257816;Note=Putative pyridoxal reductase +Q06494 UniProtKB Active site 60 60 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P00950 1 247 +P00950 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.8 +P00950 UniProtKB Chain 2 247 . . . ID=PRO_0000179839;Note=Phosphoglycerate mutase 1 +P00950 UniProtKB Region 8 15 . . . Note=Substrate binding;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10369755,ECO:0000269|PubMed:10531478,ECO:0000269|PubMed:6115412;Dbxref=PMID:10369755,PMID:10531478,PMID:6115412 +P00950 UniProtKB Region 21 22 . . . Note=Substrate binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10369755,ECO:0000269|PubMed:10531478;Dbxref=PMID:10369755,PMID:10531478 +P00950 UniProtKB Region 87 90 . . . Note=Substrate binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10369755,ECO:0000269|PubMed:6115412;Dbxref=PMID:10369755,PMID:6115412 +P00950 UniProtKB Region 114 115 . . . Note=Substrate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10369755;Dbxref=PMID:10369755 +P00950 UniProtKB Region 183 184 . . . Note=Substrate binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10369755,ECO:0000269|PubMed:6115412;Dbxref=PMID:10369755,PMID:6115412 +P00950 UniProtKB Compositional bias 233 242 . . . Note=Ala-rich +P00950 UniProtKB Active site 9 9 . . . Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10064712,ECO:0000269|PubMed:10531478,ECO:0000269|PubMed:6115412,ECO:0000269|PubMed:9512715;Dbxref=PMID:10064712,PMID:10531478,PMID:6115412,PMID:9512715 +P00950 UniProtKB Active site 87 87 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10064712;Dbxref=PMID:10064712 +P00950 UniProtKB Binding site 60 60 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10531478;Dbxref=PMID:10531478 +P00950 UniProtKB Binding site 98 98 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10369755;Dbxref=PMID:10369755 +P00950 UniProtKB Site 182 182 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10064712;Dbxref=PMID:10064712 +P00950 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P00950 UniProtKB Modified residue 49 49 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00950 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P00950 UniProtKB Modified residue 127 127 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P00950 UniProtKB Modified residue 128 128 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00950 UniProtKB Modified residue 185 185 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P00950 UniProtKB Modified residue 197 197 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P00950 UniProtKB Cross-link 31 31 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00950 UniProtKB Cross-link 57 57 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00950 UniProtKB Cross-link 71 71 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00950 UniProtKB Cross-link 139 139 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00950 UniProtKB Cross-link 175 175 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00950 UniProtKB Cross-link 191 191 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P00950 UniProtKB Mutagenesis 169 169 . . . Note=Causes dissociation of the homotetramer to dimers at low concentrations. K->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8240286;Dbxref=PMID:8240286 +P00950 UniProtKB Mutagenesis 182 182 . . . Note=Reduces kcat of the mutase reaction 10000-fold. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1386023;Dbxref=PMID:1386023 +P00950 UniProtKB Beta strand 3 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Helix 13 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Helix 30 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Beta strand 51 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Helix 59 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Beta strand 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Helix 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Helix 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Helix 98 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Beta strand 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PGM +P00950 UniProtKB Beta strand 126 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PGM +P00950 UniProtKB Helix 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Helix 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Helix 152 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Helix 167 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Beta strand 177 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Helix 183 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Turn 198 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Helix 201 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Beta strand 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PGM +P00950 UniProtKB Beta strand 212 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Turn 218 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PGM +P00950 UniProtKB Beta strand 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Beta strand 227 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +P00950 UniProtKB Turn 231 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHF +##sequence-region P33775 1 817 +P33775 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P33775 UniProtKB Chain 2 817 . . . ID=PRO_0000121491;Note=Dolichyl-phosphate-mannose--protein mannosyltransferase 1 +P33775 UniProtKB Topological domain 2 50 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156 +P33775 UniProtKB Transmembrane 51 70 . . . Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156 +P33775 UniProtKB Topological domain 71 135 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156 +P33775 UniProtKB Transmembrane 136 154 . . . Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156 +P33775 UniProtKB Topological domain 155 179 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156 +P33775 UniProtKB Transmembrane 180 200 . . . Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156 +P33775 UniProtKB Topological domain 201 234 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156 +P33775 UniProtKB Transmembrane 235 259 . . . Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156 +P33775 UniProtKB Topological domain 260 273 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156 +P33775 UniProtKB Transmembrane 274 291 . . . Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156 +P33775 UniProtKB Topological domain 292 584 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156 +P33775 UniProtKB Transmembrane 585 605 . . . Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156 +P33775 UniProtKB Topological domain 606 685 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156 +P33775 UniProtKB Transmembrane 686 710 . . . Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156 +P33775 UniProtKB Topological domain 711 817 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085156;Dbxref=PMID:10085156 +P33775 UniProtKB Domain 324 378 . . . Note=MIR 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +P33775 UniProtKB Domain 388 448 . . . Note=MIR 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +P33775 UniProtKB Domain 459 514 . . . Note=MIR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +P33775 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P33775 UniProtKB Glycosylation 390 390 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33775 UniProtKB Glycosylation 513 513 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33775 UniProtKB Glycosylation 743 743 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33775 UniProtKB Mutagenesis 64 64 . . . Note=Reduces mannosyltransferase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10764776;Dbxref=PMID:10764776 +P33775 UniProtKB Mutagenesis 77 78 . . . Note=Impairs mannosyltransferase activity. DE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21956107;Dbxref=PMID:21956107 +P33775 UniProtKB Mutagenesis 78 78 . . . Note=Decreases substrate-binding and reduces mannosyltransferase activity. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10764776,ECO:0000269|PubMed:21956107;Dbxref=PMID:10764776,PMID:21956107 +P33775 UniProtKB Mutagenesis 88 88 . . . Note=Moderately decreases complex formation with PMT2. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21956107;Dbxref=PMID:21956107 +P33775 UniProtKB Mutagenesis 100 100 . . . Note=Moderately decreases complex formation with PMT2. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21956107;Dbxref=PMID:21956107 +P33775 UniProtKB Mutagenesis 138 138 . . . Note=Impairs complex formation with PMT2. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10764776;Dbxref=PMID:10764776 +P33775 UniProtKB Mutagenesis 408 408 . . . Note=Reduces mannosyltransferase activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10764776;Dbxref=PMID:10764776 +##sequence-region P31382 1 759 +P31382 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P31382 UniProtKB Chain 2 759 . . . ID=PRO_0000121492;Note=Dolichyl-phosphate-mannose--protein mannosyltransferase 2 +P31382 UniProtKB Topological domain 2 64 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Transmembrane 65 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Topological domain 86 167 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Transmembrane 168 188 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Topological domain 189 198 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Transmembrane 199 219 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Topological domain 220 251 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Transmembrane 252 272 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Topological domain 273 289 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Transmembrane 290 310 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Topological domain 311 609 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Transmembrane 610 630 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Topological domain 631 647 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Transmembrane 648 668 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Topological domain 669 676 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Transmembrane 677 697 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Topological domain 698 710 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Transmembrane 711 731 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Topological domain 732 759 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Domain 339 394 . . . Note=MIR 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +P31382 UniProtKB Domain 407 463 . . . Note=MIR 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +P31382 UniProtKB Domain 471 529 . . . Note=MIR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +P31382 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P31382 UniProtKB Modified residue 32 32 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P31382 UniProtKB Modified residue 38 38 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P31382 UniProtKB Modified residue 39 39 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P31382 UniProtKB Glycosylation 131 131 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Glycosylation 155 155 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31382 UniProtKB Glycosylation 403 403 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P46971 1 762 +P46971 UniProtKB Chain 1 762 . . . ID=PRO_0000121494;Note=Dolichyl-phosphate-mannose--protein mannosyltransferase 4 +P46971 UniProtKB Topological domain 1 53 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Transmembrane 54 74 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Topological domain 75 136 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Transmembrane 137 157 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Topological domain 158 166 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Transmembrane 167 187 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Topological domain 188 189 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Transmembrane 190 210 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Topological domain 211 217 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Transmembrane 218 238 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Topological domain 239 242 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Transmembrane 243 263 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Topological domain 264 283 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Transmembrane 284 304 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Topological domain 305 593 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Transmembrane 594 614 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Topological domain 615 635 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Transmembrane 636 656 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Topological domain 657 716 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Transmembrane 717 737 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Topological domain 738 762 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46971 UniProtKB Domain 331 391 . . . Note=MIR 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +P46971 UniProtKB Domain 399 458 . . . Note=MIR 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +P46971 UniProtKB Domain 464 521 . . . Note=MIR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 +P46971 UniProtKB Glycosylation 759 759 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39685 1 1337 +P39685 UniProtKB Chain 1 1337 . . . ID=PRO_0000204910;Note=Nucleoporin POM152 +P39685 UniProtKB Topological domain 1 110 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:16847258,ECO:0000305|PubMed:9988776;Dbxref=PMID:16847258,PMID:9988776 +P39685 UniProtKB Transmembrane 111 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39685 UniProtKB Topological domain 132 148 . . . Note=Perinuclear space;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:16847258,ECO:0000305|PubMed:9988776;Dbxref=PMID:16847258,PMID:9988776 +P39685 UniProtKB Transmembrane 149 169 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39685 UniProtKB Topological domain 170 172 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:16847258,ECO:0000305|PubMed:9988776;Dbxref=PMID:16847258,PMID:9988776 +P39685 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39685 UniProtKB Topological domain 194 1337 . . . Note=Perinuclear space;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:16847258,ECO:0000305|PubMed:9988776;Dbxref=PMID:16847258,PMID:9988776 +P39685 UniProtKB Repeat 390 413 . . . Note=1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8138573;Dbxref=PMID:8138573 +P39685 UniProtKB Repeat 626 650 . . . Note=2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8138573;Dbxref=PMID:8138573 +P39685 UniProtKB Repeat 732 755 . . . Note=3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8138573;Dbxref=PMID:8138573 +P39685 UniProtKB Repeat 836 859 . . . Note=4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8138573;Dbxref=PMID:8138573 +P39685 UniProtKB Repeat 943 966 . . . Note=5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8138573;Dbxref=PMID:8138573 +P39685 UniProtKB Repeat 1058 1077 . . . Note=6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8138573;Dbxref=PMID:8138573 +P39685 UniProtKB Repeat 1157 1178 . . . Note=7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8138573;Dbxref=PMID:8138573 +P39685 UniProtKB Repeat 1253 1276 . . . Note=8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8138573;Dbxref=PMID:8138573 +P39685 UniProtKB Region 1 175 . . . Note=Pore side;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39685 UniProtKB Region 196 1337 . . . Note=Cisternal side;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39685 UniProtKB Region 390 1276 . . . Note=8 X 24 AA approximate repeats +P39685 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P39685 UniProtKB Modified residue 60 60 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P39685 UniProtKB Glycosylation 280 280 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8138573;Dbxref=PMID:8138573 +P39685 UniProtKB Beta strand 722 726 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ +P39685 UniProtKB Beta strand 729 733 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ +P39685 UniProtKB Beta strand 737 746 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ +P39685 UniProtKB Beta strand 748 763 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ +P39685 UniProtKB Beta strand 766 773 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ +P39685 UniProtKB Beta strand 776 787 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ +P39685 UniProtKB Beta strand 790 800 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ +P39685 UniProtKB Turn 801 803 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ +P39685 UniProtKB Beta strand 804 807 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ +P39685 UniProtKB Beta strand 813 817 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TVZ +##sequence-region Q05778 1 276 +Q05778 UniProtKB Chain 1 276 . . . ID=PRO_0000203234;Note=Proteasome chaperone 1 +Q05778 UniProtKB Beta strand 35 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Beta strand 49 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Helix 55 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Turn 63 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Beta strand 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Beta strand 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Beta strand 124 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Turn 139 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Helix 144 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Beta strand 164 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Beta strand 178 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Helix 196 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Turn 208 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Beta strand 214 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Beta strand 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Helix 232 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Helix 252 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Helix 265 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Helix 268 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +Q05778 UniProtKB Beta strand 274 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +##sequence-region Q12245 1 148 +Q12245 UniProtKB Chain 1 148 . . . ID=PRO_0000238635;Note=Proteasome chaperone 4 +Q12245 UniProtKB Sequence conflict 9 9 . . . Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12245 UniProtKB Beta strand 3 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +Q12245 UniProtKB Beta strand 21 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +Q12245 UniProtKB Beta strand 32 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +Q12245 UniProtKB Beta strand 38 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +Q12245 UniProtKB Beta strand 55 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +Q12245 UniProtKB Beta strand 80 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +Q12245 UniProtKB Helix 91 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +Q12245 UniProtKB Beta strand 112 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +Q12245 UniProtKB Helix 125 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +Q12245 UniProtKB Helix 131 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z5B +##sequence-region P23594 1 369 +P23594 UniProtKB Chain 1 369 . . . ID=PRO_0000058873;Note=Serine/threonine-protein phosphatase PP2A-1 catalytic subunit +P23594 UniProtKB Active site 178 178 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23594 UniProtKB Metal binding 117 117 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23594 UniProtKB Metal binding 119 119 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23594 UniProtKB Metal binding 145 145 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23594 UniProtKB Metal binding 145 145 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23594 UniProtKB Metal binding 177 177 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23594 UniProtKB Metal binding 227 227 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23594 UniProtKB Metal binding 301 301 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23594 UniProtKB Modified residue 369 369 . . . Note=Leucine methyl ester;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11060018;Dbxref=PMID:11060018 +P23594 UniProtKB Mutagenesis 99 99 . . . Note=Reduced interaction with TAP42. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14551259;Dbxref=PMID:14551259 +P23594 UniProtKB Mutagenesis 102 102 . . . Note=Reduced interaction with TAP42. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14551259;Dbxref=PMID:14551259 +P23594 UniProtKB Mutagenesis 103 103 . . . Note=Reduced interaction with TAP42. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14551259;Dbxref=PMID:14551259 +##sequence-region P38797 1 343 +P38797 UniProtKB Transit peptide 1 39 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38797 UniProtKB Chain 40 343 . . . ID=PRO_0000057779;Note=Protein phosphatase 2C homolog 7%2C mitochondrial +P38797 UniProtKB Domain 76 342 . . . Note=PPM-type phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01082 +P38797 UniProtKB Metal binding 109 109 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38797 UniProtKB Metal binding 109 109 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38797 UniProtKB Metal binding 110 110 . . . Note=Manganese 1%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38797 UniProtKB Metal binding 265 265 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P00635 1 467 +P00635 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:6093051,ECO:0000269|PubMed:6300772;Dbxref=PMID:6093051,PMID:6300772 +P00635 UniProtKB Chain 18 467 . . . ID=PRO_0000023954;Note=Repressible acid phosphatase +P00635 UniProtKB Active site 75 75 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00635 UniProtKB Active site 338 338 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00635 UniProtKB Glycosylation 97 97 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00635 UniProtKB Glycosylation 103 103 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00635 UniProtKB Glycosylation 162 162 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00635 UniProtKB Glycosylation 192 192 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00635 UniProtKB Glycosylation 250 250 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00635 UniProtKB Glycosylation 315 315 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00635 UniProtKB Glycosylation 356 356 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00635 UniProtKB Glycosylation 390 390 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00635 UniProtKB Glycosylation 439 439 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00635 UniProtKB Glycosylation 445 445 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00635 UniProtKB Glycosylation 456 456 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00635 UniProtKB Glycosylation 461 461 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P00635 UniProtKB Sequence conflict 36 36 . . . Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00635 UniProtKB Sequence conflict 130 130 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00635 UniProtKB Sequence conflict 294 294 . . . Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00635 UniProtKB Sequence conflict 446 446 . . . Note=S->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00635 UniProtKB Sequence conflict 462 463 . . . Note=AS->DT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00635 UniProtKB Sequence conflict 466 466 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40035 1 300 +P40035 UniProtKB Chain 1 300 . . . ID=PRO_0000090640;Note=Mitochondrial phosphate carrier protein 2 +P40035 UniProtKB Transmembrane 22 42 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40035 UniProtKB Transmembrane 70 89 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40035 UniProtKB Transmembrane 108 128 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40035 UniProtKB Transmembrane 171 192 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40035 UniProtKB Transmembrane 211 231 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40035 UniProtKB Transmembrane 260 280 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40035 UniProtKB Repeat 16 100 . . . Note=Solcar 1 +P40035 UniProtKB Repeat 107 193 . . . Note=Solcar 2 +P40035 UniProtKB Repeat 209 293 . . . Note=Solcar 3 +P40035 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P38969 1 423 +P38969 UniProtKB Transmembrane 199 219 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38969 UniProtKB Sequence conflict 406 423 . . . Note=NISLLKYNSELVATKDIQ->IYHC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40473 1 351 +P40473 UniProtKB Chain 1 351 . . . ID=PRO_0000202962;Note=Transcriptional activator POG1 +P40473 UniProtKB Compositional bias 193 302 . . . Note=Gln-rich +P40473 UniProtKB Modified residue 152 152 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40473 UniProtKB Modified residue 168 168 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40473 UniProtKB Modified residue 314 314 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P39008 1 433 +P39008 UniProtKB Chain 1 433 . . . ID=PRO_0000212849;Note=Poly(A) ribonuclease POP2 +P39008 UniProtKB Compositional bias 81 90 . . . Note=Poly-Gln +P39008 UniProtKB Compositional bias 111 125 . . . Note=Poly-Gln +P39008 UniProtKB Compositional bias 363 369 . . . Note=Poly-Gln +P39008 UniProtKB Metal binding 188 188 . . . Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39008 UniProtKB Metal binding 190 190 . . . Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39008 UniProtKB Metal binding 310 310 . . . Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39008 UniProtKB Metal binding 394 394 . . . Note=Divalent metal cation%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39008 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P39008 UniProtKB Modified residue 97 97 . . . Note=Phosphothreonine%3B by YAK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11358866;Dbxref=PMID:11358866 +P39008 UniProtKB Natural variant 41 41 . . . Note=In strain: A364A. K->Q +P39008 UniProtKB Natural variant 91 91 . . . Note=In strain: A364A. Q->QQQQQQQQQQQQQQQQQQ +P39008 UniProtKB Natural variant 118 122 . . . Note=In strain: A364A. Missing +P39008 UniProtKB Natural variant 278 278 . . . Note=In strain: A364A. L->S +P39008 UniProtKB Natural variant 412 412 . . . Note=K->M +P39008 UniProtKB Mutagenesis 97 97 . . . Note=No cell-cycle stop in response to glucose deprivation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11358866;Dbxref=PMID:11358866 +P39008 UniProtKB Mutagenesis 188 188 . . . Note=Abolishes poly(A) RNA degradation%3B when associated with A-190. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14618157;Dbxref=PMID:14618157 +P39008 UniProtKB Mutagenesis 190 190 . . . Note=Abolishes poly(A) RNA degradation%3B when associated with A-188. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14618157;Dbxref=PMID:14618157 +P39008 UniProtKB Helix 155 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Beta strand 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Turn 165 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Helix 168 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Turn 179 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Beta strand 184 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Beta strand 197 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8C +P39008 UniProtKB Helix 205 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Beta strand 221 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Beta strand 238 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Beta strand 242 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Turn 252 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8A +P39008 UniProtKB Helix 259 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Helix 272 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Helix 282 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Beta strand 292 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8A +P39008 UniProtKB Beta strand 300 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Helix 309 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Helix 327 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Beta strand 339 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Helix 344 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Helix 353 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B8A +P39008 UniProtKB Helix 373 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Helix 386 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Helix 391 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Turn 409 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +P39008 UniProtKB Helix 419 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UOC +##sequence-region P17157 1 305 +P17157 UniProtKB Chain 1 305 . . . ID=PRO_0000086521;Note=Cyclin-dependent protein kinase PHO85 +P17157 UniProtKB Domain 7 297 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P17157 UniProtKB Nucleotide binding 13 21 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P17157 UniProtKB Active site 133 133 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P17157 UniProtKB Binding site 36 36 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P17157 UniProtKB Site 166 166 . . . Note=Not phosphorylated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10490639;Dbxref=PMID:10490639 +P17157 UniProtKB Site 167 167 . . . Note=Not phosphorylated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10490639;Dbxref=PMID:10490639 +P17157 UniProtKB Modified residue 18 18 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10620010;Dbxref=PMID:10620010 +P17157 UniProtKB Cross-link 289 289 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P17157 UniProtKB Mutagenesis 18 18 . . . Note=Reduces kinase activity. Abolishes interaction to PHO80 cyclin%2C but not to PCL1. Y->F +P17157 UniProtKB Mutagenesis 36 36 . . . Note=Loss of kinase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15057567;Dbxref=PMID:15057567 +P17157 UniProtKB Mutagenesis 53 53 . . . Note=Loss of kinase activity. Abolishes interaction to PHO80 and PCL1 cyclins. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10620010;Dbxref=PMID:10620010 +P17157 UniProtKB Mutagenesis 82 82 . . . Note=Functional kinase%2C that can be rapidly inhibited by small%2C cell-permeable drugs like 1-Na PP1 (4-amino-1-tert-butyl-3-(1'-naphthyl)pyrazolo[3%2C4-d]pyrimidine). F->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11675494;Dbxref=PMID:11675494 +P17157 UniProtKB Sequence conflict 99 99 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17157 UniProtKB Sequence conflict 99 99 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17157 UniProtKB Helix 4 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Beta strand 7 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Beta strand 19 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Turn 27 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Beta strand 32 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Turn 42 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Helix 48 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Turn 56 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Beta strand 68 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Beta strand 77 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Beta strand 86 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Helix 89 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Beta strand 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PMI +P17157 UniProtKB Helix 107 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Helix 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Beta strand 139 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Beta strand 147 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Helix 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRC +P17157 UniProtKB Beta strand 156 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Helix 172 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Helix 177 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Helix 189 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Helix 214 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Turn 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Helix 234 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Beta strand 244 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRC +P17157 UniProtKB Helix 254 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Helix 259 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Helix 268 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Helix 282 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Helix 288 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +P17157 UniProtKB Helix 295 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KRD +##sequence-region P53191 1 635 +P53191 UniProtKB Chain 1 635 . . . ID=PRO_0000058425;Note=Phosphatidylinositol 3-phosphate-binding protein 2 +P53191 UniProtKB Zinc finger 452 527 . . . Note=FYVE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091 +P53191 UniProtKB Compositional bias 15 18 . . . Note=Poly-Glu +P53191 UniProtKB Compositional bias 195 201 . . . Note=Poly-Asp +P53191 UniProtKB Compositional bias 238 250 . . . Note=Poly-Ser +P53191 UniProtKB Modified residue 46 46 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53191 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53191 UniProtKB Modified residue 56 56 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53191 UniProtKB Modified residue 73 73 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53191 UniProtKB Modified residue 113 113 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53191 UniProtKB Modified residue 124 124 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53191 UniProtKB Modified residue 148 148 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P53191 UniProtKB Modified residue 165 165 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53191 UniProtKB Modified residue 174 174 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53191 UniProtKB Modified residue 300 300 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53191 UniProtKB Modified residue 309 309 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53191 UniProtKB Modified residue 381 381 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53191 UniProtKB Sequence conflict 152 152 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03760 1 334 +Q03760 UniProtKB Chain 1 334 . . . ID=PRO_0000203243;Note=Pre-mRNA leakage protein 39 +Q03760 UniProtKB Compositional bias 134 137 . . . Note=Poly-Cys +##sequence-region P07283 1 254 +P07283 UniProtKB Chain 1 254 . . . ID=PRO_0000199703;Note=Phosphomannomutase +P07283 UniProtKB Active site 19 19 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07283 UniProtKB Active site 21 21 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07283 UniProtKB Binding site 28 28 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07283 UniProtKB Binding site 130 130 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07283 UniProtKB Binding site 141 141 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07283 UniProtKB Binding site 148 148 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07283 UniProtKB Binding site 186 186 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07283 UniProtKB Binding site 188 188 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07283 UniProtKB Modified residue 240 240 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P07283 UniProtKB Natural variant 234 234 . . . Note=In strain: CLIB 556 haplotype Ha1. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P07283 UniProtKB Natural variant 249 249 . . . Note=In strain: R12 haplotype Ha1. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +##sequence-region P40975 1 43 +P40975 UniProtKB Propeptide 1 5 . . . ID=PRO_0000022073;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8063750;Dbxref=PMID:8063750 +P40975 UniProtKB Chain 6 43 . . . ID=PRO_0000022074;Note=Plasma membrane ATPase proteolipid 2 +P40975 UniProtKB Transmembrane 9 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40975 UniProtKB Topological domain 30 43 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36069 1 295 +P36069 UniProtKB Chain 1 295 . . . ID=PRO_0000203152;Note=Probable phosphoglycerate mutase PMU1 +P36069 UniProtKB Active site 61 61 . . . Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62707 +P36069 UniProtKB Active site 170 170 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62707 +P36069 UniProtKB Site 254 254 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62707 +P36069 UniProtKB Sequence conflict 44 44 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38218 1 177 +P38218 UniProtKB Chain 1 177 . . . ID=PRO_0000202470;Note=ADP-ribose 1''-phosphate phosphatase +P38218 UniProtKB Domain 1 177 . . . Note=Macro;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00490 +P38218 UniProtKB Region 9 11 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38218 UniProtKB Region 24 26 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38218 UniProtKB Region 31 36 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38218 UniProtKB Region 147 153 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q04636 1 552 +Q04636 UniProtKB Chain 1 552 . . . ID=PRO_0000203250;Note=FACT complex subunit POB3 +Q04636 UniProtKB Mutagenesis 20 20 . . . Note=In pob3-11%3B causes severe defects in rate of growth%3B when associated with C-109. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10924459;Dbxref=PMID:10924459 +Q04636 UniProtKB Mutagenesis 78 78 . . . Note=In pob3-1%3B causes severe defects in rate of growth%3B when associated with K-419 and T-489. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10924459;Dbxref=PMID:10924459 +Q04636 UniProtKB Mutagenesis 109 109 . . . Note=In pob3-11%3B causes severe defects in rate of growth%3B when associated with H-20. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10924459;Dbxref=PMID:10924459 +Q04636 UniProtKB Mutagenesis 308 308 . . . Note=No effect. Q->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16678108;Dbxref=PMID:16678108 +Q04636 UniProtKB Mutagenesis 308 308 . . . Note=Confers sensitivity to HU indicating a disturbed activity in DNA replication%3B confers a SPT- phenotype indicating a disturbed activity in transcription. Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16678108;Dbxref=PMID:16678108 +Q04636 UniProtKB Mutagenesis 308 308 . . . Note=Confers sensitivity to HU indicating a disturbed activity in DNA replication. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16678108;Dbxref=PMID:16678108 +Q04636 UniProtKB Mutagenesis 311 311 . . . Note=No change of sensitivity to HU%3B confers a SPT- phenotype indicating a disturbed activity in transcription. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16678108;Dbxref=PMID:16678108 +Q04636 UniProtKB Mutagenesis 419 419 . . . Note=In pob3-1%3B causes severe defects in rate of growth%3B when associated with R-78 and T-489. M->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10924459;Dbxref=PMID:10924459 +Q04636 UniProtKB Mutagenesis 489 489 . . . Note=In pob3-1%3B causes severe defects in rate of growth%3B when associated with R-78 and K-419. S->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10924459;Dbxref=PMID:10924459 +Q04636 UniProtKB Mutagenesis 547 547 . . . Note=In pob3-21%3B causes severe defects in rate of growth. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10924459;Dbxref=PMID:10924459 +Q04636 UniProtKB Beta strand 1 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R +Q04636 UniProtKB Beta strand 17 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R +Q04636 UniProtKB Beta strand 25 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R +Q04636 UniProtKB Turn 35 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R +Q04636 UniProtKB Helix 38 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R +Q04636 UniProtKB Beta strand 45 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R +Q04636 UniProtKB Helix 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R +Q04636 UniProtKB Beta strand 52 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R +Q04636 UniProtKB Beta strand 61 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R +Q04636 UniProtKB Beta strand 75 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R +Q04636 UniProtKB Helix 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R +Q04636 UniProtKB Helix 86 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R +Q04636 UniProtKB Turn 107 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F5R +Q04636 UniProtKB Beta strand 242 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Beta strand 255 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Beta strand 263 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Beta strand 274 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Helix 279 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Beta strand 282 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Beta strand 293 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Beta strand 311 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Beta strand 325 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Helix 334 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Turn 341 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Beta strand 347 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Helix 353 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Beta strand 384 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Beta strand 391 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Beta strand 399 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Beta strand 410 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Helix 414 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Beta strand 417 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Beta strand 434 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Helix 442 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Beta strand 447 454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Helix 455 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +Q04636 UniProtKB Helix 458 467 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQ0 +##sequence-region P38336 1 279 +P38336 UniProtKB Chain 1 279 . . . ID=PRO_0000128422;Note=RNases MRP/P 32.9 kDa subunit +P38336 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P53218 1 158 +P53218 UniProtKB Chain 1 158 . . . ID=PRO_0000058517;Note=Ribonucleases P/MRP protein subunit POP6 +P53218 UniProtKB Coiled coil 51 71 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53218 UniProtKB Beta strand 5 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P53218 UniProtKB Beta strand 10 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P53218 UniProtKB Helix 19 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P53218 UniProtKB Turn 29 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P53218 UniProtKB Beta strand 38 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P53218 UniProtKB Helix 55 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P53218 UniProtKB Turn 71 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P53218 UniProtKB Beta strand 76 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P53218 UniProtKB Helix 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P53218 UniProtKB Helix 88 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P53218 UniProtKB Turn 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P53218 UniProtKB Beta strand 110 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P53218 UniProtKB Beta strand 133 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P53218 UniProtKB Beta strand 155 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +##sequence-region P38291 1 140 +P38291 UniProtKB Chain 1 140 . . . ID=PRO_0000058519;Note=Ribonucleases P/MRP protein subunit POP7 +P38291 UniProtKB Modified residue 115 115 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38291 UniProtKB Sequence conflict 92 92 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38291 UniProtKB Helix 26 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P38291 UniProtKB Beta strand 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P38291 UniProtKB Helix 41 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P38291 UniProtKB Beta strand 61 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P38291 UniProtKB Helix 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P38291 UniProtKB Helix 72 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P38291 UniProtKB Beta strand 90 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +P38291 UniProtKB Beta strand 126 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IAB +##sequence-region P23595 1 377 +P23595 UniProtKB Chain 1 377 . . . ID=PRO_0000058874;Note=Serine/threonine-protein phosphatase PP2A-2 catalytic subunit +P23595 UniProtKB Active site 186 186 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23595 UniProtKB Metal binding 125 125 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23595 UniProtKB Metal binding 127 127 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23595 UniProtKB Metal binding 153 153 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23595 UniProtKB Metal binding 153 153 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23595 UniProtKB Metal binding 185 185 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23595 UniProtKB Metal binding 235 235 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23595 UniProtKB Metal binding 309 309 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23595 UniProtKB Modified residue 38 38 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P23595 UniProtKB Modified residue 43 43 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P23595 UniProtKB Modified residue 377 377 . . . Note=Leucine methyl ester;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11060018,ECO:0000269|PubMed:11697862;Dbxref=PMID:11060018,PMID:11697862 +##sequence-region P35182 1 281 +P35182 UniProtKB Chain 1 281 . . . ID=PRO_0000057774;Note=Protein phosphatase 2C homolog 1 +P35182 UniProtKB Domain 20 281 . . . Note=PPM-type phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01082 +P35182 UniProtKB Metal binding 58 58 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35182 UniProtKB Metal binding 58 58 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35182 UniProtKB Metal binding 59 59 . . . Note=Manganese 1%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35182 UniProtKB Metal binding 233 233 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35182 UniProtKB Metal binding 272 272 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35182 UniProtKB Sequence conflict 53 53 . . . Note=Y->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35182 UniProtKB Sequence conflict 124 124 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P34221 1 468 +P34221 UniProtKB Chain 1 468 . . . ID=PRO_0000057776;Note=Protein phosphatase 2C homolog 3 +P34221 UniProtKB Domain 23 293 . . . Note=PPM-type phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01082 +P34221 UniProtKB Metal binding 62 62 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P34221 UniProtKB Metal binding 62 62 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P34221 UniProtKB Metal binding 63 63 . . . Note=Manganese 1%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P34221 UniProtKB Metal binding 234 234 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P34221 UniProtKB Metal binding 284 284 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P34221 UniProtKB Modified residue 324 324 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P34221 UniProtKB Modified residue 332 332 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P34221 UniProtKB Sequence conflict 369 369 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P34221 UniProtKB Sequence conflict 369 369 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40164 1 858 +P40164 UniProtKB Chain 1 858 . . . ID=PRO_0000203395;Note=Serine/threonine-protein phosphatase 4 regulatory subunit 3 +##sequence-region P35842 1 467 +P35842 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35842 UniProtKB Chain 18 467 . . . ID=PRO_0000023956;Note=Acid phosphatase PHO11 +P35842 UniProtKB Active site 75 75 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35842 UniProtKB Active site 338 338 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35842 UniProtKB Glycosylation 97 97 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35842 UniProtKB Glycosylation 162 162 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35842 UniProtKB Glycosylation 192 192 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35842 UniProtKB Glycosylation 250 250 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35842 UniProtKB Glycosylation 315 315 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35842 UniProtKB Glycosylation 356 356 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35842 UniProtKB Glycosylation 390 390 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35842 UniProtKB Glycosylation 439 439 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35842 UniProtKB Glycosylation 445 445 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35842 UniProtKB Glycosylation 461 461 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35842 UniProtKB Sequence conflict 17 17 . . . Note=A->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35842 UniProtKB Sequence conflict 82 83 . . . Note=VS->AR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35842 UniProtKB Sequence conflict 150 150 . . . Note=R->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35842 UniProtKB Sequence conflict 354 354 . . . Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35842 UniProtKB Sequence conflict 423 423 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04705 1 352 +Q04705 UniProtKB Chain 1 352 . . . ID=PRO_0000203256;Note=Pheromone-regulated membrane protein 6 +Q04705 UniProtKB Transmembrane 37 57 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04705 UniProtKB Transmembrane 77 97 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04705 UniProtKB Transmembrane 228 248 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39551 1 298 +P39551 UniProtKB Chain 1 298 . . . ID=PRO_0000207524;Note=Pheromone-regulated membrane protein 9 +P39551 UniProtKB Topological domain 1 111 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39551 UniProtKB Transmembrane 112 132 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39551 UniProtKB Topological domain 133 137 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39551 UniProtKB Transmembrane 138 158 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39551 UniProtKB Topological domain 159 298 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39551 UniProtKB Region 297 298 . . . Note=COPII binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P32264 1 428 +P32264 UniProtKB Chain 1 428 . . . ID=PRO_0000109768;Note=Glutamate 5-kinase +P32264 UniProtKB Domain 321 412 . . . Note=PUA +P32264 UniProtKB Nucleotide binding 175 176 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32264 UniProtKB Nucleotide binding 219 225 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32264 UniProtKB Binding site 56 56 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32264 UniProtKB Binding site 143 143 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32264 UniProtKB Binding site 155 155 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32264 UniProtKB Sequence conflict 332 332 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53549 1 437 +P53549 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901 +P53549 UniProtKB Chain 2 437 . . . ID=PRO_0000084737;Note=26S proteasome subunit RPT4 +P53549 UniProtKB Nucleotide binding 222 229 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53549 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901 +P53549 UniProtKB Sequence conflict 121 121 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53549 UniProtKB Sequence conflict 135 135 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q01939 1 405 +Q01939 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901 +Q01939 UniProtKB Chain 2 405 . . . ID=PRO_0000084730;Note=26S proteasome regulatory subunit 8 homolog +Q01939 UniProtKB Nucleotide binding 189 196 . . . Note=ATP +Q01939 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901 +Q01939 UniProtKB Sequence conflict 41 41 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25375 1 712 +P25375 UniProtKB Chain 1 712 . . . ID=PRO_0000078156;Note=Saccharolysin +P25375 UniProtKB Active site 502 502 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P25375 UniProtKB Metal binding 501 501 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P25375 UniProtKB Metal binding 505 505 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P25375 UniProtKB Metal binding 508 508 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P25375 UniProtKB Modified residue 73 73 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P25375 UniProtKB Sequence conflict 384 384 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47032 1 299 +P47032 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47032 UniProtKB Chain 20 299 . . . ID=PRO_0000006317;Note=Protein PRY1 +P47032 UniProtKB Domain 167 281 . . . Note=SCP +P47032 UniProtKB Compositional bias 102 165 . . . Note=Ala/Ser/Thr-rich +P47032 UniProtKB Helix 161 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS +P47032 UniProtKB Helix 187 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS +P47032 UniProtKB Beta strand 212 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS +P47032 UniProtKB Helix 223 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS +P47032 UniProtKB Helix 232 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS +P47032 UniProtKB Turn 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS +P47032 UniProtKB Helix 249 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS +P47032 UniProtKB Beta strand 261 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS +P47032 UniProtKB Turn 271 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS +P47032 UniProtKB Beta strand 275 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS +P47032 UniProtKB Helix 291 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JYS +##sequence-region Q06892 1 414 +Q06892 UniProtKB Sequence conflict 37 38 . . . Note=KP->EA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06892 UniProtKB Sequence conflict 180 180 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06892 UniProtKB Sequence conflict 329 329 . . . Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06892 UniProtKB Sequence conflict 343 343 . . . Note=I->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06892 UniProtKB Sequence conflict 398 401 . . . Note=LGFN->CRIH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06892 UniProtKB Beta strand 34 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Helix 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 59 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 69 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Helix 79 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Helix 105 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Helix 119 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 127 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Helix 134 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 142 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Helix 150 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Turn 159 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 168 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Helix 184 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Helix 187 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 200 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 207 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 220 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 239 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 248 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Helix 264 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Helix 269 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 284 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 300 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 308 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 321 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 325 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 332 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 342 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Beta strand 379 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +Q06892 UniProtKB Helix 389 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3AFO +##sequence-region P40506 1 365 +P40506 UniProtKB Chain 1 365 . . . ID=PRO_0000182042;Note=Phosphopantothenate--cysteine ligase CAB2 +P40506 UniProtKB Sequence conflict 338 338 . . . Note=S->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38796 1 400 +P38796 UniProtKB Chain 1 400 . . . ID=PRO_0000030588;Note=Protein phosphatase methylesterase 1 +P38796 UniProtKB Domain 114 365 . . . Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38796 UniProtKB Active site 205 205 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38796 UniProtKB Active site 233 233 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38796 UniProtKB Active site 359 359 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38796 UniProtKB Sequence conflict 36 36 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38796 UniProtKB Sequence conflict 39 39 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38796 UniProtKB Sequence conflict 44 44 . . . Note=S->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04119 1 674 +Q04119 UniProtKB Propeptide 1 83 . . . ID=PRO_0000022089;Note=Removed in mature form;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15792812;Dbxref=PMID:15792812 +Q04119 UniProtKB Chain 84 384 . . . ID=PRO_0000022090;Note=Endopolyphosphatase +Q04119 UniProtKB Propeptide 385 674 . . . ID=PRO_0000022091;Note=Removed in mature form;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15792812;Dbxref=PMID:15792812 +Q04119 UniProtKB Topological domain 1 21 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04119 UniProtKB Transmembrane 22 42 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04119 UniProtKB Topological domain 43 674 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04119 UniProtKB Glycosylation 58 58 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04119 UniProtKB Glycosylation 505 505 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04119 UniProtKB Glycosylation 511 511 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04119 UniProtKB Cross-link 6 6 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11566881;Dbxref=PMID:11566881 +Q04119 UniProtKB Mutagenesis 6 6 . . . Note=Causes accumulation in vacuoles and abolishes sorting into internal vesicles in late endosomes. K->R%2CG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11566881;Dbxref=PMID:11566881 +Q04119 UniProtKB Mutagenesis 11 11 . . . Note=Abolishes enzyme activity%3B when associated with A-505 and A-511. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15792812;Dbxref=PMID:15792812 +Q04119 UniProtKB Mutagenesis 505 505 . . . Note=Abolishes enzyme activity%3B when associated with A-11 and A-511. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15792812;Dbxref=PMID:15792812 +Q04119 UniProtKB Mutagenesis 511 511 . . . Note=Abolishes enzyme activity%3B when associated with A-11 and A-505. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15792812;Dbxref=PMID:15792812 +##sequence-region P42946 1 383 +P42946 UniProtKB Chain 1 383 . . . ID=PRO_0000203045;Note=Pheromone-regulated membrane protein 10 +P42946 UniProtKB Topological domain 1 65 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Transmembrane 66 86 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Topological domain 87 87 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Transmembrane 88 108 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Topological domain 109 117 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Transmembrane 118 138 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Topological domain 139 141 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Transmembrane 142 162 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Topological domain 163 180 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Transmembrane 181 201 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Topological domain 202 216 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Transmembrane 217 237 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Topological domain 238 241 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Transmembrane 242 262 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Topological domain 263 271 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Transmembrane 272 292 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Topological domain 293 293 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Transmembrane 294 314 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Topological domain 315 352 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Transmembrane 353 373 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Topological domain 374 383 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42946 UniProtKB Sequence conflict 129 129 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12498 1 284 +Q12498 UniProtKB Chain 1 284 . . . ID=PRO_0000058579;Note=Pheromone-regulated membrane protein 4 +Q12498 UniProtKB Transmembrane 20 38 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12498 UniProtKB Domain 157 272 . . . Note=Glutaredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00686 +Q12498 UniProtKB Compositional bias 129 135 . . . Note=Poly-Thr +##sequence-region P32524 1 280 +P32524 UniProtKB Chain 1 280 . . . ID=PRO_0000174322;Note=Pre-mRNA-splicing factor PRP21 +P32524 UniProtKB Repeat 11 49 . . . Note=SURP motif 1 +P32524 UniProtKB Repeat 95 135 . . . Note=SURP motif 2 +P32524 UniProtKB Mutagenesis 168 168 . . . Note=In SPP91-1%3B corrects the PRP9-1 growth defect through partial restoration of splicing and by a complete reversion of the pre-mRNA escape phenotype. T->A +P32524 UniProtKB Sequence conflict 205 205 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32524 UniProtKB Helix 90 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P32524 UniProtKB Helix 109 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P32524 UniProtKB Helix 123 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P32524 UniProtKB Helix 132 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P32524 UniProtKB Helix 157 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P32524 UniProtKB Turn 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +##sequence-region P20053 1 465 +P20053 UniProtKB Chain 1 465 . . . ID=PRO_0000051152;Note=U4/U6 small nuclear ribonucleoprotein PRP4 +P20053 UniProtKB Repeat 173 212 . . . Note=WD 1 +P20053 UniProtKB Repeat 216 256 . . . Note=WD 2 +P20053 UniProtKB Repeat 263 302 . . . Note=WD 3 +P20053 UniProtKB Repeat 305 344 . . . Note=WD 4 +P20053 UniProtKB Repeat 347 386 . . . Note=WD 5 +P20053 UniProtKB Repeat 391 432 . . . Note=WD 6 +P20053 UniProtKB Repeat 435 464 . . . Note=WD 7 +##sequence-region Q06449 1 215 +Q06449 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q06449 UniProtKB Chain 2 215 . . . ID=PRO_0000268696;Note=[PSI+] inducibility protein 3 +Q06449 UniProtKB Domain 54 113 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +Q06449 UniProtKB Motif 124 127 . . . Note=PY motif +Q06449 UniProtKB Compositional bias 122 125 . . . Note=Poly-Pro +Q06449 UniProtKB Compositional bias 126 181 . . . Note=Asn/Gln-rich +Q06449 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q06449 UniProtKB Modified residue 52 52 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06449 UniProtKB Modified residue 55 55 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06449 UniProtKB Cross-link 80 80 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q06449 UniProtKB Mutagenesis 80 80 . . . Note=Abolishes formation of ubiquitinated protein forms. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21777813;Dbxref=PMID:21777813 +Q06449 UniProtKB Mutagenesis 91 91 . . . Note=Abolishes interaction with LAS17%2C but not with SUP35. Blocks colocalization with actin%2C aggregation%2C and prion-inducing ability. W->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21777813;Dbxref=PMID:21777813 +Q06449 UniProtKB Mutagenesis 124 125 . . . Note=Abolishes RSP5 binding site and consequently ubiquitination. PP->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21777813;Dbxref=PMID:21777813 +Q06449 UniProtKB Mutagenesis 174 175 . . . Note=Reduces%2C but does not abolish the ability to promote [PSI+] induction. QQ->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21777813;Dbxref=PMID:21777813 +Q06449 UniProtKB Beta strand 58 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZX6 +Q06449 UniProtKB Beta strand 80 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZX6 +Q06449 UniProtKB Beta strand 88 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZX6 +Q06449 UniProtKB Beta strand 99 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZX6 +Q06449 UniProtKB Helix 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZX6 +Q06449 UniProtKB Beta strand 108 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZX6 +##sequence-region P34217 1 668 +P34217 UniProtKB Chain 1 668 . . . ID=PRO_0000082028;Note=RNA-binding protein PIN4 +P34217 UniProtKB Domain 85 163 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P34217 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P34217 UniProtKB Modified residue 189 189 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P34217 UniProtKB Modified residue 191 191 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34217 UniProtKB Modified residue 194 194 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34217 UniProtKB Modified residue 197 197 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P34217 UniProtKB Modified residue 305 305 . . . Note=Phosphothreonine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15024067;Dbxref=PMID:15024067 +P34217 UniProtKB Modified residue 393 393 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34217 UniProtKB Modified residue 466 466 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P34217 UniProtKB Modified residue 541 541 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P34217 UniProtKB Modified residue 636 636 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34217 UniProtKB Modified residue 638 638 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198 +P34217 UniProtKB Modified residue 640 640 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34217 UniProtKB Modified residue 653 653 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P34217 UniProtKB Modified residue 655 655 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P34217 UniProtKB Mutagenesis 305 305 . . . Note=No interaction with RAD53. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15024067;Dbxref=PMID:15024067 +##sequence-region Q12017 1 286 +Q12017 UniProtKB Chain 1 286 . . . ID=PRO_0000163762;Note=Phosducin-like protein 2 +Q12017 UniProtKB Region 96 286 . . . Note=Thioredoxin fold;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12017 UniProtKB Modified residue 35 35 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +Q12017 UniProtKB Modified residue 62 62 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region Q12008 1 311 +Q12008 UniProtKB Chain 1 311 . . . ID=PRO_0000179840;Note=Phosphoglycerate mutase 2 +Q12008 UniProtKB Region 16 23 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +Q12008 UniProtKB Region 29 30 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +Q12008 UniProtKB Region 126 129 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +Q12008 UniProtKB Region 153 154 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +Q12008 UniProtKB Region 243 244 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +Q12008 UniProtKB Active site 17 17 . . . Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +Q12008 UniProtKB Active site 126 126 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +Q12008 UniProtKB Binding site 73 73 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +Q12008 UniProtKB Binding site 137 137 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +Q12008 UniProtKB Site 242 242 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00950 +##sequence-region P36110 1 329 +P36110 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36110 UniProtKB Chain 19 329 . . . ID=PRO_0000006318;Note=Protein PRY2 +P36110 UniProtKB Domain 197 311 . . . Note=SCP +P36110 UniProtKB Compositional bias 132 195 . . . Note=Ser/Thr-rich +##sequence-region P30657 1 266 +P30657 UniProtKB Propeptide 1 33 . . . ID=PRO_0000331490 +P30657 UniProtKB Chain 34 266 . . . ID=PRO_0000148073;Note=Proteasome subunit beta type-7 +P30657 UniProtKB Sequence conflict 188 188 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P30657 UniProtKB Beta strand 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Beta strand 44 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Beta strand 52 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Beta strand 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Beta strand 66 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Beta strand 75 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Turn 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Beta strand 82 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Helix 90 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Turn 112 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Helix 122 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Beta strand 145 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Beta strand 158 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Beta strand 169 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QVP +P30657 UniProtKB Beta strand 173 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Helix 179 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Turn 189 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Beta strand 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GPJ +P30657 UniProtKB Helix 195 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Helix 203 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Beta strand 226 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Turn 235 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Beta strand 238 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Helix 253 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30657 UniProtKB Beta strand 260 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +##sequence-region Q12161 1 406 +Q12161 UniProtKB Chain 1 406 . . . ID=PRO_0000235918;Note=RING finger protein PSH1 +Q12161 UniProtKB Zinc finger 30 72 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +Q12161 UniProtKB Compositional bias 184 325 . . . Note=Glu-rich +Q12161 UniProtKB Modified residue 143 143 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12161 UniProtKB Modified residue 191 191 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12161 UniProtKB Modified residue 310 310 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12161 UniProtKB Modified residue 403 403 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P40555 1 220 +P40555 UniProtKB Chain 1 220 . . . ID=PRO_0000173856;Note=Probable 26S proteasome regulatory subunit p27 +P40555 UniProtKB Domain 119 196 . . . Note=PDZ +P40555 UniProtKB Compositional bias 2 5 . . . Note=Poly-Glu +P40555 UniProtKB Helix 2 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHJ +P40555 UniProtKB Helix 17 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHJ +P40555 UniProtKB Turn 25 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHJ +P40555 UniProtKB Helix 31 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHJ +P40555 UniProtKB Helix 73 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHJ +P40555 UniProtKB Beta strand 135 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06 +P40555 UniProtKB Helix 145 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06 +P40555 UniProtKB Beta strand 156 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06 +P40555 UniProtKB Turn 165 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06 +P40555 UniProtKB Turn 169 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06 +P40555 UniProtKB Helix 172 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06 +P40555 UniProtKB Turn 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06 +P40555 UniProtKB Beta strand 186 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06 +P40555 UniProtKB Beta strand 195 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06 +P40555 UniProtKB Beta strand 207 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06 +P40555 UniProtKB Beta strand 215 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O06 +##sequence-region P08456 1 276 +P08456 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2830250;Dbxref=PMID:2830250 +P08456 UniProtKB Chain 2 276 . . . ID=PRO_0000056801;Note=CDP-diacylglycerol--serine O-phosphatidyltransferase +P08456 UniProtKB Transmembrane 82 102 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08456 UniProtKB Transmembrane 163 183 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08456 UniProtKB Transmembrane 210 230 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08456 UniProtKB Transmembrane 248 268 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08456 UniProtKB Modified residue 4 4 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P08456 UniProtKB Modified residue 34 34 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P08456 UniProtKB Modified residue 42 42 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P08456 UniProtKB Modified residue 46 46 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P08456 UniProtKB Modified residue 47 47 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P08456 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P08456 UniProtKB Sequence conflict 123 123 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08456 UniProtKB Sequence conflict 191 191 . . . Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08456 UniProtKB Sequence conflict 276 276 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36002 1 662 +P36002 UniProtKB Chain 1 662 . . . ID=PRO_0000086589;Note=Serine/threonine-protein kinase PTK1/STK1 +P36002 UniProtKB Domain 196 503 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P36002 UniProtKB Nucleotide binding 202 210 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P36002 UniProtKB Compositional bias 4 146 . . . Note=Ser-rich +P36002 UniProtKB Compositional bias 567 624 . . . Note=Pro-rich +P36002 UniProtKB Active site 329 329 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P36002 UniProtKB Binding site 226 226 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P36002 UniProtKB Sequence conflict 241 244 . . . Note=KRCS->NAAP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36002 UniProtKB Sequence conflict 300 300 . . . Note=S->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36002 UniProtKB Sequence conflict 356 375 . . . Note=TDPHDLSSPVKKCAGMIGSP->HGSTRPVQPCQEVRRDDRLA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36002 UniProtKB Sequence conflict 637 662 . . . Note=VHHHLNIVNSLVHSSSAASSQVPAST->GASPSEHCQQLGP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40100 1 303 +P40100 UniProtKB Chain 1 303 . . . ID=PRO_0000202661;Note=Protoporphyrin uptake protein 1 +P40100 UniProtKB Topological domain 1 18 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40100 UniProtKB Transmembrane 19 39 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40100 UniProtKB Topological domain 40 76 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40100 UniProtKB Transmembrane 77 97 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40100 UniProtKB Topological domain 98 111 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40100 UniProtKB Transmembrane 112 132 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40100 UniProtKB Topological domain 133 154 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40100 UniProtKB Transmembrane 155 175 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40100 UniProtKB Topological domain 176 183 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40100 UniProtKB Transmembrane 184 204 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40100 UniProtKB Topological domain 205 226 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40100 UniProtKB Transmembrane 227 247 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40100 UniProtKB Topological domain 248 264 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40100 UniProtKB Transmembrane 265 285 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40100 UniProtKB Topological domain 286 303 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P28708 1 518 +P28708 UniProtKB Chain 1 518 . . . ID=PRO_0000086149;Note=Serine/threonine-protein kinase PRR1 +P28708 UniProtKB Domain 192 508 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P28708 UniProtKB Nucleotide binding 198 206 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P28708 UniProtKB Active site 354 354 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P28708 UniProtKB Binding site 225 225 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P28708 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P28708 UniProtKB Modified residue 132 132 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P23639 1 250 +P23639 UniProtKB Chain 1 250 . . . ID=PRO_0000124090;Note=Proteasome subunit alpha type-2 +P23639 UniProtKB Cross-link 108 108 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P23639 UniProtKB Beta strand 7 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G65 +P23639 UniProtKB Turn 14 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G0U +P23639 UniProtKB Helix 19 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Beta strand 34 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Beta strand 42 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Beta strand 54 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Helix 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Beta strand 63 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Beta strand 71 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Helix 79 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Helix 98 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Helix 107 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Turn 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Beta strand 132 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Turn 141 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Beta strand 144 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Beta strand 156 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Helix 168 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Helix 185 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Turn 206 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Beta strand 209 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Helix 219 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Beta strand 223 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Beta strand 234 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23639 UniProtKB Helix 240 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +##sequence-region P50109 1 593 +P50109 UniProtKB Chain 1 593 . . . ID=PRO_0000097069;Note=Protein PSP2 +P50109 UniProtKB Compositional bias 408 547 . . . Note=Asn-rich +P50109 UniProtKB Modified residue 238 238 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198 +P50109 UniProtKB Modified residue 340 340 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region Q07949 1 397 +Q07949 UniProtKB Chain 1 397 . . . ID=PRO_0000212577;Note=Probable phosphatase PSR2 +Q07949 UniProtKB Domain 223 381 . . . Note=FCP1 homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00336 +Q07949 UniProtKB Lipidation 9 9 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255,ECO:0000303;evidence=ECO:0000255,ECO:0000303|PubMed:10777497;Dbxref=PMID:10777497 +Q07949 UniProtKB Lipidation 10 10 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255,ECO:0000303;evidence=ECO:0000255,ECO:0000303|PubMed:10777497;Dbxref=PMID:10777497 +Q07949 UniProtKB Sequence conflict 59 59 . . . Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12335 1 198 +Q12335 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12335 UniProtKB Chain 22 198 . . . ID=PRO_0000041482;Note=Protoplast secreted protein 2 +Q12335 UniProtKB Domain 22 191 . . . Note=Flavodoxin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00088 +##sequence-region P38958 1 111 +P38958 UniProtKB Transmembrane 18 36 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P08468 1 800 +P08468 UniProtKB Sequence conflict 278 278 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08468 UniProtKB Sequence conflict 709 709 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P10355 1 254 +P10355 UniProtKB Transit peptide 1 8 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8389363;Dbxref=PMID:8389363 +P10355 UniProtKB Chain 9 254 . . . ID=PRO_0000022177;Note=Protein PET122%2C mitochondrial +P10355 UniProtKB Region 185 254 . . . Note=Essential for PET122 function +##sequence-region Q12461 1 358 +Q12461 UniProtKB Chain 1 358 . . . ID=PRO_0000226120;Note=Serine/threonine-protein phosphatase 2A activator 2 +Q12461 UniProtKB Turn 10 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Helix 14 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Helix 20 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Turn 35 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Helix 50 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Helix 84 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Helix 109 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Turn 126 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Helix 133 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Helix 154 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Helix 165 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Beta strand 192 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Helix 199 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Turn 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Helix 216 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Helix 222 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Turn 229 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Helix 233 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Turn 245 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Helix 250 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Helix 255 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Helix 266 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Turn 281 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Helix 285 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +Q12461 UniProtKB Beta strand 295 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IXN +##sequence-region P32901 1 601 +P32901 UniProtKB Chain 1 601 . . . ID=PRO_0000064317;Note=Peptide transporter PTR2 +P32901 UniProtKB Topological domain 1 150 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Transmembrane 151 172 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Topological domain 173 182 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Transmembrane 183 202 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Topological domain 203 210 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Transmembrane 211 229 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Topological domain 230 267 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Transmembrane 268 287 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Topological domain 288 294 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Transmembrane 295 316 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Topological domain 317 378 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Transmembrane 379 399 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Topological domain 400 412 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Transmembrane 413 429 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Topological domain 430 448 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Transmembrane 449 466 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Topological domain 467 494 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Transmembrane 495 513 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Topological domain 514 526 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Transmembrane 527 547 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Topological domain 548 554 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Transmembrane 555 577 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Topological domain 578 601 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32901 UniProtKB Modified residue 37 37 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P32901 UniProtKB Modified residue 39 39 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32901 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P32901 UniProtKB Modified residue 594 594 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32901 UniProtKB Sequence conflict 39 39 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P43606 1 678 +P43606 UniProtKB Chain 1 678 . . . ID=PRO_0000097093;Note=SPS-sensor component PTR3 +P43606 UniProtKB Mutagenesis 321 321 . . . Note=No effect. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17984223;Dbxref=PMID:17984223 +P43606 UniProtKB Mutagenesis 435 435 . . . Note=In PTR3-17%3B constitutively active%2C confers increased STP1 processing in the absence of amino acids. T->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15947203,ECO:0000269|PubMed:17984223;Dbxref=PMID:15947203,PMID:17984223 +P43606 UniProtKB Mutagenesis 439 439 . . . Note=In PTR3-5%3B constitutively active and hyperphosphorylated%2C confers increased STP1 processing in the absence of amino acids. Q->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15947203,ECO:0000269|PubMed:17984223;Dbxref=PMID:15947203,PMID:17984223 +P43606 UniProtKB Mutagenesis 525 525 . . . Note=Loss of function. Abolishes hyperphosphorylation of PTR3 and%2C consequently%2C results in a failure to activate STP1. T->A%2CD%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17984223;Dbxref=PMID:17984223 +P43606 UniProtKB Mutagenesis 635 635 . . . Note=No effect. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17984223;Dbxref=PMID:17984223 +##sequence-region P38089 1 393 +P38089 UniProtKB Chain 1 393 . . . ID=PRO_0000057777;Note=Protein phosphatase 2C homolog 4 +P38089 UniProtKB Domain 33 368 . . . Note=PPM-type phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01082 +P38089 UniProtKB Metal binding 83 83 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38089 UniProtKB Metal binding 83 83 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38089 UniProtKB Metal binding 84 84 . . . Note=Manganese 1%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38089 UniProtKB Metal binding 310 310 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38089 UniProtKB Metal binding 359 359 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38193 1 441 +P38193 UniProtKB Chain 1 441 . . . ID=PRO_0000202458;Note=Serine/threonine-protein phosphatase 4 regulatory subunit 2 +P38193 UniProtKB Compositional bias 198 302 . . . Note=Asp-rich +P38193 UniProtKB Modified residue 347 347 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38193 UniProtKB Sequence conflict 374 374 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38698 1 397 +P38698 UniProtKB Chain 1 397 . . . ID=PRO_0000158601;Note=Exopolyphosphatase +P38698 UniProtKB Metal binding 39 39 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38698 UniProtKB Metal binding 41 41 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38698 UniProtKB Metal binding 127 127 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38698 UniProtKB Metal binding 127 127 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38698 UniProtKB Metal binding 148 148 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38698 UniProtKB Metal binding 202 202 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38698 UniProtKB Sequence conflict 193 193 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38698 UniProtKB Sequence conflict 284 284 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38698 UniProtKB Helix 8 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Helix 20 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Beta strand 28 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Helix 40 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Helix 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Beta strand 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Beta strand 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Helix 79 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Helix 86 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Helix 99 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Helix 105 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Beta strand 120 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Helix 133 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Turn 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Beta strand 141 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Beta strand 159 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Helix 169 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Turn 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Helix 185 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Turn 203 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Helix 212 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Helix 235 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Helix 259 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Beta strand 267 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Beta strand 275 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Beta strand 280 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Helix 291 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Helix 301 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Beta strand 318 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Beta strand 331 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Helix 342 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Beta strand 358 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Helix 365 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Beta strand 369 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +P38698 UniProtKB Helix 381 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QB7 +##sequence-region P20457 1 528 +P20457 UniProtKB Chain 1 528 . . . ID=PRO_0000046776;Note=DNA primase large subunit +P20457 UniProtKB Region 210 239 . . . Note=H-T-H-like motif;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20457 UniProtKB Metal binding 336 336 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20404922;Dbxref=PMID:20404922 +P20457 UniProtKB Metal binding 417 417 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20404922;Dbxref=PMID:20404922 +P20457 UniProtKB Metal binding 434 434 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20404922;Dbxref=PMID:20404922 +P20457 UniProtKB Metal binding 474 474 . . . Note=Iron-sulfur (4Fe-4S);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20404922;Dbxref=PMID:20404922 +P20457 UniProtKB Mutagenesis 152 152 . . . Note=Temperature-sensitive. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2023935;Dbxref=PMID:2023935 +P20457 UniProtKB Mutagenesis 336 336 . . . Note=Mild disruption of iron-sulfur-binding. Strong disruption of iron-sulfur-binding%3B when associated with S-474. Strong disruption of iron-sulfur-binding%2C leading to destabilization of the protein and preventing its purification%3B when associated with S-417 or S-434. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17704817;Dbxref=PMID:17704817 +P20457 UniProtKB Mutagenesis 401 401 . . . Note=Lethal. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2023935;Dbxref=PMID:2023935 +P20457 UniProtKB Mutagenesis 417 417 . . . Note=Mild disruption of iron-sulfur-binding. Strong disruption of iron-sulfur-binding%2C leading to destabilization of the protein and preventing its purification%3B when associated with S-336. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17704817;Dbxref=PMID:17704817 +P20457 UniProtKB Mutagenesis 434 434 . . . Note=Mild disruption of iron-sulfur-binding. Strong disruption of iron-sulfur-binding%2C leading to destabilization of the protein and preventing its purification%3B when associated with S-336. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17704817;Dbxref=PMID:17704817 +P20457 UniProtKB Mutagenesis 434 434 . . . Note=Temperature-sensitive. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17704817;Dbxref=PMID:17704817 +P20457 UniProtKB Mutagenesis 474 474 . . . Note=Mild disruption of iron-sulfur-binding. Strong disruption of iron-sulfur-binding%3B when associated with S-336. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17704817;Dbxref=PMID:17704817 +P20457 UniProtKB Helix 323 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB +P20457 UniProtKB Helix 327 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB +P20457 UniProtKB Helix 335 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB +P20457 UniProtKB Helix 352 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB +P20457 UniProtKB Helix 369 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB +P20457 UniProtKB Helix 388 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB +P20457 UniProtKB Helix 396 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB +P20457 UniProtKB Helix 417 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB +P20457 UniProtKB Helix 435 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB +P20457 UniProtKB Helix 441 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB +P20457 UniProtKB Helix 455 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB +P20457 UniProtKB Helix 470 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB +P20457 UniProtKB Helix 500 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LGB +##sequence-region Q12459 1 698 +Q12459 UniProtKB Chain 1 698 . . . ID=PRO_0000262750;Note=Pheromone-regulated protein PRM7 +Q12459 UniProtKB Compositional bias 6 520 . . . Note=Ser-rich +Q12459 UniProtKB Compositional bias 11 372 . . . Note=Thr-rich +##sequence-region P38876 1 190 +P38876 UniProtKB Chain 1 190 . . . ID=PRO_0000187867;Note=Peptidyl-tRNA hydrolase +##sequence-region P32857 1 523 +P32857 UniProtKB Signal peptide 1 26 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32857 UniProtKB Chain 27 523 . . . ID=PRO_0000022180;Note=Membrane protein PTM1 +P32857 UniProtKB Topological domain 27 197 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32857 UniProtKB Transmembrane 198 218 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32857 UniProtKB Topological domain 219 230 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32857 UniProtKB Transmembrane 231 251 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32857 UniProtKB Topological domain 252 265 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32857 UniProtKB Transmembrane 266 286 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32857 UniProtKB Topological domain 287 304 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32857 UniProtKB Transmembrane 305 325 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32857 UniProtKB Topological domain 326 333 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32857 UniProtKB Transmembrane 334 354 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32857 UniProtKB Topological domain 355 381 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32857 UniProtKB Transmembrane 382 402 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32857 UniProtKB Topological domain 403 417 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32857 UniProtKB Transmembrane 418 438 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32857 UniProtKB Topological domain 439 523 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32857 UniProtKB Modified residue 480 480 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32857 UniProtKB Modified residue 483 483 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32857 UniProtKB Modified residue 498 498 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32857 UniProtKB Glycosylation 132 132 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07350 1 266 +Q07350 UniProtKB Chain 1 266 . . . ID=PRO_0000174317;Note=Pre-mRNA-splicing factor PRP11 +Q07350 UniProtKB Zinc finger 66 96 . . . Note=Matrin-type +Q07350 UniProtKB Compositional bias 12 15 . . . Note=Poly-Gly +Q07350 UniProtKB Beta strand 153 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +Q07350 UniProtKB Beta strand 162 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +Q07350 UniProtKB Beta strand 179 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +Q07350 UniProtKB Beta strand 197 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +Q07350 UniProtKB Beta strand 204 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +Q07350 UniProtKB Helix 235 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +Q07350 UniProtKB Beta strand 241 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +Q07350 UniProtKB Turn 245 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +Q07350 UniProtKB Beta strand 249 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +##sequence-region P40968 1 455 +P40968 UniProtKB Chain 1 455 . . . ID=PRO_0000051144;Note=Pre-mRNA-processing factor 17 +P40968 UniProtKB Repeat 160 200 . . . Note=WD 1 +P40968 UniProtKB Repeat 204 243 . . . Note=WD 2 +P40968 UniProtKB Repeat 291 330 . . . Note=WD 3 +P40968 UniProtKB Repeat 334 373 . . . Note=WD 4 +P40968 UniProtKB Repeat 379 422 . . . Note=WD 5 +P40968 UniProtKB Repeat 424 454 . . . Note=WD 6 +P40968 UniProtKB Sequence conflict 390 390 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40968 UniProtKB Helix 53 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Turn 66 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 153 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 168 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Turn 172 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 177 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 183 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 188 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 198 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 211 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 216 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 226 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 230 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Turn 235 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 239 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 253 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Turn 258 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 262 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 270 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 287 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 296 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 303 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 308 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 317 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Turn 322 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 326 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 342 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 352 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 361 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 381 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 387 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 394 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Turn 403 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 408 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Helix 424 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 429 434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 442 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Turn 447 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40968 UniProtKB Beta strand 450 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P23394 1 588 +P23394 UniProtKB Chain 1 588 . . . ID=PRO_0000055127;Note=Pre-mRNA-splicing ATP-dependent RNA helicase PRP28 +P23394 UniProtKB Domain 208 399 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P23394 UniProtKB Domain 427 579 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P23394 UniProtKB Nucleotide binding 221 228 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P23394 UniProtKB Motif 172 202 . . . Note=Q motif +P23394 UniProtKB Motif 341 344 . . . Note=DEAD box +P23394 UniProtKB Modified residue 69 69 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P23394 UniProtKB Mutagenesis 221 221 . . . Note=In PRP28-103%3B no growth at 15 and 37 degrees Celsius. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 223 223 . . . Note=In PRP28-117%3B no growth at 15 degrees Celsius. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 264 264 . . . Note=Lethal. R->D%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 265 265 . . . Note=In PRP28-99%3B no growth at 15 and 37 degrees Celsius. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 297 297 . . . Note=In PRP28-1%3B no growth at 15 degrees Celsius. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2010088;Dbxref=PMID:2010088 +P23394 UniProtKB Mutagenesis 317 317 . . . Note=In PRP28-36%3B slow growth at 30 degrees Celsius%2C and no growth at 15 and 37 degrees Celsius. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 317 317 . . . Note=Lethal. T->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 319 319 . . . Note=No growth at 15 and 37 degrees Celsius. G->E%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 376 376 . . . Note=In PRP28-32%3B no growth at 15 degrees Celsius. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 379 379 . . . Note=In PRP28-102%3B no growth at 25 degrees Celsius or lower. A->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 438 438 . . . Note=In PRP28-61%3B no growth at 37 degrees Celsius%3B when associated with L-468 and D-486. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 440 440 . . . Note=In PRP28-56%3B no growth at 37 degrees Celsius%3B when associated with S-546 and E-584. I->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 442 442 . . . Note=In PRP28-101%3B no growth at 15 and 37 degrees Celsius. F->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 442 442 . . . Note=In PRP28-55%3B no growth at 37 degrees Celsius. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 449 449 . . . Note=In PRP28-66%3B no growth at 37 degrees Celsius%3B when associated with A-541%3B V-549%3B N-580 and V-586. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 468 468 . . . Note=In PRP28-61%3B no growth at 37 degrees Celsius%3B when associated with L-438 and D-486. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 486 486 . . . Note=In PRP28-61%3B no growth at 37 degrees Celsius%3B when associated with L-438 and L-468. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 491 491 . . . Note=In PRP28-52%3B no growth at 37 degrees Celsius. M->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 499 499 . . . Note=In PRP28-86%3B lethal. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 499 499 . . . Note=No growth at 15 degrees Celsius. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 502 502 . . . Note=Lethal. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 521 521 . . . Note=In PRP28-37%3B no growth at 37 degrees Celsius. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 527 527 . . . Note=Lethal. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 541 541 . . . Note=In PRP28-66%3B no growth at 37 degrees Celsius%3B when associated with T-449%3B V-549%3B N-580 and V-586. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 546 546 . . . Note=In PRP28-56%3B no growth at 37 degrees Celsius%3B when associated with F-440 and E-584. D->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 549 549 . . . Note=In PRP28-66%3B no growth at 37 degrees Celsius%3B when associated with T-449%3B A-541%3B N-580 and V-586. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 580 580 . . . Note=In PRP28-66%3B no growth at 37 degrees Celsius%3B when associated with T-449%3B A-541%3B V-549 and V-586. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 584 584 . . . Note=In PRP28-56%3B no growth at 37 degrees Celsius%3B when associated with F-440 and S-546. N->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Mutagenesis 586 586 . . . Note=In PRP28-66%3B no growth at 37 degrees Celsius%3B when associated with T-449%3B A-541%3B V-549 and N-580. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9396812;Dbxref=PMID:9396812 +P23394 UniProtKB Sequence conflict 493 493 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23394 UniProtKB Helix 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Helix 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Helix 148 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Beta strand 160 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Beta strand 172 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Helix 182 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Helix 199 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Beta strand 217 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Helix 227 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Helix 247 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Beta strand 256 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Helix 264 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Beta strand 284 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Beta strand 291 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Helix 300 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Beta strand 312 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Helix 318 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Beta strand 337 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Helix 343 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Helix 352 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Beta strand 373 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Helix 383 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Beta strand 397 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Beta strand 410 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Helix 421 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Beta strand 439 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Helix 446 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Beta strand 464 467 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Helix 473 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Beta strand 487 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Turn 495 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Beta strand 506 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Helix 518 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Beta strand 534 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Helix 547 559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +P23394 UniProtKB Helix 570 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4W7S +##sequence-region P25043 1 261 +P25043 UniProtKB Propeptide 1 29 . . . ID=PRO_0000026657;Note=Removed in mature form +P25043 UniProtKB Chain 30 261 . . . ID=PRO_0000026658;Note=Proteasome subunit beta type-2 +P25043 UniProtKB Active site 30 30 . . . Note=Nucleophile;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9087403;Dbxref=PMID:9087403 +P25043 UniProtKB Beta strand 23 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FGI +P25043 UniProtKB Beta strand 32 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25043 UniProtKB Beta strand 40 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25043 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25043 UniProtKB Beta strand 54 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25043 UniProtKB Beta strand 63 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25043 UniProtKB Beta strand 70 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25043 UniProtKB Helix 78 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25043 UniProtKB Helix 105 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25043 UniProtKB Turn 119 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25043 UniProtKB Beta strand 125 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25043 UniProtKB Beta strand 136 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25043 UniProtKB Turn 144 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G0U +P25043 UniProtKB Beta strand 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25043 UniProtKB Beta strand 152 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25043 UniProtKB Helix 160 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25043 UniProtKB Helix 177 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25043 UniProtKB Beta strand 202 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25043 UniProtKB Beta strand 213 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25043 UniProtKB Beta strand 241 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +##sequence-region P22141 1 198 +P22141 UniProtKB Chain 1 198 . . . ID=PRO_0000148055;Note=Proteasome subunit beta type-4 +P22141 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P22141 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P22141 UniProtKB Sequence conflict 183 183 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22141 UniProtKB Sequence conflict 188 188 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22141 UniProtKB Beta strand 4 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P22141 UniProtKB Beta strand 13 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P22141 UniProtKB Beta strand 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P22141 UniProtKB Beta strand 26 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P22141 UniProtKB Beta strand 35 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P22141 UniProtKB Beta strand 42 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P22141 UniProtKB Helix 50 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P22141 UniProtKB Helix 77 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P22141 UniProtKB Beta strand 94 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P22141 UniProtKB Beta strand 100 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P22141 UniProtKB Turn 109 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P22141 UniProtKB Beta strand 113 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P22141 UniProtKB Turn 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G65 +P22141 UniProtKB Beta strand 125 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P22141 UniProtKB Beta strand 129 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P22141 UniProtKB Helix 136 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P22141 UniProtKB Helix 154 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P22141 UniProtKB Beta strand 179 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P22141 UniProtKB Beta strand 188 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P22141 UniProtKB Turn 194 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HNP +##sequence-region P30656 1 287 +P30656 UniProtKB Propeptide 1 75 . . . ID=PRO_0000026611;Note=Removed in mature form;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7781614;Dbxref=PMID:7781614 +P30656 UniProtKB Chain 76 287 . . . ID=PRO_0000026612;Note=Proteasome subunit beta type-5 +P30656 UniProtKB Active site 76 76 . . . Note=Nucleophile;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9087403;Dbxref=PMID:9087403 +P30656 UniProtKB Binding site 124 124 . . . Note=Bortezomib%3B via amide nitrogen +P30656 UniProtKB Mutagenesis 126 126 . . . Note=In DOA3-1%3B decrease in activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7781614;Dbxref=PMID:7781614 +P30656 UniProtKB Sequence conflict 282 287 . . . Note=FNNVIG->STTLLAK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P30656 UniProtKB Beta strand 78 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30656 UniProtKB Beta strand 86 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30656 UniProtKB Beta strand 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30656 UniProtKB Beta strand 100 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30656 UniProtKB Beta strand 109 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30656 UniProtKB Beta strand 116 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30656 UniProtKB Beta strand 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GPJ +P30656 UniProtKB Helix 124 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30656 UniProtKB Helix 151 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30656 UniProtKB Turn 165 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30656 UniProtKB Beta strand 172 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30656 UniProtKB Turn 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30656 UniProtKB Beta strand 184 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30656 UniProtKB Turn 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G0U +P30656 UniProtKB Beta strand 196 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30656 UniProtKB Beta strand 200 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30656 UniProtKB Helix 208 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30656 UniProtKB Helix 225 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30656 UniProtKB Beta strand 243 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EU2 +P30656 UniProtKB Beta strand 248 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30656 UniProtKB Beta strand 259 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P30656 UniProtKB Helix 268 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +##sequence-region P23724 1 241 +P23724 UniProtKB Propeptide 1 19 . . . ID=PRO_0000331489 +P23724 UniProtKB Chain 20 241 . . . ID=PRO_0000148042;Note=Proteasome subunit beta type-6 +P23724 UniProtKB Beta strand 30 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23724 UniProtKB Beta strand 40 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23724 UniProtKB Beta strand 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23724 UniProtKB Beta strand 53 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23724 UniProtKB Beta strand 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R18 +P23724 UniProtKB Beta strand 70 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23724 UniProtKB Helix 77 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23724 UniProtKB Turn 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23724 UniProtKB Helix 105 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23724 UniProtKB Turn 118 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23724 UniProtKB Beta strand 126 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23724 UniProtKB Beta strand 139 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23724 UniProtKB Beta strand 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MG0 +P23724 UniProtKB Beta strand 150 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23724 UniProtKB Helix 162 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23724 UniProtKB Turn 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QVP +P23724 UniProtKB Beta strand 186 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R17 +P23724 UniProtKB Helix 196 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23724 UniProtKB Beta strand 214 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G65 +P23724 UniProtKB Beta strand 219 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23724 UniProtKB Beta strand 230 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +##sequence-region P53043 1 513 +P53043 UniProtKB Chain 1 513 . . . ID=PRO_0000058898;Note=Serine/threonine-protein phosphatase T +P53043 UniProtKB Repeat 12 45 . . . Note=TPR 1 +P53043 UniProtKB Repeat 46 79 . . . Note=TPR 2 +P53043 UniProtKB Repeat 80 113 . . . Note=TPR 3 +P53043 UniProtKB Region 188 513 . . . Note=Catalytic +P53043 UniProtKB Active site 311 311 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53043 UniProtKB Metal binding 249 249 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53043 UniProtKB Metal binding 251 251 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53043 UniProtKB Metal binding 278 278 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53043 UniProtKB Metal binding 278 278 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53043 UniProtKB Metal binding 310 310 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53043 UniProtKB Metal binding 359 359 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53043 UniProtKB Metal binding 434 434 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53043 UniProtKB Mutagenesis 311 311 . . . Note=Loss of phosphatase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16407978;Dbxref=PMID:16407978 +P53043 UniProtKB Helix 192 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Helix 203 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Helix 211 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Beta strand 230 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Beta strand 237 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Beta strand 243 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Helix 254 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Beta strand 271 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Beta strand 280 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Helix 286 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Turn 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Beta strand 304 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Helix 314 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Helix 322 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Helix 332 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Beta strand 347 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Turn 352 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Beta strand 355 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Helix 370 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Beta strand 384 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Helix 387 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Beta strand 398 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Beta strand 411 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Helix 415 424 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Beta strand 428 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Beta strand 439 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Helix 445 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Beta strand 449 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Helix 458 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Beta strand 465 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Turn 480 482 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Beta strand 488 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +P53043 UniProtKB Turn 503 506 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ICF +##sequence-region P33329 1 710 +P33329 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33329 UniProtKB Chain 2 710 . . . ID=PRO_0000058892;Note=Serine/threonine-protein phosphatase PP-Z2 +P33329 UniProtKB Compositional bias 346 353 . . . Note=Poly-Ser +P33329 UniProtKB Active site 515 515 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33329 UniProtKB Metal binding 454 454 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33329 UniProtKB Metal binding 456 456 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33329 UniProtKB Metal binding 482 482 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33329 UniProtKB Metal binding 482 482 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33329 UniProtKB Metal binding 514 514 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33329 UniProtKB Metal binding 563 563 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33329 UniProtKB Metal binding 638 638 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33329 UniProtKB Modified residue 55 55 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26570 +P33329 UniProtKB Modified residue 71 71 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33329 UniProtKB Modified residue 161 161 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26570 +P33329 UniProtKB Modified residue 203 203 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P33329 UniProtKB Modified residue 224 224 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33329 UniProtKB Modified residue 271 271 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26570 +P33329 UniProtKB Modified residue 275 275 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26570 +P33329 UniProtKB Modified residue 310 310 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33329 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33329 UniProtKB Sequence conflict 231 231 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P10363 1 409 +P10363 UniProtKB Chain 1 409 . . . ID=PRO_0000046736;Note=DNA primase small subunit +P10363 UniProtKB Motif 123 133 . . . Note=Zinc knuckle motif +P10363 UniProtKB Active site 46 46 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10363 UniProtKB Active site 111 111 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10363 UniProtKB Active site 113 113 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10363 UniProtKB Mutagenesis 184 184 . . . Note=Temperature-sensitive. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2023935;Dbxref=PMID:2023935 +P10363 UniProtKB Mutagenesis 316 316 . . . Note=Cold-sensitive. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2023935;Dbxref=PMID:2023935 +P10363 UniProtKB Sequence conflict 231 232 . . . Note=EQ->DE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10363 UniProtKB Helix 12 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 25 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Beta strand 34 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 40 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Beta strand 45 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Beta strand 56 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 65 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Beta strand 78 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Beta strand 103 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Beta strand 108 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 114 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Turn 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 131 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Beta strand 157 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Beta strand 163 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 174 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 181 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Beta strand 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 211 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 224 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 228 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 238 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 252 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 270 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Beta strand 287 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 290 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 315 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Turn 333 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 348 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 354 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +P10363 UniProtKB Helix 367 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LIM +P10363 UniProtKB Helix 373 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MM2 +##sequence-region P40494 1 810 +P40494 UniProtKB Chain 1 810 . . . ID=PRO_0000086581;Note=Actin-regulating kinase PRK1 +P40494 UniProtKB Domain 22 298 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P40494 UniProtKB Nucleotide binding 28 36 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P40494 UniProtKB Region 743 756 . . . Note=Interaction with SH3 domain of ABP1 +P40494 UniProtKB Active site 158 158 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P40494 UniProtKB Binding site 56 56 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P40494 UniProtKB Modified residue 402 402 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40494 UniProtKB Modified residue 428 428 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40494 UniProtKB Modified residue 484 484 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40494 UniProtKB Modified residue 553 553 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40494 UniProtKB Modified residue 556 556 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40494 UniProtKB Mutagenesis 56 56 . . . Note=Abolishes protein kinase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10087264;Dbxref=PMID:10087264 +P40494 UniProtKB Sequence conflict 786 786 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53835 1 661 +P53835 UniProtKB Chain 1 661 . . . ID=PRO_0000203377;Note=Plasma membrane fusion protein PRM1 +P53835 UniProtKB Topological domain 1 16 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Transmembrane 17 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Topological domain 38 105 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Transmembrane 106 126 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Topological domain 127 296 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Transmembrane 297 317 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Topological domain 318 424 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Transmembrane 425 445 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Topological domain 446 629 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Transmembrane 630 650 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Topological domain 651 661 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Glycosylation 135 135 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Glycosylation 145 145 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Glycosylation 188 188 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Glycosylation 197 197 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Glycosylation 231 231 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Glycosylation 252 252 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Glycosylation 272 272 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Glycosylation 280 280 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Glycosylation 490 490 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Glycosylation 505 505 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Glycosylation 512 512 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Glycosylation 531 531 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Glycosylation 573 573 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53835 UniProtKB Glycosylation 587 587 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P49704 1 494 +P49704 UniProtKB Chain 1 494 . . . ID=PRO_0000058589;Note=Pre-mRNA-processing factor 31 +P49704 UniProtKB Domain 225 346 . . . Note=Nop;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00690 +P49704 UniProtKB Coiled coil 88 122 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49704 UniProtKB Coiled coil 191 225 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49704 UniProtKB Site 257 257 . . . Note=Interaction with U4 snRNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P49704 UniProtKB Sequence conflict 31 31 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P28004 1 379 +P28004 UniProtKB Chain 1 379 . . . ID=PRO_0000084825;Note=Pre-mRNA-processing protein 45 +P28004 UniProtKB Helix 31 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28004 UniProtKB Turn 35 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28004 UniProtKB Helix 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28004 UniProtKB Turn 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28004 UniProtKB Helix 63 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28004 UniProtKB Helix 90 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28004 UniProtKB Beta strand 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28004 UniProtKB Beta strand 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28004 UniProtKB Helix 159 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28004 UniProtKB Helix 182 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P28004 UniProtKB Helix 199 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P19735 1 899 +P19735 UniProtKB Chain 1 899 . . . ID=PRO_0000205756;Note=Pre-mRNA-splicing factor 6 +P19735 UniProtKB Repeat 221 253 . . . Note=HAT 1 +P19735 UniProtKB Repeat 255 287 . . . Note=HAT 2 +P19735 UniProtKB Repeat 289 318 . . . Note=HAT 3 +P19735 UniProtKB Repeat 319 350 . . . Note=HAT 4 +P19735 UniProtKB Repeat 352 381 . . . Note=HAT 5 +P19735 UniProtKB Repeat 383 414 . . . Note=HAT 6 +P19735 UniProtKB Repeat 493 525 . . . Note=HAT 7 +P19735 UniProtKB Repeat 545 578 . . . Note=HAT 8 +P19735 UniProtKB Repeat 608 645 . . . Note=HAT 9 +P19735 UniProtKB Repeat 648 680 . . . Note=HAT 10 +P19735 UniProtKB Repeat 682 714 . . . Note=HAT 11 +P19735 UniProtKB Repeat 751 783 . . . Note=HAT 12 +P19735 UniProtKB Repeat 819 851 . . . Note=HAT 13 +##sequence-region P33334 1 2413 +P33334 UniProtKB Chain 1 2413 . . . ID=PRO_0000097042;Note=Pre-mRNA-splicing factor 8 +P33334 UniProtKB Domain 2182 2311 . . . Note=MPN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182 +P33334 UniProtKB Region 253 543 . . . Note=SNU114/CWC21 interacting domain (SCwid) +P33334 UniProtKB Region 885 1375 . . . Note=Reverse transcriptase homology domain +P33334 UniProtKB Region 1376 1649 . . . Note=Linker +P33334 UniProtKB Region 1585 1598 . . . Note=Important for branch point selection +P33334 UniProtKB Region 1653 1824 . . . Note=Restriction endonuclease homology domain +P33334 UniProtKB Region 1839 2092 . . . Note=RNase H homology domain +P33334 UniProtKB Compositional bias 5 9 . . . Note=Poly-Pro +P33334 UniProtKB Compositional bias 20 27 . . . Note=Poly-Pro +P33334 UniProtKB Compositional bias 50 56 . . . Note=Poly-Pro +P33334 UniProtKB Compositional bias 72 78 . . . Note=Poly-Pro +P33334 UniProtKB Mutagenesis 1658 1658 . . . Note=No effect on viability. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23354046;Dbxref=PMID:23354046 +P33334 UniProtKB Mutagenesis 1684 1684 . . . Note=No effect on viability. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23354046;Dbxref=PMID:23354046 +P33334 UniProtKB Mutagenesis 1687 1687 . . . Note=No effect on viability. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23354046;Dbxref=PMID:23354046 +P33334 UniProtKB Mutagenesis 1700 1700 . . . Note=No effect on viability. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23354046;Dbxref=PMID:23354046 +P33334 UniProtKB Mutagenesis 1735 1735 . . . Note=No effect on viability. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23354046;Dbxref=PMID:23354046 +P33334 UniProtKB Mutagenesis 1853 1853 . . . Note=Alters protein folding. Severely impaired growth. Strongly reduced growth at 35 degrees Celsius%3B when associated with A-1854. D->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18779563,ECO:0000269|PubMed:18836455,ECO:0000269|PubMed:18843295;Dbxref=PMID:18779563,PMID:18836455,PMID:18843295 +P33334 UniProtKB Mutagenesis 1853 1853 . . . Note=Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. D->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18779563,ECO:0000269|PubMed:18836455,ECO:0000269|PubMed:18843295;Dbxref=PMID:18779563,PMID:18836455,PMID:18843295 +P33334 UniProtKB Mutagenesis 1854 1854 . . . Note=Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. Strongly reduced growth at 35 degrees Celsius%3B when associated with A-1853. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18836455,ECO:0000269|PubMed:18843295;Dbxref=PMID:18836455,PMID:18843295 +P33334 UniProtKB Mutagenesis 1854 1854 . . . Note=Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18836455,ECO:0000269|PubMed:18843295;Dbxref=PMID:18836455,PMID:18843295 +P33334 UniProtKB Mutagenesis 1855 1855 . . . Note=Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18843295;Dbxref=PMID:18843295 +P33334 UniProtKB Mutagenesis 1936 1936 . . . Note=Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18843295;Dbxref=PMID:18843295 +P33334 UniProtKB Mutagenesis 1937 1937 . . . Note=Severely impaired growth. Reduced growth at 30 degrees Celsius. Strongly reduced growth at 16 degrees Celsius. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18843295;Dbxref=PMID:18843295 +P33334 UniProtKB Sequence conflict 388 420 . . . Note=PHLYNSRPRSVRIPWYNNPVSCIIQNDEEYDTP->LIYIIPGPVQCAYHGIIIQCRVLSRTMRSTTRL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33334 UniProtKB Sequence conflict 1132 1132 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33334 UniProtKB Sequence conflict 1575 1575 . . . Note=W->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33334 UniProtKB Helix 136 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 155 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 165 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 168 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Beta strand 188 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Beta strand 200 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 210 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Beta strand 239 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Turn 251 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Turn 272 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Beta strand 282 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Beta strand 290 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 305 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 316 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 325 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 333 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 370 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 381 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 388 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Beta strand 392 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Beta strand 417 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Turn 461 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 473 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 484 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 496 498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 503 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Beta strand 512 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 516 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Turn 541 544 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 547 551 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Beta strand 557 563 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 564 585 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Beta strand 590 593 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Beta strand 599 603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 607 612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 617 640 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 647 663 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 666 668 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 671 673 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 674 689 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Beta strand 697 699 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 705 735 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Turn 747 749 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 750 769 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 776 794 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 806 835 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 842 870 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 885 892 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 908 924 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 931 945 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 947 960 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 967 969 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 975 979 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 986 1005 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1013 1015 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1021 1033 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Turn 1036 1039 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1042 1044 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Beta strand 1046 1053 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Turn 1056 1060 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1063 1071 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1076 1085 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1087 1092 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1095 1098 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1110 1135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1138 1140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZEF +P33334 UniProtKB Helix 1150 1154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1156 1164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1167 1174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1176 1189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Turn 1197 1200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1205 1207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 1209 1211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1217 1231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Turn 1236 1238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1243 1245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1246 1252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1258 1262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1265 1271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1272 1274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1283 1289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Turn 1291 1293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1295 1304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1306 1320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1328 1346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1348 1351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1354 1375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Turn 1380 1382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 1385 1389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1392 1394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1409 1412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1414 1417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1422 1425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1427 1429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1434 1436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZEF +P33334 UniProtKB Helix 1440 1443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1447 1470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1477 1479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Turn 1480 1482 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Turn 1487 1490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1491 1495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1499 1502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1508 1514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1515 1517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1530 1533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1540 1549 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1552 1558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1559 1561 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Helix 1563 1565 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1603 1614 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Turn 1617 1619 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1624 1626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Beta strand 1628 1630 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P33334 UniProtKB Beta strand 1633 1636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1641 1648 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Turn 1649 1652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1653 1670 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Turn 1671 1677 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1678 1683 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1690 1692 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1700 1711 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1726 1739 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1743 1745 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1748 1759 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1763 1766 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1768 1778 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Turn 1779 1782 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Beta strand 1783 1788 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1794 1808 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1810 1822 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Turn 1837 1839 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1840 1844 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Beta strand 1845 1847 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Beta strand 1849 1853 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Beta strand 1857 1864 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Beta strand 1866 1868 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ILG +P33334 UniProtKB Beta strand 1870 1875 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Beta strand 1877 1882 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Turn 1884 1886 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Beta strand 1888 1894 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Helix 1896 1899 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Helix 1905 1923 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Helix 1926 1928 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Beta strand 1931 1937 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Helix 1938 1940 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Helix 1941 1947 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Turn 1948 1950 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Beta strand 1954 1957 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Beta strand 1959 1961 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 1965 1970 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Helix 1972 1980 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Beta strand 1985 1990 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Turn 1991 1994 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Helix 1995 1997 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Helix 2001 2017 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Helix 2019 2026 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Beta strand 2030 2032 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3E9P +P33334 UniProtKB Beta strand 2039 2041 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ILH +P33334 UniProtKB Helix 2045 2067 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Helix 2071 2073 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ILH +P33334 UniProtKB Helix 2076 2084 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBT +P33334 UniProtKB Helix 2149 2159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Helix 2160 2167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Beta strand 2168 2171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Beta strand 2178 2180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P33334 UniProtKB Beta strand 2182 2186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Helix 2187 2195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Beta strand 2199 2201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Beta strand 2204 2211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Beta strand 2218 2225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Beta strand 2229 2231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Beta strand 2236 2238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Beta strand 2245 2247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZEF +P33334 UniProtKB Beta strand 2254 2264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Helix 2271 2281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Turn 2282 2284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Beta strand 2289 2296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Beta strand 2299 2307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Helix 2309 2316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Turn 2317 2320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SBG +P33334 UniProtKB Turn 2323 2325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BGD +P33334 UniProtKB Helix 2331 2333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Beta strand 2334 2345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Beta strand 2348 2352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Helix 2360 2362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I43 +P33334 UniProtKB Helix 2363 2365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Beta strand 2374 2376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Helix 2385 2387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OG4 +P33334 UniProtKB Helix 2389 2396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5DCA +P33334 UniProtKB Turn 2406 2408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M52 +##sequence-region P21243 1 252 +P21243 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P21243 UniProtKB Chain 2 252 . . . ID=PRO_0000124141;Note=Proteasome subunit alpha type-1 +P21243 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P21243 UniProtKB Modified residue 237 237 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P21243 UniProtKB Cross-link 232 232 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P21243 UniProtKB Helix 11 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Beta strand 16 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Turn 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD2 +P21243 UniProtKB Helix 26 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Turn 35 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Beta strand 42 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Beta strand 48 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Beta strand 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D29 +P21243 UniProtKB Helix 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Beta strand 71 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Beta strand 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Beta strand 80 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Helix 87 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Helix 114 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Beta strand 131 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QVP +P21243 UniProtKB Beta strand 140 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Turn 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Beta strand 151 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Turn 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G0U +P21243 UniProtKB Beta strand 163 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Helix 175 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Beta strand 191 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Helix 199 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Beta strand 222 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Beta strand 232 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Helix 238 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21243 UniProtKB Turn 249 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G65 +##sequence-region P21242 1 288 +P21242 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:1697860;Dbxref=PMID:22814378,PMID:1697860 +P21242 UniProtKB Chain 2 288 . . . ID=PRO_0000124102;Note=Probable proteasome subunit alpha type-7 +P21242 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P21242 UniProtKB Helix 8 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R18 +P21242 UniProtKB Beta strand 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4INU +P21242 UniProtKB Beta strand 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QLV +P21242 UniProtKB Helix 22 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21242 UniProtKB Beta strand 37 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21242 UniProtKB Beta strand 45 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21242 UniProtKB Turn 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21242 UniProtKB Beta strand 68 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21242 UniProtKB Turn 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21242 UniProtKB Beta strand 74 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21242 UniProtKB Helix 82 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21242 UniProtKB Helix 109 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21242 UniProtKB Turn 123 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FZC +P21242 UniProtKB Beta strand 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GPT +P21242 UniProtKB Beta strand 134 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21242 UniProtKB Beta strand 145 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21242 UniProtKB Turn 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD2 +P21242 UniProtKB Beta strand 157 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21242 UniProtKB Helix 169 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21242 UniProtKB Helix 189 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21242 UniProtKB Helix 204 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21242 UniProtKB Beta strand 212 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21242 UniProtKB Turn 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21242 UniProtKB Beta strand 227 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P21242 UniProtKB Helix 234 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +##sequence-region P07272 1 904 +P07272 UniProtKB Chain 1 904 . . . ID=PRO_0000114965;Note=Pyrimidine pathway regulatory protein 1 +P07272 UniProtKB DNA binding 34 61 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P07272 UniProtKB Metal binding 34 34 . . . Note=Zinc 1 +P07272 UniProtKB Metal binding 34 34 . . . Note=Zinc 2 +P07272 UniProtKB Metal binding 37 37 . . . Note=Zinc 1 +P07272 UniProtKB Metal binding 44 44 . . . Note=Zinc 1 +P07272 UniProtKB Metal binding 51 51 . . . Note=Zinc 1 +P07272 UniProtKB Metal binding 51 51 . . . Note=Zinc 2 +P07272 UniProtKB Metal binding 54 54 . . . Note=Zinc 2 +P07272 UniProtKB Metal binding 61 61 . . . Note=Zinc 2 +P07272 UniProtKB Helix 35 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PYI +P07272 UniProtKB Helix 52 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PYI +P07272 UniProtKB Beta strand 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PYI +P07272 UniProtKB Turn 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PYI +P07272 UniProtKB Beta strand 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PYI +P07272 UniProtKB Helix 74 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PYI +P07272 UniProtKB Turn 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PYI +##sequence-region P38148 1 807 +P38148 UniProtKB Chain 1 807 . . . ID=PRO_0000094921;Note=Dual specificity protein phosphatase PPS1 +P38148 UniProtKB Region 593 807 . . . Note=Catalytic +P38148 UniProtKB Active site 725 725 . . . Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10044 +##sequence-region P26570 1 692 +P26570 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P26570 UniProtKB Chain 2 692 . . . ID=PRO_0000058891;Note=Serine/threonine-protein phosphatase PP-Z1 +P26570 UniProtKB Compositional bias 2 319 . . . Note=Ser-rich +P26570 UniProtKB Active site 480 480 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26570 UniProtKB Metal binding 419 419 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26570 UniProtKB Metal binding 421 421 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26570 UniProtKB Metal binding 447 447 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26570 UniProtKB Metal binding 447 447 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26570 UniProtKB Metal binding 479 479 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26570 UniProtKB Metal binding 528 528 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26570 UniProtKB Metal binding 603 603 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26570 UniProtKB Modified residue 49 49 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P26570 UniProtKB Modified residue 171 171 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P26570 UniProtKB Modified residue 209 209 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33329 +P26570 UniProtKB Modified residue 222 222 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P26570 UniProtKB Modified residue 261 261 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P26570 UniProtKB Modified residue 265 265 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P26570 UniProtKB Modified residue 690 690 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P26570 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P26570 UniProtKB Sequence conflict 340 340 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P26570 UniProtKB Sequence conflict 440 440 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P26570 UniProtKB Sequence conflict 649 649 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P49960 1 444 +P49960 UniProtKB Chain 1 444 . . . ID=PRO_0000081736;Note=U4/U6 snRNA-associated-splicing factor PRP24 +P49960 UniProtKB Domain 41 116 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P49960 UniProtKB Domain 117 195 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P49960 UniProtKB Domain 210 289 . . . Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P49960 UniProtKB Modified residue 19 19 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P49960 UniProtKB Sequence conflict 197 197 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P49960 UniProtKB Helix 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Beta strand 42 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GO9 +P49960 UniProtKB Helix 54 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Beta strand 67 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Beta strand 78 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 90 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Turn 98 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Beta strand 110 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Beta strand 118 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 130 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Turn 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KH9 +P49960 UniProtKB Beta strand 144 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GHP +P49960 UniProtKB Beta strand 160 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 168 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Beta strand 189 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 204 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Turn 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GHP +P49960 UniProtKB Beta strand 211 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 219 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 224 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 232 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Beta strand 237 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Turn 244 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Beta strand 252 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 263 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 270 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Beta strand 275 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TF6 +P49960 UniProtKB Beta strand 283 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 290 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 307 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Beta strand 313 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 325 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 340 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Beta strand 343 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 350 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Beta strand 354 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 362 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Beta strand 373 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9W +P49960 UniProtKB Beta strand 383 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +P49960 UniProtKB Helix 387 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4N0T +##sequence-region P39682 1 629 +P39682 UniProtKB Chain 1 629 . . . ID=PRO_0000205758;Note=Pre-mRNA-processing factor 39 +P39682 UniProtKB Repeat 68 100 . . . Note=HAT 1 +P39682 UniProtKB Repeat 102 134 . . . Note=HAT 2 +P39682 UniProtKB Repeat 138 173 . . . Note=HAT 3 +P39682 UniProtKB Repeat 175 208 . . . Note=HAT 4 +P39682 UniProtKB Repeat 233 265 . . . Note=HAT 5 +P39682 UniProtKB Repeat 270 302 . . . Note=HAT 6 +P39682 UniProtKB Repeat 446 480 . . . Note=HAT 7 +P39682 UniProtKB Sequence conflict 615 615 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P33203 1 583 +P33203 UniProtKB Chain 1 583 . . . ID=PRO_0000076084;Note=Pre-mRNA-processing protein PRP40 +P33203 UniProtKB Domain 1 31 . . . Note=WW 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00224 +P33203 UniProtKB Domain 42 72 . . . Note=WW 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00224 +P33203 UniProtKB Domain 132 188 . . . Note=FF 1 +P33203 UniProtKB Domain 201 257 . . . Note=FF 2 +P33203 UniProtKB Domain 262 332 . . . Note=FF 3 +P33203 UniProtKB Domain 354 413 . . . Note=FF 4 +P33203 UniProtKB Domain 427 488 . . . Note=FF 5 +P33203 UniProtKB Domain 491 552 . . . Note=FF 6 +P33203 UniProtKB Modified residue 576 576 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33203 UniProtKB Mutagenesis 240 240 . . . Note=In PRP40-1 suppressor%3B affects SAR1 mRNA accumulation in U1-U4 mutant at 18 degrees Celsius. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8622699;Dbxref=PMID:8622699 +P33203 UniProtKB Mutagenesis 274 274 . . . Note=Temperature sensitive growth at 36 degrees Celsius. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15020406;Dbxref=PMID:15020406 +P33203 UniProtKB Mutagenesis 277 277 . . . Note=Temperature sensitive growth at 36 degrees Celsius. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15020406;Dbxref=PMID:15020406 +P33203 UniProtKB Mutagenesis 281 281 . . . Note=Temperature sensitive growth at 36 degrees Celsius. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15020406;Dbxref=PMID:15020406 +P33203 UniProtKB Mutagenesis 340 340 . . . Note=Wild-type growth at 36 degrees Celsius. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15020406;Dbxref=PMID:15020406 +P33203 UniProtKB Mutagenesis 344 344 . . . Note=Wild-type growth at 36 degrees Celsius. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15020406;Dbxref=PMID:15020406 +P33203 UniProtKB Mutagenesis 347 347 . . . Note=Wild-type growth at 36 degrees Celsius. L->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15020406;Dbxref=PMID:15020406 +P33203 UniProtKB Beta strand 4 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O6W +P33203 UniProtKB Beta strand 14 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O6W +P33203 UniProtKB Turn 19 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O6W +P33203 UniProtKB Beta strand 23 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O6W +P33203 UniProtKB Helix 30 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O6W +P33203 UniProtKB Beta strand 46 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O6W +P33203 UniProtKB Beta strand 55 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O6W +P33203 UniProtKB Turn 60 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O6W +P33203 UniProtKB Beta strand 64 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1O6W +P33203 UniProtKB Helix 134 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7E +P33203 UniProtKB Helix 154 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7E +P33203 UniProtKB Helix 167 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7E +P33203 UniProtKB Helix 175 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7E +P33203 UniProtKB Helix 489 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KFD +P33203 UniProtKB Beta strand 510 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KFD +P33203 UniProtKB Helix 519 526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KFD +P33203 UniProtKB Helix 533 535 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KFD +P33203 UniProtKB Helix 539 549 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KFD +##sequence-region P40303 1 254 +P40303 UniProtKB Chain 1 254 . . . ID=PRO_0000124165;Note=Proteasome subunit alpha type-4 +P40303 UniProtKB Modified residue 60 60 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P40303 UniProtKB Beta strand 7 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FNT +P40303 UniProtKB Turn 13 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40303 UniProtKB Helix 18 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40303 UniProtKB Beta strand 33 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40303 UniProtKB Beta strand 42 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40303 UniProtKB Turn 57 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40303 UniProtKB Beta strand 63 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40303 UniProtKB Beta strand 71 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40303 UniProtKB Helix 79 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40303 UniProtKB Helix 106 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40303 UniProtKB Turn 120 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +P40303 UniProtKB Beta strand 123 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FNT +P40303 UniProtKB Beta strand 130 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40303 UniProtKB Beta strand 146 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40303 UniProtKB Turn 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FNT +P40303 UniProtKB Beta strand 156 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40303 UniProtKB Helix 168 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40303 UniProtKB Beta strand 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QVP +P40303 UniProtKB Helix 188 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40303 UniProtKB Beta strand 204 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R17 +P40303 UniProtKB Beta strand 210 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40303 UniProtKB Turn 217 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40303 UniProtKB Beta strand 220 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40303 UniProtKB Helix 226 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40303 UniProtKB Helix 238 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +##sequence-region P38624 1 215 +P38624 UniProtKB Propeptide 1 19 . . . ID=PRO_0000026643;Note=Removed in mature form +P38624 UniProtKB Chain 20 215 . . . ID=PRO_0000026644;Note=Proteasome subunit beta type-1 +P38624 UniProtKB Active site 20 20 . . . Note=Nucleophile;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9087403;Dbxref=PMID:9087403 +P38624 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38624 UniProtKB Helix 6 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FGI +P38624 UniProtKB Beta strand 22 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P38624 UniProtKB Beta strand 30 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P38624 UniProtKB Beta strand 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P38624 UniProtKB Beta strand 44 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P38624 UniProtKB Beta strand 53 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P38624 UniProtKB Beta strand 60 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P38624 UniProtKB Helix 68 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P38624 UniProtKB Helix 94 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P38624 UniProtKB Turn 108 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P38624 UniProtKB Beta strand 114 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P38624 UniProtKB Turn 123 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P38624 UniProtKB Beta strand 126 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P38624 UniProtKB Turn 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JD2 +P38624 UniProtKB Beta strand 139 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P38624 UniProtKB Helix 148 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P38624 UniProtKB Helix 154 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P38624 UniProtKB Helix 167 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P38624 UniProtKB Beta strand 185 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3SDK +P38624 UniProtKB Beta strand 192 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P38624 UniProtKB Beta strand 201 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P38624 UniProtKB Helix 209 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +##sequence-region P25451 1 205 +P25451 UniProtKB Chain 1 205 . . . ID=PRO_0000148070;Note=Proteasome subunit beta type-3 +P25451 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25451 UniProtKB Cross-link 70 70 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25451 UniProtKB Helix 4 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25451 UniProtKB Beta strand 11 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25451 UniProtKB Beta strand 18 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25451 UniProtKB Beta strand 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25451 UniProtKB Beta strand 34 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25451 UniProtKB Beta strand 43 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25451 UniProtKB Beta strand 49 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25451 UniProtKB Helix 57 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25451 UniProtKB Helix 84 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25451 UniProtKB Turn 97 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25451 UniProtKB Beta strand 105 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25451 UniProtKB Turn 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25451 UniProtKB Beta strand 119 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25451 UniProtKB Beta strand 130 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G65 +P25451 UniProtKB Beta strand 134 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25451 UniProtKB Helix 143 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25451 UniProtKB Helix 160 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25451 UniProtKB Beta strand 178 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NNN +P25451 UniProtKB Beta strand 185 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P25451 UniProtKB Beta strand 195 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +##sequence-region P40359 1 213 +P40359 UniProtKB Chain 1 213 . . . ID=PRO_0000194822;Note=DNA replication complex GINS protein PSF2 +##sequence-region Q08217 1 1101 +Q08217 UniProtKB Chain 1 1101 . . . ID=PRO_0000086156;Note=Serine/threonine-protein kinase PSK2 +Q08217 UniProtKB Domain 841 1099 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q08217 UniProtKB Nucleotide binding 847 855 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q08217 UniProtKB Active site 975 975 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q08217 UniProtKB Binding site 870 870 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q08217 UniProtKB Modified residue 118 118 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P14747 1 604 +P14747 UniProtKB Chain 1 604 . . . ID=PRO_0000058837;Note=Serine/threonine-protein phosphatase 2B catalytic subunit A2 +P14747 UniProtKB Region 501 523 . . . Note=Calmodulin-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14747 UniProtKB Active site 205 205 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14747 UniProtKB Metal binding 144 144 . . . Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14747 UniProtKB Metal binding 146 146 . . . Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14747 UniProtKB Metal binding 172 172 . . . Note=Iron;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14747 UniProtKB Metal binding 172 172 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14747 UniProtKB Metal binding 204 204 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14747 UniProtKB Metal binding 253 253 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14747 UniProtKB Metal binding 359 359 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P14747 UniProtKB Modified residue 31 31 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14747 UniProtKB Modified residue 489 489 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14747 UniProtKB Modified residue 520 520 . . . Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14747 UniProtKB Sequence conflict 87 88 . . . Note=EL->DV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14747 UniProtKB Sequence conflict 581 581 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P24031 1 467 +P24031 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P24031 UniProtKB Chain 18 467 . . . ID=PRO_0000023953;Note=Constitutive acid phosphatase +P24031 UniProtKB Active site 75 75 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P24031 UniProtKB Active site 338 338 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P24031 UniProtKB Glycosylation 97 97 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P24031 UniProtKB Glycosylation 103 103 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P24031 UniProtKB Glycosylation 162 162 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P24031 UniProtKB Glycosylation 192 192 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P24031 UniProtKB Glycosylation 250 250 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P24031 UniProtKB Glycosylation 315 315 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P24031 UniProtKB Glycosylation 356 356 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P24031 UniProtKB Glycosylation 390 390 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P24031 UniProtKB Glycosylation 439 439 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P24031 UniProtKB Glycosylation 445 445 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P24031 UniProtKB Glycosylation 456 456 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P24031 UniProtKB Glycosylation 461 461 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P24031 UniProtKB Sequence conflict 219 221 . . . Note=DED->MKT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P52290 1 468 +P52290 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52290 UniProtKB Chain 21 468 . . . ID=PRO_0000023958;Note=Probable acid phosphatase DIA3 +P52290 UniProtKB Active site 76 76 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52290 UniProtKB Active site 339 339 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52290 UniProtKB Glycosylation 98 98 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52290 UniProtKB Glycosylation 163 163 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52290 UniProtKB Glycosylation 193 193 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52290 UniProtKB Glycosylation 202 202 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52290 UniProtKB Glycosylation 238 238 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52290 UniProtKB Glycosylation 251 251 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52290 UniProtKB Glycosylation 316 316 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52290 UniProtKB Glycosylation 357 357 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52290 UniProtKB Glycosylation 391 391 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52290 UniProtKB Glycosylation 457 457 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52290 UniProtKB Glycosylation 462 462 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40347 1 161 +P40347 UniProtKB Chain 1 161 . . . ID=PRO_0000046565;Note=Low molecular weight phosphotyrosine protein phosphatase +P40347 UniProtKB Active site 14 14 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40347 UniProtKB Active site 20 20 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40347 UniProtKB Active site 133 133 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40347 UniProtKB Modified residue 57 57 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40347 UniProtKB Beta strand 8 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q +P40347 UniProtKB Helix 20 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q +P40347 UniProtKB Helix 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q +P40347 UniProtKB Beta strand 41 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q +P40347 UniProtKB Turn 52 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1P +P40347 UniProtKB Helix 60 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q +P40347 UniProtKB Helix 82 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q +P40347 UniProtKB Beta strand 89 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q +P40347 UniProtKB Helix 96 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q +P40347 UniProtKB Beta strand 113 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q +P40347 UniProtKB Helix 117 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q +P40347 UniProtKB Beta strand 124 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q +P40347 UniProtKB Helix 139 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D1Q +##sequence-region P40012 1 539 +P40012 UniProtKB Chain 1 539 . . . ID=PRO_0000135274;Note=Protoporphyrinogen oxidase +P40012 UniProtKB Nucleotide binding 18 23 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40012 UniProtKB Nucleotide binding 43 44 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40012 UniProtKB Nucleotide binding 70 73 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40012 UniProtKB Nucleotide binding 521 523 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40012 UniProtKB Binding site 51 51 . . . Note=FAD%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40012 UniProtKB Binding site 300 300 . . . Note=FAD%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40012 UniProtKB Mutagenesis 422 422 . . . Note=In HEM14-1%3B loss of activity. L->P +P40012 UniProtKB Mutagenesis 424 424 . . . Note=In HEM14-1%3B loss of activity. K->E +##sequence-region P32945 1 549 +P32945 UniProtKB Chain 1 549 . . . ID=PRO_0000058893;Note=Serine/threonine-protein phosphatase PPQ +P32945 UniProtKB Compositional bias 113 219 . . . Note=Ser-rich +P32945 UniProtKB Active site 362 362 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32945 UniProtKB Metal binding 301 301 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32945 UniProtKB Metal binding 303 303 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32945 UniProtKB Metal binding 329 329 . . . Note=Manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32945 UniProtKB Metal binding 329 329 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32945 UniProtKB Metal binding 361 361 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32945 UniProtKB Metal binding 410 410 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32945 UniProtKB Metal binding 485 485 . . . Note=Manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q12036 1 173 +Q12036 UniProtKB Chain 1 173 . . . ID=PRO_0000175745;Note=Mitochondrial holo-[acyl-carrier-protein] synthase +##sequence-region P40534 1 656 +P40534 UniProtKB Chain 1 656 . . . ID=PRO_0000202994;Note=Pheromone-regulated membrane protein 2 +P40534 UniProtKB Transmembrane 16 36 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40534 UniProtKB Transmembrane 320 340 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40534 UniProtKB Transmembrane 422 442 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40534 UniProtKB Transmembrane 634 654 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08931 1 133 +Q08931 UniProtKB Chain 1 133 . . . ID=PRO_0000262749;Note=Pheromone-regulated membrane protein 3 +Q08931 UniProtKB Topological domain 1 104 . . . Note=Nuclear;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08931 UniProtKB Transmembrane 105 127 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08931 UniProtKB Topological domain 128 133 . . . Note=Perinuclear space;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08931 UniProtKB Motif 69 75 . . . Note=Bipartite nuclear localization signal +Q08931 UniProtKB Mutagenesis 106 106 . . . Note=In pmr3-7%3B leads to mislocalization and decreases nuclear fusion efficiency when temperature rises. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19297527;Dbxref=PMID:19297527 +Q08931 UniProtKB Mutagenesis 108 108 . . . Note=In pmr3-1%3B decreases nuclear fusion efficiency. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19297527;Dbxref=PMID:19297527 +Q08931 UniProtKB Mutagenesis 112 112 . . . Note=In pmr3-8%3B leads to mislocalization and decreases nuclear fusion efficiency. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19297527;Dbxref=PMID:19297527 +Q08931 UniProtKB Mutagenesis 114 114 . . . Note=In pmr3-3%3B leads to mislocalization and decreases nuclear fusion efficiency. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19297527;Dbxref=PMID:19297527 +Q08931 UniProtKB Mutagenesis 115 115 . . . Note=In pmr3-5%3B leads to mislocalization and decreases nuclear fusion efficiency. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19297527;Dbxref=PMID:19297527 +Q08931 UniProtKB Mutagenesis 121 121 . . . Note=In pmr3-6%3B leads to mislocalization. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19297527;Dbxref=PMID:19297527 +Q08931 UniProtKB Mutagenesis 122 122 . . . Note=In pmr3-2%3B leads to mislocalization and decreases nuclear fusion efficiency. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19297527;Dbxref=PMID:19297527 +##sequence-region P40476 1 318 +P40476 UniProtKB Chain 1 318 . . . ID=PRO_0000202963;Note=Pheromone-regulated membrane protein 5 +P40476 UniProtKB Transmembrane 75 98 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40476 UniProtKB Compositional bias 17 54 . . . Note=Ser-rich +P40476 UniProtKB Compositional bias 240 246 . . . Note=Poly-Ser +P40476 UniProtKB Modified residue 129 129 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40476 UniProtKB Modified residue 279 279 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40476 UniProtKB Modified residue 282 282 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40476 UniProtKB Modified residue 288 288 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40476 UniProtKB Cross-link 314 314 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P53174 1 237 +P53174 UniProtKB Chain 1 237 . . . ID=PRO_0000207523;Note=Pheromone-regulated membrane protein 8 +P53174 UniProtKB Topological domain 1 47 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53174 UniProtKB Transmembrane 48 68 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53174 UniProtKB Topological domain 69 74 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53174 UniProtKB Transmembrane 75 95 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53174 UniProtKB Topological domain 96 237 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53174 UniProtKB Region 236 237 . . . Note=COPII binding +##sequence-region P07274 1 126 +P07274 UniProtKB Chain 1 126 . . . ID=PRO_0000199608;Note=Profilin +P07274 UniProtKB Helix 3 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR +P07274 UniProtKB Beta strand 17 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR +P07274 UniProtKB Beta strand 29 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR +P07274 UniProtKB Helix 40 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR +P07274 UniProtKB Helix 54 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR +P07274 UniProtKB Beta strand 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR +P07274 UniProtKB Beta strand 66 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR +P07274 UniProtKB Beta strand 75 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR +P07274 UniProtKB Beta strand 85 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR +P07274 UniProtKB Beta strand 93 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR +P07274 UniProtKB Helix 107 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YPR +##sequence-region P15938 1 1071 +P15938 UniProtKB Chain 1 1071 . . . ID=PRO_0000055150;Note=Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16 +P15938 UniProtKB Domain 360 526 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P15938 UniProtKB Domain 540 735 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P15938 UniProtKB Nucleotide binding 373 380 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P15938 UniProtKB Motif 473 476 . . . Note=DEAH box +P15938 UniProtKB Mutagenesis 386 386 . . . Note=Suppressor phenotype. Y->D +P15938 UniProtKB Sequence conflict 698 698 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P33411 1 251 +P33411 UniProtKB Chain 1 251 . . . ID=PRO_0000058586;Note=Pre-mRNA-splicing factor 18 +P33411 UniProtKB Sequence conflict 194 249 . . . Note=PIGVTSVGIHARSAHSKIQGGRNAANIMIDERTRLWITSIKRLITFEEWYTSNHDS->LLVL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33411 UniProtKB Sequence conflict 201 251 . . . Note=GIHARSAHSKIQGGRNAANIMIDERTRLWITSIKRLITFEEWYTSNHDSLA->AFMLVVHIRKFKEAGMLLT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33411 UniProtKB Helix 82 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK +P33411 UniProtKB Helix 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK +P33411 UniProtKB Helix 106 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK +P33411 UniProtKB Helix 127 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK +P33411 UniProtKB Turn 133 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK +P33411 UniProtKB Helix 136 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK +P33411 UniProtKB Helix 157 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK +P33411 UniProtKB Helix 173 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK +P33411 UniProtKB Helix 176 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK +P33411 UniProtKB Helix 224 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DVK +##sequence-region Q00723 1 242 +Q00723 UniProtKB Chain 1 242 . . . ID=PRO_0000058590;Note=Pre-mRNA-splicing factor 38 +Q00723 UniProtKB Compositional bias 217 242 . . . Note=Ser-rich +Q00723 UniProtKB Mutagenesis 87 87 . . . Note=In PRP83-2%3B temperature-sensitive%3B blocks splicing of RPS17A after a 2 hour shift to the restrictive temperature of 37 degrees Celsius%3B spliceosome assembly arrested at the complex I stage. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9582287;Dbxref=PMID:9582287 +##sequence-region Q03776 1 544 +Q03776 UniProtKB Chain 1 544 . . . ID=PRO_0000262751;Note=U1 small nuclear ribonucleoprotein component PRP42 +Q03776 UniProtKB Repeat 7 39 . . . Note=HAT 1 +Q03776 UniProtKB Repeat 51 83 . . . Note=HAT 2 +Q03776 UniProtKB Repeat 85 118 . . . Note=HAT 3 +Q03776 UniProtKB Repeat 121 156 . . . Note=HAT 4 +Q03776 UniProtKB Repeat 163 195 . . . Note=HAT 5 +Q03776 UniProtKB Repeat 255 288 . . . Note=HAT 6 +Q03776 UniProtKB Repeat 290 322 . . . Note=HAT 7 +Q03776 UniProtKB Repeat 366 397 . . . Note=HAT 8 +Q03776 UniProtKB Repeat 456 488 . . . Note=HAT 9 +Q03776 UniProtKB Motif 230 235 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53131 1 767 +P53131 UniProtKB Chain 1 767 . . . ID=PRO_0000055145;Note=Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43 +P53131 UniProtKB Domain 103 268 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P53131 UniProtKB Domain 293 473 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P53131 UniProtKB Nucleotide binding 116 123 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P53131 UniProtKB Motif 215 218 . . . Note=DEAH box +P53131 UniProtKB Modified residue 8 8 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53131 UniProtKB Modified residue 9 9 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53131 UniProtKB Mutagenesis 194 194 . . . Note=In PRP43-DN1%3B dominant-negative phenotype. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9342317;Dbxref=PMID:9342317 +P53131 UniProtKB Mutagenesis 247 247 . . . Note=In PRP43-DN2%3B dominant-negative phenotype. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9342317;Dbxref=PMID:9342317 +P53131 UniProtKB Mutagenesis 395 395 . . . Note=In PRP43-1%3B temperature-sensitive. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9342317;Dbxref=PMID:9342317 +P53131 UniProtKB Beta strand 9 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Turn 14 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 19 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Turn 49 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 60 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Turn 73 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JPT +P53131 UniProtKB Helix 81 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 94 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 99 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 110 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 122 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 136 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 142 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 150 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Turn 169 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 172 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 179 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 187 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 193 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 209 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 217 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 222 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 242 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 253 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 264 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 274 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 286 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 305 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 313 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 339 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 350 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 354 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 364 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 370 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 378 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 388 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 395 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Turn 404 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 408 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 418 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 427 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 430 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 442 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 456 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 463 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 477 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 488 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 512 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 520 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 524 532 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 533 536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 539 549 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 559 561 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JPT +P53131 UniProtKB Helix 562 570 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 578 589 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 592 597 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 599 605 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 610 629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 644 656 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 659 663 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Turn 665 667 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KX2 +P53131 UniProtKB Beta strand 670 672 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Turn 673 675 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 678 681 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Beta strand 692 712 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 715 721 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Turn 723 725 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 728 730 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +P53131 UniProtKB Helix 735 748 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XAU +##sequence-region P21372 1 849 +P21372 UniProtKB Chain 1 849 . . . ID=PRO_0000055126;Note=Pre-mRNA-processing ATP-dependent RNA helicase PRP5 +P21372 UniProtKB Domain 287 467 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P21372 UniProtKB Domain 502 661 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P21372 UniProtKB Nucleotide binding 300 307 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P21372 UniProtKB Coiled coil 13 81 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21372 UniProtKB Motif 90 96 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21372 UniProtKB Motif 255 284 . . . Note=Q motif +P21372 UniProtKB Motif 415 418 . . . Note=DEAD box +P21372 UniProtKB Mutagenesis 293 293 . . . Note=In PRP5-1%3B no growth at 37 degrees Celsius and impairs pre-spliceosome formation in vitro. G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11927574,ECO:0000269|PubMed:8405998;Dbxref=PMID:11927574,PMID:8405998 +P21372 UniProtKB Helix 223 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 230 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Beta strand 243 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 257 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 264 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 281 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Beta strand 296 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 306 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Beta strand 332 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 340 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Beta strand 362 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 372 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Beta strand 383 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 389 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 398 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Beta strand 411 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 417 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 426 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Beta strand 441 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 451 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Beta strand 461 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Beta strand 465 472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Beta strand 479 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 489 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Beta strand 528 533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 535 547 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Beta strand 553 555 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 561 573 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Beta strand 578 582 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 583 586 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Beta strand 595 601 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 606 613 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 614 616 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 619 621 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Beta strand 624 630 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 634 643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 646 650 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +P21372 UniProtKB Helix 654 672 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LJY +##sequence-region P19736 1 530 +P19736 UniProtKB Chain 1 530 . . . ID=PRO_0000174321;Note=Pre-mRNA-splicing factor PRP9 +P19736 UniProtKB Zinc finger 280 310 . . . Note=Matrin-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00130 +P19736 UniProtKB Zinc finger 421 452 . . . Note=Matrin-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00130 +P19736 UniProtKB Helix 3 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 30 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 51 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Beta strand 58 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 69 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 113 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 137 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Beta strand 149 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 166 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Turn 172 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 183 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 200 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 209 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Beta strand 212 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 215 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 227 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 253 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 268 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Turn 276 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Turn 283 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Beta strand 289 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 292 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Beta strand 299 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 302 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 312 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 329 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +P19736 UniProtKB Helix 347 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DGW +##sequence-region Q12310 1 699 +Q12310 UniProtKB Chain 1 699 . . . ID=PRO_0000262752;Note=Serine/threonine-protein kinase PRR2 +Q12310 UniProtKB Domain 361 653 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12310 UniProtKB Nucleotide binding 367 375 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12310 UniProtKB Active site 484 484 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q12310 UniProtKB Binding site 390 390 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12310 UniProtKB Mutagenesis 390 390 . . . Note=Abolishes kinase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11337509;Dbxref=PMID:11337509 +##sequence-region P40327 1 437 +P40327 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901 +P40327 UniProtKB Chain 2 437 . . . ID=PRO_0000084685;Note=26S proteasome regulatory subunit 4 homolog +P40327 UniProtKB Nucleotide binding 223 230 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40327 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901 +P40327 UniProtKB Cross-link 234 234 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P40327 UniProtKB Cross-link 255 255 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P40327 UniProtKB Cross-link 290 290 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P40327 UniProtKB Mutagenesis 229 229 . . . Note=73%25 loss of ATPase activity. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7721833;Dbxref=PMID:7721833 +P40327 UniProtKB Sequence conflict 347 347 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P33297 1 434 +P33297 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:12504901;Dbxref=PMID:22814378,PMID:12504901 +P33297 UniProtKB Chain 2 434 . . . ID=PRO_0000084708;Note=26S proteasome regulatory subunit 6A +P33297 UniProtKB Nucleotide binding 222 229 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33297 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:12504901;Dbxref=PMID:22814378,PMID:12504901 +P33297 UniProtKB Modified residue 180 180 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33297 UniProtKB Helix 356 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHK +P33297 UniProtKB Helix 376 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHK +P33297 UniProtKB Turn 382 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHK +P33297 UniProtKB Helix 388 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHK +P33297 UniProtKB Beta strand 408 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHK +P33297 UniProtKB Helix 412 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WHK +##sequence-region P33298 1 428 +P33298 UniProtKB Chain 1 428 . . . ID=PRO_0000084697;Note=26S proteasome regulatory subunit 6B homolog +P33298 UniProtKB Nucleotide binding 213 220 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33298 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901 +P33298 UniProtKB Cross-link 280 280 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P33298 UniProtKB Sequence conflict 342 342 . . . Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33298 UniProtKB Sequence conflict 342 342 . . . Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33298 UniProtKB Helix 351 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P33298 UniProtKB Helix 368 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZO +P33298 UniProtKB Helix 380 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P33298 UniProtKB Beta strand 400 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +P33298 UniProtKB Helix 404 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DZN +##sequence-region P09232 1 635 +P09232 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P09232 UniProtKB Propeptide 20 280 . . . ID=PRO_0000027136;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3325823;Dbxref=PMID:3325823 +P09232 UniProtKB Chain 281 574 . . . ID=PRO_0000027137;Note=Cerevisin +P09232 UniProtKB Propeptide 575 635 . . . ID=PRO_0000417567 +P09232 UniProtKB Domain 322 568 . . . Note=Peptidase S8 +P09232 UniProtKB Compositional bias 63 154 . . . Note=Lys-rich +P09232 UniProtKB Active site 325 325 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09232 UniProtKB Active site 357 357 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09232 UniProtKB Active site 519 519 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09232 UniProtKB Glycosylation 594 594 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09232 UniProtKB Disulfide bond 460 491 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P09232 UniProtKB Sequence conflict 622 622 . . . Note=F->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09232 UniProtKB Sequence conflict 622 622 . . . Note=F->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P23638 1 258 +P23638 UniProtKB Chain 1 258 . . . ID=PRO_0000124116;Note=Proteasome subunit alpha type-3 +P23638 UniProtKB Cross-link 100 100 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P23638 UniProtKB Cross-link 199 199 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P23638 UniProtKB Cross-link 231 231 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P23638 UniProtKB Helix 4 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Helix 20 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Beta strand 35 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Beta strand 43 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Beta strand 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Helix 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CZ4 +P23638 UniProtKB Beta strand 64 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Helix 81 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Helix 108 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Beta strand 125 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Beta strand 133 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Turn 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Beta strand 145 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Beta strand 157 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Helix 169 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Helix 186 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Beta strand 202 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Helix 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Beta strand 211 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Beta strand 220 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Beta strand 226 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Helix 232 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P23638 UniProtKB Turn 242 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BDM +##sequence-region P53633 1 176 +P53633 UniProtKB Chain 1 176 . . . ID=PRO_0000220887;Note=Prenylated Rab acceptor 1 +P53633 UniProtKB Transmembrane 84 104 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53633 UniProtKB Transmembrane 129 149 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53633 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53633 UniProtKB Modified residue 18 18 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53633 UniProtKB Sequence conflict 29 29 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53633 UniProtKB Sequence conflict 29 29 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P54885 1 456 +P54885 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P54885 UniProtKB Chain 2 456 . . . ID=PRO_0000189824;Note=Gamma-glutamyl phosphate reductase +P54885 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P54885 UniProtKB Helix 3 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Helix 23 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Helix 41 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Helix 62 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Helix 75 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Beta strand 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Beta strand 96 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Beta strand 106 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Beta strand 117 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Helix 127 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Beta strand 142 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Helix 149 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Helix 152 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Beta strand 179 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Helix 190 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Turn 196 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Beta strand 201 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Helix 208 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Beta strand 230 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Helix 240 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Beta strand 262 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Helix 273 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Beta strand 288 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Helix 292 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Helix 310 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Beta strand 335 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Helix 342 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Beta strand 357 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Helix 365 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Beta strand 378 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Helix 386 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Helix 416 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +P54885 UniProtKB Beta strand 419 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1VLU +##sequence-region P32523 1 503 +P32523 UniProtKB Chain 1 503 . . . ID=PRO_0000058587;Note=Pre-mRNA-processing factor 19 +P32523 UniProtKB Domain 1 71 . . . Note=U-box +P32523 UniProtKB Repeat 328 367 . . . Note=WD 1 +P32523 UniProtKB Repeat 372 410 . . . Note=WD 2 +P32523 UniProtKB Repeat 418 458 . . . Note=WD 3 +P32523 UniProtKB Region 57 144 . . . Note=Required for self-association +P32523 UniProtKB Region 76 134 . . . Note=Interaction with CEF1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15601865;Dbxref=PMID:15601865 +P32523 UniProtKB Sequence conflict 239 239 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32523 UniProtKB Turn 4 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BAY +P32523 UniProtKB Beta strand 11 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BAY +P32523 UniProtKB Turn 17 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BAY +P32523 UniProtKB Beta strand 21 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BAY +P32523 UniProtKB Helix 25 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BAY +P32523 UniProtKB Turn 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BAY +P32523 UniProtKB Helix 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2BAY +P32523 UniProtKB Beta strand 57 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P32523 UniProtKB Helix 78 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P32523 UniProtKB Helix 149 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 170 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P32523 UniProtKB Beta strand 179 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 197 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 204 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 219 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 232 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Helix 241 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 247 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Turn 253 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 256 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Turn 262 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 265 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Turn 271 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 275 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 288 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 295 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 301 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 311 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 321 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Turn 327 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P32523 UniProtKB Beta strand 335 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 342 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 354 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Turn 359 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P32523 UniProtKB Beta strand 363 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P32523 UniProtKB Beta strand 377 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 386 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Turn 402 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P32523 UniProtKB Beta strand 409 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 424 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 432 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Turn 440 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 444 451 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Turn 452 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 456 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 462 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P32523 UniProtKB Beta strand 466 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P32523 UniProtKB Helix 473 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P32523 UniProtKB Beta strand 476 482 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 485 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +P32523 UniProtKB Beta strand 493 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZB4 +##sequence-region P24384 1 1145 +P24384 UniProtKB Chain 1 1145 . . . ID=PRO_0000055135;Note=Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22 +P24384 UniProtKB Domain 178 250 . . . Note=S1 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180 +P24384 UniProtKB Domain 493 656 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P24384 UniProtKB Domain 678 854 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P24384 UniProtKB Nucleotide binding 506 513 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P24384 UniProtKB Motif 603 606 . . . Note=DEAH box +##sequence-region P20095 1 876 +P20095 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P20095 UniProtKB Chain 2 876 . . . ID=PRO_0000055130;Note=Pre-mRNA-splicing factor ATP-dependent RNA helicase-like protein PRP2 +P20095 UniProtKB Domain 233 399 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P20095 UniProtKB Domain 424 598 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P20095 UniProtKB Nucleotide binding 246 253 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P20095 UniProtKB Motif 346 349 . . . Note=DEAH box +P20095 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P20095 UniProtKB Mutagenesis 6 206 . . . Note=No affect on activity. Missing +P20095 UniProtKB Mutagenesis 89 552 . . . Note=Loss of ATPase and splicing activity. Missing +P20095 UniProtKB Mutagenesis 89 206 . . . Note=Wild-type RNA-dependent ATPase activity%3B bound tightly to the spliceosome and after addition of ATP released from the spliceosome. Missing +P20095 UniProtKB Mutagenesis 349 349 . . . Note=Fails to release from the spliceosome%3B when associated with H-548. H->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14730020;Dbxref=PMID:14730020 +P20095 UniProtKB Mutagenesis 378 378 . . . Note=In PRP2-dn1%3B 40%25 of wild-type RNA-stimulated ATPase activity%3B splicing activity abolished%3B accumulates stalled splicing complexes. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8112301;Dbxref=PMID:8112301 +P20095 UniProtKB Mutagenesis 548 548 . . . Note=Fails to release from the spliceosome%3B when associated with D-349. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14730020;Dbxref=PMID:14730020 +P20095 UniProtKB Mutagenesis 551 551 . . . Note=Fails to release from the spliceosome. G->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14730020;Dbxref=PMID:14730020 +P20095 UniProtKB Mutagenesis 554 876 . . . Note=Has small amount of ATPase activity%2C but no splicing activity. Missing +P20095 UniProtKB Mutagenesis 615 876 . . . Note=Loss of activity. Missing +P20095 UniProtKB Mutagenesis 824 876 . . . Note=Spliceosome binding mutant%3B not active in splicing%3B when associated with N-551. Missing +P20095 UniProtKB Mutagenesis 833 876 . . . Note=Spliceosome binding mutant%3B not active in splicing%3B when associated with N-551. Missing +P20095 UniProtKB Mutagenesis 834 876 . . . Note=Spliceosome binding mutant%3B not active in splicing%3B when associated with N-551. Almost wild-type RNA-dependent ATPase activity. Missing +P20095 UniProtKB Mutagenesis 845 846 . . . Note=Spliceosome binding mutant%3B not active in splicing%3B when associated with N-551%2C or D-349 and H-548. Loss of interaction with SPP2. DC->NY;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14730020,ECO:0000269|PubMed:15542821;Dbxref=PMID:14730020,PMID:15542821 +P20095 UniProtKB Mutagenesis 845 845 . . . Note=Temperature-sensitive%3B decreased interaction with SPP2%2C decreased cell growth on benomyl and decreased splicing at elevated temperatures%3B when associated with D-349 and H-548. D->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15542821;Dbxref=PMID:15542821 +P20095 UniProtKB Mutagenesis 854 855 . . . Note=Loss of interaction with SPP2. WL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15542821;Dbxref=PMID:15542821 +##sequence-region Q03338 1 469 +Q03338 UniProtKB Chain 1 469 . . . ID=PRO_0000097037;Note=U4/U6 small nuclear ribonucleoprotein PRP3 +Q03338 UniProtKB Beta strand 337 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV +Q03338 UniProtKB Helix 350 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV +Q03338 UniProtKB Beta strand 366 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV +Q03338 UniProtKB Beta strand 378 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV +Q03338 UniProtKB Helix 386 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV +Q03338 UniProtKB Beta strand 406 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV +Q03338 UniProtKB Beta strand 414 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV +Q03338 UniProtKB Beta strand 424 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV +Q03338 UniProtKB Beta strand 439 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV +Q03338 UniProtKB Helix 448 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV +Q03338 UniProtKB Helix 461 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YHV +##sequence-region Q12417 1 451 +Q12417 UniProtKB Chain 1 451 . . . ID=PRO_0000051169;Note=Pre-mRNA-splicing factor PRP46 +Q12417 UniProtKB Repeat 137 168 . . . Note=WD 1 +Q12417 UniProtKB Repeat 180 210 . . . Note=WD 2 +Q12417 UniProtKB Repeat 222 252 . . . Note=WD 3 +Q12417 UniProtKB Repeat 264 294 . . . Note=WD 4 +Q12417 UniProtKB Repeat 306 335 . . . Note=WD 5 +Q12417 UniProtKB Repeat 348 377 . . . Note=WD 6 +Q12417 UniProtKB Repeat 397 427 . . . Note=WD 7 +Q12417 UniProtKB Helix 112 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 129 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Turn 149 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 154 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 165 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Turn 169 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 174 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 187 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 192 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 202 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 206 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Turn 211 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 215 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 229 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Turn 234 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 238 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 246 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Turn 253 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 260 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 269 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 276 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 281 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 290 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Turn 295 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 299 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 314 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Turn 318 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 321 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 332 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 353 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 362 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Turn 378 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 383 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Helix 397 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 402 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 409 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Turn 419 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12417 UniProtKB Beta strand 422 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region Q12428 1 516 +Q12428 UniProtKB Chain 1 516 . . . ID=PRO_0000215027;Note=Probable 2-methylcitrate dehydratase +##sequence-region P33299 1 467 +P33299 UniProtKB Chain 1 467 . . . ID=PRO_0000084719;Note=26S proteasome regulatory subunit 7 homolog +P33299 UniProtKB Nucleotide binding 250 257 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33299 UniProtKB Modified residue 164 164 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P33299 UniProtKB Modified residue 231 231 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P34227 1 261 +P34227 UniProtKB Transit peptide 1 13 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34227 UniProtKB Chain 14 261 . . . ID=PRO_0000135151;Note=Peroxiredoxin PRX1%2C mitochondrial +P34227 UniProtKB Domain 49 212 . . . Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +P34227 UniProtKB Active site 91 91 . . . Note=Cysteine sulfenic acid (-SOH) intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10681558;Dbxref=PMID:10681558 +P34227 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P34227 UniProtKB Disulfide bond 38 38 . . . Note=Interchain;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10821871;Dbxref=PMID:10821871 +P34227 UniProtKB Mutagenesis 38 38 . . . Note=Impairs dimer formation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10821871;Dbxref=PMID:10821871 +P34227 UniProtKB Mutagenesis 91 91 . . . Note=No activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10681558;Dbxref=PMID:10681558 +##sequence-region P47033 1 881 +P47033 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47033 UniProtKB Chain 19 853 . . . ID=PRO_0000211549;Note=Cell wall protein PRY3 +P47033 UniProtKB Propeptide 854 881 . . . ID=PRO_0000372447;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47033 UniProtKB Domain 30 144 . . . Note=SCP +P47033 UniProtKB Compositional bias 163 845 . . . Note=Ser/Thr-rich +P47033 UniProtKB Lipidation 853 853 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47033 UniProtKB Glycosylation 101 101 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23038983;Dbxref=PMID:23038983 +P47033 UniProtKB Glycosylation 360 360 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47033 UniProtKB Glycosylation 488 488 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47033 UniProtKB Glycosylation 535 535 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47033 UniProtKB Glycosylation 547 547 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47033 UniProtKB Glycosylation 569 569 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47033 UniProtKB Glycosylation 625 625 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32379 1 260 +P32379 UniProtKB Chain 1 260 . . . ID=PRO_0000124129;Note=Proteasome subunit alpha type-5 +P32379 UniProtKB Modified residue 55 55 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P32379 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P32379 UniProtKB Modified residue 251 251 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P32379 UniProtKB Mutagenesis 49 49 . . . Note=In DOA5-1%3B slight decrease in activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7781614;Dbxref=PMID:7781614 +P32379 UniProtKB Sequence conflict 192 192 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32379 UniProtKB Beta strand 19 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QBY +P32379 UniProtKB Helix 22 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Beta strand 37 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Beta strand 46 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Beta strand 55 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G65 +P32379 UniProtKB Helix 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Beta strand 67 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Beta strand 74 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Helix 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Helix 85 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Helix 109 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Turn 118 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Beta strand 124 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Beta strand 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LTC +P32379 UniProtKB Beta strand 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Beta strand 139 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Turn 149 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Beta strand 152 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Turn 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4G4S +P32379 UniProtKB Beta strand 164 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Helix 176 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Helix 193 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Beta strand 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FNT +P32379 UniProtKB Beta strand 216 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Turn 224 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Beta strand 227 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P32379 UniProtKB Helix 233 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +##sequence-region P40302 1 234 +P40302 UniProtKB Chain 1 234 . . . ID=PRO_0000124076;Note=Proteasome subunit alpha type-6 +P40302 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P40302 UniProtKB Cross-link 191 191 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P40302 UniProtKB Helix 3 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40302 UniProtKB Beta strand 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FZC +P40302 UniProtKB Helix 20 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40302 UniProtKB Beta strand 35 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40302 UniProtKB Beta strand 41 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40302 UniProtKB Beta strand 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4R17 +P40302 UniProtKB Beta strand 63 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40302 UniProtKB Beta strand 70 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40302 UniProtKB Helix 78 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40302 UniProtKB Helix 105 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40302 UniProtKB Beta strand 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QVP +P40302 UniProtKB Beta strand 130 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40302 UniProtKB Beta strand 141 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40302 UniProtKB Turn 149 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G0U +P40302 UniProtKB Beta strand 153 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40302 UniProtKB Turn 163 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40302 UniProtKB Helix 166 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40302 UniProtKB Helix 186 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40302 UniProtKB Helix 198 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4QVP +P40302 UniProtKB Beta strand 202 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EU2 +P40302 UniProtKB Turn 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40302 UniProtKB Beta strand 211 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40302 UniProtKB Beta strand 220 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +P40302 UniProtKB Helix 227 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RYP +##sequence-region Q12146 1 194 +Q12146 UniProtKB Chain 1 194 . . . ID=PRO_0000132325;Note=DNA replication complex GINS protein PSF3 +##sequence-region Q07800 1 427 +Q07800 UniProtKB Chain 1 427 . . . ID=PRO_0000212576;Note=Phosphatase PSR1 +Q07800 UniProtKB Domain 253 411 . . . Note=FCP1 homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00336 +Q07800 UniProtKB Compositional bias 152 189 . . . Note=Gln-rich +Q07800 UniProtKB Modified residue 110 110 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +Q07800 UniProtKB Lipidation 9 9 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255,ECO:0000303;evidence=ECO:0000255,ECO:0000303|PubMed:10777497;Dbxref=PMID:10777497 +Q07800 UniProtKB Lipidation 10 10 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255,ECO:0000303;evidence=ECO:0000255,ECO:0000303|PubMed:10777497;Dbxref=PMID:10777497 +Q07800 UniProtKB Cross-link 154 154 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q07800 UniProtKB Mutagenesis 2 2 . . . Note=No effect on membrane association. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10777497;Dbxref=PMID:10777497 +Q07800 UniProtKB Mutagenesis 9 10 . . . Note=Impairs membrane association. CC->GG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10777497;Dbxref=PMID:10777497 +Q07800 UniProtKB Mutagenesis 263 263 . . . Note=Low residual phosphatase activity. Loss of stress response functions. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10777497;Dbxref=PMID:10777497 +Q07800 UniProtKB Mutagenesis 265 265 . . . Note=Low residual phosphatase activity. Loss of stress response functions. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10777497;Dbxref=PMID:10777497 +##sequence-region Q12211 1 544 +Q12211 UniProtKB Chain 1 544 . . . ID=PRO_0000057530;Note=tRNA pseudouridine synthase 1 +Q12211 UniProtKB Active site 134 134 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12211 UniProtKB Binding site 190 190 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P48567 1 403 +P48567 UniProtKB Chain 1 403 . . . ID=PRO_0000121976;Note=tRNA pseudouridine synthase 4 +P48567 UniProtKB Active site 75 75 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P07275 1 575 +P07275 UniProtKB Nucleotide binding 297 302 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07275 UniProtKB Active site 317 317 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008 +P07275 UniProtKB Active site 351 351 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10007,ECO:0000255|PROSITE-ProRule:PRU10008 +P07275 UniProtKB Site 212 212 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07275 UniProtKB Sequence conflict 187 188 . . . Note=ES->SR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07275 UniProtKB Sequence conflict 264 264 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07275 UniProtKB Sequence conflict 541 541 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07275 UniProtKB Sequence conflict 561 561 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07275 UniProtKB Helix 44 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 68 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Turn 73 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 78 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 86 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 99 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 121 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Turn 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 140 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 155 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 164 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 193 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 202 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 214 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 231 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 237 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 240 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 259 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 267 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 280 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 289 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 313 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 322 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 332 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 345 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 354 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 361 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 405 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 424 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 435 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 443 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 453 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 461 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 471 473 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 474 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 489 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 498 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Turn 508 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 513 519 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Helix 548 552 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +P07275 UniProtKB Beta strand 553 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OE6 +##sequence-region P15380 1 627 +P15380 UniProtKB Chain 1 627 . . . ID=PRO_0000054158;Note=Proline-specific permease +P15380 UniProtKB Transmembrane 115 136 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15380 UniProtKB Transmembrane 142 162 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15380 UniProtKB Transmembrane 191 210 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15380 UniProtKB Transmembrane 229 247 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15380 UniProtKB Transmembrane 262 281 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15380 UniProtKB Transmembrane 306 326 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15380 UniProtKB Transmembrane 351 370 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15380 UniProtKB Transmembrane 408 427 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15380 UniProtKB Transmembrane 455 473 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15380 UniProtKB Transmembrane 483 503 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15380 UniProtKB Transmembrane 522 542 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15380 UniProtKB Transmembrane 558 578 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15380 UniProtKB Glycosylation 72 72 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15380 UniProtKB Glycosylation 78 78 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15380 UniProtKB Sequence conflict 38 38 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P07259 1 2214 +P07259 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P07259 UniProtKB Chain 2 2214 . . . ID=PRO_0000199511;Note=Protein URA2 +P07259 UniProtKB Domain 228 413 . . . Note=Glutamine amidotransferase type-1 +P07259 UniProtKB Domain 562 754 . . . Note=ATP-grasp 1 +P07259 UniProtKB Domain 1099 1290 . . . Note=ATP-grasp 2 +P07259 UniProtKB Region 2 400 . . . Note=GATase (Glutamine amidotransferase) +P07259 UniProtKB Region 401 440 . . . Note=Linker +P07259 UniProtKB Region 441 1482 . . . Note=CPSase (Carbamoyl-phosphate synthase) +P07259 UniProtKB Region 1483 1492 . . . Note=Linker +P07259 UniProtKB Region 1493 1821 . . . Note=Defective DHOase domain +P07259 UniProtKB Region 1822 1909 . . . Note=Linker +P07259 UniProtKB Region 1910 2214 . . . Note=ATCase (Aspartate transcarbamylase) +P07259 UniProtKB Active site 302 302 . . . Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07259 UniProtKB Active site 386 386 . . . Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07259 UniProtKB Active site 388 388 . . . Note=For GATase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07259 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P07259 UniProtKB Modified residue 1857 1857 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:1977585;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198,PMID:1977585 +P07259 UniProtKB Cross-link 1853 1853 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P07259 UniProtKB Sequence conflict 86 86 . . . Note=H->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 123 123 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 250 257 . . . Note=ELKVVPWN->RIESCSMD;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 270 270 . . . Note=I->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 313 314 . . . Note=GA->VQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 372 373 . . . Note=GI->RF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 394 402 . . . Note=RDTEFLFDV->EIQNSCLT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 431 433 . . . Note=KAH->QGT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 482 482 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 485 485 . . . Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 492 492 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 501 510 . . . Note=TAEFVRKVIL->NAAKQRDVDR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 1411 1412 . . . Note=EV->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 1582 1582 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 1588 1588 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 1592 1592 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 1595 1595 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 1872 1872 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 1937 1937 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 1937 1937 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 1997 1997 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 2039 2039 . . . Note=H->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07259 UniProtKB Sequence conflict 2158 2165 . . . Note=KILAHAKE->VRSWHTQQK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q9ZZX8 1 53 +Q9ZZX8 UniProtKB Chain 1 53 . . . ID=PRO_0000299679;Note=Putative uncharacterized protein Q0017%2C mitochondrial +##sequence-region P22289 1 66 +P22289 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2174427;Dbxref=PMID:2174427 +P22289 UniProtKB Chain 2 66 . . . ID=PRO_0000193558;Note=Cytochrome b-c1 complex subunit 9 +P22289 UniProtKB Transmembrane 16 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22289 UniProtKB Helix 4 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P22289 UniProtKB Helix 18 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P22289 UniProtKB Turn 44 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P22289 UniProtKB Helix 49 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +##sequence-region P32849 1 1169 +P32849 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32849 UniProtKB Chain 2 1169 . . . ID=PRO_0000056130;Note=DNA repair protein RAD5 +P32849 UniProtKB Domain 519 730 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P32849 UniProtKB Domain 995 1165 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P32849 UniProtKB Nucleotide binding 532 539 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P32849 UniProtKB Zinc finger 914 961 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +P32849 UniProtKB Motif 681 684 . . . Note=DEGH box +P32849 UniProtKB Compositional bias 42 60 . . . Note=Asp/Glu-rich (acidic) +P32849 UniProtKB Compositional bias 303 315 . . . Note=Arg/Lys-rich (basic) +P32849 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32849 UniProtKB Modified residue 20 20 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32849 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32849 UniProtKB Modified residue 129 129 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32849 UniProtKB Modified residue 130 130 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32849 UniProtKB Mutagenesis 538 539 . . . Note=Increased sensitivity toward ionizing radiation. KT->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16224103;Dbxref=PMID:16224103 +P32849 UniProtKB Mutagenesis 914 914 . . . Note=Abolishes interaction with UBC13. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10880451,ECO:0000269|PubMed:12496280;Dbxref=PMID:10880451,PMID:12496280 +P32849 UniProtKB Mutagenesis 916 916 . . . Note=Abolishes interaction with UBC13. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12496280;Dbxref=PMID:12496280 +P32849 UniProtKB Mutagenesis 944 944 . . . Note=Abolishes interaction with UBC13. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12496280;Dbxref=PMID:12496280 +P32849 UniProtKB Mutagenesis 959 959 . . . Note=Abolishes interaction with UBC13. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12496280;Dbxref=PMID:12496280 +P32849 UniProtKB Sequence conflict 478 478 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32849 UniProtKB Sequence conflict 635 635 . . . Note=T->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32849 UniProtKB Sequence conflict 846 846 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32849 UniProtKB Sequence conflict 898 898 . . . Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32849 UniProtKB Sequence conflict 973 973 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32849 UniProtKB Sequence conflict 1063 1063 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P14737 1 1309 +P14737 UniProtKB Chain 1 1309 . . . ID=PRO_0000097158;Note=DNA repair protein RAD9 +P14737 UniProtKB Domain 994 1122 . . . Note=BRCT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033 +P14737 UniProtKB Modified residue 26 26 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P14737 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P14737 UniProtKB Modified residue 205 205 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14737 UniProtKB Modified residue 218 218 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14737 UniProtKB Modified residue 248 248 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14737 UniProtKB Modified residue 312 312 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14737 UniProtKB Modified residue 315 315 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P14737 UniProtKB Modified residue 462 462 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P14737 UniProtKB Modified residue 471 471 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14737 UniProtKB Modified residue 474 474 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14737 UniProtKB Modified residue 568 568 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14737 UniProtKB Modified residue 729 729 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P14737 UniProtKB Sequence conflict 433 433 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14737 UniProtKB Sequence conflict 433 433 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14737 UniProtKB Beta strand 190 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K3Q +##sequence-region P20051 1 364 +P20051 UniProtKB Chain 1 364 . . . ID=PRO_0000147292;Note=Dihydroorotase +P20051 UniProtKB Metal binding 14 14 . . . Note=Zinc 1%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05020 +P20051 UniProtKB Metal binding 16 16 . . . Note=Zinc 1%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05020 +P20051 UniProtKB Metal binding 98 98 . . . Note=Zinc 1%3B via carbamate group;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05020 +P20051 UniProtKB Metal binding 98 98 . . . Note=Zinc 2%3B via carbamate group;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05020 +P20051 UniProtKB Metal binding 137 137 . . . Note=Zinc 2%3B via pros nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05020 +P20051 UniProtKB Metal binding 180 180 . . . Note=Zinc 2%3B via tele nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05020 +P20051 UniProtKB Metal binding 258 258 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05020 +P20051 UniProtKB Modified residue 98 98 . . . Note=N6-carboxylysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05020 +P20051 UniProtKB Sequence conflict 107 119 . . . Note=NSAAGVDPNDFSA->IRLLGWIQMTSAH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20051 UniProtKB Sequence conflict 156 156 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20051 UniProtKB Sequence conflict 240 240 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20051 UniProtKB Sequence conflict 269 269 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20051 UniProtKB Sequence conflict 319 319 . . . Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P07257 1 368 +P07257 UniProtKB Transit peptide 1 16 . . . Note=Mitochondrion +P07257 UniProtKB Chain 17 368 . . . ID=PRO_0000026801;Note=Cytochrome b-c1 complex subunit 2%2C mitochondrial +P07257 UniProtKB Modified residue 141 141 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P07257 UniProtKB Modified residue 168 168 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07257 UniProtKB Beta strand 18 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Beta strand 27 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Helix 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Helix 47 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Beta strand 59 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Helix 64 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Beta strand 77 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Beta strand 87 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Helix 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Helix 98 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Helix 116 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Helix 123 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Helix 138 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Turn 152 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Beta strand 163 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Helix 169 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Helix 182 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Beta strand 185 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Helix 194 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Turn 205 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Beta strand 228 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Beta strand 234 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Turn 247 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Helix 250 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Beta strand 262 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1P84 +P07257 UniProtKB Helix 268 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Beta strand 272 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Beta strand 282 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Helix 294 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Helix 315 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Helix 318 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Helix 329 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KB9 +P07257 UniProtKB Helix 340 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Beta strand 352 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Helix 359 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P07257 UniProtKB Helix 365 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +##sequence-region P00128 1 127 +P00128 UniProtKB Chain 1 127 . . . ID=PRO_0000193539;Note=Cytochrome b-c1 complex subunit 7 +P00128 UniProtKB Sequence conflict 92 92 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00128 UniProtKB Helix 5 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00128 UniProtKB Helix 19 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00128 UniProtKB Helix 38 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00128 UniProtKB Helix 45 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00128 UniProtKB Helix 54 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00128 UniProtKB Helix 65 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00128 UniProtKB Helix 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00128 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00128 UniProtKB Helix 104 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +##sequence-region P40475 1 563 +P40475 UniProtKB Chain 1 563 . . . ID=PRO_0000173441;Note=Quinidine resistance protein 1 +P40475 UniProtKB Topological domain 1 75 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Transmembrane 76 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Topological domain 97 108 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Transmembrane 109 129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Topological domain 130 135 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Topological domain 157 165 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Transmembrane 166 186 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Topological domain 187 195 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Transmembrane 196 216 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Topological domain 217 224 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Transmembrane 225 245 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Topological domain 246 296 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Transmembrane 297 317 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Topological domain 318 341 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Transmembrane 342 362 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Topological domain 363 421 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Transmembrane 422 442 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Topological domain 443 445 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Transmembrane 446 466 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Topological domain 467 481 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Transmembrane 482 502 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Topological domain 503 511 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Transmembrane 512 532 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40475 UniProtKB Topological domain 533 563 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40474 1 542 +P40474 UniProtKB Chain 1 542 . . . ID=PRO_0000173442;Note=Quinidine resistance protein 2 +P40474 UniProtKB Topological domain 1 67 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Transmembrane 68 88 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Topological domain 89 100 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Transmembrane 101 121 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Topological domain 122 127 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Transmembrane 128 148 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Topological domain 149 149 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Transmembrane 150 170 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Topological domain 171 187 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Transmembrane 188 208 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Topological domain 209 216 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Transmembrane 217 237 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Topological domain 238 300 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Transmembrane 301 321 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Topological domain 322 333 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Transmembrane 334 354 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Topological domain 355 413 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Transmembrane 414 434 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Topological domain 435 437 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Transmembrane 438 458 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Topological domain 459 472 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Transmembrane 473 493 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Topological domain 494 503 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Transmembrane 504 524 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Topological domain 525 542 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40474 UniProtKB Modified residue 21 21 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40474 UniProtKB Modified residue 38 38 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40474 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38227 1 689 +P38227 UniProtKB Chain 1 689 . . . ID=PRO_0000173437;Note=Quinidine resistance protein 3 +P38227 UniProtKB Topological domain 1 108 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Transmembrane 109 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Topological domain 132 139 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Transmembrane 140 163 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Topological domain 164 175 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Transmembrane 176 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Topological domain 194 235 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Transmembrane 236 256 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Topological domain 257 265 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Transmembrane 266 283 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Topological domain 284 475 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Transmembrane 476 493 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Topological domain 494 510 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Transmembrane 511 532 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Topological domain 533 558 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Transmembrane 559 577 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Topological domain 578 586 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Transmembrane 587 609 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Topological domain 610 624 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Transmembrane 625 642 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Topological domain 643 648 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Transmembrane 649 668 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Topological domain 669 689 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38227 UniProtKB Modified residue 436 436 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38227 UniProtKB Sequence conflict 37 37 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P48581 1 401 +P48581 UniProtKB Chain 1 401 . . . ID=PRO_0000097150;Note=DNA damage checkpoint control protein RAD17 +P48581 UniProtKB Modified residue 383 383 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P48581 UniProtKB Mutagenesis 128 128 . . . Note=In RAD17-1%3B UV-sensitive. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8649984;Dbxref=PMID:8649984 +##sequence-region P40352 1 1085 +P40352 UniProtKB Chain 1 1085 . . . ID=PRO_0000074336;Note=DNA repair and recombination protein RAD26 +P40352 UniProtKB Domain 309 518 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P40352 UniProtKB Domain 655 818 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P40352 UniProtKB Nucleotide binding 322 329 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P40352 UniProtKB Motif 469 472 . . . Note=DEGH box +P40352 UniProtKB Compositional bias 173 228 . . . Note=Asp/Glu-rich (acidic) +P40352 UniProtKB Modified residue 30 30 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40352 UniProtKB Sequence conflict 366 366 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40352 UniProtKB Sequence conflict 963 963 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12223 1 238 +Q12223 UniProtKB Chain 1 238 . . . ID=PRO_0000173897;Note=DNA repair protein RAD59 +##sequence-region P21827 1 482 +P21827 UniProtKB Chain 1 482 . . . ID=PRO_0000206634;Note=Guanine nucleotide exchange factor SRM1 +P21827 UniProtKB Repeat 45 101 . . . Note=RCC1 1 +P21827 UniProtKB Repeat 103 152 . . . Note=RCC1 2 +P21827 UniProtKB Repeat 183 238 . . . Note=RCC1 3 +P21827 UniProtKB Repeat 239 291 . . . Note=RCC1 4 +P21827 UniProtKB Repeat 292 347 . . . Note=RCC1 5 +P21827 UniProtKB Repeat 349 411 . . . Note=RCC1 6 +P21827 UniProtKB Repeat 412 466 . . . Note=RCC1 7 +P21827 UniProtKB Motif 15 26 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11523802;Dbxref=PMID:11523802 +P21827 UniProtKB Modified residue 135 135 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P21827 UniProtKB Modified residue 136 136 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P21827 UniProtKB Mutagenesis 19 19 . . . Note=Impairs correct nuclear localization%3B when associated with T-20 and T-23. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11523802;Dbxref=PMID:11523802 +P21827 UniProtKB Mutagenesis 20 20 . . . Note=Impairs activity. K->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11523802;Dbxref=PMID:11523802 +P21827 UniProtKB Mutagenesis 20 20 . . . Note=Impairs correct nuclear localization%3B when associated with T-19 and T-23. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11523802;Dbxref=PMID:11523802 +P21827 UniProtKB Mutagenesis 23 23 . . . Note=Impairs correct nuclear localization%3B when associated with T-19 and T-20. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11523802;Dbxref=PMID:11523802 +P21827 UniProtKB Mutagenesis 282 282 . . . Note=Leads to temperature-dependent mislocalization of nucleoporins (nups) and the pore-membrane protein POM152. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654904;Dbxref=PMID:12654904 +P21827 UniProtKB Helix 33 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Helix 37 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 47 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Helix 65 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 69 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Turn 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 86 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 93 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 105 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Helix 145 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Helix 155 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Helix 159 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 167 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 174 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 186 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 197 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Turn 203 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 209 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 223 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 230 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 242 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Helix 259 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Turn 262 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 275 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 283 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 295 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 317 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 332 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 339 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 351 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Helix 366 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 381 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 396 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 403 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 415 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 435 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Turn 444 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 449 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Beta strand 458 467 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +P21827 UniProtKB Helix 470 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OF7 +##sequence-region P53972 1 490 +P53972 UniProtKB Chain 1 490 . . . ID=PRO_0000203461;Note=25S rRNA (cytosine(2278)-C(5))-methyltransferase +P53972 UniProtKB Region 250 256 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023 +P53972 UniProtKB Active site 404 404 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023 +P53972 UniProtKB Binding site 280 280 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023 +P53972 UniProtKB Binding site 308 308 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023 +P53972 UniProtKB Binding site 327 327 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01023 +P53972 UniProtKB Mutagenesis 330 330 . . . Note=Lethal. Blocks the separation of the enzyme from its RNA substrate. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23913415;Dbxref=PMID:23913415 +P53972 UniProtKB Mutagenesis 404 404 . . . Note=Fails to ctalyze the C-5 methylation of the C2278 residue. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23913415;Dbxref=PMID:23913415 +##sequence-region P30402 1 227 +P30402 UniProtKB Chain 1 227 . . . ID=PRO_0000110805;Note=Orotate phosphoribosyltransferase 2 +P30402 UniProtKB Region 41 42 . . . Note=Orotate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P30402 UniProtKB Region 79 80 . . . Note=5-phosphoribose 1-diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P30402 UniProtKB Region 135 143 . . . Note=5-phosphoribose 1-diphosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P30402 UniProtKB Binding site 109 109 . . . Note=5-phosphoribose 1-diphosphate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P30402 UniProtKB Binding site 110 110 . . . Note=5-phosphoribose 1-diphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P30402 UniProtKB Binding site 113 113 . . . Note=5-phosphoribose 1-diphosphate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P30402 UniProtKB Binding site 115 115 . . . Note=5-phosphoribose 1-diphosphate%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P30402 UniProtKB Binding site 139 139 . . . Note=Orotate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P30402 UniProtKB Binding site 167 167 . . . Note=Orotate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P30402 UniProtKB Sequence conflict 143 143 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P30402 UniProtKB Sequence conflict 158 158 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q9ZZX7 1 96 +Q9ZZX7 UniProtKB Chain 1 96 . . . ID=PRO_0000299680;Note=Putative uncharacterized protein Q0032%2C mitochondrial +##sequence-region Q9ZZW3 1 50 +Q9ZZW3 UniProtKB Chain 1 50 . . . ID=PRO_0000299683;Note=Putative uncharacterized protein Q0143%2C mitochondrial +##sequence-region P00127 1 147 +P00127 UniProtKB Chain 1 147 . . . ID=PRO_0000193542;Note=Cytochrome b-c1 complex subunit 6 +P00127 UniProtKB Compositional bias 26 80 . . . Note=Asp/Glu-rich (acidic) +P00127 UniProtKB Disulfide bond 101 123 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10873857,ECO:0000269|PubMed:11726495,ECO:0000269|PubMed:11880631,ECO:0000269|PubMed:12782631,ECO:0000269|PubMed:17337272,ECO:0000269|PubMed:18390544;Dbxref=PMID:10873857,PMID:11726495,PMID:11880631,PMID:12782631,PMID:17337272,PMID:18390544 +P00127 UniProtKB Sequence conflict 2 2 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00127 UniProtKB Helix 77 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00127 UniProtKB Helix 89 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00127 UniProtKB Helix 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00127 UniProtKB Helix 124 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +P00127 UniProtKB Helix 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CX5 +##sequence-region P07276 1 1031 +P07276 UniProtKB Chain 1 1031 . . . ID=PRO_0000154035;Note=DNA repair protein RAD2 +P07276 UniProtKB Region 1 95 . . . Note=N-domain +P07276 UniProtKB Region 756 884 . . . Note=I-domain +P07276 UniProtKB Metal binding 30 30 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07276 UniProtKB Metal binding 77 77 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07276 UniProtKB Metal binding 792 792 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07276 UniProtKB Metal binding 794 794 . . . Note=Magnesium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07276 UniProtKB Metal binding 813 813 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07276 UniProtKB Metal binding 815 815 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07276 UniProtKB Metal binding 864 864 . . . Note=Magnesium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07276 UniProtKB Modified residue 118 118 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07276 UniProtKB Modified residue 367 367 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P07276 UniProtKB Modified residue 583 583 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P07276 UniProtKB Sequence conflict 782 782 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07276 UniProtKB Helix 6 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Helix 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Beta strand 15 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Helix 19 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Beta strand 26 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Helix 34 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Beta strand 45 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0Z +P07276 UniProtKB Helix 53 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Beta strand 71 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Helix 82 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Beta strand 667 669 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LOX +P07276 UniProtKB Helix 769 781 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Beta strand 786 788 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Helix 793 802 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Beta strand 807 810 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Helix 815 818 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Beta strand 823 827 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Beta strand 830 839 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Helix 840 847 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Helix 851 861 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Helix 874 884 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Helix 887 899 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Helix 901 904 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Helix 909 920 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Helix 932 939 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Helix 957 968 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +P07276 UniProtKB Helix 972 982 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Q0W +##sequence-region Q12465 1 1220 +Q12465 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Chain 21 1220 . . . ID=PRO_0000262737;Note=Bud site selection protein RAX2 +Q12465 UniProtKB Topological domain 21 1162 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Transmembrane 1163 1183 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Topological domain 1184 1220 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Compositional bias 1149 1156 . . . Note=Poly-Lys +Q12465 UniProtKB Glycosylation 41 41 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 45 45 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 69 69 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 88 88 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 124 124 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 134 134 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 145 145 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 158 158 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 166 166 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 171 171 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 187 187 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 200 200 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 235 235 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 238 238 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 244 244 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 333 333 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 365 365 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 379 379 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 432 432 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 445 445 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 516 516 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 524 524 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 613 613 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 620 620 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 626 626 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 640 640 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 677 677 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 705 705 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 713 713 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 721 721 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 731 731 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 749 749 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 758 758 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 792 792 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 821 821 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 848 848 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 861 861 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 884 884 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 890 890 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 908 908 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 923 923 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 942 942 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 956 956 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 980 980 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 983 983 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 1011 1011 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 1024 1024 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 1031 1031 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 1060 1060 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 1071 1071 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 1098 1098 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12465 UniProtKB Glycosylation 1126 1126 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A0B7P221 1 28 +A0A0B7P221 UniProtKB Chain 1 28 . . . ID=PRO_0000434005;Note=Uncharacterized protein RDT1 +##sequence-region P21651 1 314 +P21651 UniProtKB Chain 1 314 . . . ID=PRO_0000096421;Note=Recombination protein 107 +P21651 UniProtKB Sequence conflict 279 279 . . . Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21651 UniProtKB Sequence conflict 279 279 . . . Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21651 UniProtKB Sequence conflict 284 314 . . . Note=DNDDASHRLKRAARTIIPWEELRPDTLESEL->TMMTLAIG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21651 UniProtKB Sequence conflict 284 314 . . . Note=DNDDASHRLKRAARTIIPWEELRPDTLESEL->TMMTLAIG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P31244 1 790 +P31244 UniProtKB Chain 1 790 . . . ID=PRO_0000056132;Note=DNA repair protein RAD16 +P31244 UniProtKB Domain 197 371 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P31244 UniProtKB Domain 623 777 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P31244 UniProtKB Nucleotide binding 210 217 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P31244 UniProtKB Zinc finger 537 581 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +P31244 UniProtKB Motif 322 325 . . . Note=DEAH box +P31244 UniProtKB Compositional bias 8 13 . . . Note=Poly-Arg +P31244 UniProtKB Compositional bias 65 70 . . . Note=Poly-Asp +P31244 UniProtKB Compositional bias 125 129 . . . Note=Poly-Lys +P31244 UniProtKB Modified residue 25 25 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P31244 UniProtKB Modified residue 109 109 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P25301 1 460 +P25301 UniProtKB Chain 1 460 . . . ID=PRO_0000122956;Note=DNA repair protein RAD57 +P25301 UniProtKB Nucleotide binding 125 132 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q99359 1 647 +Q99359 UniProtKB Chain 1 647 . . . ID=PRO_0000255971;Note=Protein RAD61 +##sequence-region P11938 1 827 +P11938 UniProtKB Chain 1 827 . . . ID=PRO_0000197112;Note=DNA-binding protein RAP1 +P11938 UniProtKB Domain 121 208 . . . Note=BRCT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033 +P11938 UniProtKB Domain 355 415 . . . Note=HTH myb-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +P11938 UniProtKB DNA binding 388 411 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +P11938 UniProtKB Region 630 695 . . . Note=Activation domain +P11938 UniProtKB Compositional bias 71 74 . . . Note=Poly-Asp +P11938 UniProtKB Compositional bias 81 84 . . . Note=Poly-Thr +P11938 UniProtKB Compositional bias 313 320 . . . Note=Poly-Asn +P11938 UniProtKB Compositional bias 614 627 . . . Note=Poly-Ala +P11938 UniProtKB Modified residue 486 486 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P11938 UniProtKB Modified residue 731 731 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P11938 UniProtKB Sequence conflict 672 672 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11938 UniProtKB Helix 365 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN +P11938 UniProtKB Helix 379 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN +P11938 UniProtKB Helix 386 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN +P11938 UniProtKB Turn 392 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN +P11938 UniProtKB Helix 400 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN +P11938 UniProtKB Helix 412 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN +P11938 UniProtKB Beta strand 437 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN +P11938 UniProtKB Helix 451 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN +P11938 UniProtKB Beta strand 474 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN +P11938 UniProtKB Beta strand 509 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UKG +P11938 UniProtKB Helix 525 532 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN +P11938 UniProtKB Turn 533 535 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN +P11938 UniProtKB Helix 538 547 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN +P11938 UniProtKB Helix 549 552 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN +P11938 UniProtKB Helix 554 562 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1IGN +P11938 UniProtKB Turn 595 597 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UKG +P11938 UniProtKB Helix 681 684 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT +P11938 UniProtKB Helix 688 690 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT +P11938 UniProtKB Turn 700 702 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT +P11938 UniProtKB Helix 705 708 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT +P11938 UniProtKB Helix 713 724 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT +P11938 UniProtKB Turn 730 732 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ6 +P11938 UniProtKB Helix 733 744 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT +P11938 UniProtKB Helix 748 757 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT +P11938 UniProtKB Turn 758 760 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT +P11938 UniProtKB Helix 762 764 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT +P11938 UniProtKB Helix 765 775 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT +P11938 UniProtKB Beta strand 781 783 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ6 +P11938 UniProtKB Helix 789 796 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT +P11938 UniProtKB Helix 800 810 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT +P11938 UniProtKB Helix 812 823 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJT +##sequence-region P53295 1 368 +P53295 UniProtKB Chain 1 368 . . . ID=PRO_0000205450;Note=Ribosome-interacting GTPase 2 +P53295 UniProtKB Domain 64 292 . . . Note=OBG-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +P53295 UniProtKB Nucleotide binding 70 77 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +P53295 UniProtKB Nucleotide binding 116 120 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +P53295 UniProtKB Nucleotide binding 250 253 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +P53295 UniProtKB Modified residue 364 364 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q06835 1 107 +Q06835 UniProtKB Chain 1 107 . . . ID=PRO_0000218722;Note=Pre-mRNA-splicing factor RDS3 +Q06835 UniProtKB Beta strand 15 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0A +Q06835 UniProtKB Helix 24 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0A +Q06835 UniProtKB Turn 31 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0A +Q06835 UniProtKB Beta strand 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0A +Q06835 UniProtKB Helix 47 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0A +Q06835 UniProtKB Turn 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0A +Q06835 UniProtKB Beta strand 62 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0A +Q06835 UniProtKB Helix 74 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K0A +##sequence-region Q08096 1 367 +Q08096 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q08096 UniProtKB Chain 2 367 . . . ID=PRO_0000156444;Note=RNA 3'-terminal phosphate cyclase-like protein +Q08096 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q08096 UniProtKB Beta strand 9 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Helix 17 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Beta strand 31 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Turn 36 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Beta strand 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Helix 47 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Beta strand 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Beta strand 64 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Beta strand 74 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Beta strand 84 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Helix 96 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Helix 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Beta strand 114 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Beta strand 125 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Helix 130 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Helix 137 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Beta strand 150 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Turn 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Beta strand 164 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Beta strand 190 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Helix 203 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Beta strand 219 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Helix 233 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Beta strand 240 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Turn 250 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Beta strand 254 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Helix 268 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Beta strand 287 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Turn 291 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Helix 294 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Beta strand 306 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Helix 315 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Helix 320 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Beta strand 338 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +Q08096 UniProtKB Beta strand 350 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLQ +##sequence-region Q03446 1 210 +Q03446 UniProtKB Chain 1 210 . . . ID=PRO_0000097205;Note=Protein RCR2 +Q03446 UniProtKB Transmembrane 41 61 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03446 UniProtKB Modified residue 161 161 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03446 UniProtKB Modified residue 191 191 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P39531 1 840 +P39531 UniProtKB Chain 1 840 . . . ID=PRO_0000119953;Note=Recyclin-1 +P39531 UniProtKB Domain 1 48 . . . Note=F-box +P39531 UniProtKB Modified residue 409 409 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q08904 1 546 +Q08904 UniProtKB Chain 1 546 . . . ID=PRO_0000114972;Note=Protein RDR1 +Q08904 UniProtKB DNA binding 20 46 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +##sequence-region P03872 1 296 +P03872 UniProtKB Chain 1 296 . . . ID=PRO_0000150898;Note=Partitioning protein REP2 +P03872 UniProtKB Region 1 57 . . . Note=Interaction with REP1 +P03872 UniProtKB Region 58 296 . . . Note=DNA-binding%2C and self-association +P03872 UniProtKB Region 276 296 . . . Note=Nuclear localization +P03872 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P25560 1 188 +P25560 UniProtKB Chain 1 188 . . . ID=PRO_0000207593;Note=Protein RER1 +P25560 UniProtKB Topological domain 1 61 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25560 UniProtKB Transmembrane 62 82 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25560 UniProtKB Topological domain 83 138 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25560 UniProtKB Transmembrane 139 161 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25560 UniProtKB Topological domain 162 188 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25560 UniProtKB Sequence conflict 109 125 . . . Note=RPFIRRLPEFKFWYNSI->LSIHQKTYQSSNSGITAF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25560 UniProtKB Sequence conflict 136 136 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25560 UniProtKB Sequence conflict 141 141 . . . Note=D->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25560 UniProtKB Sequence conflict 145 188 . . . Note=FWPILLMYFILLFFLTMRRQIQHMIKYRYIPLDIGKKKYSHSSN->IFAHSLFDCYFHYYCFF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P43556 1 714 +P43556 UniProtKB Chain 1 714 . . . ID=PRO_0000097318;Note=Rho-GTPase-activating protein RGD2 +P43556 UniProtKB Domain 2 441 . . . Note=F-BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01077 +P43556 UniProtKB Domain 218 298 . . . Note=DEP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00066 +P43556 UniProtKB Domain 475 704 . . . Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172 +##sequence-region P06780 1 209 +P06780 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.5;Dbxref=PMID:22814378 +P06780 UniProtKB Chain 2 206 . . . ID=PRO_0000198945;Note=GTP-binding protein RHO1 +P06780 UniProtKB Propeptide 207 209 . . . ID=PRO_0000281275;Note=Removed in mature form +P06780 UniProtKB Nucleotide binding 17 24 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06780 UniProtKB Nucleotide binding 64 68 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06780 UniProtKB Nucleotide binding 122 125 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06780 UniProtKB Motif 39 47 . . . Note=Effector region;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06780 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.5;Dbxref=PMID:22814378 +P06780 UniProtKB Modified residue 206 206 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06780 UniProtKB Lipidation 206 206 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06780 UniProtKB Mutagenesis 22 22 . . . Note=Abolishes GTP-binding. G->A +P06780 UniProtKB Mutagenesis 24 24 . . . Note=Abolishes GTP-binding. T->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8947028;Dbxref=PMID:8947028 +P06780 UniProtKB Mutagenesis 42 42 . . . Note=Impairs interaction with targets. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8947028;Dbxref=PMID:8947028 +P06780 UniProtKB Mutagenesis 43 43 . . . Note=Temperature sensitive growth defect. V->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8846785;Dbxref=PMID:8846785 +P06780 UniProtKB Mutagenesis 44 44 . . . Note=Temperature sensitive growth defect. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8846785;Dbxref=PMID:8846785 +P06780 UniProtKB Mutagenesis 45 45 . . . Note=Temperature sensitive growth defect. E->I;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11574532,ECO:0000269|PubMed:8846785;Dbxref=PMID:11574532,PMID:8846785 +P06780 UniProtKB Mutagenesis 45 45 . . . Note=In RHO1-2%3B temperature sensitive%2C fails to activate PKC1. E->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11574532,ECO:0000269|PubMed:8846785;Dbxref=PMID:11574532,PMID:8846785 +P06780 UniProtKB Mutagenesis 60 60 . . . Note=In RHO1-3%3B temperature sensitive%2C severely decreases beta-1%2C3-glucan synthase activation. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11574532;Dbxref=PMID:11574532 +P06780 UniProtKB Mutagenesis 68 68 . . . Note=Locks RHO1 in the GTP-bound form by abolishing GTP hydrolysis. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3543936;Dbxref=PMID:3543936 +P06780 UniProtKB Mutagenesis 70 70 . . . Note=In RHO1-10%3B temperature sensitive%2C severely decreases beta-1%2C3-glucan synthase activation%3B when associated with P-165. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11574532;Dbxref=PMID:11574532 +P06780 UniProtKB Mutagenesis 102 102 . . . Note=In RHO1-11%3B temperature sensitive%2C severely decreases beta-1%2C3-glucan synthase activation%3B when associated with E-166. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11574532;Dbxref=PMID:11574532 +P06780 UniProtKB Mutagenesis 104 104 . . . Note=In RHO1-4%3B temperature sensitive%2C severely decreases beta-1%2C3-glucan synthase activation. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11574532;Dbxref=PMID:11574532 +P06780 UniProtKB Mutagenesis 121 121 . . . Note=In RHO1-5%3B temperature sensitive%2C fails to activate PCK1. G->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11574532;Dbxref=PMID:11574532 +P06780 UniProtKB Mutagenesis 165 165 . . . Note=In RHO1-10%3B temperature sensitive%2C severely decreases beta-1%2C3-glucan synthase activation%3B when associated with G-69. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11574532;Dbxref=PMID:11574532 +P06780 UniProtKB Mutagenesis 167 167 . . . Note=In RHO1-11%3B temperature sensitive%2C severely decreases beta-1%2C3-glucan synthase activation%3B when associated with K-101. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11574532;Dbxref=PMID:11574532 +P06780 UniProtKB Beta strand 9 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58 +P06780 UniProtKB Helix 23 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58 +P06780 UniProtKB Beta strand 45 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58 +P06780 UniProtKB Beta strand 56 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58 +P06780 UniProtKB Helix 69 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58 +P06780 UniProtKB Beta strand 83 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58 +P06780 UniProtKB Helix 94 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58 +P06780 UniProtKB Helix 104 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58 +P06780 UniProtKB Beta strand 117 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58 +P06780 UniProtKB Helix 124 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58 +P06780 UniProtKB Helix 130 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58 +P06780 UniProtKB Helix 146 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58 +P06780 UniProtKB Beta strand 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58 +P06780 UniProtKB Turn 166 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58 +P06780 UniProtKB Helix 172 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58 +##sequence-region Q06665 1 692 +Q06665 UniProtKB Chain 1 692 . . . ID=PRO_0000253814;Note=DNA repair protein RAD34 +##sequence-region P25454 1 400 +P25454 UniProtKB Chain 1 400 . . . ID=PRO_0000122925;Note=DNA repair protein RAD51 +P25454 UniProtKB Nucleotide binding 185 192 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25454 UniProtKB Helix 83 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Helix 93 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Helix 107 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Helix 115 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Helix 126 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Helix 147 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Helix 165 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Turn 171 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Beta strand 174 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Beta strand 179 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Helix 191 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Helix 206 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Beta strand 212 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Helix 226 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Helix 240 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Beta strand 247 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Helix 255 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Beta strand 274 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Helix 282 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Helix 296 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Beta strand 320 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Helix 349 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Beta strand 355 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Beta strand 367 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Beta strand 376 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Beta strand 382 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +P25454 UniProtKB Beta strand 391 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LDA +##sequence-region Q03956 1 351 +Q03956 UniProtKB Chain 1 351 . . . ID=PRO_0000097175;Note=Regulator of V-ATPase in vacuolar membrane protein 2 +##sequence-region Q05672 1 457 +Q05672 UniProtKB Chain 1 457 . . . ID=PRO_0000076298;Note=RNA-binding suppressor of PAS kinase protein 1 +Q05672 UniProtKB Domain 26 88 . . . Note=R3H;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00382 +Q05672 UniProtKB Compositional bias 234 239 . . . Note=Poly-Ser +Q05672 UniProtKB Modified residue 198 198 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q05672 UniProtKB Modified residue 435 435 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +Q05672 UniProtKB Modified residue 439 439 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +Q05672 UniProtKB Modified residue 447 447 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05672 UniProtKB Sequence conflict 1 3 . . . Note=MTA->MRVSLSVSSFFHIQLDKFWRRQLSHIVPASRGDT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q05672 UniProtKB Sequence conflict 43 43 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q05672 UniProtKB Sequence conflict 81 81 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25332 1 333 +P25332 UniProtKB Chain 1 333 . . . ID=PRO_0000080094;Note=Ribokinase +P25332 UniProtKB Nucleotide binding 248 253 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215 +P25332 UniProtKB Nucleotide binding 282 283 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215 +P25332 UniProtKB Region 10 12 . . . Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215 +P25332 UniProtKB Region 38 42 . . . Note=Substrate binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215 +P25332 UniProtKB Active site 283 283 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215 +P25332 UniProtKB Metal binding 277 277 . . . Note=Potassium;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215 +P25332 UniProtKB Metal binding 279 279 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215 +P25332 UniProtKB Metal binding 313 313 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215 +P25332 UniProtKB Metal binding 316 316 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215 +P25332 UniProtKB Metal binding 318 318 . . . Note=Potassium%3B via carbonyl oxygen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215 +P25332 UniProtKB Metal binding 322 322 . . . Note=Potassium;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215 +P25332 UniProtKB Binding site 149 149 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215 +P25332 UniProtKB Binding site 193 193 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215 +P25332 UniProtKB Binding site 283 283 . . . Note=Substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03215 +P25332 UniProtKB Sequence conflict 178 178 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25332 UniProtKB Sequence conflict 301 301 . . . Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08273 1 121 +Q08273 UniProtKB Chain 1 121 . . . ID=PRO_0000056022;Note=RING-box protein HRT1 +Q08273 UniProtKB Zinc finger 55 111 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +Q08273 UniProtKB Metal binding 55 55 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878 +Q08273 UniProtKB Metal binding 58 58 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878 +Q08273 UniProtKB Metal binding 66 66 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878 +Q08273 UniProtKB Metal binding 69 69 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878 +Q08273 UniProtKB Metal binding 81 81 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878 +Q08273 UniProtKB Metal binding 88 88 . . . Note=Zinc 3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878 +Q08273 UniProtKB Metal binding 90 90 . . . Note=Zinc 3%3B via pros nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878 +Q08273 UniProtKB Metal binding 93 93 . . . Note=Zinc 1%3B via pros nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878 +Q08273 UniProtKB Metal binding 95 95 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878 +Q08273 UniProtKB Metal binding 107 107 . . . Note=Zinc 3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878 +Q08273 UniProtKB Metal binding 110 110 . . . Note=Zinc 3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62878 +Q08273 UniProtKB Modified residue 15 15 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08273 UniProtKB Mutagenesis 72 72 . . . Note=In RBX1-1%3B temperature-sensitive allele. At 38 degrees Celsius induces defects in ubiquitin ligase activity%3B when associated with R-81. K->R +Q08273 UniProtKB Mutagenesis 81 81 . . . Note=In RBX1-1%3B temperature-sensitive allele. At 38 degrees Celsius induces defects in ubiquitin ligase activity%3B when associated with R-72. C->R +Q08273 UniProtKB Mutagenesis 81 81 . . . Note=In HRT1-C81Y%3B defects in ubiquitin ligase activity. C->Y +##sequence-region Q03530 1 315 +Q03530 UniProtKB Chain 1 315 . . . ID=PRO_0000194834;Note=CAAX prenyl protease 2 +Q03530 UniProtKB Topological domain 1 3 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03530 UniProtKB Transmembrane 4 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03530 UniProtKB Topological domain 24 44 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03530 UniProtKB Transmembrane 45 65 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03530 UniProtKB Topological domain 66 74 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03530 UniProtKB Transmembrane 75 95 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03530 UniProtKB Topological domain 96 105 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03530 UniProtKB Transmembrane 106 126 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03530 UniProtKB Topological domain 127 148 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03530 UniProtKB Transmembrane 149 169 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03530 UniProtKB Topological domain 170 208 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03530 UniProtKB Transmembrane 209 229 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03530 UniProtKB Topological domain 230 237 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03530 UniProtKB Transmembrane 238 258 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03530 UniProtKB Topological domain 259 275 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03530 UniProtKB Transmembrane 276 296 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03530 UniProtKB Topological domain 297 315 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03530 UniProtKB Active site 156 156 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6LZY8 +Q03530 UniProtKB Active site 194 194 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6LZY8 +Q03530 UniProtKB Site 248 248 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6LZY8 +Q03530 UniProtKB Site 252 252 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6LZY8 +##sequence-region P38622 1 512 +P38622 UniProtKB Chain 1 512 . . . ID=PRO_0000086603;Note=Serine/threonine-protein kinase RCK1 +P38622 UniProtKB Domain 121 414 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38622 UniProtKB Nucleotide binding 127 135 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38622 UniProtKB Region 502 512 . . . Note=Calmodulin-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38622 UniProtKB Active site 259 259 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P38622 UniProtKB Binding site 152 152 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +##sequence-region P32841 1 428 +P32841 UniProtKB Chain 1 428 . . . ID=PRO_0000097219;Note=Meiotic recombination protein REC114 +P32841 UniProtKB Sequence conflict 96 97 . . . Note=KY->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32841 UniProtKB Sequence conflict 100 103 . . . Note=EEFG->RRIR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32841 UniProtKB Sequence conflict 377 377 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P21538 1 810 +P21538 UniProtKB Chain 1 810 . . . ID=PRO_0000197089;Note=DNA-binding protein REB1 +P21538 UniProtKB Domain 470 523 . . . Note=HTH myb-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +P21538 UniProtKB Domain 692 717 . . . Note=Myb-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00133 +P21538 UniProtKB DNA binding 497 519 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +P21538 UniProtKB Modified residue 355 355 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P21538 UniProtKB Cross-link 807 807 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15542864;Dbxref=PMID:15542864 +P21538 UniProtKB Sequence conflict 56 56 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21538 UniProtKB Sequence conflict 592 618 . . . Note=AAAAIQEQQQLLQQKQQDDDDAIAAAA->RAVVFKNNNNFFNKSSKMMTMLLRSC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21538 UniProtKB Sequence conflict 627 627 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21538 UniProtKB Sequence conflict 636 636 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P42073 1 533 +P42073 UniProtKB Chain 1 533 . . . ID=PRO_0000097239;Note=RNA end formation protein 2 +P42073 UniProtKB Compositional bias 321 331 . . . Note=Ser/Thr-rich +##sequence-region P28519 1 371 +P28519 UniProtKB Chain 1 371 . . . ID=PRO_0000208654;Note=DNA repair protein RAD14 +P28519 UniProtKB Zinc finger 191 216 . . . . +P28519 UniProtKB Mutagenesis 207 207 . . . Note=In RAD14-2%3B loss of recognition of cyclobutane pyrimidine dimers. V->M +P28519 UniProtKB Mutagenesis 216 216 . . . Note=In RAD14-2%3B loss of recognition of cyclobutane pyrimidine dimers. C->Y +P28519 UniProtKB Turn 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D +P28519 UniProtKB Helix 202 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D +P28519 UniProtKB Helix 214 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D +P28519 UniProtKB Helix 221 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D +P28519 UniProtKB Beta strand 226 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D +P28519 UniProtKB Helix 229 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D +P28519 UniProtKB Helix 240 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D +P28519 UniProtKB Turn 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D +P28519 UniProtKB Beta strand 252 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D +P28519 UniProtKB Beta strand 265 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D +P28519 UniProtKB Helix 270 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D +P28519 UniProtKB Helix 283 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5A3D +##sequence-region P10862 1 487 +P10862 UniProtKB Chain 1 487 . . . ID=PRO_0000056161;Note=Postreplication repair E3 ubiquitin-protein ligase RAD18 +P10862 UniProtKB Domain 278 312 . . . Note=SAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00186 +P10862 UniProtKB Zinc finger 28 66 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +P10862 UniProtKB Zinc finger 190 210 . . . Note=UBZ-type +P10862 UniProtKB Modified residue 155 155 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P10862 UniProtKB Modified residue 174 174 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P10862 UniProtKB Cross-link 204 204 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q12021 1 506 +Q12021 UniProtKB Chain 1 506 . . . ID=PRO_0000268697;Note=Radiation-sensitive protein 28 +Q12021 UniProtKB Repeat 55 94 . . . Note=WD 1 +Q12021 UniProtKB Repeat 193 233 . . . Note=WD 2 +Q12021 UniProtKB Repeat 285 325 . . . Note=WD 3 +Q12021 UniProtKB Repeat 357 396 . . . Note=WD 4 +Q12021 UniProtKB Repeat 404 451 . . . Note=WD 5 +##sequence-region P12753 1 1312 +P12753 UniProtKB Chain 1 1312 . . . ID=PRO_0000138648;Note=DNA repair protein RAD50 +P12753 UniProtKB Domain 640 741 . . . Note=Zinc-hook;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00471 +P12753 UniProtKB Nucleotide binding 34 41 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12753 UniProtKB Coiled coil 185 347 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12753 UniProtKB Coiled coil 403 558 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12753 UniProtKB Coiled coil 640 678 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12753 UniProtKB Coiled coil 712 741 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12753 UniProtKB Coiled coil 787 1108 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12753 UniProtKB Compositional bias 1204 1241 . . . Note=Ala/Asp-rich (DA-box) +P12753 UniProtKB Metal binding 687 687 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00471 +P12753 UniProtKB Metal binding 690 690 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00471 +P12753 UniProtKB Modified residue 469 469 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P12753 UniProtKB Modified residue 568 568 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P32863 1 898 +P32863 UniProtKB Chain 1 898 . . . ID=PRO_0000074344;Note=DNA repair and recombination protein RAD54 +P32863 UniProtKB Domain 322 504 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P32863 UniProtKB Domain 659 812 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P32863 UniProtKB Nucleotide binding 335 342 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P32863 UniProtKB Motif 21 25 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32863 UniProtKB Motif 41 45 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32863 UniProtKB Motif 455 458 . . . Note=DEGH box +##sequence-region Q08760 1 435 +Q08760 UniProtKB Chain 1 435 . . . ID=PRO_0000262736;Note=Bud site selection protein RAX1 +Q08760 UniProtKB Topological domain 1 297 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08760 UniProtKB Transmembrane 298 318 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08760 UniProtKB Topological domain 319 325 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08760 UniProtKB Transmembrane 326 346 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08760 UniProtKB Topological domain 347 409 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08760 UniProtKB Transmembrane 410 430 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08760 UniProtKB Topological domain 431 435 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08760 UniProtKB Domain 126 257 . . . Note=RGS +Q08760 UniProtKB Modified residue 167 167 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region Q03713 1 159 +Q03713 UniProtKB Chain 1 159 . . . ID=PRO_0000215779;Note=Respiratory supercomplex factor 1%2C mitochondrial +Q03713 UniProtKB Transmembrane 32 52 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00836 +Q03713 UniProtKB Transmembrane 68 88 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00836 +Q03713 UniProtKB Domain 5 96 . . . Note=HIG1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00836 +Q03713 UniProtKB Coiled coil 88 159 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12044 1 265 +Q12044 UniProtKB Chain 1 265 . . . ID=PRO_0000237641;Note=Regulator of calcineurin 2 +Q12044 UniProtKB Compositional bias 141 204 . . . Note=Ser-rich +Q12044 UniProtKB Modified residue 104 104 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q12044 UniProtKB Modified residue 110 110 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12044 UniProtKB Modified residue 132 132 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12044 UniProtKB Modified residue 152 152 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q12044 UniProtKB Modified residue 157 157 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12044 UniProtKB Modified residue 160 160 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q12044 UniProtKB Modified residue 183 183 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198 +Q12044 UniProtKB Modified residue 187 187 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12044 UniProtKB Modified residue 193 193 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12044 UniProtKB Modified residue 201 201 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12044 UniProtKB Modified residue 255 255 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q04779 1 684 +Q04779 UniProtKB Chain 1 684 . . . ID=PRO_0000203282;Note=Transcriptional regulatory protein RCO1 +Q04779 UniProtKB Zinc finger 260 309 . . . Note=PHD-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 +Q04779 UniProtKB Zinc finger 414 472 . . . Note=PHD-type 2%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 +Q04779 UniProtKB Compositional bias 15 30 . . . Note=Poly-Ser +Q04779 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q04779 UniProtKB Modified residue 68 68 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04779 UniProtKB Modified residue 683 683 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P38212 1 213 +P38212 UniProtKB Chain 1 213 . . . ID=PRO_0000202466;Note=Protein RCR1 +P38212 UniProtKB Topological domain 1 39 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38212 UniProtKB Transmembrane 40 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38212 UniProtKB Topological domain 63 213 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38212 UniProtKB Motif 104 107 . . . Note=PY motif +P38212 UniProtKB Mutagenesis 82 83 . . . Note=Reduced interaction with WW domain of RSP5. No interaction with WW domain of RSP5%3B when in association with A-105. PP->QA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17213653;Dbxref=PMID:17213653 +P38212 UniProtKB Mutagenesis 105 105 . . . Note=Reduced interaction with WW domain of RSP5. No interaction with WW domain of RSP5%3B when in association with 82-QA-83. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17213653;Dbxref=PMID:17213653 +P38212 UniProtKB Mutagenesis 130 130 . . . Note=No effect in conferring Congo red resistance%3B when associated with A-208. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17213653;Dbxref=PMID:17213653 +P38212 UniProtKB Mutagenesis 208 208 . . . Note=No effect in conferring Congo red resistance%3B when associated with A-130. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17213653;Dbxref=PMID:17213653 +##sequence-region P25611 1 832 +P25611 UniProtKB Chain 1 832 . . . ID=PRO_0000114994;Note=Regulator of drug sensitivity 1 +P25611 UniProtKB DNA binding 15 42 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +##sequence-region P19541 1 446 +P19541 UniProtKB Chain 1 446 . . . ID=PRO_0000115006;Note=Regulator of drug sensitivity 2 +P19541 UniProtKB DNA binding 15 45 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P19541 UniProtKB Modified residue 102 102 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P19541 UniProtKB Modified residue 231 231 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P14291 1 827 +P14291 UniProtKB Chain 1 827 . . . ID=PRO_0000097234;Note=Protein RED1 +##sequence-region P40893 1 198 +P40893 UniProtKB Chain 1 198 . . . ID=PRO_0000203011;Note=Regulation of enolase protein 1 +P40893 UniProtKB Helix 9 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12 +P40893 UniProtKB Beta strand 13 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12 +P40893 UniProtKB Beta strand 19 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12 +P40893 UniProtKB Beta strand 27 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12 +P40893 UniProtKB Beta strand 38 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12 +P40893 UniProtKB Turn 42 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12 +P40893 UniProtKB Beta strand 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12 +P40893 UniProtKB Beta strand 51 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12 +P40893 UniProtKB Beta strand 60 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12 +P40893 UniProtKB Beta strand 78 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12 +P40893 UniProtKB Beta strand 89 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12 +P40893 UniProtKB Beta strand 101 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12 +P40893 UniProtKB Beta strand 126 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12 +P40893 UniProtKB Beta strand 137 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12 +P40893 UniProtKB Beta strand 151 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12 +P40893 UniProtKB Beta strand 164 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12 +P40893 UniProtKB Beta strand 172 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12 +P40893 UniProtKB Beta strand 178 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O12 +##sequence-region Q00816 1 1014 +Q00816 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +Q00816 UniProtKB Chain 2 1014 . . . ID=PRO_0000083953;Note=Resistance to glucose repression protein 1 +Q00816 UniProtKB Motif 277 283 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q00816 UniProtKB Motif 595 599 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q00816 UniProtKB Motif 873 879 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q00816 UniProtKB Compositional bias 543 552 . . . Note=Ser-rich +Q00816 UniProtKB Compositional bias 742 760 . . . Note=Asp/Glu-rich (acidic) +Q00816 UniProtKB Compositional bias 834 844 . . . Note=Asp/Glu-rich (acidic) +Q00816 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +Q00816 UniProtKB Modified residue 73 73 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q00816 UniProtKB Modified residue 75 75 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +Q00816 UniProtKB Modified residue 242 242 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00816 UniProtKB Modified residue 254 254 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q00816 UniProtKB Modified residue 311 311 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q00816 UniProtKB Modified residue 421 421 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q00816 UniProtKB Modified residue 480 480 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q00816 UniProtKB Modified residue 490 490 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q00816 UniProtKB Modified residue 570 570 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00816 UniProtKB Modified residue 572 572 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q00816 UniProtKB Modified residue 576 576 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q00816 UniProtKB Modified residue 610 610 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00816 UniProtKB Modified residue 614 614 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00816 UniProtKB Modified residue 680 680 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q00816 UniProtKB Modified residue 896 896 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00816 UniProtKB Modified residue 898 898 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00816 UniProtKB Modified residue 980 980 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00816 UniProtKB Sequence conflict 376 377 . . . Note=DK->EE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00816 UniProtKB Sequence conflict 534 534 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00816 UniProtKB Sequence conflict 657 657 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00816 UniProtKB Sequence conflict 889 889 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00816 UniProtKB Sequence conflict 988 1014 . . . Note=ARGMASKYLHSWKKSDVKPQENGNDSS->QEVWQASTCTLGKRVTSSHKKMEMTAVRRKNFEVNMKRK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06709 1 432 +Q06709 UniProtKB Chain 1 432 . . . ID=PRO_0000268700;Note=Cytoplasmic 60S subunit biogenesis factor REH1 +Q06709 UniProtKB Zinc finger 6 30 . . . Note=C2H2-type 1 +Q06709 UniProtKB Zinc finger 186 209 . . . Note=C2H2-type 2 +Q06709 UniProtKB Zinc finger 237 261 . . . Note=C2H2-type 3 +##sequence-region P38344 1 393 +P38344 UniProtKB Chain 1 393 . . . ID=PRO_0000202529;Note=Cytoplasmic 60S subunit biogenesis factor REI1 +P38344 UniProtKB Zinc finger 7 31 . . . Note=C2H2-type 1 +P38344 UniProtKB Zinc finger 162 187 . . . Note=C2H2-type 2 +P38344 UniProtKB Zinc finger 215 239 . . . Note=C2H2-type 3 +P38344 UniProtKB Modified residue 140 140 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38344 UniProtKB Sequence conflict 152 153 . . . Note=KL->NV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38344 UniProtKB Sequence conflict 152 153 . . . Note=KL->NV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12090 1 404 +Q12090 UniProtKB Chain 1 404 . . . ID=PRO_0000120937;Note=RNA exonuclease 3 +Q12090 UniProtKB Domain 243 389 . . . Note=Exonuclease +##sequence-region Q04418 1 439 +Q04418 UniProtKB Chain 1 439 . . . ID=PRO_0000255972;Note=RNA polymerase II-associated protein RBA50 +Q04418 UniProtKB Sequence conflict 192 194 . . . Note=EEA->GEG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39729 1 369 +P39729 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P39729 UniProtKB Chain 2 369 . . . ID=PRO_0000205449;Note=Ribosome-interacting GTPase 1 +P39729 UniProtKB Domain 66 292 . . . Note=OBG-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +P39729 UniProtKB Nucleotide binding 72 79 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +P39729 UniProtKB Nucleotide binding 118 122 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +P39729 UniProtKB Nucleotide binding 250 253 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01047 +P39729 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P39729 UniProtKB Helix 3 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Turn 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Helix 25 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Turn 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 64 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Helix 76 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Helix 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 102 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 112 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Helix 120 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Helix 132 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 144 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Helix 155 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 171 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 180 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 186 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 190 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Helix 203 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 217 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Helix 228 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Turn 236 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 241 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 245 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Helix 252 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Helix 257 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 269 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Turn 274 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Helix 280 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 294 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 307 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 311 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Helix 320 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Helix 329 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 335 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 345 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +P39729 UniProtKB Beta strand 363 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A9A +##sequence-region P53721 1 224 +P53721 UniProtKB Chain 1 224 . . . ID=PRO_0000215780;Note=Respiratory supercomplex factor 2%2C mitochondrial +P53721 UniProtKB Transmembrane 19 39 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00836 +P53721 UniProtKB Transmembrane 50 70 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00836 +P53721 UniProtKB Transmembrane 152 172 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00836 +P53721 UniProtKB Domain 89 180 . . . Note=HIG1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00836 +P53721 UniProtKB Compositional bias 196 199 . . . Note=Poly-Glu +##sequence-region P38623 1 610 +P38623 UniProtKB Chain 1 610 . . . ID=PRO_0000086604;Note=Serine/threonine-protein kinase RCK2 +P38623 UniProtKB Domain 163 478 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38623 UniProtKB Nucleotide binding 169 177 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38623 UniProtKB Region 493 506 . . . Note=Calmodulin-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38623 UniProtKB Active site 313 313 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P38623 UniProtKB Binding site 201 201 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38623 UniProtKB Modified residue 46 46 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38623 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38623 UniProtKB Modified residue 187 187 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38623 UniProtKB Modified residue 350 350 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38623 UniProtKB Modified residue 520 520 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10805732;Dbxref=PMID:10805732 +P38623 UniProtKB Sequence conflict 109 109 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38623 UniProtKB Sequence conflict 109 109 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38623 UniProtKB Sequence conflict 188 188 . . . Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38623 UniProtKB Sequence conflict 188 188 . . . Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38623 UniProtKB Sequence conflict 233 233 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38623 UniProtKB Sequence conflict 233 233 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38623 UniProtKB Sequence conflict 328 328 . . . Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38623 UniProtKB Sequence conflict 328 328 . . . Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38623 UniProtKB Sequence conflict 456 456 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38623 UniProtKB Sequence conflict 456 456 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36054 1 211 +P36054 UniProtKB Chain 1 211 . . . ID=PRO_0000211424;Note=Calcipressin-like protein +P36054 UniProtKB Modified residue 113 113 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36054 UniProtKB Modified residue 117 117 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P36054 UniProtKB Modified residue 182 182 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38086 1 958 +P38086 UniProtKB Chain 1 958 . . . ID=PRO_0000074346;Note=DNA repair and recombination protein RDH54 +P38086 UniProtKB Domain 333 521 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P38086 UniProtKB Domain 665 824 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P38086 UniProtKB Nucleotide binding 380 387 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P38086 UniProtKB Motif 506 509 . . . Note=DEGH box +P38086 UniProtKB Cross-link 649 649 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38086 UniProtKB Mutagenesis 352 352 . . . Note=1%25-2%25 of the ATPase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10970884;Dbxref=PMID:10970884 +P38086 UniProtKB Sequence conflict 752 752 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38086 UniProtKB Sequence conflict 752 752 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08742 1 149 +Q08742 UniProtKB Transit peptide 1 25 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08742 UniProtKB Chain 26 149 . . . ID=PRO_0000245268;Note=Thiosulfate sulfurtransferase RDL2%2C mitochondrial +Q08742 UniProtKB Domain 45 146 . . . Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173 +Q08742 UniProtKB Active site 106 106 . . . Note=Cysteine persulfide intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173 +##sequence-region P33323 1 182 +P33323 UniProtKB Chain 1 182 . . . ID=PRO_0000097216;Note=Meiotic recombination protein REC104 +##sequence-region Q12188 1 680 +Q12188 UniProtKB Chain 1 680 . . . ID=PRO_0000268699;Note=Meiotic recombination protein REC8 +Q12188 UniProtKB Site 431 432 . . . Note=Cleavage%3B by ESP1 +Q12188 UniProtKB Site 453 454 . . . Note=Cleavage%3B by ESP1 +Q12188 UniProtKB Mutagenesis 428 428 . . . Note=Abolishes cleavage by ESP1 at position R-431%3B when associated with E-431. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11081626;Dbxref=PMID:11081626 +Q12188 UniProtKB Mutagenesis 431 431 . . . Note=Reduces cleavage by ESP1 at position R-431. Abolishes cleavage by ESP1 at position R-431%3B when associated with R-428. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11081626;Dbxref=PMID:11081626 +Q12188 UniProtKB Mutagenesis 453 453 . . . Note=Abolishes cleavage by ESP1 at position R-453. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11081626;Dbxref=PMID:11081626 +##sequence-region P38232 1 338 +P38232 UniProtKB Chain 1 338 . . . ID=PRO_0000071523;Note=Protein REG2 +##sequence-region P01119 1 309 +P01119 UniProtKB Chain 1 306 . . . ID=PRO_0000030193;Note=Ras-like protein 1 +P01119 UniProtKB Propeptide 307 309 . . . ID=PRO_0000030194;Note=Removed in mature form +P01119 UniProtKB Nucleotide binding 17 24 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P01119 UniProtKB Nucleotide binding 64 68 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P01119 UniProtKB Nucleotide binding 123 126 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P01119 UniProtKB Motif 39 47 . . . Note=Effector region +P01119 UniProtKB Modified residue 306 306 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2050108;Dbxref=PMID:2050108 +P01119 UniProtKB Lipidation 305 305 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3513173;Dbxref=PMID:3513173 +P01119 UniProtKB Lipidation 306 306 . . . Note=S-farnesyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1763050;Dbxref=PMID:1763050 +P01119 UniProtKB Mutagenesis 66 66 . . . Note=Impaired GTPase activity%2C autophosphorylating activity. A->T +P01119 UniProtKB Mutagenesis 68 68 . . . Note=Impaired GTPase activity. Q->L +P01119 UniProtKB Sequence conflict 204 204 . . . Note=R->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P01120 1 322 +P01120 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2406252;Dbxref=PMID:2406252 +P01120 UniProtKB Chain 2 319 . . . ID=PRO_0000030195;Note=Ras-like protein 2 +P01120 UniProtKB Propeptide 320 322 . . . ID=PRO_0000030196;Note=Removed in mature form +P01120 UniProtKB Nucleotide binding 17 24 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P01120 UniProtKB Nucleotide binding 64 68 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P01120 UniProtKB Nucleotide binding 123 126 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P01120 UniProtKB Motif 39 47 . . . Note=Effector region +P01120 UniProtKB Modified residue 198 198 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P01120 UniProtKB Modified residue 202 202 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P01120 UniProtKB Modified residue 207 207 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P01120 UniProtKB Modified residue 214 214 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P01120 UniProtKB Modified residue 235 235 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198 +P01120 UniProtKB Modified residue 238 238 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198 +P01120 UniProtKB Modified residue 319 319 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2050108,ECO:0000269|PubMed:2663844;Dbxref=PMID:2050108,PMID:2663844 +P01120 UniProtKB Lipidation 318 318 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2406252;Dbxref=PMID:2406252 +P01120 UniProtKB Lipidation 319 319 . . . Note=S-farnesyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1763050;Dbxref=PMID:1763050 +P01120 UniProtKB Cross-link 131 131 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P01120 UniProtKB Mutagenesis 19 19 . . . Note=Low sporulation efficiency. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6327067;Dbxref=PMID:6327067 +P01120 UniProtKB Mutagenesis 70 70 . . . Note=In GLC5-1%3B low glycogen accumulation and sporulation deficiency. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8150278;Dbxref=PMID:8150278 +P01120 UniProtKB Sequence conflict 108 108 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P01120 UniProtKB Sequence conflict 210 210 . . . Note=H->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P01120 UniProtKB Sequence conflict 255 255 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P01120 UniProtKB Sequence conflict 298 299 . . . Note=KQ->SK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47104 1 1357 +P47104 UniProtKB Chain 1 1357 . . . ID=PRO_0000051183;Note=Regulator of V-ATPase in vacuolar membrane protein 1 +P47104 UniProtKB Repeat 98 134 . . . Note=WD 1 +P47104 UniProtKB Repeat 142 182 . . . Note=WD 2 +P47104 UniProtKB Repeat 190 239 . . . Note=WD 3 +P47104 UniProtKB Repeat 384 423 . . . Note=WD 4 +P47104 UniProtKB Repeat 431 470 . . . Note=WD 5 +P47104 UniProtKB Repeat 595 636 . . . Note=WD 6 +P47104 UniProtKB Repeat 638 679 . . . Note=WD 7 +P47104 UniProtKB Repeat 898 939 . . . Note=WD 8 +P47104 UniProtKB Modified residue 1244 1244 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198 +P47104 UniProtKB Modified residue 1248 1248 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q12192 1 310 +Q12192 UniProtKB Chain 1 310 . . . ID=PRO_0000097309;Note=Repression factor of MSEs protein 1 +Q12192 UniProtKB Compositional bias 95 100 . . . Note=Poly-Ser +Q12192 UniProtKB Compositional bias 128 135 . . . Note=Poly-Arg +Q12192 UniProtKB Modified residue 215 215 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P40043 1 161 +P40043 UniProtKB Chain 1 161 . . . ID=PRO_0000202633;Note=Respiratory growth induced protein 1 +P40043 UniProtKB Cross-link 68 68 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P40043 UniProtKB Beta strand 17 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY +P40043 UniProtKB Helix 28 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY +P40043 UniProtKB Beta strand 48 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY +P40043 UniProtKB Helix 56 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY +P40043 UniProtKB Turn 61 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY +P40043 UniProtKB Helix 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY +P40043 UniProtKB Helix 78 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY +P40043 UniProtKB Helix 92 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY +P40043 UniProtKB Beta strand 108 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY +P40043 UniProtKB Beta strand 116 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY +P40043 UniProtKB Beta strand 132 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY +P40043 UniProtKB Beta strand 149 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BCY +##sequence-region P32862 1 1170 +P32862 UniProtKB Chain 1 1170 . . . ID=PRO_0000115001;Note=Glucose transport transcription regulator RGT1 +P32862 UniProtKB DNA binding 47 76 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P32862 UniProtKB Modified residue 202 202 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +P32862 UniProtKB Modified residue 205 205 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32862 UniProtKB Modified residue 208 208 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32862 UniProtKB Modified residue 229 229 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198 +P32862 UniProtKB Modified residue 283 283 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32862 UniProtKB Modified residue 284 284 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32862 UniProtKB Modified residue 410 410 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32862 UniProtKB Modified residue 414 414 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32862 UniProtKB Modified residue 1130 1130 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P25378 1 209 +P25378 UniProtKB Chain 1 206 . . . ID=PRO_0000082713;Note=Rheb-like protein RHB1 +P25378 UniProtKB Propeptide 207 209 . . . ID=PRO_0000281370;Note=Removed in mature form +P25378 UniProtKB Nucleotide binding 23 30 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25378 UniProtKB Nucleotide binding 70 74 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25378 UniProtKB Nucleotide binding 129 132 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25378 UniProtKB Motif 45 53 . . . Note=Effector region +P25378 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P25378 UniProtKB Modified residue 206 206 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25378 UniProtKB Lipidation 206 206 . . . Note=S-farnesyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10753927;Dbxref=PMID:10753927 +##sequence-region Q12305 1 139 +Q12305 UniProtKB Chain 1 139 . . . ID=PRO_0000245269;Note=Thiosulfate sulfurtransferase RDL1%2C mitochondrial +Q12305 UniProtKB Domain 37 138 . . . Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173 +Q12305 UniProtKB Active site 98 98 . . . Note=Cysteine persulfide intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173 +Q12305 UniProtKB Modified residue 26 26 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12305 UniProtKB Helix 27 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P +Q12305 UniProtKB Beta strand 41 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P +Q12305 UniProtKB Helix 49 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P +Q12305 UniProtKB Turn 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P +Q12305 UniProtKB Helix 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P +Q12305 UniProtKB Helix 76 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P +Q12305 UniProtKB Beta strand 92 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P +Q12305 UniProtKB Beta strand 99 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P +Q12305 UniProtKB Helix 102 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P +Q12305 UniProtKB Turn 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P +Q12305 UniProtKB Beta strand 118 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P +Q12305 UniProtKB Helix 125 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P +Q12305 UniProtKB Helix 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3D1P +##sequence-region P53331 1 553 +P53331 UniProtKB Chain 1 553 . . . ID=PRO_0000202869;Note=RNA exonuclease 1 +P53331 UniProtKB Domain 225 373 . . . Note=Exonuclease +P53331 UniProtKB Coiled coil 167 194 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53331 UniProtKB Coiled coil 509 533 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53331 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53331 UniProtKB Mutagenesis 305 305 . . . Note=In REX1-1%3B impairs 5S rRNA maturation. L->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16100378;Dbxref=PMID:16100378 +##sequence-region Q08237 1 289 +Q08237 UniProtKB Chain 1 289 . . . ID=PRO_0000131702;Note=RNA exonuclease 4 +Q08237 UniProtKB Domain 121 273 . . . Note=Exonuclease +##sequence-region P38630 1 861 +P38630 UniProtKB Chain 1 861 . . . ID=PRO_0000121776;Note=Replication factor C subunit 1 +P38630 UniProtKB Domain 153 243 . . . Note=BRCT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033 +P38630 UniProtKB Nucleotide binding 353 361 . . . Note=ATP +P38630 UniProtKB Motif 830 834 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38630 UniProtKB Motif 855 860 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38630 UniProtKB Binding site 299 299 . . . Note=ATP%3B via carbonyl oxygen +P38630 UniProtKB Binding site 311 311 . . . Note=ATP%3B via amide nitrogen and carbonyl oxygen +P38630 UniProtKB Binding site 456 456 . . . Note=ATP +P38630 UniProtKB Modified residue 38 38 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38630 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38630 UniProtKB Modified residue 63 63 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38630 UniProtKB Mutagenesis 427 427 . . . Note=In cs mutant CDC44-2%3B causes cell cycle arrest. D->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8264593;Dbxref=PMID:8264593 +P38630 UniProtKB Mutagenesis 436 436 . . . Note=In cs mutant CDC44-3/4%3B causes cell cycle arrest. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8264593;Dbxref=PMID:8264593 +P38630 UniProtKB Mutagenesis 512 512 . . . Note=In cs mutant CDC44-9%3B no effect. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8264593;Dbxref=PMID:8264593 +P38630 UniProtKB Mutagenesis 513 513 . . . Note=In cs mutants CDC44-1/5/8 and CDC44-9%3B causes cell cycle arrest. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8264593;Dbxref=PMID:8264593 +P38630 UniProtKB Helix 298 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 307 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 314 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 327 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Turn 333 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Beta strand 347 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 359 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Beta strand 373 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 385 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 392 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Turn 402 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Beta strand 418 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 426 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 436 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Beta strand 451 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 464 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Turn 467 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Beta strand 470 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 480 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 502 509 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Turn 510 512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 514 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 523 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 535 544 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Turn 545 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 550 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 561 563 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 568 570 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 574 581 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Turn 585 587 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 588 595 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Beta strand 596 602 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 610 631 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 638 640 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 641 648 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 650 654 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 669 687 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Turn 688 692 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 699 703 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Turn 704 706 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 707 714 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 725 730 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Turn 731 733 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38630 UniProtKB Helix 737 746 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +##sequence-region P38629 1 340 +P38629 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38629 UniProtKB Chain 2 340 . . . ID=PRO_0000121756;Note=Replication factor C subunit 3 +P38629 UniProtKB Nucleotide binding 16 19 . . . Note=ATP +P38629 UniProtKB Nucleotide binding 53 61 . . . Note=ATP +P38629 UniProtKB Binding site 20 20 . . . Note=ATP +P38629 UniProtKB Binding site 28 28 . . . Note=ATP%3B via amide nitrogen and carbonyl oxygen +P38629 UniProtKB Binding site 148 148 . . . Note=ATP +P38629 UniProtKB Binding site 206 206 . . . Note=ATP +P38629 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38629 UniProtKB Helix 15 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 24 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 31 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Beta strand 49 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Beta strand 54 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 59 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 75 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Beta strand 79 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 90 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 96 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Beta strand 106 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Beta strand 112 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 119 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 124 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Turn 137 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Beta strand 141 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 155 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Beta strand 161 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 171 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Turn 184 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 191 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 205 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Turn 212 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Beta strand 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 229 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 241 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 256 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Turn 269 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 274 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 293 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38629 UniProtKB Helix 316 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +##sequence-region Q99188 1 309 +Q99188 UniProtKB Chain 1 309 . . . ID=PRO_0000268701;Note=Regulator of G-protein signaling 2 +Q99188 UniProtKB Domain 37 161 . . . Note=RGS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00171 +Q99188 UniProtKB Mutagenesis 63 63 . . . Note=Decreases the ability to suppress glucose-induced cAMP signaling when overexpressed. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523302;Dbxref=PMID:10523302 +Q99188 UniProtKB Mutagenesis 144 144 . . . Note=Abolishes the ability to suppress glucose-induced cAMP signaling when overexpressed. L->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10523302;Dbxref=PMID:10523302 +##sequence-region Q06624 1 347 +Q06624 UniProtKB Chain 1 347 . . . ID=PRO_0000194975;Note=DNA damage tolerance protein RHC31 +Q06624 UniProtKB Modified residue 9 9 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06624 UniProtKB Cross-link 35 35 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15166219;Dbxref=PMID:15166219 +##sequence-region P40395 1 1056 +P40395 UniProtKB Chain 1 1056 . . . ID=PRO_0000097332;Note=Guanine nucleotide exchange factor subunit RIC1 +##sequence-region P43565 1 1770 +P43565 UniProtKB Chain 1 1770 . . . ID=PRO_0000086605;Note=Serine/threonine-protein kinase RIM15 +P43565 UniProtKB Domain 794 1254 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P43565 UniProtKB Domain 1255 1320 . . . Note=AGC-kinase C-terminal +P43565 UniProtKB Domain 1636 1750 . . . Note=Response regulatory;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00169 +P43565 UniProtKB Nucleotide binding 800 808 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P43565 UniProtKB Compositional bias 343 358 . . . Note=Poly-Asn +P43565 UniProtKB Compositional bias 620 624 . . . Note=Poly-Ser +P43565 UniProtKB Compositional bias 975 980 . . . Note=Poly-Asn +P43565 UniProtKB Compositional bias 1213 1218 . . . Note=Poly-Glu +P43565 UniProtKB Compositional bias 1386 1391 . . . Note=Poly-Thr +P43565 UniProtKB Active site 918 918 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P43565 UniProtKB Binding site 823 823 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P43565 UniProtKB Modified residue 380 380 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P43565 UniProtKB Modified residue 476 476 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P43565 UniProtKB Modified residue 704 704 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P43565 UniProtKB Modified residue 709 709 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43565 UniProtKB Modified residue 733 733 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P43565 UniProtKB Modified residue 736 736 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43565 UniProtKB Modified residue 737 737 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43565 UniProtKB Modified residue 747 747 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P43565 UniProtKB Modified residue 1044 1044 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43565 UniProtKB Modified residue 1048 1048 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43565 UniProtKB Modified residue 1064 1064 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43565 UniProtKB Modified residue 1075 1075 . . . Note=Phosphothreonine%3B by PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16308562;Dbxref=PMID:16308562 +P43565 UniProtKB Modified residue 1421 1421 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43565 UniProtKB Modified residue 1531 1531 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43565 UniProtKB Modified residue 1538 1538 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43565 UniProtKB Modified residue 1542 1542 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43565 UniProtKB Modified residue 1565 1565 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43565 UniProtKB Modified residue 1764 1764 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P43565 UniProtKB Mutagenesis 823 823 . . . Note=Loss of kinase activity. K->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9744870;Dbxref=PMID:9744870 +##sequence-region Q08003 1 200 +Q08003 UniProtKB Chain 1 200 . . . ID=PRO_0000247248;Note=Regulator of free ubiquitin chains 1 +Q08003 UniProtKB Compositional bias 75 81 . . . Note=Poly-Ser +##sequence-region P39083 1 1007 +P39083 UniProtKB Chain 1 1007 . . . ID=PRO_0000075899;Note=Rho-type GTPase-activating protein 1 +P39083 UniProtKB Domain 13 66 . . . Note=LIM zinc-binding 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125 +P39083 UniProtKB Domain 70 122 . . . Note=LIM zinc-binding 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125 +P39083 UniProtKB Domain 791 1006 . . . Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172 +P39083 UniProtKB Modified residue 278 278 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P39083 UniProtKB Modified residue 291 291 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39083 UniProtKB Modified residue 532 532 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39083 UniProtKB Natural variant 866 866 . . . Note=V->A +P39083 UniProtKB Natural variant 898 898 . . . Note=K->R +P39083 UniProtKB Natural variant 926 926 . . . Note=S->G +P39083 UniProtKB Mutagenesis 37 37 . . . Note=Bipolar budding. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8657111;Dbxref=PMID:8657111 +P39083 UniProtKB Mutagenesis 40 40 . . . Note=Bipolar budding. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8657111;Dbxref=PMID:8657111 +P39083 UniProtKB Mutagenesis 98 98 . . . Note=Bipolar budding. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8657111;Dbxref=PMID:8657111 +P39083 UniProtKB Mutagenesis 101 101 . . . Note=Bipolar budding. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8657111;Dbxref=PMID:8657111 +P39083 UniProtKB Sequence conflict 457 457 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39083 UniProtKB Sequence conflict 507 507 . . . Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06108 1 1083 +Q06108 UniProtKB Chain 1 1083 . . . ID=PRO_0000242488;Note=Regulator of the glycerol channel 1 +Q06108 UniProtKB Domain 495 606 . . . Note=PH +Q06108 UniProtKB Modified residue 136 136 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06108 UniProtKB Modified residue 249 249 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06108 UniProtKB Modified residue 252 252 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06108 UniProtKB Modified residue 481 481 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06108 UniProtKB Modified residue 537 537 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06108 UniProtKB Modified residue 652 652 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06108 UniProtKB Modified residue 765 765 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06108 UniProtKB Modified residue 813 813 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06108 UniProtKB Modified residue 817 817 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06108 UniProtKB Modified residue 857 857 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06108 UniProtKB Modified residue 866 866 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06108 UniProtKB Modified residue 879 879 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06108 UniProtKB Modified residue 918 918 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06108 UniProtKB Modified residue 966 966 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06108 UniProtKB Modified residue 969 969 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06108 UniProtKB Modified residue 975 975 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06108 UniProtKB Modified residue 1059 1059 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06108 UniProtKB Modified residue 1081 1081 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06108 UniProtKB Modified residue 1082 1082 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P16664 1 663 +P16664 UniProtKB Chain 1 663 . . . ID=PRO_0000097319;Note=Guanine nucleotide exchange factor subunit RGP1 +P16664 UniProtKB Modified residue 351 351 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P16664 UniProtKB Modified residue 354 354 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P16664 UniProtKB Modified residue 357 357 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P16664 UniProtKB Modified residue 363 363 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P16664 UniProtKB Modified residue 364 364 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P16664 UniProtKB Modified residue 370 370 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P16664 UniProtKB Sequence conflict 52 56 . . . Note=EKLLT->KAS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12300 1 763 +Q12300 UniProtKB Chain 1 763 . . . ID=PRO_0000050389;Note=High-affinity glucose transporter RGT2 +Q12300 UniProtKB Topological domain 1 99 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Transmembrane 100 120 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Topological domain 121 144 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Transmembrane 145 165 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Topological domain 166 175 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Transmembrane 176 196 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Topological domain 197 197 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Transmembrane 198 218 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Topological domain 219 231 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Transmembrane 232 252 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Topological domain 253 266 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Transmembrane 267 287 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Topological domain 288 357 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Transmembrane 358 378 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Topological domain 379 393 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Transmembrane 394 414 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Topological domain 415 421 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Transmembrane 422 442 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Topological domain 443 452 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Transmembrane 453 473 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Topological domain 474 491 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Transmembrane 492 512 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Topological domain 513 524 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Transmembrane 525 545 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Topological domain 546 763 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Glycosylation 136 136 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Glycosylation 385 385 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12300 UniProtKB Mutagenesis 231 231 . . . Note=In RGT2-1%3B constitutively signaling glucose receptor. R->K +##sequence-region P21524 1 888 +P21524 UniProtKB Chain 1 888 . . . ID=PRO_0000187203;Note=Ribonucleoside-diphosphate reductase large chain 1 +P21524 UniProtKB Domain 1 92 . . . Note=ATP-cone;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00492 +P21524 UniProtKB Region 11 17 . . . Note=Allosteric activator binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21524 UniProtKB Region 217 218 . . . Note=Substrate binding +P21524 UniProtKB Region 285 288 . . . Note=Allosteric effector binding%2C determines substrate specificity +P21524 UniProtKB Region 426 430 . . . Note=Substrate binding +P21524 UniProtKB Region 607 611 . . . Note=Substrate binding +P21524 UniProtKB Active site 426 426 . . . Note=Proton acceptor +P21524 UniProtKB Active site 428 428 . . . Note=Cysteine radical intermediate +P21524 UniProtKB Active site 430 430 . . . Note=Proton acceptor +P21524 UniProtKB Binding site 5 5 . . . Note=Allosteric activator;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21524 UniProtKB Binding site 53 53 . . . Note=Allosteric activator;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21524 UniProtKB Binding site 88 88 . . . Note=Allosteric activator;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21524 UniProtKB Binding site 202 202 . . . Note=Substrate +P21524 UniProtKB Binding site 247 247 . . . Note=Substrate%3B via amide nitrogen +P21524 UniProtKB Site 218 218 . . . Note=Important for hydrogen atom transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21524 UniProtKB Site 226 226 . . . Note=Allosteric effector binding%2C determines substrate specificity +P21524 UniProtKB Site 256 256 . . . Note=Allosteric effector binding%2C determines substrate specificity +P21524 UniProtKB Site 443 443 . . . Note=Important for hydrogen atom transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21524 UniProtKB Site 741 741 . . . Note=Important for electron transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21524 UniProtKB Site 742 742 . . . Note=Important for electron transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21524 UniProtKB Site 883 883 . . . Note=Interacts with thioredoxin/glutaredoxin;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21524 UniProtKB Site 886 886 . . . Note=Interacts with thioredoxin/glutaredoxin;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21524 UniProtKB Modified residue 227 227 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P21524 UniProtKB Modified residue 816 816 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21672 +P21524 UniProtKB Modified residue 837 837 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P21524 UniProtKB Modified residue 887 887 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P21524 UniProtKB Disulfide bond 218 443 . . . Note=Redox-active;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16537479;Dbxref=PMID:16537479 +P21524 UniProtKB Cross-link 387 387 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P21524 UniProtKB Cross-link 853 853 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P21524 UniProtKB Mutagenesis 428 428 . . . Note=Completely abolishes reductase activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11893751;Dbxref=PMID:11893751 +P21524 UniProtKB Sequence conflict 329 329 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21524 UniProtKB Sequence conflict 587 589 . . . Note=TLR->NLK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21524 UniProtKB Sequence conflict 666 666 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21524 UniProtKB Sequence conflict 679 679 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21524 UniProtKB Helix 19 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ +P21524 UniProtKB Turn 31 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ +P21524 UniProtKB Helix 36 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ +P21524 UniProtKB Helix 53 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ +P21524 UniProtKB Turn 67 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ +P21524 UniProtKB Helix 79 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVX +P21524 UniProtKB Helix 94 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Turn 107 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 118 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 128 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 137 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 145 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Beta strand 158 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVX +P21524 UniProtKB Helix 167 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 183 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Beta strand 197 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 202 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Beta strand 210 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Beta strand 218 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 228 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Turn 243 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S8A +P21524 UniProtKB Beta strand 247 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Turn 263 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 272 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Turn 288 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVX +P21524 UniProtKB Beta strand 297 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 308 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Turn 312 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Beta strand 317 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 321 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVX +P21524 UniProtKB Beta strand 328 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 336 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Beta strand 347 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Turn 353 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 359 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 364 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Beta strand 380 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 385 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Beta strand 403 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 407 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Turn 415 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Beta strand 427 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ +P21524 UniProtKB Beta strand 441 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Beta strand 445 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 450 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Beta strand 454 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVX +P21524 UniProtKB Beta strand 458 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EUD +P21524 UniProtKB Beta strand 463 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVX +P21524 UniProtKB Helix 467 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 493 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Beta strand 506 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 512 519 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 526 554 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 564 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 571 574 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Beta strand 581 583 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZLG +P21524 UniProtKB Helix 585 595 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 611 615 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Beta strand 619 622 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVS +P21524 UniProtKB Beta strand 627 629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVX +P21524 UniProtKB Beta strand 634 636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ +P21524 UniProtKB Beta strand 638 641 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ +P21524 UniProtKB Helix 643 651 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 657 664 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Turn 665 668 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 678 683 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 687 689 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Helix 692 703 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Beta strand 714 718 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVX +P21524 UniProtKB Helix 721 734 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Beta strand 737 741 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8T +P21524 UniProtKB Beta strand 743 745 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CVX +P21524 UniProtKB Turn 748 751 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ +P21524 UniProtKB Helix 760 763 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ +P21524 UniProtKB Helix 764 766 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ +P21524 UniProtKB Turn 789 791 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZYZ +##sequence-region Q07844 1 837 +Q07844 UniProtKB Chain 1 837 . . . ID=PRO_0000084762;Note=Ribosome biogenesis ATPase RIX7 +Q07844 UniProtKB Nucleotide binding 246 253 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07844 UniProtKB Nucleotide binding 574 581 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07844 UniProtKB Modified residue 42 42 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P26785 1 198 +P26785 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921 +P26785 UniProtKB Chain 2 198 . . . ID=PRO_0000133792;Note=60S ribosomal protein L16-B +P26785 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine%3B partial;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921 +P26785 UniProtKB Modified residue 43 43 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P26785 UniProtKB Modified residue 181 181 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P26785 UniProtKB Modified residue 185 185 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P26785 UniProtKB Modified residue 187 187 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P26785 UniProtKB Cross-link 176 176 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P26785 UniProtKB Sequence conflict 14 14 . . . Note=L->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P46990 1 184 +P46990 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18782943;Dbxref=PMID:18782943 +P46990 UniProtKB Chain 2 184 . . . ID=PRO_0000125348;Note=60S ribosomal protein L17-B +P46990 UniProtKB Modified residue 70 70 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05740 +P46990 UniProtKB Cross-link 46 46 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P38222 1 552 +P38222 UniProtKB Chain 1 552 . . . ID=PRO_0000202472;Note=Ribosomal lysine N-methyltransferase 3 +P38222 UniProtKB Domain 26 335 . . . Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 +P38222 UniProtKB Compositional bias 418 427 . . . Note=Poly-Glu +P38222 UniProtKB Binding site 334 334 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 +##sequence-region P36105 1 138 +P36105 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P36105 UniProtKB Chain 2 138 . . . ID=PRO_0000132043;Note=60S ribosomal protein L14-A +P36105 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P36105 UniProtKB Beta strand 19 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P36105 UniProtKB Beta strand 25 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P36105 UniProtKB Beta strand 32 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P36105 UniProtKB Beta strand 40 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P36105 UniProtKB Helix 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P36105 UniProtKB Beta strand 53 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P36105 UniProtKB Helix 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P36105 UniProtKB Beta strand 63 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P36105 UniProtKB Helix 78 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P36105 UniProtKB Helix 90 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P36105 UniProtKB Helix 98 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P36105 UniProtKB Helix 114 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P36105 UniProtKB Turn 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P0CX49 1 186 +P0CX49 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983894;Dbxref=PMID:11983894 +P0CX49 UniProtKB Chain 2 186 . . . ID=PRO_0000132784;Note=60S ribosomal protein L18-A +P0CX49 UniProtKB Modified residue 50 50 . . . Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22522802;Dbxref=PMID:22522802 +P0CX49 UniProtKB Cross-link 116 116 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX49 UniProtKB Helix 24 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX49 UniProtKB Helix 43 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX49 UniProtKB Helix 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX49 UniProtKB Helix 64 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX49 UniProtKB Turn 74 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P0CX49 UniProtKB Beta strand 79 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX49 UniProtKB Beta strand 100 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX49 UniProtKB Helix 108 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX49 UniProtKB Beta strand 120 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX49 UniProtKB Helix 124 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX49 UniProtKB Beta strand 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX49 UniProtKB Helix 144 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX49 UniProtKB Helix 148 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX49 UniProtKB Turn 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX49 UniProtKB Turn 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P0CX49 UniProtKB Beta strand 169 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3N +P0CX49 UniProtKB Beta strand 177 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX49 UniProtKB Helix 180 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U51 +##sequence-region P0CX24 1 172 +P0CX24 UniProtKB Chain 1 172 . . . ID=PRO_0000409758;Note=60S ribosomal protein L20-B +P0CX24 UniProtKB Modified residue 32 32 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX24 UniProtKB Cross-link 125 125 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX24 UniProtKB Cross-link 131 131 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX24 UniProtKB Cross-link 149 149 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q12672 1 160 +Q12672 UniProtKB Chain 1 160 . . . ID=PRO_0000149683;Note=60S ribosomal protein L21-B +Q12672 UniProtKB Cross-link 32 32 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P0CX41 1 137 +P0CX41 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:16096273;Dbxref=PMID:22814378,PMID:16096273 +P0CX41 UniProtKB Chain 2 137 . . . ID=PRO_0000128630;Note=60S ribosomal protein L23-A +P0CX41 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:16096273;Dbxref=PMID:22814378,PMID:16096273 +P0CX41 UniProtKB Modified residue 106 106 . . . Note=N6%2CN6-dimethyllysine%3B by RKM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17327221;Dbxref=PMID:17327221 +P0CX41 UniProtKB Modified residue 110 110 . . . Note=N6%2CN6-dimethyllysine%3B by RKM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17327221;Dbxref=PMID:17327221 +P0CX41 UniProtKB Beta strand 22 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX41 UniProtKB Beta strand 27 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX41 UniProtKB Beta strand 33 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX41 UniProtKB Beta strand 57 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX41 UniProtKB Beta strand 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX41 UniProtKB Helix 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX41 UniProtKB Beta strand 70 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX41 UniProtKB Beta strand 74 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX41 UniProtKB Beta strand 92 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX41 UniProtKB Beta strand 99 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX41 UniProtKB Turn 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M +P0CX41 UniProtKB Beta strand 109 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX41 UniProtKB Helix 120 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX41 UniProtKB Helix 127 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX41 UniProtKB Beta strand 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P35196 1 286 +P35196 UniProtKB Chain 1 286 . . . ID=PRO_0000123759;Note=Dehydrodolichyl diphosphate synthase complex subunit RER2 +P35196 UniProtKB Mutagenesis 164 164 . . . Note=In RER2-1%3B loss of activity. G->D +P35196 UniProtKB Mutagenesis 209 209 . . . Note=In RER2-2%3B loss of activity. S->N +##sequence-region P30775 1 413 +P30775 UniProtKB Modified residue 287 287 . . . Note=N5-methylglutamine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16321977;Dbxref=PMID:16321977 +##sequence-region P53893 1 1110 +P53893 UniProtKB Chain 1 1110 . . . ID=PRO_0000091559;Note=Ribosome assembly protein 1 +P53893 UniProtKB Domain 17 262 . . . Note=tr-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P53893 UniProtKB Nucleotide binding 26 33 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53893 UniProtKB Nucleotide binding 102 106 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53893 UniProtKB Nucleotide binding 156 159 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53893 UniProtKB Modified residue 431 431 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q06208 1 395 +Q06208 UniProtKB Chain 1 395 . . . ID=PRO_0000097337;Note=Protein RIF2 +Q06208 UniProtKB Sequence conflict 387 387 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06208 UniProtKB Helix 37 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ6 +Q06208 UniProtKB Helix 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ6 +Q06208 UniProtKB Helix 71 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Helix 93 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Beta strand 104 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Beta strand 109 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Helix 119 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Beta strand 137 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Helix 146 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Helix 189 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Turn 200 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ6 +Q06208 UniProtKB Beta strand 204 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Beta strand 217 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ5 +Q06208 UniProtKB Helix 226 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Beta strand 245 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Helix 260 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Beta strand 274 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Helix 284 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Helix 304 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Helix 323 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Helix 337 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Helix 355 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Turn 368 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ1 +Q06208 UniProtKB Helix 373 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJ6 +##sequence-region Q03778 1 218 +Q03778 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03778 UniProtKB Chain 20 218 . . . ID=PRO_0000030437;Note=Riboflavin kinase +Q03778 UniProtKB Active site 155 155 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03778 UniProtKB Metal binding 72 72 . . . Note=Magnesium or zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q03792 1 727 +Q03792 UniProtKB Chain 1 727 . . . ID=PRO_0000207746;Note=Calpain-like protease 1 +Q03792 UniProtKB Domain 70 317 . . . Note=Calpain catalytic +Q03792 UniProtKB Active site 128 128 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03792 UniProtKB Active site 271 271 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03792 UniProtKB Active site 296 296 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03792 UniProtKB Mutagenesis 128 128 . . . Note=Loss of function. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9928935;Dbxref=PMID:9928935 +##sequence-region Q08961 1 583 +Q08961 UniProtKB Chain 1 583 . . . ID=PRO_0000228984;Note=Ribosomal lysine N-methyltransferase 1 +Q08961 UniProtKB Domain 22 274 . . . Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 +Q08961 UniProtKB Coiled coil 378 407 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08961 UniProtKB Coiled coil 433 459 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08961 UniProtKB Binding site 273 273 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 +##sequence-region P22336 1 621 +P22336 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P22336 UniProtKB Chain 2 621 . . . ID=PRO_0000097268;Note=Replication factor A protein 1 +P22336 UniProtKB DNA binding 197 284 . . . Note=OB +P22336 UniProtKB Zinc finger 486 508 . . . Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22336 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P22336 UniProtKB Modified residue 178 178 . . . Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P22336 UniProtKB Helix 10 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X +P22336 UniProtKB Helix 18 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X +P22336 UniProtKB Beta strand 28 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X +P22336 UniProtKB Turn 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X +P22336 UniProtKB Beta strand 44 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X +P22336 UniProtKB Beta strand 53 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X +P22336 UniProtKB Helix 63 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X +P22336 UniProtKB Beta strand 79 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X +P22336 UniProtKB Turn 91 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X +P22336 UniProtKB Beta strand 95 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X +P22336 UniProtKB Helix 120 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M1X +P22336 UniProtKB Helix 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX +P22336 UniProtKB Turn 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX +P22336 UniProtKB Beta strand 198 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX +P22336 UniProtKB Beta strand 218 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX +P22336 UniProtKB Beta strand 231 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX +P22336 UniProtKB Helix 239 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX +P22336 UniProtKB Beta strand 251 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX +P22336 UniProtKB Beta strand 261 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX +P22336 UniProtKB Turn 267 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX +P22336 UniProtKB Beta strand 270 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX +P22336 UniProtKB Beta strand 276 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX +P22336 UniProtKB Beta strand 285 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YNX +##sequence-region P26754 1 273 +P26754 UniProtKB Chain 1 273 . . . ID=PRO_0000097275;Note=Replication factor A protein 2 +P26754 UniProtKB DNA binding 69 157 . . . Note=OB +P26754 UniProtKB Compositional bias 1 30 . . . Note=Gly/Ser-rich +P26754 UniProtKB Modified residue 27 27 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P26754 UniProtKB Modified residue 122 122 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:17287358,PMID:18407956 +##sequence-region P26755 1 122 +P26755 UniProtKB Chain 1 122 . . . ID=PRO_0000097279;Note=Replication factor A protein 3 +##sequence-region P40348 1 353 +P40348 UniProtKB Chain 1 353 . . . ID=PRO_0000121760;Note=Replication factor C subunit 2 +P40348 UniProtKB Nucleotide binding 65 73 . . . Note=ATP +P40348 UniProtKB Binding site 28 28 . . . Note=ATP%3B via carbonyl oxygen +P40348 UniProtKB Binding site 32 32 . . . Note=ATP +P40348 UniProtKB Binding site 171 171 . . . Note=ATP +P40348 UniProtKB Binding site 229 229 . . . Note=ATP +P40348 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40348 UniProtKB Sequence conflict 12 12 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40348 UniProtKB Helix 27 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Turn 36 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 46 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Beta strand 61 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 71 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Beta strand 91 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Beta strand 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 103 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 109 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 125 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Beta strand 135 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 147 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Turn 160 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Beta strand 164 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 173 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 178 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Beta strand 184 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 194 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Turn 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 214 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 228 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 239 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 253 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 266 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 280 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 300 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Beta strand 312 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 316 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40348 UniProtKB Helix 339 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +##sequence-region P40339 1 323 +P40339 UniProtKB Chain 1 323 . . . ID=PRO_0000121771;Note=Replication factor C subunit 4 +P40339 UniProtKB Nucleotide binding 49 57 . . . Note=ATP +P40339 UniProtKB Binding site 12 12 . . . Note=ATP%3B via carbonyl oxygen +P40339 UniProtKB Binding site 24 24 . . . Note=ATP%3B via amide nitrogen +P40339 UniProtKB Binding site 145 145 . . . Note=ATP +P40339 UniProtKB Binding site 203 203 . . . Note=ATP +P40339 UniProtKB Helix 11 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 28 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Beta strand 45 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 55 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 68 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 71 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Beta strand 75 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 86 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 92 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Beta strand 109 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 121 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 128 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Turn 134 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Beta strand 138 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 147 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 152 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Beta strand 158 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 168 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 188 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 202 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Beta strand 217 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 221 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 233 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 245 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Turn 255 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 263 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 282 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P40339 UniProtKB Helix 306 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +##sequence-region P38251 1 354 +P38251 UniProtKB Chain 1 354 . . . ID=PRO_0000121765;Note=Replication factor C subunit 5 +P38251 UniProtKB Nucleotide binding 43 51 . . . Note=ATP +P38251 UniProtKB Binding site 5 5 . . . Note=ATP%3B via carbonyl oxygen +P38251 UniProtKB Binding site 17 17 . . . Note=ATP +P38251 UniProtKB Binding site 231 231 . . . Note=ATP +P38251 UniProtKB Turn 5 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Helix 13 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Helix 20 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Turn 28 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Beta strand 39 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Helix 49 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Helix 56 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Beta strand 91 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Helix 106 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Turn 117 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Beta strand 136 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Helix 148 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Turn 162 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Beta strand 165 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Helix 179 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Beta strand 185 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Helix 195 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Helix 217 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Helix 230 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Helix 239 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Turn 243 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Helix 258 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Helix 276 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Turn 291 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Helix 296 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Turn 306 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Helix 315 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +P38251 UniProtKB Helix 338 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SXJ +##sequence-region P06781 1 192 +P06781 UniProtKB Chain 1 189 . . . ID=PRO_0000198946;Note=GTP-binding protein RHO2 +P06781 UniProtKB Propeptide 190 192 . . . ID=PRO_0000281276;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06781 UniProtKB Nucleotide binding 14 21 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06781 UniProtKB Nucleotide binding 61 65 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06781 UniProtKB Nucleotide binding 119 122 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06781 UniProtKB Motif 36 44 . . . Note=Effector region;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06781 UniProtKB Modified residue 189 189 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06781 UniProtKB Lipidation 188 188 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107 +P06781 UniProtKB Lipidation 189 189 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P06781 UniProtKB Sequence conflict 48 48 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12362 1 591 +Q12362 UniProtKB Chain 1 591 . . . ID=PRO_0000162725;Note=Bifunctional protein RIB2 +Q12362 UniProtKB Domain 99 168 . . . Note=S4 RNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00182 +Q12362 UniProtKB Domain 433 552 . . . Note=CMP/dCMP-type deaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01083 +Q12362 UniProtKB Region 1 432 . . . Note=tRNA pseudouridine synthase +Q12362 UniProtKB Region 433 591 . . . Note=DRAP deaminase +Q12362 UniProtKB Active site 211 211 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12362 UniProtKB Active site 484 484 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12362 UniProtKB Metal binding 482 482 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12362 UniProtKB Metal binding 515 515 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12362 UniProtKB Metal binding 525 525 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q3E757 1 174 +Q3E757 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260 +Q3E757 UniProtKB Chain 2 174 . . . ID=PRO_0000125105;Note=60S ribosomal protein L11-B +Q3E757 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260 +Q3E757 UniProtKB Modified residue 75 75 . . . Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22522802;Dbxref=PMID:22522802 +Q3E757 UniProtKB Sequence conflict 138 138 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q3E757 UniProtKB Beta strand 14 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E757 UniProtKB Beta strand 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +Q3E757 UniProtKB Helix 28 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E757 UniProtKB Beta strand 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E757 UniProtKB Beta strand 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E757 UniProtKB Beta strand 66 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E757 UniProtKB Helix 74 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E757 UniProtKB Turn 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E757 UniProtKB Beta strand 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E757 UniProtKB Beta strand 93 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E757 UniProtKB Beta strand 102 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E757 UniProtKB Helix 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E757 UniProtKB Turn 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E757 UniProtKB Beta strand 125 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E757 UniProtKB Turn 134 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E757 UniProtKB Helix 137 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E757 UniProtKB Beta strand 141 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Q +Q3E757 UniProtKB Helix 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E757 UniProtKB Helix 156 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E757 UniProtKB Turn 165 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E757 UniProtKB Beta strand 170 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P03871 1 373 +P03871 UniProtKB Chain 1 373 . . . ID=PRO_0000150892;Note=Partitioning protein REP1 +P03871 UniProtKB Region 1 129 . . . Note=Interaction with REP2 and self-association +P03871 UniProtKB Region 1 76 . . . Note=Interaction with REP2 +P03871 UniProtKB Region 349 373 . . . Note=Nuclear localization +P03871 UniProtKB Natural variant 8 8 . . . Note=In strain: ATCC 44827 and ATCC 7754. A->V +P03871 UniProtKB Natural variant 22 22 . . . Note=In strain: ATCC 44827 and ATCC 7754. V->I +P03871 UniProtKB Natural variant 38 38 . . . Note=In strain: ATCC 44827 and ATCC 7754. P->S +P03871 UniProtKB Natural variant 87 87 . . . Note=In strain: ATCC 44827 and ATCC 7754. I->R +P03871 UniProtKB Natural variant 107 107 . . . Note=In strain: ATCC 44827 and ATCC 7754. T->A +P03871 UniProtKB Natural variant 111 123 . . . Note=In strain: ATCC 44827. GLDINVKGTLNRR->VRYQCKRHVKPQ +P03871 UniProtKB Natural variant 117 117 . . . Note=In strain: ATCC 7754. K->R +P03871 UniProtKB Natural variant 131 132 . . . Note=In strain: ATCC 44827. KG->N +P03871 UniProtKB Natural variant 149 149 . . . Note=In strain: ATCC 44827 and ATCC 7754. A->D +P03871 UniProtKB Natural variant 177 177 . . . Note=In strain: ATCC 44827 and ATCC 7754. Q->K +P03871 UniProtKB Natural variant 184 184 . . . Note=In strain: ATCC 44827 and ATCC 7754. P->Q +P03871 UniProtKB Natural variant 198 198 . . . Note=In strain: ATCC 44827 and ATCC 7754. I->V +P03871 UniProtKB Natural variant 204 204 . . . Note=In strain: ATCC 44827 and ATCC 7754. K->R +P03871 UniProtKB Natural variant 211 214 . . . Note=In strain: ATCC 44827 and ATCC 7754. DKGH->GL +P03871 UniProtKB Natural variant 220 222 . . . Note=In strain: ATCC 44827. LPP->QPR +P03871 UniProtKB Natural variant 225 228 . . . Note=In strain: ATCC 44827. DPSR->NSSP +P03871 UniProtKB Natural variant 231 231 . . . Note=In strain: ATCC 44827. N->S +P03871 UniProtKB Natural variant 239 241 . . . Note=In strain: ATCC 44827 and ATCC 7754. SLT->NLI +P03871 UniProtKB Natural variant 246 246 . . . Note=In strain: ATCC 44827 and ATCC 7754. E->A +P03871 UniProtKB Natural variant 253 253 . . . Note=In strain: ATCC 44827 and ATCC 7754. G->S +P03871 UniProtKB Natural variant 261 261 . . . Note=In strain: ATCC 7754. K->R +P03871 UniProtKB Natural variant 270 270 . . . Note=In strain: ATCC 44827 and ATCC 7754. T->A +P03871 UniProtKB Natural variant 372 373 . . . Note=In strain: ATCC 44827 and ATCC 7754. DG->NE +P03871 UniProtKB Mutagenesis 32 32 . . . Note=Abolishes interaction with REP2 and STB. T->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893 +P03871 UniProtKB Mutagenesis 43 43 . . . Note=Abolishes interaction with REP2%2C but not with STB. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893 +P03871 UniProtKB Mutagenesis 50 50 . . . Note=Abolishes interaction with REP2%2C but not with STB. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893 +P03871 UniProtKB Mutagenesis 78 78 . . . Note=Abolishes interaction with REP2%2C but not with STB. V->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893 +P03871 UniProtKB Mutagenesis 93 93 . . . Note=Abolishes interaction with REP2%2C but not with STB. S->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893 +P03871 UniProtKB Mutagenesis 154 154 . . . Note=Abolishes interaction with STB%2C but not with REP2. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893 +P03871 UniProtKB Mutagenesis 200 200 . . . Note=Abolishes interaction with REP2%2C but not with STB. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893 +P03871 UniProtKB Mutagenesis 276 276 . . . Note=Abolishes interaction with REP2%2C but not with STB. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893 +P03871 UniProtKB Mutagenesis 297 297 . . . Note=Abolishes interaction with STB%2C but not with REP2. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893 +P03871 UniProtKB Mutagenesis 301 301 . . . Note=Abolishes interaction with REP2%2C but not with STB. Y->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893 +P03871 UniProtKB Mutagenesis 308 308 . . . Note=Abolishes interaction with REP2%2C but not with STB. I->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893 +P03871 UniProtKB Mutagenesis 317 317 . . . Note=Abolishes interaction with STB%2C but not with REP2. Y->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893 +P03871 UniProtKB Mutagenesis 330 330 . . . Note=Abolishes interaction with STB%2C but not with REP2. S->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15169893;Dbxref=PMID:15169893 +##sequence-region P12689 1 985 +P12689 UniProtKB Chain 1 985 . . . ID=PRO_0000173995;Note=DNA repair protein REV1 +P12689 UniProtKB Domain 161 249 . . . Note=BRCT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033 +P12689 UniProtKB Domain 358 554 . . . Note=UmuC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00216 +P12689 UniProtKB Nucleotide binding 362 366 . . . Note=dCTP binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16195463,ECO:0000269|PubMed:18275815;Dbxref=PMID:16195463,PMID:18275815 +P12689 UniProtKB Nucleotide binding 402 408 . . . Note=dCTP binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16195463,ECO:0000269|PubMed:18275815;Dbxref=PMID:16195463,PMID:18275815 +P12689 UniProtKB Region 319 329 . . . Note=Interaction with target DNA +P12689 UniProtKB Region 395 397 . . . Note=Interaction with target DNA +P12689 UniProtKB Region 554 557 . . . Note=Interaction with target DNA +P12689 UniProtKB Region 620 628 . . . Note=Interaction with target DNA +P12689 UniProtKB Metal binding 362 362 . . . Note=Magnesium 1;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00216,ECO:0000269|PubMed:18275815;Dbxref=PMID:18275815 +P12689 UniProtKB Metal binding 362 362 . . . Note=Magnesium 2;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00216,ECO:0000269|PubMed:18275815;Dbxref=PMID:18275815 +P12689 UniProtKB Metal binding 363 363 . . . Note=Magnesium 2%3B via carbonyl oxygen;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00216,ECO:0000269|PubMed:18275815;Dbxref=PMID:18275815 +P12689 UniProtKB Metal binding 467 467 . . . Note=Magnesium 1;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00216,ECO:0000269|PubMed:18275815;Dbxref=PMID:18275815 +P12689 UniProtKB Metal binding 468 468 . . . Note=Magnesium 1;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00216,ECO:0000269|PubMed:18275815;Dbxref=PMID:18275815 +P12689 UniProtKB Binding site 324 324 . . . Note=dCTP;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16195463,ECO:0000269|PubMed:18275815;Dbxref=PMID:16195463,PMID:18275815 +P12689 UniProtKB Binding site 414 414 . . . Note=dCTP;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16195463,ECO:0000269|PubMed:18275815;Dbxref=PMID:16195463,PMID:18275815 +P12689 UniProtKB Binding site 467 467 . . . Note=dCTP;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16195463,ECO:0000269|PubMed:18275815;Dbxref=PMID:16195463,PMID:18275815 +P12689 UniProtKB Site 681 681 . . . Note=Interaction with target DNA +P12689 UniProtKB Site 692 692 . . . Note=Interaction with target DNA +P12689 UniProtKB Site 694 694 . . . Note=Interaction with target DNA +P12689 UniProtKB Mutagenesis 193 193 . . . Note=Loss of activity. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2492497;Dbxref=PMID:2492497 +P12689 UniProtKB Mutagenesis 467 468 . . . Note=Loss of dCTP transferase activity. DE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11316789;Dbxref=PMID:11316789 +P12689 UniProtKB Sequence conflict 646 646 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12689 UniProtKB Sequence conflict 816 816 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12689 UniProtKB Turn 165 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3 +P12689 UniProtKB Beta strand 170 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3 +P12689 UniProtKB Helix 181 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3 +P12689 UniProtKB Beta strand 194 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3 +P12689 UniProtKB Turn 202 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3 +P12689 UniProtKB Beta strand 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3 +P12689 UniProtKB Helix 215 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3 +P12689 UniProtKB Turn 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3 +P12689 UniProtKB Beta strand 224 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2M2I +P12689 UniProtKB Helix 230 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3 +P12689 UniProtKB Helix 244 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ID3 +P12689 UniProtKB Helix 315 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 324 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Turn 343 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Beta strand 355 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Turn 364 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 368 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 377 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Turn 384 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Beta strand 389 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Beta strand 395 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Beta strand 401 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 405 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 418 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Beta strand 432 434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 438 454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Beta strand 459 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Beta strand 468 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 485 501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Beta strand 506 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 514 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 534 536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 539 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 547 549 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 555 564 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 571 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 580 587 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 591 598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Turn 599 601 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 605 612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 614 618 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Beta strand 623 627 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 636 656 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Beta strand 659 671 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Beta strand 687 701 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 704 718 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Helix 722 724 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +P12689 UniProtKB Beta strand 725 737 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AQ4 +##sequence-region P38206 1 574 +P38206 UniProtKB Chain 1 574 . . . ID=PRO_0000212420;Note=Oligosaccharide translocation protein RFT1 +P38206 UniProtKB Topological domain 1 24 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Transmembrane 25 45 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Topological domain 46 48 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Transmembrane 49 69 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Topological domain 70 110 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Transmembrane 111 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Topological domain 132 148 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Transmembrane 149 169 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Topological domain 170 181 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Transmembrane 182 202 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Topological domain 203 218 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Transmembrane 219 239 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Topological domain 240 319 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Transmembrane 320 340 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Topological domain 341 372 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Transmembrane 373 393 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Topological domain 394 413 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Transmembrane 414 434 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Topological domain 435 443 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Transmembrane 444 464 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Topological domain 465 469 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Transmembrane 470 490 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Topological domain 491 509 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Transmembrane 510 530 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Topological domain 531 532 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Transmembrane 533 553 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Topological domain 554 574 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38206 UniProtKB Sequence conflict 74 75 . . . Note=IR->MF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38206 UniProtKB Sequence conflict 207 216 . . . Note=PMGVVTSDID->QWGLSHRTLT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q00453 1 211 +Q00453 UniProtKB Chain 1 211 . . . ID=PRO_0000046817;Note=Probable transcription repressor protein RGM1 +Q00453 UniProtKB Zinc finger 19 44 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q00453 UniProtKB Zinc finger 50 73 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q00453 UniProtKB Motif 6 11 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q00453 UniProtKB Compositional bias 95 211 . . . Note=Pro-rich +Q00453 UniProtKB Sequence conflict 114 114 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P50861 1 169 +P50861 UniProtKB Chain 1 169 . . . ID=PRO_0000134857;Note=6%2C7-dimethyl-8-ribityllumazine synthase +P50861 UniProtKB Region 61 63 . . . Note=5-amino-6-(D-ribitylamino)uracil binding +P50861 UniProtKB Region 90 92 . . . Note=5-amino-6-(D-ribitylamino)uracil binding +P50861 UniProtKB Region 95 96 . . . Note=1-deoxy-L-glycero-tetrulose 4-phosphate binding +P50861 UniProtKB Active site 98 98 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50861 UniProtKB Binding site 27 27 . . . Note=5-amino-6-(D-ribitylamino)uracil +P50861 UniProtKB Binding site 123 123 . . . Note=5-amino-6-(D-ribitylamino)uracil%3B via amide nitrogen and carbonyl oxygen +P50861 UniProtKB Binding site 137 137 . . . Note=1-deoxy-L-glycero-tetrulose 4-phosphate +P50861 UniProtKB Sequence conflict 44 44 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P50861 UniProtKB Sequence conflict 51 51 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P50861 UniProtKB Beta strand 20 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB +P50861 UniProtKB Helix 29 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB +P50861 UniProtKB Helix 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB +P50861 UniProtKB Beta strand 53 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB +P50861 UniProtKB Helix 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB +P50861 UniProtKB Helix 64 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB +P50861 UniProtKB Beta strand 83 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB +P50861 UniProtKB Beta strand 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB +P50861 UniProtKB Helix 98 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB +P50861 UniProtKB Beta strand 124 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB +P50861 UniProtKB Helix 131 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB +P50861 UniProtKB Helix 149 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EJB +##sequence-region P38234 1 210 +P38234 UniProtKB Chain 1 210 . . . ID=PRO_0000200767;Note=Protein RFS1 +P38234 UniProtKB Domain 4 203 . . . Note=Flavodoxin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00088 +##sequence-region P48743 1 811 +P48743 UniProtKB Chain 1 811 . . . ID=PRO_0000215295;Note=RFX-like DNA-binding protein RFX1 +P48743 UniProtKB DNA binding 285 360 . . . Note=RFX-type winged-helix;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00858 +P48743 UniProtKB Modified residue 173 173 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q06407 1 1009 +Q06407 UniProtKB Chain 1 1009 . . . ID=PRO_0000075900;Note=Rho-type GTPase-activating protein 2 +Q06407 UniProtKB Domain 11 68 . . . Note=LIM zinc-binding 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125 +Q06407 UniProtKB Domain 69 129 . . . Note=LIM zinc-binding 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00125 +Q06407 UniProtKB Domain 788 1006 . . . Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172 +Q06407 UniProtKB Modified residue 763 763 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P38339 1 666 +P38339 UniProtKB Chain 1 666 . . . ID=PRO_0000056736;Note=RHO GTPase-activating protein RGD1 +P38339 UniProtKB Domain 33 295 . . . Note=F-BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01077 +P38339 UniProtKB Domain 472 663 . . . Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172 +P38339 UniProtKB Coiled coil 139 226 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38339 UniProtKB Modified residue 386 386 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38339 UniProtKB Helix 33 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPC +P38339 UniProtKB Helix 43 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPC +P38339 UniProtKB Beta strand 86 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPC +P38339 UniProtKB Helix 97 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPC +P38339 UniProtKB Helix 195 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPC +P38339 UniProtKB Helix 233 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPC +P38339 UniProtKB Helix 279 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPC +P38339 UniProtKB Helix 283 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPC +P38339 UniProtKB Helix 292 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WPC +P38339 UniProtKB Beta strand 470 472 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K +P38339 UniProtKB Helix 474 477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K +P38339 UniProtKB Helix 487 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K +P38339 UniProtKB Turn 500 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K +P38339 UniProtKB Turn 504 508 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K +P38339 UniProtKB Helix 513 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K +P38339 UniProtKB Helix 527 533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K +P38339 UniProtKB Helix 541 556 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K +P38339 UniProtKB Beta strand 558 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K +P38339 UniProtKB Helix 565 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K +P38339 UniProtKB Helix 568 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K +P38339 UniProtKB Helix 580 592 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K +P38339 UniProtKB Helix 596 614 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K +P38339 UniProtKB Helix 616 619 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K +P38339 UniProtKB Helix 623 634 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K +P38339 UniProtKB Helix 646 662 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3K +##sequence-region P40160 1 425 +P40160 UniProtKB Chain 1 425 . . . ID=PRO_0000213532;Note=Serine/threonine-protein kinase RIO2 +P40160 UniProtKB Domain 95 257 . . . Note=Protein kinase +P40160 UniProtKB Active site 229 229 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40160 UniProtKB Binding site 123 123 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40160 UniProtKB Modified residue 346 346 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40160 UniProtKB Mutagenesis 73 73 . . . Note=In RIO2-1%3B nuclear export of ribosomal 40S subunits impaired%3B when associated with V-186%2C H-210%2C D-364%2C G-371 and G-417. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12628929;Dbxref=PMID:12628929 +P40160 UniProtKB Mutagenesis 105 105 . . . Note=No change in activity. K->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12690111;Dbxref=PMID:12690111 +P40160 UniProtKB Mutagenesis 186 186 . . . Note=In RIO2-1%3B nuclear export of ribosomal 40S subunits impaired%3B when associated with H-73%2C H-210%2C D-364%2C G-371 and G-417. I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12628929;Dbxref=PMID:12628929 +P40160 UniProtKB Mutagenesis 210 210 . . . Note=In RIO2-1%3B nuclear export of ribosomal 40S subunits impaired%3B when associated with H-73%2C V-186%2C D-364%2C G-371 and G-417. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12628929;Dbxref=PMID:12628929 +P40160 UniProtKB Mutagenesis 227 227 . . . Note=No change in activity. H->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12690111;Dbxref=PMID:12690111 +P40160 UniProtKB Mutagenesis 229 229 . . . Note=Decrease in activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12690111;Dbxref=PMID:12690111 +P40160 UniProtKB Mutagenesis 364 364 . . . Note=In RIO2-1%3B nuclear export of ribosomal 40S subunits impaired%3B when associated with H-73%2C V-186%2C H-210%2C G-371 and G-417. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12628929;Dbxref=PMID:12628929 +P40160 UniProtKB Mutagenesis 371 371 . . . Note=In RIO2-1%3B nuclear export of ribosomal 40S subunits impaired%3B when associated with H-73%2C V-186%2C H-210%2C D-364 and G-417. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12628929;Dbxref=PMID:12628929 +P40160 UniProtKB Mutagenesis 417 417 . . . Note=In RIO2-1%3B nuclear export of ribosomal 40S subunits impaired%3B when associated with H-73%2C V-186%2C H-210%2C D-364 and G-371. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12628929;Dbxref=PMID:12628929 +##sequence-region P49723 1 345 +P49723 UniProtKB Chain 1 345 . . . ID=PRO_0000190465;Note=Ribonucleoside-diphosphate reductase small chain 2 +P49723 UniProtKB Active site 131 131 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10014 +P49723 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.5;Dbxref=PMID:22814378 +P49723 UniProtKB Modified residue 169 169 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P49723 UniProtKB Modified residue 332 332 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P49723 UniProtKB Modified residue 334 334 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P49723 UniProtKB Modified residue 336 336 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P49723 UniProtKB Cross-link 337 337 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P49723 UniProtKB Sequence conflict 127 127 . . . Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P49723 UniProtKB Helix 4 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SMS +P49723 UniProtKB Helix 13 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Turn 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Turn 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Helix 43 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Helix 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Turn 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Turn 69 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Helix 78 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Helix 101 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Helix 111 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Helix 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SMS +P49723 UniProtKB Helix 148 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Helix 155 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Beta strand 169 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Helix 175 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Turn 188 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Helix 191 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Beta strand 202 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Helix 207 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Helix 240 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Turn 265 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SMS +P49723 UniProtKB Helix 277 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P49723 UniProtKB Helix 316 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SMS +##sequence-region P38145 1 238 +P38145 UniProtKB Chain 1 238 . . . ID=PRO_0000068174;Note=Riboflavin synthase +P38145 UniProtKB Repeat 1 103 . . . Note=Lumazine-binding 1 +P38145 UniProtKB Repeat 104 205 . . . Note=Lumazine-binding 2 +P38145 UniProtKB Region 4 6 . . . Note=Lumazine 1 binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q2YN92 +P38145 UniProtKB Region 54 56 . . . Note=Lumazine 2 binding%3B shared with one trimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q2YN92 +P38145 UniProtKB Region 68 73 . . . Note=Lumazine 2 binding%3B shared with one trimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AFU8 +P38145 UniProtKB Region 107 109 . . . Note=Lumazine 2 binding%3B shared with one trimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q2YN92 +P38145 UniProtKB Region 152 154 . . . Note=Lumazine 1 binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q2YN92 +P38145 UniProtKB Region 170 175 . . . Note=Lumazine 1 binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q2YN92 +P38145 UniProtKB Binding site 143 143 . . . Note=Lumazine 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q2YN92 +P38145 UniProtKB Modified residue 95 95 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P40188 1 164 +P40188 UniProtKB Chain 1 164 . . . ID=PRO_0000202987;Note=Respiratory growth induced protein 2 +##sequence-region Q00245 1 231 +Q00245 UniProtKB Chain 1 228 . . . ID=PRO_0000198947;Note=GTP-binding protein RHO3 +Q00245 UniProtKB Propeptide 229 231 . . . ID=PRO_0000281277;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00245 UniProtKB Nucleotide binding 23 30 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00245 UniProtKB Nucleotide binding 70 74 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00245 UniProtKB Nucleotide binding 128 131 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00245 UniProtKB Motif 45 53 . . . Note=Effector region;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00245 UniProtKB Modified residue 228 228 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00245 UniProtKB Lipidation 228 228 . . . Note=S-farnesyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00245 UniProtKB Sequence conflict 129 129 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53879 1 331 +P53879 UniProtKB Chain 1 328 . . . ID=PRO_0000198949;Note=GTP-binding protein RHO5 +P53879 UniProtKB Propeptide 329 331 . . . ID=PRO_0000281279;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53879 UniProtKB Nucleotide binding 10 17 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53879 UniProtKB Nucleotide binding 87 91 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53879 UniProtKB Nucleotide binding 156 159 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53879 UniProtKB Modified residue 223 223 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53879 UniProtKB Modified residue 228 228 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53879 UniProtKB Modified residue 232 232 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53879 UniProtKB Modified residue 244 244 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53879 UniProtKB Modified residue 328 328 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53879 UniProtKB Lipidation 328 328 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53879 UniProtKB Cross-link 276 276 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P53879 UniProtKB Mutagenesis 91 91 . . . Note=Cells sensitive to calcofluor%2C caffeine and Congo red. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12118069;Dbxref=PMID:12118069 +##sequence-region P09938 1 399 +P09938 UniProtKB Chain 1 399 . . . ID=PRO_0000190464;Note=Ribonucleoside-diphosphate reductase small chain 1 +P09938 UniProtKB Active site 183 183 . . . . +P09938 UniProtKB Metal binding 145 145 . . . Note=Iron 1 +P09938 UniProtKB Metal binding 176 176 . . . Note=Iron 1 +P09938 UniProtKB Metal binding 176 176 . . . Note=Iron 2 +P09938 UniProtKB Metal binding 179 179 . . . Note=Iron 1 +P09938 UniProtKB Metal binding 239 239 . . . Note=Iron 2 +P09938 UniProtKB Metal binding 273 273 . . . Note=Iron 2 +P09938 UniProtKB Metal binding 276 276 . . . Note=Iron 2 +P09938 UniProtKB Modified residue 15 15 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +P09938 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P09938 UniProtKB Modified residue 41 41 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P09938 UniProtKB Sequence conflict 101 103 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09938 UniProtKB Sequence conflict 111 111 . . . Note=E->ETAE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09938 UniProtKB Helix 27 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 38 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 51 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 63 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 73 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 94 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 118 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 128 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 147 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 153 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 163 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 194 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 208 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Beta strand 223 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 228 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Turn 241 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 244 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 260 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 293 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 317 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 324 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Turn 341 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +P09938 UniProtKB Helix 355 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1JK0 +##sequence-region P21672 1 869 +P21672 UniProtKB Chain 1 869 . . . ID=PRO_0000187204;Note=Ribonucleoside-diphosphate reductase large chain 2 +P21672 UniProtKB Domain 1 92 . . . Note=ATP-cone;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00492 +P21672 UniProtKB Region 11 17 . . . Note=Allosteric activator binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Region 217 218 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Region 285 288 . . . Note=Allosteric effector binding%2C determines substrate specificity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Region 426 430 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Region 607 611 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Active site 426 426 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Active site 428 428 . . . Note=Cysteine radical intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Active site 430 430 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Binding site 5 5 . . . Note=Allosteric activator;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Binding site 53 53 . . . Note=Allosteric activator;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Binding site 88 88 . . . Note=Allosteric activator;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Binding site 202 202 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Binding site 247 247 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Site 218 218 . . . Note=Important for hydrogen atom transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Site 226 226 . . . Note=Allosteric effector binding%2C determines substrate specificity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Site 256 256 . . . Note=Allosteric effector binding%2C determines substrate specificity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Site 443 443 . . . Note=Important for hydrogen atom transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Site 741 741 . . . Note=Important for electron transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Site 742 742 . . . Note=Important for electron transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Site 864 864 . . . Note=Interacts with thioredoxin/glutaredoxin;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Site 867 867 . . . Note=Interacts with thioredoxin/glutaredoxin;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Modified residue 227 227 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21524 +P21672 UniProtKB Modified residue 806 806 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P21672 UniProtKB Modified residue 827 827 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21524 +P21672 UniProtKB Modified residue 868 868 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21524 +P21672 UniProtKB Disulfide bond 218 443 . . . Note=Redox-active;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21672 UniProtKB Cross-link 387 387 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21524 +P21672 UniProtKB Sequence conflict 21 22 . . . Note=RI->VL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21672 UniProtKB Sequence conflict 37 37 . . . Note=V->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21672 UniProtKB Sequence conflict 58 58 . . . Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21672 UniProtKB Sequence conflict 69 69 . . . Note=T->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21672 UniProtKB Sequence conflict 83 83 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21672 UniProtKB Sequence conflict 212 212 . . . Note=H->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21672 UniProtKB Sequence conflict 249 249 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P21672 UniProtKB Sequence conflict 311 311 . . . Note=F->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P26784 1 199 +P26784 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921 +P26784 UniProtKB Chain 2 199 . . . ID=PRO_0000133791;Note=60S ribosomal protein L16-A +P26784 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921 +P26784 UniProtKB Modified residue 44 44 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26785 +P26784 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26785 +P26784 UniProtKB Cross-link 177 177 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P26784 UniProtKB Sequence conflict 14 14 . . . Note=H->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P26784 UniProtKB Sequence conflict 21 21 . . . Note=S->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P26784 UniProtKB Beta strand 5 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26784 UniProtKB Helix 16 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26784 UniProtKB Beta strand 32 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26784 UniProtKB Helix 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26784 UniProtKB Beta strand 42 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26784 UniProtKB Helix 47 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26784 UniProtKB Helix 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26784 UniProtKB Helix 76 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26784 UniProtKB Turn 86 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P26784 UniProtKB Helix 93 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26784 UniProtKB Beta strand 102 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26784 UniProtKB Helix 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26784 UniProtKB Beta strand 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U51 +P26784 UniProtKB Helix 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26784 UniProtKB Helix 125 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26784 UniProtKB Beta strand 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26784 UniProtKB Helix 138 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26784 UniProtKB Helix 150 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26784 UniProtKB Turn 185 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P26784 UniProtKB Helix 189 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P38066 1 345 +P38066 UniProtKB Chain 1 345 . . . ID=PRO_0000151786;Note=GTP cyclohydrolase-2 +P38066 UniProtKB Nucleotide binding 143 147 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38066 UniProtKB Nucleotide binding 197 199 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38066 UniProtKB Active site 231 231 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38066 UniProtKB Active site 233 233 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38066 UniProtKB Metal binding 148 148 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38066 UniProtKB Metal binding 159 159 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38066 UniProtKB Metal binding 161 161 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38066 UniProtKB Binding site 164 164 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38066 UniProtKB Binding site 219 219 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38066 UniProtKB Binding site 254 254 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38066 UniProtKB Binding site 259 259 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q99258 1 208 +Q99258 UniProtKB Chain 1 208 . . . ID=PRO_0000151829;Note=3%2C4-dihydroxy-2-butanone 4-phosphate synthase +Q99258 UniProtKB Region 26 27 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99258 UniProtKB Region 145 149 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99258 UniProtKB Metal binding 27 27 . . . Note=Magnesium or manganese 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99258 UniProtKB Metal binding 27 27 . . . Note=Magnesium or manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99258 UniProtKB Metal binding 148 148 . . . Note=Magnesium or manganese 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99258 UniProtKB Binding site 31 31 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99258 UniProtKB Binding site 169 169 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99258 UniProtKB Site 131 131 . . . Note=Essential for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99258 UniProtKB Site 169 169 . . . Note=Essential for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99258 UniProtKB Modified residue 3 3 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P29539 1 1916 +P29539 UniProtKB Chain 1 1916 . . . ID=PRO_0000097336;Note=Telomere length regulator protein RIF1 +P29539 UniProtKB Modified residue 97 97 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P29539 UniProtKB Modified residue 1637 1637 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P29539 UniProtKB Modified residue 1795 1795 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P29539 UniProtKB Modified residue 1852 1852 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P29539 UniProtKB Sequence conflict 580 580 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29539 UniProtKB Sequence conflict 732 732 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29539 UniProtKB Sequence conflict 732 732 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P29539 UniProtKB Helix 1859 1861 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJS +P29539 UniProtKB Helix 1866 1876 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJS +P29539 UniProtKB Helix 1880 1885 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJS +P29539 UniProtKB Helix 1888 1907 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BJS +##sequence-region P38127 1 377 +P38127 UniProtKB Chain 1 377 . . . ID=PRO_0000090690;Note=Mitochondrial carrier protein RIM2 +P38127 UniProtKB Transmembrane 53 73 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38127 UniProtKB Transmembrane 131 151 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38127 UniProtKB Transmembrane 179 199 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38127 UniProtKB Transmembrane 238 258 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38127 UniProtKB Transmembrane 286 306 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38127 UniProtKB Transmembrane 347 368 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38127 UniProtKB Repeat 50 163 . . . Note=Solcar 1 +P38127 UniProtKB Repeat 173 262 . . . Note=Solcar 2 +P38127 UniProtKB Repeat 286 375 . . . Note=Solcar 3 +##sequence-region P23796 1 513 +P23796 UniProtKB Chain 1 513 . . . ID=PRO_0000097353;Note=tRNA A64-2'-O-ribosylphosphate transferase +##sequence-region P38883 1 763 +P38883 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38883 UniProtKB Chain 2 763 . . . ID=PRO_0000202938;Note=Pre-rRNA-processing protein RIX1 +P38883 UniProtKB Compositional bias 690 763 . . . Note=Glu-rich +P38883 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38883 UniProtKB Sequence conflict 762 762 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CX53 1 165 +P0CX53 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17005568;Dbxref=PMID:17005568 +P0CX53 UniProtKB Chain 2 165 . . . ID=PRO_0000104467;Note=60S ribosomal protein L12-A +P0CX53 UniProtKB Modified residue 2 2 . . . Note=N%2CN-dimethylproline%3B by NTM1;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18957409,ECO:0000269|PubMed:20481588;Dbxref=PMID:18957409,PMID:20481588 +P0CX53 UniProtKB Modified residue 4 4 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B by RKM2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17005568,ECO:0000269|PubMed:18957409;Dbxref=PMID:17005568,PMID:18957409 +P0CX53 UniProtKB Modified residue 11 11 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B by RKM2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17005568;Dbxref=PMID:17005568 +P0CX53 UniProtKB Modified residue 25 25 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX53 UniProtKB Modified residue 38 38 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P0CX53 UniProtKB Modified residue 67 67 . . . Note=N5-methylarginine%3B by RMT2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11856739,ECO:0000269|PubMed:18957409;Dbxref=PMID:11856739,PMID:18957409 +P0CX53 UniProtKB Cross-link 130 130 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX53 UniProtKB Cross-link 146 146 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX53 UniProtKB Mutagenesis 67 67 . . . Note=Abolishes monomethylation by RMT2. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11856739;Dbxref=PMID:11856739 +##sequence-region Q12690 1 199 +Q12690 UniProtKB Chain 1 199 . . . ID=PRO_0000192938;Note=60S ribosomal protein L13-A +Q12690 UniProtKB Modified residue 144 144 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P40212 +Q12690 UniProtKB Modified residue 152 152 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P40212 +Q12690 UniProtKB Helix 18 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q12690 UniProtKB Beta strand 21 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q12690 UniProtKB Helix 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Y +Q12690 UniProtKB Helix 28 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q12690 UniProtKB Turn 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q12690 UniProtKB Beta strand 57 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q12690 UniProtKB Helix 62 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q12690 UniProtKB Beta strand 68 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q12690 UniProtKB Helix 77 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q12690 UniProtKB Helix 87 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q12690 UniProtKB Helix 106 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q12690 UniProtKB Beta strand 123 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q12690 UniProtKB Beta strand 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q12690 UniProtKB Turn 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q12690 UniProtKB Beta strand 155 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q12690 UniProtKB Helix 166 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q12690 UniProtKB Helix 180 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P05748 1 204 +P05748 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1544921,ECO:0000269|PubMed:6814480;Dbxref=PMID:1544921,PMID:6814480 +P05748 UniProtKB Chain 2 204 . . . ID=PRO_0000127566;Note=60S ribosomal protein L15-A +P05748 UniProtKB Sequence conflict 28 28 . . . Note=W->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05748 UniProtKB Helix 3 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Helix 17 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Beta strand 35 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Helix 45 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Beta strand 59 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Helix 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Helix 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Beta strand 89 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Helix 98 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Turn 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Beta strand 113 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Beta strand 125 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Beta strand 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56 +P05748 UniProtKB Helix 140 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Turn 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Helix 149 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Helix 154 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Turn 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Helix 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Helix 166 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Helix 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Beta strand 183 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Helix 187 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05748 UniProtKB Beta strand 197 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P38927 1 245 +P38927 UniProtKB Chain 1 245 . . . ID=PRO_0000126116;Note=DNA polymerase zeta processivity subunit +P38927 UniProtKB Domain 3 203 . . . Note=HORMA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00109 +##sequence-region Q00246 1 291 +Q00246 UniProtKB Chain 1 288 . . . ID=PRO_0000198948;Note=GTP-binding protein RHO4 +Q00246 UniProtKB Propeptide 289 291 . . . ID=PRO_0000281278;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00246 UniProtKB Nucleotide binding 79 86 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00246 UniProtKB Nucleotide binding 127 131 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00246 UniProtKB Nucleotide binding 185 188 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00246 UniProtKB Motif 101 109 . . . Note=Effector region;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00246 UniProtKB Modified residue 264 264 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00246 UniProtKB Modified residue 268 268 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00246 UniProtKB Modified residue 276 276 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q00246 UniProtKB Modified residue 288 288 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00246 UniProtKB Lipidation 288 288 . . . Note=S-farnesyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00246 UniProtKB Sequence conflict 43 48 . . . Note=PRLPTP->QIAYS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00246 UniProtKB Sequence conflict 143 143 . . . Note=T->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00246 UniProtKB Sequence conflict 201 211 . . . Note=PSSAESLAKRL->QVQQNPWPSVW;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00246 UniProtKB Sequence conflict 213 218 . . . Note=AFAHIQ->HLHIFK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P33312 1 244 +P33312 UniProtKB Chain 1 244 . . . ID=PRO_0000135942;Note=2%2C5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase +P33312 UniProtKB Nucleotide binding 182 186 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33312 UniProtKB Binding site 79 79 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33312 UniProtKB Binding site 83 83 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33312 UniProtKB Binding site 159 159 . . . Note=NADP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33312 UniProtKB Helix 10 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Helix 19 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Beta strand 31 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Beta strand 42 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Helix 58 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Beta strand 71 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Helix 79 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Beta strand 101 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Helix 117 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Beta strand 131 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Beta strand 146 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Turn 154 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Beta strand 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Helix 161 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Beta strand 176 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Helix 183 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Turn 193 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Beta strand 197 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Beta strand 223 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +P33312 UniProtKB Beta strand 232 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4HA7 +##sequence-region P38615 1 370 +P38615 UniProtKB Chain 1 370 . . . ID=PRO_0000086319;Note=Serine/threonine-protein kinase RIM11/MSD1 +P38615 UniProtKB Domain 39 322 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38615 UniProtKB Nucleotide binding 45 53 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38615 UniProtKB Active site 164 164 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P38615 UniProtKB Binding site 68 68 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38615 UniProtKB Modified residue 199 199 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:10679022;Dbxref=PMID:17330950,PMID:19779198,PMID:10679022 +P38615 UniProtKB Sequence conflict 57 57 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38615 UniProtKB Sequence conflict 331 331 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38615 UniProtKB Sequence conflict 343 343 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32445 1 135 +P32445 UniProtKB Transit peptide 1 17 . . . Note=Mitochondrion +P32445 UniProtKB Chain 18 135 . . . ID=PRO_0000033262;Note=Single-stranded DNA-binding protein RIM1%2C mitochondrial +P32445 UniProtKB Domain 19 117 . . . Note=SSB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00252 +##sequence-region Q12196 1 484 +Q12196 UniProtKB Chain 1 484 . . . ID=PRO_0000213531;Note=Serine/threonine-protein kinase RIO1 +Q12196 UniProtKB Domain 76 402 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12196 UniProtKB Region 403 484 . . . Note=Interaction with CKA2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17725716;Dbxref=PMID:17725716 +Q12196 UniProtKB Region 440 484 . . . Note=Asociation with (pre-)40S ribosomal subunit;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24948609;Dbxref=PMID:24948609 +Q12196 UniProtKB Compositional bias 436 484 . . . Note=Lys-rich +Q12196 UniProtKB Active site 244 244 . . . Note=Proton acceptor +Q12196 UniProtKB Active site 261 261 . . . Note=4-aspartylphosphate intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9BRS2 +Q12196 UniProtKB Metal binding 249 249 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9BRS2 +Q12196 UniProtKB Metal binding 261 261 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9BRS2 +Q12196 UniProtKB Binding site 125 125 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9BRS2 +Q12196 UniProtKB Binding site 198 198 . . . Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9BRS2 +Q12196 UniProtKB Modified residue 402 402 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17725716;Dbxref=PMID:17725716 +Q12196 UniProtKB Modified residue 403 403 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17725716;Dbxref=PMID:17725716 +Q12196 UniProtKB Modified residue 409 409 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17725716;Dbxref=PMID:17725716 +Q12196 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17725716;Dbxref=PMID:17725716 +Q12196 UniProtKB Modified residue 417 417 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17725716;Dbxref=PMID:17725716 +Q12196 UniProtKB Modified residue 419 419 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17725716;Dbxref=PMID:17725716 +Q12196 UniProtKB Mutagenesis 125 125 . . . Note=No activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12135737;Dbxref=PMID:12135737 +Q12196 UniProtKB Mutagenesis 244 244 . . . Note=Inhibits cell growth%3B enhances association with pre-40S ribosomal subunits%3B inhibits 20S pre-rRNA to mature 18S rRNA processing%3B translation initiation-like defect. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24948609;Dbxref=PMID:24948609 +Q12196 UniProtKB Mutagenesis 244 244 . . . Note=No activity. D->E%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12135737;Dbxref=PMID:12135737 +Q12196 UniProtKB Mutagenesis 261 261 . . . Note=Inhibits cell growth. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24948609;Dbxref=PMID:24948609 +Q12196 UniProtKB Sequence conflict 203 203 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12504 1 494 +Q12504 UniProtKB Chain 1 494 . . . ID=PRO_0000097367;Note=Ribosomal lysine N-methyltransferase 4 +Q12504 UniProtKB Domain 25 265 . . . Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 +Q12504 UniProtKB Compositional bias 201 206 . . . Note=Poly-Glu +Q12504 UniProtKB Binding site 264 264 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 +Q12504 UniProtKB Sequence conflict 10 13 . . . Note=NFVC->KLCF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12504 UniProtKB Sequence conflict 168 174 . . . Note=RVATSFE->TCVANCPSK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12367 1 367 +Q12367 UniProtKB Chain 1 367 . . . ID=PRO_0000262873;Note=Ribosomal lysine N-methyltransferase 5 +Q12367 UniProtKB Region 170 172 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867 +Q12367 UniProtKB Binding site 110 110 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867 +Q12367 UniProtKB Binding site 192 192 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867 +Q12367 UniProtKB Binding site 256 256 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867 +Q12367 UniProtKB Binding site 288 288 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H867 +##sequence-region P41805 1 221 +P41805 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P41805 UniProtKB Chain 2 221 . . . ID=PRO_0000147129;Note=60S ribosomal protein L10 +P41805 UniProtKB Repeat 167 181 . . . Note=1 +P41805 UniProtKB Repeat 200 216 . . . Note=2 +P41805 UniProtKB Region 167 216 . . . Note=2 X 15-17 AA approximate repeats +P41805 UniProtKB Modified residue 143 143 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P41805 UniProtKB Modified residue 205 205 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P41805 UniProtKB Cross-link 40 40 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P41805 UniProtKB Cross-link 101 101 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P41805 UniProtKB Mutagenesis 194 194 . . . Note=In QSR1-1%3B synthetic lethal. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7730379;Dbxref=PMID:7730379 +P41805 UniProtKB Helix 6 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +##sequence-region P38741 1 713 +P38741 UniProtKB Chain 1 713 . . . ID=PRO_0000082031;Note=Meiotic activator RIM4 +P38741 UniProtKB Domain 93 172 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P38741 UniProtKB Domain 346 420 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P38741 UniProtKB Compositional bias 288 299 . . . Note=Poly-Asn +P38741 UniProtKB Compositional bias 581 594 . . . Note=Poly-Asn +P38741 UniProtKB Modified residue 525 525 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38741 UniProtKB Mutagenesis 96 96 . . . Note=Leads to absolute sporulation defect. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10806425;Dbxref=PMID:10806425 +P38741 UniProtKB Mutagenesis 139 139 . . . Note=Leads to absolute sporulation defect. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10806425;Dbxref=PMID:10806425 +P38741 UniProtKB Mutagenesis 349 349 . . . Note=Leads to mild sporulation defect. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10806425;Dbxref=PMID:10806425 +P38741 UniProtKB Mutagenesis 385 385 . . . Note=Leads to absolute sporulation defect. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10806425;Dbxref=PMID:10806425 +P38741 UniProtKB Sequence conflict 385 385 . . . Note=F->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0C0W9 1 174 +P0C0W9 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921 +P0C0W9 UniProtKB Chain 2 174 . . . ID=PRO_0000125104;Note=60S ribosomal protein L11-A +P0C0W9 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921 +P0C0W9 UniProtKB Modified residue 75 75 . . . Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22522802;Dbxref=PMID:22522802 +P0C0W9 UniProtKB Sequence conflict 12 12 . . . Note=L->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0C0W9 UniProtKB Sequence conflict 25 25 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CX54 1 165 +P0CX54 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17005568;Dbxref=PMID:17005568 +P0CX54 UniProtKB Chain 2 165 . . . ID=PRO_0000409773;Note=60S ribosomal protein L12-B +P0CX54 UniProtKB Modified residue 2 2 . . . Note=N%2CN-dimethylproline%3B by NTM1;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18957409,ECO:0000269|PubMed:20481588;Dbxref=PMID:18957409,PMID:20481588 +P0CX54 UniProtKB Modified residue 4 4 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B by RKM2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17005568,ECO:0000269|PubMed:18957409;Dbxref=PMID:17005568,PMID:18957409 +P0CX54 UniProtKB Modified residue 11 11 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B by RKM2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17005568;Dbxref=PMID:17005568 +P0CX54 UniProtKB Modified residue 25 25 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX54 UniProtKB Modified residue 38 38 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P0CX54 UniProtKB Modified residue 67 67 . . . Note=N5-methylarginine%3B by RMT2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11856739,ECO:0000269|PubMed:18957409;Dbxref=PMID:11856739,PMID:18957409 +P0CX54 UniProtKB Cross-link 130 130 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX54 UniProtKB Cross-link 146 146 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX54 UniProtKB Mutagenesis 67 67 . . . Note=Abolishes monomethylation by RMT2. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11856739;Dbxref=PMID:11856739 +##sequence-region P54780 1 204 +P54780 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1544921,ECO:0000269|PubMed:6814480;Dbxref=PMID:1544921,PMID:6814480 +P54780 UniProtKB Chain 2 204 . . . ID=PRO_0000127567;Note=60S ribosomal protein L15-B +P54780 UniProtKB Sequence conflict 28 28 . . . Note=W->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CX44 1 217 +P0CX44 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260 +P0CX44 UniProtKB Chain 2 217 . . . ID=PRO_0000409768;Note=60S ribosomal protein L1-B +P0CX44 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260 +P0CX44 UniProtKB Modified residue 47 47 . . . Note=N6-methyllysine%3B by RKM5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460220;Dbxref=PMID:21460220 +P0CX44 UniProtKB Modified residue 79 79 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P0CX44 UniProtKB Modified residue 86 86 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P0CX23 1 172 +P0CX23 UniProtKB Chain 1 172 . . . ID=PRO_0000278969;Note=60S ribosomal protein L20-A +P0CX23 UniProtKB Modified residue 32 32 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX23 UniProtKB Cross-link 125 125 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX23 UniProtKB Cross-link 131 131 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX23 UniProtKB Cross-link 149 149 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX23 UniProtKB Beta strand 5 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX23 UniProtKB Beta strand 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX23 UniProtKB Beta strand 25 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX23 UniProtKB Helix 34 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX23 UniProtKB Turn 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX23 UniProtKB Helix 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX23 UniProtKB Beta strand 56 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX23 UniProtKB Beta strand 73 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX23 UniProtKB Beta strand 86 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX23 UniProtKB Helix 99 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX23 UniProtKB Helix 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX23 UniProtKB Beta strand 121 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX23 UniProtKB Beta strand 131 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P0CX23 UniProtKB Helix 138 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX23 UniProtKB Helix 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX23 UniProtKB Beta strand 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4N +P0CX23 UniProtKB Beta strand 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX23 UniProtKB Beta strand 164 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P05749 1 121 +P05749 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:6814480;Dbxref=PMID:10601260,PMID:6814480 +P05749 UniProtKB Chain 2 121 . . . ID=PRO_0000215514;Note=60S ribosomal protein L22-A +P05749 UniProtKB Sequence conflict 49 49 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05749 UniProtKB Beta strand 13 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05749 UniProtKB Helix 20 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05749 UniProtKB Turn 24 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P05749 UniProtKB Helix 30 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05749 UniProtKB Beta strand 42 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05749 UniProtKB Beta strand 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05749 UniProtKB Turn 49 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05749 UniProtKB Beta strand 54 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05749 UniProtKB Beta strand 60 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05749 UniProtKB Helix 73 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05749 UniProtKB Turn 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05749 UniProtKB Beta strand 94 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05749 UniProtKB Beta strand 102 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P24000 1 155 +P24000 UniProtKB Chain 1 155 . . . ID=PRO_0000136895;Note=60S ribosomal protein L24-B +P24000 UniProtKB Modified residue 7 7 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P0C2H6 1 136 +P0C2H6 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P0C2H6 UniProtKB Chain 2 136 . . . ID=PRO_0000126092;Note=60S ribosomal protein L27-A +P0C2H6 UniProtKB Turn 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56 +P0C2H6 UniProtKB Beta strand 9 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H6 UniProtKB Beta strand 15 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H6 UniProtKB Beta strand 22 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H6 UniProtKB Beta strand 34 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H6 UniProtKB Beta strand 40 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H6 UniProtKB Beta strand 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4N +P0C2H6 UniProtKB Helix 61 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H6 UniProtKB Beta strand 69 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H6 UniProtKB Helix 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H6 UniProtKB Beta strand 80 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H6 UniProtKB Helix 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H6 UniProtKB Turn 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H6 UniProtKB Turn 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H6 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H6 UniProtKB Helix 104 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H6 UniProtKB Turn 123 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H6 UniProtKB Helix 128 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P0CX46 1 254 +P0CX46 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1544921,ECO:0000269|PubMed:18782943;Dbxref=PMID:1544921,PMID:18782943 +P0CX46 UniProtKB Chain 2 254 . . . ID=PRO_0000409769;Note=60S ribosomal protein L2-B +P0CX46 UniProtKB Modified residue 52 52 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX46 UniProtKB Modified residue 95 95 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX46 UniProtKB Modified residue 159 159 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX46 UniProtKB Modified residue 160 160 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX46 UniProtKB Modified residue 249 249 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX46 UniProtKB Cross-link 46 46 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX46 UniProtKB Cross-link 93 93 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX46 UniProtKB Cross-link 119 119 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX46 UniProtKB Cross-link 145 145 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P0C2H8 1 113 +P0C2H8 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:18782943 +P0C2H8 UniProtKB Chain 2 113 . . . ID=PRO_0000153788;Note=60S ribosomal protein L31-A +P0C2H8 UniProtKB Beta strand 9 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H8 UniProtKB Helix 16 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H8 UniProtKB Turn 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H8 UniProtKB Helix 28 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H8 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H8 UniProtKB Helix 53 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H8 UniProtKB Helix 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U6F +P0C2H8 UniProtKB Beta strand 69 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H8 UniProtKB Beta strand 86 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H8 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C2H8 UniProtKB Beta strand 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Q +##sequence-region P51402 1 88 +P51402 UniProtKB Chain 1 88 . . . ID=PRO_0000139723;Note=60S ribosomal protein L37-B +P51402 UniProtKB Zinc finger 19 37 . . . Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P51402 UniProtKB Metal binding 19 19 . . . Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22096102;Dbxref=PMID:22096102 +P51402 UniProtKB Metal binding 22 22 . . . Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22096102;Dbxref=PMID:22096102 +P51402 UniProtKB Metal binding 34 34 . . . Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22096102;Dbxref=PMID:22096102 +P51402 UniProtKB Metal binding 37 37 . . . Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22096102;Dbxref=PMID:22096102 +##sequence-region P0CX45 1 254 +P0CX45 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1544921,ECO:0000269|PubMed:18782943;Dbxref=PMID:1544921,PMID:18782943 +P0CX45 UniProtKB Chain 2 254 . . . ID=PRO_0000129761;Note=60S ribosomal protein L2-A +P0CX45 UniProtKB Modified residue 52 52 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX45 UniProtKB Modified residue 95 95 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX45 UniProtKB Modified residue 159 159 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX45 UniProtKB Modified residue 160 160 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX45 UniProtKB Modified residue 249 249 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX45 UniProtKB Cross-link 46 46 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX45 UniProtKB Cross-link 93 93 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX45 UniProtKB Cross-link 119 119 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX45 UniProtKB Cross-link 145 145 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX45 UniProtKB Helix 6 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Helix 10 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Helix 14 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Helix 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P0CX45 UniProtKB Helix 34 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Beta strand 41 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Beta strand 58 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Beta strand 68 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Beta strand 87 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Helix 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Beta strand 112 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Beta strand 118 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56 +P0CX45 UniProtKB Beta strand 134 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Turn 141 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Beta strand 145 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Beta strand 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Q +P0CX45 UniProtKB Beta strand 155 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Beta strand 163 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Beta strand 169 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P0CX45 UniProtKB Helix 174 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Helix 182 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Beta strand 191 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P0CX45 UniProtKB Helix 201 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Helix 206 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Turn 210 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P0CX45 UniProtKB Turn 214 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Beta strand 223 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Turn 231 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX45 UniProtKB Beta strand 236 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P14120 1 105 +P14120 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:3316213;Dbxref=PMID:10601260,PMID:3316213 +P14120 UniProtKB Chain 2 105 . . . ID=PRO_0000146143;Note=60S ribosomal protein L30 +P14120 UniProtKB Cross-link 22 22 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P14120 UniProtKB Cross-link 53 53 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P14120 UniProtKB Cross-link 83 83 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P14120 UniProtKB Helix 7 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NMU +P14120 UniProtKB Beta strand 21 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NMU +P14120 UniProtKB Helix 26 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NMU +P14120 UniProtKB Beta strand 40 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NMU +P14120 UniProtKB Helix 53 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NMU +P14120 UniProtKB Beta strand 67 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NMU +P14120 UniProtKB Helix 79 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NMU +P14120 UniProtKB Beta strand 88 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NMU +P14120 UniProtKB Helix 100 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NMU +##sequence-region P05744 1 107 +P05744 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:18782943 +P05744 UniProtKB Chain 2 107 . . . ID=PRO_0000192807;Note=60S ribosomal protein L33-A +P05744 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P05744 UniProtKB Cross-link 47 47 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P05744 UniProtKB Sequence conflict 24 24 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05744 UniProtKB Beta strand 8 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05744 UniProtKB Beta strand 23 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05744 UniProtKB Helix 38 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05744 UniProtKB Turn 42 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05744 UniProtKB Beta strand 48 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05744 UniProtKB Beta strand 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05744 UniProtKB Beta strand 63 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05744 UniProtKB Beta strand 76 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05744 UniProtKB Beta strand 81 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05744 UniProtKB Turn 92 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05744 UniProtKB Beta strand 97 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P87262 1 121 +P87262 UniProtKB Chain 1 121 . . . ID=PRO_0000131845;Note=60S ribosomal protein L34-A +P87262 UniProtKB Beta strand 8 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P87262 UniProtKB Helix 16 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P87262 UniProtKB Beta strand 19 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P87262 UniProtKB Turn 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U53 +P87262 UniProtKB Beta strand 30 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P87262 UniProtKB Turn 45 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P87262 UniProtKB Beta strand 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U50 +P87262 UniProtKB Helix 59 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P87262 UniProtKB Helix 67 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P87262 UniProtKB Turn 75 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P87262 UniProtKB Helix 83 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P0CX84 1 120 +P0CX84 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983894;Dbxref=PMID:11983894 +P0CX84 UniProtKB Chain 2 120 . . . ID=PRO_0000130552;Note=60S ribosomal protein L35-A +P0CX84 UniProtKB Modified residue 13 13 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX84 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX84 UniProtKB Helix 6 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX84 UniProtKB Helix 14 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX84 UniProtKB Helix 43 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX84 UniProtKB Turn 69 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX84 UniProtKB Helix 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX84 UniProtKB Helix 86 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX84 UniProtKB Helix 94 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX84 UniProtKB Helix 102 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX84 UniProtKB Beta strand 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P05745 1 100 +P05745 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P05745 UniProtKB Chain 2 100 . . . ID=PRO_0000195020;Note=60S ribosomal protein L36-A +P05745 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P05745 UniProtKB Beta strand 6 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05745 UniProtKB Helix 26 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05745 UniProtKB Helix 35 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05745 UniProtKB Helix 52 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05745 UniProtKB Helix 66 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05745 UniProtKB Beta strand 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Z +P05745 UniProtKB Helix 80 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05745 UniProtKB Turn 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P49626 1 362 +P49626 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921 +P49626 UniProtKB Chain 2 362 . . . ID=PRO_0000129368;Note=60S ribosomal protein L4-B +P49626 UniProtKB Region 277 362 . . . Note=C-terminal-extended nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P49626 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921 +P49626 UniProtKB Mutagenesis 95 95 . . . Note=Leads to a slower growth at higher temperatures but allows RPL4 assembly into the 60S subunit%3B when associated with E-98. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P49626 UniProtKB Mutagenesis 98 98 . . . Note=Leads to a slower growth at higher temperatures but allows RPL4 assembly into the mature 60S%3B when associated with E-95. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P49626 UniProtKB Mutagenesis 289 289 . . . Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with A-290 and A-295. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P49626 UniProtKB Mutagenesis 290 290 . . . Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with A-289 and A-295. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P49626 UniProtKB Mutagenesis 295 295 . . . Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with A-289 and A-290. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P49626 UniProtKB Mutagenesis 314 314 . . . Note=Significantly diminished nuclear localization%3B when associated with A-315 and A-319. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P49626 UniProtKB Mutagenesis 315 315 . . . Note=Significantly diminished nuclear localization%3B when associated with A-314 and A-319. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P49626 UniProtKB Mutagenesis 319 319 . . . Note=Significantly diminished nuclear localization%3B when associated with A-314 and A-315. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P49626 UniProtKB Mutagenesis 332 332 . . . Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with A-334. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P49626 UniProtKB Mutagenesis 334 334 . . . Note=Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit%3B when associated with e-332. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25936803;Dbxref=PMID:25936803 +P49626 UniProtKB Sequence conflict 88 88 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02753 1 160 +Q02753 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +Q02753 UniProtKB Chain 2 160 . . . ID=PRO_0000149682;Note=60S ribosomal protein L21-A +Q02753 UniProtKB Cross-link 32 32 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12672 +Q02753 UniProtKB Turn 7 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q02753 UniProtKB Turn 12 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q02753 UniProtKB Helix 28 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q02753 UniProtKB Beta strand 39 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q02753 UniProtKB Helix 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q02753 UniProtKB Beta strand 61 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q02753 UniProtKB Beta strand 69 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q02753 UniProtKB Beta strand 83 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q02753 UniProtKB Helix 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q02753 UniProtKB Beta strand 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q02753 UniProtKB Helix 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M +Q02753 UniProtKB Helix 103 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q02753 UniProtKB Turn 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P0CX82 1 189 +P0CX82 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1544921,ECO:0000269|PubMed:6355773;Dbxref=PMID:1544921,PMID:6355773 +P0CX82 UniProtKB Chain 2 189 . . . ID=PRO_0000131184;Note=60S ribosomal protein L19-A +P0CX82 UniProtKB Modified residue 30 30 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX82 UniProtKB Modified residue 37 37 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX82 UniProtKB Modified residue 91 91 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX82 UniProtKB Cross-link 21 21 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX82 UniProtKB Cross-link 53 53 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX82 UniProtKB Cross-link 60 60 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX82 UniProtKB Cross-link 146 146 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX82 UniProtKB Cross-link 186 186 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX82 UniProtKB Sequence conflict 54 54 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0CX82 UniProtKB Helix 5 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX82 UniProtKB Helix 19 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX82 UniProtKB Beta strand 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX82 UniProtKB Helix 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P0CX82 UniProtKB Helix 29 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX82 UniProtKB Helix 38 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX82 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX82 UniProtKB Helix 61 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX82 UniProtKB Turn 72 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX82 UniProtKB Helix 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX82 UniProtKB Helix 85 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX82 UniProtKB Helix 91 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX82 UniProtKB Turn 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX82 UniProtKB Helix 117 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX82 UniProtKB Beta strand 129 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX82 UniProtKB Beta strand 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56 +P0CX82 UniProtKB Helix 135 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX82 UniProtKB Turn 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX82 UniProtKB Helix 183 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P56628 1 122 +P56628 UniProtKB Chain 1 122 . . . ID=PRO_0000215515;Note=60S ribosomal protein L22-B +##sequence-region P0CX83 1 189 +P0CX83 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1544921,ECO:0000269|PubMed:6355773;Dbxref=PMID:1544921,PMID:6355773 +P0CX83 UniProtKB Chain 2 189 . . . ID=PRO_0000410446;Note=60S ribosomal protein L19-B +P0CX83 UniProtKB Modified residue 30 30 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX83 UniProtKB Modified residue 37 37 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX83 UniProtKB Modified residue 91 91 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX83 UniProtKB Cross-link 21 21 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX83 UniProtKB Cross-link 53 53 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX83 UniProtKB Cross-link 60 60 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX83 UniProtKB Cross-link 146 146 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX83 UniProtKB Cross-link 186 186 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P36144 1 274 +P36144 UniProtKB Chain 1 274 . . . ID=PRO_0000203217;Note=Ribosome biogenesis protein UTP30 +##sequence-region P05743 1 127 +P05743 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18782943;Dbxref=PMID:18782943 +P05743 UniProtKB Chain 2 127 . . . ID=PRO_0000130801;Note=60S ribosomal protein L26-A +P05743 UniProtKB Beta strand 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P05743 UniProtKB Helix 12 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05743 UniProtKB Helix 24 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05743 UniProtKB Beta strand 32 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05743 UniProtKB Helix 37 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05743 UniProtKB Beta strand 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05743 UniProtKB Beta strand 55 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05743 UniProtKB Turn 62 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05743 UniProtKB Beta strand 67 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05743 UniProtKB Helix 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05743 UniProtKB Beta strand 79 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05743 UniProtKB Beta strand 86 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05743 UniProtKB Beta strand 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05743 UniProtKB Beta strand 94 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05743 UniProtKB Helix 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05743 UniProtKB Beta strand 104 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05743 UniProtKB Helix 113 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region Q03942 1 479 +Q03942 UniProtKB Chain 1 479 . . . ID=PRO_0000253809;Note=Ribosomal lysine N-methyltransferase 2 +Q03942 UniProtKB Domain 22 325 . . . Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 +Q03942 UniProtKB Binding site 324 324 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 +##sequence-region P40212 1 199 +P40212 UniProtKB Chain 1 199 . . . ID=PRO_0000192939;Note=60S ribosomal protein L13-B +P40212 UniProtKB Modified residue 144 144 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40212 UniProtKB Modified residue 152 152 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38754 1 138 +P38754 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36105 +P38754 UniProtKB Chain 2 138 . . . ID=PRO_0000132044;Note=60S ribosomal protein L14-B +P38754 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36105 +##sequence-region P05740 1 184 +P05740 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:18782943 +P05740 UniProtKB Chain 2 184 . . . ID=PRO_0000125347;Note=60S ribosomal protein L17-A +P05740 UniProtKB Modified residue 70 70 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P05740 UniProtKB Cross-link 46 46 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P05740 UniProtKB Sequence conflict 104 114 . . . Note=AKGLDATKLYV->VCQEYYMFSTR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05740 UniProtKB Helix 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05740 UniProtKB Beta strand 14 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05740 UniProtKB Helix 26 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05740 UniProtKB Turn 35 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05740 UniProtKB Helix 41 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05740 UniProtKB Beta strand 54 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56 +P05740 UniProtKB Beta strand 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05740 UniProtKB Helix 71 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05740 UniProtKB Beta strand 79 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P05740 UniProtKB Helix 85 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05740 UniProtKB Beta strand 111 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05740 UniProtKB Beta strand 125 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05740 UniProtKB Helix 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05740 UniProtKB Beta strand 135 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05740 UniProtKB Beta strand 144 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05740 UniProtKB Helix 170 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P0CX50 1 186 +P0CX50 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11983894;Dbxref=PMID:11983894 +P0CX50 UniProtKB Chain 2 186 . . . ID=PRO_0000409771;Note=60S ribosomal protein L18-B +P0CX50 UniProtKB Modified residue 50 50 . . . Note=N6%2CN6%2CN6-trimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22522802;Dbxref=PMID:22522802 +P0CX50 UniProtKB Cross-link 116 116 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P0CX43 1 217 +P0CX43 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260 +P0CX43 UniProtKB Chain 2 217 . . . ID=PRO_0000125842;Note=60S ribosomal protein L1-A +P0CX43 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260 +P0CX43 UniProtKB Modified residue 47 47 . . . Note=N6-methyllysine%3B by RKM5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21460220;Dbxref=PMID:21460220 +P0CX43 UniProtKB Modified residue 79 79 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P0CX43 UniProtKB Modified residue 86 86 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P04449 1 155 +P04449 UniProtKB Chain 1 155 . . . ID=PRO_0000136894;Note=60S ribosomal protein L24-A +P04449 UniProtKB Modified residue 7 7 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24000 +P04449 UniProtKB Turn 7 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04449 UniProtKB Beta strand 18 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04449 UniProtKB Beta strand 24 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P04449 UniProtKB Beta strand 28 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04449 UniProtKB Helix 34 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04449 UniProtKB Helix 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04449 UniProtKB Helix 53 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04449 UniProtKB Turn 59 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04449 UniProtKB Helix 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04449 UniProtKB Beta strand 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04449 UniProtKB Turn 87 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04449 UniProtKB Beta strand 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04449 UniProtKB Helix 98 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04449 UniProtKB Helix 113 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P04449 UniProtKB Turn 130 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P53221 1 127 +P53221 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18782943;Dbxref=PMID:18782943 +P53221 UniProtKB Chain 2 127 . . . ID=PRO_0000130802;Note=60S ribosomal protein L26-B +##sequence-region P0C2H7 1 136 +P0C2H7 UniProtKB Chain 1 136 . . . ID=PRO_0000278967;Note=60S ribosomal protein L27-B +##sequence-region P41056 1 107 +P41056 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18782943;Dbxref=PMID:18782943 +P41056 UniProtKB Chain 2 107 . . . ID=PRO_0000192808;Note=60S ribosomal protein L33-B +P41056 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine%3B partial;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05744 +P41056 UniProtKB Cross-link 47 47 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05744 +P41056 UniProtKB Sequence conflict 24 24 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12338 1 110 +Q12338 UniProtKB Chain 1 110 . . . ID=PRO_0000248387;Note=Ribonuclease H2 subunit C +Q12338 UniProtKB Sequence conflict 64 64 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32385 1 249 +P32385 UniProtKB Chain 1 249 . . . ID=PRO_0000081810;Note=Ribonucleoprotein 1 +P32385 UniProtKB Domain 35 114 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P32385 UniProtKB Domain 140 231 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +##sequence-region P25367 1 405 +P25367 UniProtKB Chain 1 405 . . . ID=PRO_0000097390;Note=[PIN+] prion protein RNQ1 +P25367 UniProtKB Region 153 402 . . . Note=Prion domain (PrD) +P25367 UniProtKB Modified residue 143 143 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25367 UniProtKB Cross-link 5 5 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25367 UniProtKB Cross-link 84 84 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25367 UniProtKB Natural variant 166 169 . . . Note=In strain: SCI7.2/b%2C SCI11.5/a and SCI11.5/c. Missing +P25367 UniProtKB Natural variant 171 172 . . . Note=In strain: SCI7.2/a%2C SCI7.2/d%2C SCI11.5/b and SCI11.5/d. Missing +P25367 UniProtKB Natural variant 289 299 . . . Note=In strain: SCI7.2/b%2C SCI7.2/d and SCI11.5/c. Missing +P25367 UniProtKB Natural variant 293 303 . . . Note=In strain: SCI9. Missing +P25367 UniProtKB Natural variant 360 360 . . . Note=In strain: SCI3%2C SCI4%2C SCI7.2/a%2C SCI7.2/b%2C SCI7.2/d%2C SCI11.5/a%2C SCI11.5/b%2C SCI11.5/c and SCI11.5/d. Q->H +P25367 UniProtKB Natural variant 372 372 . . . Note=In strain: SCI7.2/b%2C SCI7.2/d and SCI11.5/c. P->PQHNGQQQSNEYGRP +P25367 UniProtKB Natural variant 383 383 . . . Note=In strain: SCI7.2/b%2CSCI7.2/d and SCI11.5/c. Q->H +P25367 UniProtKB Natural variant 387 387 . . . Note=In strain: SCI4. F->L +P25367 UniProtKB Sequence conflict 181 181 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02555 1 471 +Q02555 UniProtKB Chain 1 471 . . . ID=PRO_0000180466;Note=Ribonuclease 3 +Q02555 UniProtKB Domain 227 331 . . . Note=RNase III;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00177 +Q02555 UniProtKB Domain 369 437 . . . Note=DRBM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00266 +Q02555 UniProtKB Helix 46 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Helix 73 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Beta strand 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Helix 88 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Helix 97 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Helix 116 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Beta strand 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Helix 140 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Helix 208 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Helix 218 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Helix 229 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Helix 238 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Helix 265 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Helix 278 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Helix 290 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Beta strand 303 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T16 +Q02555 UniProtKB Turn 306 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Helix 313 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Helix 331 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Helix 358 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Helix 370 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T4O +Q02555 UniProtKB Helix 381 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T4O +Q02555 UniProtKB Beta strand 386 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T4O +Q02555 UniProtKB Beta strand 394 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T4N +Q02555 UniProtKB Beta strand 400 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T4O +Q02555 UniProtKB Turn 407 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T4L +Q02555 UniProtKB Beta strand 411 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T4O +Q02555 UniProtKB Helix 420 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T4O +Q02555 UniProtKB Helix 435 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1T4O +Q02555 UniProtKB Helix 450 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OOG +Q02555 UniProtKB Beta strand 455 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T16 +##sequence-region P39956 1 796 +P39956 UniProtKB Chain 1 796 . . . ID=PRO_0000046849;Note=DNA damage-responsive transcriptional repressor RPH1 +P39956 UniProtKB Domain 14 55 . . . Note=JmjN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00537 +P39956 UniProtKB Domain 193 355 . . . Note=JmjC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00538 +P39956 UniProtKB Zinc finger 709 732 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P39956 UniProtKB Zinc finger 738 763 . . . Note=C2H2-type 2%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P39956 UniProtKB Motif 455 471 . . . Note=Bipartite nuclear localization signal +P39956 UniProtKB Modified residue 399 399 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39956 UniProtKB Modified residue 430 430 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39956 UniProtKB Modified residue 459 459 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39956 UniProtKB Modified residue 557 557 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39956 UniProtKB Modified residue 561 561 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P39956 UniProtKB Modified residue 575 575 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P39956 UniProtKB Modified residue 584 584 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39956 UniProtKB Modified residue 652 652 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P39956 UniProtKB Modified residue 689 689 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P39956 UniProtKB Beta strand 9 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Helix 21 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Helix 27 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Helix 35 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Beta strand 41 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Helix 50 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Helix 62 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Beta strand 69 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Beta strand 74 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Beta strand 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Helix 98 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Turn 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPW +P39956 UniProtKB Helix 142 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Turn 149 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Helix 157 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPW +P39956 UniProtKB Helix 162 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Turn 175 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Beta strand 182 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Beta strand 201 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPW +P39956 UniProtKB Beta strand 222 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Beta strand 231 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Helix 238 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Beta strand 242 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Beta strand 253 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Helix 260 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Helix 263 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Helix 275 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Turn 285 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Beta strand 290 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Helix 294 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Turn 299 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Beta strand 305 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Beta strand 314 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +P39956 UniProtKB Beta strand 323 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPT +##sequence-region P23250 1 407 +P23250 UniProtKB Chain 1 407 . . . ID=PRO_0000197113;Note=Negative RAS protein regulator protein +P23250 UniProtKB Domain 90 158 . . . Note=Myb-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00133 +P23250 UniProtKB Sequence conflict 37 37 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23250 UniProtKB Sequence conflict 37 37 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23250 UniProtKB Sequence conflict 71 73 . . . Note=SNS->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23250 UniProtKB Sequence conflict 71 73 . . . Note=SNS->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23250 UniProtKB Sequence conflict 91 91 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23250 UniProtKB Sequence conflict 91 91 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23250 UniProtKB Sequence conflict 170 174 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23250 UniProtKB Sequence conflict 170 174 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23250 UniProtKB Sequence conflict 190 190 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23250 UniProtKB Sequence conflict 240 240 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23250 UniProtKB Sequence conflict 240 240 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23250 UniProtKB Sequence conflict 242 242 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23250 UniProtKB Sequence conflict 242 242 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23250 UniProtKB Sequence conflict 252 252 . . . Note=N->NNNNSNN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P23250 UniProtKB Sequence conflict 252 252 . . . Note=N->NNNNSNN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38886 1 268 +P38886 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901 +P38886 UniProtKB Chain 2 268 . . . ID=PRO_0000173834;Note=26S proteasome regulatory subunit RPN10 +P38886 UniProtKB Domain 5 190 . . . Note=VWFA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00219 +P38886 UniProtKB Domain 223 242 . . . Note=UIM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213 +P38886 UniProtKB Compositional bias 248 255 . . . Note=Poly-Gln +P38886 UniProtKB Beta strand 4 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1 +P38886 UniProtKB Helix 14 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1 +P38886 UniProtKB Beta strand 19 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1 +P38886 UniProtKB Helix 25 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1 +P38886 UniProtKB Beta strand 48 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1 +P38886 UniProtKB Beta strand 55 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1 +P38886 UniProtKB Beta strand 60 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1 +P38886 UniProtKB Helix 69 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1 +P38886 UniProtKB Helix 87 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1 +P38886 UniProtKB Beta strand 106 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1 +P38886 UniProtKB Helix 122 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1 +P38886 UniProtKB Beta strand 137 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1 +P38886 UniProtKB Helix 154 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1 +P38886 UniProtKB Beta strand 164 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1 +P38886 UniProtKB Beta strand 171 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1 +P38886 UniProtKB Beta strand 176 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1 +P38886 UniProtKB Helix 181 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LN1 +##sequence-region P53196 1 417 +P53196 UniProtKB Chain 1 417 . . . ID=PRO_0000051475;Note=26S proteasome regulatory subunit RPN14 +P53196 UniProtKB Repeat 134 173 . . . Note=WD 1 +P53196 UniProtKB Repeat 176 215 . . . Note=WD 2 +P53196 UniProtKB Repeat 242 281 . . . Note=WD 3 +P53196 UniProtKB Repeat 285 325 . . . Note=WD 4 +P53196 UniProtKB Repeat 330 371 . . . Note=WD 5 +P53196 UniProtKB Repeat 380 416 . . . Note=WD 6 +P53196 UniProtKB Beta strand 3 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 8 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Helix 14 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 27 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 38 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Turn 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 60 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 68 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 76 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Turn 87 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 96 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 108 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 118 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 127 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 134 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 139 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 148 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 158 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Turn 165 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 172 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 181 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Turn 188 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 192 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 202 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Turn 207 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 211 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 226 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Helix 240 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 257 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 268 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Turn 273 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 278 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 290 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 302 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 310 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 324 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 335 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 344 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Turn 350 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 353 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 366 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ACP +P53196 UniProtKB Beta strand 376 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 387 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 394 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 399 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Turn 405 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +P53196 UniProtKB Beta strand 408 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3VL1 +##sequence-region P40011 1 234 +P40011 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40011 UniProtKB Chain 2 234 . . . ID=PRO_0000202621;Note=4-hydroxy-4-methyl-2-oxoglutarate aldolase +P40011 UniProtKB Region 100 103 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40011 UniProtKB Metal binding 123 123 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40011 UniProtKB Binding site 122 122 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40011 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40011 UniProtKB Helix 3 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Helix 12 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Turn 26 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Beta strand 35 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Beta strand 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Beta strand 45 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Beta strand 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Helix 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Beta strand 74 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Helix 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Helix 101 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Beta strand 114 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Helix 124 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Beta strand 134 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Turn 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Beta strand 148 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Beta strand 157 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Beta strand 166 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Beta strand 174 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Beta strand 181 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Turn 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Helix 192 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Helix 219 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +P40011 UniProtKB Helix 228 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Q +##sequence-region P35178 1 278 +P35178 UniProtKB Chain 1 278 . . . ID=PRO_0000097452;Note=Ribosomal RNA-processing protein 1 +P35178 UniProtKB Compositional bias 266 274 . . . Note=Poly-Glu +P35178 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P35178 UniProtKB Modified residue 267 267 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region Q08285 1 240 +Q08285 UniProtKB Chain 1 240 . . . ID=PRO_0000097453;Note=Exosome complex component RRP40 +Q08285 UniProtKB Domain 67 137 . . . Note=S1 motif +Q08285 UniProtKB Sequence conflict 160 160 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08285 UniProtKB Beta strand 3 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Beta strand 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Beta strand 19 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Beta strand 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Turn 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Beta strand 34 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Beta strand 40 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Beta strand 53 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Beta strand 71 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Beta strand 81 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Beta strand 95 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Beta strand 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Beta strand 118 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Beta strand 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Beta strand 133 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Turn 139 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Beta strand 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Beta strand 154 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Helix 160 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Helix 174 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Beta strand 185 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Turn 190 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Beta strand 193 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Helix 201 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08285 UniProtKB Helix 220 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36 +Q08285 UniProtKB Helix 223 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +##sequence-region Q05636 1 305 +Q05636 UniProtKB Chain 1 305 . . . ID=PRO_0000139974;Note=Exosome complex component RRP45 +Q05636 UniProtKB Helix 9 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Beta strand 36 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Beta strand 46 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Beta strand 54 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Beta strand 76 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Helix 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +Q05636 UniProtKB Helix 99 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Turn 113 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Beta strand 123 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Turn 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Beta strand 130 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Helix 147 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Beta strand 167 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Beta strand 173 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Turn 179 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Beta strand 194 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Helix 206 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Beta strand 218 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Helix 225 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Beta strand 232 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Beta strand 243 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Helix 258 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q05636 UniProtKB Beta strand 299 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WP8 +##sequence-region Q05022 1 1729 +Q05022 UniProtKB Chain 1 1729 . . . ID=PRO_0000205763;Note=rRNA biogenesis protein RRP5 +Q05022 UniProtKB Domain 119 200 . . . Note=S1 motif 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180 +Q05022 UniProtKB Domain 338 410 . . . Note=S1 motif 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180 +Q05022 UniProtKB Domain 510 580 . . . Note=S1 motif 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180 +Q05022 UniProtKB Domain 607 676 . . . Note=S1 motif 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180 +Q05022 UniProtKB Domain 690 769 . . . Note=S1 motif 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180 +Q05022 UniProtKB Domain 794 863 . . . Note=S1 motif 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180 +Q05022 UniProtKB Domain 895 971 . . . Note=S1 motif 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180 +Q05022 UniProtKB Domain 1003 1083 . . . Note=S1 motif 8;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180 +Q05022 UniProtKB Domain 1088 1159 . . . Note=S1 motif 9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180 +Q05022 UniProtKB Domain 1177 1245 . . . Note=S1 motif 10;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180 +Q05022 UniProtKB Domain 1265 1336 . . . Note=S1 motif 11;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180 +Q05022 UniProtKB Repeat 1455 1487 . . . Note=HAT 1 +Q05022 UniProtKB Repeat 1561 1594 . . . Note=HAT 2 +Q05022 UniProtKB Repeat 1632 1664 . . . Note=HAT 3 +Q05022 UniProtKB Repeat 1666 1701 . . . Note=HAT 4 +Q05022 UniProtKB Modified residue 47 47 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950;Dbxref=PMID:15665377,PMID:17330950 +Q05022 UniProtKB Modified residue 187 187 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q05022 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q05022 UniProtKB Modified residue 1724 1724 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q05022 UniProtKB Helix 1409 1416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S +Q05022 UniProtKB Helix 1461 1470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S +Q05022 UniProtKB Helix 1475 1487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S +Q05022 UniProtKB Helix 1491 1504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S +Q05022 UniProtKB Helix 1510 1527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S +Q05022 UniProtKB Helix 1530 1543 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S +Q05022 UniProtKB Helix 1546 1560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S +Q05022 UniProtKB Helix 1563 1577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S +Q05022 UniProtKB Turn 1578 1580 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S +Q05022 UniProtKB Helix 1583 1594 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S +Q05022 UniProtKB Helix 1598 1611 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S +Q05022 UniProtKB Helix 1614 1616 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S +Q05022 UniProtKB Helix 1617 1630 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S +Q05022 UniProtKB Helix 1634 1647 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S +Q05022 UniProtKB Helix 1652 1665 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S +Q05022 UniProtKB Helix 1668 1679 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S +Q05022 UniProtKB Helix 1685 1702 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S +Q05022 UniProtKB Helix 1705 1719 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C9S +##sequence-region P25368 1 297 +P25368 UniProtKB Chain 1 297 . . . ID=PRO_0000097457;Note=Ribosomal RNA-processing protein 7 +P25368 UniProtKB Sequence conflict 66 66 . . . Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25368 UniProtKB Beta strand 14 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P25368 UniProtKB Beta strand 34 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P25368 UniProtKB Helix 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P25368 UniProtKB Beta strand 51 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P25368 UniProtKB Helix 64 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P25368 UniProtKB Beta strand 84 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P25368 UniProtKB Helix 100 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P25368 UniProtKB Beta strand 123 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P25368 UniProtKB Helix 131 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P25368 UniProtKB Helix 147 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P25368 UniProtKB Helix 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P25368 UniProtKB Helix 165 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P25368 UniProtKB Helix 177 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M5D +P25368 UniProtKB Helix 256 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MBY +P25368 UniProtKB Helix 269 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MBY +##sequence-region P25381 1 491 +P25381 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25381 UniProtKB Chain 18 491 . . . ID=PRO_0000027205;Note=Subtilase-type proteinase RRT12 +P25381 UniProtKB Domain 156 389 . . . Note=Peptidase S8 +P25381 UniProtKB Active site 174 174 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25381 UniProtKB Active site 205 205 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25381 UniProtKB Active site 365 365 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25381 UniProtKB Glycosylation 38 38 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25381 UniProtKB Glycosylation 64 64 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25381 UniProtKB Glycosylation 106 106 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25381 UniProtKB Glycosylation 121 121 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25381 UniProtKB Glycosylation 268 268 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25381 UniProtKB Glycosylation 356 356 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25381 UniProtKB Glycosylation 449 449 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25381 UniProtKB Mutagenesis 365 365 . . . Note=Abolishes protease activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19779569;Dbxref=PMID:19779569 +##sequence-region P32611 1 393 +P32611 UniProtKB Transit peptide 1 43 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32611 UniProtKB Chain 44 393 . . . ID=PRO_0000030512;Note=54S ribosomal protein RML2%2C mitochondrial +P32611 UniProtKB Mutagenesis 336 342 . . . Note=Loss of function. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9079633;Dbxref=PMID:9079633 +P32611 UniProtKB Mutagenesis 343 343 . . . Note=Causes a cold-sensitive respiratory growth defect. Does not impair assembly of the ribosomal subunit. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9079633;Dbxref=PMID:9079633 +##sequence-region P53942 1 307 +P53942 UniProtKB Chain 1 307 . . . ID=PRO_0000111718;Note=Ribonuclease H2 subunit A +P53942 UniProtKB Metal binding 39 39 . . . Note=Divalent metal cation +P53942 UniProtKB Metal binding 40 40 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53942 UniProtKB Metal binding 155 155 . . . Note=Divalent metal cation +P53942 UniProtKB Mutagenesis 39 39 . . . Note=Abolishes enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14734815;Dbxref=PMID:14734815 +P53942 UniProtKB Mutagenesis 155 155 . . . Note=Abolishes enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14734815;Dbxref=PMID:14734815 +P53942 UniProtKB Mutagenesis 183 183 . . . Note=Strongly impairs enzyme activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14734815;Dbxref=PMID:14734815 +##sequence-region P45818 1 564 +P45818 UniProtKB Chain 1 564 . . . ID=PRO_0000055063;Note=ATP-dependent RNA helicase ROK1 +P45818 UniProtKB Domain 153 333 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P45818 UniProtKB Domain 344 506 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P45818 UniProtKB Nucleotide binding 166 173 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P45818 UniProtKB Motif 122 150 . . . Note=Q motif +P45818 UniProtKB Motif 280 283 . . . Note=DEAD box +P45818 UniProtKB Mutagenesis 166 166 . . . Note=No cell growth and 2-fold decrease in ATPase activity in vitro. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10373593;Dbxref=PMID:10373593 +P45818 UniProtKB Mutagenesis 172 172 . . . Note=Slow cell growth. K->G%2CR%2CS%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10373593;Dbxref=PMID:10373593 +P45818 UniProtKB Mutagenesis 172 172 . . . Note=No cell growth and drastic decrease in ATPase activity in vitro. K->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10373593;Dbxref=PMID:10373593 +P45818 UniProtKB Mutagenesis 280 280 . . . Note=Slow cell growth. D->A%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10373593;Dbxref=PMID:10373593 +##sequence-region P36121 1 282 +P36121 UniProtKB Chain 1 282 . . . ID=PRO_0000203203;Note=DNA-directed RNA polymerase III subunit RPC5 +P36121 UniProtKB Modified residue 61 61 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P32565 1 945 +P32565 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:12504901;Dbxref=PMID:22814378,PMID:12504901 +P32565 UniProtKB Chain 2 945 . . . ID=PRO_0000173808;Note=26S proteasome regulatory subunit RPN2 +P32565 UniProtKB Repeat 366 399 . . . Note=PC 1 +P32565 UniProtKB Repeat 403 440 . . . Note=PC 2 +P32565 UniProtKB Repeat 445 479 . . . Note=PC 3 +P32565 UniProtKB Repeat 480 514 . . . Note=PC 4 +P32565 UniProtKB Repeat 516 549 . . . Note=PC 5 +P32565 UniProtKB Repeat 550 585 . . . Note=PC 6 +P32565 UniProtKB Repeat 586 618 . . . Note=PC 7 +P32565 UniProtKB Repeat 620 654 . . . Note=PC 8 +P32565 UniProtKB Repeat 655 692 . . . Note=PC 9 +P32565 UniProtKB Repeat 698 734 . . . Note=PC 10 +P32565 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:12504901;Dbxref=PMID:22814378,PMID:12504901 +P32565 UniProtKB Modified residue 801 801 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32565 UniProtKB Modified residue 932 932 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32565 UniProtKB Sequence conflict 333 334 . . . Note=SV->RL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32565 UniProtKB Helix 7 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 18 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 43 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 58 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 75 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 86 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 96 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 123 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 131 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 150 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 163 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 179 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 200 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Beta strand 217 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 222 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 235 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 251 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 267 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 284 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 293 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 311 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 326 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Turn 340 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 347 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 353 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 362 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Turn 379 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 382 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Turn 387 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 398 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Turn 412 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 417 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 437 453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 460 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 475 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 495 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 511 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Turn 525 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 529 532 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 533 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 545 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Turn 559 561 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 565 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 581 594 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Beta strand 596 598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 602 605 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Turn 606 608 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 609 611 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 615 628 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Beta strand 630 632 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 635 645 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 650 663 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Turn 669 671 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 675 687 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Beta strand 689 691 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 693 706 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 709 711 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Beta strand 713 715 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Turn 720 722 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 727 736 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Turn 737 741 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 743 752 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Beta strand 753 755 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Beta strand 757 762 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Turn 763 766 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Beta strand 767 769 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Beta strand 772 775 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Turn 779 782 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Beta strand 866 869 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 878 881 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Beta strand 886 894 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Beta strand 898 908 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +P32565 UniProtKB Helix 920 924 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ADY +##sequence-region P36523 1 253 +P36523 UniProtKB Transit peptide 1 28 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626 +P36523 UniProtKB Chain 29 253 . . . ID=PRO_0000030572;Note=54S ribosomal protein L15%2C mitochondrial +P36523 UniProtKB Sequence conflict 58 58 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36526 1 146 +P36526 UniProtKB Transit peptide 1 16 . . . Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1764528,ECO:0000269|PubMed:2060626;Dbxref=PMID:1764528,PMID:2060626 +P36526 UniProtKB Chain 17 146 . . . ID=PRO_0000030574;Note=54S ribosomal protein L27%2C mitochondrial +P36526 UniProtKB Sequence conflict 17 17 . . . Note=L->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36526 UniProtKB Sequence conflict 21 21 . . . Note=W->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36526 UniProtKB Sequence conflict 48 48 . . . Note=G->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36526 UniProtKB Sequence conflict 57 57 . . . Note=R->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36526 UniProtKB Sequence conflict 72 72 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36526 UniProtKB Sequence conflict 77 77 . . . Note=V->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36526 UniProtKB Sequence conflict 101 101 . . . Note=L->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36526 UniProtKB Sequence conflict 122 122 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36526 UniProtKB Sequence conflict 126 126 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P14063 1 131 +P14063 UniProtKB Transit peptide 1 12 . . . Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2666132,ECO:0000269|PubMed:3060376;Dbxref=PMID:2666132,PMID:3060376 +P14063 UniProtKB Chain 13 131 . . . ID=PRO_0000030579;Note=54S ribosomal protein L31%2C mitochondrial +##sequence-region P02381 1 398 +P02381 UniProtKB Chain 1 398 . . . ID=PRO_0000220076;Note=Ribosomal protein VAR1%2C mitochondrial +P02381 UniProtKB Sequence conflict 169 170 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02381 UniProtKB Sequence conflict 169 170 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02381 UniProtKB Sequence conflict 200 200 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02381 UniProtKB Sequence conflict 200 200 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02381 UniProtKB Sequence conflict 200 200 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02381 UniProtKB Sequence conflict 284 284 . . . Note=N->NNNNNNN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03441 1 430 +Q03441 UniProtKB Chain 1 430 . . . ID=PRO_0000097360;Note=Sporulation protein RMD1 +##sequence-region P53140 1 646 +P53140 UniProtKB Transit peptide 1 14 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53140 UniProtKB Chain 15 646 . . . ID=PRO_0000202752;Note=Protein RMD9%2C mitochondrial +P53140 UniProtKB Mutagenesis 363 363 . . . Note=Causes respiratory deficiency in absence of RSM28. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17194786;Dbxref=PMID:17194786 +P53140 UniProtKB Sequence conflict 426 426 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12530 1 201 +Q12530 UniProtKB Chain 1 201 . . . ID=PRO_0000270572;Note=Ribonuclease MRP protein subunit RMP1 +Q12530 UniProtKB Transmembrane 86 108 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12530 UniProtKB Compositional bias 183 193 . . . Note=Poly-Lys;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12530 UniProtKB Mutagenesis 103 103 . . . Note=In RMP1-6%3B temperature-sensitive phenotype. Defective in 5.8S rRNA processing. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637077;Dbxref=PMID:15637077 +##sequence-region Q03305 1 412 +Q03305 UniProtKB Chain 1 412 . . . ID=PRO_0000228980;Note=Protein arginine N-methyltransferase 2 +Q03305 UniProtKB Domain 189 412 . . . Note=RMT2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00892 +Q03305 UniProtKB Region 250 255 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00892 +Q03305 UniProtKB Region 271 273 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00892 +Q03305 UniProtKB Region 298 299 . . . Note=S-adenosyl-L-methionine binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00892 +Q03305 UniProtKB Binding site 196 196 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00892 +Q03305 UniProtKB Binding site 226 226 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00892 +Q03305 UniProtKB Binding site 319 319 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00892 +Q03305 UniProtKB Modified residue 181 181 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q03305 UniProtKB Modified residue 184 184 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region Q04740 1 348 +Q04740 UniProtKB Chain 1 348 . . . ID=PRO_0000195438;Note=Ribonuclease H +Q04740 UniProtKB Domain 184 346 . . . Note=RNase H;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00408 +Q04740 UniProtKB Metal binding 193 193 . . . Note=Magnesium 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00408 +Q04740 UniProtKB Metal binding 193 193 . . . Note=Magnesium 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00408 +Q04740 UniProtKB Metal binding 235 235 . . . Note=Magnesium 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00408 +Q04740 UniProtKB Metal binding 264 264 . . . Note=Magnesium 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00408 +Q04740 UniProtKB Metal binding 338 338 . . . Note=Magnesium 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00408 +Q04740 UniProtKB Beta strand 6 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHK +Q04740 UniProtKB Beta strand 12 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHK +Q04740 UniProtKB Beta strand 17 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHK +Q04740 UniProtKB Helix 22 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHK +Q04740 UniProtKB Beta strand 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHK +Q04740 UniProtKB Beta strand 38 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHK +Q04740 UniProtKB Helix 43 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QHK +##sequence-region P22138 1 1203 +P22138 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P22138 UniProtKB Chain 2 1203 . . . ID=PRO_0000048080;Note=DNA-directed RNA polymerase I subunit RPA135 +P22138 UniProtKB Zinc finger 1104 1131 . . . Note=C4-type +P22138 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P22138 UniProtKB Modified residue 81 81 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P22138 UniProtKB Modified residue 1156 1156 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P22138 UniProtKB Mutagenesis 1104 1104 . . . Note=No effect%3B when associated with A-1107%3B A-1128 and A-1131. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14555487;Dbxref=PMID:14555487 +P22138 UniProtKB Mutagenesis 1107 1107 . . . Note=Lethal. Abolishes recruitment of RPA1 to Pol I. No effect%3B when associated with A-1104%3B A-1128 and A-1131. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14555487;Dbxref=PMID:14555487 +P22138 UniProtKB Mutagenesis 1127 1127 . . . Note=Responsible of suppression of RPA190-5 and RPA190-1 mutations. C->R +P22138 UniProtKB Mutagenesis 1128 1128 . . . Note=No effect%3B when associated with A-1104%3B A-1107 and A-1131. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14555487;Dbxref=PMID:14555487 +P22138 UniProtKB Mutagenesis 1131 1131 . . . Note=No effect%3B when associated with A-1104%3B A-1107 and A-1128. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14555487;Dbxref=PMID:14555487 +P22138 UniProtKB Helix 18 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 30 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 36 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P22138 UniProtKB Helix 60 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 71 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 86 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P22138 UniProtKB Beta strand 94 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 108 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P22138 UniProtKB Beta strand 117 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P22138 UniProtKB Helix 123 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 134 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 146 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 150 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 171 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 177 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 194 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 199 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 205 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 214 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 220 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 229 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 245 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 258 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 267 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 273 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 285 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 300 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 314 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 323 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 335 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 342 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P22138 UniProtKB Helix 346 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 360 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 367 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 387 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P22138 UniProtKB Helix 397 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 400 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 405 434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 443 451 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 457 467 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 485 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 493 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 502 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 507 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 516 518 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 522 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 525 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 537 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 542 545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 558 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P22138 UniProtKB Helix 561 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 573 575 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 583 588 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 591 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 598 614 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 618 620 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P22138 UniProtKB Beta strand 625 629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 633 636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 639 643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 649 655 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 656 659 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 660 664 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 666 669 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 674 677 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 678 680 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 683 685 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 687 689 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 693 696 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 699 703 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 707 709 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 712 722 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 733 735 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 739 745 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 751 753 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 755 759 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 762 764 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 769 777 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 779 781 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 786 790 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 791 795 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 796 799 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 801 810 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 813 815 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 823 826 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 835 838 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 844 846 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 857 863 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 864 867 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 868 873 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 880 888 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 892 894 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 900 909 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 916 919 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 924 931 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 933 935 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 938 942 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P22138 UniProtKB Beta strand 946 949 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 951 953 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 955 957 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 960 975 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 988 990 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P22138 UniProtKB Helix 992 1003 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 1009 1011 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 1016 1018 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 1026 1036 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 1040 1043 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P22138 UniProtKB Beta strand 1045 1049 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 1054 1056 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 1063 1065 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P22138 UniProtKB Beta strand 1069 1071 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 1073 1082 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 1085 1092 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 1093 1097 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 1098 1104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Turn 1105 1107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 1110 1115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 1120 1122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P22138 UniProtKB Beta strand 1126 1131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 1135 1139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 1155 1157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 1158 1160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 1166 1168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 1173 1179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Helix 1180 1191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P22138 UniProtKB Beta strand 1194 1201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +##sequence-region P20435 1 155 +P20435 UniProtKB Chain 1 155 . . . ID=PRO_0000133797;Note=DNA-directed RNA polymerases I%2C II%2C and III subunit RPABC2 +P20435 UniProtKB Region 111 132 . . . Note=Leucine-zipper +P20435 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P20435 UniProtKB Helix 56 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P20435 UniProtKB Beta strand 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P20435 UniProtKB Helix 87 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P20435 UniProtKB Helix 117 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P20435 UniProtKB Beta strand 132 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P20435 UniProtKB Beta strand 139 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I3Q +P20435 UniProtKB Beta strand 143 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P20435 UniProtKB Turn 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +##sequence-region P28000 1 142 +P28000 UniProtKB Chain 1 142 . . . ID=PRO_0000149319;Note=DNA-directed RNA polymerases I and III subunit RPAC2 +P28000 UniProtKB Modified residue 15 15 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P28000 UniProtKB Modified residue 33 33 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P28000 UniProtKB Cross-link 134 134 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P28000 UniProtKB Beta strand 46 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P28000 UniProtKB Turn 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P28000 UniProtKB Beta strand 58 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P28000 UniProtKB Helix 70 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P28000 UniProtKB Beta strand 86 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P28000 UniProtKB Beta strand 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3H +P28000 UniProtKB Beta strand 100 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P28000 UniProtKB Beta strand 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P28000 UniProtKB Helix 113 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +##sequence-region P04050 1 1733 +P04050 UniProtKB Chain 1 1733 . . . ID=PRO_0000073946;Note=DNA-directed RNA polymerase II subunit RPB1 +P04050 UniProtKB Repeat 1549 1555 . . . Note=1 +P04050 UniProtKB Repeat 1556 1562 . . . Note=2 +P04050 UniProtKB Repeat 1563 1569 . . . Note=3 +P04050 UniProtKB Repeat 1570 1576 . . . Note=4 +P04050 UniProtKB Repeat 1577 1583 . . . Note=5 +P04050 UniProtKB Repeat 1584 1590 . . . Note=6 +P04050 UniProtKB Repeat 1591 1597 . . . Note=7 +P04050 UniProtKB Repeat 1598 1604 . . . Note=8 +P04050 UniProtKB Repeat 1605 1611 . . . Note=9 +P04050 UniProtKB Repeat 1612 1618 . . . Note=10 +P04050 UniProtKB Repeat 1619 1625 . . . Note=11 +P04050 UniProtKB Repeat 1626 1632 . . . Note=12 +P04050 UniProtKB Repeat 1633 1639 . . . Note=13 +P04050 UniProtKB Repeat 1640 1646 . . . Note=14 +P04050 UniProtKB Repeat 1647 1653 . . . Note=15 +P04050 UniProtKB Repeat 1654 1660 . . . Note=16 +P04050 UniProtKB Repeat 1661 1667 . . . Note=17 +P04050 UniProtKB Repeat 1668 1674 . . . Note=18 +P04050 UniProtKB Repeat 1675 1681 . . . Note=19 +P04050 UniProtKB Repeat 1682 1688 . . . Note=20 +P04050 UniProtKB Repeat 1689 1695 . . . Note=21 +P04050 UniProtKB Repeat 1696 1702 . . . Note=22 +P04050 UniProtKB Repeat 1703 1709 . . . Note=23 +P04050 UniProtKB Repeat 1710 1716 . . . Note=24%3B approximate +P04050 UniProtKB Region 248 260 . . . Note=Lid loop +P04050 UniProtKB Region 306 323 . . . Note=Rudder loop +P04050 UniProtKB Region 810 822 . . . Note=Bridging helix +P04050 UniProtKB Region 1549 1716 . . . Note=C-terminal domain (CTD)%3B 24 X 7 AA approximate tandem repeats of Y-S-P-T-S-P-[A-S-N-G] +P04050 UniProtKB Metal binding 67 67 . . . Note=Zinc 1;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824 +P04050 UniProtKB Metal binding 70 70 . . . Note=Zinc 1;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824 +P04050 UniProtKB Metal binding 77 77 . . . Note=Zinc 1;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824 +P04050 UniProtKB Metal binding 80 80 . . . Note=Zinc 1%3B via tele nitrogen;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824 +P04050 UniProtKB Metal binding 107 107 . . . Note=Zinc 2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824 +P04050 UniProtKB Metal binding 110 110 . . . Note=Zinc 2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824 +P04050 UniProtKB Metal binding 148 148 . . . Note=Zinc 2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824 +P04050 UniProtKB Metal binding 167 167 . . . Note=Zinc 2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824 +P04050 UniProtKB Metal binding 481 481 . . . Note=Magnesium 1%3B catalytic;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824 +P04050 UniProtKB Metal binding 481 481 . . . Note=Magnesium 2%3B shared with RPB2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824 +P04050 UniProtKB Metal binding 483 483 . . . Note=Magnesium 1%3B catalytic;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824 +P04050 UniProtKB Metal binding 483 483 . . . Note=Magnesium 2%3B shared with RPB2;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824 +P04050 UniProtKB Metal binding 485 485 . . . Note=Magnesium 1%3B catalytic;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:4BBR,ECO:0000244|PDB:4V1M,ECO:0000269|PubMed:23151482,ECO:0000269|PubMed:25652824;Dbxref=PMID:23151482,PMID:25652824 +P04050 UniProtKB Modified residue 1471 1471 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P04050 UniProtKB Cross-link 695 695 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P04050 UniProtKB Cross-link 1246 1246 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P04050 UniProtKB Cross-link 1350 1350 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P04050 UniProtKB Natural variant 1653 1659 . . . Note=In strain: A364A. Missing +P04050 UniProtKB Sequence conflict 1514 1514 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04050 UniProtKB Sequence conflict 1524 1524 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04050 UniProtKB Sequence conflict 1601 1601 . . . Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04050 UniProtKB Beta strand 16 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 24 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BXX +P04050 UniProtKB Beta strand 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NVT +P04050 UniProtKB Beta strand 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWC +P04050 UniProtKB Beta strand 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14 +P04050 UniProtKB Beta strand 51 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ +P04050 UniProtKB Beta strand 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Turn 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50 +P04050 UniProtKB Beta strand 84 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 96 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Turn 108 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50 +P04050 UniProtKB Beta strand 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NVQ +P04050 UniProtKB Helix 120 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2I +P04050 UniProtKB Helix 131 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 160 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50 +P04050 UniProtKB Beta strand 173 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50 +P04050 UniProtKB Beta strand 181 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 187 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 198 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 204 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 212 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S2H +P04050 UniProtKB Helix 216 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Turn 226 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 231 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 235 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Turn 244 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 253 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 257 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P04050 UniProtKB Helix 261 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Turn 281 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ +P04050 UniProtKB Helix 286 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 307 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14 +P04050 UniProtKB Beta strand 313 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P04050 UniProtKB Beta strand 318 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14 +P04050 UniProtKB Helix 325 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50 +P04050 UniProtKB Turn 330 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 338 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 341 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Y7N +P04050 UniProtKB Beta strand 347 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 363 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 368 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 375 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Turn 382 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 385 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Turn 395 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 398 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 402 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 408 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14 +P04050 UniProtKB Beta strand 412 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Turn 415 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ +P04050 UniProtKB Turn 419 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 431 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 441 445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 452 454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 455 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 472 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 475 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 482 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 486 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 495 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 507 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 511 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Turn 514 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 518 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 525 535 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 536 538 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1N +P04050 UniProtKB Beta strand 540 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 543 552 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 553 555 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ +P04050 UniProtKB Beta strand 567 569 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 571 573 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 574 581 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 588 590 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 596 598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2I +P04050 UniProtKB Beta strand 600 602 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO2 +P04050 UniProtKB Beta strand 604 608 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 611 615 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 619 622 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 626 628 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50 +P04050 UniProtKB Helix 629 637 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 639 658 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 666 669 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 673 699 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 706 708 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50 +P04050 UniProtKB Helix 710 736 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 742 749 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 750 752 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K83 +P04050 UniProtKB Helix 755 762 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 770 774 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I3Q +P04050 UniProtKB Beta strand 778 781 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P04050 UniProtKB Beta strand 782 784 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Turn 794 798 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Turn 804 806 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 810 845 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 863 867 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 868 870 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 875 877 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 878 882 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 884 886 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 890 897 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 901 903 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YU9 +P04050 UniProtKB Turn 904 906 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Turn 910 912 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 913 915 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S15 +P04050 UniProtKB Helix 916 919 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 923 946 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Turn 947 949 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 953 958 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 960 970 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 975 977 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K83 +P04050 UniProtKB Helix 983 994 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1005 1013 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1016 1025 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1028 1033 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1039 1056 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1064 1076 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1079 1082 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1Q +P04050 UniProtKB Helix 1086 1088 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NVQ +P04050 UniProtKB Beta strand 1089 1091 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ +P04050 UniProtKB Beta strand 1092 1094 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1Q +P04050 UniProtKB Helix 1097 1104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Turn 1105 1107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1115 1120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1122 1126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1128 1138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1143 1145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1147 1154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1158 1160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1164 1166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1167 1171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1172 1174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50 +P04050 UniProtKB Beta strand 1179 1182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P04050 UniProtKB Beta strand 1190 1197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1199 1204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1209 1220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1221 1223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1224 1228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1233 1235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1237 1242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1258 1270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1272 1275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1282 1292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1296 1310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1313 1316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1317 1322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M3Y +P04050 UniProtKB Turn 1324 1326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1328 1330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50 +P04050 UniProtKB Helix 1332 1339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1341 1357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Turn 1358 1360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1365 1374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Turn 1375 1377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1378 1380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1384 1386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1388 1390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1392 1394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14 +P04050 UniProtKB Helix 1396 1399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14 +P04050 UniProtKB Turn 1400 1402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14 +P04050 UniProtKB Helix 1406 1415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1424 1429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1437 1439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Beta strand 1440 1445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P04050 UniProtKB Helix 1447 1450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P04050 UniProtKB Beta strand 1677 1680 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LO6 +##sequence-region P20433 1 221 +P20433 UniProtKB Chain 1 221 . . . ID=PRO_0000073984;Note=DNA-directed RNA polymerase II subunit RPB4 +P20433 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P20433 UniProtKB Modified residue 91 91 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P20433 UniProtKB Modified residue 92 92 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P20433 UniProtKB Beta strand 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO2 +P20433 UniProtKB Helix 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P20433 UniProtKB Beta strand 24 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P20433 UniProtKB Helix 31 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HOU +P20433 UniProtKB Beta strand 35 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P20433 UniProtKB Turn 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VUM +P20433 UniProtKB Beta strand 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P20433 UniProtKB Beta strand 47 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P20433 UniProtKB Helix 52 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P20433 UniProtKB Turn 73 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BXX +P20433 UniProtKB Helix 119 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P20433 UniProtKB Helix 139 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P20433 UniProtKB Helix 157 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P20433 UniProtKB Turn 169 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P20433 UniProtKB Helix 174 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P20433 UniProtKB Helix 188 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P20433 UniProtKB Helix 196 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P20433 UniProtKB Turn 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +P20433 UniProtKB Helix 204 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Y14 +##sequence-region Q02773 1 1202 +Q02773 UniProtKB Transit peptide 1 122 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1409716;Dbxref=PMID:1409716 +Q02773 UniProtKB Chain 123 1202 . . . ID=PRO_0000022247;Note=Ribonuclease P protein component%2C mitochondrial +##sequence-region Q04847 1 553 +Q04847 UniProtKB Chain 1 553 . . . ID=PRO_0000203342;Note=Non-SCF-type F-box protein ROY1 +Q04847 UniProtKB Domain 3 49 . . . Note=F-box +##sequence-region P50106 1 137 +P50106 UniProtKB Chain 1 137 . . . ID=PRO_0000073962;Note=DNA-directed RNA polymerase I subunit RPA14 +P50106 UniProtKB Modified residue 121 121 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P50106 UniProtKB Turn 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P50106 UniProtKB Beta strand 20 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P50106 UniProtKB Helix 33 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P50106 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RF4 +P50106 UniProtKB Helix 81 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +##sequence-region P04051 1 1460 +P04051 UniProtKB Chain 1 1460 . . . ID=PRO_0000073953;Note=DNA-directed RNA polymerase III subunit RPC1 +P04051 UniProtKB Region 858 870 . . . Note=Bridging helix;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04051 UniProtKB Metal binding 67 67 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04051 UniProtKB Metal binding 70 70 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04051 UniProtKB Metal binding 77 77 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04051 UniProtKB Metal binding 80 80 . . . Note=Zinc 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04051 UniProtKB Metal binding 107 107 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04051 UniProtKB Metal binding 110 110 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04051 UniProtKB Metal binding 154 154 . . . Note=Zinc 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04051 UniProtKB Metal binding 511 511 . . . Note=Magnesium%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04051 UniProtKB Metal binding 513 513 . . . Note=Magnesium%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04051 UniProtKB Metal binding 515 515 . . . Note=Magnesium%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04051 UniProtKB Mutagenesis 506 506 . . . Note=Temperature-sensitive. T->I +P04051 UniProtKB Mutagenesis 509 509 . . . Note=Temperature-sensitive. N->Y +P04051 UniProtKB Mutagenesis 518 518 . . . Note=Temperature-sensitive. N->Q +##sequence-region P32349 1 654 +P32349 UniProtKB Chain 1 654 . . . ID=PRO_0000073966;Note=DNA-directed RNA polymerase III subunit RPC3 +P32349 UniProtKB Region 581 602 . . . Note=Leucine-zipper +P32349 UniProtKB Modified residue 27 27 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32349 UniProtKB Modified residue 392 392 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32349 UniProtKB Modified residue 394 394 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32349 UniProtKB Sequence conflict 637 637 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P17890 1 251 +P17890 UniProtKB Chain 1 251 . . . ID=PRO_0000073980;Note=DNA-directed RNA polymerase III subunit RPC7 +P17890 UniProtKB Compositional bias 202 248 . . . Note=Asp/Glu-rich (acidic) +P17890 UniProtKB Modified residue 189 189 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P17890 UniProtKB Sequence conflict 12 12 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P17890 UniProtKB Sequence conflict 205 205 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P35718 1 212 +P35718 UniProtKB Chain 1 212 . . . ID=PRO_0000073996;Note=DNA-directed RNA polymerase III subunit RPC8 +P35718 UniProtKB Modified residue 162 162 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P35718 UniProtKB Beta strand 2 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P35718 UniProtKB Helix 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P35718 UniProtKB Helix 22 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P35718 UniProtKB Beta strand 37 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P35718 UniProtKB Turn 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P35718 UniProtKB Beta strand 43 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P35718 UniProtKB Beta strand 61 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P35718 UniProtKB Beta strand 66 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P35718 UniProtKB Beta strand 84 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P35718 UniProtKB Beta strand 96 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P35718 UniProtKB Beta strand 108 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P35718 UniProtKB Turn 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P35718 UniProtKB Beta strand 120 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P35718 UniProtKB Turn 123 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P35718 UniProtKB Beta strand 127 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P35718 UniProtKB Beta strand 137 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P35718 UniProtKB Beta strand 145 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P35718 UniProtKB Beta strand 193 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +P35718 UniProtKB Helix 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CKZ +##sequence-region P46969 1 238 +P46969 UniProtKB Chain 1 238 . . . ID=PRO_0000171595;Note=Ribulose-phosphate 3-epimerase +P46969 UniProtKB Region 156 159 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46969 UniProtKB Region 207 208 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46969 UniProtKB Active site 36 36 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46969 UniProtKB Active site 185 185 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46969 UniProtKB Metal binding 34 34 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46969 UniProtKB Metal binding 36 36 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46969 UniProtKB Metal binding 80 80 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46969 UniProtKB Metal binding 185 185 . . . Note=Divalent metal cation;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46969 UniProtKB Binding site 9 9 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46969 UniProtKB Binding site 80 80 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46969 UniProtKB Binding site 187 187 . . . Note=Substrate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q03465 1 531 +Q03465 UniProtKB Chain 1 531 . . . ID=PRO_0000173871;Note=Protein RPN4 +Q03465 UniProtKB Motif 382 398 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03465 UniProtKB Compositional bias 211 229 . . . Note=Asp/Glu-rich (acidic) +Q03465 UniProtKB Compositional bias 300 315 . . . Note=Asp/Glu-rich (acidic) +Q03465 UniProtKB Sequence conflict 231 231 . . . Note=C->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12377 1 434 +Q12377 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:12504901;Dbxref=PMID:22814378,PMID:12504901 +Q12377 UniProtKB Chain 2 434 . . . ID=PRO_0000173860;Note=26S proteasome regulatory subunit RPN6 +Q12377 UniProtKB Domain 229 401 . . . Note=PCI +Q12377 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:12504901;Dbxref=PMID:22814378,PMID:12504901 +Q12377 UniProtKB Mutagenesis 132 132 . . . Note=In rpn6-2%3B temperature-sensitive mutant that shows defects in proteasome assembly when incubated at 37 degrees Celsius%3B when associated with P-377. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611133;Dbxref=PMID:15611133 +Q12377 UniProtKB Mutagenesis 377 377 . . . Note=In rpn6-2%3B temperature-sensitive mutant that shows defects in proteasome assembly when incubated at 37 degrees Celsius%3B when associated with L-132. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15611133;Dbxref=PMID:15611133 +Q12377 UniProtKB Helix 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 59 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Turn 65 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 71 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Turn 84 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 94 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Beta strand 106 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 112 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 131 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Turn 145 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 152 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 171 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 192 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 212 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 232 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 254 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 276 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Turn 284 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 288 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 294 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 311 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Turn 317 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 322 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 329 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Beta strand 354 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 359 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 370 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Beta strand 388 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Turn 392 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Beta strand 396 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q12377 UniProtKB Helix 407 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +##sequence-region Q06506 1 573 +Q06506 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q06506 UniProtKB Chain 2 573 . . . ID=PRO_0000269482;Note=Ribosomal RNA-processing protein 9 +Q06506 UniProtKB Repeat 234 273 . . . Note=WD 1 +Q06506 UniProtKB Repeat 278 317 . . . Note=WD 2 +Q06506 UniProtKB Repeat 320 359 . . . Note=WD 3 +Q06506 UniProtKB Repeat 397 435 . . . Note=WD 4 +Q06506 UniProtKB Repeat 471 509 . . . Note=WD 5 +Q06506 UniProtKB Repeat 516 562 . . . Note=WD 6 +Q06506 UniProtKB Coiled coil 32 106 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06506 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q06506 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06506 UniProtKB Turn 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 141 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 157 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 186 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 194 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 209 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Helix 218 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 239 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 248 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 258 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Turn 265 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 269 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 283 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 292 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 302 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Turn 309 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 313 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 327 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 332 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 345 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Turn 351 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 355 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Helix 365 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 402 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 412 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 422 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 433 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Turn 437 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 477 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 484 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 492 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 496 501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 508 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 519 528 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 537 546 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +Q06506 UniProtKB Beta strand 562 569 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4J0X +##sequence-region P40042 1 185 +P40042 UniProtKB Chain 1 185 . . . ID=PRO_0000051472;Note=Regulator of rDNA transcription protein 13 +P40042 UniProtKB Repeat 9 48 . . . Note=WD 1 +P40042 UniProtKB Repeat 71 108 . . . Note=WD 2 +P40042 UniProtKB Repeat 111 148 . . . Note=WD 3 +##sequence-region Q07829 1 113 +Q07829 UniProtKB Chain 1 113 . . . ID=PRO_0000299603;Note=Regulator of rDNA transcription protein 7 +Q07829 UniProtKB Transmembrane 13 35 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07829 UniProtKB Transmembrane 70 92 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07829 UniProtKB Sequence conflict 10 10 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08745 1 105 +Q08745 UniProtKB Chain 1 105 . . . ID=PRO_0000116376;Note=40S ribosomal protein S10-A +Q08745 UniProtKB Helix 5 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q08745 UniProtKB Beta strand 19 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q08745 UniProtKB Beta strand 33 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q08745 UniProtKB Helix 39 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q08745 UniProtKB Beta strand 53 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q08745 UniProtKB Turn 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q08745 UniProtKB Beta strand 63 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q08745 UniProtKB Helix 70 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q08745 UniProtKB Helix 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +Q08745 UniProtKB Turn 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U52 +##sequence-region P46784 1 105 +P46784 UniProtKB Chain 1 105 . . . ID=PRO_0000116377;Note=40S ribosomal protein S10-B +P46784 UniProtKB Helix 5 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M +P46784 UniProtKB Beta strand 19 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M +P46784 UniProtKB Beta strand 33 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M +P46784 UniProtKB Helix 39 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M +P46784 UniProtKB Beta strand 54 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M +P46784 UniProtKB Beta strand 65 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M +P46784 UniProtKB Helix 70 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M +##sequence-region P0CX48 1 156 +P0CX48 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:1544921 +P0CX48 UniProtKB Chain 2 156 . . . ID=PRO_0000409770;Note=40S ribosomal protein S11-B +P0CX48 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:1544921 +P0CX48 UniProtKB Cross-link 15 15 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX48 UniProtKB Cross-link 46 46 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX48 UniProtKB Cross-link 56 56 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX48 UniProtKB Cross-link 57 57 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX48 UniProtKB Cross-link 79 79 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX48 UniProtKB Cross-link 96 96 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX48 UniProtKB Cross-link 105 105 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX48 UniProtKB Cross-link 133 133 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX48 UniProtKB Cross-link 141 141 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX48 UniProtKB Cross-link 148 148 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX48 UniProtKB Sequence conflict 12 13 . . . Note=AF->FA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40693 1 322 +P40693 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40693 UniProtKB Chain 2 322 . . . ID=PRO_0000104658;Note=Ribosome biogenesis protein RLP7 +P40693 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40693 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40693 UniProtKB Modified residue 120 120 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40693 UniProtKB Modified residue 278 278 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +##sequence-region Q04599 1 285 +##sequence-region P32904 1 214 +P32904 UniProtKB Transit peptide 1 16 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9151978;Dbxref=PMID:9151978 +P32904 UniProtKB Chain 17 214 . . . ID=PRO_0000030546;Note=54S ribosomal protein L6%2C mitochondrial +P32904 UniProtKB Sequence conflict 19 19 . . . Note=V->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32904 UniProtKB Sequence conflict 27 27 . . . Note=S->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32904 UniProtKB Sequence conflict 201 214 . . . Note=VNDETIKLKDKKIK->GTVKQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P31334 1 269 +P31334 UniProtKB Transit peptide 1 19 . . . Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1597181,ECO:0000269|PubMed:3060376;Dbxref=PMID:1597181,PMID:3060376 +P31334 UniProtKB Chain 20 269 . . . ID=PRO_0000030536;Note=54S ribosomal protein L9%2C mitochondrial +P31334 UniProtKB Sequence conflict 21 21 . . . Note=S->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P31334 UniProtKB Sequence conflict 139 139 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36521 1 249 +P36521 UniProtKB Transit peptide 1 31 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626 +P36521 UniProtKB Chain 32 249 . . . ID=PRO_0000030440;Note=54S ribosomal protein L11%2C mitochondrial +P36521 UniProtKB Sequence conflict 35 35 . . . Note=S->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36521 UniProtKB Sequence conflict 42 42 . . . Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36521 UniProtKB Sequence conflict 48 48 . . . Note=S->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36521 UniProtKB Sequence conflict 51 51 . . . Note=T->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36521 UniProtKB Sequence conflict 56 56 . . . Note=T->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36521 UniProtKB Sequence conflict 60 60 . . . Note=L->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53875 1 158 +P53875 UniProtKB Transit peptide 1 73 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9151978;Dbxref=PMID:9151978 +P53875 UniProtKB Chain 74 158 . . . ID=PRO_0000030447;Note=54S ribosomal protein L19%2C mitochondrial +##sequence-region P36525 1 258 +P36525 UniProtKB Transit peptide 1 21 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2060626;Dbxref=PMID:2060626 +P36525 UniProtKB Chain 22 258 . . . ID=PRO_0000030509;Note=54S ribosomal protein L24%2C mitochondrial +P36525 UniProtKB Sequence conflict 72 72 . . . Note=G->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36525 UniProtKB Sequence conflict 76 76 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P36525 UniProtKB Sequence conflict 130 130 . . . Note=G->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06678 1 367 +Q06678 UniProtKB Transit peptide 1 29 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06678 UniProtKB Chain 30 367 . . . ID=PRO_0000023284;Note=54S ribosomal protein L35%2C mitochondrial +Q06678 UniProtKB Sequence conflict 113 113 . . . Note=P->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P19956 1 98 +P19956 UniProtKB Chain 1 98 . . . ID=PRO_0000087696;Note=54S ribosomal protein L44%2C mitochondrial +##sequence-region P40858 1 161 +P40858 UniProtKB Transit peptide 1 35 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40858 UniProtKB Chain 36 161 . . . ID=PRO_0000030483;Note=54S ribosomal protein L49%2C mitochondrial +P40858 UniProtKB Sequence conflict 115 115 . . . Note=T->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25298 1 677 +P25298 UniProtKB Chain 1 677 . . . ID=PRO_0000205761;Note=mRNA 3'-end-processing protein RNA14 +P25298 UniProtKB Repeat 56 88 . . . Note=HAT 1 +P25298 UniProtKB Repeat 90 124 . . . Note=HAT 2 +P25298 UniProtKB Repeat 138 170 . . . Note=HAT 3 +P25298 UniProtKB Repeat 181 214 . . . Note=HAT 4 +P25298 UniProtKB Repeat 257 289 . . . Note=HAT 5 +P25298 UniProtKB Repeat 298 330 . . . Note=HAT 6 +P25298 UniProtKB Helix 633 641 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B +P25298 UniProtKB Helix 645 648 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B +P25298 UniProtKB Helix 655 664 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L9B +##sequence-region Q02805 1 837 +Q02805 UniProtKB Chain 1 837 . . . ID=PRO_0000097396;Note=Protein ROD1 +Q02805 UniProtKB Motif 487 490 . . . Note=PY-motif +Q02805 UniProtKB Motif 656 659 . . . Note=PY-motif +Q02805 UniProtKB Compositional bias 3 6 . . . Note=Poly-Ser +Q02805 UniProtKB Compositional bias 524 601 . . . Note=Asn-rich +Q02805 UniProtKB Compositional bias 684 815 . . . Note=Ser-rich +Q02805 UniProtKB Modified residue 138 138 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02805 UniProtKB Modified residue 141 141 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q02805 UniProtKB Modified residue 436 436 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q02805 UniProtKB Modified residue 536 536 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q02805 UniProtKB Modified residue 720 720 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q02805 UniProtKB Modified residue 725 725 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02805 UniProtKB Cross-link 401 401 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q02805 UniProtKB Mutagenesis 487 488 . . . Note=Reduced binding to RSP5. PP->QA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12163175;Dbxref=PMID:12163175 +Q02805 UniProtKB Mutagenesis 656 657 . . . Note=Reduced binding to RSP5. PP->QA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12163175;Dbxref=PMID:12163175 +Q02805 UniProtKB Sequence conflict 618 618 . . . Note=Y->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P43602 1 733 +P43602 UniProtKB Chain 1 733 . . . ID=PRO_0000202690;Note=Protein ROG3 +P43602 UniProtKB Motif 460 463 . . . Note=PY-motif +P43602 UniProtKB Motif 625 628 . . . Note=PY-motif +P43602 UniProtKB Compositional bias 641 710 . . . Note=Ser-rich +P43602 UniProtKB Mutagenesis 460 461 . . . Note=Reduced binding to RSP5. PP->QA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12163175;Dbxref=PMID:12163175 +P43602 UniProtKB Mutagenesis 625 626 . . . Note=Reduced binding to RSP5. PP->QA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12163175;Dbxref=PMID:12163175 +##sequence-region P53046 1 1155 +P53046 UniProtKB Chain 1 1155 . . . ID=PRO_0000080968;Note=RHO1 GDP-GTP exchange protein 1 +P53046 UniProtKB Domain 464 651 . . . Note=DH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00062 +P53046 UniProtKB Domain 842 1137 . . . Note=CNH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00795 +P53046 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53046 UniProtKB Modified residue 154 154 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53046 UniProtKB Modified residue 155 155 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53046 UniProtKB Modified residue 180 180 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53046 UniProtKB Modified residue 433 433 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53046 UniProtKB Sequence conflict 214 214 . . . Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53046 UniProtKB Sequence conflict 214 214 . . . Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53046 UniProtKB Sequence conflict 250 250 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53046 UniProtKB Sequence conflict 279 281 . . . Note=KLS->QLG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53046 UniProtKB Sequence conflict 385 385 . . . Note=Y->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53046 UniProtKB Sequence conflict 515 515 . . . Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53046 UniProtKB Sequence conflict 557 557 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53046 UniProtKB Sequence conflict 844 844 . . . Note=R->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53046 UniProtKB Sequence conflict 852 852 . . . Note=H->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53046 UniProtKB Sequence conflict 897 897 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53046 UniProtKB Sequence conflict 959 959 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53046 UniProtKB Sequence conflict 960 960 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53046 UniProtKB Sequence conflict 961 961 . . . Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53046 UniProtKB Sequence conflict 1037 1037 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53046 UniProtKB Sequence conflict 1151 1151 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03691 1 256 +Q03691 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03691 UniProtKB Chain 25 256 . . . ID=PRO_0000203327;Note=Protein ROT1 +Q03691 UniProtKB Topological domain 25 235 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03691 UniProtKB Transmembrane 236 256 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03691 UniProtKB Glycosylation 103 103 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17914748;Dbxref=PMID:17914748 +Q03691 UniProtKB Glycosylation 107 107 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17914748;Dbxref=PMID:17914748 +Q03691 UniProtKB Glycosylation 139 139 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17914748;Dbxref=PMID:17914748 +##sequence-region P47006 1 233 +P47006 UniProtKB Chain 1 233 . . . ID=PRO_0000203031;Note=DNA-directed RNA polymerase I subunit RPA34 +P47006 UniProtKB Compositional bias 184 233 . . . Note=Glu/Lys-rich +P47006 UniProtKB Compositional bias 208 215 . . . Note=Poly-Lys +P47006 UniProtKB Compositional bias 221 230 . . . Note=Poly-Lys +P47006 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P47006 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P47006 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P47006 UniProtKB Modified residue 60 60 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47006 UniProtKB Beta strand 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P47006 UniProtKB Beta strand 52 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P47006 UniProtKB Turn 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P47006 UniProtKB Beta strand 68 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P47006 UniProtKB Beta strand 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P47006 UniProtKB Beta strand 79 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P47006 UniProtKB Beta strand 85 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P47006 UniProtKB Helix 93 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P47006 UniProtKB Beta strand 99 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P47006 UniProtKB Beta strand 106 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P47006 UniProtKB Beta strand 116 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P47006 UniProtKB Beta strand 125 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P47006 UniProtKB Beta strand 134 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P47006 UniProtKB Helix 150 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P47006 UniProtKB Helix 177 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +##sequence-region P46669 1 326 +P46669 UniProtKB Chain 1 326 . . . ID=PRO_0000073960;Note=DNA-directed RNA polymerase I subunit RPA43 +P46669 UniProtKB Modified residue 244 244 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P46669 UniProtKB Modified residue 251 251 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P46669 UniProtKB Modified residue 265 265 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P46669 UniProtKB Modified residue 269 269 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P46669 UniProtKB Modified residue 285 285 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +P46669 UniProtKB Sequence conflict 318 318 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46669 UniProtKB Helix 11 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P46669 UniProtKB Beta strand 30 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Beta strand 38 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Helix 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Beta strand 54 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P46669 UniProtKB Helix 57 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Helix 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Beta strand 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Turn 75 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Beta strand 79 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Beta strand 103 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Beta strand 109 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Beta strand 114 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Beta strand 132 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Beta strand 142 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Turn 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Beta strand 153 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Turn 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Beta strand 167 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Beta strand 216 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Beta strand 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P46669 UniProtKB Beta strand 227 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Beta strand 239 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Beta strand 244 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Beta strand 264 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P46669 UniProtKB Turn 267 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P46669 UniProtKB Helix 273 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P46669 UniProtKB Beta strand 307 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +##sequence-region P20434 1 215 +P20434 UniProtKB Chain 1 215 . . . ID=PRO_0000146086;Note=DNA-directed RNA polymerases I%2C II%2C and III subunit RPABC1 +P20434 UniProtKB Sequence conflict 37 37 . . . Note=L->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20434 UniProtKB Turn 3 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWC +P20434 UniProtKB Helix 7 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Helix 32 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Helix 39 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NVQ +P20434 UniProtKB Helix 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Beta strand 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Helix 66 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Beta strand 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NVY +P20434 UniProtKB Beta strand 78 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Beta strand 84 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Helix 90 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Beta strand 106 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Helix 118 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Turn 122 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Beta strand 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1M +P20434 UniProtKB Beta strand 131 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Helix 137 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Helix 144 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Beta strand 147 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3RZD +P20434 UniProtKB Beta strand 152 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Helix 158 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Helix 172 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Beta strand 177 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P20434 UniProtKB Beta strand 180 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2I +P20434 UniProtKB Helix 183 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Beta strand 195 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Beta strand 204 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +P20434 UniProtKB Beta strand 210 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1DZF +##sequence-region P20436 1 146 +P20436 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P20436 UniProtKB Chain 2 146 . . . ID=PRO_0000074001;Note=DNA-directed RNA polymerases I%2C II%2C and III subunit RPABC3 +P20436 UniProtKB Region 16 39 . . . Note=Non-specific ssDNA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20436 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P20436 UniProtKB Modified residue 68 68 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P20436 UniProtKB Beta strand 7 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P20436 UniProtKB Beta strand 21 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P20436 UniProtKB Beta strand 37 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P20436 UniProtKB Helix 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P20436 UniProtKB Beta strand 54 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P20436 UniProtKB Turn 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P20436 UniProtKB Helix 89 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C2M +P20436 UniProtKB Beta strand 93 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P20436 UniProtKB Beta strand 108 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C3I +P20436 UniProtKB Beta strand 112 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P20436 UniProtKB Beta strand 121 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P20436 UniProtKB Turn 129 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P20436 UniProtKB Beta strand 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P20436 UniProtKB Beta strand 140 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +##sequence-region P22139 1 70 +P22139 UniProtKB Chain 1 70 . . . ID=PRO_0000121342;Note=DNA-directed RNA polymerases I%2C II%2C and III subunit RPABC5 +P22139 UniProtKB Metal binding 7 7 . . . Note=Zinc +P22139 UniProtKB Metal binding 10 10 . . . Note=Zinc +P22139 UniProtKB Metal binding 44 44 . . . Note=Zinc +P22139 UniProtKB Metal binding 45 45 . . . Note=Zinc +P22139 UniProtKB Cross-link 59 59 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P22139 UniProtKB Turn 8 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P22139 UniProtKB Helix 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3M3Y +P22139 UniProtKB Helix 18 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P22139 UniProtKB Turn 27 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I6H +P22139 UniProtKB Helix 32 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P22139 UniProtKB Helix 44 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P22139 UniProtKB Helix 57 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +##sequence-region Q04307 1 110 +Q04307 UniProtKB Chain 1 110 . . . ID=PRO_0000121478;Note=DNA-directed RNA polymerase III subunit RPC10 +Q04307 UniProtKB Zinc finger 5 29 . . . Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04307 UniProtKB Zinc finger 65 108 . . . Note=TFIIS-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00472 +##sequence-region P25441 1 422 +P25441 UniProtKB Chain 1 422 . . . ID=PRO_0000073969;Note=DNA-directed RNA polymerase III subunit RPC4 +P25441 UniProtKB Motif 25 29 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25441 UniProtKB Modified residue 137 137 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P25441 UniProtKB Modified residue 138 138 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P25441 UniProtKB Modified residue 178 178 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P25441 UniProtKB Modified residue 182 182 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P25441 UniProtKB Modified residue 224 224 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956 +P25441 UniProtKB Modified residue 228 228 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950 +P25441 UniProtKB Modified residue 232 232 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950 +P25441 UniProtKB Sequence conflict 42 42 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25441 UniProtKB Sequence conflict 264 264 . . . Note=L->LGL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25441 UniProtKB Sequence conflict 284 285 . . . Note=NA->KR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25441 UniProtKB Sequence conflict 392 392 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12167 1 365 +Q12167 UniProtKB Chain 1 365 . . . ID=PRO_0000244438;Note=Required for respiratory growth protein 1%2C mitochondrial +Q12167 UniProtKB Sequence conflict 364 364 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12754 1 1228 +Q12754 UniProtKB Chain 1 1228 . . . ID=PRO_0000270563;Note=Ribosomal RNA-processing protein 12 +Q12754 UniProtKB Modified residue 1059 1059 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12754 UniProtKB Modified residue 1067 1067 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region Q06511 1 250 +Q06511 UniProtKB Chain 1 250 . . . ID=PRO_0000270562;Note=Ribosomal RNA-processing protein 15 +Q06511 UniProtKB Compositional bias 77 80 . . . Note=Poly-Glu;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06511 UniProtKB Modified residue 69 69 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P32786 1 894 +P32786 UniProtKB Chain 1 894 . . . ID=PRO_0000097448;Note=RNA polymerase I-specific transcription initiation factor RRN6 +P32786 UniProtKB Compositional bias 882 888 . . . Note=Lys-rich (basic) +P32786 UniProtKB Sequence conflict 39 39 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32786 UniProtKB Sequence conflict 39 39 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32786 UniProtKB Sequence conflict 663 663 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32786 UniProtKB Helix 23 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 61 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 184 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61 +P32786 UniProtKB Beta strand 193 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 207 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 216 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 220 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 229 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 246 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 265 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 272 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 284 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 295 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 300 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 315 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 323 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 344 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 361 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 372 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 379 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Turn 385 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 389 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 397 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 404 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Turn 409 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61 +P32786 UniProtKB Beta strand 414 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 422 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 428 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 439 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61 +P32786 UniProtKB Beta strand 450 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 462 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 476 482 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Turn 485 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 488 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61 +P32786 UniProtKB Beta strand 495 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 500 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61 +P32786 UniProtKB Beta strand 505 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 535 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 546 552 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Helix 572 578 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Helix 583 585 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Helix 587 612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Turn 613 615 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61 +P32786 UniProtKB Helix 617 643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Helix 645 647 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 657 659 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Helix 664 667 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Helix 672 685 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 688 691 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Helix 697 704 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Helix 711 723 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Beta strand 725 727 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61 +P32786 UniProtKB Helix 729 744 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Turn 752 754 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Helix 755 765 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P32786 UniProtKB Helix 768 773 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +##sequence-region P25359 1 394 +P25359 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P25359 UniProtKB Chain 2 394 . . . ID=PRO_0000139970;Note=Exosome complex component RRP43 +P25359 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P25359 UniProtKB Modified residue 26 26 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25359 UniProtKB Mutagenesis 162 162 . . . Note=Interaction with RRP46 abolished%3B when associated with T-246. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12364597;Dbxref=PMID:12364597 +P25359 UniProtKB Mutagenesis 212 212 . . . Note=Interaction with RRP46 abolished. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12364597;Dbxref=PMID:12364597 +P25359 UniProtKB Mutagenesis 230 230 . . . Note=Interaction with RRP46 abolished%3B when associated with T-274 and Y-276. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12364597;Dbxref=PMID:12364597 +P25359 UniProtKB Mutagenesis 246 246 . . . Note=Interaction with RRP46 abolished%3B when associated with F-162. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12364597;Dbxref=PMID:12364597 +P25359 UniProtKB Mutagenesis 274 274 . . . Note=Interaction with RRP46 abolished%3B when associated with Y-230 and Y-276. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12364597;Dbxref=PMID:12364597 +P25359 UniProtKB Mutagenesis 276 276 . . . Note=Interaction with RRP46 abolished%3B when associated with Y-230 and T-274. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12364597;Dbxref=PMID:12364597 +P25359 UniProtKB Sequence conflict 102 102 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25359 UniProtKB Sequence conflict 363 363 . . . Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25359 UniProtKB Beta strand 10 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +P25359 UniProtKB Helix 19 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Helix 27 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Turn 36 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Beta strand 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +P25359 UniProtKB Beta strand 52 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Helix 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OO1 +P25359 UniProtKB Beta strand 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Beta strand 75 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Beta strand 85 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Helix 103 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36 +P25359 UniProtKB Helix 109 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36 +P25359 UniProtKB Helix 124 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Beta strand 131 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Helix 146 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Helix 167 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Beta strand 175 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Turn 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Beta strand 184 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Beta strand 209 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Helix 227 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Beta strand 242 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Beta strand 257 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +P25359 UniProtKB Beta strand 265 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +P25359 UniProtKB Beta strand 275 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Helix 288 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Beta strand 293 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Helix 304 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Helix 322 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36 +P25359 UniProtKB Beta strand 327 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Helix 338 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Beta strand 345 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Turn 353 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36 +P25359 UniProtKB Beta strand 357 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P25359 UniProtKB Helix 371 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +##sequence-region P50943 1 142 +P50943 UniProtKB Chain 1 142 . . . ID=PRO_0000203437;Note=Putative regulator of rDNA transcription protein 16 +P50943 UniProtKB Transmembrane 19 39 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50943 UniProtKB Transmembrane 84 104 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50943 UniProtKB Transmembrane 111 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53117 1 311 +P53117 UniProtKB Chain 1 311 . . . ID=PRO_0000202734;Note=Regulator of rDNA transcription protein 6 +P53117 UniProtKB Transmembrane 32 52 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53117 UniProtKB Transmembrane 271 291 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q01855 1 142 +Q01855 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260 +Q01855 UniProtKB Chain 2 142 . . . ID=PRO_0000130051;Note=40S ribosomal protein S15 +Q01855 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260 +Q01855 UniProtKB Cross-link 24 24 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q01855 UniProtKB Cross-link 35 35 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q01855 UniProtKB Cross-link 64 64 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q01855 UniProtKB Beta strand 16 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q01855 UniProtKB Helix 22 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q01855 UniProtKB Helix 30 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q01855 UniProtKB Helix 39 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q01855 UniProtKB Beta strand 50 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q01855 UniProtKB Helix 54 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q01855 UniProtKB Beta strand 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q01855 UniProtKB Beta strand 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q01855 UniProtKB Beta strand 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q01855 UniProtKB Helix 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q01855 UniProtKB Beta strand 93 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q01855 UniProtKB Helix 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q01855 UniProtKB Helix 116 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q01855 UniProtKB Beta strand 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U6F +##sequence-region P38701 1 121 +P38701 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|Ref.4;Dbxref=PMID:22814378,PMID:10601260 +P38701 UniProtKB Chain 2 121 . . . ID=PRO_0000146692;Note=40S ribosomal protein S20 +P38701 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|Ref.4;Dbxref=PMID:22814378,PMID:10601260 +P38701 UniProtKB Cross-link 6 6 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38701 UniProtKB Cross-link 8 8 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38701 UniProtKB Cross-link 21 21 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38701 UniProtKB Cross-link 32 32 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38701 UniProtKB Cross-link 101 101 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38701 UniProtKB Beta strand 22 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P38701 UniProtKB Helix 31 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P38701 UniProtKB Turn 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4N +P38701 UniProtKB Beta strand 51 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P38701 UniProtKB Beta strand 61 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P38701 UniProtKB Beta strand 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P38701 UniProtKB Beta strand 79 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P38701 UniProtKB Helix 97 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P38701 UniProtKB Beta strand 112 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P0C0V8 1 87 +P0C0V8 UniProtKB Chain 1 87 . . . ID=PRO_0000194761;Note=40S ribosomal protein S21-A +P0C0V8 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P0C0V8 UniProtKB Beta strand 4 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P0C0V8 UniProtKB Turn 18 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0V8 UniProtKB Beta strand 32 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0V8 UniProtKB Beta strand 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0V8 UniProtKB Beta strand 50 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0V8 UniProtKB Helix 57 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0V8 UniProtKB Turn 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P0C0V8 UniProtKB Helix 65 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0V8 UniProtKB Turn 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0V8 UniProtKB Beta strand 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P08518 1 1224 +P08518 UniProtKB Chain 1 1224 . . . ID=PRO_0000048091;Note=DNA-directed RNA polymerase II subunit RPB2 +P08518 UniProtKB Zinc finger 1163 1185 . . . Note=C4-type +P08518 UniProtKB Region 467 478 . . . Note=Fork loop 1 +P08518 UniProtKB Metal binding 837 837 . . . Note=Magnesium%3B shared with RPB1 +P08518 UniProtKB Metal binding 1163 1163 . . . Note=Zinc +P08518 UniProtKB Metal binding 1166 1166 . . . Note=Zinc +P08518 UniProtKB Metal binding 1182 1182 . . . Note=Zinc +P08518 UniProtKB Metal binding 1185 1185 . . . Note=Zinc +P08518 UniProtKB Modified residue 919 919 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P08518 UniProtKB Sequence conflict 1003 1006 . . . Note=AEGI->RRRY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08518 UniProtKB Beta strand 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1M +P08518 UniProtKB Helix 29 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 42 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I6H +P08518 UniProtKB Helix 45 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 58 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P08518 UniProtKB Beta strand 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GTJ +P08518 UniProtKB Beta strand 96 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14 +P08518 UniProtKB Helix 114 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 125 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 141 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E2I +P08518 UniProtKB Beta strand 166 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 176 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I3Q +P08518 UniProtKB Helix 180 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 186 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 202 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 208 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 214 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 224 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 232 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 245 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 253 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 264 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K83 +P08518 UniProtKB Beta strand 269 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 277 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2NVQ +P08518 UniProtKB Helix 282 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 294 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 308 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Turn 321 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 327 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 337 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P08518 UniProtKB Helix 342 344 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3GTJ +P08518 UniProtKB Helix 345 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 359 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWA +P08518 UniProtKB Turn 362 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 367 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 371 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 390 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3 +P08518 UniProtKB Helix 401 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 404 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 409 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Turn 434 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S2H +P08518 UniProtKB Helix 444 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P08518 UniProtKB Helix 451 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 467 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14 +P08518 UniProtKB Helix 474 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14 +P08518 UniProtKB Beta strand 477 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PO3 +P08518 UniProtKB Beta strand 480 482 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 488 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 497 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Turn 510 512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HOU +P08518 UniProtKB Helix 516 518 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Turn 519 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 530 532 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Turn 533 535 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K83 +P08518 UniProtKB Beta strand 536 539 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 552 560 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 563 565 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ +P08518 UniProtKB Helix 566 568 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 571 573 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 574 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P08518 UniProtKB Beta strand 578 582 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 585 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 593 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 607 609 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 614 618 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Turn 619 622 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 623 627 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 633 641 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 646 649 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50 +P08518 UniProtKB Beta strand 650 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 655 666 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 681 686 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 689 694 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 695 698 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 703 706 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 707 710 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 725 727 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1N +P08518 UniProtKB Beta strand 739 741 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14 +P08518 UniProtKB Helix 745 748 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 753 755 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 756 758 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 759 761 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 764 773 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 774 776 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 779 781 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2YU9 +P08518 UniProtKB Turn 783 787 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 791 798 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 803 805 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 809 812 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Turn 813 816 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 821 827 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 829 832 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Turn 833 837 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 838 842 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 843 847 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Turn 848 851 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 853 861 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 866 869 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWC +P08518 UniProtKB Beta strand 873 875 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 880 882 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 886 888 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BBR +P08518 UniProtKB Helix 890 892 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 895 899 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HOU +P08518 UniProtKB Beta strand 904 906 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQZ +P08518 UniProtKB Beta strand 910 912 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 914 916 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1K83 +P08518 UniProtKB Beta strand 935 940 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50 +P08518 UniProtKB Beta strand 947 956 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 958 960 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 962 972 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 979 981 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 983 985 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1I50 +P08518 UniProtKB Beta strand 987 994 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Turn 996 998 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 1009 1012 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 1014 1016 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Turn 1018 1021 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 1023 1038 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 1046 1049 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 1052 1060 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Turn 1061 1063 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 1068 1070 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 1071 1073 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1Q +P08518 UniProtKB Turn 1075 1077 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 1080 1084 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S1Q +P08518 UniProtKB Beta strand 1085 1097 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 1099 1101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 1104 1106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Turn 1113 1115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14 +P08518 UniProtKB Helix 1122 1124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14 +P08518 UniProtKB Beta strand 1128 1130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3S14 +P08518 UniProtKB Helix 1132 1141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 1144 1151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 1152 1156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BY7 +P08518 UniProtKB Beta strand 1159 1166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 1172 1174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Turn 1175 1178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 1179 1182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Turn 1183 1186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 1187 1195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Helix 1198 1209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +P08518 UniProtKB Beta strand 1215 1218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1TWF +##sequence-region P32561 1 433 +P32561 UniProtKB Chain 1 433 . . . ID=PRO_0000114724;Note=Histone deacetylase RPD3 +P32561 UniProtKB Region 19 331 . . . Note=Histone deacetylase +P32561 UniProtKB Motif 320 340 . . . Note=ESA1-RPD3 motif +P32561 UniProtKB Active site 151 151 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32561 UniProtKB Modified residue 394 394 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P32561 UniProtKB Modified residue 408 408 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32561 UniProtKB Mutagenesis 150 150 . . . Note=Impairs histone deacetylase activity and transcription repression. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9512514;Dbxref=PMID:9512514 +P32561 UniProtKB Mutagenesis 151 151 . . . Note=Impairs histone deacetylase activity and transcription repression. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9512514;Dbxref=PMID:9512514 +P32561 UniProtKB Mutagenesis 188 188 . . . Note=Impairs histone deacetylase activity and transcription repression. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9512514;Dbxref=PMID:9512514 +P32561 UniProtKB Mutagenesis 322 322 . . . Note=Reduces strongly HDAC activity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +P32561 UniProtKB Mutagenesis 325 325 . . . Note=Reduces strongly HDAC activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +P32561 UniProtKB Mutagenesis 327 327 . . . Note=Reduces strongly HDAC activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +P32561 UniProtKB Mutagenesis 328 328 . . . Note=Reduces strongly HDAC activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +P32561 UniProtKB Mutagenesis 329 329 . . . Note=Reduces strongly HDAC activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +P32561 UniProtKB Mutagenesis 332 332 . . . Note=Reduces strongly HDAC activity. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +P32561 UniProtKB Mutagenesis 334 334 . . . Note=Reduces strongly HDAC activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +P32561 UniProtKB Mutagenesis 335 335 . . . Note=Reduces strongly HDAC activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +P32561 UniProtKB Mutagenesis 338 338 . . . Note=Reduces strongly HDAC activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +P32561 UniProtKB Mutagenesis 339 339 . . . Note=Reduces strongly HDAC activity. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12110674;Dbxref=PMID:12110674 +##sequence-region P38805 1 295 +P38805 UniProtKB Chain 1 295 . . . ID=PRO_0000120255;Note=Ribosome production factor 1 +P38805 UniProtKB Domain 93 276 . . . Note=Brix;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00034 +P38805 UniProtKB Region 254 271 . . . Note=RNA-binding +##sequence-region P43588 1 306 +P43588 UniProtKB Chain 1 306 . . . ID=PRO_0000213960;Note=Ubiquitin carboxyl-terminal hydrolase RPN11 +P43588 UniProtKB Domain 27 162 . . . Note=MPN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182 +P43588 UniProtKB Motif 109 122 . . . Note=JAMM motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182 +P43588 UniProtKB Metal binding 109 109 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182 +P43588 UniProtKB Metal binding 111 111 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182 +P43588 UniProtKB Metal binding 122 122 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182 +P43588 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901 +P43588 UniProtKB Natural variant 208 208 . . . Note=In strain: NRRL Y-53. K->Q +P43588 UniProtKB Natural variant 239 239 . . . Note=In strain: NRRL Y-53. A->T +P43588 UniProtKB Natural variant 262 262 . . . Note=In strain: NRRL Y-53. T->S +P43588 UniProtKB Natural variant 280 281 . . . Note=In strain: NRRL Y-53. LS->IF +P43588 UniProtKB Mutagenesis 109 109 . . . Note=Stabilizes ubiquitin pathway substrates%3B when associated wirh Ala-111. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12183636;Dbxref=PMID:12183636 +P43588 UniProtKB Mutagenesis 111 111 . . . Note=Stabilizes ubiquitin pathway substrates%3B when associated wirh Ala-109. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12183636;Dbxref=PMID:12183636 +P43588 UniProtKB Beta strand 26 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +P43588 UniProtKB Helix 31 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +P43588 UniProtKB Beta strand 50 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +P43588 UniProtKB Beta strand 62 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +P43588 UniProtKB Helix 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +P43588 UniProtKB Helix 85 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +P43588 UniProtKB Turn 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +P43588 UniProtKB Beta strand 103 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +P43588 UniProtKB Beta strand 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OCM +P43588 UniProtKB Helix 120 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +P43588 UniProtKB Beta strand 137 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +P43588 UniProtKB Turn 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +P43588 UniProtKB Beta strand 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P43588 UniProtKB Beta strand 153 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +P43588 UniProtKB Helix 162 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OCM +P43588 UniProtKB Helix 182 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OCM +P43588 UniProtKB Beta strand 195 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +P43588 UniProtKB Beta strand 200 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +P43588 UniProtKB Helix 207 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +P43588 UniProtKB Turn 214 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +P43588 UniProtKB Turn 220 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P43588 UniProtKB Helix 230 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P43588 UniProtKB Helix 263 270 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P43588 UniProtKB Helix 276 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +##sequence-region P38764 1 993 +P38764 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901 +P38764 UniProtKB Chain 2 993 . . . ID=PRO_0000173815;Note=26S proteasome regulatory subunit RPN1 +P38764 UniProtKB Repeat 417 449 . . . Note=PC 1 +P38764 UniProtKB Repeat 450 487 . . . Note=PC 2 +P38764 UniProtKB Repeat 488 522 . . . Note=PC 3 +P38764 UniProtKB Repeat 523 563 . . . Note=PC 4 +P38764 UniProtKB Repeat 566 598 . . . Note=PC 5 +P38764 UniProtKB Repeat 778 809 . . . Note=PC 6 +P38764 UniProtKB Repeat 810 844 . . . Note=PC 7 +P38764 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38764 UniProtKB Modified residue 19 19 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38764 UniProtKB Modified residue 24 24 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38764 UniProtKB Modified residue 178 178 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38764 UniProtKB Modified residue 187 187 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38764 UniProtKB Modified residue 695 695 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38764 UniProtKB Helix 485 496 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T +P38764 UniProtKB Helix 497 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T +P38764 UniProtKB Helix 503 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T +P38764 UniProtKB Beta strand 516 518 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T +P38764 UniProtKB Helix 520 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T +P38764 UniProtKB Helix 540 552 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T +P38764 UniProtKB Helix 555 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T +P38764 UniProtKB Helix 562 572 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T +P38764 UniProtKB Turn 573 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T +P38764 UniProtKB Helix 579 590 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T +P38764 UniProtKB Turn 594 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3U +P38764 UniProtKB Helix 597 605 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3T +P38764 UniProtKB Turn 608 610 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2N3U +##sequence-region P40016 1 523 +P40016 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901 +P40016 UniProtKB Chain 2 523 . . . ID=PRO_0000173827;Note=26S proteasome regulatory subunit RPN3 +P40016 UniProtKB Domain 343 447 . . . Note=PCI +P40016 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901 +P40016 UniProtKB Modified residue 454 454 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40016 UniProtKB Sequence conflict 355 355 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40016 UniProtKB Sequence conflict 355 355 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40016 UniProtKB Helix 132 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Helix 153 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Helix 163 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Helix 175 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Helix 201 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Helix 227 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Helix 248 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Helix 266 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Helix 289 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Beta strand 303 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Helix 307 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Helix 330 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Beta strand 334 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Helix 337 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Helix 343 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Helix 357 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Helix 376 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Turn 381 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Helix 384 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Beta strand 400 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Helix 404 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Helix 416 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Beta strand 434 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Turn 438 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Beta strand 442 445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +P40016 UniProtKB Helix 456 477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +##sequence-region P13433 1 1351 +P13433 UniProtKB Active site 945 945 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13433 UniProtKB Active site 1014 1014 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13433 UniProtKB Active site 1189 1189 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13433 UniProtKB Sequence conflict 485 485 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13433 UniProtKB Sequence conflict 900 901 . . . Note=NP->KS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06109 1 277 +Q06109 UniProtKB Chain 1 277 . . . ID=PRO_0000242626;Note=Required for respiratory growth protein 8%2C mitochondrial +##sequence-region Q02983 1 363 +Q02983 UniProtKB Chain 1 363 . . . ID=PRO_0000097447;Note=RNA polymerase I-specific transcription initiation factor RRN5 +Q02983 UniProtKB Sequence conflict 25 25 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q02983 UniProtKB Sequence conflict 197 198 . . . Note=SA->RP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q02983 UniProtKB Sequence conflict 260 260 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38204 1 145 +P38204 UniProtKB Chain 1 145 . . . ID=PRO_0000097445;Note=RNA polymerase I-specific transcription initiation factor RRN10 +##sequence-region P40992 1 514 +P40992 UniProtKB Chain 1 514 . . . ID=PRO_0000097450;Note=RNA polymerase I-specific transcription initiation factor RRN7 +P40992 UniProtKB Zinc finger 3 36 . . . Note=RRN7-type +P40992 UniProtKB Region 37 66 . . . Note=B-reader +P40992 UniProtKB Region 67 101 . . . Note=B-linker +P40992 UniProtKB Region 102 210 . . . Note=N-terminal cyclin fold +P40992 UniProtKB Region 211 320 . . . Note=C-terminal cyclin fold +P40992 UniProtKB Compositional bias 71 87 . . . Note=Gln-rich +P40992 UniProtKB Metal binding 10 10 . . . Note=Zinc;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40992 UniProtKB Metal binding 15 15 . . . Note=Zinc;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40992 UniProtKB Metal binding 29 29 . . . Note=Zinc;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40992 UniProtKB Metal binding 33 33 . . . Note=Zinc;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40992 UniProtKB Mutagenesis 29 29 . . . Note=Impaired binding to Pol I. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21921198;Dbxref=PMID:21921198 +P40992 UniProtKB Mutagenesis 33 33 . . . Note=Impaired binding to Pol I. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21921198;Dbxref=PMID:21921198 +P40992 UniProtKB Beta strand 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61 +P40992 UniProtKB Helix 101 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Helix 128 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Helix 158 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Helix 178 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Beta strand 189 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61 +P40992 UniProtKB Beta strand 193 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Helix 209 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Turn 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Helix 225 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Turn 240 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Helix 249 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Helix 265 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Beta strand 289 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Beta strand 294 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61 +P40992 UniProtKB Helix 302 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Helix 330 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Helix 345 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Beta strand 358 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Helix 362 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Helix 371 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Helix 406 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Helix 438 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Helix 472 490 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +P40992 UniProtKB Helix 495 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +##sequence-region P0CX47 1 156 +P0CX47 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921 +P0CX47 UniProtKB Chain 2 156 . . . ID=PRO_0000128523;Note=40S ribosomal protein S11-A +P0CX47 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921 +P0CX47 UniProtKB Cross-link 15 15 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX47 UniProtKB Cross-link 46 46 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX47 UniProtKB Cross-link 56 56 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX47 UniProtKB Cross-link 57 57 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX47 UniProtKB Cross-link 79 79 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX47 UniProtKB Cross-link 96 96 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX47 UniProtKB Cross-link 105 105 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX47 UniProtKB Cross-link 133 133 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX47 UniProtKB Cross-link 141 141 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX47 UniProtKB Cross-link 148 148 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX47 UniProtKB Sequence conflict 12 13 . . . Note=AF->FA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0CX47 UniProtKB Beta strand 10 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX47 UniProtKB Beta strand 23 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P0CX47 UniProtKB Beta strand 28 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX47 UniProtKB Helix 46 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX47 UniProtKB Turn 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX47 UniProtKB Beta strand 70 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX47 UniProtKB Beta strand 83 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX47 UniProtKB Turn 95 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX47 UniProtKB Beta strand 99 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX47 UniProtKB Beta strand 122 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX47 UniProtKB Beta strand 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX47 UniProtKB Beta strand 137 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX47 UniProtKB Beta strand 145 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX47 UniProtKB Helix 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P22276 1 1149 +P22276 UniProtKB Chain 1 1149 . . . ID=PRO_0000048096;Note=DNA-directed RNA polymerase III subunit RPC2 +P22276 UniProtKB Zinc finger 1095 1110 . . . Note=C4-type;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22276 UniProtKB Metal binding 1095 1095 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22276 UniProtKB Metal binding 1098 1098 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22276 UniProtKB Metal binding 1107 1107 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22276 UniProtKB Metal binding 1110 1110 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22276 UniProtKB Sequence conflict 213 213 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32910 1 317 +P32910 UniProtKB Chain 1 317 . . . ID=PRO_0000073977;Note=DNA-directed RNA polymerase III subunit RPC6 +P32910 UniProtKB Mutagenesis 89 89 . . . Note=Cold-sensitive. Abolishes interaction with BRF1/TDS4. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9312031;Dbxref=PMID:9312031 +P32910 UniProtKB Mutagenesis 102 103 . . . Note=Cold-sensitive. No effect on interaction with BRF1/TDS4. RE->VA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9312031;Dbxref=PMID:9312031 +P32910 UniProtKB Mutagenesis 135 138 . . . Note=Temperature-sensitive%3B cold-sensitive. Abolishes interaction with BRF1/TDS4. Stabilizes Pol III open complex formation. KSVK->ASVA +P32910 UniProtKB Mutagenesis 135 135 . . . Note=Cold-sensitive. Abolishes interaction with BRF1/TDS4. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9312031;Dbxref=PMID:9312031 +P32910 UniProtKB Mutagenesis 171 173 . . . Note=Cold-sensitive. Abolishes interaction with BRF1/TDS4. DIE->AIA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9312031;Dbxref=PMID:9312031 +P32910 UniProtKB Mutagenesis 171 171 . . . Note=Cold-sensitive. Abolishes interaction with BRF1/TDS4. D->H +##sequence-region P36160 1 344 +P36160 UniProtKB Chain 1 344 . . . ID=PRO_0000120256;Note=Ribosome biogenesis protein RPF2 +P36160 UniProtKB Domain 28 243 . . . Note=Brix;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00034 +P36160 UniProtKB Modified residue 73 73 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P36160 UniProtKB Beta strand 30 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Helix 40 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Beta strand 56 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Turn 68 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Helix 73 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Beta strand 85 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Beta strand 94 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Beta strand 99 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Beta strand 109 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Helix 125 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Beta strand 140 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Helix 147 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Helix 152 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Beta strand 171 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Helix 175 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Beta strand 180 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Beta strand 199 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Beta strand 220 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Beta strand 229 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +P36160 UniProtKB Helix 242 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +##sequence-region O13563 1 156 +O13563 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +O13563 UniProtKB Chain 2 156 . . . ID=PRO_0000268704;Note=26S proteasome regulatory subunit RPN13 +O13563 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +O13563 UniProtKB Modified residue 133 133 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +O13563 UniProtKB Modified residue 135 135 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +O13563 UniProtKB Modified residue 140 140 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +O13563 UniProtKB Alternative sequence 1 2 . . . ID=VSP_058121;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +O13563 UniProtKB Beta strand 8 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D +O13563 UniProtKB Beta strand 15 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D +O13563 UniProtKB Turn 19 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D +O13563 UniProtKB Beta strand 23 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D +O13563 UniProtKB Beta strand 32 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D +O13563 UniProtKB Turn 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D +O13563 UniProtKB Beta strand 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D +O13563 UniProtKB Beta strand 46 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D +O13563 UniProtKB Beta strand 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D +O13563 UniProtKB Turn 70 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D +O13563 UniProtKB Beta strand 73 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D +O13563 UniProtKB Beta strand 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D +O13563 UniProtKB Beta strand 86 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D +O13563 UniProtKB Beta strand 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D +O13563 UniProtKB Beta strand 97 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Z4D +##sequence-region Q08723 1 338 +Q08723 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901 +Q08723 UniProtKB Chain 2 338 . . . ID=PRO_0000213951;Note=26S proteasome regulatory subunit RPN8 +Q08723 UniProtKB Domain 8 143 . . . Note=MPN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01182 +Q08723 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12504901;Dbxref=PMID:12504901 +Q08723 UniProtKB Modified residue 314 314 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08723 UniProtKB Modified residue 317 317 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08723 UniProtKB Modified residue 319 319 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198 +Q08723 UniProtKB Modified residue 327 327 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08723 UniProtKB Sequence conflict 126 126 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08723 UniProtKB Beta strand 7 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +Q08723 UniProtKB Helix 12 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +Q08723 UniProtKB Beta strand 34 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +Q08723 UniProtKB Beta strand 42 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +Q08723 UniProtKB Beta strand 56 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +Q08723 UniProtKB Beta strand 62 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +Q08723 UniProtKB Helix 70 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +Q08723 UniProtKB Beta strand 87 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +Q08723 UniProtKB Beta strand 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q08723 UniProtKB Helix 103 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +Q08723 UniProtKB Beta strand 115 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +Q08723 UniProtKB Beta strand 119 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +Q08723 UniProtKB Beta strand 129 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +Q08723 UniProtKB Beta strand 133 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +Q08723 UniProtKB Turn 145 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OCN +Q08723 UniProtKB Beta strand 151 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +Q08723 UniProtKB Beta strand 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +Q08723 UniProtKB Helix 165 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4O8Y +Q08723 UniProtKB Helix 186 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q08723 UniProtKB Helix 223 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +Q08723 UniProtKB Helix 261 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JCK +##sequence-region Q12532 1 1038 +Q12532 UniProtKB Chain 1 1038 . . . ID=PRO_0000244627;Note=Ribosome quality control complex subunit 2 +Q12532 UniProtKB Coiled coil 350 383 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12532 UniProtKB Coiled coil 713 768 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12532 UniProtKB Coiled coil 830 912 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12532 UniProtKB Compositional bias 720 752 . . . Note=Poly-Glu +Q12532 UniProtKB Modified residue 797 797 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12532 UniProtKB Mutagenesis 9 9 . . . Note=Abolishes CAT tail synthesis and heat shock response%2C but still binds to 60S ribosomal subunits and supports LTN1-dependent ubiquitination of nascent chains%3B when associated with A-98 and A-99. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25554787;Dbxref=PMID:25554787 +Q12532 UniProtKB Mutagenesis 98 98 . . . Note=Abolishes CAT tail synthesis and heat shock response%2C but still binds to 60S ribosomal subunits and supports LTN1-dependent ubiquitination of nascent chains%3B when associated with A-9 and A-99. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25554787;Dbxref=PMID:25554787 +Q12532 UniProtKB Mutagenesis 99 99 . . . Note=Abolishes CAT tail synthesis and heat shock response%2C but still binds to 60S ribosomal subunits and supports LTN1-dependent ubiquitination of nascent chains%3B when associated with A-9 and A-98. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25554787;Dbxref=PMID:25554787 +##sequence-region P53437 1 365 +P53437 UniProtKB Chain 1 365 . . . ID=PRO_0000097451;Note=RNA polymerase I-specific transcription initiation factor RRN9 +P53437 UniProtKB Sequence conflict 255 255 . . . Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04031 1 235 +Q04031 UniProtKB Chain 1 235 . . . ID=PRO_0000253822;Note=Ribosomal RNA-processing protein 17 +Q04031 UniProtKB Coiled coil 49 110 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04031 UniProtKB Modified residue 113 113 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04031 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04031 UniProtKB Modified residue 122 122 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P38961 1 392 +P38961 UniProtKB Chain 1 392 . . . ID=PRO_0000202594;Note=25S rRNA (adenine(645)-N(1))-methyltransferase +P38961 UniProtKB Coiled coil 32 61 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38961 UniProtKB Coiled coil 344 382 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38961 UniProtKB Binding site 156 156 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43159 +P38961 UniProtKB Binding site 207 207 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43159 +P38961 UniProtKB Binding site 242 242 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43159 +P38961 UniProtKB Binding site 254 254 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43159 +P38961 UniProtKB Binding site 271 271 . . . Note=S-adenosyl-L-methionine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O43159 +P38961 UniProtKB Modified residue 62 62 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38961 UniProtKB Mutagenesis 209 209 . . . Note=Impaired methyltransferase activity and ribosomal 60S subunit biogenesis. Does not affect pre-rRNA cleavage at site A2 activity. G->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23180764;Dbxref=PMID:23180764 +P38961 UniProtKB Mutagenesis 390 390 . . . Note=In RRP8-1%3B no effect. Synthetic lethal with GAR1 mutant allele lacking its N- and C-terminal glycine/arginine-rich (GAR) domains. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10864042;Dbxref=PMID:10864042 +##sequence-region P40571 1 144 +P40571 UniProtKB Chain 1 144 . . . ID=PRO_0000153847;Note=Ribonuclease P protein subunit RPR2 +P40571 UniProtKB Metal binding 90 90 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40571 UniProtKB Metal binding 93 93 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40571 UniProtKB Metal binding 115 115 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40571 UniProtKB Metal binding 117 117 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P39677 1 819 +P39677 UniProtKB Transit peptide 1 30 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03059 +P39677 UniProtKB Chain 31 819 . . . ID=PRO_0000007453;Note=Ribosome-releasing factor 2%2C mitochondrial +P39677 UniProtKB Domain 39 327 . . . Note=tr-type G +P39677 UniProtKB Nucleotide binding 48 55 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03059 +P39677 UniProtKB Nucleotide binding 113 117 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03059 +P39677 UniProtKB Nucleotide binding 165 168 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03059 +##sequence-region Q08774 1 242 +Q08774 UniProtKB Chain 1 242 . . . ID=PRO_0000245286;Note=Required for respiratory growth protein 7%2C mitochondrial +##sequence-region Q04712 1 507 +Q04712 UniProtKB Chain 1 507 . . . ID=PRO_0000203257;Note=RNA polymerase I-specific transcription initiation factor RRN11 +Q04712 UniProtKB Helix 11 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Helix 75 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Beta strand 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61 +Q04712 UniProtKB Helix 159 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Helix 169 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Helix 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Helix 182 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Beta strand 196 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Helix 202 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Helix 208 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Helix 229 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Helix 250 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Beta strand 262 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Helix 267 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Beta strand 278 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Beta strand 296 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Beta strand 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61 +Q04712 UniProtKB Helix 307 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Helix 346 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Beta strand 353 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61 +Q04712 UniProtKB Helix 362 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Helix 402 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +Q04712 UniProtKB Turn 418 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N61 +Q04712 UniProtKB Helix 429 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5N5X +##sequence-region P36080 1 434 +P36080 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P36080 UniProtKB Chain 2 434 . . . ID=PRO_0000203167;Note=Ribosomal RNA-processing protein 14 +P36080 UniProtKB Coiled coil 162 230 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36080 UniProtKB Coiled coil 293 360 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36080 UniProtKB Compositional bias 122 130 . . . Note=Asp/Glu-rich (acidic) +P36080 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P46948 1 246 +P46948 UniProtKB Chain 1 246 . . . ID=PRO_0000139962;Note=Exosome complex component SKI6 +P46948 UniProtKB Mutagenesis 62 63 . . . Note=Impairs RNA-binding (at the proposed ring entry site). KS->ED;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19879841;Dbxref=PMID:19879841 +P46948 UniProtKB Mutagenesis 95 96 . . . Note=Impairs RNA-binding (at the proposed ring exit site). RR->EE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19879841;Dbxref=PMID:19879841 +P46948 UniProtKB Beta strand 14 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OO1 +P46948 UniProtKB Beta strand 25 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Turn 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Beta strand 37 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Beta strand 47 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Beta strand 60 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Beta strand 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Beta strand 71 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Beta strand 82 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Helix 95 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Turn 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Helix 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Beta strand 121 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Helix 135 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Beta strand 154 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Beta strand 158 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Beta strand 169 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Helix 176 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Beta strand 182 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Beta strand 193 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Helix 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P46948 UniProtKB Helix 210 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +##sequence-region Q12277 1 265 +Q12277 UniProtKB Chain 1 265 . . . ID=PRO_0000139966;Note=Exosome complex component RRP42 +Q12277 UniProtKB Helix 5 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Beta strand 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Beta strand 34 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Beta strand 44 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Beta strand 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OO1 +Q12277 UniProtKB Beta strand 57 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Turn 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Beta strand 76 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Helix 90 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Turn 105 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Helix 111 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Beta strand 117 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Helix 138 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Beta strand 153 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Turn 163 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +Q12277 UniProtKB Beta strand 171 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Beta strand 186 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Beta strand 196 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Helix 203 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Beta strand 210 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Beta strand 226 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Beta strand 233 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Helix 241 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q12277 UniProtKB Helix 256 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +##sequence-region P53256 1 223 +P53256 UniProtKB Chain 1 223 . . . ID=PRO_0000139978;Note=Exosome complex component RRP46 +P53256 UniProtKB Beta strand 4 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Beta strand 11 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Beta strand 24 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Turn 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Beta strand 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Beta strand 47 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Beta strand 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Helix 61 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Helix 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Beta strand 87 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Turn 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Helix 106 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Beta strand 127 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Turn 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Beta strand 145 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Helix 151 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Beta strand 157 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Turn 169 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Beta strand 173 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Helix 188 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P53256 UniProtKB Helix 218 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +##sequence-region P40470 1 206 +P40470 UniProtKB Chain 1 206 . . . ID=PRO_0000202961;Note=Regulator of rDNA transcription protein 14 +P40470 UniProtKB Compositional bias 66 100 . . . Note=Lys-rich +P40470 UniProtKB Modified residue 197 197 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40470 UniProtKB Modified residue 202 202 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40470 UniProtKB Modified residue 203 203 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P43607 1 289 +P43607 UniProtKB Chain 1 289 . . . ID=PRO_0000082029;Note=Regulator of rDNA transcription protein 5 +P43607 UniProtKB Domain 18 105 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +##sequence-region Q08219 1 342 +Q08219 UniProtKB Chain 1 342 . . . ID=PRO_0000203488;Note=Outer spore wall protein RRT8 +Q08219 UniProtKB Topological domain 1 109 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q08219 UniProtKB Transmembrane 110 130 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08219 UniProtKB Topological domain 131 131 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q08219 UniProtKB Transmembrane 132 152 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08219 UniProtKB Topological domain 153 240 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q08219 UniProtKB Transmembrane 241 261 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08219 UniProtKB Topological domain 262 299 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +Q08219 UniProtKB Transmembrane 300 320 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08219 UniProtKB Topological domain 321 342 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +Q08219 UniProtKB Sequence conflict 138 138 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P07281 1 144 +P07281 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:6814480;Dbxref=PMID:10601260,PMID:6814480 +P07281 UniProtKB Chain 2 144 . . . ID=PRO_0000153836;Note=40S ribosomal protein S19-B +##sequence-region Q3E792 1 108 +Q3E792 UniProtKB Initiator methionine 1 1 . . . Note=Removed +Q3E792 UniProtKB Chain 2 108 . . . ID=PRO_0000043376;Note=40S ribosomal protein S25-A +Q3E792 UniProtKB Modified residue 2 2 . . . Note=N%2CN-dimethylproline%3B by NTM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20481588;Dbxref=PMID:20481588 +Q3E792 UniProtKB Natural variant 8 8 . . . Note=In strain: SK1. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +Q3E792 UniProtKB Natural variant 13 13 . . . Note=In strain: SK1. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +Q3E792 UniProtKB Sequence conflict 16 16 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q3E792 UniProtKB Beta strand 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E792 UniProtKB Helix 45 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E792 UniProtKB Helix 54 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E792 UniProtKB Beta strand 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E792 UniProtKB Helix 62 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E792 UniProtKB Helix 73 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E792 UniProtKB Beta strand 84 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E792 UniProtKB Beta strand 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +Q3E792 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P39939 1 119 +P39939 UniProtKB Chain 1 119 . . . ID=PRO_0000204529;Note=40S ribosomal protein S26-B +P39939 UniProtKB Sequence conflict 110 110 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39939 UniProtKB Beta strand 6 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P39939 UniProtKB Beta strand 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P39939 UniProtKB Turn 24 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P39939 UniProtKB Beta strand 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P39939 UniProtKB Turn 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P39939 UniProtKB Beta strand 37 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P39939 UniProtKB Helix 49 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P39939 UniProtKB Beta strand 58 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P39939 UniProtKB Beta strand 66 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P39939 UniProtKB Helix 76 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P39939 UniProtKB Beta strand 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U6F +P39939 UniProtKB Helix 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P41058 1 56 +P41058 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:18782943 +P41058 UniProtKB Chain 2 56 . . . ID=PRO_0000131033;Note=40S ribosomal protein S29-B +P41058 UniProtKB Metal binding 21 21 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41058 UniProtKB Metal binding 24 24 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41058 UniProtKB Metal binding 39 39 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41058 UniProtKB Metal binding 42 42 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41058 UniProtKB Modified residue 25 25 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P41058 UniProtKB Sequence conflict 7 7 . . . Note=W->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P26783 1 225 +P26783 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921 +P26783 UniProtKB Chain 2 225 . . . ID=PRO_0000124540;Note=40S ribosomal protein S5 +P26783 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921 +P26783 UniProtKB Modified residue 27 27 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P26783 UniProtKB Cross-link 45 45 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P26783 UniProtKB Cross-link 203 203 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P26783 UniProtKB Sequence conflict 21 21 . . . Note=T->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P26783 UniProtKB Helix 31 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26783 UniProtKB Beta strand 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26783 UniProtKB Beta strand 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M +P26783 UniProtKB Turn 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26783 UniProtKB Turn 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26783 UniProtKB Beta strand 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26783 UniProtKB Beta strand 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26783 UniProtKB Helix 83 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26783 UniProtKB Helix 89 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26783 UniProtKB Helix 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26783 UniProtKB Helix 107 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26783 UniProtKB Helix 129 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26783 UniProtKB Beta strand 143 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26783 UniProtKB Beta strand 151 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26783 UniProtKB Beta strand 157 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26783 UniProtKB Helix 164 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26783 UniProtKB Beta strand 186 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26783 UniProtKB Helix 190 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26783 UniProtKB Beta strand 206 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P26783 UniProtKB Helix 209 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P48164 1 190 +P48164 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P48164 UniProtKB Chain 2 190 . . . ID=PRO_0000174213;Note=40S ribosomal protein S7-B +P48164 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P48164 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P48164 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region Q06488 1 889 +Q06488 UniProtKB Chain 1 889 . . . ID=PRO_0000211212;Note=Chromatin structure-remodeling complex subunit RSC2 +Q06488 UniProtKB Domain 35 103 . . . Note=Bromo 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 +Q06488 UniProtKB Domain 295 365 . . . Note=Bromo 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 +Q06488 UniProtKB Domain 408 526 . . . Note=BAH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00370 +Q06488 UniProtKB Compositional bias 667 716 . . . Note=Gln-rich +Q06488 UniProtKB Modified residue 612 612 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06488 UniProtKB Modified residue 682 682 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +Q06488 UniProtKB Mutagenesis 468 468 . . . Note=In dpm3%3B defective in plasmid maintenance. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12024034;Dbxref=PMID:12024034 +Q06488 UniProtKB Mutagenesis 601 601 . . . Note=In dpm18%3B defective in plasmid maintenance. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12024034;Dbxref=PMID:12024034 +Q06488 UniProtKB Beta strand 403 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Beta strand 408 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Beta strand 415 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Beta strand 428 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Beta strand 443 451 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Helix 453 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Beta strand 462 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Beta strand 470 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Helix 480 482 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Beta strand 483 486 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Beta strand 488 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Helix 492 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Beta strand 498 501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Beta strand 508 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Beta strand 513 516 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Turn 517 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Beta strand 521 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Helix 528 531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Helix 534 536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Beta strand 543 545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Beta strand 547 555 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Helix 559 561 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Beta strand 621 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Turn 627 630 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +Q06488 UniProtKB Beta strand 631 633 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BB7 +##sequence-region P43609 1 557 +P43609 UniProtKB Chain 1 557 . . . ID=PRO_0000197114;Note=Chromatin structure-remodeling complex protein RSC8 +P43609 UniProtKB Domain 80 177 . . . Note=SWIRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00247 +P43609 UniProtKB Domain 310 362 . . . Note=SANT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00624 +P43609 UniProtKB Zinc finger 254 298 . . . Note=ZZ-type +P43609 UniProtKB Coiled coil 38 77 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43609 UniProtKB Coiled coil 462 494 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43609 UniProtKB Modified residue 485 485 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43609 UniProtKB Mutagenesis 347 351 . . . Note=Loss of function. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12419236;Dbxref=PMID:12419236 +P43609 UniProtKB Sequence conflict 192 192 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03246 1 237 +Q03246 UniProtKB Chain 1 237 . . . ID=PRO_0000128525;Note=37S ribosomal protein S17%2C mitochondrial +##sequence-region P36056 1 628 +P36056 UniProtKB Transit peptide 1 15 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36056 UniProtKB Chain 16 628 . . . ID=PRO_0000203144;Note=Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22%2C mitochondrial +##sequence-region Q03976 1 319 +Q03976 UniProtKB Transit peptide 1 30 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03976 UniProtKB Chain 31 319 . . . ID=PRO_0000268705;Note=37S ribosomal protein S24%2C mitochondrial +##sequence-region Q02950 1 344 +Q02950 UniProtKB Chain 1 344 . . . ID=PRO_0000087701;Note=37S ribosomal protein MRP51%2C mitochondrial +Q02950 UniProtKB Modified residue 327 327 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02950 UniProtKB Mutagenesis 235 235 . . . Note=Suppresses defects in the 5'UTLs of COX2 and COX3 mitochondrial mRNAs. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528754;Dbxref=PMID:9528754 +Q02950 UniProtKB Mutagenesis 241 241 . . . Note=Suppresses defects in the 5'UTLs of COX2 and COX3 mitochondrial mRNAs. N->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528754;Dbxref=PMID:9528754 +Q02950 UniProtKB Mutagenesis 260 260 . . . Note=Suppresses defects in the 5'UTLs of COX2 and COX3 mitochondrial mRNAs. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528754;Dbxref=PMID:9528754 +Q02950 UniProtKB Mutagenesis 261 261 . . . Note=Suppresses defects in the 5'UTLs of COX2 and COX3 mitochondrial mRNAs. P->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528754;Dbxref=PMID:9528754 +Q02950 UniProtKB Mutagenesis 279 279 . . . Note=Suppresses defects in the 5'UTLs of COX2 and COX3 mitochondrial mRNAs. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528754;Dbxref=PMID:9528754 +##sequence-region Q03919 1 77 +Q03919 UniProtKB Chain 1 76 . . . ID=PRO_0000035979;Note=NEDD8-like protein RUB1 +Q03919 UniProtKB Propeptide 77 77 . . . ID=PRO_0000035980;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03919 UniProtKB Domain 1 74 . . . Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 +Q03919 UniProtKB Cross-link 76 76 . . . Note=Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 +##sequence-region Q12464 1 471 +Q12464 UniProtKB Chain 1 471 . . . ID=PRO_0000165675;Note=RuvB-like protein 2 +Q12464 UniProtKB Nucleotide binding 75 82 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12464 UniProtKB Mutagenesis 75 75 . . . Note=Lethal. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11604509;Dbxref=PMID:11604509 +Q12464 UniProtKB Mutagenesis 80 80 . . . Note=Growth defect at 37 degrees Celsius. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11604509;Dbxref=PMID:11604509 +Q12464 UniProtKB Mutagenesis 81 81 . . . Note=Defect in snoRNA accumulation. Growth defect at 37 degrees Celsius. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10787406,ECO:0000269|PubMed:11278922,ECO:0000269|PubMed:11604509;Dbxref=PMID:10787406,PMID:11278922,PMID:11604509 +Q12464 UniProtKB Mutagenesis 81 81 . . . Note=Lethal. K->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10787406,ECO:0000269|PubMed:11278922,ECO:0000269|PubMed:11604509;Dbxref=PMID:10787406,PMID:11278922,PMID:11604509 +Q12464 UniProtKB Mutagenesis 81 81 . . . Note=Growth defect at 37 degrees Celsius. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10787406,ECO:0000269|PubMed:11278922,ECO:0000269|PubMed:11604509;Dbxref=PMID:10787406,PMID:11278922,PMID:11604509 +Q12464 UniProtKB Mutagenesis 296 296 . . . Note=Lethal. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11604509;Dbxref=PMID:11604509 +Q12464 UniProtKB Mutagenesis 297 297 . . . Note=Lethal. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278922;Dbxref=PMID:11278922 +##sequence-region Q3E754 1 87 +Q3E754 UniProtKB Chain 1 87 . . . ID=PRO_0000194762;Note=40S ribosomal protein S21-B +Q3E754 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +##sequence-region P0CX31 1 135 +P0CX31 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921 +P0CX31 UniProtKB Chain 2 135 . . . ID=PRO_0000137636;Note=40S ribosomal protein S24-A +P0CX31 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921 +P0CX31 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P0CX31 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX31 UniProtKB Cross-link 21 21 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX31 UniProtKB Sequence conflict 16 16 . . . Note=P->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0CX31 UniProtKB Beta strand 7 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX31 UniProtKB Helix 16 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX31 UniProtKB Beta strand 20 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX31 UniProtKB Beta strand 30 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P0CX31 UniProtKB Helix 37 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX31 UniProtKB Turn 46 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX31 UniProtKB Helix 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX31 UniProtKB Beta strand 55 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX31 UniProtKB Beta strand 66 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX31 UniProtKB Helix 79 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX31 UniProtKB Helix 88 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX31 UniProtKB Beta strand 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U52 +P0CX31 UniProtKB Helix 105 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX31 UniProtKB Beta strand 120 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56 +P0CX31 UniProtKB Helix 123 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region Q08932 1 381 +Q08932 UniProtKB Chain 1 381 . . . ID=PRO_0000097460;Note=Ribosome assembly 1 protein +Q08932 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q08932 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q08932 UniProtKB Helix 240 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT +Q08932 UniProtKB Helix 261 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT +Q08932 UniProtKB Helix 320 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJF +Q08932 UniProtKB Helix 343 349 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2MJF +##sequence-region P38781 1 883 +P38781 UniProtKB Chain 1 883 . . . ID=PRO_0000114974;Note=Chromatin structure-remodeling complex protein RSC30 +P38781 UniProtKB DNA binding 14 45 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P38781 UniProtKB Modified residue 150 150 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38781 UniProtKB Mutagenesis 15 15 . . . Note=Complete inactivation. C->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11336698;Dbxref=PMID:11336698 +##sequence-region Q05043 1 376 +Q05043 UniProtKB Chain 1 376 . . . ID=PRO_0000203272;Note=Respiration factor 1 +##sequence-region Q03430 1 361 +Q03430 UniProtKB Mutagenesis 121 187 . . . Note=In RSM28-1%3B allows translation of defective COX2 mRNAs. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15701796;Dbxref=PMID:15701796 +##sequence-region Q03201 1 203 +Q03201 UniProtKB Transit peptide 1 14 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03201 UniProtKB Chain 15 203 . . . ID=PRO_0000042756;Note=37S ribosomal protein S10%2C mitochondrial +Q03201 UniProtKB Modified residue 193 193 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P38175 1 177 +P38175 UniProtKB Transit peptide 1 17 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38175 UniProtKB Chain 18 177 . . . ID=PRO_0000202444;Note=37S ribosomal protein MRP21%2C mitochondrial +P38175 UniProtKB Mutagenesis 115 115 . . . Note=In MRP21-1%3B suppresses translation defects of mutations in the 5'-untranslated leaders of mitochondrial mRNAs. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528754;Dbxref=PMID:9528754 +P38175 UniProtKB Mutagenesis 121 121 . . . Note=In MRP21-3%3B suppresses translation defects of mutations in the 5'-untranslated leaders of mitochondrial mRNAs. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9528754;Dbxref=PMID:9528754 +##sequence-region P21771 1 286 +P21771 UniProtKB Transit peptide 1 33 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2263452;Dbxref=PMID:2263452 +P21771 UniProtKB Chain 34 286 . . . ID=PRO_0000030613;Note=37S ribosomal protein S28%2C mitochondrial +##sequence-region P38786 1 293 +P38786 UniProtKB Chain 1 293 . . . ID=PRO_0000140034;Note=Ribonuclease P/MRP protein subunit RPP1 +##sequence-region Q05468 1 723 +Q05468 UniProtKB Chain 1 723 . . . ID=PRO_0000253842;Note=Ribosome quality control complex subunit 1 +Q05468 UniProtKB Compositional bias 120 125 . . . Note=Poly-Asp +Q05468 UniProtKB Modified residue 119 119 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +Q05468 UniProtKB Modified residue 158 158 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q05468 UniProtKB Modified residue 160 160 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region Q04225 1 511 +Q04225 UniProtKB Chain 1 511 . . . ID=PRO_0000051202;Note=Ribosome assembly protein RRB1 +Q04225 UniProtKB Repeat 319 359 . . . Note=WD 1 +Q04225 UniProtKB Repeat 364 404 . . . Note=WD 2 +Q04225 UniProtKB Repeat 415 455 . . . Note=WD 3 +Q04225 UniProtKB Repeat 477 510 . . . Note=WD 4 +Q04225 UniProtKB Modified residue 5 5 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38771 1 230 +P38771 UniProtKB Transit peptide 1 24 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38771 UniProtKB Chain 25 230 . . . ID=PRO_0000031091;Note=Ribosome-recycling factor%2C mitochondrial +##sequence-region P40156 1 214 +P40156 UniProtKB Transit peptide 1 18 . . . Note=Mitochondrion;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40156 UniProtKB Chain 19 214 . . . ID=PRO_0000203389;Note=Required for respiratory growth protein 9%2C mitochondrial +##sequence-region P38766 1 723 +P38766 UniProtKB Chain 1 723 . . . ID=PRO_0000101986;Note=ATP-dependent DNA helicase RRM3 +P38766 UniProtKB Nucleotide binding 254 261 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03177 +P38766 UniProtKB DNA binding 682 701 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03177 +P38766 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38766 UniProtKB Mutagenesis 41 41 . . . Note=Reduces the interaction with POL30%3B when associated with A-42 or D-42. F->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12239216;Dbxref=PMID:12239216 +P38766 UniProtKB Mutagenesis 42 42 . . . Note=Reduces the interaction with POL30%3B when associated with A-42 or D-42. F->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12239216;Dbxref=PMID:12239216 +##sequence-region P36070 1 627 +P36070 UniProtKB Chain 1 627 . . . ID=PRO_0000211430;Note=RNA polymerase I-specific transcription initiation factor RRN3 +P36070 UniProtKB Compositional bias 252 259 . . . Note=Poly-Asp +P36070 UniProtKB Compositional bias 267 274 . . . Note=Poly-Asp +P36070 UniProtKB Compositional bias 277 280 . . . Note=Poly-Asp +P36070 UniProtKB Compositional bias 546 549 . . . Note=Poly-Asn +P36070 UniProtKB Helix 49 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 69 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 90 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 103 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 113 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 125 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 130 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 151 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 166 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 184 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 187 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 205 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 223 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 226 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 323 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 326 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 349 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 357 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Turn 371 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 383 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 393 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Beta strand 410 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 414 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 436 457 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 458 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Beta strand 463 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 467 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 471 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 488 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 499 501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 502 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 516 519 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 522 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 541 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 579 590 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 600 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 607 609 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +P36070 UniProtKB Helix 613 616 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TJ1 +##sequence-region P38712 1 501 +P38712 UniProtKB Chain 1 501 . . . ID=PRO_0000055064;Note=ATP-dependent rRNA helicase RRP3 +P38712 UniProtKB Domain 112 284 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P38712 UniProtKB Domain 307 461 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P38712 UniProtKB Nucleotide binding 125 132 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P38712 UniProtKB Coiled coil 3 44 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38712 UniProtKB Motif 81 109 . . . Note=Q motif;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38712 UniProtKB Motif 231 234 . . . Note=DEAD box;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38712 UniProtKB Modified residue 43 43 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38712 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38712 UniProtKB Modified residue 47 47 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38712 UniProtKB Mutagenesis 131 131 . . . Note=Leads to defects in A1 and A2 processing. K->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16449634;Dbxref=PMID:16449634 +P38712 UniProtKB Mutagenesis 231 231 . . . Note=Leads to defects in A1 and A2 processing. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16449634;Dbxref=PMID:16449634 +P38712 UniProtKB Mutagenesis 263 263 . . . Note=Leads to defects in A1 and A2 processing. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16449634;Dbxref=PMID:16449634 +##sequence-region Q08162 1 1001 +Q08162 UniProtKB Chain 1 1001 . . . ID=PRO_0000166423;Note=Exosome complex exonuclease DIS3 +Q08162 UniProtKB Domain 904 1001 . . . Note=S1 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00180 +Q08162 UniProtKB Region 1 235 . . . Note=Endoribonuclease +Q08162 UniProtKB Mutagenesis 47 47 . . . Note=Slow growth%3B when associated with S-52 and S-55. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19060898;Dbxref=PMID:19060898 +Q08162 UniProtKB Mutagenesis 52 52 . . . Note=Slow growth%3B when associated with S-47 and S-55. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19060898;Dbxref=PMID:19060898 +Q08162 UniProtKB Mutagenesis 55 55 . . . Note=Slow growth%3B when associated with S-47 and S-52. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19060898;Dbxref=PMID:19060898 +Q08162 UniProtKB Mutagenesis 171 171 . . . Note=Abolishes endoribonucleolytic activity%3B no effect on growth. No growth%3B when associated with N-551. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19060898;Dbxref=PMID:19060898 +Q08162 UniProtKB Mutagenesis 198 198 . . . Note=Abolishes endoribonucleolytic activity%3B no effect on growth. No growth%3B when associated with N-551. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19060898;Dbxref=PMID:19060898 +Q08162 UniProtKB Mutagenesis 551 551 . . . Note=Exoribonucleolytic activity abolished. Accumulation of partially processed 5.8S rRNA and partially degraded 5' ETS. No growth%3B when associated with A-171. No growth%3B when associated with A-198. D->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17173052,ECO:0000269|PubMed:18374646,ECO:0000269|PubMed:19060898;Dbxref=PMID:17173052,PMID:18374646,PMID:19060898 +Q08162 UniProtKB Beta strand 10 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36 +Q08162 UniProtKB Beta strand 14 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Beta strand 18 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Beta strand 33 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +Q08162 UniProtKB Helix 55 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Turn 80 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +Q08162 UniProtKB Beta strand 85 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Helix 92 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Turn 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WP8 +Q08162 UniProtKB Beta strand 110 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Helix 115 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Helix 126 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Beta strand 144 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Turn 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Turn 154 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Helix 166 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Turn 186 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Beta strand 191 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Helix 199 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +Q08162 UniProtKB Helix 209 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36 +Q08162 UniProtKB Beta strand 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Helix 218 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Helix 228 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Helix 232 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +Q08162 UniProtKB Helix 261 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 272 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 282 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 287 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 293 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 299 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 304 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 315 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 323 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Turn 336 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 367 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Beta strand 385 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Beta strand 389 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 402 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 409 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 420 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 434 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 441 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 447 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 458 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36 +Q08162 UniProtKB Beta strand 464 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 478 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 497 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 507 509 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 519 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 526 530 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 531 533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 540 546 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 552 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 564 571 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 573 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 579 581 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WP8 +Q08162 UniProtKB Helix 582 590 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 594 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WP8 +Q08162 UniProtKB Beta strand 599 601 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WP8 +Q08162 UniProtKB Helix 606 609 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Turn 610 612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 619 630 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 636 653 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 654 662 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 663 665 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +Q08162 UniProtKB Helix 669 690 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 701 705 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 707 710 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 712 717 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 722 745 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Turn 747 749 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 751 755 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 760 763 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 764 774 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 783 791 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 801 810 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 817 820 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 821 823 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 826 829 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Turn 832 835 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 836 838 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2WP8 +Q08162 UniProtKB Turn 845 847 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 849 861 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 869 872 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 874 908 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 912 922 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 925 929 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Turn 931 933 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 936 940 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 941 944 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Helix 948 950 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 952 954 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Turn 955 958 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 959 962 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 964 967 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08162 UniProtKB Beta strand 971 974 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 978 983 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 985 987 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +Q08162 UniProtKB Turn 989 991 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +Q08162 UniProtKB Beta strand 995 997 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VNU +Q08162 UniProtKB Beta strand 998 1000 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +##sequence-region P48589 1 143 +P48589 UniProtKB Chain 1 143 . . . ID=PRO_0000122340;Note=40S ribosomal protein S12 +P48589 UniProtKB Cross-link 85 85 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P48589 UniProtKB Cross-link 95 95 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P48589 UniProtKB Cross-link 114 114 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P48589 UniProtKB Sequence conflict 90 92 . . . Note=KVA->EGLP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P48589 UniProtKB Helix 26 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P48589 UniProtKB Beta strand 41 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P48589 UniProtKB Helix 45 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P48589 UniProtKB Turn 51 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P48589 UniProtKB Beta strand 58 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P48589 UniProtKB Beta strand 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P48589 UniProtKB Helix 70 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P48589 UniProtKB Beta strand 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P48589 UniProtKB Helix 94 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P48589 UniProtKB Beta strand 107 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P48589 UniProtKB Beta strand 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P48589 UniProtKB Helix 131 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P07280 1 144 +P07280 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6814480;Dbxref=PMID:6814480 +P07280 UniProtKB Chain 2 144 . . . ID=PRO_0000153835;Note=40S ribosomal protein S19-A +P07280 UniProtKB Mutagenesis 15 15 . . . Note=Partial loss of function%3B decreased 18S rRNA%2C decreases binding to 20S pre-rRNA complex%2C slow growth in double RPS19A/RPS19B mutant. I->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17726054;Dbxref=PMID:17726054 +P07280 UniProtKB Mutagenesis 57 57 . . . Note=Loss of mature 18S rRNA%2C protein doesn't bind 20S pre-RNA complex. Lethal in double RPS19A/RPS19B mutant. R->E%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17726054;Dbxref=PMID:17726054 +P07280 UniProtKB Mutagenesis 63 63 . . . Note=Loss of mature 18S rRNA%2C protein binds 20S pre-RNA complex poorly. Lethal in double RPS19A/RPS19B mutant. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17726054;Dbxref=PMID:17726054 +P07280 UniProtKB Mutagenesis 65 65 . . . Note=Lethal in double RPS19A/RPS19B mutant%2C considerable decrease in 18S rRNA production. I->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16159874,ECO:0000269|PubMed:17726054;Dbxref=PMID:16159874,PMID:17726054 +P07280 UniProtKB Mutagenesis 102 102 . . . Note=Decreases mature 18S rRNA%2C protein binds 20S pre-RNA complex poorly. Lethal in double RPS19A/RPS19B mutant. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17726054;Dbxref=PMID:17726054 +P07280 UniProtKB Mutagenesis 122 122 . . . Note=Decreases mature 18S rRNA%2C protein binds 20S pre-RNA complex poorly. Lethal in double RPS19A/RPS19B mutant. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17726054;Dbxref=PMID:17726054 +P07280 UniProtKB Helix 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P07280 UniProtKB Helix 11 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P07280 UniProtKB Beta strand 34 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P07280 UniProtKB Beta strand 39 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P07280 UniProtKB Beta strand 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P07280 UniProtKB Helix 54 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P07280 UniProtKB Beta strand 68 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P07280 UniProtKB Helix 73 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P07280 UniProtKB Beta strand 83 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P07280 UniProtKB Beta strand 89 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P07280 UniProtKB Helix 98 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P07280 UniProtKB Beta strand 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P07280 UniProtKB Beta strand 120 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P07280 UniProtKB Helix 126 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P23248 1 255 +P23248 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03122,ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921 +P23248 UniProtKB Chain 2 255 . . . ID=PRO_0000153542;Note=40S ribosomal protein S1-B +P23248 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine%3B partial;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P33442,ECO:0000255|HAMAP-Rule:MF_03122 +P23248 UniProtKB Modified residue 245 245 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P23248 UniProtKB Modified residue 254 254 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P23248 UniProtKB Cross-link 248 248 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P39516 1 138 +P39516 UniProtKB Chain 1 138 . . . ID=PRO_0000123360;Note=40S ribosomal protein S14-B +P39516 UniProtKB Sequence conflict 3 3 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CX52 1 143 +P0CX52 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921 +P0CX52 UniProtKB Chain 2 143 . . . ID=PRO_0000409772;Note=40S ribosomal protein S16-B +P0CX52 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1544921;Dbxref=PMID:1544921 +P0CX52 UniProtKB Modified residue 34 34 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P0CX52 UniProtKB Modified residue 61 61 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX52 UniProtKB Modified residue 70 70 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX52 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX52 UniProtKB Cross-link 30 30 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX52 UniProtKB Cross-link 47 47 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX52 UniProtKB Cross-link 59 59 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P0CX56 1 146 +P0CX56 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|Ref.3;Dbxref=PMID:22814378,PMID:10601260 +P0CX56 UniProtKB Chain 2 146 . . . ID=PRO_0000409774;Note=40S ribosomal protein S18-B +P0CX56 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|Ref.3;Dbxref=PMID:22814378,PMID:10601260 +P0CX56 UniProtKB Modified residue 48 48 . . . Note=N6-methyllysine%3B by RKM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22522802;Dbxref=PMID:22522802 +P0CX56 UniProtKB Cross-link 36 36 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX56 UniProtKB Cross-link 49 49 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX56 UniProtKB Cross-link 80 80 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX56 UniProtKB Cross-link 96 96 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX56 UniProtKB Sequence conflict 27 29 . . . Note=KIV->EFG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CX29 1 145 +P0CX29 UniProtKB Chain 1 145 . . . ID=PRO_0000146482;Note=40S ribosomal protein S23-A +P0CX29 UniProtKB Modified residue 64 64 . . . Note=3%2C4-dihydroxyproline;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24550462;Dbxref=PMID:24550462 +P0CX29 UniProtKB Cross-link 56 56 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX29 UniProtKB Mutagenesis 64 64 . . . Note=Lethal mutation. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24550462;Dbxref=PMID:24550462 +P0CX29 UniProtKB Mutagenesis 65 65 . . . Note=Lethal mutation. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24550462;Dbxref=PMID:24550462 +P0CX29 UniProtKB Turn 9 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M +P0CX29 UniProtKB Helix 12 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX29 UniProtKB Helix 27 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX29 UniProtKB Helix 36 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX29 UniProtKB Beta strand 40 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX29 UniProtKB Beta strand 45 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX29 UniProtKB Beta strand 68 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX29 UniProtKB Turn 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX29 UniProtKB Beta strand 82 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX29 UniProtKB Beta strand 89 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX29 UniProtKB Turn 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX29 UniProtKB Beta strand 101 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX29 UniProtKB Beta strand 108 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX29 UniProtKB Beta strand 115 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P0CX29 UniProtKB Beta strand 122 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX29 UniProtKB Turn 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P0CX29 UniProtKB Helix 132 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX29 UniProtKB Beta strand 137 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56 +##sequence-region P0CX32 1 135 +P0CX32 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:1544921 +P0CX32 UniProtKB Chain 2 135 . . . ID=PRO_0000409762;Note=40S ribosomal protein S24-B +P0CX32 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:1544921 +P0CX32 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P0CX32 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX32 UniProtKB Cross-link 21 21 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX32 UniProtKB Sequence conflict 16 16 . . . Note=P->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0C0T4 1 108 +P0C0T4 UniProtKB Initiator methionine 1 1 . . . Note=Removed +P0C0T4 UniProtKB Chain 2 108 . . . ID=PRO_0000030634;Note=40S ribosomal protein S25-B +P0C0T4 UniProtKB Modified residue 2 2 . . . Note=N%2CN-dimethylproline%3B by NTM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20481588;Dbxref=PMID:20481588 +##sequence-region P0CX35 1 261 +P0CX35 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P0CX35 UniProtKB Chain 2 261 . . . ID=PRO_0000130843;Note=40S ribosomal protein S4-A +P0CX35 UniProtKB Domain 42 105 . . . Note=S4 RNA-binding +P0CX35 UniProtKB Modified residue 32 32 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P0CX35 UniProtKB Modified residue 115 115 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX35 UniProtKB Modified residue 247 247 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P0CX35 UniProtKB Cross-link 62 62 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX35 UniProtKB Cross-link 134 134 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX35 UniProtKB Cross-link 161 161 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX35 UniProtKB Cross-link 168 168 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX35 UniProtKB Cross-link 174 174 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX35 UniProtKB Cross-link 179 179 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX35 UniProtKB Cross-link 211 211 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX35 UniProtKB Cross-link 233 233 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX35 UniProtKB Turn 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Helix 16 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 22 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 33 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Helix 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Helix 44 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Turn 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Helix 59 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 70 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 89 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Helix 94 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 97 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U52 +P0CX35 UniProtKB Beta strand 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Z +P0CX35 UniProtKB Helix 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 122 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Helix 133 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 137 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Turn 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P0CX35 UniProtKB Beta strand 146 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 159 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 164 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 169 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Turn 187 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U53 +P0CX35 UniProtKB Beta strand 197 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 202 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Q +P0CX35 UniProtKB Beta strand 207 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 217 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Helix 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 225 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Beta strand 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P0CX35 UniProtKB Beta strand 234 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Turn 240 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Helix 248 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX35 UniProtKB Turn 256 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +##sequence-region P32832 1 435 +P32832 UniProtKB Chain 1 435 . . . ID=PRO_0000057945;Note=Chromatin structure-remodeling complex subunit RSC7 +P32832 UniProtKB Region 248 435 . . . Note=Functional region%3B able to complement all NPL6 null allele phenotypes +P32832 UniProtKB Modified residue 86 86 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q03124 1 581 +Q03124 UniProtKB Chain 1 581 . . . ID=PRO_0000097475;Note=Chromatin structure-remodeling complex subunit RSC9 +Q03124 UniProtKB DNA binding 395 476 . . . Note=RFX-type winged-helix;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00858 +Q03124 UniProtKB Modified residue 44 44 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03124 UniProtKB Sequence conflict 60 60 . . . Note=Y->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04693 1 1361 +Q04693 UniProtKB Chain 1 1361 . . . ID=PRO_0000218638;Note=Pre-mRNA-splicing factor RSE1 +##sequence-region P38792 1 359 +P38792 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38792 UniProtKB Chain 2 359 . . . ID=PRO_0000097455;Note=Exosome complex component RRP4 +P38792 UniProtKB Domain 107 187 . . . Note=S1 motif +P38792 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38792 UniProtKB Modified residue 28 28 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38792 UniProtKB Modified residue 268 268 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38792 UniProtKB Natural variant 136 136 . . . Note=In RRP4-1%3B temperature-sensitive(ts) lethal mutation. L->P +P38792 UniProtKB Beta strand 7 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +P38792 UniProtKB Beta strand 60 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Beta strand 65 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Beta strand 73 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Beta strand 79 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Beta strand 94 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Beta strand 111 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Beta strand 121 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Beta strand 129 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Beta strand 134 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Helix 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Helix 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +P38792 UniProtKB Beta strand 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36 +P38792 UniProtKB Helix 154 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Helix 159 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Beta strand 168 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Beta strand 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +P38792 UniProtKB Beta strand 182 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Beta strand 188 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +P38792 UniProtKB Beta strand 196 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Helix 204 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Beta strand 213 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Turn 218 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Beta strand 221 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Beta strand 229 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Helix 238 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Helix 244 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OO1 +P38792 UniProtKB Helix 270 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Beta strand 279 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +P38792 UniProtKB Helix 291 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Helix 316 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Beta strand 329 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Helix 332 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +P38792 UniProtKB Helix 338 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +##sequence-region Q12149 1 733 +Q12149 UniProtKB Chain 1 733 . . . ID=PRO_0000097456;Note=Exosome complex exonuclease RRP6 +Q12149 UniProtKB Domain 435 515 . . . Note=HRDC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00328 +Q12149 UniProtKB Modified residue 138 138 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12149 UniProtKB Modified residue 520 520 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12149 UniProtKB Modified residue 640 640 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12149 UniProtKB Modified residue 645 645 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12149 UniProtKB Sequence conflict 402 402 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12149 UniProtKB Helix 8 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFC +Q12149 UniProtKB Helix 28 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFC +Q12149 UniProtKB Helix 36 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFC +Q12149 UniProtKB Helix 76 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFC +Q12149 UniProtKB Helix 132 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Beta strand 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OO1 +Q12149 UniProtKB Helix 162 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Beta strand 173 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Helix 184 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Helix 194 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Helix 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Beta strand 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Helix 219 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Beta strand 233 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Beta strand 244 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Beta strand 250 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Beta strand 262 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Turn 267 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Helix 274 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Helix 278 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Beta strand 286 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Helix 294 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Beta strand 309 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Helix 314 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Helix 328 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Turn 343 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Beta strand 351 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5K36 +Q12149 UniProtKB Helix 356 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Helix 369 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Helix 386 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Helix 404 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Beta strand 413 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Beta strand 421 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Helix 436 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C0Y +Q12149 UniProtKB Helix 439 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Helix 460 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Helix 466 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Helix 480 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Helix 492 496 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Helix 498 515 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBJ +Q12149 UniProtKB Turn 534 536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +Q12149 UniProtKB Helix 539 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +Q12149 UniProtKB Turn 555 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OO1 +Q12149 UniProtKB Beta strand 570 572 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +Q12149 UniProtKB Turn 573 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +Q12149 UniProtKB Beta strand 582 585 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +Q12149 UniProtKB Beta strand 591 594 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +Q12149 UniProtKB Helix 596 611 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +Q12149 UniProtKB Helix 612 614 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +Q12149 UniProtKB Beta strand 617 619 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IFD +##sequence-region Q08746 1 203 +Q08746 UniProtKB Chain 1 203 . . . ID=PRO_0000185379;Note=Regulator of ribosome biosynthesis +Q08746 UniProtKB Beta strand 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +Q08746 UniProtKB Helix 23 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +Q08746 UniProtKB Beta strand 27 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +Q08746 UniProtKB Helix 36 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +Q08746 UniProtKB Helix 46 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +Q08746 UniProtKB Beta strand 70 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +Q08746 UniProtKB Beta strand 88 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5WXL +##sequence-region P38192 1 103 +P38192 UniProtKB Chain 1 103 . . . ID=PRO_0000202456;Note=Regulator of rDNA transcription protein 1 +P38192 UniProtKB Transmembrane 9 33 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38192 UniProtKB Transmembrane 40 57 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0C0W1 1 130 +P0C0W1 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:6814480;Dbxref=PMID:10601260,PMID:6814480 +P0C0W1 UniProtKB Chain 2 130 . . . ID=PRO_0000126623;Note=40S ribosomal protein S22-A +P0C0W1 UniProtKB Helix 6 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0W1 UniProtKB Beta strand 23 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0W1 UniProtKB Helix 32 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0W1 UniProtKB Beta strand 50 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0W1 UniProtKB Beta strand 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0W1 UniProtKB Beta strand 60 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0W1 UniProtKB Beta strand 70 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0W1 UniProtKB Helix 85 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0W1 UniProtKB Beta strand 94 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0W1 UniProtKB Beta strand 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0W1 UniProtKB Beta strand 101 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0W1 UniProtKB Beta strand 109 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0W1 UniProtKB Helix 113 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0C0W1 UniProtKB Beta strand 123 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P35997 1 82 +P35997 UniProtKB Chain 1 82 . . . ID=PRO_0000149066;Note=40S ribosomal protein S27-A +P35997 UniProtKB Zinc finger 37 59 . . . Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35997 UniProtKB Modified residue 40 40 . . . Note=S-methylcysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22650761;Dbxref=PMID:22650761 +P35997 UniProtKB Beta strand 7 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P35997 UniProtKB Helix 12 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P35997 UniProtKB Beta strand 22 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P35997 UniProtKB Beta strand 32 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P35997 UniProtKB Beta strand 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P35997 UniProtKB Beta strand 44 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P35997 UniProtKB Beta strand 57 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P35997 UniProtKB Beta strand 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P35997 UniProtKB Beta strand 68 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P35997 UniProtKB Beta strand 78 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P0C0X0 1 67 +P0C0X0 UniProtKB Chain 1 67 . . . ID=PRO_0000136843;Note=40S ribosomal protein S28-B +P0C0X0 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260 +##sequence-region P25443 1 254 +P25443 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921 +P25443 UniProtKB Chain 2 254 . . . ID=PRO_0000131684;Note=40S ribosomal protein S2 +P25443 UniProtKB Domain 76 139 . . . Note=S5 DRBM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00268 +P25443 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921 +P25443 UniProtKB Modified residue 11 11 . . . Note=Asymmetric dimethylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20035717,ECO:0000269|PubMed:22650761;Dbxref=PMID:20035717,PMID:22650761 +P25443 UniProtKB Modified residue 11 11 . . . Note=Omega-N-methylarginine%3B by HMT1%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20035717,ECO:0000269|PubMed:22650761;Dbxref=PMID:20035717,PMID:22650761 +P25443 UniProtKB Cross-link 33 33 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25443 UniProtKB Helix 40 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Helix 53 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Helix 66 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Beta strand 80 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Beta strand 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Beta strand 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Beta strand 98 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Beta strand 107 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Helix 121 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Beta strand 144 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Beta strand 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56 +P25443 UniProtKB Beta strand 153 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Beta strand 158 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Beta strand 165 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Beta strand 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Helix 182 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Beta strand 195 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Helix 207 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Helix 220 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Helix 227 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Helix 239 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P25443 UniProtKB Helix 244 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P0CX34 1 63 +P0CX34 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P0CX34 UniProtKB Chain 2 63 . . . ID=PRO_0000409763;Note=40S ribosomal protein S30-B +P0CX34 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX34 UniProtKB Modified residue 48 48 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region Q05942 1 220 +Q05942 UniProtKB Chain 1 220 . . . ID=PRO_0000097468;Note=Ribosome assembly protein 3 +Q05942 UniProtKB Compositional bias 29 42 . . . Note=Ser-rich +Q05942 UniProtKB Modified residue 83 83 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05942 UniProtKB Modified residue 88 88 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05942 UniProtKB Modified residue 99 99 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P53236 1 928 +P53236 UniProtKB Chain 1 928 . . . ID=PRO_0000211211;Note=Chromatin structure-remodeling complex subunit RSC1 +P53236 UniProtKB Domain 27 95 . . . Note=Bromo 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 +P53236 UniProtKB Domain 255 325 . . . Note=Bromo 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 +P53236 UniProtKB Domain 368 486 . . . Note=BAH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00370 +P53236 UniProtKB Modified residue 670 670 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53236 UniProtKB Mutagenesis 228 230 . . . Note=Loss of function. GRP->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10619019;Dbxref=PMID:10619019 +P53236 UniProtKB Sequence conflict 112 112 . . . Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53236 UniProtKB Sequence conflict 302 302 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53236 UniProtKB Sequence conflict 520 520 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53236 UniProtKB Sequence conflict 712 712 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53236 UniProtKB Sequence conflict 820 820 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02206 1 625 +Q02206 UniProtKB Chain 1 625 . . . ID=PRO_0000211213;Note=Chromatin structure-remodeling complex subunit RSC4 +Q02206 UniProtKB Domain 72 141 . . . Note=Bromo 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 +Q02206 UniProtKB Domain 205 275 . . . Note=Bromo 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 +Q02206 UniProtKB Modified residue 199 199 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02206 UniProtKB Modified residue 545 545 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q02206 UniProtKB Sequence conflict 390 390 . . . Note=K->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q02206 UniProtKB Sequence conflict 390 390 . . . Note=K->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q02206 UniProtKB Helix 47 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Helix 58 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Helix 74 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Helix 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Turn 86 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Helix 90 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Helix 102 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Helix 115 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Beta strand 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R10 +Q02206 UniProtKB Helix 139 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Helix 160 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Helix 169 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Helix 187 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Helix 196 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Beta strand 205 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0S +Q02206 UniProtKB Helix 211 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Turn 219 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Helix 223 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Helix 235 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Helix 250 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Helix 273 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Helix 293 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +Q02206 UniProtKB Turn 313 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R0Y +##sequence-region P33442 1 255 +P33442 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03122,ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P33442 UniProtKB Chain 2 255 . . . ID=PRO_0000153541;Note=40S ribosomal protein S1-A +P33442 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine%3B partial;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03122,ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P33442 UniProtKB Modified residue 245 245 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P33442 UniProtKB Modified residue 254 254 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P33442 UniProtKB Cross-link 248 248 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23248 +P33442 UniProtKB Turn 23 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Beta strand 29 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Beta strand 36 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Beta strand 41 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Beta strand 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Helix 57 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Beta strand 65 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Helix 71 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Beta strand 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V88 +P33442 UniProtKB Beta strand 83 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Beta strand 93 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3M +P33442 UniProtKB Beta strand 99 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Helix 107 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Beta strand 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P33442 UniProtKB Beta strand 120 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Beta strand 125 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Beta strand 130 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Beta strand 134 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Beta strand 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Beta strand 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P33442 UniProtKB Helix 159 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Beta strand 176 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Helix 180 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Turn 189 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Helix 192 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Beta strand 208 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Beta strand 215 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Helix 225 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P33442 UniProtKB Helix 229 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +##sequence-region P0CX37 1 236 +P0CX37 UniProtKB Chain 1 236 . . . ID=PRO_0000137342;Note=40S ribosomal protein S6-A +P0CX37 UniProtKB Modified residue 163 163 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX37 UniProtKB Cross-link 116 116 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX37 UniProtKB Cross-link 131 131 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX37 UniProtKB Cross-link 149 149 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX37 UniProtKB Cross-link 214 214 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX37 UniProtKB Beta strand 2 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Turn 8 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Beta strand 12 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Helix 21 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Helix 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Beta strand 31 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Beta strand 35 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Turn 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Beta strand 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Beta strand 49 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Helix 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Beta strand 69 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Beta strand 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P0CX37 UniProtKB Beta strand 87 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U51 +P0CX37 UniProtKB Beta strand 93 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Beta strand 106 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Helix 122 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Helix 138 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Turn 144 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P0CX37 UniProtKB Helix 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Helix 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Beta strand 160 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Beta strand 168 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Helix 181 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Beta strand 219 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX37 UniProtKB Turn 223 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P0CX40 1 200 +P0CX40 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18782943;Dbxref=PMID:18782943 +P0CX40 UniProtKB Chain 2 200 . . . ID=PRO_0000409766;Note=40S ribosomal protein S8-B +P0CX40 UniProtKB Modified residue 62 62 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX40 UniProtKB Modified residue 66 66 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX40 UniProtKB Modified residue 69 69 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P0CX40 UniProtKB Modified residue 73 73 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P0CX40 UniProtKB Modified residue 86 86 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX40 UniProtKB Modified residue 107 107 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P0CX40 UniProtKB Modified residue 154 154 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX40 UniProtKB Modified residue 155 155 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX40 UniProtKB Modified residue 158 158 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P0CX40 UniProtKB Modified residue 161 161 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX40 UniProtKB Sequence conflict 49 49 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08417 1 382 +Q08417 UniProtKB Chain 1 382 . . . ID=PRO_0000262738;Note=Sphingoid long-chain base transporter RSB1 +Q08417 UniProtKB Topological domain 1 34 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08417 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08417 UniProtKB Topological domain 56 57 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08417 UniProtKB Transmembrane 58 78 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08417 UniProtKB Topological domain 79 90 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08417 UniProtKB Transmembrane 91 111 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08417 UniProtKB Topological domain 112 135 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08417 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08417 UniProtKB Topological domain 157 171 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08417 UniProtKB Transmembrane 172 192 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08417 UniProtKB Topological domain 193 241 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08417 UniProtKB Transmembrane 242 262 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08417 UniProtKB Topological domain 263 281 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08417 UniProtKB Transmembrane 282 302 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08417 UniProtKB Topological domain 303 382 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08417 UniProtKB Glycosylation 3 3 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16407254;Dbxref=PMID:16407254 +Q08417 UniProtKB Glycosylation 6 6 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16407254;Dbxref=PMID:16407254 +Q08417 UniProtKB Mutagenesis 3 3 . . . Note=Increases sensitivity towards LCBs. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16407254;Dbxref=PMID:16407254 +Q08417 UniProtKB Mutagenesis 6 6 . . . Note=Increases sensitivity towards LCBs. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16407254;Dbxref=PMID:16407254 +##sequence-region P46974 1 1380 +P46974 UniProtKB Chain 1 1380 . . . ID=PRO_0000046861;Note=Respiration factor 2 +P46974 UniProtKB Zinc finger 151 173 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P46974 UniProtKB Zinc finger 179 202 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P46974 UniProtKB Compositional bias 64 67 . . . Note=Poly-Phe +P46974 UniProtKB Compositional bias 424 433 . . . Note=Poly-Gln +P46974 UniProtKB Modified residue 231 231 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46974 UniProtKB Modified residue 322 322 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P46974 UniProtKB Modified residue 544 544 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P46974 UniProtKB Modified residue 632 632 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P46974 UniProtKB Sequence conflict 1117 1118 . . . Note=NL->IF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46974 UniProtKB Sequence conflict 1131 1131 . . . Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40033 1 138 +##sequence-region Q03516 1 953 +Q03516 UniProtKB Chain 1 953 . . . ID=PRO_0000203348;Note=Uncharacterized protein RSN1 +Q03516 UniProtKB Transmembrane 23 43 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03516 UniProtKB Transmembrane 103 123 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03516 UniProtKB Transmembrane 148 168 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03516 UniProtKB Transmembrane 392 412 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03516 UniProtKB Transmembrane 435 455 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03516 UniProtKB Transmembrane 481 501 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03516 UniProtKB Transmembrane 540 560 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03516 UniProtKB Transmembrane 575 595 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03516 UniProtKB Transmembrane 599 619 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03516 UniProtKB Transmembrane 642 662 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03516 UniProtKB Transmembrane 666 686 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03516 UniProtKB Modified residue 949 949 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region P32905 1 252 +P32905 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03015,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:9298649;Dbxref=PMID:10601260,PMID:9298649 +P32905 UniProtKB Chain 2 252 . . . ID=PRO_0000134370;Note=40S ribosomal protein S0-A +P32905 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03015,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:9298649;Dbxref=PMID:10601260,PMID:9298649 +P32905 UniProtKB Beta strand 5 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U6F +P32905 UniProtKB Helix 11 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Turn 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Helix 31 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V88 +P32905 UniProtKB Beta strand 37 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Turn 42 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Beta strand 45 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Helix 50 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Beta strand 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Helix 70 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Beta strand 73 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Helix 80 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Beta strand 96 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Beta strand 106 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Beta strand 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P32905 UniProtKB Beta strand 119 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Turn 126 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Helix 130 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Turn 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Beta strand 143 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Beta strand 149 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P32905 UniProtKB Beta strand 157 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Beta strand 164 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Y +P32905 UniProtKB Helix 169 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Beta strand 183 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Beta strand 190 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P32905 UniProtKB Helix 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +##sequence-region P38120 1 278 +P38120 UniProtKB Transit peptide 1 10 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38120 UniProtKB Chain 11 278 . . . ID=PRO_0000030653;Note=37S ribosomal protein S9%2C mitochondrial +##sequence-region P40063 1 208 +P40063 UniProtKB Chain 1 208 . . . ID=PRO_0000202644;Note=Regulator of Ty1 transposition protein 105 +##sequence-region P40161 1 455 +P40161 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40161 UniProtKB Chain 2 455 . . . ID=PRO_0000203392;Note=Histone chaperone RTT106 +P40161 UniProtKB Domain 68 200 . . . Note=PH 1 +P40161 UniProtKB Domain 217 301 . . . Note=PH 2 +P40161 UniProtKB Region 2 67 . . . Note=Dimeric region +P40161 UniProtKB Region 68 301 . . . Note=Double PH domain +P40161 UniProtKB Region 315 455 . . . Note=Disordered acidic region +P40161 UniProtKB Compositional bias 351 448 . . . Note=Asp/Glu-rich +P40161 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40161 UniProtKB Modified residue 408 408 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40161 UniProtKB Modified residue 411 411 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40161 UniProtKB Modified residue 450 450 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40161 UniProtKB Mutagenesis 259 259 . . . Note=Decreases histone-binding. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22307274;Dbxref=PMID:22307274 +P40161 UniProtKB Mutagenesis 261 261 . . . Note=Impairs histone-binding. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22307274;Dbxref=PMID:22307274 +P40161 UniProtKB Mutagenesis 269 269 . . . Note=Impairs histone-binding. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22307274;Dbxref=PMID:22307274 +P40161 UniProtKB Mutagenesis 288 288 . . . Note=Decreases histone-binding. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22307274;Dbxref=PMID:22307274 +P40161 UniProtKB Mutagenesis 291 291 . . . Note=Impairs histone-binding. Y->A +P40161 UniProtKB Mutagenesis 294 294 . . . Note=Impairs histone-binding. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22307274;Dbxref=PMID:22307274 +P40161 UniProtKB Helix 5 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LH0 +P40161 UniProtKB Helix 11 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LH0 +P40161 UniProtKB Helix 27 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LH0 +P40161 UniProtKB Beta strand 60 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LH0 +P40161 UniProtKB Beta strand 71 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Beta strand 87 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Turn 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Beta strand 102 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Beta strand 111 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Helix 119 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Beta strand 123 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Beta strand 137 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Helix 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Beta strand 156 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Helix 162 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Helix 183 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Beta strand 220 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Beta strand 237 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Beta strand 249 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Helix 253 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Beta strand 256 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Beta strand 266 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Beta strand 280 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Helix 288 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +P40161 UniProtKB Helix 291 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FSS +##sequence-region Q07794 1 436 +Q07794 UniProtKB Chain 1 436 . . . ID=PRO_0000268738;Note=Histone acetyltransferase RTT109 +Q07794 UniProtKB Domain 2 404 . . . Note=Rtt109-type HAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01064 +Q07794 UniProtKB Mutagenesis 89 89 . . . Note=Losses histone acetylase activity. D->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17272723;Dbxref=PMID:17272723 +Q07794 UniProtKB Mutagenesis 287 288 . . . Note=Reduces histone acetylase activity. DD->AA%2CNN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17272723;Dbxref=PMID:17272723 +Q07794 UniProtKB Helix 3 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Beta strand 16 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Beta strand 27 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Beta strand 37 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q68 +Q07794 UniProtKB Beta strand 44 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Beta strand 60 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Beta strand 79 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Helix 100 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Helix 117 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Beta strand 121 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Helix 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Helix 144 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q66 +Q07794 UniProtKB Beta strand 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q66 +Q07794 UniProtKB Helix 164 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q66 +Q07794 UniProtKB Helix 169 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q66 +Q07794 UniProtKB Beta strand 175 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q66 +Q07794 UniProtKB Helix 182 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QM0 +Q07794 UniProtKB Beta strand 186 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Helix 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q66 +Q07794 UniProtKB Beta strand 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Helix 204 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Beta strand 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QM0 +Q07794 UniProtKB Helix 215 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Beta strand 239 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Helix 249 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Beta strand 259 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q68 +Q07794 UniProtKB Beta strand 264 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Helix 273 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CZ7 +Q07794 UniProtKB Helix 278 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Helix 289 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Turn 303 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Helix 308 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Helix 320 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Turn 324 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q66 +Q07794 UniProtKB Beta strand 328 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Beta strand 336 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Turn 346 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Helix 355 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Helix 373 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Beta strand 396 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2ZFN +Q07794 UniProtKB Helix 411 423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3Q66 +##sequence-region P53732 1 153 +P53732 UniProtKB Transit peptide 1 20 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53732 UniProtKB Chain 21 153 . . . ID=PRO_0000146483;Note=37S ribosomal protein S12%2C mitochondrial +##sequence-region P53064 1 558 +P53064 UniProtKB Chain 1 558 . . . ID=PRO_0000097512;Note=RNA polymerase-associated protein RTF1 +P53064 UniProtKB Domain 238 370 . . . Note=Plus3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00693 +P53064 UniProtKB Compositional bias 72 76 . . . Note=Poly-Glu +P53064 UniProtKB Modified residue 17 17 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53064 UniProtKB Modified residue 69 69 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53064 UniProtKB Modified residue 71 71 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P53064 UniProtKB Modified residue 477 477 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53064 UniProtKB Turn 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EMX +P53064 UniProtKB Beta strand 86 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EMX +P53064 UniProtKB Helix 89 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EMX +P53064 UniProtKB Helix 100 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5EMX +##sequence-region P0CX30 1 145 +P0CX30 UniProtKB Chain 1 145 . . . ID=PRO_0000409761;Note=40S ribosomal protein S23-B +P0CX30 UniProtKB Modified residue 64 64 . . . Note=3%2C4-dihydroxyproline;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24550462;Dbxref=PMID:24550462 +P0CX30 UniProtKB Cross-link 56 56 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX30 UniProtKB Mutagenesis 64 64 . . . Note=Lethal mutation. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24550462;Dbxref=PMID:24550462 +P0CX30 UniProtKB Mutagenesis 65 65 . . . Note=Lethal mutation. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24550462;Dbxref=PMID:24550462 +##sequence-region P41057 1 56 +P41057 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:18782943 +P41057 UniProtKB Chain 2 56 . . . ID=PRO_0000131032;Note=40S ribosomal protein S29-A +P41057 UniProtKB Metal binding 21 21 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41057 UniProtKB Metal binding 24 24 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41057 UniProtKB Metal binding 39 39 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41057 UniProtKB Metal binding 42 42 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41057 UniProtKB Modified residue 25 25 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41058 +P41057 UniProtKB Sequence conflict 7 7 . . . Note=W->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41057 UniProtKB Sequence conflict 14 14 . . . Note=Y->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41057 UniProtKB Beta strand 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P41057 UniProtKB Beta strand 13 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P41057 UniProtKB Helix 16 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P41057 UniProtKB Turn 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P41057 UniProtKB Beta strand 28 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P41057 UniProtKB Helix 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P41057 UniProtKB Helix 40 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P05750 1 240 +P05750 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:1544921,PMID:18782943 +P05750 UniProtKB Chain 2 240 . . . ID=PRO_0000130332;Note=40S ribosomal protein S3 +P05750 UniProtKB Domain 21 92 . . . Note=KH type-2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00118 +P05750 UniProtKB Modified residue 44 44 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P05750 UniProtKB Modified residue 70 70 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P05750 UniProtKB Modified residue 97 97 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P05750 UniProtKB Modified residue 129 129 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P05750 UniProtKB Modified residue 146 146 . . . Note=Omega-N-methylarginine%3B by SFM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22650761;Dbxref=PMID:22650761 +P05750 UniProtKB Modified residue 221 221 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P05750 UniProtKB Modified residue 231 231 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P05750 UniProtKB Cross-link 106 106 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P05750 UniProtKB Cross-link 132 132 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P05750 UniProtKB Cross-link 141 141 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P05750 UniProtKB Cross-link 151 151 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P05750 UniProtKB Cross-link 200 200 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P05750 UniProtKB Cross-link 212 212 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P05750 UniProtKB Sequence conflict 17 17 . . . Note=F->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05750 UniProtKB Sequence conflict 223 224 . . . Note=KD->NH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05750 UniProtKB Helix 15 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P05750 UniProtKB Turn 29 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P05750 UniProtKB Beta strand 34 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P05750 UniProtKB Beta strand 45 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P05750 UniProtKB Helix 55 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P05750 UniProtKB Helix 64 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P05750 UniProtKB Beta strand 83 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P05750 UniProtKB Helix 94 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P05750 UniProtKB Helix 98 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P05750 UniProtKB Helix 115 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P05750 UniProtKB Beta strand 134 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P05750 UniProtKB Beta strand 152 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P05750 UniProtKB Helix 163 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P05750 UniProtKB Beta strand 168 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P05750 UniProtKB Beta strand 181 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P05750 UniProtKB Helix 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +##sequence-region O13516 1 197 +O13516 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6814480;Dbxref=PMID:6814480 +O13516 UniProtKB Chain 2 197 . . . ID=PRO_0000132703;Note=40S ribosomal protein S9-A +O13516 UniProtKB Domain 107 181 . . . Note=S4 RNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00182 +O13516 UniProtKB Modified residue 184 184 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05755 +O13516 UniProtKB Cross-link 180 180 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05755 +O13516 UniProtKB Sequence conflict 20 22 . . . Note=ESS->QSB;Ontology_term=ECO:0000305;evidence=ECO:0000305 +O13516 UniProtKB Beta strand 16 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +O13516 UniProtKB Helix 21 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +O13516 UniProtKB Beta strand 37 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +O13516 UniProtKB Helix 40 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +O13516 UniProtKB Helix 67 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +O13516 UniProtKB Beta strand 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U6F +O13516 UniProtKB Beta strand 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +O13516 UniProtKB Turn 94 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +O13516 UniProtKB Helix 101 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +O13516 UniProtKB Helix 109 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +O13516 UniProtKB Beta strand 116 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +O13516 UniProtKB Helix 122 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +O13516 UniProtKB Beta strand 135 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +O13516 UniProtKB Helix 150 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +O13516 UniProtKB Beta strand 156 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Y +O13516 UniProtKB Beta strand 160 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +O13516 UniProtKB Helix 171 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +O13516 UniProtKB Turn 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region Q07979 1 502 +Q07979 UniProtKB Chain 1 502 . . . ID=PRO_0000097473;Note=Chromatin structure-remodeling complex protein RSC58 +##sequence-region Q12481 1 300 +Q12481 UniProtKB Chain 1 300 . . . ID=PRO_0000268165;Note=rRNA biogenesis protein RRP36 +Q12481 UniProtKB Coiled coil 184 248 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12481 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12481 UniProtKB Modified residue 41 41 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12481 UniProtKB Modified residue 42 42 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region Q3E811 1 62 +Q3E811 UniProtKB Chain 1 62 . . . ID=PRO_0000262879;Note=Regulator of rDNA transcription protein 15 +##sequence-region P05756 1 151 +P05756 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:6814480;Dbxref=PMID:10601260,PMID:6814480 +P05756 UniProtKB Chain 2 151 . . . ID=PRO_0000115689;Note=40S ribosomal protein S13 +P05756 UniProtKB Modified residue 32 32 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P05756 UniProtKB Cross-link 39 39 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P05756 UniProtKB Cross-link 43 43 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P05756 UniProtKB Sequence conflict 25 25 . . . Note=W->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05756 UniProtKB Sequence conflict 32 32 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P05756 UniProtKB Beta strand 4 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05756 UniProtKB Helix 30 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05756 UniProtKB Helix 47 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05756 UniProtKB Turn 57 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P05756 UniProtKB Helix 63 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05756 UniProtKB Beta strand 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05756 UniProtKB Helix 71 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05756 UniProtKB Helix 86 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05756 UniProtKB Turn 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P05756 UniProtKB Helix 109 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05756 UniProtKB Helix 143 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P06367 1 137 +P06367 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921 +P06367 UniProtKB Chain 2 137 . . . ID=PRO_0000123359;Note=40S ribosomal protein S14-A +P06367 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:22814378,PMID:10601260,PMID:1544921 +P06367 UniProtKB Sequence conflict 72 72 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06367 UniProtKB Sequence conflict 123 123 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06367 UniProtKB Beta strand 14 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P06367 UniProtKB Beta strand 19 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P06367 UniProtKB Beta strand 25 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P06367 UniProtKB Beta strand 30 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P06367 UniProtKB Beta strand 35 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P06367 UniProtKB Turn 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P06367 UniProtKB Beta strand 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4N +P06367 UniProtKB Beta strand 54 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P06367 UniProtKB Helix 57 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P06367 UniProtKB Beta strand 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P06367 UniProtKB Beta strand 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P06367 UniProtKB Beta strand 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4U +P06367 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P06367 UniProtKB Helix 99 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P06367 UniProtKB Turn 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P06367 UniProtKB Beta strand 111 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P06367 UniProtKB Turn 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4Z +##sequence-region P39938 1 119 +P39938 UniProtKB Chain 1 119 . . . ID=PRO_0000204528;Note=40S ribosomal protein S26-A +P39938 UniProtKB Beta strand 8 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V88 +P39938 UniProtKB Beta strand 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P39938 UniProtKB Turn 24 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P39938 UniProtKB Beta strand 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P39938 UniProtKB Helix 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P39938 UniProtKB Beta strand 37 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P39938 UniProtKB Turn 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V88 +P39938 UniProtKB Helix 50 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P39938 UniProtKB Beta strand 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P39938 UniProtKB Beta strand 67 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P39938 UniProtKB Helix 76 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P39938 UniProtKB Turn 89 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +##sequence-region P38711 1 82 +P38711 UniProtKB Chain 1 82 . . . ID=PRO_0000149067;Note=40S ribosomal protein S27-B +P38711 UniProtKB Zinc finger 37 59 . . . Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P05759 1 152 +P05759 UniProtKB Chain 1 76 . . . ID=PRO_0000396487;Note=Ubiquitin +P05759 UniProtKB Chain 77 152 . . . ID=PRO_0000137688;Note=40S ribosomal protein S31 +P05759 UniProtKB Domain 1 76 . . . Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 +P05759 UniProtKB Zinc finger 121 144 . . . Note=C4-type +P05759 UniProtKB Compositional bias 77 99 . . . Note=Lys-rich (highly basic) +P05759 UniProtKB Modified residue 122 122 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P05759 UniProtKB Cross-link 76 76 . . . Note=Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) +P05759 UniProtKB Mutagenesis 29 29 . . . Note=Deficiency in ubiquitin-protein conjugate formation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550 +P05759 UniProtKB Mutagenesis 48 48 . . . Note=Deficiency in ubiquitin-protein conjugate formation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550 +P05759 UniProtKB Mutagenesis 63 63 . . . Note=Deficiency in ubiquitin-protein conjugate formation. Loss of DNA repair function. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7615550;Dbxref=PMID:7615550 +P05759 UniProtKB Beta strand 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P05759 UniProtKB Beta strand 106 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05759 UniProtKB Beta strand 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P05759 UniProtKB Beta strand 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P05759 UniProtKB Beta strand 120 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P05759 UniProtKB Turn 124 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V88 +P05759 UniProtKB Beta strand 128 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P05759 UniProtKB Beta strand 139 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P0CX51 1 143 +P0CX51 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921 +P0CX51 UniProtKB Chain 2 143 . . . ID=PRO_0000111503;Note=40S ribosomal protein S16-A +P0CX51 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921 +P0CX51 UniProtKB Modified residue 34 34 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P0CX51 UniProtKB Modified residue 61 61 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX51 UniProtKB Modified residue 70 70 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX51 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX51 UniProtKB Cross-link 30 30 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX51 UniProtKB Cross-link 47 47 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX51 UniProtKB Cross-link 59 59 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX51 UniProtKB Beta strand 5 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX51 UniProtKB Beta strand 16 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX51 UniProtKB Beta strand 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX51 UniProtKB Turn 36 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX51 UniProtKB Beta strand 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P0CX51 UniProtKB Turn 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX51 UniProtKB Helix 46 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX51 UniProtKB Helix 57 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX51 UniProtKB Beta strand 63 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX51 UniProtKB Helix 76 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX51 UniProtKB Helix 99 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX51 UniProtKB Beta strand 114 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX51 UniProtKB Beta strand 129 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P14127 1 136 +P14127 UniProtKB Chain 1 136 . . . ID=PRO_0000141547;Note=40S ribosomal protein S17-B +##sequence-region P0CX55 1 146 +P0CX55 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|Ref.3;Dbxref=PMID:22814378,PMID:10601260 +P0CX55 UniProtKB Chain 2 146 . . . ID=PRO_0000132227;Note=40S ribosomal protein S18-A +P0CX55 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260,ECO:0000269|Ref.3;Dbxref=PMID:22814378,PMID:10601260 +P0CX55 UniProtKB Modified residue 48 48 . . . Note=N6-methyllysine%3B by RKM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22522802;Dbxref=PMID:22522802 +P0CX55 UniProtKB Cross-link 36 36 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX55 UniProtKB Cross-link 49 49 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX55 UniProtKB Cross-link 80 80 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX55 UniProtKB Cross-link 96 96 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX55 UniProtKB Beta strand 13 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX55 UniProtKB Beta strand 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX55 UniProtKB Beta strand 24 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX55 UniProtKB Helix 28 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX55 UniProtKB Helix 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX55 UniProtKB Helix 40 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX55 UniProtKB Turn 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX55 UniProtKB Helix 63 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX55 UniProtKB Turn 76 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX55 UniProtKB Helix 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX55 UniProtKB Beta strand 86 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX55 UniProtKB Beta strand 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX55 UniProtKB Helix 103 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX55 UniProtKB Helix 122 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX55 UniProtKB Beta strand 133 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V88 +P0CX55 UniProtKB Beta strand 139 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region Q3E7Y3 1 130 +Q3E7Y3 UniProtKB Chain 1 130 . . . ID=PRO_0000126624;Note=40S ribosomal protein S22-B +##sequence-region Q3E7X9 1 67 +Q3E7X9 UniProtKB Chain 1 67 . . . ID=PRO_0000136842;Note=40S ribosomal protein S28-A +Q3E7X9 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:10601260;Dbxref=PMID:22814378,PMID:10601260 +Q3E7X9 UniProtKB Beta strand 9 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E7X9 UniProtKB Beta strand 25 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E7X9 UniProtKB Beta strand 39 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E7X9 UniProtKB Beta strand 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +Q3E7X9 UniProtKB Beta strand 57 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P0CX33 1 63 +P0CX33 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10601260;Dbxref=PMID:10601260 +P0CX33 UniProtKB Chain 2 63 . . . ID=PRO_0000174009;Note=40S ribosomal protein S30-A +P0CX33 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX33 UniProtKB Modified residue 48 48 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX33 UniProtKB Turn 9 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX33 UniProtKB Helix 13 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX33 UniProtKB Helix 33 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX33 UniProtKB Turn 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4V88 +P0CX33 UniProtKB Beta strand 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P0CX36 1 261 +P0CX36 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6814480;Dbxref=PMID:6814480 +P0CX36 UniProtKB Chain 2 261 . . . ID=PRO_0000409764;Note=40S ribosomal protein S4-B +P0CX36 UniProtKB Domain 42 105 . . . Note=S4 RNA-binding +P0CX36 UniProtKB Modified residue 32 32 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P0CX36 UniProtKB Modified residue 115 115 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX36 UniProtKB Modified residue 247 247 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P0CX36 UniProtKB Cross-link 62 62 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX36 UniProtKB Cross-link 134 134 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX36 UniProtKB Cross-link 161 161 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX36 UniProtKB Cross-link 168 168 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX36 UniProtKB Cross-link 174 174 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX36 UniProtKB Cross-link 179 179 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX36 UniProtKB Cross-link 211 211 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX36 UniProtKB Cross-link 233 233 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P0CX38 1 236 +P0CX38 UniProtKB Chain 1 236 . . . ID=PRO_0000409765;Note=40S ribosomal protein S6-B +P0CX38 UniProtKB Modified residue 163 163 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX38 UniProtKB Cross-link 116 116 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX38 UniProtKB Cross-link 131 131 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX38 UniProtKB Cross-link 149 149 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX38 UniProtKB Cross-link 214 214 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P0CX38 UniProtKB Sequence conflict 181 181 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P0CX39 1 200 +P0CX39 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:18782943;Dbxref=PMID:10601260,PMID:18782943 +P0CX39 UniProtKB Chain 2 200 . . . ID=PRO_0000122258;Note=40S ribosomal protein S8-A +P0CX39 UniProtKB Modified residue 62 62 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX39 UniProtKB Modified residue 66 66 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P0CX39 UniProtKB Modified residue 69 69 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P0CX39 UniProtKB Modified residue 73 73 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P0CX39 UniProtKB Modified residue 86 86 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX39 UniProtKB Modified residue 107 107 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P0CX39 UniProtKB Modified residue 154 154 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX39 UniProtKB Modified residue 155 155 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX39 UniProtKB Modified residue 158 158 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P0CX39 UniProtKB Modified residue 161 161 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P0CX39 UniProtKB Sequence conflict 49 49 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0CX39 UniProtKB Sequence conflict 101 102 . . . Note=IV->MS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P0CX39 UniProtKB Beta strand 7 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Turn 13 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P0CX39 UniProtKB Helix 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Beta strand 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Beta strand 43 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Beta strand 53 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Beta strand 62 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Helix 68 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Beta strand 72 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Beta strand 80 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Helix 89 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Beta strand 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Helix 107 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Helix 138 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Beta strand 147 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3N +P0CX39 UniProtKB Helix 154 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Turn 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Beta strand 166 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Helix 173 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Beta strand 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P0CX39 UniProtKB Helix 186 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P05755 1 195 +P05755 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6814480;Dbxref=PMID:6814480 +P05755 UniProtKB Chain 2 195 . . . ID=PRO_0000132704;Note=40S ribosomal protein S9-B +P05755 UniProtKB Domain 107 181 . . . Note=S4 RNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00182 +P05755 UniProtKB Modified residue 184 184 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P05755 UniProtKB Cross-link 180 180 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P05755 UniProtKB Sequence conflict 20 22 . . . Note=ESS->QSB;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P02407 1 136 +P02407 UniProtKB Chain 1 136 . . . ID=PRO_0000141546;Note=40S ribosomal protein S17-A +P02407 UniProtKB Helix 7 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02407 UniProtKB Helix 21 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02407 UniProtKB Helix 28 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02407 UniProtKB Beta strand 39 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02407 UniProtKB Helix 44 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02407 UniProtKB Beta strand 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56 +P02407 UniProtKB Helix 73 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02407 UniProtKB Beta strand 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P02407 UniProtKB Helix 104 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region Q06639 1 885 +Q06639 UniProtKB Chain 1 885 . . . ID=PRO_0000114973;Note=Chromatin structure-remodeling complex protein RSC3 +Q06639 UniProtKB DNA binding 14 42 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +Q06639 UniProtKB Modified residue 95 95 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q06639 UniProtKB Modified residue 236 236 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06639 UniProtKB Mutagenesis 14 14 . . . Note=Complete inactivation. C->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11336698;Dbxref=PMID:11336698 +##sequence-region P40018 1 196 +P40018 UniProtKB Chain 1 196 . . . ID=PRO_0000125527;Note=Small nuclear ribonucleoprotein-associated protein B +P40018 UniProtKB Motif 105 132 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40018 UniProtKB Beta strand 10 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40018 UniProtKB Helix 13 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40018 UniProtKB Beta strand 19 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40018 UniProtKB Beta strand 29 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40018 UniProtKB Beta strand 43 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40018 UniProtKB Beta strand 78 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40018 UniProtKB Turn 89 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40018 UniProtKB Beta strand 92 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region O14464 1 93 +##sequence-region P38165 1 486 +P38165 UniProtKB Chain 1 486 . . . ID=PRO_0000127434;Note=Retrograde regulation protein 3 +P38165 UniProtKB Domain 285 344 . . . Note=bHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981 +P38165 UniProtKB Motif 27 35 . . . Note=9aaTAD 1 +P38165 UniProtKB Motif 189 197 . . . Note=9aaTAD 2 +P38165 UniProtKB Modified residue 81 81 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38165 UniProtKB Modified residue 123 123 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38165 UniProtKB Modified residue 142 142 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38165 UniProtKB Modified residue 150 150 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38165 UniProtKB Modified residue 227 227 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38165 UniProtKB Modified residue 236 236 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38165 UniProtKB Modified residue 241 241 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38165 UniProtKB Modified residue 269 269 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q12443 1 393 +Q12443 UniProtKB Chain 1 393 . . . ID=PRO_0000168169;Note=Reticulon-like protein 2 +Q12443 UniProtKB Topological domain 1 60 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12443 UniProtKB Transmembrane 61 81 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12443 UniProtKB Topological domain 82 149 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12443 UniProtKB Transmembrane 150 170 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12443 UniProtKB Topological domain 171 393 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12443 UniProtKB Domain 30 236 . . . Note=Reticulon;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00170 +Q12443 UniProtKB Modified residue 278 278 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12443 UniProtKB Glycosylation 137 137 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q05900 1 231 +Q05900 UniProtKB Chain 1 231 . . . ID=PRO_0000097528;Note=U1 small nuclear ribonucleoprotein C +Q05900 UniProtKB Zinc finger 4 36 . . . Note=Matrin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03153 +Q05900 UniProtKB Mutagenesis 13 13 . . . Note=Gives rise to unstable commitment complexes. L->A%2CD%2CE%2CF%2CG%2CH%2CK%2CP%2CR%2CS%2CT%2CW%2CY;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11172727,ECO:0000269|PubMed:15465910;Dbxref=PMID:11172727,PMID:15465910 +Q05900 UniProtKB Mutagenesis 13 13 . . . Note=No effect. L->C%2CI%2CM%2CN%2CQ%2CV;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11172727,ECO:0000269|PubMed:15465910;Dbxref=PMID:11172727,PMID:15465910 +##sequence-region P26786 1 190 +P26786 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921 +P26786 UniProtKB Chain 2 190 . . . ID=PRO_0000174212;Note=40S ribosomal protein S7-A +P26786 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10601260,ECO:0000269|PubMed:1544921;Dbxref=PMID:10601260,PMID:1544921 +P26786 UniProtKB Cross-link 124 124 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P26786 UniProtKB Sequence conflict 24 24 . . . Note=F->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P26786 UniProtKB Helix 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Beta strand 9 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Helix 16 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Helix 31 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Beta strand 35 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Beta strand 45 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Beta strand 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Beta strand 56 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Beta strand 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P26786 UniProtKB Helix 67 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Beta strand 71 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Helix 77 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Beta strand 87 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Beta strand 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Helix 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P26786 UniProtKB Helix 118 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Beta strand 135 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Beta strand 144 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V88 +P26786 UniProtKB Beta strand 148 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Beta strand 156 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P26786 UniProtKB Helix 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Turn 162 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Helix 166 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P26786 UniProtKB Beta strand 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P26786 UniProtKB Beta strand 181 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region P25632 1 483 +P25632 UniProtKB Chain 1 483 . . . ID=PRO_0000097474;Note=Chromatin structure-remodeling complex protein RSC6 +##sequence-region P28778 1 131 +P28778 UniProtKB Chain 1 131 . . . ID=PRO_0000087697;Note=37S ribosomal protein MRP17%2C mitochondrial +##sequence-region Q05543 1 409 +Q05543 UniProtKB Chain 1 409 . . . ID=PRO_0000268707;Note=Regulator of Ty1 transposition protein 103 +Q05543 UniProtKB Domain 1 135 . . . Note=CID;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00724 +Q05543 UniProtKB Compositional bias 267 296 . . . Note=Asp-rich +Q05543 UniProtKB Helix 5 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4 +Q05543 UniProtKB Helix 19 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4 +Q05543 UniProtKB Helix 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4 +Q05543 UniProtKB Helix 36 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4 +Q05543 UniProtKB Beta strand 49 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4 +Q05543 UniProtKB Helix 54 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4 +Q05543 UniProtKB Helix 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4 +Q05543 UniProtKB Helix 78 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4 +Q05543 UniProtKB Helix 87 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4 +Q05543 UniProtKB Helix 100 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4 +Q05543 UniProtKB Helix 121 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KM4 +##sequence-region P53305 1 110 +P53305 UniProtKB Chain 1 110 . . . ID=PRO_0000202847;Note=Mitochondrial 37S ribosomal protein S27 +P53305 UniProtKB Compositional bias 103 110 . . . Note=Poly-Lys +##sequence-region P19955 1 123 +P19955 UniProtKB Transit peptide 1 8 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2693936;Dbxref=PMID:2693936 +P19955 UniProtKB Chain 9 123 . . . ID=PRO_0000030587;Note=37S ribosomal protein YMR-31%2C mitochondrial +##sequence-region Q12751 1 981 +Q12751 UniProtKB Chain 1 981 . . . ID=PRO_0000203322;Note=RNA polymerase II assembly factor RTP1 +Q12751 UniProtKB Repeat 64 101 . . . Note=HEAT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12751 UniProtKB Repeat 161 199 . . . Note=HEAT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12751 UniProtKB Repeat 226 261 . . . Note=HEAT 3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12751 UniProtKB Repeat 366 403 . . . Note=HEAT 4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12751 UniProtKB Repeat 609 646 . . . Note=HEAT 5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12751 UniProtKB Repeat 655 692 . . . Note=HEAT 6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12751 UniProtKB Repeat 765 799 . . . Note=HEAT 7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12751 UniProtKB Repeat 800 836 . . . Note=HEAT 8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12751 UniProtKB Repeat 945 980 . . . Note=HEAT 9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12751 UniProtKB Compositional bias 49 56 . . . Note=Poly-Ser;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12751 UniProtKB Compositional bias 669 674 . . . Note=Poly-Ser;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12751 UniProtKB Compositional bias 815 818 . . . Note=Poly-Lys;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P17558 1 318 +P17558 UniProtKB Chain 1 318 . . . ID=PRO_0000030589;Note=37S ribosomal protein PET123%2C mitochondrial +##sequence-region Q12378 1 196 +Q12378 UniProtKB Chain 1 196 . . . ID=PRO_0000244439;Note=RNA polymerase II subunit B1 CTD phosphatase RTR2 +Q12378 UniProtKB Zinc finger 52 123 . . . Note=RTR1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812 +Q12378 UniProtKB Metal binding 75 75 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812 +Q12378 UniProtKB Metal binding 80 80 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812 +Q12378 UniProtKB Metal binding 99 99 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812 +Q12378 UniProtKB Metal binding 103 103 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812 +##sequence-region Q12330 1 94 +Q12330 UniProtKB Chain 1 94 . . . ID=PRO_0000125535;Note=Small nuclear ribonucleoprotein E +Q12330 UniProtKB Helix 13 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12330 UniProtKB Beta strand 27 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12330 UniProtKB Beta strand 34 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12330 UniProtKB Beta strand 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12330 UniProtKB Beta strand 52 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12330 UniProtKB Beta strand 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q12330 UniProtKB Helix 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P38850 1 1070 +P38850 UniProtKB Chain 1 1070 . . . ID=PRO_0000097502;Note=Regulator of Ty1 transposition protein 107 +P38850 UniProtKB Domain 2 103 . . . Note=BRCT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033 +P38850 UniProtKB Domain 117 213 . . . Note=BRCT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033 +P38850 UniProtKB Domain 260 352 . . . Note=BRCT 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033 +P38850 UniProtKB Domain 369 453 . . . Note=BRCT 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033 +P38850 UniProtKB Domain 829 910 . . . Note=BRCT 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033 +P38850 UniProtKB Domain 934 1049 . . . Note=BRCT 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033 +P38850 UniProtKB Modified residue 304 304 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38850 UniProtKB Modified residue 532 532 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38850 UniProtKB Modified residue 591 591 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38850 UniProtKB Modified residue 593 593 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38850 UniProtKB Modified residue 720 720 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38850 UniProtKB Modified residue 800 800 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38850 UniProtKB Modified residue 806 806 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38850 UniProtKB Helix 822 827 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Beta strand 837 844 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Helix 851 859 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Beta strand 862 864 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Helix 870 872 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Beta strand 876 878 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Helix 886 891 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Beta strand 899 901 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Helix 904 913 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Helix 927 930 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7I +P38850 UniProtKB Helix 937 942 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Beta strand 945 947 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Helix 949 952 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Beta strand 957 961 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Helix 968 977 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Beta strand 982 986 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Turn 988 990 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Helix 993 995 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Beta strand 1011 1015 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Helix 1019 1032 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Beta strand 1038 1041 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Helix 1043 1051 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +P38850 UniProtKB Beta strand 1063 1067 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T7K +##sequence-region P42847 1 217 +P42847 UniProtKB Transit peptide 1 59 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9151978;Dbxref=PMID:9151978 +P42847 UniProtKB Chain 60 217 . . . ID=PRO_0000030586;Note=37S ribosomal protein S18%2C mitochondrial +##sequence-region Q01163 1 450 +Q01163 UniProtKB Transit peptide 1 14 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01163 UniProtKB Chain 15 450 . . . ID=PRO_0000202743;Note=37S ribosomal protein S23%2C mitochondrial +Q01163 UniProtKB Nucleotide binding 150 157 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P51398 +##sequence-region P40496 1 264 +P40496 UniProtKB Chain 1 264 . . . ID=PRO_0000202972;Note=37S ribosomal protein S25%2C mitochondrial +##sequence-region P53292 1 345 +P53292 UniProtKB Transit peptide 1 27 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53292 UniProtKB Chain 28 345 . . . ID=PRO_0000202837;Note=37S ribosomal protein S35%2C mitochondrial +##sequence-region Q08281 1 1341 +Q08281 UniProtKB Chain 1 1341 . . . ID=PRO_0000223528;Note=Restriction of telomere capping protein 1 +Q08281 UniProtKB Repeat 207 248 . . . Note=WD 1 +Q08281 UniProtKB Repeat 256 296 . . . Note=WD 2 +Q08281 UniProtKB Repeat 305 342 . . . Note=WD 3 +Q08281 UniProtKB Repeat 367 406 . . . Note=WD 4 +Q08281 UniProtKB Repeat 439 486 . . . Note=WD 5 +Q08281 UniProtKB Repeat 489 527 . . . Note=WD 6 +Q08281 UniProtKB Repeat 843 883 . . . Note=WD 7 +Q08281 UniProtKB Repeat 1129 1169 . . . Note=WD 8 +Q08281 UniProtKB Repeat 1216 1255 . . . Note=WD 9 +Q08281 UniProtKB Zinc finger 1293 1335 . . . Note=RING-type%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +Q08281 UniProtKB Compositional bias 753 765 . . . Note=Poly-Asp +Q08281 UniProtKB Modified residue 1036 1036 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q08281 UniProtKB Modified residue 1080 1080 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q08281 UniProtKB Modified residue 1087 1087 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q08281 UniProtKB Modified residue 1089 1089 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q08281 UniProtKB Modified residue 1123 1123 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q08281 UniProtKB Modified residue 1133 1133 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q08281 UniProtKB Sequence conflict 393 393 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08281 UniProtKB Sequence conflict 393 393 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08281 UniProtKB Sequence conflict 548 548 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08281 UniProtKB Sequence conflict 548 548 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08281 UniProtKB Sequence conflict 1222 1222 . . . Note=D->DV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40084 1 226 +P40084 UniProtKB Chain 1 226 . . . ID=PRO_0000202653;Note=RNA polymerase II subunit B1 CTD phosphatase RTR1 +P40084 UniProtKB Zinc finger 50 136 . . . Note=RTR1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812 +P40084 UniProtKB Metal binding 73 73 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812 +P40084 UniProtKB Metal binding 78 78 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812 +P40084 UniProtKB Metal binding 112 112 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812 +P40084 UniProtKB Metal binding 116 116 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00812 +P40084 UniProtKB Mutagenesis 73 73 . . . Note=Loss of function. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18408053;Dbxref=PMID:18408053 +P40084 UniProtKB Mutagenesis 112 112 . . . Note=Loss of function%3B when associated with S-116. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18408053;Dbxref=PMID:18408053 +P40084 UniProtKB Mutagenesis 116 116 . . . Note=Loss of function%3B when associated with S-112. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18408053;Dbxref=PMID:18408053 +P40084 UniProtKB Helix 4 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y +P40084 UniProtKB Helix 13 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y +P40084 UniProtKB Helix 23 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y +P40084 UniProtKB Beta strand 38 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y +P40084 UniProtKB Beta strand 42 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y +P40084 UniProtKB Helix 45 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y +P40084 UniProtKB Helix 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y +P40084 UniProtKB Helix 57 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y +P40084 UniProtKB Helix 91 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y +P40084 UniProtKB Beta strand 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y +P40084 UniProtKB Helix 105 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y +P40084 UniProtKB Beta strand 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y +P40084 UniProtKB Helix 114 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y +P40084 UniProtKB Helix 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y +P40084 UniProtKB Turn 136 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y +P40084 UniProtKB Helix 146 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y +P40084 UniProtKB Helix 158 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y +P40084 UniProtKB Helix 168 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C2Y +##sequence-region Q00916 1 300 +Q00916 UniProtKB Chain 1 300 . . . ID=PRO_0000081886;Note=U1 small nuclear ribonucleoprotein 70 kDa homolog +Q00916 UniProtKB Domain 107 198 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +Q00916 UniProtKB Mutagenesis 18 98 . . . Note=Severely temperature-sensitive. Defective in pre-mRNA splicing. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7565787;Dbxref=PMID:7565787 +Q00916 UniProtKB Mutagenesis 18 93 . . . Note=Fails to complement the growth and splicing defective%2C temperature-sensitive phenotype of the null allele at 30 degrees Celsius. No association with U1 snRNP. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8643384;Dbxref=PMID:8643384 +Q00916 UniProtKB Mutagenesis 92 248 . . . Note=Associates with U1 snRNP. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7565787,ECO:0000269|PubMed:8643384;Dbxref=PMID:7565787,PMID:8643384 +Q00916 UniProtKB Mutagenesis 148 148 . . . Note=No splicing defects. Associates with U1 snRNP%3B when associated with T-150 and L-152. K->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7565787,ECO:0000269|PubMed:8643384;Dbxref=PMID:7565787,PMID:8643384 +Q00916 UniProtKB Mutagenesis 150 150 . . . Note=No splicing defects. Associates with U1 snRNP%3B when associated with L-148 and L-152. Y->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7565787,ECO:0000269|PubMed:8643384;Dbxref=PMID:7565787,PMID:8643384 +Q00916 UniProtKB Mutagenesis 152 152 . . . Note=No splicing defects. Associates with U1 snRNP%3B when associated with L-148 and T-150. F->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7565787,ECO:0000269|PubMed:8643384;Dbxref=PMID:7565787,PMID:8643384 +##sequence-region P32605 1 298 +P32605 UniProtKB Chain 1 298 . . . ID=PRO_0000081891;Note=U1 small nuclear ribonucleoprotein A +P32605 UniProtKB Domain 2 113 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P32605 UniProtKB Domain 227 298 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P32605 UniProtKB Mutagenesis 4 4 . . . Note=Sensitive in DMS protection of U1 snRNA%3B when associated with 6-I-N-7. L->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781 +P32605 UniProtKB Mutagenesis 6 7 . . . Note=Sensitive in DMS protection of U1 snRNA%3B when associated with I-4. FQ->IN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781 +P32605 UniProtKB Mutagenesis 63 63 . . . Note=Sensitive in DMS protection of U1 snRNA%3B when associated with 65-D--L-67. L->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781 +P32605 UniProtKB Mutagenesis 65 67 . . . Note=Sensitive in DMS protection of U1 snRNA%3B when associated with I-63. VSI->DIL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781 +P32605 UniProtKB Mutagenesis 69 72 . . . Note=Sensitive in DMS protection of U1 snRNA. RSSK->LKTM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781 +P32605 UniProtKB Mutagenesis 74 75 . . . Note=Sensitive in DMS protection of U1 snRNA%3B when associated with 79-V-I-80. TN->RG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781 +P32605 UniProtKB Mutagenesis 79 80 . . . Note=Sensitive in DMS protection of U1 snRNA%3B when associated with 74-R-G-75. LT->VI;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781 +P32605 UniProtKB Mutagenesis 228 228 . . . Note=Splicing defects%3B when associated with 230-F--T-232. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781 +P32605 UniProtKB Mutagenesis 230 232 . . . Note=Splicing defects%3B when associated with I-228. LIQ->FLT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781 +P32605 UniProtKB Mutagenesis 258 260 . . . Note=Splicing defects. VSV->PGH;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781 +P32605 UniProtKB Mutagenesis 262 263 . . . Note=Splicing defects%3B when associated with F-268. NL->DI;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781 +P32605 UniProtKB Mutagenesis 268 268 . . . Note=Splicing defects%3B when associated with 262-D-I-263. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781 +P32605 UniProtKB Mutagenesis 291 293 . . . Note=Splicing defects%3B when associated with S-295. DVT->AMK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781 +P32605 UniProtKB Mutagenesis 295 295 . . . Note=Splicing defects%3B when associated with 291-A--K-293. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8849781;Dbxref=PMID:8849781 +P32605 UniProtKB Sequence conflict 1 3 . . . Note=MSA->MTNKNR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08963 1 238 +Q08963 UniProtKB Chain 1 238 . . . ID=PRO_0000074189;Note=U2 small nuclear ribonucleoprotein A' +Q08963 UniProtKB Repeat 53 74 . . . Note=LRR 1 +Q08963 UniProtKB Repeat 75 95 . . . Note=LRR 2 +Q08963 UniProtKB Repeat 97 118 . . . Note=LRR 3 +Q08963 UniProtKB Domain 132 170 . . . Note=LRRCT +Q08963 UniProtKB Helix 5 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q08963 UniProtKB Beta strand 13 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q08963 UniProtKB Beta strand 34 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q08963 UniProtKB Helix 47 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q08963 UniProtKB Beta strand 55 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q08963 UniProtKB Beta strand 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q08963 UniProtKB Beta strand 100 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q08963 UniProtKB Helix 111 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q08963 UniProtKB Beta strand 126 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q08963 UniProtKB Helix 133 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q08963 UniProtKB Helix 140 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q08963 UniProtKB Beta strand 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P54999 1 86 +P54999 UniProtKB Chain 1 86 . . . ID=PRO_0000125544;Note=Small nuclear ribonucleoprotein F +P54999 UniProtKB Helix 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N9R +P54999 UniProtKB Beta strand 25 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N9R +P54999 UniProtKB Beta strand 36 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N9R +P54999 UniProtKB Turn 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N9R +P54999 UniProtKB Beta strand 51 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N9R +P54999 UniProtKB Beta strand 63 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N9R +P54999 UniProtKB Beta strand 70 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N9R +P54999 UniProtKB Helix 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N9R +P54999 UniProtKB Beta strand 78 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1N9R +##sequence-region P25343 1 265 +P25343 UniProtKB Chain 1 265 . . . ID=PRO_0000192960;Note=Reduced viability upon starvation protein 161 +P25343 UniProtKB Domain 15 239 . . . Note=BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00361 +P25343 UniProtKB Coiled coil 126 193 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25343 UniProtKB Sequence conflict 95 95 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P22470 1 610 +P22470 UniProtKB Chain 1 610 . . . ID=PRO_0000056162;Note=Protein SAN1 +P22470 UniProtKB Zinc finger 240 280 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +##sequence-region P53330 1 157 +P53330 UniProtKB Chain 1 157 . . . ID=PRO_0000097501;Note=Regulator of Ty1 transposition protein 102 +P53330 UniProtKB Modified residue 77 77 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53330 UniProtKB Modified residue 122 122 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53330 UniProtKB Helix 3 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +P53330 UniProtKB Beta strand 25 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +P53330 UniProtKB Beta strand 60 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +P53330 UniProtKB Beta strand 86 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +##sequence-region Q02608 1 121 +Q02608 UniProtKB Chain 1 121 . . . ID=PRO_0000167326;Note=37S ribosomal protein S16%2C mitochondrial +##sequence-region P53047 1 317 +P53047 UniProtKB Chain 1 317 . . . ID=PRO_0000097510;Note=Protein RTA1 +P53047 UniProtKB Topological domain 1 16 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53047 UniProtKB Transmembrane 17 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53047 UniProtKB Topological domain 38 64 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53047 UniProtKB Transmembrane 65 85 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53047 UniProtKB Topological domain 86 99 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53047 UniProtKB Transmembrane 100 120 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53047 UniProtKB Topological domain 121 142 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53047 UniProtKB Transmembrane 143 163 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53047 UniProtKB Topological domain 164 178 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53047 UniProtKB Transmembrane 179 199 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53047 UniProtKB Topological domain 200 214 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53047 UniProtKB Transmembrane 215 235 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53047 UniProtKB Topological domain 236 259 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53047 UniProtKB Transmembrane 260 280 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53047 UniProtKB Topological domain 281 317 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53047 UniProtKB Sequence conflict 234 234 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53850 1 401 +P53850 UniProtKB Chain 1 401 . . . ID=PRO_0000203384;Note=Restriction of telomere capping protein 4 +P53850 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q12108 1 567 +Q12108 UniProtKB Chain 1 567 . . . ID=PRO_0000237657;Note=Restriction of telomere capping protein 5 +##sequence-region P32608 1 588 +P32608 UniProtKB Chain 1 588 . . . ID=PRO_0000194312;Note=Retrograde regulation protein 2 +##sequence-region Q04947 1 295 +Q04947 UniProtKB Chain 1 295 . . . ID=PRO_0000168168;Note=Reticulon-like protein 1 +Q04947 UniProtKB Topological domain 1 50 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04947 UniProtKB Transmembrane 51 73 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04947 UniProtKB Topological domain 74 142 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04947 UniProtKB Transmembrane 143 163 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04947 UniProtKB Topological domain 164 295 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04947 UniProtKB Domain 20 220 . . . Note=Reticulon;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00170 +Q04947 UniProtKB Coiled coil 265 295 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04947 UniProtKB Compositional bias 9 16 . . . Note=Poly-Gln +Q04947 UniProtKB Modified residue 186 186 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q04947 UniProtKB Modified residue 219 219 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04947 UniProtKB Modified residue 232 232 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40962 1 232 +P40962 UniProtKB Chain 1 232 . . . ID=PRO_0000046850;Note=Zinc finger protein RTS2 +P40962 UniProtKB Zinc finger 24 48 . . . Note=C2H2-type +##sequence-region P20606 1 190 +P20606 UniProtKB Chain 1 190 . . . ID=PRO_0000206275;Note=Small COPII coat GTPase SAR1 +P20606 UniProtKB Nucleotide binding 30 37 . . . Note=GTP +P20606 UniProtKB Nucleotide binding 73 76 . . . Note=GTP +P20606 UniProtKB Nucleotide binding 132 135 . . . Note=GTP +P20606 UniProtKB Modified residue 155 155 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P20606 UniProtKB Modified residue 157 157 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P20606 UniProtKB Cross-link 133 133 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P20606 UniProtKB Mutagenesis 32 32 . . . Note=No cell growth at 37 degrees Celsius. Decreases GTP binding and ER-to-Golgi vesicle transport. D->G;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7822237,ECO:0000269|PubMed:8889833,ECO:0000269|PubMed:9756629;Dbxref=PMID:7822237,PMID:8889833,PMID:9756629 +P20606 UniProtKB Mutagenesis 36 36 . . . Note=No cell growth at 23 or 37 degrees Celsius. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7822237;Dbxref=PMID:7822237 +P20606 UniProtKB Mutagenesis 54 54 . . . Note=No cell growth at 23 or 37 degrees Celsius. Decreases GTP binding and impairs ER-to-Golgi vesicle transport. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7822237,ECO:0000269|PubMed:9756629;Dbxref=PMID:7822237,PMID:9756629 +P20606 UniProtKB Mutagenesis 73 73 . . . Note=No cell growth at 23 or 37 degrees Celsius. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7822237;Dbxref=PMID:7822237 +P20606 UniProtKB Mutagenesis 77 77 . . . Note=No cell growth at 23 or 37 degrees Celsius. Impairs ER-to-Golgi vesicle transport. H->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7822237,ECO:0000269|PubMed:9756629;Dbxref=PMID:7822237,PMID:9756629 +P20606 UniProtKB Mutagenesis 112 112 . . . Note=Decreases guanine nucleotide binding. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:8889833,ECO:0000269|PubMed:9756629;Dbxref=PMID:8889833,PMID:9756629 +P20606 UniProtKB Mutagenesis 132 132 . . . Note=No cell growth at 37 degrees Celsius. N->I;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7822237,ECO:0000269|PubMed:8889833;Dbxref=PMID:7822237,PMID:8889833 +P20606 UniProtKB Mutagenesis 171 171 . . . Note=Normal cell growth. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7822237;Dbxref=PMID:7822237 +P20606 UniProtKB Beta strand 25 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P20606 UniProtKB Helix 36 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P20606 UniProtKB Beta strand 58 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P20606 UniProtKB Beta strand 67 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P20606 UniProtKB Helix 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P20606 UniProtKB Helix 84 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P20606 UniProtKB Beta strand 93 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P20606 UniProtKB Helix 103 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P20606 UniProtKB Helix 106 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P20606 UniProtKB Helix 120 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P20606 UniProtKB Beta strand 127 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P20606 UniProtKB Beta strand 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QTV +P20606 UniProtKB Helix 142 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P20606 UniProtKB Beta strand 166 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P20606 UniProtKB Turn 173 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P20606 UniProtKB Helix 179 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +##sequence-region P28707 1 216 +P28707 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P28707 UniProtKB Chain 2 216 . . . ID=PRO_0000218959;Note=Co-chaperone protein SBA1 +P28707 UniProtKB Domain 5 108 . . . Note=CS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00547 +P28707 UniProtKB Repeat 141 156 . . . . +P28707 UniProtKB Repeat 160 174 . . . . +P28707 UniProtKB Compositional bias 203 213 . . . Note=Poly-Glu +P28707 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P28707 UniProtKB Beta strand 17 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9 +P28707 UniProtKB Beta strand 23 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9 +P28707 UniProtKB Beta strand 33 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9 +P28707 UniProtKB Beta strand 44 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9 +P28707 UniProtKB Beta strand 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9 +P28707 UniProtKB Beta strand 67 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9 +P28707 UniProtKB Beta strand 77 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9 +P28707 UniProtKB Beta strand 91 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9 +P28707 UniProtKB Beta strand 98 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9 +P28707 UniProtKB Beta strand 107 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9 +P28707 UniProtKB Beta strand 115 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9 +P28707 UniProtKB Turn 121 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9 +P28707 UniProtKB Beta strand 127 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2CG9 +##sequence-region P06105 1 1222 +P06105 UniProtKB Chain 1 1222 . . . ID=PRO_0000050128;Note=Protein SCP160 +P06105 UniProtKB Domain 177 249 . . . Note=KH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117 +P06105 UniProtKB Domain 634 702 . . . Note=KH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117 +P06105 UniProtKB Domain 712 771 . . . Note=KH 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117 +P06105 UniProtKB Domain 782 851 . . . Note=KH 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117 +P06105 UniProtKB Domain 861 929 . . . Note=KH 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117 +P06105 UniProtKB Domain 939 1001 . . . Note=KH 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117 +P06105 UniProtKB Domain 1153 1216 . . . Note=KH 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117 +P06105 UniProtKB Modified residue 50 50 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P06105 UniProtKB Modified residue 54 54 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06105 UniProtKB Modified residue 63 63 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P06105 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P06105 UniProtKB Modified residue 87 87 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06105 UniProtKB Modified residue 89 89 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P06105 UniProtKB Modified residue 630 630 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P06105 UniProtKB Modified residue 1112 1112 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P06105 UniProtKB Sequence conflict 287 287 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06105 UniProtKB Sequence conflict 303 303 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06105 UniProtKB Sequence conflict 308 308 . . . Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06105 UniProtKB Sequence conflict 330 330 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06105 UniProtKB Sequence conflict 362 362 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06105 UniProtKB Sequence conflict 411 411 . . . Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06105 UniProtKB Sequence conflict 884 884 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06105 UniProtKB Sequence conflict 886 886 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06105 UniProtKB Sequence conflict 960 960 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06105 UniProtKB Sequence conflict 1067 1067 . . . Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06105 UniProtKB Sequence conflict 1087 1087 . . . Note=A->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P52871 1 88 +P52871 UniProtKB Chain 1 88 . . . ID=PRO_0000157262;Note=Protein transport protein SBH2 +P52871 UniProtKB Topological domain 1 61 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52871 UniProtKB Transmembrane 62 82 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40541 1 1150 +P40541 UniProtKB Chain 1 1150 . . . ID=PRO_0000120191;Note=Cohesin subunit SCC3 +P40541 UniProtKB Domain 367 457 . . . Note=SCD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00750 +P40541 UniProtKB Coiled coil 305 349 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40541 UniProtKB Compositional bias 44 48 . . . Note=Poly-Glu +P40541 UniProtKB Compositional bias 65 70 . . . Note=Poly-Asp +P40541 UniProtKB Modified residue 28 28 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40541 UniProtKB Modified residue 628 628 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40541 UniProtKB Sequence conflict 939 939 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40541 UniProtKB Helix 675 678 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 680 691 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 700 707 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 721 736 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Turn 742 744 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 747 761 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 764 788 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 798 808 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 810 819 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 826 835 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 837 839 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 840 843 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 844 846 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 849 854 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 858 876 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Turn 890 893 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 894 911 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Turn 917 919 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 920 946 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 953 962 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 969 989 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 1002 1005 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 1016 1032 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 1038 1045 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Turn 1046 1050 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +P40541 UniProtKB Helix 1053 1058 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UVJ +##sequence-region P03878 1 556 +P03878 UniProtKB Region 1 240 . . . Note=COX1 exons 1 to 4 encoded +P03878 UniProtKB Region 241 556 . . . Note=COX1 intron 4 encoded +P03878 UniProtKB Natural variant 457 458 . . . Note=In strain: D273-10B. IS->KT +P03878 UniProtKB Mutagenesis 362 362 . . . Note=Confers mRNA maturase activity. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6285204;Dbxref=PMID:6285204 +P03878 UniProtKB Sequence conflict 57 57 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03878 UniProtKB Sequence conflict 69 69 . . . Note=F->CT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03878 UniProtKB Sequence conflict 224 224 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03878 UniProtKB Sequence conflict 315 315 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03878 UniProtKB Sequence conflict 320 320 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P03877 1 415 +P03877 UniProtKB Transmembrane 16 36 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P03877 UniProtKB Transmembrane 57 77 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P03877 UniProtKB Region 1 81 . . . Note=COX1 exons 1 to 3 encoded +P03877 UniProtKB Region 82 415 . . . Note=COX1 intron 3 encoded +P03877 UniProtKB Compositional bias 88 92 . . . Note=Poly-Asn +P03877 UniProtKB Compositional bias 284 291 . . . Note=Poly-Asn +P03877 UniProtKB Natural variant 55 55 . . . Note=In strain: Capensis / YB4237. F->Y +P03877 UniProtKB Natural variant 60 60 . . . Note=In strain: Capensis / YB4237. V->A +P03877 UniProtKB Natural variant 71 71 . . . Note=In strain: Capensis / YB4237. V->W +P03877 UniProtKB Natural variant 76 76 . . . Note=In strain: Capensis / YB4237. I->M +P03877 UniProtKB Natural variant 399 399 . . . Note=In strain: Capensis / YB4237. R->M +P03877 UniProtKB Sequence conflict 122 122 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03877 UniProtKB Sequence conflict 176 176 . . . Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03877 UniProtKB Sequence conflict 200 200 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03877 UniProtKB Sequence conflict 217 218 . . . Note=TI->NQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03877 UniProtKB Sequence conflict 247 248 . . . Note=GM->IL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03877 UniProtKB Sequence conflict 269 269 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03877 UniProtKB Sequence conflict 284 284 . . . Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P03877 UniProtKB Sequence conflict 380 380 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P11792 1 824 +P11792 UniProtKB Chain 1 824 . . . ID=PRO_0000086638;Note=Serine/threonine-protein kinase SCH9 +P11792 UniProtKB Domain 185 361 . . . Note=C2 +P11792 UniProtKB Domain 412 671 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P11792 UniProtKB Domain 672 748 . . . Note=AGC-kinase C-terminal +P11792 UniProtKB Nucleotide binding 418 426 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P11792 UniProtKB Compositional bias 227 267 . . . Note=Asn-rich +P11792 UniProtKB Active site 538 538 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P11792 UniProtKB Binding site 441 441 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P11792 UniProtKB Modified residue 570 570 . . . Note=Phosphothreonine%3B by PKH1 or PKH2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17560372;Dbxref=PMID:17560372 +P11792 UniProtKB Modified residue 711 711 . . . Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17560372;Dbxref=PMID:17560372 +P11792 UniProtKB Modified residue 723 723 . . . Note=Phosphothreonine%3B by TORC1;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:17560372;Dbxref=PMID:17330950,PMID:19779198,PMID:17560372 +P11792 UniProtKB Modified residue 726 726 . . . Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:17560372;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:17560372 +P11792 UniProtKB Modified residue 737 737 . . . Note=Phosphothreonine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17560372;Dbxref=PMID:17560372 +P11792 UniProtKB Modified residue 758 758 . . . Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17560372;Dbxref=PMID:17560372 +P11792 UniProtKB Modified residue 765 765 . . . Note=Phosphoserine%3B by TORC1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17560372;Dbxref=PMID:17560372 +P11792 UniProtKB Sequence conflict 366 366 . . . Note=I->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11792 UniProtKB Sequence conflict 751 751 . . . Note=N->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P10663 1 115 +P10663 UniProtKB Chain 1 115 . . . ID=PRO_0000131017;Note=37S ribosomal protein MRP2%2C mitochondrial +##sequence-region P47150 1 247 +P47150 UniProtKB Transit peptide 1 26 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47150 UniProtKB Chain 27 247 . . . ID=PRO_0000124541;Note=37S ribosomal protein S7%2C mitochondrial +##sequence-region P12686 1 339 +P12686 UniProtKB Transit peptide 1 37 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9151978;Dbxref=PMID:9151978 +P12686 UniProtKB Chain 38 339 . . . ID=PRO_0000030585;Note=37S ribosomal protein MRP13%2C mitochondrial +P12686 UniProtKB Sequence conflict 114 114 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12686 UniProtKB Sequence conflict 328 334 . . . Note=PPPQEST->HSQDQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53733 1 91 +P53733 UniProtKB Chain 1 91 . . . ID=PRO_0000130025;Note=37S ribosomal protein S19%2C mitochondrial +##sequence-region P47141 1 266 +P47141 UniProtKB Chain 1 266 . . . ID=PRO_0000203110;Note=37S ribosomal protein S26%2C mitochondrial +##sequence-region P32607 1 177 +P32607 UniProtKB Chain 1 177 . . . ID=PRO_0000127433;Note=Retrograde regulation protein 1 +P32607 UniProtKB Domain 11 96 . . . Note=bHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981 +P32607 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32607 UniProtKB Modified residue 52 52 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32607 UniProtKB Modified residue 60 60 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32607 UniProtKB Sequence conflict 105 113 . . . Note=REEVELMVK->KRGGGTDGE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03940 1 463 +Q03940 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15525518;Dbxref=PMID:15525518 +Q03940 UniProtKB Chain 2 463 . . . ID=PRO_0000165661;Note=RuvB-like protein 1 +Q03940 UniProtKB Nucleotide binding 79 86 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03940 UniProtKB Modified residue 2 2 . . . Note=N-acetylvaline;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15525518;Dbxref=PMID:15525518 +Q03940 UniProtKB Mutagenesis 85 85 . . . Note=Lethal. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278922;Dbxref=PMID:11278922 +Q03940 UniProtKB Mutagenesis 312 312 . . . Note=Lethal. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278922;Dbxref=PMID:11278922 +##sequence-region P40204 1 77 +P40204 UniProtKB Chain 1 77 . . . ID=PRO_0000125552;Note=Small nuclear ribonucleoprotein G +P40204 UniProtKB Beta strand 8 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40204 UniProtKB Beta strand 13 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40204 UniProtKB Turn 20 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40204 UniProtKB Beta strand 23 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40204 UniProtKB Beta strand 28 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40204 UniProtKB Beta strand 38 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40204 UniProtKB Beta strand 59 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40204 UniProtKB Turn 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P40204 UniProtKB Beta strand 68 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P32915 1 480 +P32915 UniProtKB Chain 1 480 . . . ID=PRO_0000131789;Note=Protein transport protein SEC61 +P32915 UniProtKB Topological domain 1 32 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Transmembrane 33 55 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Topological domain 56 75 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Transmembrane 76 95 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Topological domain 96 119 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Transmembrane 120 141 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Topological domain 142 146 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Transmembrane 147 167 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Topological domain 168 212 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Transmembrane 213 224 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Topological domain 225 240 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Transmembrane 241 260 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Topological domain 261 290 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Transmembrane 291 311 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Topological domain 312 361 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Transmembrane 362 381 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Topological domain 382 416 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Transmembrane 417 434 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Topological domain 435 437 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Transmembrane 438 459 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Topological domain 460 480 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32915 UniProtKB Mutagenesis 273 273 . . . Note=Severe growth defect. K->P%2CG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15631991;Dbxref=PMID:15631991 +P32915 UniProtKB Mutagenesis 275 275 . . . Note=Severe growth defect. R->D%2CG%2CP%2CQ%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15631991;Dbxref=PMID:15631991 +P32915 UniProtKB Mutagenesis 275 275 . . . Note=Severe growth defect%3B lowers SRP-dependent and SRP-independent translocation. R->E%2CF%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15631991;Dbxref=PMID:15631991 +P32915 UniProtKB Mutagenesis 276 276 . . . Note=Severe growth defect. G->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15631991;Dbxref=PMID:15631991 +P32915 UniProtKB Mutagenesis 405 405 . . . Note=Severe growth defect. K->D%2CE%2CP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15631991;Dbxref=PMID:15631991 +P32915 UniProtKB Mutagenesis 406 406 . . . Note=Severe growth defect%3B lowers SRP-dependent translocation. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15631991;Dbxref=PMID:15631991 +P32915 UniProtKB Mutagenesis 406 406 . . . Note=Severe growth defect%3B lowers SRP-dependent and SRP-independent translocation. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15631991;Dbxref=PMID:15631991 +P32915 UniProtKB Mutagenesis 406 406 . . . Note=Severe growth defect. R->H%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15631991;Dbxref=PMID:15631991 +##sequence-region P52870 1 82 +P52870 UniProtKB Chain 1 82 . . . ID=PRO_0000157261;Note=Protein transport protein SBH1 +P52870 UniProtKB Topological domain 1 53 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P52870 UniProtKB Transmembrane 54 74 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12158 1 566 +Q12158 UniProtKB Chain 1 566 . . . ID=PRO_0000097881;Note=Sister chromatid cohesion protein 1 +Q12158 UniProtKB Compositional bias 258 261 . . . Note=Poly-Asp +Q12158 UniProtKB Site 180 181 . . . Note=Cleavage%3B by ESP1 +Q12158 UniProtKB Site 268 269 . . . Note=Cleavage%3B by ESP1 +Q12158 UniProtKB Modified residue 161 161 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12158 UniProtKB Modified residue 175 175 . . . Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11371343;Dbxref=PMID:11371343 +Q12158 UniProtKB Modified residue 210 210 . . . Note=N6-acetyllysine%3B by ECO1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574 +Q12158 UniProtKB Modified residue 263 263 . . . Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11371343;Dbxref=PMID:11371343 +Q12158 UniProtKB Modified residue 307 307 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12158 UniProtKB Modified residue 354 354 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12158 UniProtKB Mutagenesis 175 175 . . . Note=Reduces phosphorylation. Abolishes phosphorylation%3B when associated with A-263. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11371343;Dbxref=PMID:11371343 +Q12158 UniProtKB Mutagenesis 180 180 . . . Note=Abolishes cleavage by ESP1%3B when associated with D-268. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10403247;Dbxref=PMID:10403247 +Q12158 UniProtKB Mutagenesis 210 210 . . . Note=Loss of acetylation by ECO1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574 +Q12158 UniProtKB Mutagenesis 252 252 . . . Note=No effect on acetylation by ECO1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574 +Q12158 UniProtKB Mutagenesis 263 263 . . . Note=Reduces phosphorylation. Abolishes phosphorylation%3B when associated with A-175. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11371343;Dbxref=PMID:11371343 +Q12158 UniProtKB Mutagenesis 268 268 . . . Note=Abolishes first cleavage by ESP1. Abolishes all cleavage by ESP1%3B when associated with D-180. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10403247;Dbxref=PMID:10403247 +Q12158 UniProtKB Mutagenesis 290 290 . . . Note=No effect on acetylation by ECO1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574 +Q12158 UniProtKB Mutagenesis 310 310 . . . Note=No effect on acetylation by ECO1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574 +Q12158 UniProtKB Mutagenesis 319 319 . . . Note=No effect on acetylation by ECO1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574 +Q12158 UniProtKB Mutagenesis 324 324 . . . Note=No effect on acetylation by ECO1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11864574;Dbxref=PMID:11864574 +Q12158 UniProtKB Helix 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +Q12158 UniProtKB Helix 44 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +Q12158 UniProtKB Turn 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +Q12158 UniProtKB Beta strand 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +Q12158 UniProtKB Helix 69 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +Q12158 UniProtKB Beta strand 134 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FRP +Q12158 UniProtKB Helix 484 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +Q12158 UniProtKB Helix 504 509 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +Q12158 UniProtKB Helix 522 537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +Q12158 UniProtKB Beta strand 539 544 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +Q12158 UniProtKB Beta strand 551 555 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +Q12158 UniProtKB Helix 557 559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +##sequence-region P34758 1 872 +P34758 UniProtKB Chain 1 872 . . . ID=PRO_0000097621;Note=Protein SCD5 +P34758 UniProtKB Repeat 405 424 . . . Note=1-1 +P34758 UniProtKB Repeat 439 458 . . . Note=1-2 +P34758 UniProtKB Repeat 479 498 . . . Note=1-3 +P34758 UniProtKB Repeat 534 545 . . . Note=2-1 +P34758 UniProtKB Repeat 564 575 . . . Note=2-2 +P34758 UniProtKB Repeat 593 604 . . . Note=2-3 +P34758 UniProtKB Repeat 608 619 . . . Note=2-4 +P34758 UniProtKB Repeat 623 634 . . . Note=2-5 +P34758 UniProtKB Repeat 636 647 . . . Note=2-5 +P34758 UniProtKB Repeat 650 661 . . . Note=2-7 +P34758 UniProtKB Repeat 683 694 . . . Note=2-8 +P34758 UniProtKB Repeat 717 728 . . . Note=2-9 +P34758 UniProtKB Region 405 448 . . . Note=3 X 20 AA approximate repeats +P34758 UniProtKB Region 534 728 . . . Note=9 X 12 AA approximate repeats +P34758 UniProtKB Modified residue 564 564 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P21801 1 266 +P21801 UniProtKB Transit peptide 1 20 . . . Note=Mitochondrion +P21801 UniProtKB Chain 21 266 . . . ID=PRO_0000010353;Note=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit%2C mitochondrial +P21801 UniProtKB Domain 36 127 . . . Note=2Fe-2S ferredoxin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00465 +P21801 UniProtKB Domain 169 199 . . . Note=4Fe-4S ferredoxin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00711 +P21801 UniProtKB Metal binding 87 87 . . . Note=Iron-sulfur 1 (2Fe-2S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21801 UniProtKB Metal binding 92 92 . . . Note=Iron-sulfur 1 (2Fe-2S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21801 UniProtKB Metal binding 95 95 . . . Note=Iron-sulfur 1 (2Fe-2S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21801 UniProtKB Metal binding 107 107 . . . Note=Iron-sulfur 1 (2Fe-2S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21801 UniProtKB Metal binding 179 179 . . . Note=Iron-sulfur 2 (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21801 UniProtKB Metal binding 182 182 . . . Note=Iron-sulfur 2 (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21801 UniProtKB Metal binding 185 185 . . . Note=Iron-sulfur 2 (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21801 UniProtKB Metal binding 189 189 . . . Note=Iron-sulfur 3 (3Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21801 UniProtKB Metal binding 236 236 . . . Note=Iron-sulfur 3 (3Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21801 UniProtKB Metal binding 242 242 . . . Note=Iron-sulfur 3 (3Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21801 UniProtKB Metal binding 246 246 . . . Note=Iron-sulfur 2 (4Fe-4S);Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21801 UniProtKB Binding site 194 194 . . . Note=Ubiquinone%3B shared with DHSD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P21801 UniProtKB Mutagenesis 260 266 . . . Note=Abolishes SDH activity and complex assembly. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1390628;Dbxref=PMID:1390628 +P21801 UniProtKB Mutagenesis 260 260 . . . Note=Abolishes SDH activity. No effect on complex assembly and stability%3B when associated with T-261. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1390628;Dbxref=PMID:1390628 +P21801 UniProtKB Mutagenesis 261 261 . . . Note=Abolishes SDH activity. No effect on complex assembly and stability%3B when associated with T-260. K->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1390628;Dbxref=PMID:1390628 +##sequence-region Q07534 1 307 +Q07534 UniProtKB Chain 1 307 . . . ID=PRO_0000240707;Note=Solute carrier family 25 member 38 homolog +Q07534 UniProtKB Transmembrane 14 39 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03064 +Q07534 UniProtKB Transmembrane 62 88 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03064 +Q07534 UniProtKB Transmembrane 121 146 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03064 +Q07534 UniProtKB Transmembrane 174 197 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03064 +Q07534 UniProtKB Transmembrane 225 251 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03064 +Q07534 UniProtKB Transmembrane 280 298 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03064 +Q07534 UniProtKB Repeat 8 87 . . . Note=Solcar 1 +Q07534 UniProtKB Repeat 115 199 . . . Note=Solcar 2 +Q07534 UniProtKB Repeat 221 305 . . . Note=Solcar 3 +##sequence-region P43612 1 1002 +P43612 UniProtKB Chain 1 1002 . . . ID=PRO_0000097561;Note=SIT4-associating protein SAP155 +P43612 UniProtKB Compositional bias 938 997 . . . Note=Asn-rich +P43612 UniProtKB Modified residue 58 58 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P43612 UniProtKB Modified residue 255 255 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P43612 UniProtKB Modified residue 613 613 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P43612 UniProtKB Modified residue 618 618 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P43612 UniProtKB Sequence conflict 663 663 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43612 UniProtKB Sequence conflict 663 663 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43612 UniProtKB Sequence conflict 668 668 . . . Note=T->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43612 UniProtKB Sequence conflict 674 690 . . . Note=DLFKIKLYDTRIVSKIM->TYSKSNYMIRDCFQNN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43612 UniProtKB Sequence conflict 815 824 . . . Note=ELISPDIQVI->DYISRYSSN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P17121 1 654 +P17121 UniProtKB Chain 1 654 . . . ID=PRO_0000056764;Note=GTPase-activating protein SAC7 +P17121 UniProtKB Domain 134 393 . . . Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172 +P17121 UniProtKB Modified residue 37 37 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P17121 UniProtKB Modified residue 46 46 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P17121 UniProtKB Modified residue 435 435 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P17121 UniProtKB Modified residue 491 491 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P17121 UniProtKB Modified residue 632 632 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q12136 1 610 +Q12136 UniProtKB Chain 1 610 . . . ID=PRO_0000114330;Note=Something about silencing protein 10 +Q12136 UniProtKB Compositional bias 75 86 . . . Note=Poly-Glu +Q12136 UniProtKB Compositional bias 167 172 . . . Note=Poly-Glu +Q12136 UniProtKB Compositional bias 360 365 . . . Note=Poly-Glu +Q12136 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12136 UniProtKB Modified residue 314 314 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12136 UniProtKB Modified residue 316 316 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12136 UniProtKB Modified residue 336 336 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12136 UniProtKB Modified residue 339 339 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12136 UniProtKB Modified residue 477 477 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region Q04002 1 1493 +Q04002 UniProtKB Chain 1 1493 . . . ID=PRO_0000218603;Note=Sister chromatid cohesion protein 2 +Q04002 UniProtKB Repeat 695 732 . . . Note=HEAT 1 +Q04002 UniProtKB Repeat 734 771 . . . Note=HEAT 2 +Q04002 UniProtKB Repeat 806 843 . . . Note=HEAT 3 +Q04002 UniProtKB Repeat 1132 1169 . . . Note=HEAT 4 +Q04002 UniProtKB Repeat 1244 1281 . . . Note=HEAT 5 +Q04002 UniProtKB Modified residue 43 43 . . . Note=Phosphoserine%3B in mutant scc2-8A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Modified residue 67 67 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Modified residue 74 74 . . . Note=Phosphoserine%3B in mutant scc2-8A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Modified residue 127 127 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Modified residue 157 157 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Modified residue 162 162 . . . Note=Phosphoserine%3B in mutant scc2-8A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Modified residue 163 163 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Modified residue 231 231 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Modified residue 236 236 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Modified residue 305 305 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Modified residue 320 320 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Modified residue 360 360 . . . Note=Phosphothreonine%3B in mutant scc2-8A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Modified residue 753 753 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Modified residue 1179 1179 . . . Note=Phosphoserine%3B in mutant scc2-8A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Modified residue 1182 1182 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Modified residue 1183 1183 . . . Note=Phosphoserine%3B in mutant scc2-8A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Modified residue 1185 1185 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 67 67 . . . Note=In ssc2-8A%3B mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43%2C Ser-74%2C Ser-162%2C Ser-360%2C Ser-1179 and Ser-1183%3B when assocated with A-127%3B A-157%3B A-163%3B A-231%3B A-236%3B A-305 and A-320. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 67 67 . . . Note=In ssc2-8E%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-127%3B E-157%3B E-163%3B E-231%3B E-236%3B E-305 and E-320. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 127 127 . . . Note=In ssc2-8A%3B mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43%2C Ser-74%2C Ser-162%2C Ser-360%2C Ser-1179 and Ser-1183%3B when assocated with A-67%3B A-157%3B A-163%3B A-231%3B A-236%3B A-305 and A-320. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 127 127 . . . Note=In ssc2-8E%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-67%3B E-157%3B E-163%3B E-231%3B E-236%3B E-305 and E-320. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 157 157 . . . Note=In ssc2-8A%3B mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43%2C Ser-74%2C Ser-162%2C Ser-360%2C Ser-1179 and Ser-1183%3B when assocated with A-67%3B A-127%3B A-163%3B A-231%3B A-236%3B A-305 and A-320. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 157 157 . . . Note=In ssc2-8E%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-67%3B E-127%3B E-163%3B E-231%3B E-236%3B E-305 and E-320. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 163 163 . . . Note=In ssc2-8A%3B mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43%2C Ser-74%2C Ser-162%2C Ser-360%2C Ser-1179 and Ser-1183%3B when assocated with A-67%3B A-127%3B A-157%3B A-231%3B A-236%3B A-305 and A-320. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 163 163 . . . Note=In ssc2-8E%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-67%3B E-127%3B E-157%3B E-231%3B E-236%3B E-305 and E-320. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 231 231 . . . Note=In ssc2-8A%3B mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43%2C Ser-74%2C Ser-162%2C Ser-360%2C Ser-1179 and Ser-1183%3B when assocated with A-67%3B A-127%3B A-157%3B A-163%3B A-236%3B A-305 and A-320. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 231 231 . . . Note=In ssc2-8E%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-67%3B E-127%3B E-157%3B E-163%3B E-236%3B E-305 and E-320. In ssc2-2NE%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-236%3B E-305 and E-320. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 236 236 . . . Note=In ssc2-8A%3B mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43%2C Ser-74%2C Ser-162%2C Ser-360%2C Ser-1179 and Ser-1183%3B when assocated with A-67%3B A-127%3B A-157%3B A-163%3B A-231%3B A-305 and A-320. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 236 236 . . . Note=In ssc2-8E%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-67%3B E-127%3B E-157%3B E-163%3B E-231%3B E-305 and E-320. In ssc2-2NE%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-231%3B E-305 and E-320. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 305 305 . . . Note=In ssc2-8A%3B mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43%3B S-74%3B S-162%3B S-360%3B S-1179 and Ser-1183%3B when assocated with A-67%3B A-127%3B A-157%3B A-163%3B A-231%3B A-236 and A-320. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 305 305 . . . Note=In ssc2-8E%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-67%3B E-127%3B E-157%3B E-163%3B E-231%3B E-236 and E-320. In ssc2-2NE%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-231%3B E-236 and E-320. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 320 320 . . . Note=In ssc2-8A%3B mimics unphosphorylated form and leads to novel phosphorylation sites at S-43%3B S-74%3B S-162%3B S-360%3B S-1179 and S-1183%3B when assocated with A-67%3B A-127%3B A-157%3B A-163%3B A-231%3B A-236 and A-305. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 320 320 . . . Note=In ssc2-8E%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-67%3B E-127%3B E-157%3B E-163%3B E-231%3B E-236 and E-305. In ssc2-2NE%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%2C and decreased stability of the MCD1 cohesin subunit in mitotic cells%3B when associated with E-231%3B E-236 and E-305. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 753 753 . . . Note=Mimics constitutive phosphorylation and causes inviability through protein instability. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 1182 1182 . . . Note=In ssc2-CE%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%3B when associated with E-1185. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Mutagenesis 1185 1185 . . . Note=In ssc2-CE%3B mimics constitutive phosphorylation%2C retains normal SCC2-SCC4 interactions and chromatin association%2C but exhibits decreased viability%2C sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU)%3B when associated with E-1182. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26354421;Dbxref=PMID:26354421 +Q04002 UniProtKB Turn 4 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +Q04002 UniProtKB Helix 14 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +Q04002 UniProtKB Turn 18 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +Q04002 UniProtKB Helix 32 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +Q04002 UniProtKB Beta strand 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +Q04002 UniProtKB Beta strand 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +Q04002 UniProtKB Helix 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +Q04002 UniProtKB Beta strand 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +Q04002 UniProtKB Turn 106 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +Q04002 UniProtKB Helix 112 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +Q04002 UniProtKB Beta strand 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +##sequence-region P40090 1 624 +P40090 UniProtKB Chain 1 624 . . . ID=PRO_0000193217;Note=MAU2 chromatid cohesion factor homolog +P40090 UniProtKB Mutagenesis 256 256 . . . Note=In scc4m7%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with A-298%3B D-299%3B A-313%3B A-324%3B D-327%3B and D-331. L->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942 +P40090 UniProtKB Mutagenesis 298 298 . . . Note=In scc4m7%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with K-256%3B D-299%3B A-313%3B A-324%3B D-327%3B and D-331. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942 +P40090 UniProtKB Mutagenesis 299 299 . . . Note=In scc4m7%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with K-256%3B A-298%3B A-313%3B A-324%3B D-327%3B and D-331. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942 +P40090 UniProtKB Mutagenesis 313 313 . . . Note=In scc4m7%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with K-256%3B A-298%3B D-299%3B A-324%3B D-327%3B and D-331. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942 +P40090 UniProtKB Mutagenesis 324 324 . . . Note=In scc4m35%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with A-327%3B A-331%3B A-540 and A-541. In scc4m7%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with K-256%3B A-298%3B D-299%3B A-313%3B D-327%3B and D-331. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942 +P40090 UniProtKB Mutagenesis 327 327 . . . Note=In scc4m35%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with A-324%3B A-331%3B A-540 and A-541. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942 +P40090 UniProtKB Mutagenesis 327 327 . . . Note=In scc4m7%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with K-256%3B A-298%3B D-299%3B A-313%3B A-324 and D-331. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942 +P40090 UniProtKB Mutagenesis 331 331 . . . Note=In scc4m35%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with A-324%3B A-327%3B A-540 and A-541. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942 +P40090 UniProtKB Mutagenesis 331 331 . . . Note=In scc4m7%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with K-256%3B A-298%3B D-299%3B A-313%3B A-324 and D-327. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942 +P40090 UniProtKB Mutagenesis 540 540 . . . Note=In scc4m35%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with A-324%3B A-327%3B A-331 and A-541. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942 +P40090 UniProtKB Mutagenesis 541 541 . . . Note=In scc4m35%3B eliminates centromeric localization of SCC2 in mitotic cells and reduces association of the cohesin subunit SCC1 with the centromere and pericentromere%3B when associated with A-324%3B A-327%3B A-331 and A-540. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26038942;Dbxref=PMID:26038942 +P40090 UniProtKB Beta strand 7 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 10 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Turn 27 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 34 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 62 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 83 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Turn 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 107 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 120 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 128 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 151 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 174 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 193 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 215 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 226 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 231 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 253 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Turn 273 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Beta strand 278 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Beta strand 286 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 293 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 298 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Turn 313 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 320 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 350 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 396 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 413 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 427 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Turn 450 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 453 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 475 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 480 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Turn 496 498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 507 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 543 556 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 561 574 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 575 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 582 599 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +P40090 UniProtKB Helix 602 619 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4XDN +##sequence-region P45978 1 349 +P45978 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P45978 UniProtKB Chain 2 349 . . . ID=PRO_0000097622;Note=Protein SCD6 +P45978 UniProtKB Domain 193 229 . . . Note=DFDF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00845 +P45978 UniProtKB Motif 241 257 . . . Note=FFD box +P45978 UniProtKB Motif 260 280 . . . Note=TFG box +P45978 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P03882 1 235 +P03882 UniProtKB Chain 1 235 . . . ID=PRO_0000192785;Note=Intron-encoded endonuclease I-SceI +P03882 UniProtKB Helix 6 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Beta strand 10 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OOR +P03882 UniProtKB Helix 17 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Helix 31 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Beta strand 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Beta strand 50 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R7M +P03882 UniProtKB Beta strand 56 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Helix 65 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Helix 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Beta strand 84 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Beta strand 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0X +P03882 UniProtKB Beta strand 95 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Helix 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Helix 110 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Beta strand 117 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Helix 128 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Helix 135 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Beta strand 146 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Beta strand 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OOR +P03882 UniProtKB Beta strand 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Helix 169 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Beta strand 187 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Beta strand 195 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Helix 202 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Helix 205 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Helix 213 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +P03882 UniProtKB Helix 218 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3C0W +##sequence-region P32564 1 187 +P32564 UniProtKB Chain 1 187 . . . ID=PRO_0000097626;Note=Protein SCM4 +P32564 UniProtKB Transmembrane 11 31 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32564 UniProtKB Transmembrane 45 65 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32564 UniProtKB Transmembrane 80 100 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32564 UniProtKB Transmembrane 162 182 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04951 1 389 +Q04951 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04951 UniProtKB Propeptide 19 29 . . . ID=PRO_0000011901;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9748433;Dbxref=PMID:9748433 +Q04951 UniProtKB Chain 30 389 . . . ID=PRO_0000011902;Note=Probable family 17 glucosidase SCW10 +Q04951 UniProtKB Compositional bias 65 134 . . . Note=Ser-rich +Q04951 UniProtKB Active site 326 326 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04951 UniProtKB Active site 380 380 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04951 UniProtKB Glycosylation 279 279 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04951 UniProtKB Sequence conflict 38 39 . . . Note=AQ->QE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03323 1 175 +Q03323 UniProtKB Chain 1 175 . . . ID=PRO_0000114686;Note=COMPASS component SDC1 +Q03323 UniProtKB Region 121 162 . . . Note=DPY-30 +##sequence-region P13856 1 272 +P13856 UniProtKB Chain 1 269 . . . ID=PRO_0000082691;Note=Ras-related protein RSR1 +P13856 UniProtKB Propeptide 270 272 . . . ID=PRO_0000281342;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13856 UniProtKB Nucleotide binding 10 17 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13856 UniProtKB Nucleotide binding 57 61 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13856 UniProtKB Nucleotide binding 116 119 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13856 UniProtKB Motif 32 40 . . . Note=Effector region;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13856 UniProtKB Modified residue 269 269 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P13856 UniProtKB Lipidation 269 269 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P46654 1 252 +P46654 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03015,ECO:0000269|PubMed:10601260,ECO:0000269|Ref.4;Dbxref=PMID:10601260 +P46654 UniProtKB Chain 2 252 . . . ID=PRO_0000134371;Note=40S ribosomal protein S0-B +P46654 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_03015,ECO:0000269|PubMed:10601260,ECO:0000269|Ref.4;Dbxref=PMID:10601260 +##sequence-region P10662 1 321 +P10662 UniProtKB Transit peptide 1 13 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10662 UniProtKB Chain 14 321 . . . ID=PRO_0000087698;Note=37S ribosomal protein MRP1%2C mitochondrial +P10662 UniProtKB Sequence conflict 113 113 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P10662 UniProtKB Sequence conflict 319 319 . . . Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32902 1 394 +P32902 UniProtKB Transit peptide 1 25 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32902 UniProtKB Chain 26 394 . . . ID=PRO_0000134345;Note=37S ribosomal protein MRP4%2C mitochondrial +##sequence-region P33759 1 307 +P33759 UniProtKB Transit peptide 1 13 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33759 UniProtKB Chain 14 307 . . . ID=PRO_0000131688;Note=37S ribosomal protein S5%2C mitochondrial +P33759 UniProtKB Domain 144 208 . . . Note=S5 DRBM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00268 +##sequence-region Q03799 1 155 +Q03799 UniProtKB Chain 1 155 . . . ID=PRO_0000126599;Note=37S ribosomal protein S8%2C mitochondrial +##sequence-region Q12100 1 620 +Q12100 UniProtKB Chain 1 620 . . . ID=PRO_0000248408;Note=Probable serine/threonine-protein kinase RTK1 +Q12100 UniProtKB Domain 302 575 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12100 UniProtKB Nucleotide binding 308 316 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12100 UniProtKB Active site 430 430 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q12100 UniProtKB Binding site 330 330 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12100 UniProtKB Modified residue 58 58 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12100 UniProtKB Modified residue 60 60 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12100 UniProtKB Modified residue 216 216 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12100 UniProtKB Cross-link 334 334 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P53289 1 263 +P53289 UniProtKB Chain 1 263 . . . ID=PRO_0000202835;Note=Protein phosphatase type 2A regulatory subunit RTS3 +P53289 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53289 UniProtKB Modified residue 192 192 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53289 UniProtKB Modified residue 214 214 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53289 UniProtKB Modified residue 238 238 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53289 UniProtKB Natural variant 20 20 . . . Note=V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.1 +P53289 UniProtKB Natural variant 201 201 . . . Note=P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.1 +##sequence-region Q12242 1 671 +Q12242 UniProtKB Chain 1 671 . . . ID=PRO_0000269644;Note=UBA domain-containing protein RUP1 +Q12242 UniProtKB Domain 1 41 . . . Note=UBA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212 +Q12242 UniProtKB Coiled coil 432 501 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12242 UniProtKB Compositional bias 354 399 . . . Note=Glu-rich +Q12242 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P39743 1 482 +P39743 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P39743 UniProtKB Chain 2 482 . . . ID=PRO_0000192961;Note=Reduced viability upon starvation protein 167 +P39743 UniProtKB Domain 17 254 . . . Note=BAR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00361 +P39743 UniProtKB Domain 421 482 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P39743 UniProtKB Coiled coil 31 64 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39743 UniProtKB Coiled coil 174 204 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39743 UniProtKB Compositional bias 292 427 . . . Note=Ala/Gly/Pro-rich +P39743 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P39743 UniProtKB Modified residue 299 299 . . . Note=Phosphoserine%3B by FUS3 and PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12857883;Dbxref=PMID:12857883 +P39743 UniProtKB Modified residue 321 321 . . . Note=Phosphoserine%3B by FUS3 and PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12857883;Dbxref=PMID:12857883 +P39743 UniProtKB Modified residue 379 379 . . . Note=Phosphoserine%3B by FUS3 and PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12857883;Dbxref=PMID:12857883 +P39743 UniProtKB Cross-link 242 242 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P39743 UniProtKB Cross-link 481 481 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P38255 1 430 +P38255 UniProtKB Chain 1 430 . . . ID=PRO_0000202482;Note=Transcriptional regulatory protein RXT2 +##sequence-region P50110 1 327 +P50110 UniProtKB Chain 1 327 . . . ID=PRO_0000072630;Note=Sorting assembly machinery 37 kDa subunit +P50110 UniProtKB Transmembrane 17 33 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50110 UniProtKB Transmembrane 247 265 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40856 1 1058 +P40856 UniProtKB Chain 1 1058 . . . ID=PRO_0000046106;Note=SIT4-associating protein SAP185 +P40856 UniProtKB Cross-link 20 20 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P89114 1 91 +P89114 UniProtKB Chain 1 91 . . . ID=PRO_0000269645;Note=Pachytene arrest protein SAE3 +##sequence-region P38352 1 637 +P38352 UniProtKB Chain 1 637 . . . ID=PRO_0000206658;Note=SCF-associated factor 1 +P38352 UniProtKB Domain 14 63 . . . Note=F-box +P38352 UniProtKB Repeat 109 202 . . . Note=RCC1 1 +P38352 UniProtKB Repeat 565 635 . . . Note=RCC1 2 +P38352 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38352 UniProtKB Modified residue 266 266 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38352 UniProtKB Mutagenesis 24 24 . . . Note=In saf1-5%3B impairs the interaction with SKP1. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885 +P38352 UniProtKB Mutagenesis 35 35 . . . Note=In saf1-6%3B impairs the interaction with SKP1. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885 +P38352 UniProtKB Mutagenesis 263 263 . . . Note=In saf1-4%3B impairs the protein stability%3B when associated with K-264. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885 +P38352 UniProtKB Mutagenesis 264 264 . . . Note=In saf1-4%3B impairs the protein stability%3B when associated with K-263. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885 +P38352 UniProtKB Mutagenesis 372 372 . . . Note=In saf1-1%3B impairs the protein stability. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885 +P38352 UniProtKB Mutagenesis 387 387 . . . Note=In saf1-2%3B impairs the protein stability. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885 +P38352 UniProtKB Mutagenesis 580 580 . . . Note=In saf1-3%3B impairs the protein stability. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17517885;Dbxref=PMID:17517885 +##sequence-region P20840 1 650 +P20840 UniProtKB Signal peptide 1 19 . . . . +P20840 UniProtKB Chain 20 627 . . . ID=PRO_0000022265;Note=Alpha-agglutinin +P20840 UniProtKB Propeptide 628 650 . . . ID=PRO_0000022266;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20840 UniProtKB Repeat 339 378 . . . Note=1 +P20840 UniProtKB Repeat 384 423 . . . Note=2 +P20840 UniProtKB Region 216 322 . . . Note=Ig-like fold domain important for alpha-agglutinin activity%2C contributing to a functional binding site for a-agglutinin +P20840 UniProtKB Region 339 423 . . . Note=2 X 40 AA tandem repeats +P20840 UniProtKB Compositional bias 331 359 . . . Note=Ser/Thr-rich +P20840 UniProtKB Site 348 348 . . . Note=Not glycosylated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Lipidation 627 627 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20840 UniProtKB Glycosylation 79 79 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20840 UniProtKB Glycosylation 109 109 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20840 UniProtKB Glycosylation 135 135 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20840 UniProtKB Glycosylation 248 248 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 282 282 . . . Note=O-linked (Man...) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 289 289 . . . Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 299 299 . . . Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 303 303 . . . Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 306 306 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 307 307 . . . Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 308 308 . . . Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 311 311 . . . Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 314 314 . . . Note=O-linked (Man...) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 315 315 . . . Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 316 316 . . . Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 329 329 . . . Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 331 331 . . . Note=O-linked (Man...) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 334 334 . . . Note=O-linked (Man...) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 335 335 . . . Note=O-linked (Man...) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 338 338 . . . Note=O-linked (Man...) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 339 339 . . . Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 340 340 . . . Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 341 341 . . . Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 342 342 . . . Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 345 345 . . . Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 346 346 . . . Note=O-linked (Man...) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 349 349 . . . Note=O-linked (Man...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 350 350 . . . Note=O-linked (Man...) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Glycosylation 364 364 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20840 UniProtKB Glycosylation 402 402 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20840 UniProtKB Glycosylation 460 460 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20840 UniProtKB Glycosylation 485 485 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20840 UniProtKB Glycosylation 501 501 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20840 UniProtKB Glycosylation 614 614 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20840 UniProtKB Disulfide bond 97 114 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Disulfide bond 202 300 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592821;Dbxref=PMID:7592821 +P20840 UniProtKB Mutagenesis 211 211 . . . Note=Little effect on secreted alpha-agglutinin activity. T->I +P20840 UniProtKB Mutagenesis 214 214 . . . Note=No effect on secreted alpha-agglutinin activity. I->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 215 215 . . . Note=Little or no effect on secreted alpha-agglutinin activity. D->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 216 216 . . . Note=Complete loss of alpha-agglutinin activity. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 216 216 . . . Note=No effect on secreted alpha-agglutinin activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 216 216 . . . Note=Decreases secreted alpha-agglutinin activity by 100-fold. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 216 216 . . . Note=Decreases secreted alpha-agglutinin activity by 10-fold. Y->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 217 217 . . . Note=Little effect on secreted alpha-agglutinin activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 217 217 . . . Note=Decreases secreted alpha-agglutinin activity by 10-fold. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 289 289 . . . Note=Decreases secreted alpha-agglutinin activity by less than 2-fold. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 290 290 . . . Note=Decreases secreted alpha-agglutinin activity by less than 2-fold. I->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 291 291 . . . Note=Decreases secreted alpha-agglutinin activity by 4-fold. D->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 292 292 . . . Note=Almost complete loss of secreted alpha-agglutinin activity. H->L%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 294 294 . . . Note=Decreases secreted alpha-agglutinin activity by more than 20-fold. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 295 295 . . . Note=Decreases secreted alpha-agglutinin activity by 2-fold. E->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 296 296 . . . Note=Decreases secreted alpha-agglutinin activity by more than 20-fold. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 298 298 . . . Note=Decreases secreted alpha-agglutinin activity by less than 2-fold. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 322 322 . . . Note=Decreases secreted alpha-agglutinin activity by 60-fold. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 322 322 . . . Note=Almost complete loss of secreted alpha-agglutinin activity by 10-fold. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 322 322 . . . Note=Decreases secreted alpha-agglutinin activity by 15-fold. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 323 323 . . . Note=Decreases secreted alpha-agglutinin activity by 2-fold. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 324 324 . . . Note=Little effect on secreted alpha-agglutinin activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Mutagenesis 325 325 . . . Note=Little effect on secreted alpha-agglutinin activity. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8741846;Dbxref=PMID:8741846 +P20840 UniProtKB Sequence conflict 449 449 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20840 UniProtKB Sequence conflict 556 556 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20840 UniProtKB Sequence conflict 581 581 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39954 1 449 +P39954 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P39954 UniProtKB Chain 2 449 . . . ID=PRO_0000116937;Note=Adenosylhomocysteinase +P39954 UniProtKB Nucleotide binding 160 162 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39954 UniProtKB Nucleotide binding 223 228 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39954 UniProtKB Nucleotide binding 302 304 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39954 UniProtKB Binding site 58 58 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39954 UniProtKB Binding site 134 134 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39954 UniProtKB Binding site 159 159 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39954 UniProtKB Binding site 189 189 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39954 UniProtKB Binding site 193 193 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39954 UniProtKB Binding site 194 194 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39954 UniProtKB Binding site 246 246 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39954 UniProtKB Binding site 349 349 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39954 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P39954 UniProtKB Modified residue 393 393 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P39954 UniProtKB Cross-link 21 21 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P39954 UniProtKB Cross-link 413 413 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q08985 1 325 +Q08985 UniProtKB Chain 1 325 . . . ID=PRO_0000114619;Note=Homocysteine S-methyltransferase 2 +Q08985 UniProtKB Domain 6 321 . . . Note=Hcy-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00333 +Q08985 UniProtKB Metal binding 239 239 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00333 +Q08985 UniProtKB Metal binding 306 306 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00333 +Q08985 UniProtKB Metal binding 307 307 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00333 +Q08985 UniProtKB Modified residue 138 138 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q08873 1 200 +Q08873 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q08873 UniProtKB Chain 2 200 . . . ID=PRO_0000204795;Note=Transgelin +Q08873 UniProtKB Domain 26 136 . . . Note=Calponin-homology (CH);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00044 +Q08873 UniProtKB Region 151 164 . . . Note=Interaction with SH3 domain of ABP1 +Q08873 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q08873 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q08873 UniProtKB Mutagenesis 185 185 . . . Note=Greatly reduces actin-binding and actin-bundling activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12857851;Dbxref=PMID:12857851 +Q08873 UniProtKB Mutagenesis 185 185 . . . Note=Moderately reduces actin-binding and actin-bundling activity. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12857851;Dbxref=PMID:12857851 +##sequence-region P40075 1 244 +P40075 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.5 +P40075 UniProtKB Chain 2 244 . . . ID=PRO_0000213467;Note=Vesicle-associated membrane protein-associated protein SCS2 +P40075 UniProtKB Topological domain 2 222 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40075 UniProtKB Transmembrane 223 243 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40075 UniProtKB Topological domain 244 244 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40075 UniProtKB Domain 3 126 . . . Note=MSP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00132 +P40075 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.5 +P40075 UniProtKB Modified residue 106 106 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198 +P40075 UniProtKB Mutagenesis 40 40 . . . Note=Disrupts binding to FFAT motif and causes OPI1 mislocalization. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15668246;Dbxref=PMID:15668246 +P40075 UniProtKB Mutagenesis 41 42 . . . Note=Disrupts binding to FFAT motif and causes OPI1 mislocalization. TT->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15668246;Dbxref=PMID:15668246 +P40075 UniProtKB Mutagenesis 84 84 . . . Note=Disrupts binding to FFAT motif%3B when associated with D-86. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16004875;Dbxref=PMID:16004875 +P40075 UniProtKB Mutagenesis 86 86 . . . Note=Disrupts binding to FFAT motif%3B when associated with D-84. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16004875;Dbxref=PMID:16004875 +P40075 UniProtKB Mutagenesis 120 120 . . . Note=Reduces binding to FFAT motif and impairs OPI1 function. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15668246;Dbxref=PMID:15668246 +##sequence-region Q08230 1 162 +Q08230 UniProtKB Transit peptide 1 35 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19837041;Dbxref=PMID:19837041 +Q08230 UniProtKB Chain 36 162 . . . ID=PRO_0000007814;Note=Succinate dehydrogenase assembly factor 2%2C mitochondrial +Q08230 UniProtKB Mutagenesis 68 68 . . . Note=Loss of covalent FAD in SDH1. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23062074;Dbxref=PMID:23062074 +Q08230 UniProtKB Mutagenesis 71 71 . . . Note=Loss of covalent FAD in SDH1. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23062074;Dbxref=PMID:23062074 +Q08230 UniProtKB Mutagenesis 98 99 . . . Note=No effect. EE->KK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23062074;Dbxref=PMID:23062074 +Q08230 UniProtKB Mutagenesis 113 113 . . . Note=Loss of covalent FAD in SDH1. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23062074;Dbxref=PMID:23062074 +Q08230 UniProtKB Helix 62 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LM4 +Q08230 UniProtKB Helix 79 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LM4 +Q08230 UniProtKB Helix 98 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LM4 +Q08230 UniProtKB Helix 112 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LM4 +Q08230 UniProtKB Turn 123 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LM4 +Q08230 UniProtKB Helix 130 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LM4 +Q08230 UniProtKB Helix 136 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LM4 +##sequence-region P40357 1 651 +P40357 UniProtKB Chain 1 651 . . . ID=PRO_0000213613;Note=Protein transport protein SEC9 +P40357 UniProtKB Domain 434 496 . . . Note=t-SNARE coiled-coil homology 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202 +P40357 UniProtKB Domain 588 650 . . . Note=t-SNARE coiled-coil homology 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202 +P40357 UniProtKB Modified residue 79 79 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40357 UniProtKB Modified residue 92 92 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40357 UniProtKB Modified residue 186 186 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40357 UniProtKB Modified residue 190 190 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40357 UniProtKB Modified residue 213 213 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40357 UniProtKB Modified residue 271 271 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40357 UniProtKB Modified residue 273 273 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40357 UniProtKB Modified residue 315 315 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40357 UniProtKB Modified residue 355 355 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40357 UniProtKB Modified residue 359 359 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40357 UniProtKB Helix 433 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B5N +P40357 UniProtKB Helix 589 648 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B5N +##sequence-region Q01589 1 338 +Q01589 UniProtKB Signal peptide 1 18 . . . . +Q01589 UniProtKB Chain 19 318 . . . ID=PRO_0000022292;Note=Cell wall protein SED1 +Q01589 UniProtKB Propeptide 319 338 . . . ID=PRO_0000022293;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01589 UniProtKB Repeat 58 65 . . . Note=1-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q01589 UniProtKB Repeat 66 79 . . . Note=1-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q01589 UniProtKB Repeat 80 93 . . . Note=1-3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q01589 UniProtKB Repeat 94 101 . . . Note=1-4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q01589 UniProtKB Repeat 102 115 . . . Note=1-5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q01589 UniProtKB Repeat 116 123 . . . Note=1-6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q01589 UniProtKB Repeat 124 137 . . . Note=1-7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q01589 UniProtKB Repeat 169 211 . . . Note=2-1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q01589 UniProtKB Repeat 220 262 . . . Note=2-2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16086015;Dbxref=PMID:16086015 +Q01589 UniProtKB Region 58 137 . . . Note=7 X approximate tandem repeats +Q01589 UniProtKB Region 169 262 . . . Note=2 X 43 AA repeats +Q01589 UniProtKB Lipidation 318 318 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01589 UniProtKB Glycosylation 22 22 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01589 UniProtKB Glycosylation 56 56 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01589 UniProtKB Glycosylation 78 78 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01589 UniProtKB Glycosylation 92 92 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01589 UniProtKB Glycosylation 114 114 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01589 UniProtKB Glycosylation 136 136 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01589 UniProtKB Glycosylation 152 152 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01589 UniProtKB Natural variant 80 93 . . . Note=In strain: CBS 1171 and in allele SED1-1%2C SED1-2%2C SED1-3%2C SED1-4%2C SED1-5%2C SED1-6 and SED1-7. Missing +Q01589 UniProtKB Natural variant 94 94 . . . Note=In allele SED1-2. T->TSTEAPTTDTTSEAPTTAIPTNG +Q01589 UniProtKB Natural variant 94 94 . . . Note=In allele SED1-5. T->TSTEAPTTDTTTEAPTTAIPTNG +Q01589 UniProtKB Natural variant 94 94 . . . Note=In allele SED1-3 and SED1-6. T->TSTEAPTTDTTTEAPTTALPTNGTSTEAPTDTTTEAPTTALPTNG +Q01589 UniProtKB Natural variant 212 212 . . . Note=In allele SED1-4%2C SED1-5 and SED1-6. P->PTTTSTTEYTVVTEYTTYCPEPTTFTTNGKTYTVTEPTTLTITDCPCTIEK +Q01589 UniProtKB Natural variant 212 212 . . . Note=In allele SED1-7. P->PTTTSTTEYTVVTEYTTYCPEPTTFTTNGKTYTVTEPTTLTITDCPCTIEKPTTTSTTEYTVVTEYTTYCPEPTTFTTNGKTYTVTEPTTLTITDCPCTIEK +Q01589 UniProtKB Sequence conflict 309 309 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q01590 1 340 +Q01590 UniProtKB Chain 1 340 . . . ID=PRO_0000210273;Note=Integral membrane protein SED5 +Q01590 UniProtKB Topological domain 1 319 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01590 UniProtKB Transmembrane 320 340 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01590 UniProtKB Domain 249 311 . . . Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202 +Q01590 UniProtKB Coiled coil 146 173 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q01590 UniProtKB Mutagenesis 206 206 . . . Note=Loss of interaction with SEC23/SEC24 complex. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941276;Dbxref=PMID:12941276 +Q01590 UniProtKB Helix 1 4 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +Q01590 UniProtKB Helix 7 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +##sequence-region P34228 1 1148 +P34228 UniProtKB Chain 1 1148 . . . ID=PRO_0000114977;Note=Putative transcription factor SEF1 +P34228 UniProtKB DNA binding 57 87 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P34228 UniProtKB Compositional bias 278 322 . . . Note=Thr-rich +P34228 UniProtKB Compositional bias 536 539 . . . Note=Poly-Asn +P34228 UniProtKB Modified residue 8 8 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34228 UniProtKB Modified residue 263 263 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P34228 UniProtKB Modified residue 806 806 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P16658 1 377 +P16658 UniProtKB Chain 1 377 . . . ID=PRO_0000109462;Note=tRNA-splicing endonuclease subunit SEN2 +P16658 UniProtKB Coiled coil 119 174 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P16658 UniProtKB Active site 289 289 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P16658 UniProtKB Active site 297 297 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P16658 UniProtKB Active site 328 328 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P16658 UniProtKB Natural variant 292 292 . . . Note=In the cold-sensitive allele sen2-3%3B defective in cleavage only at the 5'-splice site of tRNA precursors. G->E +##sequence-region P36123 1 1033 +P36123 UniProtKB Chain 1 1033 . . . ID=PRO_0000046107;Note=SIT4-associating protein SAP190 +P36123 UniProtKB Modified residue 774 774 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P36123 UniProtKB Modified residue 857 857 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P36123 UniProtKB Modified residue 862 862 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36123 UniProtKB Modified residue 892 892 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36123 UniProtKB Modified residue 990 990 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36123 UniProtKB Modified residue 991 991 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P32368 1 623 +P32368 UniProtKB Chain 1 623 . . . ID=PRO_0000209737;Note=Phosphoinositide phosphatase SAC1 +P32368 UniProtKB Topological domain 1 521 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32368 UniProtKB Transmembrane 522 544 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32368 UniProtKB Topological domain 545 623 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32368 UniProtKB Domain 115 454 . . . Note=SAC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00183 +P32368 UniProtKB Compositional bias 507 521 . . . Note=Pro-rich +P32368 UniProtKB Cross-link 246 246 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32368 UniProtKB Cross-link 358 358 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32368 UniProtKB Beta strand 5 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 13 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 28 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Turn 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 38 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Helix 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 53 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 67 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 85 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Turn 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TU3 +P32368 UniProtKB Helix 106 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 124 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4TU3 +P32368 UniProtKB Beta strand 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Helix 136 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Helix 148 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Turn 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Turn 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Helix 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Helix 163 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Helix 173 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 183 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 197 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 213 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 218 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 230 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Turn 242 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 247 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 261 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 269 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Helix 279 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 297 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Helix 313 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 330 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Turn 341 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Helix 344 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 366 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 377 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Beta strand 386 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Helix 396 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Helix 427 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Helix 431 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +P32368 UniProtKB Turn 449 451 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LWT +##sequence-region P46674 1 1301 +P46674 UniProtKB Chain 1 1301 . . . ID=PRO_0000097562;Note=Nuclear mRNA export protein SAC3 +P46674 UniProtKB Region 1 572 . . . Note=Required for interaction with MEX67%2C SUB2 and THP1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12411502;Dbxref=PMID:12411502 +P46674 UniProtKB Region 573 1301 . . . Note=Required for targeting SAC3 to the nuclear pore +P46674 UniProtKB Region 733 860 . . . Note=Interaction with CDC31;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15311284;Dbxref=PMID:15311284 +P46674 UniProtKB Modified residue 568 568 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46674 UniProtKB Modified residue 748 748 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14718168;Dbxref=PMID:14718168 +P46674 UniProtKB Modified residue 866 866 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P46674 UniProtKB Helix 258 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Helix 273 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Turn 276 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Helix 280 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Helix 302 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Helix 331 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Helix 362 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Helix 378 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Helix 388 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Helix 394 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Helix 426 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Helix 440 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Helix 447 449 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Helix 450 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Helix 474 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Helix 486 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Turn 502 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Helix 508 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Beta strand 514 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Helix 530 537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Helix 541 545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T5V +P46674 UniProtKB Helix 753 803 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FWB +##sequence-region P43589 1 448 +P43589 UniProtKB Chain 1 448 . . . ID=PRO_0000202682;Note=Pre-mRNA-splicing factor SAD1 +P43589 UniProtKB Domain 150 447 . . . Note=USP +P43589 UniProtKB Zinc finger 46 107 . . . Note=UBP-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502 +P43589 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P43589 UniProtKB Helix 30 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Helix 37 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Turn 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 55 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Turn 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Helix 75 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 87 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Turn 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Turn 99 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Helix 108 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Helix 112 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Helix 127 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 144 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Helix 155 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Helix 172 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Helix 188 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 206 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Helix 213 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Helix 232 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Helix 248 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 260 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 281 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Helix 305 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 310 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Helix 313 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Helix 318 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 331 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 339 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 352 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Turn 355 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 363 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 368 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 375 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 403 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Turn 413 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 417 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 425 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Helix 431 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +P43589 UniProtKB Beta strand 437 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4MSX +##sequence-region P14693 1 329 +P14693 UniProtKB Chain 1 329 . . . ID=PRO_0000202903;Note=Sorting assembly machinery 35 kDa subunit +##sequence-region Q08986 1 587 +Q08986 UniProtKB Chain 1 587 . . . ID=PRO_0000054163;Note=S-adenosylmethionine permease SAM3 +Q08986 UniProtKB Topological domain 1 80 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Transmembrane 81 103 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Topological domain 104 109 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Transmembrane 110 129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Topological domain 130 162 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Transmembrane 163 183 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Topological domain 184 186 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Transmembrane 187 207 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Topological domain 208 219 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Transmembrane 220 240 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Topological domain 241 266 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Transmembrane 267 287 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Topological domain 288 302 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Transmembrane 303 323 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Topological domain 324 360 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Transmembrane 361 381 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Topological domain 382 406 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Transmembrane 407 427 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Topological domain 428 431 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Transmembrane 432 452 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Topological domain 453 475 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Transmembrane 476 496 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Topological domain 497 509 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Transmembrane 510 530 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Topological domain 531 587 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q08986 UniProtKB Modified residue 27 27 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12372 +Q08986 UniProtKB Modified residue 44 44 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08986 UniProtKB Glycosylation 184 184 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08986 UniProtKB Glycosylation 243 243 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53969 1 484 +P53969 UniProtKB Chain 1 484 . . . ID=PRO_0000215943;Note=Sorting assembly machinery 50 kDa subunit +##sequence-region P38429 1 201 +P38429 UniProtKB Chain 1 201 . . . ID=PRO_0000203345;Note=Transcriptional regulatory protein SAP30 +P38429 UniProtKB Compositional bias 26 58 . . . Note=Asn-rich +P38429 UniProtKB Sequence conflict 31 31 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38429 UniProtKB Sequence conflict 48 48 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04003 1 481 +Q04003 UniProtKB Chain 1 481 . . . ID=PRO_0000097593;Note=Something about silencing protein 4 +Q04003 UniProtKB Coiled coil 90 120 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04003 UniProtKB Coiled coil 139 160 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53324 1 424 +P53324 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53324 UniProtKB Chain 2 424 . . . ID=PRO_0000202862;Note=Steryl acetyl hydrolase 1 +P53324 UniProtKB Topological domain 2 45 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53324 UniProtKB Transmembrane 46 66 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53324 UniProtKB Topological domain 67 424 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53324 UniProtKB Motif 176 178 . . . Note=Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5NUF3 +P53324 UniProtKB Active site 250 250 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5NUF3 +P53324 UniProtKB Active site 395 395 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5NUF3 +P53324 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53324 UniProtKB Glycosylation 85 85 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53324 UniProtKB Glycosylation 283 283 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53324 UniProtKB Glycosylation 401 401 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38814 1 852 +P38814 UniProtKB Chain 1 852 . . . ID=PRO_0000202909;Note=Protein SBE22 +P38814 UniProtKB Modified residue 72 72 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38814 UniProtKB Modified residue 201 201 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38814 UniProtKB Modified residue 459 459 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38814 UniProtKB Modified residue 517 517 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38814 UniProtKB Modified residue 520 520 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P42223 1 864 +P42223 UniProtKB Chain 1 864 . . . ID=PRO_0000097602;Note=Protein SBE2 +P42223 UniProtKB Modified residue 82 82 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P42223 UniProtKB Modified residue 83 83 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P42223 UniProtKB Modified residue 450 450 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P42223 UniProtKB Modified residue 532 532 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P25303 1 377 +P25303 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25303 UniProtKB Chain 22 377 . . . ID=PRO_0000071091;Note=DnaJ-related protein SCJ1 +P25303 UniProtKB Domain 23 88 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +P25303 UniProtKB Repeat 169 176 . . . Note=CXXCXGXG motif +P25303 UniProtKB Repeat 185 192 . . . Note=CXXCXGXG motif +P25303 UniProtKB Repeat 211 218 . . . Note=CXXCXGXG motif +P25303 UniProtKB Repeat 225 232 . . . Note=CXXCXGXG motif +P25303 UniProtKB Zinc finger 156 237 . . . Note=CR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00546 +P25303 UniProtKB Motif 288 290 . . . Note=Cell attachment site;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25303 UniProtKB Motif 374 377 . . . Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10138 +P25303 UniProtKB Compositional bias 95 132 . . . Note=Gly-rich +##sequence-region P47052 1 634 +P47052 UniProtKB Transit peptide 1 25 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47052 UniProtKB Chain 26 634 . . . ID=PRO_0000010343;Note=Succinate dehydrogenase [ubiquinone] flavoprotein subunit 2%2C mitochondrial +P47052 UniProtKB Nucleotide binding 53 58 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +P47052 UniProtKB Nucleotide binding 76 91 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +P47052 UniProtKB Nucleotide binding 443 444 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +P47052 UniProtKB Active site 325 325 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +P47052 UniProtKB Binding site 260 260 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +P47052 UniProtKB Binding site 281 281 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +P47052 UniProtKB Binding site 293 293 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +P47052 UniProtKB Binding site 392 392 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +P47052 UniProtKB Binding site 427 427 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +P47052 UniProtKB Binding site 438 438 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +P47052 UniProtKB Modified residue 84 84 . . . Note=Tele-8alpha-FAD histidine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +##sequence-region P36047 1 338 +P36047 UniProtKB Chain 1 338 . . . ID=PRO_0000071447;Note=Protein phosphatase 1 regulatory subunit SDS22 +P36047 UniProtKB Repeat 43 64 . . . Note=LRR 1 +P36047 UniProtKB Repeat 67 88 . . . Note=LRR 2 +P36047 UniProtKB Repeat 91 113 . . . Note=LRR 3 +P36047 UniProtKB Repeat 114 135 . . . Note=LRR 4 +P36047 UniProtKB Repeat 136 157 . . . Note=LRR 5 +P36047 UniProtKB Repeat 158 179 . . . Note=LRR 6 +P36047 UniProtKB Repeat 182 203 . . . Note=LRR 7 +P36047 UniProtKB Repeat 204 225 . . . Note=LRR 8 +P36047 UniProtKB Repeat 226 247 . . . Note=LRR 9 +P36047 UniProtKB Repeat 248 269 . . . Note=LRR 10 +P36047 UniProtKB Repeat 270 292 . . . Note=LRR 11 +P36047 UniProtKB Domain 306 338 . . . Note=LRRCT +P36047 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q06245 1 871 +Q06245 UniProtKB Chain 1 871 . . . ID=PRO_0000118950;Note=Exocyst complex component SEC10 +Q06245 UniProtKB Coiled coil 74 101 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06245 UniProtKB Modified residue 142 142 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q06245 UniProtKB Modified residue 485 485 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06245 UniProtKB Modified residue 507 507 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P48415 1 2195 +P48415 UniProtKB Chain 1 2195 . . . ID=PRO_0000097658;Note=COPII coat assembly protein SEC16 +P48415 UniProtKB Compositional bias 1997 2094 . . . Note=Lys-rich +P48415 UniProtKB Compositional bias 2078 2145 . . . Note=Pro-rich +P48415 UniProtKB Modified residue 28 28 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48415 UniProtKB Modified residue 73 73 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P48415 UniProtKB Modified residue 144 144 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P48415 UniProtKB Modified residue 313 313 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P48415 UniProtKB Modified residue 472 472 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48415 UniProtKB Modified residue 483 483 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P48415 UniProtKB Modified residue 595 595 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48415 UniProtKB Modified residue 607 607 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198 +P48415 UniProtKB Modified residue 660 660 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48415 UniProtKB Modified residue 663 663 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48415 UniProtKB Modified residue 665 665 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48415 UniProtKB Modified residue 674 674 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P48415 UniProtKB Modified residue 678 678 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P48415 UniProtKB Modified residue 681 681 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P48415 UniProtKB Modified residue 701 701 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48415 UniProtKB Modified residue 704 704 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P48415 UniProtKB Modified residue 706 706 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +P48415 UniProtKB Modified residue 759 759 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P48415 UniProtKB Modified residue 762 762 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P48415 UniProtKB Modified residue 765 765 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P48415 UniProtKB Modified residue 768 768 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48415 UniProtKB Modified residue 843 843 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P48415 UniProtKB Modified residue 1511 1511 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P48415 UniProtKB Modified residue 1515 1515 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +P48415 UniProtKB Modified residue 1578 1578 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P48415 UniProtKB Modified residue 1602 1602 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48415 UniProtKB Modified residue 1603 1603 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P48415 UniProtKB Modified residue 1611 1611 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P48415 UniProtKB Modified residue 1617 1617 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48415 UniProtKB Modified residue 1778 1778 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P48415 UniProtKB Modified residue 1875 1875 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P48415 UniProtKB Modified residue 1973 1973 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48415 UniProtKB Modified residue 1986 1986 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P48415 UniProtKB Modified residue 1992 1992 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P48415 UniProtKB Modified residue 2049 2049 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P48415 UniProtKB Modified residue 2130 2130 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P48415 UniProtKB Mutagenesis 1059 1059 . . . Note=In SEC16-4%3B ts accumulation of ER membranes. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7593161;Dbxref=PMID:7593161 +P48415 UniProtKB Mutagenesis 1084 1084 . . . Note=In SEC16-3%3B ts accumulation of ER membranes. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7593161;Dbxref=PMID:7593161 +P48415 UniProtKB Mutagenesis 1089 1089 . . . Note=In SEC16-2%3B ts accumulation of ER membranes. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7593161;Dbxref=PMID:7593161 +P48415 UniProtKB Mutagenesis 1231 1231 . . . Note=In SEC16-1%3B ts accumulation of ER membranes. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7593161;Dbxref=PMID:7593161 +P48415 UniProtKB Sequence conflict 522 522 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P48415 UniProtKB Sequence conflict 560 560 . . . Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P48415 UniProtKB Beta strand 995 998 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Beta strand 1002 1007 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Beta strand 1027 1031 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1032 1034 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1040 1044 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1056 1073 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1080 1090 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1095 1102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1106 1113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1130 1141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1145 1154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1158 1166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1170 1182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1193 1205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Turn 1206 1208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1210 1219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1221 1229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1231 1240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1254 1269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1273 1282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Beta strand 1288 1293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1309 1323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1332 1334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1335 1347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1351 1366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +P48415 UniProtKB Helix 1373 1388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +##sequence-region P18759 1 758 +P18759 UniProtKB Chain 1 758 . . . ID=PRO_0000084571;Note=Vesicular-fusion protein SEC18 +P18759 UniProtKB Nucleotide binding 281 288 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18759 UniProtKB Nucleotide binding 564 571 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18759 UniProtKB Modified residue 226 226 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P18759 UniProtKB Sequence conflict 381 381 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18759 UniProtKB Sequence conflict 381 381 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18759 UniProtKB Beta strand 27 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5 +P18759 UniProtKB Helix 37 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5 +P18759 UniProtKB Turn 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5 +P18759 UniProtKB Beta strand 44 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5 +P18759 UniProtKB Turn 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5 +P18759 UniProtKB Beta strand 57 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5 +P18759 UniProtKB Turn 61 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5 +P18759 UniProtKB Beta strand 64 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5 +P18759 UniProtKB Beta strand 78 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5 +P18759 UniProtKB Helix 83 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5 +P18759 UniProtKB Beta strand 96 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5 +P18759 UniProtKB Helix 104 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5 +P18759 UniProtKB Beta strand 113 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5 +P18759 UniProtKB Helix 136 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5 +P18759 UniProtKB Beta strand 157 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5 +P18759 UniProtKB Beta strand 165 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5 +P18759 UniProtKB Beta strand 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5 +P18759 UniProtKB Beta strand 203 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1CR5 +##sequence-region P28791 1 383 +P28791 UniProtKB Chain 1 383 . . . ID=PRO_0000097659;Note=Protein transport protein SEC20 +P28791 UniProtKB Topological domain 1 275 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28791 UniProtKB Transmembrane 276 292 . . . Note=Helical%3B Anchor for type IV membrane protein +P28791 UniProtKB Topological domain 293 383 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28791 UniProtKB Coiled coil 6 26 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P28791 UniProtKB Motif 380 383 . . . Note=Prevents secretion from ER +##sequence-region P15303 1 768 +P15303 UniProtKB Chain 1 768 . . . ID=PRO_0000205145;Note=Protein transport protein SEC23 +P15303 UniProtKB Metal binding 56 56 . . . Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12239560;Dbxref=PMID:12239560 +P15303 UniProtKB Metal binding 61 61 . . . Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12239560;Dbxref=PMID:12239560 +P15303 UniProtKB Metal binding 80 80 . . . Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12239560;Dbxref=PMID:12239560 +P15303 UniProtKB Metal binding 83 83 . . . Note=Zinc;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12239560;Dbxref=PMID:12239560 +P15303 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P15303 UniProtKB Helix 3 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 11 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 23 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 33 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 48 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QTV +P15303 UniProtKB Turn 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 69 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2V +P15303 UniProtKB Turn 73 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QTV +P15303 UniProtKB Turn 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 86 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QTV +P15303 UniProtKB Helix 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2V +P15303 UniProtKB Helix 103 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 108 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 123 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 134 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 156 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 172 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 190 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 224 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 228 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 231 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 262 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 283 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 294 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 311 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 322 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 342 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 355 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 369 373 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 378 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 394 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 399 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 412 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 437 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 443 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 456 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 484 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Turn 496 498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 499 512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 517 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 525 539 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 545 563 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 564 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QTV +P15303 UniProtKB Helix 571 573 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Turn 578 581 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 582 592 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Turn 594 596 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 603 613 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 618 625 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 628 632 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 634 636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 645 647 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 653 657 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 659 666 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 668 676 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 678 680 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 682 684 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2V +P15303 UniProtKB Helix 685 703 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 710 715 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 719 721 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Helix 722 725 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +P15303 UniProtKB Beta strand 740 742 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QTV +P15303 UniProtKB Helix 752 763 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2O +##sequence-region P17065 1 759 +P17065 UniProtKB Chain 1 759 . . . ID=PRO_0000097661;Note=Rab guanine nucleotide exchange factor SEC2 +P17065 UniProtKB Region 451 508 . . . Note=Required for proper polarized localization of the protein +P17065 UniProtKB Coiled coil 26 164 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17065 UniProtKB Coiled coil 651 682 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17065 UniProtKB Coiled coil 732 759 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P17065 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P17065 UniProtKB Modified residue 168 168 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P17065 UniProtKB Modified residue 171 171 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P17065 UniProtKB Modified residue 515 515 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P17065 UniProtKB Mutagenesis 483 483 . . . Note=In SEC2-78%3B temperature-sensitive%3B causes mislocalization of the protein%2C displaying many cytoplasmic punctae. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10747090;Dbxref=PMID:10747090 +P17065 UniProtKB Turn 34 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E7S +P17065 UniProtKB Helix 52 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EQB +P17065 UniProtKB Turn 147 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2E7S +##sequence-region P38968 1 1273 +P38968 UniProtKB Chain 1 1273 . . . ID=PRO_0000051436;Note=Protein transport protein SEC31 +P38968 UniProtKB Repeat 6 46 . . . Note=WD 1 +P38968 UniProtKB Repeat 60 99 . . . Note=WD 2 +P38968 UniProtKB Repeat 106 146 . . . Note=WD 3 +P38968 UniProtKB Repeat 158 198 . . . Note=WD 4 +P38968 UniProtKB Repeat 207 250 . . . Note=WD 5 +P38968 UniProtKB Repeat 255 295 . . . Note=WD 6 +P38968 UniProtKB Repeat 298 338 . . . Note=WD 7 +P38968 UniProtKB Repeat 385 405 . . . Note=WD 8%3B interaction with SEC13 +P38968 UniProtKB Compositional bias 773 1149 . . . Note=Pro-rich +P38968 UniProtKB Modified residue 349 349 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38968 UniProtKB Modified residue 836 836 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38968 UniProtKB Modified residue 974 974 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38968 UniProtKB Modified residue 977 977 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38968 UniProtKB Modified residue 980 980 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38968 UniProtKB Modified residue 988 988 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38968 UniProtKB Modified residue 992 992 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38968 UniProtKB Modified residue 999 999 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38968 UniProtKB Modified residue 1050 1050 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +P38968 UniProtKB Modified residue 1053 1053 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38968 UniProtKB Sequence conflict 317 317 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38968 UniProtKB Sequence conflict 367 367 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38968 UniProtKB Sequence conflict 367 367 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38968 UniProtKB Sequence conflict 691 691 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38968 UniProtKB Sequence conflict 754 754 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38968 UniProtKB Sequence conflict 877 877 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38968 UniProtKB Beta strand 6 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 17 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 22 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 28 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 43 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Helix 50 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 65 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 72 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 77 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 86 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 100 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 113 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 123 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 129 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 133 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Turn 138 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Turn 145 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 165 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 175 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 185 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Turn 190 193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 194 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 212 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 224 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 232 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 260 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 273 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 287 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 292 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 299 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 306 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 315 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 321 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +P38968 UniProtKB Beta strand 385 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Turn 388 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Beta strand 391 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Beta strand 402 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 416 424 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 428 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 441 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 458 466 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 509 519 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 523 531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Turn 532 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 536 543 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 549 563 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 568 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 582 587 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 590 592 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 593 603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 608 623 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Turn 624 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 628 637 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 641 650 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 652 661 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 666 685 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 697 711 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Turn 712 714 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 716 725 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Helix 731 744 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +P38968 UniProtKB Beta strand 909 911 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QTV +P38968 UniProtKB Helix 916 919 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QTV +##sequence-region P21825 1 274 +P21825 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P21825 UniProtKB Chain 2 274 . . . ID=PRO_0000206627;Note=Translocation protein SEC62 +P21825 UniProtKB Topological domain 2 149 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21825 UniProtKB Transmembrane 150 169 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21825 UniProtKB Topological domain 170 183 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21825 UniProtKB Transmembrane 184 204 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21825 UniProtKB Topological domain 205 274 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P21825 UniProtKB Compositional bias 246 270 . . . Note=Arg/Lys-rich (basic) +P21825 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P33754 1 206 +P33754 UniProtKB Chain 1 206 . . . ID=PRO_0000097663;Note=Translocation protein SEC66 +P33754 UniProtKB Topological domain 1 27 . . . Note=Lumenal +P33754 UniProtKB Transmembrane 28 48 . . . Note=Helical%3B Signal-anchor for type II membrane protein +P33754 UniProtKB Topological domain 49 206 . . . Note=Cytoplasmic +P33754 UniProtKB Glycosylation 5 5 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33754 UniProtKB Glycosylation 12 12 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39742 1 193 +P39742 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8051213;Dbxref=PMID:8051213 +P39742 UniProtKB Chain 2 193 . . . ID=PRO_0000097664;Note=Translocation protein SEC72 +P39742 UniProtKB Sequence conflict 33 33 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39742 UniProtKB Sequence conflict 187 187 . . . Note=L->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04675 1 128 +Q04675 UniProtKB Chain 1 128 . . . ID=PRO_0000194028;Note=tRNA-splicing endonuclease subunit SEN15 +##sequence-region Q00416 1 2231 +Q00416 UniProtKB Chain 1 2231 . . . ID=PRO_0000080722;Note=Helicase SEN1 +Q00416 UniProtKB Nucleotide binding 1360 1364 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00416 UniProtKB Motif 1909 1927 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q00416 UniProtKB Compositional bias 1908 1961 . . . Note=Lys-rich (basic) +Q00416 UniProtKB Binding site 1339 1339 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00416 UniProtKB Binding site 1619 1619 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00416 UniProtKB Binding site 1655 1655 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00416 UniProtKB Binding site 1787 1787 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q00416 UniProtKB Mutagenesis 1597 1597 . . . Note=Causes read-through of both a snoRNA gene terminator and the poly(A) site of a protein-coding gene. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17157256;Dbxref=PMID:17157256 +Q00416 UniProtKB Mutagenesis 1747 1747 . . . Note=In SEN1-1%3B gives rise to a temperature-sensitive mutant. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1569945;Dbxref=PMID:1569945 +Q00416 UniProtKB Helix 1100 1109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1114 1120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1129 1133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1137 1139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1150 1174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1181 1191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1194 1202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1203 1208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1215 1220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1233 1237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1240 1252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1256 1265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1269 1273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1279 1287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1289 1300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1301 1303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1307 1312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1323 1333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1337 1348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1351 1356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1363 1379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1406 1412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1413 1423 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1439 1441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1450 1453 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1457 1465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Turn 1466 1469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1542 1559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1561 1566 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1568 1571 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1573 1576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1584 1589 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1595 1599 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1600 1604 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1608 1613 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1615 1617 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1625 1629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Turn 1630 1633 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1636 1641 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1657 1667 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1678 1681 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1685 1688 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1694 1700 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1717 1734 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Turn 1735 1737 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1744 1749 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1751 1765 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1766 1769 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Turn 1770 1772 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1773 1777 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Turn 1778 1783 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1786 1792 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1802 1815 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1818 1827 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1829 1832 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1836 1847 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Beta strand 1851 1854 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Turn 1856 1859 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +Q00416 UniProtKB Helix 1864 1871 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5MZN +##sequence-region P47008 1 294 +P47008 UniProtKB Chain 1 294 . . . ID=PRO_0000203033;Note=Phosphatidylinositol transfer protein SFH5 +P47008 UniProtKB Domain 100 266 . . . Note=CRAL-TRIO;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00056 +P47008 UniProtKB Sequence conflict 70 70 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q05567 1 589 +Q05567 UniProtKB Chain 1 589 . . . ID=PRO_0000147018;Note=Sphingosine-1-phosphate lyase +Q05567 UniProtKB Modified residue 380 380 . . . Note=N6-(pyridoxal phosphate)lysine +Q05567 UniProtKB Mutagenesis 172 172 . . . Note=Loss of enzyme activity. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20696404;Dbxref=PMID:20696404 +Q05567 UniProtKB Mutagenesis 174 174 . . . Note=Mildly decreased enzyme activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20696404;Dbxref=PMID:20696404 +Q05567 UniProtKB Mutagenesis 198 198 . . . Note=Decreased enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20696404;Dbxref=PMID:20696404 +Q05567 UniProtKB Mutagenesis 380 380 . . . Note=Loss of enzyme activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20696404;Dbxref=PMID:20696404 +Q05567 UniProtKB Mutagenesis 386 386 . . . Note=Loss of enzyme activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20696404;Dbxref=PMID:20696404 +Q05567 UniProtKB Mutagenesis 554 554 . . . Note=Decreased enzyme activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20696404;Dbxref=PMID:20696404 +Q05567 UniProtKB Helix 145 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Helix 164 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Beta strand 169 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Helix 178 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Turn 199 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Helix 203 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Turn 224 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Beta strand 229 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Helix 235 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Beta strand 260 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Helix 269 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Beta strand 281 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Turn 289 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Turn 296 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Helix 300 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Beta strand 305 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Turn 317 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Turn 326 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Helix 331 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Beta strand 339 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Turn 343 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Helix 347 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Helix 351 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Turn 354 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Beta strand 373 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Turn 378 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Beta strand 389 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Helix 396 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Turn 400 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Beta strand 417 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Helix 425 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Beta strand 476 482 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Turn 484 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Helix 488 496 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Turn 497 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Beta strand 511 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Turn 517 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Helix 523 537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +Q05567 UniProtKB Helix 567 575 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MC6 +##sequence-region P36136 1 271 +P36136 UniProtKB Chain 1 271 . . . ID=PRO_0000203211;Note=Sedoheptulose 1%2C7-bisphosphatase +P36136 UniProtKB Region 24 25 . . . Note=Substrate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Region 99 102 . . . Note=Substrate binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Active site 13 13 . . . Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Active site 99 99 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Binding site 12 12 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Binding site 69 69 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Binding site 181 181 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Binding site 244 244 . . . Note=Substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Site 176 176 . . . Note=Transition state stabilizer;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Mutagenesis 12 12 . . . Note=Impairs catalytic activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Mutagenesis 13 13 . . . Note=Impairs catalytic activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Mutagenesis 16 16 . . . Note=Impairs catalytic activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Mutagenesis 19 19 . . . Note=Leads to reduced substrate affinity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Mutagenesis 24 24 . . . Note=Leads to low activity and reduced substrate affinity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Mutagenesis 65 65 . . . Note=Leads to low activity and reduced substrate affinity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Mutagenesis 69 69 . . . Note=Leads to reduced substrate affinity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Mutagenesis 99 99 . . . Note=Impairs catalytic activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Mutagenesis 102 102 . . . Note=Impairs catalytic activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Mutagenesis 131 131 . . . Note=Leads to reduced substrate affinity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Mutagenesis 176 176 . . . Note=Impairs catalytic activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Mutagenesis 178 178 . . . Note=Leads to low activity and reduced substrate affinity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Mutagenesis 181 181 . . . Note=Leads to reduced substrate affinity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20427268;Dbxref=PMID:20427268 +P36136 UniProtKB Beta strand 7 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Helix 17 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Beta strand 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OI7 +P36136 UniProtKB Helix 34 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Helix 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LG2 +P36136 UniProtKB Helix 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Beta strand 59 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Helix 68 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Turn 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Helix 83 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Beta strand 89 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Helix 95 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Helix 103 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Helix 110 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Beta strand 124 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Helix 130 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Helix 141 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Beta strand 170 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Helix 177 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Beta strand 191 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Helix 199 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Beta strand 219 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Beta strand 237 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Beta strand 249 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Turn 254 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3K +P36136 UniProtKB Helix 262 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3LG2 +##sequence-region P39000 1 512 +P39000 UniProtKB Chain 1 512 . . . ID=PRO_0000202642;Note=Protein SHC1 +P39000 UniProtKB Repeat 318 353 . . . Note=Sel1-like 1 +P39000 UniProtKB Repeat 354 389 . . . Note=Sel1-like 2 +P39000 UniProtKB Repeat 390 429 . . . Note=Sel1-like 3 +P39000 UniProtKB Repeat 433 470 . . . Note=Sel1-like 4 +P39000 UniProtKB Sequence conflict 22 22 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39000 UniProtKB Sequence conflict 33 33 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39000 UniProtKB Sequence conflict 90 90 . . . Note=Y->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39000 UniProtKB Sequence conflict 176 176 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39000 UniProtKB Sequence conflict 233 233 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39000 UniProtKB Sequence conflict 311 311 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02774 1 210 +Q02774 UniProtKB Chain 1 210 . . . ID=PRO_0000097740;Note=Secretory component protein SHR3 +Q02774 UniProtKB Topological domain 1 9 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02774 UniProtKB Transmembrane 10 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02774 UniProtKB Topological domain 29 59 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02774 UniProtKB Transmembrane 60 84 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02774 UniProtKB Topological domain 85 91 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02774 UniProtKB Transmembrane 92 114 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02774 UniProtKB Topological domain 115 130 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02774 UniProtKB Transmembrane 131 160 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02774 UniProtKB Topological domain 161 210 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02774 UniProtKB Sequence conflict 125 129 . . . Note=GEVTE->EKLR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q07657 1 551 +Q07657 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q07657 UniProtKB Chain 2 551 . . . ID=PRO_0000173545;Note=Seventh homolog of septin 1 +Q07657 UniProtKB Domain 20 339 . . . Note=Septin-type G +Q07657 UniProtKB Nucleotide binding 30 37 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07657 UniProtKB Nucleotide binding 218 226 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07657 UniProtKB Coiled coil 418 518 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07657 UniProtKB Binding site 138 138 . . . Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07657 UniProtKB Binding site 288 288 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07657 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q07657 UniProtKB Modified residue 400 400 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07657 UniProtKB Modified residue 408 408 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q07657 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q07657 UniProtKB Modified residue 447 447 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +Q07657 UniProtKB Modified residue 460 460 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07657 UniProtKB Modified residue 519 519 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q07657 UniProtKB Modified residue 520 520 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07657 UniProtKB Modified residue 522 522 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07657 UniProtKB Modified residue 525 525 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q07657 UniProtKB Modified residue 539 539 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07657 UniProtKB Modified residue 545 545 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q07657 UniProtKB Modified residue 548 548 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q07657 UniProtKB Cross-link 426 426 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) +Q07657 UniProtKB Cross-link 437 437 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) +Q07657 UniProtKB Mutagenesis 426 426 . . . Note=Abolishes sumoylation in vitro%3B when associated with R-437. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10579719;Dbxref=PMID:10579719 +Q07657 UniProtKB Mutagenesis 437 437 . . . Note=Abolishes sumoylation in vitro%3B when associated with R-426. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10579719;Dbxref=PMID:10579719 +##sequence-region P38751 1 150 +P38751 UniProtKB Chain 1 150 . . . ID=PRO_0000097742;Note=Suppressor of HU sensitivity involved in recombination protein 1 +P38751 UniProtKB Sequence conflict 138 138 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P50263 1 79 +P50263 UniProtKB Chain 1 79 . . . ID=PRO_0000097764;Note=Protein SIP18 +P50263 UniProtKB Sequence conflict 47 48 . . . Note=EG->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P50263 UniProtKB Sequence conflict 76 79 . . . Note=NMKK->HENMYVFGALTKSSYFFNGLFMNCLCLCSLYSKSISAYFSEFSSTNIYKSYLRLPSVLYYVCMMHTMMPNQLDAVGIQSSESLLM;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38717 1 1229 +P38717 UniProtKB Chain 1 1229 . . . ID=PRO_0000097765;Note=Membrane-anchored lipid-binding protein SIP3 +P38717 UniProtKB Topological domain 1 1066 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:16847258,ECO:0000305|PubMed:26001273;Dbxref=PMID:16847258,PMID:26001273 +P38717 UniProtKB Transmembrane 1067 1087 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38717 UniProtKB Topological domain 1088 1229 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +P38717 UniProtKB Domain 309 423 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +P38717 UniProtKB Domain 771 976 . . . Note=VASt;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01114 +P38717 UniProtKB Glycosylation 1206 1206 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +##sequence-region P06700 1 562 +P06700 UniProtKB Chain 1 562 . . . ID=PRO_0000110280;Note=NAD-dependent histone deacetylase SIR2 +P06700 UniProtKB Domain 245 529 . . . Note=Deacetylase sirtuin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P06700 UniProtKB Nucleotide binding 262 281 . . . Note=NAD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23307867,ECO:0000269|Ref.28;Dbxref=PMID:23307867 +P06700 UniProtKB Nucleotide binding 344 347 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P53686 +P06700 UniProtKB Nucleotide binding 471 473 . . . Note=NAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23307867;Dbxref=PMID:23307867 +P06700 UniProtKB Nucleotide binding 496 498 . . . Note=NAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23307867;Dbxref=PMID:23307867 +P06700 UniProtKB Active site 364 364 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00236 +P06700 UniProtKB Metal binding 372 372 . . . Note=Zinc;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23307867,ECO:0000269|Ref.28;Dbxref=PMID:23307867 +P06700 UniProtKB Metal binding 375 375 . . . Note=Zinc;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23307867,ECO:0000269|Ref.28;Dbxref=PMID:23307867 +P06700 UniProtKB Metal binding 396 396 . . . Note=Zinc;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23307867,ECO:0000269|Ref.28;Dbxref=PMID:23307867 +P06700 UniProtKB Metal binding 399 399 . . . Note=Zinc;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23307867,ECO:0000269|Ref.28;Dbxref=PMID:23307867 +P06700 UniProtKB Binding site 513 513 . . . Note=NAD%3B via amide nitrogen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23307867;Dbxref=PMID:23307867 +P06700 UniProtKB Mutagenesis 139 139 . . . Note=Defects in telomeric silencing. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12399383;Dbxref=PMID:12399383 +P06700 UniProtKB Mutagenesis 270 270 . . . Note=Defects in telomeric silencing. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12399383;Dbxref=PMID:12399383 +P06700 UniProtKB Mutagenesis 296 296 . . . Note=Defects in telomeric silencing. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12399383;Dbxref=PMID:12399383 +P06700 UniProtKB Helix 102 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO +P06700 UniProtKB Beta strand 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO +P06700 UniProtKB Beta strand 124 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO +P06700 UniProtKB Helix 132 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO +P06700 UniProtKB Helix 163 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO +P06700 UniProtKB Beta strand 173 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO +P06700 UniProtKB Helix 178 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO +P06700 UniProtKB Beta strand 213 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Helix 244 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Beta strand 255 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Helix 263 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Beta strand 274 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Helix 280 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Helix 284 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Helix 292 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Helix 298 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Helix 306 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Helix 312 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Helix 324 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Beta strand 338 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Helix 349 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Turn 357 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Beta strand 360 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Beta strand 365 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Turn 373 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Beta strand 378 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Helix 381 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Helix 385 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Turn 397 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Helix 400 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Turn 417 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO +P06700 UniProtKB Turn 433 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Beta strand 437 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Helix 451 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Turn 461 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Beta strand 466 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Helix 479 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Helix 482 485 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Beta strand 492 498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Beta strand 506 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Helix 513 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Helix 533 537 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Beta strand 541 547 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +P06700 UniProtKB Beta strand 550 555 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HJH +##sequence-region P32900 1 734 +P32900 UniProtKB Chain 1 734 . . . ID=PRO_0000202924;Note=Protein SKG6 +P32900 UniProtKB Transmembrane 72 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32900 UniProtKB Modified residue 137 137 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32900 UniProtKB Modified residue 169 169 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P32900 UniProtKB Modified residue 191 191 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32900 UniProtKB Modified residue 193 193 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32900 UniProtKB Modified residue 219 219 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32900 UniProtKB Modified residue 221 221 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32900 UniProtKB Modified residue 222 222 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32900 UniProtKB Modified residue 251 251 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32900 UniProtKB Modified residue 369 369 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P32900 UniProtKB Modified residue 672 672 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32900 UniProtKB Modified residue 717 717 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32900 UniProtKB Sequence conflict 355 355 . . . Note=L->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32900 UniProtKB Sequence conflict 403 403 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32900 UniProtKB Sequence conflict 450 450 . . . Note=M->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32900 UniProtKB Sequence conflict 472 472 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32900 UniProtKB Sequence conflict 497 497 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32900 UniProtKB Sequence conflict 499 499 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32900 UniProtKB Sequence conflict 510 510 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P35207 1 1287 +P35207 UniProtKB Chain 1 1287 . . . ID=PRO_0000102084;Note=Antiviral helicase SKI2 +P35207 UniProtKB Domain 338 496 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P35207 UniProtKB Domain 638 815 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P35207 UniProtKB Nucleotide binding 351 358 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P35207 UniProtKB Region 556 577 . . . Note=RNA-binding RGG-box;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P35207 UniProtKB Motif 444 447 . . . Note=DEVH box +P35207 UniProtKB Compositional bias 555 597 . . . Note=Arg/Gly-rich +P35207 UniProtKB Modified residue 209 209 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P35207 UniProtKB Sequence conflict 326 326 . . . Note=W->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35207 UniProtKB Sequence conflict 759 760 . . . Note=QM->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35207 UniProtKB Beta strand 302 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 315 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 332 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 346 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 358 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 374 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 382 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 385 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 401 404 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 414 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 421 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 434 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 438 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 458 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 470 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 481 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 496 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 508 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 517 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 530 540 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 613 623 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 628 632 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 636 644 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Turn 645 648 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 654 668 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 673 676 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 679 688 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Turn 689 691 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 692 695 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 701 712 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 717 721 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 724 727 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 734 739 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 741 745 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 748 751 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 754 761 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 762 764 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Turn 767 769 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 771 778 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 786 794 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 808 817 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 821 827 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 830 854 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Turn 862 864 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4K +P35207 UniProtKB Beta strand 865 868 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4K +P35207 UniProtKB Helix 871 889 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 895 898 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 903 908 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 914 923 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Turn 924 927 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 928 933 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 943 945 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4K +P35207 UniProtKB Helix 955 961 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Beta strand 971 976 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 977 979 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4K +P35207 UniProtKB Beta strand 982 987 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 992 997 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 1000 1015 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 1031 1044 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 1051 1053 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4K +P35207 UniProtKB Helix 1061 1079 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Turn 1080 1082 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 1088 1101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 1113 1118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 1126 1134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 1137 1140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 1143 1150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 1151 1153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 1169 1191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 1198 1202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 1203 1205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Turn 1208 1211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 1212 1220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 1224 1229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 1235 1259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 1262 1275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +P35207 UniProtKB Helix 1278 1281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A4Z +##sequence-region P17883 1 1432 +P17883 UniProtKB Chain 1 1432 . . . ID=PRO_0000106323;Note=Superkiller protein 3 +P17883 UniProtKB Repeat 4 37 . . . Note=TPR 1 +P17883 UniProtKB Repeat 47 80 . . . Note=TPR 2 +P17883 UniProtKB Repeat 425 458 . . . Note=TPR 3 +P17883 UniProtKB Repeat 471 507 . . . Note=TPR 4 +P17883 UniProtKB Repeat 508 541 . . . Note=TPR 5 +P17883 UniProtKB Repeat 627 661 . . . Note=TPR 6 +P17883 UniProtKB Repeat 702 735 . . . Note=TPR 7 +P17883 UniProtKB Repeat 736 769 . . . Note=TPR 8 +P17883 UniProtKB Repeat 945 985 . . . Note=TPR 9 +P17883 UniProtKB Repeat 987 1018 . . . Note=TPR 10 +P17883 UniProtKB Repeat 1226 1259 . . . Note=TPR 11 +P17883 UniProtKB Sequence conflict 985 985 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08491 1 747 +Q08491 UniProtKB Chain 1 747 . . . ID=PRO_0000269648;Note=Superkiller protein 7 +Q08491 UniProtKB Domain 265 503 . . . Note=tr-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +Q08491 UniProtKB Nucleotide binding 274 281 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08491 UniProtKB Nucleotide binding 356 360 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08491 UniProtKB Nucleotide binding 427 430 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q08491 UniProtKB Region 274 281 . . . Note=G1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +Q08491 UniProtKB Region 331 335 . . . Note=G2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +Q08491 UniProtKB Region 356 359 . . . Note=G3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +Q08491 UniProtKB Region 427 430 . . . Note=G4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +Q08491 UniProtKB Region 467 469 . . . Note=G5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +Q08491 UniProtKB Modified residue 88 88 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q08491 UniProtKB Modified residue 90 90 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q08491 UniProtKB Helix 121 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08491 UniProtKB Helix 150 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08491 UniProtKB Beta strand 185 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08491 UniProtKB Helix 197 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08491 UniProtKB Helix 212 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JEA +Q08491 UniProtKB Helix 258 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 266 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Helix 280 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Helix 296 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Helix 306 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Turn 311 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKE +Q08491 UniProtKB Helix 318 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Helix 325 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 337 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 350 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Helix 361 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Turn 365 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Helix 368 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 378 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Helix 390 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Helix 401 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Turn 410 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 422 427 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Helix 429 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Helix 436 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Helix 458 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 461 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Turn 468 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Helix 504 515 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Turn 522 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 528 536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 542 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 562 566 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 568 571 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 573 583 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 593 595 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 597 600 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 604 612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Turn 617 619 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 629 632 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 648 660 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 673 678 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 681 691 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 696 698 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 703 710 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 717 722 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 728 732 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +Q08491 UniProtKB Beta strand 738 744 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZKD +##sequence-region P42843 1 763 +P42843 UniProtKB Chain 1 763 . . . ID=PRO_0000203366;Note=F-box protein SKP2 +P42843 UniProtKB Domain 54 100 . . . Note=F-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00080 +P42843 UniProtKB Compositional bias 22 28 . . . Note=Poly-Glu +P42843 UniProtKB Modified residue 594 594 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P42843 UniProtKB Sequence conflict 16 16 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53327 1 1967 +P53327 UniProtKB Chain 1 1967 . . . ID=PRO_0000102085;Note=Antiviral helicase SLH1 +P53327 UniProtKB Domain 297 485 . . . Note=Helicase ATP-binding 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P53327 UniProtKB Domain 516 735 . . . Note=Helicase C-terminal 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P53327 UniProtKB Domain 795 1100 . . . Note=SEC63 1 +P53327 UniProtKB Domain 1149 1324 . . . Note=Helicase ATP-binding 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P53327 UniProtKB Domain 1355 1550 . . . Note=Helicase C-terminal 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P53327 UniProtKB Domain 1626 1776 . . . Note=SEC63 2 +P53327 UniProtKB Nucleotide binding 310 317 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P53327 UniProtKB Nucleotide binding 1162 1169 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P53327 UniProtKB Motif 427 430 . . . Note=DEVH box +P53327 UniProtKB Motif 1266 1269 . . . Note=DEAH box +P53327 UniProtKB Sequence conflict 27 27 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53327 UniProtKB Sequence conflict 51 51 . . . Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53327 UniProtKB Sequence conflict 51 51 . . . Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53327 UniProtKB Sequence conflict 193 193 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53327 UniProtKB Sequence conflict 193 193 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53327 UniProtKB Sequence conflict 438 438 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53327 UniProtKB Sequence conflict 438 438 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38247 1 162 +P38247 UniProtKB Chain 1 162 . . . ID=PRO_0000202479;Note=Protein SLM4 +P38247 UniProtKB Transmembrane 127 144 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38247 UniProtKB Helix 9 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX +P38247 UniProtKB Helix 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX +P38247 UniProtKB Beta strand 33 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX +P38247 UniProtKB Turn 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX +P38247 UniProtKB Beta strand 45 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX +P38247 UniProtKB Beta strand 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX +P38247 UniProtKB Helix 59 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX +P38247 UniProtKB Beta strand 92 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX +P38247 UniProtKB Beta strand 103 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX +P38247 UniProtKB Beta strand 115 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX +P38247 UniProtKB Beta strand 125 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX +P38247 UniProtKB Helix 139 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX +P38247 UniProtKB Helix 151 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FTX +##sequence-region Q00772 1 484 +Q00772 UniProtKB Chain 1 484 . . . ID=PRO_0000186338;Note=Mitogen-activated protein kinase SLT2/MPK1 +Q00772 UniProtKB Domain 23 318 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q00772 UniProtKB Nucleotide binding 29 37 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q00772 UniProtKB Motif 190 192 . . . Note=TXY +Q00772 UniProtKB Compositional bias 370 391 . . . Note=Poly-Gln +Q00772 UniProtKB Active site 153 153 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q00772 UniProtKB Binding site 54 54 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q00772 UniProtKB Modified residue 190 190 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q00772 UniProtKB Modified residue 192 192 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q00772 UniProtKB Sequence conflict 56 56 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q00772 UniProtKB Sequence conflict 467 467 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32908 1 1225 +P32908 UniProtKB Chain 1 1225 . . . ID=PRO_0000119011;Note=Structural maintenance of chromosomes protein 1 +P32908 UniProtKB Nucleotide binding 33 40 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32908 UniProtKB Region 490 678 . . . Note=Flexible hinge +P32908 UniProtKB Coiled coil 173 489 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32908 UniProtKB Coiled coil 679 1063 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32908 UniProtKB Motif 1057 1061 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32908 UniProtKB Compositional bias 1129 1164 . . . Note=Ala/Asp-rich (DA-box) +P32908 UniProtKB Mutagenesis 173 173 . . . Note=In temperature-sensitive mutant SMC1-2. S->L +P32908 UniProtKB Mutagenesis 458 458 . . . Note=In temperature-sensitive mutant SMC1-1. N->D +P32908 UniProtKB Beta strand 4 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Beta strand 17 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Beta strand 27 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Helix 39 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Helix 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Beta strand 91 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Beta strand 103 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Beta strand 117 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Beta strand 124 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Helix 128 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Turn 142 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Helix 156 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Helix 162 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Helix 170 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Turn 175 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Helix 179 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Helix 1051 1066 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Helix 1068 1081 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Beta strand 1096 1099 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Beta strand 1101 1106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Helix 1107 1109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Beta strand 1114 1117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Helix 1126 1128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Helix 1131 1146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Beta strand 1152 1158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Turn 1159 1162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Helix 1165 1178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Beta strand 1183 1188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Helix 1192 1195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Beta strand 1199 1207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Turn 1208 1211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Beta strand 1212 1219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +P32908 UniProtKB Helix 1220 1222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1W1W +##sequence-region P32566 1 505 +P32566 UniProtKB Chain 1 505 . . . ID=PRO_0000209870;Note=Cell wall assembly regulator SMI1 +P32566 UniProtKB Modified residue 202 202 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P32566 UniProtKB Modified residue 203 203 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32566 UniProtKB Modified residue 376 376 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32566 UniProtKB Modified residue 381 381 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32566 UniProtKB Modified residue 394 394 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P32566 UniProtKB Modified residue 400 400 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P32566 UniProtKB Cross-link 453 453 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32566 UniProtKB Helix 87 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B +P32566 UniProtKB Helix 106 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B +P32566 UniProtKB Helix 118 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B +P32566 UniProtKB Helix 134 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B +P32566 UniProtKB Beta strand 157 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B +P32566 UniProtKB Helix 167 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B +P32566 UniProtKB Beta strand 221 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B +P32566 UniProtKB Turn 225 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B +P32566 UniProtKB Beta strand 230 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B +P32566 UniProtKB Beta strand 237 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B +P32566 UniProtKB Beta strand 244 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B +P32566 UniProtKB Beta strand 263 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B +P32566 UniProtKB Beta strand 272 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B +P32566 UniProtKB Helix 281 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B +P32566 UniProtKB Beta strand 313 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B +P32566 UniProtKB Turn 318 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B +P32566 UniProtKB Helix 327 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5J1B +##sequence-region Q04174 1 516 +Q04174 UniProtKB Chain 1 516 . . . ID=PRO_0000071977;Note=GPI mannosyltransferase 4 +Q04174 UniProtKB Topological domain 1 5 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Transmembrane 6 26 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Topological domain 27 60 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Transmembrane 61 81 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Topological domain 82 175 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Transmembrane 176 196 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Topological domain 197 210 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Transmembrane 211 231 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Topological domain 232 270 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Transmembrane 271 291 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Topological domain 292 295 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Transmembrane 296 316 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Topological domain 317 317 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Transmembrane 318 338 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Topological domain 339 348 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Transmembrane 349 369 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Topological domain 370 516 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Glycosylation 403 403 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Glycosylation 452 452 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04174 UniProtKB Sequence conflict 122 123 . . . Note=IK->MQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q04174 UniProtKB Sequence conflict 122 123 . . . Note=IK->MQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q04174 UniProtKB Sequence conflict 163 163 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q04174 UniProtKB Sequence conflict 169 169 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q04174 UniProtKB Sequence conflict 279 279 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38990 1 1142 +P38990 UniProtKB Chain 1 1142 . . . ID=PRO_0000086464;Note=SNF1-activating kinase 1 +P38990 UniProtKB Domain 133 448 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38990 UniProtKB Nucleotide binding 139 147 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38990 UniProtKB Active site 277 277 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P38990 UniProtKB Binding site 162 162 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P38990 UniProtKB Modified residue 43 43 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38990 UniProtKB Modified residue 964 964 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38990 UniProtKB Modified residue 1126 1126 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198 +P38990 UniProtKB Sequence conflict 171 171 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38990 UniProtKB Sequence conflict 266 268 . . . Note=EYL->DS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39955 1 897 +P39955 UniProtKB Chain 1 897 . . . ID=PRO_0000084761;Note=Protein SAP1 +P39955 UniProtKB Nucleotide binding 645 652 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39955 UniProtKB Modified residue 536 536 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P53036 1 818 +P53036 UniProtKB Chain 1 818 . . . ID=PRO_0000097585;Note=SIT4-associating protein SAP4 +##sequence-region Q99314 1 248 +Q99314 UniProtKB Chain 1 248 . . . ID=PRO_0000097596;Note=Something about silencing protein 5 +Q99314 UniProtKB Domain 8 116 . . . Note=YEATS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00376 +Q99314 UniProtKB Modified residue 144 144 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q00711 1 640 +Q00711 UniProtKB Transit peptide 1 28 . . . Note=Mitochondrion;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1518827,ECO:0000269|PubMed:8120006;Dbxref=PMID:1518827,PMID:8120006 +Q00711 UniProtKB Chain 29 640 . . . ID=PRO_0000010342;Note=Succinate dehydrogenase [ubiquinone] flavoprotein subunit%2C mitochondrial +Q00711 UniProtKB Nucleotide binding 59 64 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +Q00711 UniProtKB Nucleotide binding 82 97 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +Q00711 UniProtKB Nucleotide binding 449 450 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +Q00711 UniProtKB Active site 331 331 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +Q00711 UniProtKB Binding site 266 266 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +Q00711 UniProtKB Binding site 287 287 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +Q00711 UniProtKB Binding site 299 299 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +Q00711 UniProtKB Binding site 398 398 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +Q00711 UniProtKB Binding site 433 433 . . . Note=FAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +Q00711 UniProtKB Binding site 444 444 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +Q00711 UniProtKB Modified residue 90 90 . . . Note=Tele-8alpha-FAD histidine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9YHT1 +Q00711 UniProtKB Mutagenesis 90 90 . . . Note=Abolishes covalent attachment of FAD. No effect on complex assembly. Abolishes succinate-dehydrogenase activity but no effect on fumarate reductase activity. H->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8026509;Dbxref=PMID:8026509 +##sequence-region Q04491 1 297 +Q04491 UniProtKB Chain 1 297 . . . ID=PRO_0000051206;Note=Protein transport protein SEC13 +Q04491 UniProtKB Repeat 7 46 . . . Note=WD 1 +Q04491 UniProtKB Repeat 51 92 . . . Note=WD 2 +Q04491 UniProtKB Repeat 97 138 . . . Note=WD 3 +Q04491 UniProtKB Repeat 143 195 . . . Note=WD 4 +Q04491 UniProtKB Repeat 202 244 . . . Note=WD 5 +Q04491 UniProtKB Repeat 252 291 . . . Note=WD 6 +Q04491 UniProtKB Mutagenesis 176 176 . . . Note=Leads to mislocalization of NPCs and overproliferation of the nuclear and ER membranes at 34 degree Celsius. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12215173;Dbxref=PMID:12215173 +Q04491 UniProtKB Mutagenesis 224 224 . . . Note=Growth inhibited above 30 degrees Celsius. S->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8432727;Dbxref=PMID:8432727 +Q04491 UniProtKB Mutagenesis 262 262 . . . Note=Growth inhibited above 30 degrees Celsius. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8432727;Dbxref=PMID:8432727 +Q04491 UniProtKB Mutagenesis 266 266 . . . Note=Growth inhibited above 34 degrees Celsius. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8432727;Dbxref=PMID:8432727 +Q04491 UniProtKB Beta strand 2 4 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +Q04491 UniProtKB Beta strand 5 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JRP +Q04491 UniProtKB Beta strand 12 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 21 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 33 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 56 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Helix 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 68 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 79 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +Q04491 UniProtKB Beta strand 102 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Helix 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 114 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 123 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 139 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 148 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 157 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +Q04491 UniProtKB Turn 162 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +Q04491 UniProtKB Beta strand 166 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MZK +Q04491 UniProtKB Beta strand 172 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 182 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Turn 189 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 193 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 207 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 217 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 227 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IKO +Q04491 UniProtKB Beta strand 231 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 244 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 257 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 264 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 269 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 274 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM6 +Q04491 UniProtKB Beta strand 278 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +Q04491 UniProtKB Beta strand 285 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM9 +Q04491 UniProtKB Beta strand 289 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2PM7 +##sequence-region P24280 1 304 +P24280 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2407740;Dbxref=PMID:2407740 +P24280 UniProtKB Chain 2 304 . . . ID=PRO_0000210744;Note=SEC14 cytosolic factor +P24280 UniProtKB Domain 99 272 . . . Note=CRAL-TRIO;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00056 +P24280 UniProtKB Modified residue 302 302 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P24280 UniProtKB Cross-link 42 42 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P24280 UniProtKB Cross-link 84 84 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P24280 UniProtKB Helix 6 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Turn 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 33 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 55 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Turn 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 69 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 91 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 100 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Beta strand 110 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Beta strand 120 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 126 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 131 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Turn 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 140 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 158 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Beta strand 173 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 184 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Beta strand 209 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 219 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 229 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 234 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Beta strand 240 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 248 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Turn 252 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Beta strand 257 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 262 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 272 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 284 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +P24280 UniProtKB Helix 288 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1AUA +##sequence-region P29478 1 273 +P29478 UniProtKB Chain 1 273 . . . ID=PRO_0000135212;Note=Signal recognition particle subunit SEC65 +##sequence-region Q02825 1 467 +Q02825 UniProtKB Chain 1 467 . . . ID=PRO_0000194034;Note=tRNA-splicing endonuclease subunit SEN54 +Q02825 UniProtKB Compositional bias 19 27 . . . Note=Poly-Glu +Q02825 UniProtKB Compositional bias 353 356 . . . Note=Poly-Asp +##sequence-region P40510 1 469 +P40510 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +P40510 UniProtKB Chain 2 469 . . . ID=PRO_0000076019;Note=D-3-phosphoglycerate dehydrogenase 2 +P40510 UniProtKB Domain 399 469 . . . Note=ACT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01007 +P40510 UniProtKB Nucleotide binding 208 209 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0 +P40510 UniProtKB Nucleotide binding 285 287 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0 +P40510 UniProtKB Nucleotide binding 347 350 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0 +P40510 UniProtKB Active site 287 287 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40510 UniProtKB Active site 316 316 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40510 UniProtKB Active site 347 347 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40510 UniProtKB Binding site 228 228 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0 +P40510 UniProtKB Binding site 311 311 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0 +P40510 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +P40510 UniProtKB Modified residue 22 22 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950;Dbxref=PMID:15665377,PMID:17330950 +P40510 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40510 UniProtKB Modified residue 33 33 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P46995 1 733 +P46995 UniProtKB Chain 1 733 . . . ID=PRO_0000186087;Note=Histone-lysine N-methyltransferase%2C H3 lysine-36 specific +P46995 UniProtKB Domain 63 118 . . . Note=AWS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00562 +P46995 UniProtKB Domain 120 237 . . . Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 +P46995 UniProtKB Domain 244 260 . . . Note=Post-SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00155 +P46995 UniProtKB Domain 475 507 . . . Note=WW +P46995 UniProtKB Region 619 718 . . . Note=Binding to RNA polymerase II CTD +P46995 UniProtKB Coiled coil 548 630 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46995 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46995 UniProtKB Modified residue 522 522 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46995 UniProtKB Mutagenesis 195 195 . . . Note=Reduces dramatically histone methyltransferase activity toward nucleosomes. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11839797;Dbxref=PMID:11839797 +P46995 UniProtKB Mutagenesis 201 201 . . . Note=Reduces dramatically histone methyltransferase activity toward nucleosomes. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11839797;Dbxref=PMID:11839797 +P46995 UniProtKB Sequence conflict 594 594 . . . Note=A->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46995 UniProtKB Sequence conflict 605 605 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46995 UniProtKB Sequence conflict 716 716 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46995 UniProtKB Beta strand 481 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E0N +P46995 UniProtKB Turn 495 498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E0N +P46995 UniProtKB Beta strand 499 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1E0N +P46995 UniProtKB Helix 624 645 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Z +P46995 UniProtKB Turn 648 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Z +P46995 UniProtKB Helix 655 676 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Z +P46995 UniProtKB Helix 688 712 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2C5Z +##sequence-region Q08446 1 395 +Q08446 UniProtKB Chain 1 395 . . . ID=PRO_0000185393;Note=Protein SGT1 +Q08446 UniProtKB Domain 182 277 . . . Note=CS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00547 +Q08446 UniProtKB Domain 312 395 . . . Note=SGS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00386 +Q08446 UniProtKB Modified residue 168 168 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q08446 UniProtKB Modified residue 171 171 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q08446 UniProtKB Cross-link 32 32 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q08446 UniProtKB Mutagenesis 31 31 . . . Note=In sgt1-3%3B induces arrest of cell division in G2/M%3B when associated with L-99 and I-213. L->P +Q08446 UniProtKB Mutagenesis 99 99 . . . Note=In sgt1-3%3B induces arrest of cell division in G2/M%3B when associated with P-31 I-213. F->L +Q08446 UniProtKB Mutagenesis 213 213 . . . Note=In sgt1-3%3B induces arrest of cell division in G2/M%3B when associated with P-31 and L-99. N->I +Q08446 UniProtKB Mutagenesis 220 220 . . . Note=In sgt1-5%3B induces arrest of cell division in G2/M%3B when associated with K-364. D->V +Q08446 UniProtKB Mutagenesis 364 364 . . . Note=In sgt1-5%3B induces arrest of cell division in G2/M%3B when associated with V-220. E->K +Q08446 UniProtKB Mutagenesis 371 371 . . . Note=In A364a%3B suppressor of the cdc35-1 allele. S->N +Q08446 UniProtKB Sequence conflict 13 13 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08446 UniProtKB Helix 4 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AN3 +Q08446 UniProtKB Helix 20 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AN3 +Q08446 UniProtKB Helix 38 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AN3 +Q08446 UniProtKB Helix 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AN3 +Q08446 UniProtKB Helix 61 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AN3 +Q08446 UniProtKB Helix 84 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AN3 +Q08446 UniProtKB Helix 104 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AN3 +Q08446 UniProtKB Helix 124 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AN3 +##sequence-region P53266 1 389 +P53266 UniProtKB Chain 1 389 . . . ID=PRO_0000215659;Note=Cytochrome oxidase assembly protein SHY1 +P53266 UniProtKB Topological domain 1 71 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53266 UniProtKB Transmembrane 72 92 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53266 UniProtKB Topological domain 93 341 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53266 UniProtKB Transmembrane 342 362 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53266 UniProtKB Topological domain 363 389 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38634 1 284 +P38634 UniProtKB Chain 1 284 . . . ID=PRO_0000097751;Note=Protein SIC1 +P38634 UniProtKB Compositional bias 124 135 . . . Note=Asp/Glu-rich (acidic) +P38634 UniProtKB Compositional bias 200 206 . . . Note=Asp/Glu-rich (acidic) +P38634 UniProtKB Modified residue 5 5 . . . Note=Phosphothreonine%3B by PHO85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9725902;Dbxref=PMID:9725902 +P38634 UniProtKB Modified residue 33 33 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9725902;Dbxref=PMID:9725902 +P38634 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9725902;Dbxref=PMID:9725902 +P38634 UniProtKB Modified residue 173 173 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000269|PubMed:15448699;Dbxref=PMID:17330950,PMID:15448699 +P38634 UniProtKB Modified residue 198 198 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198 +P38634 UniProtKB Modified residue 201 201 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38634 UniProtKB Modified residue 268 268 . . . Note=Lysine derivative +P38634 UniProtKB Modified residue 272 272 . . . Note=Lysine derivative +P38634 UniProtKB Modified residue 274 274 . . . Note=Lysine derivative +P38634 UniProtKB Mutagenesis 173 173 . . . Note=Impairs the ability to arrest the cell cycle. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15448699;Dbxref=PMID:15448699 +P38634 UniProtKB Sequence conflict 167 167 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38262 1 535 +P38262 UniProtKB Chain 1 535 . . . ID=PRO_0000051216;Note=SIR4-interacting protein SIF2 +P38262 UniProtKB Domain 4 36 . . . Note=LisH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00126 +P38262 UniProtKB Repeat 155 186 . . . Note=WD 1 +P38262 UniProtKB Repeat 218 248 . . . Note=WD 2 +P38262 UniProtKB Repeat 259 289 . . . Note=WD 3 +P38262 UniProtKB Repeat 316 345 . . . Note=WD 4 +P38262 UniProtKB Repeat 357 387 . . . Note=WD 5 +P38262 UniProtKB Repeat 399 428 . . . Note=WD 6 +P38262 UniProtKB Repeat 440 470 . . . Note=WD 7 +P38262 UniProtKB Repeat 503 534 . . . Note=WD 8 +P38262 UniProtKB Modified residue 137 137 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38262 UniProtKB Sequence conflict 396 396 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38262 UniProtKB Beta strand 152 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 161 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 172 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 181 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 198 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 223 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 232 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 244 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 253 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 264 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 273 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 285 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Turn 290 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 294 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 325 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 331 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Helix 337 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 341 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 352 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 362 368 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Turn 369 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 373 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 383 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 388 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 394 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 404 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Turn 411 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 414 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 422 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Turn 429 432 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 433 439 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 445 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 454 461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 466 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Helix 472 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 496 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 509 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 518 528 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +P38262 UniProtKB Beta strand 531 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1R5M +##sequence-region Q12216 1 726 +Q12216 UniProtKB Chain 1 726 . . . ID=PRO_0000218985;Note=E3 SUMO-protein ligase SIZ2 +Q12216 UniProtKB Domain 43 77 . . . Note=SAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00186 +Q12216 UniProtKB Domain 139 291 . . . Note=PINIT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00799 +Q12216 UniProtKB Zinc finger 323 400 . . . Note=SP-RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00452 +Q12216 UniProtKB Compositional bias 7 16 . . . Note=Poly-Asn +##sequence-region Q06315 1 1026 +Q06315 UniProtKB Chain 1 1026 . . . ID=PRO_0000269649;Note=Protein SKG3 +Q06315 UniProtKB Domain 90 221 . . . Note=PH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +Q06315 UniProtKB Domain 254 433 . . . Note=PH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +Q06315 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q06315 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06315 UniProtKB Modified residue 578 578 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06315 UniProtKB Modified residue 580 580 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06315 UniProtKB Modified residue 592 592 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q06315 UniProtKB Modified residue 701 701 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06315 UniProtKB Modified residue 954 954 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38314 1 527 +P38314 UniProtKB Chain 1 527 . . . ID=PRO_0000202512;Note=Protein SDS24 +P38314 UniProtKB Domain 114 175 . . . Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +P38314 UniProtKB Domain 198 256 . . . Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +P38314 UniProtKB Domain 283 342 . . . Note=CBS 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +P38314 UniProtKB Domain 443 512 . . . Note=CBS 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +P38314 UniProtKB Modified residue 94 94 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38314 UniProtKB Modified residue 458 458 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38314 UniProtKB Modified residue 524 524 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +##sequence-region P38164 1 1038 +P38164 UniProtKB Chain 1 1038 . . . ID=PRO_0000051470;Note=SEH-associated protein 4 +P38164 UniProtKB Repeat 50 90 . . . Note=WD 1 +P38164 UniProtKB Repeat 147 189 . . . Note=WD 2 +P38164 UniProtKB Repeat 235 276 . . . Note=WD 3 +P38164 UniProtKB Repeat 544 587 . . . Note=WD 4 +P38164 UniProtKB Modified residue 123 123 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38164 UniProtKB Modified residue 136 136 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q12745 1 709 +Q12745 UniProtKB Chain 1 709 . . . ID=PRO_0000234109;Note=Protein transport protein SEC39 +Q12745 UniProtKB Helix 33 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 49 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 54 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 102 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 105 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Turn 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 120 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Turn 139 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 143 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 156 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 166 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 182 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 190 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 212 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 218 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 228 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Turn 238 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 246 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 270 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 294 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Beta strand 310 314 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Turn 315 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Beta strand 318 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 322 334 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 341 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 352 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 373 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Turn 383 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Beta strand 392 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 399 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 416 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 432 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 457 477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 479 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 515 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Turn 521 523 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 526 535 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 539 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 543 556 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 565 582 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 586 603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 605 624 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 631 633 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 637 653 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 656 658 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +Q12745 UniProtKB Helix 659 673 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K8P +##sequence-region P33332 1 1336 +P33332 UniProtKB Chain 1 1336 . . . ID=PRO_0000118917;Note=Exocyst complex component SEC3 +P33332 UniProtKB Coiled coil 319 464 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33332 UniProtKB Coiled coil 1309 1336 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33332 UniProtKB Modified residue 290 290 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P33332 UniProtKB Modified residue 606 606 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P33332 UniProtKB Helix 76 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE +P33332 UniProtKB Beta strand 94 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M4Y +P33332 UniProtKB Beta strand 99 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58 +P33332 UniProtKB Beta strand 107 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE +P33332 UniProtKB Helix 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE +P33332 UniProtKB Beta strand 134 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE +P33332 UniProtKB Beta strand 151 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE +P33332 UniProtKB Helix 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58 +P33332 UniProtKB Beta strand 164 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE +P33332 UniProtKB Helix 172 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE +P33332 UniProtKB Beta strand 177 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE +P33332 UniProtKB Beta strand 187 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE +P33332 UniProtKB Helix 203 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE +P33332 UniProtKB Turn 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3A58 +P33332 UniProtKB Beta strand 229 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE +P33332 UniProtKB Beta strand 235 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HIE +P33332 UniProtKB Helix 240 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M4Y +##sequence-region P89102 1 971 +P89102 UniProtKB Chain 1 971 . . . ID=PRO_0000118924;Note=Exocyst complex component SEC5 +P89102 UniProtKB Coiled coil 123 182 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P89102 UniProtKB Modified residue 184 184 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P38890 1 526 +P38890 UniProtKB Chain 1 526 . . . ID=PRO_0000202942;Note=Putative protein lysine methyltransferase SET5 +P38890 UniProtKB Domain 112 403 . . . Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 +P38890 UniProtKB Modified residue 517 517 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q12507 1 346 +Q12507 UniProtKB Chain 1 346 . . . ID=PRO_0000269646;Note=Superficial pseudohyphal growth protein 1 +##sequence-region P40363 1 299 +P40363 UniProtKB Chain 1 299 . . . ID=PRO_0000210342;Note=S-formylglutathione hydrolase +P40363 UniProtKB Active site 161 161 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40363 UniProtKB Active site 241 241 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40363 UniProtKB Active site 276 276 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40363 UniProtKB Beta strand 2 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Beta strand 12 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Turn 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Beta strand 25 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Helix 36 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Beta strand 51 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Helix 62 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Helix 71 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Beta strand 81 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Beta strand 102 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Helix 117 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Helix 125 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Helix 132 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Beta strand 151 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Helix 162 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Helix 175 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Beta strand 181 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Helix 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Helix 196 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Helix 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Helix 218 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Helix 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Beta strand 233 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Helix 244 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Helix 251 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Turn 261 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Beta strand 266 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +P40363 UniProtKB Helix 278 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FOL +##sequence-region P47166 1 707 +P47166 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P47166 UniProtKB Chain 2 707 . . . ID=PRO_0000203121;Note=Protein SGM1 +P47166 UniProtKB Coiled coil 122 473 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47166 UniProtKB Coiled coil 594 706 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47166 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P47166 UniProtKB Modified residue 151 151 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P47166 UniProtKB Modified residue 538 538 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47166 UniProtKB Modified residue 549 549 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47166 UniProtKB Modified residue 568 568 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47166 UniProtKB Modified residue 571 571 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P47166 UniProtKB Modified residue 576 576 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47166 UniProtKB Modified residue 589 589 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P32578 1 815 +P32578 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32578 UniProtKB Chain 2 815 . . . ID=PRO_0000204374;Note=SNF1 protein kinase subunit beta-1 +P32578 UniProtKB Region 473 716 . . . Note=Kinase-interacting sequence (KIS)%3B required for interaction with SNF1 +P32578 UniProtKB Region 724 804 . . . Note=Association with SNF1 kinase complex (ASC) domain%3B required for interaction with SNF4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9121458;Dbxref=PMID:9121458 +P32578 UniProtKB Modified residue 33 33 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32578 UniProtKB Modified residue 181 181 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32578 UniProtKB Modified residue 198 198 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32578 UniProtKB Modified residue 200 200 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P32578 UniProtKB Modified residue 206 206 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32578 UniProtKB Modified residue 209 209 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32578 UniProtKB Modified residue 220 220 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32578 UniProtKB Modified residue 331 331 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P32578 UniProtKB Modified residue 494 494 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32578 UniProtKB Modified residue 497 497 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32578 UniProtKB Modified residue 643 643 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32578 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32578 UniProtKB Mutagenesis 2 2 . . . Note=Prevents relocalization to the vacuolar membrane. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14966266;Dbxref=PMID:14966266 +##sequence-region Q02793 1 397 +Q02793 UniProtKB Chain 1 397 . . . ID=PRO_0000051218;Note=Antiviral protein SKI8 +Q02793 UniProtKB Repeat 21 42 . . . Note=WD 1 +Q02793 UniProtKB Repeat 67 101 . . . Note=WD 2 +Q02793 UniProtKB Repeat 126 157 . . . Note=WD 3 +Q02793 UniProtKB Repeat 191 213 . . . Note=WD 4 +Q02793 UniProtKB Repeat 238 264 . . . Note=WD 5 +Q02793 UniProtKB Repeat 296 319 . . . Note=WD 6 +Q02793 UniProtKB Repeat 359 392 . . . Note=WD 7 +Q02793 UniProtKB Beta strand 4 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 15 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 19 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 26 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 36 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Helix 51 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 55 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 65 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Turn 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 79 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 93 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Turn 102 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 107 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Helix 119 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 124 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 139 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 150 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Helix 161 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Turn 165 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 172 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 182 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 191 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 198 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 207 213 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Turn 214 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 218 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 236 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 247 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 257 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Turn 265 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 270 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 288 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 294 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 301 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 313 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Turn 320 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 324 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Helix 333 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Helix 339 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 357 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Turn 365 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 368 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 378 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Turn 384 386 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +Q02793 UniProtKB Beta strand 387 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SQ9 +##sequence-region P33336 1 771 +P33336 UniProtKB Chain 1 771 . . . ID=PRO_0000097780;Note=Beta-glucan synthesis-associated protein SKN1 +P33336 UniProtKB Topological domain 1 289 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33336 UniProtKB Transmembrane 290 310 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33336 UniProtKB Topological domain 311 771 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33336 UniProtKB Domain 353 716 . . . Note=GH16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01098 +P33336 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33336 UniProtKB Modified residue 65 65 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33336 UniProtKB Modified residue 67 67 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33336 UniProtKB Modified residue 92 92 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32486 +P33336 UniProtKB Modified residue 103 103 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P33336 UniProtKB Modified residue 142 142 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32486 +P33336 UniProtKB Modified residue 162 162 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32486 +P33336 UniProtKB Modified residue 165 165 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32486 +P33336 UniProtKB Modified residue 170 170 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P32486 +P33336 UniProtKB Modified residue 176 176 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P33336 UniProtKB Glycosylation 337 337 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33336 UniProtKB Glycosylation 426 426 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33336 UniProtKB Glycosylation 513 513 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33336 UniProtKB Glycosylation 590 590 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33336 UniProtKB Glycosylation 615 615 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33336 UniProtKB Glycosylation 743 743 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12505 1 502 +Q12505 UniProtKB Chain 1 502 . . . ID=PRO_0000086657;Note=Serine/threonine-protein kinase SKS1 +Q12505 UniProtKB Domain 10 338 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12505 UniProtKB Nucleotide binding 16 24 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12505 UniProtKB Active site 186 186 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q12505 UniProtKB Binding site 39 39 . . . Note=ATP +Q12505 UniProtKB Mutagenesis 39 39 . . . Note=Loss of activity. K->R +##sequence-region Q03656 1 742 +Q03656 UniProtKB Chain 1 742 . . . ID=PRO_0000086658;Note=Serine/threonine-protein kinase SKY1 +Q03656 UniProtKB Domain 158 706 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03656 UniProtKB Nucleotide binding 164 172 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03656 UniProtKB Active site 294 294 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q03656 UniProtKB Binding site 187 187 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03656 UniProtKB Modified residue 383 383 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q03656 UniProtKB Modified residue 386 386 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03656 UniProtKB Modified residue 388 388 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03656 UniProtKB Modified residue 393 393 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q03656 UniProtKB Modified residue 410 410 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03656 UniProtKB Modified residue 427 427 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03656 UniProtKB Modified residue 432 432 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03656 UniProtKB Modified residue 445 445 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03656 UniProtKB Modified residue 449 449 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q03656 UniProtKB Modified residue 453 453 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q03656 UniProtKB Turn 154 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Beta strand 158 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Beta strand 168 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Turn 178 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Beta strand 182 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Helix 193 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Helix 216 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Beta strand 230 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Beta strand 239 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Helix 253 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Turn 260 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Helix 267 286 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Helix 297 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Beta strand 300 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Turn 539 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Beta strand 543 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Helix 551 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1HOW +Q03656 UniProtKB Helix 568 570 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Helix 573 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Helix 584 599 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Beta strand 610 612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Helix 615 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Helix 631 636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Helix 640 643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Beta strand 650 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Helix 661 667 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Helix 673 683 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Helix 684 687 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Turn 691 693 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Helix 697 701 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Helix 704 706 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +Q03656 UniProtKB Turn 710 714 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q99 +Q03656 UniProtKB Helix 726 728 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q99 +Q03656 UniProtKB Beta strand 732 734 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Q8Y +##sequence-region Q03406 1 294 +Q03406 UniProtKB Chain 1 294 . . . ID=PRO_0000071955;Note=DNA replication complex GINS protein SLD5 +Q03406 UniProtKB Mutagenesis 21 21 . . . Note=In sld5-8%3B temperature-sensitive mutant%3B in association with P-66. Defective in DNA replication. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12730134;Dbxref=PMID:12730134 +Q03406 UniProtKB Mutagenesis 66 66 . . . Note=In sld5-8%3B temperature-sensitive mutant%3B in association with P-21. Defective in DNA replication. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12730134;Dbxref=PMID:12730134 +Q03406 UniProtKB Mutagenesis 67 67 . . . Note=In sld5-12%3B temperature-sensitive mutant. Defective in DNA replication. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12730134;Dbxref=PMID:12730134 +Q03406 UniProtKB Mutagenesis 150 150 . . . Note=In sld5-2%3B temperature-sensitive mutant. Defective in DNA replication. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12730134;Dbxref=PMID:12730134 +Q03406 UniProtKB Mutagenesis 293 293 . . . Note=In sld5-13%3B temperature-sensitive mutant. Defective in DNA replication. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12730134;Dbxref=PMID:12730134 +Q03406 UniProtKB Sequence conflict 232 232 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03406 UniProtKB Helix 6 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4C95 +##sequence-region P38283 1 698 +P38283 UniProtKB Chain 1 698 . . . ID=PRO_0000071956;Note=Inner centromere protein-related protein SLI15 +P38283 UniProtKB Modified residue 268 268 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38283 UniProtKB Modified residue 489 489 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P38345 1 138 +P38345 UniProtKB Transit peptide 1 32 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38345 UniProtKB Chain 33 138 . . . ID=PRO_0000041936;Note=Succinate dehydrogenase assembly factor 4%2C mitochondrial +##sequence-region P38804 1 111 +P38804 UniProtKB Chain 1 111 . . . ID=PRO_0000202905;Note=Restriction of telomere capping protein 3 +P38804 UniProtKB Beta strand 5 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NYN +P38804 UniProtKB Beta strand 12 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NYN +P38804 UniProtKB Helix 23 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NYN +P38804 UniProtKB Helix 35 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NYN +P38804 UniProtKB Beta strand 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NYN +P38804 UniProtKB Beta strand 56 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NYN +P38804 UniProtKB Helix 65 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NYN +P38804 UniProtKB Helix 79 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NYN +P38804 UniProtKB Beta strand 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NYN +##sequence-region Q07953 1 250 +Q07953 UniProtKB Chain 1 250 . . . ID=PRO_0000123764;Note=Ribosome maturation protein SDO1 +Q07953 UniProtKB Mutagenesis 31 31 . . . Note=Impairs protein folding and stability. Loss of function. C->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15701631;Dbxref=PMID:15701631 +Q07953 UniProtKB Mutagenesis 34 34 . . . Note=Impairs protein folding and stability. Loss of function. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15701631;Dbxref=PMID:15701631 +Q07953 UniProtKB Mutagenesis 71 71 . . . Note=Impairs protein folding and stability. Loss of function. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15701631;Dbxref=PMID:15701631 +##sequence-region P40479 1 209 +P40479 UniProtKB Chain 1 209 . . . ID=PRO_0000094924;Note=Dual-specificity protein phosphatase SDP1 +P40479 UniProtKB Active site 140 140 . . . Note=Phosphocysteine intermediate +P40479 UniProtKB Binding site 111 111 . . . Note=Phosphotyrosine +P40479 UniProtKB Disulfide bond 47 142 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17495930;Dbxref=PMID:17495930 +P40479 UniProtKB Beta strand 58 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16 +P40479 UniProtKB Turn 65 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16 +P40479 UniProtKB Beta strand 68 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16 +P40479 UniProtKB Turn 76 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16 +P40479 UniProtKB Beta strand 83 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16 +P40479 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16 +P40479 UniProtKB Beta strand 103 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16 +P40479 UniProtKB Helix 112 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16 +P40479 UniProtKB Helix 119 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16 +P40479 UniProtKB Beta strand 136 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16 +P40479 UniProtKB Helix 146 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16 +P40479 UniProtKB Helix 163 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16 +P40479 UniProtKB Helix 181 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J16 +##sequence-region P53078 1 280 +P53078 UniProtKB Chain 1 280 . . . ID=PRO_0000072213;Note=Suppressor of disruption of TFIIS +P53078 UniProtKB Helix 6 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Beta strand 57 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Turn 63 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Helix 71 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Helix 93 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Helix 108 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Helix 122 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Turn 130 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Helix 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Helix 143 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Beta strand 155 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Beta strand 159 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Helix 169 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Beta strand 186 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Helix 205 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Helix 220 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Beta strand 223 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Helix 230 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Beta strand 242 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Beta strand 249 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPX +P53078 UniProtKB Helix 254 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ONN +P53078 UniProtKB Beta strand 264 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Helix 269 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +P53078 UniProtKB Helix 277 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NUQ +##sequence-region P20048 1 519 +P20048 UniProtKB Chain 1 519 . . . ID=PRO_0000097662;Note=Dolichol kinase +P20048 UniProtKB Topological domain 1 47 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Transmembrane 48 68 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Topological domain 69 88 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Transmembrane 89 109 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Topological domain 110 118 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Transmembrane 119 139 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Topological domain 140 151 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Transmembrane 152 172 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Topological domain 173 181 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Transmembrane 182 203 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Topological domain 204 223 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Transmembrane 224 244 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Topological domain 245 253 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Transmembrane 254 274 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Topological domain 275 294 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Transmembrane 295 315 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Topological domain 316 326 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Transmembrane 327 347 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Topological domain 348 349 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Transmembrane 350 370 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Topological domain 371 394 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Transmembrane 395 415 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Topological domain 416 417 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Transmembrane 418 438 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Topological domain 439 449 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Transmembrane 450 470 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Topological domain 471 472 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Transmembrane 473 493 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P20048 UniProtKB Topological domain 494 519 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P14906 1 663 +P14906 UniProtKB Chain 1 663 . . . ID=PRO_0000071095;Note=Protein translocation protein SEC63 +P14906 UniProtKB Topological domain 1 13 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14906 UniProtKB Transmembrane 14 41 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14906 UniProtKB Topological domain 42 92 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14906 UniProtKB Transmembrane 93 108 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14906 UniProtKB Topological domain 109 220 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14906 UniProtKB Transmembrane 221 239 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14906 UniProtKB Topological domain 240 663 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14906 UniProtKB Domain 123 198 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +P14906 UniProtKB Domain 228 532 . . . Note=SEC63 +P14906 UniProtKB Repeat 461 471 . . . Note=1 +P14906 UniProtKB Repeat 493 503 . . . Note=2 +P14906 UniProtKB Region 461 503 . . . Note=2 X 11 AA repeats +P14906 UniProtKB Compositional bias 612 663 . . . Note=Asp/Glu-rich (highly acidic) +P14906 UniProtKB Modified residue 512 512 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P14906 UniProtKB Mutagenesis 179 179 . . . Note=Temperature-sensitive. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8514125;Dbxref=PMID:8514125 +P14906 UniProtKB Mutagenesis 426 426 . . . Note=Temperature-sensitive. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8514125;Dbxref=PMID:8514125 +P14906 UniProtKB Mutagenesis 431 431 . . . Note=Temperature-sensitive. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8514125;Dbxref=PMID:8514125 +P14906 UniProtKB Mutagenesis 503 503 . . . Note=Temperature-sensitive. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8514125;Dbxref=PMID:8514125 +P14906 UniProtKB Mutagenesis 511 511 . . . Note=Temperature-sensitive. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8514125;Dbxref=PMID:8514125 +P14906 UniProtKB Mutagenesis 652 652 . . . Note=Abolishes interaction with SEC62%3B defect in protein translocation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15671059;Dbxref=PMID:15671059 +P14906 UniProtKB Mutagenesis 654 654 . . . Note=Abolishes interaction with SEC62%3B defect in protein translocation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15671059;Dbxref=PMID:15671059 +P14906 UniProtKB Sequence conflict 263 263 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P14906 UniProtKB Sequence conflict 293 293 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04279 1 960 +Q04279 UniProtKB Chain 1 960 . . . ID=PRO_0000203284;Note=Eisosome protein SEG1 +Q04279 UniProtKB Compositional bias 941 960 . . . Note=Lys-rich (basic%2C sufficient to bind lipids%2C important for targeting the protein to the plasma membrane in small buds) +Q04279 UniProtKB Modified residue 48 48 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q04279 UniProtKB Modified residue 220 220 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04279 UniProtKB Modified residue 235 235 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q04279 UniProtKB Modified residue 238 238 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q04279 UniProtKB Modified residue 319 319 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04279 UniProtKB Modified residue 339 339 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04279 UniProtKB Modified residue 352 352 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q04279 UniProtKB Modified residue 434 434 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04279 UniProtKB Modified residue 461 461 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q04279 UniProtKB Modified residue 467 467 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04279 UniProtKB Modified residue 630 630 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04279 UniProtKB Modified residue 675 675 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +Q04279 UniProtKB Modified residue 758 758 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q04279 UniProtKB Modified residue 816 816 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q04279 UniProtKB Modified residue 818 818 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q04279 UniProtKB Modified residue 855 855 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04279 UniProtKB Sequence conflict 167 167 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53011 1 349 +P53011 UniProtKB Chain 1 349 . . . ID=PRO_0000051215;Note=Nucleoporin SEH1 +P53011 UniProtKB Repeat 7 46 . . . Note=WD 1 +P53011 UniProtKB Repeat 53 94 . . . Note=WD 2 +P53011 UniProtKB Repeat 106 147 . . . Note=WD 3 +P53011 UniProtKB Repeat 153 192 . . . Note=WD 4 +P53011 UniProtKB Repeat 210 253 . . . Note=WD 5 +P53011 UniProtKB Repeat 302 341 . . . Note=WD 6 +P53011 UniProtKB Modified residue 257 257 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53011 UniProtKB Beta strand 12 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 19 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 31 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 40 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 45 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 58 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Helix 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 70 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 77 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3P +P53011 UniProtKB Beta strand 81 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 97 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 111 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Helix 119 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 123 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 133 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 149 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 163 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3P +P53011 UniProtKB Beta strand 169 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 177 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 182 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 190 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 202 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 215 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 227 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 240 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 291 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 307 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 314 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 319 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 328 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +P53011 UniProtKB Beta strand 339 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3F3F +##sequence-region O94742 1 89 +O94742 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +O94742 UniProtKB Chain 2 89 . . . ID=PRO_0000122970;Note=26S proteasome complex subunit SEM1 +O94742 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +O94742 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +O94742 UniProtKB Helix 28 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5UBP +O94742 UniProtKB Beta strand 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5UBP +O94742 UniProtKB Beta strand 64 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5UBP +O94742 UniProtKB Helix 72 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5UBP +##sequence-region P53953 1 876 +P53953 UniProtKB Chain 1 876 . . . ID=PRO_0000205151;Note=SED5-binding protein 2 +P53953 UniProtKB Region 164 189 . . . Note=Zinc finger-like +P53953 UniProtKB Compositional bias 311 320 . . . Note=Poly-Glu +P53953 UniProtKB Modified residue 51 51 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198 +##sequence-region P43682 1 97 +P43682 UniProtKB Chain 1 97 . . . ID=PRO_0000097712;Note=Protein transport protein SFT1 +P43682 UniProtKB Topological domain 1 74 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43682 UniProtKB Transmembrane 75 94 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43682 UniProtKB Topological domain 95 97 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43682 UniProtKB Domain 7 69 . . . Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202 +##sequence-region P38166 1 215 +P38166 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38166 UniProtKB Chain 2 215 . . . ID=PRO_0000097713;Note=Protein transport protein SFT2 +P38166 UniProtKB Topological domain 2 81 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38166 UniProtKB Transmembrane 82 102 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38166 UniProtKB Topological domain 103 111 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38166 UniProtKB Transmembrane 112 132 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38166 UniProtKB Topological domain 133 145 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38166 UniProtKB Transmembrane 146 166 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38166 UniProtKB Topological domain 167 172 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38166 UniProtKB Transmembrane 173 193 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38166 UniProtKB Topological domain 194 215 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38166 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38166 UniProtKB Modified residue 60 60 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P40561 1 250 +P40561 UniProtKB Chain 1 250 . . . ID=PRO_0000081956;Note=RNA-binding protein SGN1 +P40561 UniProtKB Domain 64 141 . . . Note=RRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +##sequence-region Q08490 1 590 +Q08490 UniProtKB Chain 1 590 . . . ID=PRO_0000055450;Note=Shugoshin +Q08490 UniProtKB Coiled coil 25 86 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08490 UniProtKB Mutagenesis 379 379 . . . Note=In sgo1-100%3B induces a lack of response when chromosomes that are not under tension. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637284;Dbxref=PMID:15637284 +Q08490 UniProtKB Mutagenesis 390 390 . . . Note=In sgo1-700%3B induces a lack of response when chromosomes that are not under tension. P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15637284;Dbxref=PMID:15637284 +##sequence-region P46954 1 829 +P46954 UniProtKB Chain 1 829 . . . ID=PRO_0000114979;Note=Protein SIP4 +P46954 UniProtKB DNA binding 46 73 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P46954 UniProtKB Sequence conflict 656 656 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P21691 1 654 +P21691 UniProtKB Chain 1 654 . . . ID=PRO_0000097767;Note=Regulatory protein SIR1 +P21691 UniProtKB Region 322 654 . . . Note=Sufficient for interaction with SIR4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Region 449 587 . . . Note=ORC interacting region (OIR) +P21691 UniProtKB Mutagenesis 462 464 . . . Note=No effect. EEE->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 466 466 . . . Note=Abolishes interaction with ORC1. V->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 469 469 . . . Note=Abolishes interaction with ORC1. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 470 470 . . . Note=Abolishes interaction with ORC1 and SIR4. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 477 477 . . . Note=Abolishes interaction with ORC1 and SIR4. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 479 479 . . . Note=Abolishes interaction with ORC1. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 480 480 . . . Note=Abolishes interaction with ORC1. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 482 483 . . . Note=No effect. EE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 489 490 . . . Note=No effect. KD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 498 499 . . . Note=No effect. KD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 513 513 . . . Note=Abolishes interaction with ORC1 and SIR4. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 517 518 . . . Note=No effect. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 534 534 . . . Note=No effect. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 538 540 . . . Note=Abolishes interaction with SIR4. KKK->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 569 569 . . . Note=No effect. C->A +P21691 UniProtKB Mutagenesis 571 571 . . . Note=Abolishes interaction with ORC1 and SIR4. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 572 572 . . . Note=No effect. V->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 573 573 . . . Note=No effect. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 577 578 . . . Note=Abolishes interaction with SIR4. DD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 584 584 . . . Note=Abolishes interaction with ORC1 and SIR4. L->P%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Mutagenesis 586 587 . . . Note=Abolishes interaction with SIR4. DD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14701749;Dbxref=PMID:14701749 +P21691 UniProtKB Beta strand 464 473 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A +P21691 UniProtKB Beta strand 476 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A +P21691 UniProtKB Turn 480 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A +P21691 UniProtKB Beta strand 484 486 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A +P21691 UniProtKB Helix 493 496 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A +P21691 UniProtKB Helix 499 506 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A +P21691 UniProtKB Helix 513 516 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A +P21691 UniProtKB Beta strand 523 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A +P21691 UniProtKB Helix 530 533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A +P21691 UniProtKB Beta strand 537 543 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A +P21691 UniProtKB Beta strand 547 550 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A +P21691 UniProtKB Beta strand 566 575 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A +P21691 UniProtKB Beta strand 577 579 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZBX +P21691 UniProtKB Beta strand 581 586 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1Z1A +##sequence-region P39980 1 628 +P39980 UniProtKB Chain 1 628 . . . ID=PRO_0000084878;Note=Siderophore iron transporter 1 +P39980 UniProtKB Transmembrane 68 88 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39980 UniProtKB Transmembrane 107 127 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39980 UniProtKB Transmembrane 132 152 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39980 UniProtKB Transmembrane 164 184 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39980 UniProtKB Transmembrane 194 214 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39980 UniProtKB Transmembrane 225 245 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39980 UniProtKB Transmembrane 285 305 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39980 UniProtKB Transmembrane 317 337 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39980 UniProtKB Transmembrane 354 374 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39980 UniProtKB Transmembrane 394 414 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39980 UniProtKB Transmembrane 420 440 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39980 UniProtKB Transmembrane 448 468 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39980 UniProtKB Transmembrane 488 508 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39980 UniProtKB Transmembrane 559 579 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39980 UniProtKB Sequence conflict 386 386 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53965 1 281 +P53965 UniProtKB Chain 1 281 . . . ID=PRO_0000094922;Note=Tyrosine-protein phosphatase SIW14 +P53965 UniProtKB Active site 214 214 . . . Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10044 +P53965 UniProtKB Modified residue 94 94 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region Q04195 1 904 +Q04195 UniProtKB Chain 1 904 . . . ID=PRO_0000245783;Note=E3 SUMO-protein ligase SIZ1 +Q04195 UniProtKB Domain 34 68 . . . Note=SAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00186 +Q04195 UniProtKB Domain 162 314 . . . Note=PINIT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00799 +Q04195 UniProtKB Zinc finger 346 423 . . . Note=SP-RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00452 +Q04195 UniProtKB Region 794 904 . . . Note=Required for localization at the bud neck +Q04195 UniProtKB Modified residue 132 132 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04195 UniProtKB Modified residue 794 794 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04195 UniProtKB Mutagenesis 361 361 . . . Note=Reduces E3 activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11577116;Dbxref=PMID:11577116 +Q04195 UniProtKB Mutagenesis 377 377 . . . Note=Strongly reduces E3 activity%2C but no effect on subcellular location. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11577116,ECO:0000269|PubMed:11587849,ECO:0000269|PubMed:12761287;Dbxref=PMID:11577116,PMID:11587849,PMID:12761287 +Q04195 UniProtKB Mutagenesis 400 400 . . . Note=Reduces E3 activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11577116;Dbxref=PMID:11577116 +Q04195 UniProtKB Mutagenesis 460 460 . . . Note=No effect on E3 activity. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11577116;Dbxref=PMID:11577116 +Q04195 UniProtKB Helix 4 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNN +Q04195 UniProtKB Beta strand 16 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNN +Q04195 UniProtKB Helix 21 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNN +Q04195 UniProtKB Helix 39 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNN +Q04195 UniProtKB Helix 57 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNN +Q04195 UniProtKB Helix 79 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNN +Q04195 UniProtKB Helix 101 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2RNN +Q04195 UniProtKB Beta strand 169 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Beta strand 183 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Beta strand 199 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Helix 213 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Beta strand 226 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Helix 241 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Beta strand 250 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Beta strand 269 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JNE +Q04195 UniProtKB Helix 273 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Helix 281 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Beta strand 287 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Beta strand 291 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Beta strand 304 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Helix 316 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Helix 331 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Beta strand 354 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Turn 362 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Beta strand 365 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Beta strand 369 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Helix 385 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Turn 401 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Helix 409 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Beta strand 412 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Helix 416 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Beta strand 431 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Beta strand 440 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3I2D +Q04195 UniProtKB Beta strand 456 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JNE +Q04195 UniProtKB Beta strand 467 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JNE +Q04195 UniProtKB Helix 479 488 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JNE +Q04195 UniProtKB Helix 504 506 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JNE +Q04195 UniProtKB Beta strand 507 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JNE +Q04195 UniProtKB Turn 540 544 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JNE +Q04195 UniProtKB Beta strand 549 555 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5JNE +##sequence-region Q3E784 1 85 +Q3E784 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +Q3E784 UniProtKB Chain 2 85 . . . ID=PRO_0000076321;Note=SCOCO-like protein 1 +Q3E784 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +Q3E784 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q3E784 UniProtKB Mutagenesis 72 72 . . . Note=Disrupts interaction with ARL3. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12620189;Dbxref=PMID:12620189 +##sequence-region Q02775 1 382 +Q02775 UniProtKB Chain 1 382 . . . ID=PRO_0000218554;Note=Pre-mRNA-splicing factor SLU7 +Q02775 UniProtKB Zinc finger 120 137 . . . Note=CCHC-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00047 +Q02775 UniProtKB Region 200 224 . . . Note=Interaction with PRP8 +Q02775 UniProtKB Modified residue 120 120 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q02775 UniProtKB Modified residue 212 212 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q02775 UniProtKB Mutagenesis 122 122 . . . Note=Affects the ability to associate with the spliceosome. Loss of growth and in vitro splicing activity%3B when associated with 215-AAA-217. Cryo- and thermosensitivity%3B when associated with A-217. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12212850;Dbxref=PMID:12212850 +Q02775 UniProtKB Mutagenesis 130 130 . . . Note=Affects the ability to associate with the spliceosome. Loss of growth and in vitro splicing activity%3B when associated with 215-AAA-217. Cryo- and thermosensitivity%3B when associated with A-217. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12212850;Dbxref=PMID:12212850 +Q02775 UniProtKB Mutagenesis 135 135 . . . Note=Affects the ability to associate with the spliceosome. Loss of growth%2C spliceosome binding%2C and in vitro splicing activity%3B when associated with 215-AAA-217. Cryo- and thermosensitivity%3B when associated with A-217. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12212850;Dbxref=PMID:12212850 +Q02775 UniProtKB Mutagenesis 215 217 . . . Note=Abolishes the interaction with PRP18%2C and temperature sensitive growth defect. Loss of growth and in vitro splicing activity%3B when associated with A-122 or A-130 or A-135. EIE->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12212850;Dbxref=PMID:12212850 +Q02775 UniProtKB Mutagenesis 217 217 . . . Note=Abolishes the interaction with PRP18. Cryo- and thermosensitivity%3B when associated with A-122 or A-130 or A-135. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12212850;Dbxref=PMID:12212850 +Q02775 UniProtKB Mutagenesis 217 217 . . . Note=Abolishes the interaction with PRP18%2C and temperature sensitive growth defect. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12212850;Dbxref=PMID:12212850 +Q02775 UniProtKB Mutagenesis 221 224 . . . Note=Abolishes the interaction with PRP18%2C and temperature sensitive growth defect. LELY->AAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12212850;Dbxref=PMID:12212850 +Q02775 UniProtKB Sequence conflict 235 235 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40072 1 274 +P40072 UniProtKB Chain 1 274 . . . ID=PRO_0000056336;Note=E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX8 +P40072 UniProtKB Zinc finger 206 250 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +P40072 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40072 UniProtKB Modified residue 66 66 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P40072 UniProtKB Modified residue 67 67 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region Q12334 1 223 +Q12334 UniProtKB Chain 1 223 . . . ID=PRO_0000252298;Note=Protein SCM3 +Q12334 UniProtKB Helix 94 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L5A +Q12334 UniProtKB Beta strand 125 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L5A +Q12334 UniProtKB Helix 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L5A +Q12334 UniProtKB Helix 154 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L5A +##sequence-region P23833 1 295 +P23833 UniProtKB Transmembrane 76 92 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23833 UniProtKB Metal binding 148 148 . . . Note=Copper;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23833 UniProtKB Metal binding 152 152 . . . Note=Copper;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23833 UniProtKB Metal binding 239 239 . . . Note=Copper;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P23833 UniProtKB Beta strand 120 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K +P23833 UniProtKB Beta strand 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K +P23833 UniProtKB Helix 131 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K +P23833 UniProtKB Beta strand 139 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K +P23833 UniProtKB Helix 151 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K +P23833 UniProtKB Beta strand 175 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K +P23833 UniProtKB Turn 183 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K +P23833 UniProtKB Helix 188 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K +P23833 UniProtKB Beta strand 203 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K +P23833 UniProtKB Helix 209 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K +P23833 UniProtKB Turn 237 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K +P23833 UniProtKB Beta strand 243 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K +P23833 UniProtKB Beta strand 252 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K +P23833 UniProtKB Helix 264 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7K +P23833 UniProtKB Beta strand 284 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B7J +##sequence-region P38072 1 301 +P38072 UniProtKB Transmembrane 82 98 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38072 UniProtKB Domain 101 284 . . . Note=Thioredoxin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00691 +P38072 UniProtKB Metal binding 154 154 . . . Note=Copper;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38072 UniProtKB Metal binding 158 158 . . . Note=Copper;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38072 UniProtKB Metal binding 245 245 . . . Note=Copper;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P11655 1 471 +P11655 UniProtKB Chain 1 471 . . . ID=PRO_0000097657;Note=Guanine nucleotide-exchange factor SEC12 +P11655 UniProtKB Topological domain 1 354 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922074;Dbxref=PMID:1922074 +P11655 UniProtKB Transmembrane 355 373 . . . Note=Helical%3B Signal-anchor for type II membrane protein +P11655 UniProtKB Topological domain 374 471 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1922074;Dbxref=PMID:1922074 +P11655 UniProtKB Repeat 259 300 . . . Note=WD 1 +P11655 UniProtKB Repeat 302 341 . . . Note=WD 2 +P11655 UniProtKB Glycosylation 439 439 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P11655 UniProtKB Glycosylation 462 462 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P11655 UniProtKB Beta strand 5 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 14 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 24 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 33 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 40 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Helix 54 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 58 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 75 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 82 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Helix 91 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 103 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Turn 110 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 114 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 133 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 145 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 155 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Turn 161 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 165 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 178 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 185 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 196 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Turn 201 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 206 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 217 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 229 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 242 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 253 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 269 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 280 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 290 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Turn 295 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 299 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 307 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 312 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 323 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Beta strand 331 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +P11655 UniProtKB Turn 340 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H5I +##sequence-region P22224 1 910 +P22224 UniProtKB Chain 1 910 . . . ID=PRO_0000118959;Note=Exocyst complex component SEC15 +P22224 UniProtKB Coiled coil 88 116 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22224 UniProtKB Modified residue 286 286 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P30619 1 724 +P30619 UniProtKB Chain 1 724 . . . ID=PRO_0000206297;Note=Protein transport protein SEC1 +##sequence-region P22214 1 214 +P22214 UniProtKB Chain 1 214 . . . ID=PRO_0000206769;Note=Protein transport protein SEC22 +P22214 UniProtKB Topological domain 1 192 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22214 UniProtKB Transmembrane 193 213 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22214 UniProtKB Topological domain 214 214 . . . Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22214 UniProtKB Domain 6 117 . . . Note=Longin;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00231 +P22214 UniProtKB Domain 132 192 . . . Note=v-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00290 +P22214 UniProtKB Modified residue 160 160 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P07560 1 215 +P07560 UniProtKB Chain 1 215 . . . ID=PRO_0000121330;Note=Ras-related protein SEC4 +P07560 UniProtKB Nucleotide binding 27 34 . . . Note=GTP +P07560 UniProtKB Nucleotide binding 75 79 . . . Note=GTP +P07560 UniProtKB Nucleotide binding 133 136 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07560 UniProtKB Motif 49 57 . . . Note=Effector region;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07560 UniProtKB Modified residue 201 201 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P07560 UniProtKB Modified residue 204 204 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P07560 UniProtKB Lipidation 214 214 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07560 UniProtKB Lipidation 215 215 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07560 UniProtKB Beta strand 20 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16 +P07560 UniProtKB Beta strand 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EQB +P07560 UniProtKB Helix 33 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16 +P07560 UniProtKB Beta strand 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EQB +P07560 UniProtKB Helix 49 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z8Y +P07560 UniProtKB Beta strand 57 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16 +P07560 UniProtKB Beta strand 68 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16 +P07560 UniProtKB Helix 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16 +P07560 UniProtKB Helix 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4Z8Y +P07560 UniProtKB Helix 87 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16 +P07560 UniProtKB Beta strand 93 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16 +P07560 UniProtKB Helix 105 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16 +P07560 UniProtKB Helix 111 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16 +P07560 UniProtKB Turn 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CPH +P07560 UniProtKB Beta strand 127 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16 +P07560 UniProtKB Beta strand 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EQB +P07560 UniProtKB Helix 144 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16 +P07560 UniProtKB Beta strand 158 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16 +P07560 UniProtKB Turn 163 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16 +P07560 UniProtKB Helix 169 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1G16 +P07560 UniProtKB Turn 183 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EQB +##sequence-region P11075 1 2009 +P11075 UniProtKB Chain 1 2009 . . . ID=PRO_0000120214;Note=Protein transport protein SEC7 +P11075 UniProtKB Domain 824 1010 . . . Note=SEC7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00189 +P11075 UniProtKB Compositional bias 89 213 . . . Note=Asp/Glu-rich (highly acidic) +P11075 UniProtKB Modified residue 212 212 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198 +P11075 UniProtKB Modified residue 215 215 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P11075 UniProtKB Modified residue 334 334 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P11075 UniProtKB Modified residue 447 447 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P11075 UniProtKB Modified residue 452 452 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P11075 UniProtKB Modified residue 455 455 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P11075 UniProtKB Modified residue 807 807 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P11075 UniProtKB Modified residue 1226 1226 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P11075 UniProtKB Modified residue 1240 1240 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P11075 UniProtKB Modified residue 1741 1741 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P11075 UniProtKB Modified residue 1752 1752 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P11075 UniProtKB Cross-link 797 797 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P11075 UniProtKB Sequence conflict 188 188 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11075 UniProtKB Sequence conflict 399 400 . . . Note=FV->LL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11075 UniProtKB Sequence conflict 402 402 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11075 UniProtKB Sequence conflict 1031 1034 . . . Note=QQSA->PAIC;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11075 UniProtKB Sequence conflict 1036 1037 . . . Note=NF->QL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11075 UniProtKB Helix 830 840 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY +P11075 UniProtKB Helix 842 851 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY +P11075 UniProtKB Beta strand 854 856 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY +P11075 UniProtKB Helix 860 869 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY +P11075 UniProtKB Helix 875 883 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY +P11075 UniProtKB Helix 887 898 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY +P11075 UniProtKB Helix 907 915 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY +P11075 UniProtKB Helix 924 941 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY +P11075 UniProtKB Helix 949 967 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY +P11075 UniProtKB Beta strand 970 972 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY +P11075 UniProtKB Helix 977 983 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY +P11075 UniProtKB Turn 984 987 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY +P11075 UniProtKB Helix 995 1007 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OIY +##sequence-region P32855 1 1065 +P32855 UniProtKB Chain 1 1065 . . . ID=PRO_0000118942;Note=Exocyst complex component SEC8 +P32855 UniProtKB Coiled coil 114 148 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32855 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32855 UniProtKB Modified residue 19 19 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P40316 1 373 +P40316 UniProtKB Chain 1 373 . . . ID=PRO_0000206366;Note=Securin +P40316 UniProtKB Motif 85 88 . . . Note=D-box +P40316 UniProtKB Modified residue 185 185 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40316 UniProtKB Modified residue 186 186 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40316 UniProtKB Modified residue 212 212 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40316 UniProtKB Modified residue 213 213 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40316 UniProtKB Modified residue 277 277 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40316 UniProtKB Modified residue 292 292 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12050115;Dbxref=PMID:12050115 +P40316 UniProtKB Mutagenesis 85 88 . . . Note=Abolishes ubiquitination and subsequent degradation. RLPL->ALPA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8985178;Dbxref=PMID:8985178 +P40316 UniProtKB Mutagenesis 277 277 . . . Note=Affects phosphorylation and the interaction with ESP1. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12050115;Dbxref=PMID:12050115 +P40316 UniProtKB Mutagenesis 292 292 . . . Note=Affects phosphorylation and the interaction with ESP1. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12050115;Dbxref=PMID:12050115 +P40316 UniProtKB Mutagenesis 304 304 . . . Note=No effect. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12050115;Dbxref=PMID:12050115 +P40316 UniProtKB Helix 273 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +P40316 UniProtKB Helix 281 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +P40316 UniProtKB Helix 365 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5U1T +##sequence-region P25365 1 1065 +P25365 UniProtKB Chain 1 1065 . . . ID=PRO_0000051211;Note=Putative guanine nucleotide-exchange factor SED4 +P25365 UniProtKB Topological domain 1 346 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25365 UniProtKB Transmembrane 347 365 . . . Note=Helical%3B Signal-anchor for type II membrane protein +P25365 UniProtKB Topological domain 366 1065 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25365 UniProtKB Repeat 259 298 . . . Note=WD 1 +P25365 UniProtKB Repeat 302 341 . . . Note=WD 2 +P25365 UniProtKB Repeat 824 833 . . . Note=1 +P25365 UniProtKB Repeat 834 843 . . . Note=2 +P25365 UniProtKB Repeat 844 853 . . . Note=3 +P25365 UniProtKB Repeat 854 863 . . . Note=4 +P25365 UniProtKB Region 824 863 . . . Note=4 X 10 AA tandem repeats +P25365 UniProtKB Motif 1062 1065 . . . Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10138 +P25365 UniProtKB Compositional bias 467 476 . . . Note=Poly-Ser +P25365 UniProtKB Compositional bias 579 590 . . . Note=Poly-Ser +P25365 UniProtKB Modified residue 65 65 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25365 UniProtKB Glycosylation 388 388 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25365 UniProtKB Glycosylation 620 620 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25365 UniProtKB Glycosylation 1039 1039 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39707 1 275 +P39707 UniProtKB Chain 1 275 . . . ID=PRO_0000109468;Note=tRNA-splicing endonuclease subunit SEN34 +P39707 UniProtKB Active site 209 209 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39707 UniProtKB Active site 217 217 . . . . +P39707 UniProtKB Active site 250 250 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39707 UniProtKB Mutagenesis 217 217 . . . Note=Loss of function%3B induces a marked accumulation of 5' exon and intron-3' exon 2/3 molecule. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9200603;Dbxref=PMID:9200603 +##sequence-region P40054 1 469 +P40054 UniProtKB Chain 1 469 . . . ID=PRO_0000076018;Note=D-3-phosphoglycerate dehydrogenase 1 +P40054 UniProtKB Domain 399 469 . . . Note=ACT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01007 +P40054 UniProtKB Nucleotide binding 208 209 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0 +P40054 UniProtKB Nucleotide binding 285 287 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0 +P40054 UniProtKB Nucleotide binding 347 350 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0 +P40054 UniProtKB Active site 287 287 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40054 UniProtKB Active site 316 316 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40054 UniProtKB Active site 347 347 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40054 UniProtKB Binding site 228 228 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0 +P40054 UniProtKB Binding site 311 311 . . . Note=NAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A9T0 +P40054 UniProtKB Modified residue 22 22 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40054 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P40510 +P40054 UniProtKB Modified residue 33 33 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P40510 +##sequence-region P42941 1 309 +P42941 UniProtKB Chain 1 309 . . . ID=PRO_0000156885;Note=Phosphoserine phosphatase +P42941 UniProtKB Region 186 187 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42941 UniProtKB Active site 97 97 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42941 UniProtKB Active site 99 99 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42941 UniProtKB Metal binding 97 97 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42941 UniProtKB Metal binding 99 99 . . . Note=Magnesium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42941 UniProtKB Metal binding 255 255 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42941 UniProtKB Binding site 106 106 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42941 UniProtKB Binding site 142 142 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42941 UniProtKB Binding site 232 232 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P42941 UniProtKB Binding site 258 258 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P36124 1 751 +P36124 UniProtKB Chain 1 751 . . . ID=PRO_0000097696;Note=SET domain-containing protein 3 +P36124 UniProtKB Domain 313 456 . . . Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 +P36124 UniProtKB Zinc finger 117 166 . . . Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 +P36124 UniProtKB Modified residue 236 236 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36124 UniProtKB Modified residue 684 684 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36124 UniProtKB Modified residue 718 718 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36124 UniProtKB Modified residue 719 719 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36124 UniProtKB Modified residue 741 741 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36124 UniProtKB Beta strand 129 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TDR +P36124 UniProtKB Turn 135 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TDR +P36124 UniProtKB Beta strand 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TDR +P36124 UniProtKB Helix 143 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TDR +P36124 UniProtKB Helix 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TDR +P36124 UniProtKB Turn 161 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TDR +P36124 UniProtKB Helix 170 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TDR +##sequence-region Q12529 1 373 +Q12529 UniProtKB Chain 1 373 . . . ID=PRO_0000269653;Note=Potential protein lysine methyltransferase SET6 +Q12529 UniProtKB Domain 12 338 . . . Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 +##sequence-region Q12314 1 213 +Q12314 UniProtKB Chain 1 213 . . . ID=PRO_0000237643;Note=Protein arginine N-methyltransferase SFM1 +Q12314 UniProtKB Modified residue 204 204 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12314 UniProtKB Modified residue 207 207 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q12314 UniProtKB Beta strand 2 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Beta strand 9 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Helix 14 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Helix 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Beta strand 32 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Helix 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Helix 48 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Helix 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Helix 65 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Beta strand 79 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Beta strand 88 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Helix 93 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Beta strand 100 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Turn 110 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5C74 +Q12314 UniProtKB Helix 118 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Turn 125 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Beta strand 128 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Helix 140 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Helix 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Beta strand 162 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Beta strand 167 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Beta strand 174 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Beta strand 180 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +Q12314 UniProtKB Helix 196 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5H5F +##sequence-region P53313 1 767 +P53313 UniProtKB Chain 1 767 . . . ID=PRO_0000202858;Note=Protein SDA1 +P53313 UniProtKB Compositional bias 555 628 . . . Note=Asp-rich +P53313 UniProtKB Modified residue 278 278 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P33421 1 198 +P33421 UniProtKB Transit peptide 1 50 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8195189;Dbxref=PMID:8195189 +P33421 UniProtKB Chain 51 198 . . . ID=PRO_0000003638;Note=Succinate dehydrogenase [ubiquinone] cytochrome b subunit%2C mitochondrial +P33421 UniProtKB Topological domain 51 99 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33421 UniProtKB Transmembrane 100 120 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33421 UniProtKB Topological domain 121 139 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33421 UniProtKB Transmembrane 140 160 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33421 UniProtKB Topological domain 161 175 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33421 UniProtKB Transmembrane 176 196 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33421 UniProtKB Topological domain 197 198 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33421 UniProtKB Metal binding 156 156 . . . Note=Iron (heme axial ligand)%3B shared with second transmembrane subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33421 UniProtKB Binding site 93 93 . . . Note=Ubiquinone;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33421 UniProtKB Binding site 97 97 . . . Note=Ubiquinone;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33421 UniProtKB Mutagenesis 96 96 . . . Note=Decreases quinone reductase activity. H->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14672930;Dbxref=PMID:14672930 +P33421 UniProtKB Mutagenesis 153 153 . . . Note=Decreases quinone reductase activity. Little effect on complex assembly. F->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10446163;Dbxref=PMID:10446163 +P33421 UniProtKB Mutagenesis 156 156 . . . Note=Decreases SDH cytochrome b content. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14672930;Dbxref=PMID:14672930 +P33421 UniProtKB Mutagenesis 163 163 . . . Note=Decreases quinone reductase activity. Little effect on complex assembly. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10446163;Dbxref=PMID:10446163 +P33421 UniProtKB Mutagenesis 166 166 . . . Note=Decreases quinone reductase activity. Little effect on complex assembly. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10446163;Dbxref=PMID:10446163 +P33421 UniProtKB Mutagenesis 167 167 . . . Note=Reduces SDH FAD content. Probably impairs complex assembly. D->V +P33421 UniProtKB Sequence conflict 10 10 . . . Note=L->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32602 1 292 +P32602 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.5;Dbxref=PMID:22814378 +P32602 UniProtKB Chain 2 292 . . . ID=PRO_0000219076;Note=Alpha-soluble NSF attachment protein +P32602 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|Ref.5;Dbxref=PMID:22814378 +P32602 UniProtKB Cross-link 261 261 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32602 UniProtKB Sequence conflict 103 103 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32602 UniProtKB Sequence conflict 219 219 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32602 UniProtKB Helix 4 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +P32602 UniProtKB Helix 21 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +P32602 UniProtKB Helix 30 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +P32602 UniProtKB Helix 54 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +P32602 UniProtKB Helix 73 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +P32602 UniProtKB Helix 93 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +P32602 UniProtKB Helix 113 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +P32602 UniProtKB Helix 134 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +P32602 UniProtKB Helix 154 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +P32602 UniProtKB Helix 174 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +P32602 UniProtKB Turn 192 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +P32602 UniProtKB Helix 195 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +P32602 UniProtKB Helix 198 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +P32602 UniProtKB Helix 215 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +P32602 UniProtKB Helix 224 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +P32602 UniProtKB Helix 238 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +P32602 UniProtKB Turn 253 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +P32602 UniProtKB Helix 256 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +P32602 UniProtKB Helix 271 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QQE +##sequence-region P40482 1 926 +P40482 UniProtKB Chain 1 926 . . . ID=PRO_0000205150;Note=Protein transport protein SEC24 +P40482 UniProtKB Region 231 256 . . . Note=Zinc finger-like +P40482 UniProtKB Compositional bias 110 114 . . . Note=Poly-Gln +P40482 UniProtKB Compositional bias 157 160 . . . Note=Poly-Pro +P40482 UniProtKB Metal binding 231 231 . . . Note=Zinc;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12239560,ECO:0000269|PubMed:12941276;Dbxref=PMID:12239560,PMID:12941276 +P40482 UniProtKB Metal binding 234 234 . . . Note=Zinc;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12239560,ECO:0000269|PubMed:12941276;Dbxref=PMID:12239560,PMID:12941276 +P40482 UniProtKB Metal binding 253 253 . . . Note=Zinc;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12239560,ECO:0000269|PubMed:12941276;Dbxref=PMID:12239560,PMID:12941276 +P40482 UniProtKB Metal binding 256 256 . . . Note=Zinc;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12239560,ECO:0000269|PubMed:12941276;Dbxref=PMID:12239560,PMID:12941276 +P40482 UniProtKB Modified residue 178 178 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40482 UniProtKB Mutagenesis 230 230 . . . Note=Abolishes binding to and packaging of cargo protein BET1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941277;Dbxref=PMID:12941277 +P40482 UniProtKB Mutagenesis 231 231 . . . Note=Lethal. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10097109;Dbxref=PMID:10097109 +P40482 UniProtKB Mutagenesis 235 235 . . . Note=Abolishes binding to and packaging of cargo protein BET1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941277;Dbxref=PMID:12941277 +P40482 UniProtKB Mutagenesis 559 559 . . . Note=Abolishes binding to and packaging of cargo protein BET1. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941277;Dbxref=PMID:12941277 +P40482 UniProtKB Mutagenesis 561 561 . . . Note=Abolishes binding to and packaging of cargo protein BET1. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941277;Dbxref=PMID:12941277 +P40482 UniProtKB Mutagenesis 616 616 . . . Note=Abolishes binding to and packaging of cargo protein BET1. L->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941277;Dbxref=PMID:12941277 +P40482 UniProtKB Helix 64 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2V +P40482 UniProtKB Beta strand 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 151 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 165 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 168 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 173 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Turn 179 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 182 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 193 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 204 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 212 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Turn 232 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 243 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Turn 246 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 250 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Turn 254 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 259 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 264 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 277 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 281 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 286 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 294 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 305 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 314 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 321 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Turn 333 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 344 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 362 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 374 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Turn 390 392 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 393 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Turn 396 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 400 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Turn 414 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 424 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Turn 436 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 440 448 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 471 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2V +P40482 UniProtKB Helix 482 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 495 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 509 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Turn 518 520 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 523 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 534 549 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 554 562 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 566 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 578 587 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 594 600 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 606 618 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Turn 620 622 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2V +P40482 UniProtKB Beta strand 624 637 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 639 644 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 648 665 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 668 689 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 696 699 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2V +P40482 UniProtKB Beta strand 702 704 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 705 707 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 710 718 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Turn 721 723 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 730 742 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 745 752 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 755 758 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Turn 759 761 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1M2V +P40482 UniProtKB Helix 791 793 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PD0 +P40482 UniProtKB Beta strand 799 803 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 805 812 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 818 825 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 830 832 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 847 860 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Beta strand 870 875 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 885 899 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +P40482 UniProtKB Helix 913 923 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PCX +##sequence-region P32844 1 805 +P32844 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32844 UniProtKB Chain 2 805 . . . ID=PRO_0000118931;Note=Exocyst complex component SEC6 +P32844 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32844 UniProtKB Sequence conflict 1 91 . . . Note=MSSDPLQQVCDLIKGDLSLERVRDIKEQLLKEKSVVEYQLNKESDKYYGEVEESLKLLNLSKNSVTSIKQQINEVNKLGNDNRFAINRYDI->MKLINWVMIIDLQLIVMIY;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32844 UniProtKB Sequence conflict 501 501 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32844 UniProtKB Sequence conflict 627 628 . . . Note=QQ->HE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32844 UniProtKB Helix 412 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 463 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 485 522 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Turn 523 526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 527 529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Turn 533 535 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 541 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 572 583 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 586 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 609 612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Turn 613 616 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 618 620 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 625 640 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 641 643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 646 666 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 667 670 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 677 679 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 680 699 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Turn 700 702 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 706 725 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 728 730 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 731 739 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 748 754 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 762 785 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +P32844 UniProtKB Helix 794 797 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FJI +##sequence-region P34250 1 1132 +P34250 UniProtKB Chain 1 1132 . . . ID=PRO_0000203159;Note=Eisosome protein SEG2 +P34250 UniProtKB Compositional bias 594 643 . . . Note=Asp/Glu-rich (highly acidic) +P34250 UniProtKB Modified residue 137 137 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34250 UniProtKB Modified residue 280 280 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P34250 UniProtKB Modified residue 504 504 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34250 UniProtKB Modified residue 507 507 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P34250 UniProtKB Modified residue 556 556 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34250 UniProtKB Modified residue 980 980 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34250 UniProtKB Modified residue 1022 1022 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34250 UniProtKB Cross-link 526 526 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P34250 UniProtKB Cross-link 743 743 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P49955 1 971 +P49955 UniProtKB Chain 1 971 . . . ID=PRO_0000174327;Note=U2 snRNP component HSH155 +P49955 UniProtKB Repeat 199 237 . . . Note=HEAT 1 +P49955 UniProtKB Repeat 273 310 . . . Note=HEAT 2 +P49955 UniProtKB Repeat 350 387 . . . Note=HEAT 3 +P49955 UniProtKB Repeat 513 550 . . . Note=HEAT 4 +P49955 UniProtKB Repeat 596 633 . . . Note=HEAT 5 +P49955 UniProtKB Repeat 680 717 . . . Note=HEAT 6 +P49955 UniProtKB Repeat 722 759 . . . Note=HEAT 7 +P49955 UniProtKB Repeat 792 829 . . . Note=HEAT 8 +P49955 UniProtKB Repeat 832 870 . . . Note=HEAT 9 +##sequence-region Q03067 1 99 +Q03067 UniProtKB Chain 1 99 . . . ID=PRO_0000227805;Note=SAGA-associated factor 11 +Q03067 UniProtKB Zinc finger 71 92 . . . Note=SGF11-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03047 +Q03067 UniProtKB Mutagenesis 15 15 . . . Note=Moerately decreases the affinity of SGF11 for SUS1. I->A +Q03067 UniProtKB Mutagenesis 18 18 . . . Note=Causes a dramatic decrease in the affinity of SGF11 for SUS1. N->NA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20007317;Dbxref=PMID:20007317 +Q03067 UniProtKB Mutagenesis 19 19 . . . Note=Causes a dramatic decrease in the affinity of SGF11 for SUS1. L->LA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20007317;Dbxref=PMID:20007317 +Q03067 UniProtKB Mutagenesis 57 57 . . . Note=Reduces deubiquitination activity of the SAGA DUB module%3B when associated with A-60. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20434206;Dbxref=PMID:20434206 +Q03067 UniProtKB Mutagenesis 60 60 . . . Note=Reduces deubiquitination activity of the SAGA DUB module%3B when associated with A-57. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20434206;Dbxref=PMID:20434206 +Q03067 UniProtKB Mutagenesis 84 84 . . . Note=No effect. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20434206;Dbxref=PMID:20434206 +Q03067 UniProtKB Mutagenesis 85 85 . . . Note=Strongly reduces deubiquitination activity of the SAGA DUB module. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20434206;Dbxref=PMID:20434206 +Q03067 UniProtKB Mutagenesis 86 86 . . . Note=Moderately impairs deubiquitination activity of the SAGA DUB module. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20434206;Dbxref=PMID:20434206 +Q03067 UniProtKB Mutagenesis 89 89 . . . Note=Strongly reduces deubiquitination activity of the SAGA DUB module. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20434206;Dbxref=PMID:20434206 +Q03067 UniProtKB Mutagenesis 91 91 . . . Note=No effect. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20434206;Dbxref=PMID:20434206 +Q03067 UniProtKB Helix 8 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +Q03067 UniProtKB Helix 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FK5 +Q03067 UniProtKB Beta strand 70 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +Q03067 UniProtKB Turn 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +Q03067 UniProtKB Beta strand 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +Q03067 UniProtKB Helix 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +Q03067 UniProtKB Helix 85 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +##sequence-region P53075 1 577 +P53075 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53075 UniProtKB Chain 24 577 . . . ID=PRO_0000202713;Note=Outer spore wall assembly protein SHE10 +P53075 UniProtKB Coiled coil 379 416 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53075 UniProtKB Coiled coil 513 562 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36068 1 246 +P36068 UniProtKB Chain 1 246 . . . ID=PRO_0000203151;Note=SWI5-dependent HO expression protein 2 +P36068 UniProtKB Motif 15 23 . . . Note=Nuclear localization signal +P36068 UniProtKB Mutagenesis 36 36 . . . Note=Prevents association with ASH1 and IST2 mRNAs and leads to their mislocalization. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14561888;Dbxref=PMID:14561888 +P36068 UniProtKB Mutagenesis 43 43 . . . Note=Prevents association with ASH1 and mRNA and leads to its mislocalization. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14561888;Dbxref=PMID:14561888 +P36068 UniProtKB Mutagenesis 44 44 . . . Note=Prevents association with ASH1 and mRNA and leads to its mislocalization. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14561888;Dbxref=PMID:14561888 +P36068 UniProtKB Mutagenesis 49 49 . . . Note=Prevents association with ASH1 and mRNA and leads to its mislocalization. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14561888;Dbxref=PMID:14561888 +P36068 UniProtKB Mutagenesis 52 52 . . . Note=Prevents association with ASH1 and mRNA and leads to its mislocalization. R->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14561888;Dbxref=PMID:14561888 +P36068 UniProtKB Mutagenesis 63 63 . . . Note=Prevents association with ASH1 and IST2 mRNAs and leads to their mislocalization. R->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14561888;Dbxref=PMID:14561888 +P36068 UniProtKB Mutagenesis 68 68 . . . Note=Prevents dimerization and RNA-binding. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15537539;Dbxref=PMID:15537539 +P36068 UniProtKB Mutagenesis 120 120 . . . Note=Prevents dimerization and RNA-binding. S->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15537539;Dbxref=PMID:15537539 +P36068 UniProtKB Mutagenesis 130 130 . . . Note=Prevents tetramerization. L->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19710186;Dbxref=PMID:19710186 +P36068 UniProtKB Helix 13 42 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY +P36068 UniProtKB Helix 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY +P36068 UniProtKB Helix 49 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY +P36068 UniProtKB Helix 74 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY +P36068 UniProtKB Turn 86 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY +P36068 UniProtKB Helix 92 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY +P36068 UniProtKB Helix 120 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY +P36068 UniProtKB Helix 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY +P36068 UniProtKB Helix 138 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY +P36068 UniProtKB Helix 167 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY +P36068 UniProtKB Helix 172 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY +P36068 UniProtKB Helix 194 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WNL +P36068 UniProtKB Beta strand 197 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WNL +P36068 UniProtKB Helix 205 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1XLY +##sequence-region P38272 1 425 +P38272 UniProtKB Chain 1 425 . . . ID=PRO_0000202490;Note=SWI5-dependent HO expression protein 3 +P38272 UniProtKB Coiled coil 68 197 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38272 UniProtKB Compositional bias 377 381 . . . Note=Poly-Ser +P38272 UniProtKB Modified residue 343 343 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38272 UniProtKB Modified residue 394 394 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38272 UniProtKB Mutagenesis 343 343 . . . Note=Prevents correct localization of ASH1 mRNA%3B when associated with E-361. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19429778;Dbxref=PMID:19429778 +P38272 UniProtKB Mutagenesis 348 348 . . . Note=Prevents correct localization of ASH1 mRNA. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19429778;Dbxref=PMID:19429778 +P38272 UniProtKB Mutagenesis 361 361 . . . Note=Prevents correct localization of ASH1 mRNA%3B when associated with E-343. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19429778;Dbxref=PMID:19429778 +P38272 UniProtKB Helix 44 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LL7 +P38272 UniProtKB Helix 74 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4LL7 +##sequence-region Q04172 1 456 +Q04172 UniProtKB Transit peptide 1 30 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04172 UniProtKB Chain 31 456 . . . ID=PRO_0000022344;Note=Sensitive to high expression protein 9%2C mitochondrial +Q04172 UniProtKB Topological domain 31 296 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04172 UniProtKB Transmembrane 297 317 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04172 UniProtKB Topological domain 318 435 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04172 UniProtKB Transmembrane 436 456 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04172 UniProtKB Coiled coil 71 128 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04172 UniProtKB Coiled coil 178 277 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P35179 1 80 +P35179 UniProtKB Chain 1 80 . . . ID=PRO_0000104211;Note=Protein transport protein SSS1 +P35179 UniProtKB Topological domain 1 46 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35179 UniProtKB Transmembrane 47 75 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35179 UniProtKB Topological domain 76 80 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35179 UniProtKB Sequence conflict 58 58 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q6Q595 1 175 +Q6Q595 UniProtKB Chain 1 175 . . . ID=PRO_0000213468;Note=Vesicle-associated membrane protein-associated protein SCS22 +Q6Q595 UniProtKB Topological domain 1 154 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q6Q595 UniProtKB Transmembrane 155 175 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q6Q595 UniProtKB Domain 1 125 . . . Note=MSP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00132 +Q6Q595 UniProtKB Sequence conflict 169 169 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53012 1 380 +P53012 UniProtKB Chain 1 380 . . . ID=PRO_0000097635;Note=FIT family protein SCS3 +P53012 UniProtKB Topological domain 1 7 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53012 UniProtKB Transmembrane 8 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53012 UniProtKB Topological domain 29 43 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53012 UniProtKB Transmembrane 44 64 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53012 UniProtKB Topological domain 65 88 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53012 UniProtKB Transmembrane 89 109 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53012 UniProtKB Topological domain 110 233 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53012 UniProtKB Transmembrane 234 254 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53012 UniProtKB Topological domain 255 325 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53012 UniProtKB Transmembrane 326 346 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53012 UniProtKB Topological domain 347 356 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53012 UniProtKB Transmembrane 357 377 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53012 UniProtKB Topological domain 378 380 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53012 UniProtKB Sequence conflict 240 240 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53189 1 542 +P53189 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53189 UniProtKB Chain 21 542 . . . ID=PRO_0000011903;Note=Probable family 17 glucosidase SCW11 +P53189 UniProtKB Compositional bias 31 303 . . . Note=Ser/Thr-rich +P53189 UniProtKB Active site 478 478 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53189 UniProtKB Active site 532 532 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P53334 1 386 +P53334 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53334 UniProtKB Propeptide 20 30 . . . ID=PRO_0000011899;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9748433;Dbxref=PMID:9748433 +P53334 UniProtKB Chain 31 386 . . . ID=PRO_0000011900;Note=Probable family 17 glucosidase SCW4 +P53334 UniProtKB Compositional bias 71 155 . . . Note=Ser-rich +P53334 UniProtKB Active site 323 323 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53334 UniProtKB Active site 377 377 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53334 UniProtKB Glycosylation 89 89 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53334 UniProtKB Sequence conflict 35 35 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53334 UniProtKB Sequence conflict 40 40 . . . Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53009 1 804 +P53009 UniProtKB Chain 1 804 . . . ID=PRO_0000097636;Note=Protein kinase-like protein SCY1 +P53009 UniProtKB Domain 1 324 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53009 UniProtKB Compositional bias 36 43 . . . Note=Poly-Ser +##sequence-region Q06058 1 285 +Q06058 UniProtKB Chain 1 285 . . . ID=PRO_0000247216;Note=Seipin +Q06058 UniProtKB Topological domain 1 16 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12524434,ECO:0000305|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258 +Q06058 UniProtKB Transmembrane 17 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06058 UniProtKB Topological domain 38 244 . . . Note=Lumenal;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12524434,ECO:0000305|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258 +Q06058 UniProtKB Transmembrane 245 265 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06058 UniProtKB Topological domain 266 285 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12524434,ECO:0000269|PubMed:16847258;Dbxref=PMID:12524434,PMID:16847258 +##sequence-region P39709 1 593 +P39709 UniProtKB Chain 1 593 . . . ID=PRO_0000121368;Note=Probable transporter SEO1 +P39709 UniProtKB Topological domain 1 130 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Transmembrane 131 151 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Topological domain 152 175 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Transmembrane 176 196 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Topological domain 197 200 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Transmembrane 201 221 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Topological domain 222 234 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Transmembrane 235 255 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Topological domain 256 265 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Transmembrane 266 286 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Topological domain 287 302 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Transmembrane 303 323 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Topological domain 324 363 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Transmembrane 364 384 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Topological domain 385 411 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Transmembrane 412 432 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Topological domain 433 438 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Transmembrane 439 459 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Topological domain 460 466 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Transmembrane 467 487 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Topological domain 488 499 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Transmembrane 500 520 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Topological domain 521 532 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Transmembrane 533 553 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39709 UniProtKB Topological domain 554 593 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P33330 1 395 +P33330 UniProtKB Chain 1 395 . . . ID=PRO_0000150141;Note=Phosphoserine aminotransferase +P33330 UniProtKB Region 80 81 . . . Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33330 UniProtKB Region 271 272 . . . Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33330 UniProtKB Binding site 46 46 . . . Note=L-glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33330 UniProtKB Binding site 113 113 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33330 UniProtKB Binding site 170 170 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33330 UniProtKB Binding site 194 194 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33330 UniProtKB Binding site 217 217 . . . Note=Pyridoxal phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33330 UniProtKB Modified residue 20 20 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P33330 UniProtKB Modified residue 112 112 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P33330 UniProtKB Modified residue 218 218 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33330 UniProtKB Sequence conflict 258 259 . . . Note=FD->LH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38827 1 1080 +P38827 UniProtKB Chain 1 1080 . . . ID=PRO_0000186086;Note=Histone-lysine N-methyltransferase%2C H3 lysine-4 specific +P38827 UniProtKB Domain 938 1055 . . . Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 +P38827 UniProtKB Domain 1064 1080 . . . Note=Post-SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00155 +P38827 UniProtKB Modified residue 625 625 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P38827 UniProtKB Modified residue 875 875 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38827 UniProtKB Beta strand 249 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A +P38827 UniProtKB Helix 265 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A +P38827 UniProtKB Beta strand 279 285 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A +P38827 UniProtKB Turn 287 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A +P38827 UniProtKB Beta strand 292 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A +P38827 UniProtKB Helix 310 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A +P38827 UniProtKB Turn 321 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A +P38827 UniProtKB Beta strand 326 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A +P38827 UniProtKB Beta strand 331 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A +P38827 UniProtKB Helix 342 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J8A +##sequence-region Q12369 1 946 +Q12369 UniProtKB Chain 1 946 . . . ID=PRO_0000269647;Note=Protein SFI1 +Q12369 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12369 UniProtKB Modified residue 855 855 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q12369 UniProtKB Helix 222 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DOQ +Q12369 UniProtKB Helix 241 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DOQ +Q12369 UniProtKB Helix 247 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DOQ +Q12369 UniProtKB Helix 643 675 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GV5 +Q12369 UniProtKB Helix 677 706 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GV5 +Q12369 UniProtKB Turn 707 709 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2GV5 +##sequence-region P35735 1 353 +P35735 UniProtKB Chain 1 353 . . . ID=PRO_0000203179;Note=Protein SFK1 +P35735 UniProtKB Topological domain 1 11 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35735 UniProtKB Transmembrane 12 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35735 UniProtKB Topological domain 33 62 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35735 UniProtKB Transmembrane 63 83 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35735 UniProtKB Topological domain 84 130 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35735 UniProtKB Transmembrane 131 151 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35735 UniProtKB Topological domain 152 160 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35735 UniProtKB Transmembrane 161 181 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35735 UniProtKB Topological domain 182 231 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35735 UniProtKB Transmembrane 232 253 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35735 UniProtKB Topological domain 254 263 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35735 UniProtKB Transmembrane 264 284 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35735 UniProtKB Topological domain 285 353 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P35735 UniProtKB Modified residue 208 208 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P20134 1 766 +P20134 UniProtKB Chain 1 766 . . . ID=PRO_0000124595;Note=Flocculation suppression protein +P20134 UniProtKB DNA binding 64 186 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20134 UniProtKB Modified residue 220 220 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P20134 UniProtKB Modified residue 556 556 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P20134 UniProtKB Modified residue 733 733 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P20134 UniProtKB Sequence conflict 446 454 . . . Note=FVQYQPQSQ->LYNTNRSRN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20134 UniProtKB Sequence conflict 446 454 . . . Note=FVQYQPQSQ->LYNTNRSRN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20134 UniProtKB Sequence conflict 461 462 . . . Note=KQ->SE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P20134 UniProtKB Sequence conflict 461 462 . . . Note=KQ->SE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12234 1 484 +Q12234 UniProtKB Chain 1 484 . . . ID=PRO_0000268739;Note=GRIP domain-containing protein RUD3 +Q12234 UniProtKB Domain 401 452 . . . Note=GRIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00250 +Q12234 UniProtKB Coiled coil 84 383 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12234 UniProtKB Modified residue 55 55 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12234 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12234 UniProtKB Modified residue 468 468 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198 +##sequence-region Q07458 1 294 +Q07458 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q07458 UniProtKB Chain 2 294 . . . ID=PRO_0000234080;Note=Transcriptional regulatory protein RXT3 +Q07458 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P34218 1 831 +P34218 UniProtKB Chain 1 831 . . . ID=PRO_0000051579;Note=Histone acetyltransferase SAS3 +P34218 UniProtKB Domain 267 573 . . . Note=MYST-type HAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063 +P34218 UniProtKB Zinc finger 300 325 . . . Note=C2HC MYST-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063 +P34218 UniProtKB Region 419 421 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6 +P34218 UniProtKB Region 426 432 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6 +P34218 UniProtKB Compositional bias 736 831 . . . Note=Asp/Glu-rich (acidic) +P34218 UniProtKB Active site 452 452 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6 +P34218 UniProtKB Binding site 456 456 . . . Note=Acetyl-CoA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6 +P34218 UniProtKB Modified residue 367 367 . . . Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6 +P34218 UniProtKB Mutagenesis 303 303 . . . Note=Greatly diminishes HAT activity. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10600516,ECO:0000269|PubMed:10817755;Dbxref=PMID:10600516,PMID:10817755 +P34218 UniProtKB Mutagenesis 306 306 . . . Note=Greatly diminishes HAT activity. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10600516,ECO:0000269|PubMed:10817755;Dbxref=PMID:10600516,PMID:10817755 +P34218 UniProtKB Mutagenesis 319 319 . . . Note=Greatly diminishes HAT activity. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10600516,ECO:0000269|PubMed:10817755;Dbxref=PMID:10600516,PMID:10817755 +P34218 UniProtKB Mutagenesis 323 323 . . . Note=Abolishes HAT activity. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10600516,ECO:0000269|PubMed:10817755;Dbxref=PMID:10600516,PMID:10817755 +P34218 UniProtKB Mutagenesis 426 427 . . . Note=Loss of function. QR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10817755;Dbxref=PMID:10817755 +P34218 UniProtKB Mutagenesis 429 431 . . . Note=Loss of function. GYG->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10817755;Dbxref=PMID:10817755 +P34218 UniProtKB Mutagenesis 434 435 . . . Note=No effect. LM->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10817755;Dbxref=PMID:10817755 +##sequence-region P40963 1 338 +P40963 UniProtKB Chain 1 338 . . . ID=PRO_0000051578;Note=Histone acetyltransferase SAS2 +P40963 UniProtKB Domain 45 338 . . . Note=MYST-type HAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063 +P40963 UniProtKB Zinc finger 100 126 . . . Note=C2HC MYST-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063 +P40963 UniProtKB Region 209 211 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6 +P40963 UniProtKB Region 216 222 . . . Note=Acetyl-CoA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6 +P40963 UniProtKB Active site 242 242 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6 +P40963 UniProtKB Binding site 246 246 . . . Note=Acetyl-CoA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6 +P40963 UniProtKB Binding site 323 323 . . . Note=Acetyl-CoA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6 +P40963 UniProtKB Modified residue 168 168 . . . Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:22020126;Dbxref=PMID:22020126 +P40963 UniProtKB Mutagenesis 106 106 . . . Note=Loss of function. C->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11731479,ECO:0000269|PubMed:11731480;Dbxref=PMID:11731479,PMID:11731480 +P40963 UniProtKB Mutagenesis 168 168 . . . Note=Abolishes catalytic activity. K->A%2CQ%2CR +P40963 UniProtKB Mutagenesis 213 214 . . . Note=Loss of function. PP->AV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11731480;Dbxref=PMID:11731480 +P40963 UniProtKB Mutagenesis 216 217 . . . Note=Abolishes silencing activity. QR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11731479;Dbxref=PMID:11731479 +P40963 UniProtKB Mutagenesis 219 221 . . . Note=Does not affect silencing activity. GLG->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11731479;Dbxref=PMID:11731479 +P40963 UniProtKB Mutagenesis 224 225 . . . Note=Does not affect silencing activity. LI->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11731479;Dbxref=PMID:11731479 +##sequence-region P39735 1 261 +P39735 UniProtKB Chain 1 261 . . . ID=PRO_0000202414;Note=Single-strand annealing weakened protein 1 +##sequence-region Q9ZZX1 1 630 +Q9ZZX1 UniProtKB Transmembrane 16 36 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q9ZZX1 UniProtKB Transmembrane 57 77 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q9ZZX1 UniProtKB Transmembrane 101 121 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q9ZZX1 UniProtKB Transmembrane 147 167 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q9ZZX1 UniProtKB Transmembrane 182 202 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q9ZZX1 UniProtKB Transmembrane 235 255 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q9ZZX1 UniProtKB Transmembrane 267 287 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q9ZZX1 UniProtKB Transmembrane 305 325 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q9ZZX1 UniProtKB Transmembrane 417 437 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q9ZZX1 UniProtKB Transmembrane 464 483 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q9ZZX1 UniProtKB Region 1 324 . . . Note=COX1 exons encoded;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q9ZZX1 UniProtKB Region 325 630 . . . Note=COX1 intron aI5_alpha encoded +Q9ZZX1 UniProtKB Compositional bias 333 390 . . . Note=Asn-rich;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36048 1 1008 +P36048 UniProtKB Chain 1 1008 . . . ID=PRO_0000091565;Note=Pre-mRNA-splicing factor SNU114 +P36048 UniProtKB Domain 131 338 . . . Note=tr-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P36048 UniProtKB Nucleotide binding 140 147 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36048 UniProtKB Nucleotide binding 214 218 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36048 UniProtKB Nucleotide binding 268 271 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36048 UniProtKB Region 140 147 . . . Note=G1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P36048 UniProtKB Region 188 192 . . . Note=G2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P36048 UniProtKB Region 214 217 . . . Note=G3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P36048 UniProtKB Region 268 271 . . . Note=G4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P36048 UniProtKB Region 315 317 . . . Note=G5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01059 +P36048 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36048 UniProtKB Modified residue 88 88 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P36048 UniProtKB Turn 68 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 75 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Turn 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 110 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 120 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Turn 130 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 134 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 146 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 166 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 182 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 194 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 207 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 222 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 233 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Turn 241 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 247 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 262 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 271 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Turn 275 277 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 281 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 306 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 311 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Turn 316 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 320 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 324 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 332 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 338 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 341 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 349 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 356 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 362 364 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 372 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 378 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 393 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Turn 410 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 417 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 433 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 445 455 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 465 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 479 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 483 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 499 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 504 506 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 541 545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 547 554 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 561 566 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 568 570 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 575 579 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 583 588 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 603 611 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 612 614 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 615 628 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 633 636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 642 648 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 649 661 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 668 670 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 678 681 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 708 714 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 717 723 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 737 739 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 744 755 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 759 764 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 772 776 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 779 783 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 785 803 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 807 810 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 815 823 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 833 836 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 838 851 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 855 869 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 870 872 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 873 883 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 887 893 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 897 908 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 909 911 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 914 921 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Turn 922 924 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 928 931 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 937 939 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Beta strand 953 955 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 959 961 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P36048 UniProtKB Helix 963 974 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P10870 1 884 +P10870 UniProtKB Chain 1 884 . . . ID=PRO_0000050390;Note=High-affinity glucose transporter SNF3 +P10870 UniProtKB Topological domain 1 97 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Transmembrane 98 118 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Topological domain 119 143 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Transmembrane 144 164 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Topological domain 165 178 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Transmembrane 179 199 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Topological domain 200 202 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Transmembrane 203 223 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Topological domain 224 229 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Transmembrane 230 250 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Topological domain 251 264 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Transmembrane 265 285 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Topological domain 286 358 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Transmembrane 359 379 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Topological domain 380 391 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Transmembrane 392 412 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Topological domain 413 419 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Transmembrane 420 440 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Topological domain 441 451 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Transmembrane 452 472 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Topological domain 473 488 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Transmembrane 489 509 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Topological domain 510 521 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Transmembrane 522 542 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Topological domain 543 884 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Glycosylation 383 383 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P10870 UniProtKB Mutagenesis 112 112 . . . Note=In SNF3-142. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2406560;Dbxref=PMID:2406560 +P10870 UniProtKB Mutagenesis 153 153 . . . Note=In SNF3-72. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2406560;Dbxref=PMID:2406560 +P10870 UniProtKB Mutagenesis 229 229 . . . Note=In SNF3-1%3B constitutively signaling glucose receptor. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2406560;Dbxref=PMID:2406560 +P10870 UniProtKB Mutagenesis 402 402 . . . Note=In SNF3-39. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2406560;Dbxref=PMID:2406560 +##sequence-region P18888 1 332 +P18888 UniProtKB Chain 1 332 . . . ID=PRO_0000072006;Note=Transcription regulatory protein SNF6 +P18888 UniProtKB Motif 2 8 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18888 UniProtKB Compositional bias 264 276 . . . Note=Gln-rich +P18888 UniProtKB Modified residue 165 165 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P39929 1 240 +P39929 UniProtKB Chain 1 240 . . . ID=PRO_0000211446;Note=Vacuolar-sorting protein SNF7 +P39929 UniProtKB Compositional bias 68 71 . . . Note=Poly-Lys +P39929 UniProtKB Compositional bias 216 228 . . . Note=Asp/Glu-rich (acidic) +P39929 UniProtKB Modified residue 72 72 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950 +P39929 UniProtKB Modified residue 119 119 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39929 UniProtKB Modified residue 193 193 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39929 UniProtKB Cross-link 229 229 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P39929 UniProtKB Mutagenesis 2 2 . . . Note=Impairs binding to membrane. W->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24139821;Dbxref=PMID:24139821 +P39929 UniProtKB Mutagenesis 6 6 . . . Note=Impairs binding to membrane. F->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24139821;Dbxref=PMID:24139821 +P39929 UniProtKB Mutagenesis 8 8 . . . Note=Impairs binding to membrane. W->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24139821;Dbxref=PMID:24139821 +P39929 UniProtKB Mutagenesis 25 25 . . . Note=Leads to severe sorting defects%3B when associated with E-29 and E-36. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 29 29 . . . Note=Leads to severe sorting defects%3B when associated with E-25 and E-36. H->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 36 36 . . . Note=Leads to severe sorting defects%3B when associated with E-25 and E-29. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 52 52 . . . Note=Impairs the formation of protofilaments%3B when associated with K-90. Also impairs the formation of protofilaments%3B when associated with E-94. Also impairs the formation of protofilaments%3B when associated with E-107. Also impairs the formation of protofilaments%3B when associated with E-114. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 83 83 . . . Note=Leads to severe sorting defects. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 87 87 . . . Note=Leads to severe sorting defects. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 90 90 . . . Note=Leads to severe sorting defects. Impairs the formation of protofilaments%3B when associated with E-52. Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 94 94 . . . Note=Leads to severe sorting defects. Impairs the formation of protofilaments%3B when associated with E-52. I->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 95 95 . . . Note=Leads to severe sorting defects%3B when associated with K-102 and K-109. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 97 97 . . . Note=Leads to severe sorting defects. A->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 99 99 . . . Note=Leads to severe sorting defects. L->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 101 101 . . . Note=Leads to severe sorting defects. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 102 102 . . . Note=Leads to severe sorting defects%3B when associated with K-95 and K-109. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 103 103 . . . Note=Leads to severe sorting defects. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 104 104 . . . Note=Leads to severe sorting defects. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 107 107 . . . Note=Leads to severe sorting defects. Impairs the formation of protofilaments%3B when associated with E-52. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 109 109 . . . Note=Leads to severe sorting defects%3B when associated with K-95 and K-102. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 114 114 . . . Note=Leads to severe sorting defects. Impairs the formation of protofilaments%3B when associated with E-52. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 117 117 . . . Note=Leads to severe sorting defects. I->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Mutagenesis 121 121 . . . Note=Leads to severe sorting defects. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26670543;Dbxref=PMID:26670543 +P39929 UniProtKB Sequence conflict 173 173 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39929 UniProtKB Helix 19 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FD9 +P39929 UniProtKB Helix 60 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FD9 +P39929 UniProtKB Turn 120 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FD7 +P39929 UniProtKB Helix 127 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FD9 +P39929 UniProtKB Turn 139 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5FD9 +##sequence-region P00445 1 154 +P00445 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:6993479,ECO:0000269|Ref.6,ECO:0000269|Ref.8;Dbxref=PMID:6993479 +P00445 UniProtKB Chain 2 154 . . . ID=PRO_0000164129;Note=Superoxide dismutase [Cu-Zn] +P00445 UniProtKB Metal binding 43 43 . . . Note=Zinc 2%3B shared with CCS1%3B in apo form;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10026301,ECO:0000269|PubMed:11524675;Dbxref=PMID:10026301,PMID:11524675 +P00445 UniProtKB Metal binding 47 47 . . . Note=Copper%3B catalytic;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10026301,ECO:0000269|PubMed:8652572;Dbxref=PMID:10026301,PMID:8652572 +P00445 UniProtKB Metal binding 49 49 . . . Note=Copper%3B catalytic;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10026301,ECO:0000269|PubMed:8652572;Dbxref=PMID:10026301,PMID:8652572 +P00445 UniProtKB Metal binding 64 64 . . . Note=Copper%3B catalytic;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10026301,ECO:0000269|PubMed:8652572;Dbxref=PMID:10026301,PMID:8652572 +P00445 UniProtKB Metal binding 64 64 . . . Note=Zinc 1%3B structural;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10026301,ECO:0000269|PubMed:11524675;Dbxref=PMID:10026301,PMID:11524675 +P00445 UniProtKB Metal binding 72 72 . . . Note=Zinc 1%3B structural;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10026301,ECO:0000269|PubMed:11524675;Dbxref=PMID:10026301,PMID:11524675 +P00445 UniProtKB Metal binding 81 81 . . . Note=Zinc 1%3B structural;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10026301,ECO:0000269|PubMed:11524675;Dbxref=PMID:10026301,PMID:11524675 +P00445 UniProtKB Metal binding 84 84 . . . Note=Zinc 1%3B structural;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10026301,ECO:0000269|PubMed:11524675;Dbxref=PMID:10026301,PMID:11524675 +P00445 UniProtKB Metal binding 121 121 . . . Note=Copper%3B catalytic;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10026301,ECO:0000269|PubMed:8652572;Dbxref=PMID:10026301,PMID:8652572 +P00445 UniProtKB Binding site 144 144 . . . Note=Substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00445 UniProtKB Modified residue 26 26 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P00445 UniProtKB Modified residue 39 39 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198 +P00445 UniProtKB Modified residue 99 99 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +P00445 UniProtKB Modified residue 117 117 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P00445 UniProtKB Modified residue 132 132 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P00445 UniProtKB Modified residue 138 138 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P00445 UniProtKB Disulfide bond 58 147 . . . . +P00445 UniProtKB Disulfide bond 58 58 . . . Note=Interchain (with C-229 in CCS1)%3B in linked form +P00445 UniProtKB Cross-link 19 19 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15166219;Dbxref=PMID:15166219 +P00445 UniProtKB Cross-link 70 70 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15166219;Dbxref=PMID:15166219 +P00445 UniProtKB Mutagenesis 123 123 . . . Note=Does not enable copper chaperone-independent activation. G->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15069187;Dbxref=PMID:15069187 +P00445 UniProtKB Mutagenesis 131 132 . . . Note=Does not enable copper chaperone-independent activation. DT->GN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15069187;Dbxref=PMID:15069187 +P00445 UniProtKB Mutagenesis 143 143 . . . Note=Enables copper chaperone-independent activation%3B when associated with A-145 or with L-145. P->A%2CS;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15069187,ECO:0000269|PubMed:16234242;Dbxref=PMID:15069187,PMID:16234242 +P00445 UniProtKB Mutagenesis 145 145 . . . Note=Enables copper chaperone-independent activation%3B when associated with A-143 or with S-143. P->A%2CL;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15069187,ECO:0000269|PubMed:16234242;Dbxref=PMID:15069187,PMID:16234242 +P00445 UniProtKB Sequence conflict 56 56 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00445 UniProtKB Sequence conflict 93 93 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00445 UniProtKB Beta strand 3 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G +P00445 UniProtKB Beta strand 11 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G +P00445 UniProtKB Beta strand 15 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G +P00445 UniProtKB Beta strand 23 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SDY +P00445 UniProtKB Beta strand 29 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G +P00445 UniProtKB Beta strand 43 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G +P00445 UniProtKB Turn 55 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G +P00445 UniProtKB Helix 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G +P00445 UniProtKB Beta strand 77 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G +P00445 UniProtKB Beta strand 84 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G +P00445 UniProtKB Beta strand 96 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G +P00445 UniProtKB Beta strand 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G +P00445 UniProtKB Beta strand 116 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G +P00445 UniProtKB Beta strand 130 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G +P00445 UniProtKB Helix 135 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G +P00445 UniProtKB Beta strand 146 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G +P00445 UniProtKB Beta strand 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F1G +##sequence-region Q05676 1 74 +##sequence-region Q06411 1 708 +Q06411 UniProtKB Chain 1 708 . . . ID=PRO_0000270560;Note=Pre-mRNA-splicing factor SPP382 +Q06411 UniProtKB Domain 61 108 . . . Note=G-patch;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00092 +##sequence-region Q03954 1 165 +Q03954 UniProtKB Chain 1 165 . . . ID=PRO_0000142593;Note=DASH complex subunit SPC19 +Q03954 UniProtKB Coiled coil 74 104 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03954 UniProtKB Coiled coil 132 165 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03954 UniProtKB Modified residue 107 107 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:12408861;Dbxref=PMID:19779198,PMID:12408861 +Q03954 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:12408861;Dbxref=PMID:18407956,PMID:19779198,PMID:12408861 +##sequence-region Q03868 1 1245 +Q03868 UniProtKB Chain 1 1245 . . . ID=PRO_0000072140;Note=Sporulation-specific protein 71 +Q03868 UniProtKB Domain 1030 1229 . . . Note=PH +##sequence-region Q06134 1 477 +Q06134 UniProtKB Chain 1 477 . . . ID=PRO_0000072144;Note=Sporulation-specific protein 77 +##sequence-region P09937 1 338 +P09937 UniProtKB Chain 1 338 . . . ID=PRO_0000072154;Note=Sporulation-specific protein 4 +P09937 UniProtKB Sequence conflict 107 107 . . . Note=R->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09937 UniProtKB Sequence conflict 180 180 . . . Note=H->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12455 1 300 +Q12455 UniProtKB Chain 1 300 . . . ID=PRO_0000156540;Note=Spermine synthase +Q12455 UniProtKB Domain 12 255 . . . Note=PABS +Q12455 UniProtKB Region 151 152 . . . Note=S-adenosylmethioninamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12455 UniProtKB Active site 174 174 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12455 UniProtKB Binding site 44 44 . . . Note=S-adenosylmethioninamine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12455 UniProtKB Binding site 99 99 . . . Note=S-adenosylmethioninamine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12455 UniProtKB Binding site 119 119 . . . Note=S-adenosylmethioninamine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12455 UniProtKB Binding site 177 177 . . . Note=Spermidine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12455 UniProtKB Modified residue 5 5 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P06843 1 333 +P06843 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P06843 UniProtKB Chain 2 333 . . . ID=PRO_0000072163;Note=Protein SPT2 +P06843 UniProtKB Region 259 333 . . . Note=Important for interaction with histones;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26109053;Dbxref=PMID:26109053 +P06843 UniProtKB Coiled coil 218 242 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06843 UniProtKB Coiled coil 292 316 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06843 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P06843 UniProtKB Modified residue 126 126 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P06843 UniProtKB Mutagenesis 289 290 . . . Note=Strongly reduces histone binding. ME->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26109053;Dbxref=PMID:26109053 +P06843 UniProtKB Mutagenesis 299 300 . . . Note=Strongly reduces histone binding. EE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26109053;Dbxref=PMID:26109053 +P06843 UniProtKB Mutagenesis 310 311 . . . Note=Strongly reduces histone binding. ED->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26109053;Dbxref=PMID:26109053 +##sequence-region P35177 1 1332 +P35177 UniProtKB Chain 1 1332 . . . ID=PRO_0000211214;Note=Transcriptional activator SPT7 +P35177 UniProtKB Domain 458 528 . . . Note=Bromo;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 +P35177 UniProtKB Modified residue 78 78 . . . Note=Phosphothreonine%3B by ATM or ATR;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P35177 UniProtKB Modified residue 88 88 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P35177 UniProtKB Modified residue 1293 1293 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38985 1 146 +P38985 UniProtKB Chain 1 146 . . . ID=PRO_0000135196;Note=Signal recognition particle subunit SRP14 +P38985 UniProtKB Modified residue 8 8 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P32342 1 167 +P32342 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:7925282;Dbxref=PMID:22814378,PMID:7925282 +P32342 UniProtKB Chain 2 167 . . . ID=PRO_0000135239;Note=Signal recognition particle subunit SRP21 +P32342 UniProtKB Compositional bias 155 167 . . . Note=Lys-rich (highly basic) +P32342 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:22814378,ECO:0000269|PubMed:7925282;Dbxref=PMID:22814378,PMID:7925282 +##sequence-region P38688 1 640 +P38688 UniProtKB Chain 1 640 . . . ID=PRO_0000135238;Note=Signal recognition particle subunit SRP72 +P38688 UniProtKB Repeat 188 221 . . . Note=TPR +P38688 UniProtKB Compositional bias 539 640 . . . Note=Lys-rich +##sequence-region Q03529 1 384 +Q03529 UniProtKB Chain 1 384 . . . ID=PRO_0000185407;Note=Ceramide very long chain fatty acid hydroxylase SCS7 +Q03529 UniProtKB Topological domain 1 196 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03529 UniProtKB Transmembrane 197 217 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03529 UniProtKB Topological domain 218 222 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03529 UniProtKB Transmembrane 223 243 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03529 UniProtKB Topological domain 244 297 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03529 UniProtKB Transmembrane 298 318 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03529 UniProtKB Topological domain 319 352 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03529 UniProtKB Transmembrane 353 373 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03529 UniProtKB Topological domain 374 384 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03529 UniProtKB Domain 9 90 . . . Note=Cytochrome b5 heme-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279 +Q03529 UniProtKB Metal binding 45 45 . . . Note=Iron (heme axial ligand);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279 +Q03529 UniProtKB Metal binding 72 72 . . . Note=Iron (heme axial ligand);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00279 +Q03529 UniProtKB Helix 129 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1 +Q03529 UniProtKB Helix 138 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1 +Q03529 UniProtKB Helix 154 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1 +Q03529 UniProtKB Helix 165 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1 +Q03529 UniProtKB Helix 191 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1 +Q03529 UniProtKB Helix 200 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1 +Q03529 UniProtKB Helix 222 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1 +Q03529 UniProtKB Turn 247 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1 +Q03529 UniProtKB Helix 251 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1 +Q03529 UniProtKB Helix 258 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1 +Q03529 UniProtKB Helix 269 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1 +Q03529 UniProtKB Beta strand 280 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1 +Q03529 UniProtKB Helix 285 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1 +Q03529 UniProtKB Helix 305 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1 +Q03529 UniProtKB Helix 336 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1 +Q03529 UniProtKB Beta strand 353 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1 +Q03529 UniProtKB Helix 363 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZR1 +##sequence-region Q3E785 1 79 +Q3E785 UniProtKB Chain 1 79 . . . ID=PRO_0000253849;Note=Succinate dehydrogenase assembly factor 1%2C mitochondrial +Q3E785 UniProtKB Mutagenesis 61 61 . . . Note=Abolishes the ability to complement a yeast strain carrying a deletion for this gene. R->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19465911;Dbxref=PMID:19465911 +Q3E785 UniProtKB Mutagenesis 63 63 . . . Note=Abolishes the ability to complement a yeast strain carrying a deletion for this gene. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19465911;Dbxref=PMID:19465911 +##sequence-region Q04401 1 133 +Q04401 UniProtKB Transit peptide 1 12 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19837041;Dbxref=PMID:19837041 +Q04401 UniProtKB Chain 13 133 . . . ID=PRO_0000042652;Note=Succinate dehydrogenase assembly factor 3%2C mitochondrial +Q04401 UniProtKB Sequence conflict 13 13 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q04401 UniProtKB Sequence conflict 17 17 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40505 1 327 +P40505 UniProtKB Chain 1 327 . . . ID=PRO_0000097654;Note=Transcriptional regulatory protein SDS3 +P40505 UniProtKB Coiled coil 61 135 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40505 UniProtKB Modified residue 166 166 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40505 UniProtKB Modified residue 211 211 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P15367 1 167 +P15367 UniProtKB Chain 1 167 . . . ID=PRO_0000109540;Note=Signal peptidase complex catalytic subunit SEC11 +P15367 UniProtKB Topological domain 1 9 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15367 UniProtKB Transmembrane 10 31 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15367 UniProtKB Topological domain 32 167 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15367 UniProtKB Active site 44 44 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15367 UniProtKB Glycosylation 121 121 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15367 UniProtKB Mutagenesis 44 44 . . . Note=Nonviable. S->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10206957;Dbxref=PMID:10206957 +P15367 UniProtKB Mutagenesis 83 83 . . . Note=Nonviable%3B no protein expressed. H->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10206957;Dbxref=PMID:10206957 +P15367 UniProtKB Mutagenesis 83 83 . . . Note=Nonviable. H->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10206957;Dbxref=PMID:10206957 +P15367 UniProtKB Mutagenesis 103 103 . . . Note=Nonviable%3B no protein expressed. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10206957;Dbxref=PMID:10206957 +P15367 UniProtKB Mutagenesis 103 103 . . . Note=Nonviable. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10206957;Dbxref=PMID:10206957 +P15367 UniProtKB Mutagenesis 109 109 . . . Note=Nonviable. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10206957;Dbxref=PMID:10206957 +P15367 UniProtKB Mutagenesis 109 109 . . . Note=Nonviable%3B no protein expressed. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10206957;Dbxref=PMID:10206957 +P15367 UniProtKB Sequence conflict 162 162 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38810 1 929 +P38810 UniProtKB Chain 1 929 . . . ID=PRO_0000205152;Note=SED5-binding protein 3 +P38810 UniProtKB Region 220 244 . . . Note=Zinc finger-like +P38810 UniProtKB Modified residue 15 15 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38810 UniProtKB Modified residue 72 72 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38810 UniProtKB Modified residue 83 83 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38810 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38810 UniProtKB Modified residue 94 94 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38810 UniProtKB Modified residue 101 101 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38810 UniProtKB Modified residue 110 110 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38810 UniProtKB Modified residue 216 216 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P33303 1 322 +P33303 UniProtKB Chain 1 322 . . . ID=PRO_0000090679;Note=Succinate/fumarate mitochondrial transporter +P33303 UniProtKB Transmembrane 11 31 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33303 UniProtKB Transmembrane 68 88 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33303 UniProtKB Transmembrane 114 134 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33303 UniProtKB Transmembrane 177 193 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33303 UniProtKB Transmembrane 219 235 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33303 UniProtKB Transmembrane 278 295 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33303 UniProtKB Repeat 8 99 . . . Note=Solcar 1 +P33303 UniProtKB Repeat 111 202 . . . Note=Solcar 2 +P33303 UniProtKB Repeat 212 303 . . . Note=Solcar 3 +P33303 UniProtKB Sequence conflict 300 322 . . . Note=VREHLENLGIFKKNDTPKPKPLK->RKGAFQKIWVYSRRMTHQSQSH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P51534 1 789 +P51534 UniProtKB Chain 1 789 . . . ID=PRO_0000097736;Note=SWI5-dependent HO expression protein 4 +P51534 UniProtKB Modified residue 18 18 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P51534 UniProtKB Sequence conflict 254 254 . . . Note=L->LKL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P51534 UniProtKB Sequence conflict 628 628 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P51534 UniProtKB Sequence conflict 770 770 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P51534 UniProtKB Beta strand 4 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 14 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Turn 26 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 33 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Turn 44 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Turn 57 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Beta strand 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 65 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 83 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 97 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 112 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 122 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 126 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 144 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Turn 163 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 167 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Turn 174 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 179 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 223 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Turn 235 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 239 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Turn 248 250 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 251 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 265 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 282 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 303 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 306 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 318 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 327 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Turn 338 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 361 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 377 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 386 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Turn 397 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 404 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 449 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Turn 464 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 469 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 477 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 482 496 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 499 501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 502 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 510 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 527 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 545 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Beta strand 549 552 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 557 563 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Beta strand 568 570 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 584 599 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 603 614 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 616 624 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 625 627 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 631 645 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 648 650 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 652 654 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 661 672 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 673 675 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 679 695 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 697 703 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 707 719 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Turn 720 722 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 724 738 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Turn 744 747 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 751 754 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 757 767 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Beta strand 768 772 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +P51534 UniProtKB Helix 779 784 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OPB +##sequence-region P38337 1 142 +P38337 UniProtKB Chain 1 142 . . . ID=PRO_0000212515;Note=COMPASS component SHG1 +##sequence-region P40073 1 367 +P40073 UniProtKB Chain 1 367 . . . ID=PRO_0000072231;Note=High osmolarity signaling protein SHO1 +P40073 UniProtKB Topological domain 1 32 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40073 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40073 UniProtKB Topological domain 54 65 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40073 UniProtKB Transmembrane 66 86 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40073 UniProtKB Topological domain 87 93 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40073 UniProtKB Transmembrane 94 114 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40073 UniProtKB Topological domain 115 122 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40073 UniProtKB Transmembrane 123 143 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40073 UniProtKB Topological domain 144 367 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40073 UniProtKB Domain 300 361 . . . Note=SH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P40073 UniProtKB Modified residue 166 166 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17363249;Dbxref=PMID:17363249 +P40073 UniProtKB Glycosylation 59 59 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40073 UniProtKB Mutagenesis 166 166 . . . Note=Diminishes the formation of oligomers%2C dampens activation of the HOG1 kinase%2C and impairs growth in high-salt or sorbitol conditions. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17363249;Dbxref=PMID:17363249 +P40073 UniProtKB Mutagenesis 309 309 . . . Note=Decreases the interaction with PBS2 and leads to decreased HOG pathway response and increased aberrant mating pathway activation. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15200958;Dbxref=PMID:15200958 +P40073 UniProtKB Mutagenesis 317 317 . . . Note=Decreases the interaction with PBS2 and leads to decreased HOG pathway response and increased aberrant mating pathway activation. D->I%2CH;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15200958;Dbxref=PMID:15200958 +P40073 UniProtKB Mutagenesis 355 355 . . . Note=Decreases the interaction with PBS2 and leads to decreased HOG pathway response and increased aberrant mating pathway activation. Y->A%2CF%2CI%2CM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15200958;Dbxref=PMID:15200958 +P40073 UniProtKB Beta strand 302 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VKN +P40073 UniProtKB Beta strand 315 317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VKN +P40073 UniProtKB Beta strand 328 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VKN +P40073 UniProtKB Beta strand 336 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VKN +P40073 UniProtKB Beta strand 348 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VKN +P40073 UniProtKB Helix 353 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VKN +P40073 UniProtKB Beta strand 356 363 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2VKN +##sequence-region P25294 1 352 +P25294 UniProtKB Chain 1 352 . . . ID=PRO_0000071090;Note=Protein SIS1 +P25294 UniProtKB Domain 4 70 . . . Note=J;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00286 +P25294 UniProtKB Compositional bias 75 166 . . . Note=Gly-rich +P25294 UniProtKB Modified residue 275 275 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25294 UniProtKB Helix 6 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RWU +P25294 UniProtKB Helix 19 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RWU +P25294 UniProtKB Helix 42 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RWU +P25294 UniProtKB Helix 58 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RWU +P25294 UniProtKB Helix 69 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RWU +P25294 UniProtKB Beta strand 181 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G +P25294 UniProtKB Helix 190 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G +P25294 UniProtKB Beta strand 198 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G +P25294 UniProtKB Turn 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G +P25294 UniProtKB Beta strand 211 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G +P25294 UniProtKB Beta strand 230 235 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G +P25294 UniProtKB Beta strand 237 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G +P25294 UniProtKB Beta strand 241 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G +P25294 UniProtKB Beta strand 248 255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G +P25294 UniProtKB Beta strand 259 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G +P25294 UniProtKB Beta strand 267 272 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G +P25294 UniProtKB Helix 276 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G +P25294 UniProtKB Beta strand 283 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G +P25294 UniProtKB Beta strand 290 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G +P25294 UniProtKB Beta strand 294 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G +P25294 UniProtKB Beta strand 308 310 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G +P25294 UniProtKB Beta strand 319 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2B26 +P25294 UniProtKB Beta strand 328 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G +P25294 UniProtKB Helix 344 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1C3G +##sequence-region P52286 1 194 +P52286 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8670864;Dbxref=PMID:8670864 +P52286 UniProtKB Chain 2 194 . . . ID=PRO_0000187257;Note=Suppressor of kinetochore protein 1 +P52286 UniProtKB Region 135 194 . . . Note=Interaction with the F-box domain of F-box proteins;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P52286 UniProtKB Compositional bias 66 74 . . . Note=Asp/Glu-rich (highly acidic) +P52286 UniProtKB Modified residue 177 177 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P52286 UniProtKB Sequence conflict 48 48 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P52286 UniProtKB Beta strand 5 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P52286 UniProtKB Beta strand 15 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P52286 UniProtKB Helix 20 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P52286 UniProtKB Helix 27 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P52286 UniProtKB Beta strand 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P52286 UniProtKB Helix 84 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P52286 UniProtKB Turn 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P52286 UniProtKB Helix 118 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P52286 UniProtKB Helix 128 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P52286 UniProtKB Helix 144 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P52286 UniProtKB Helix 163 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +P52286 UniProtKB Helix 178 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V7D +##sequence-region P33338 1 968 +P33338 UniProtKB Chain 1 968 . . . ID=PRO_0000071945;Note=Protein SLA2 +P33338 UniProtKB Transmembrane 772 791 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243 +P33338 UniProtKB Domain 1 127 . . . Note=ENTH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00243 +P33338 UniProtKB Domain 717 965 . . . Note=I/LWEQ;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00292 +P33338 UniProtKB Modified residue 294 294 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P33338 UniProtKB Modified residue 298 298 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33338 UniProtKB Modified residue 308 308 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P33338 UniProtKB Modified residue 555 555 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P33338 UniProtKB Sequence conflict 52 52 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33338 UniProtKB Sequence conflict 344 344 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33338 UniProtKB Sequence conflict 344 344 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33338 UniProtKB Sequence conflict 560 560 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33338 UniProtKB Sequence conflict 915 915 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P43321 1 101 +P43321 UniProtKB Chain 1 101 . . . ID=PRO_0000122220;Note=Small nuclear ribonucleoprotein Sm D3 +P43321 UniProtKB Sequence conflict 88 88 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P43321 UniProtKB Helix 6 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P43321 UniProtKB Beta strand 17 25 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P43321 UniProtKB Beta strand 29 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P43321 UniProtKB Beta strand 42 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P43321 UniProtKB Beta strand 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P43321 UniProtKB Beta strand 56 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P43321 UniProtKB Helix 66 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P43321 UniProtKB Beta strand 69 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P43321 UniProtKB Helix 76 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P43321 UniProtKB Beta strand 81 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region Q12078 1 473 +Q12078 UniProtKB Chain 1 473 . . . ID=PRO_0000270538;Note=Iron transporter SMF3 +Q12078 UniProtKB Transmembrane 14 34 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12078 UniProtKB Transmembrane 44 64 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12078 UniProtKB Transmembrane 97 117 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12078 UniProtKB Transmembrane 119 139 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12078 UniProtKB Transmembrane 152 172 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12078 UniProtKB Transmembrane 198 218 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12078 UniProtKB Transmembrane 257 277 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12078 UniProtKB Transmembrane 297 317 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12078 UniProtKB Transmembrane 352 372 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12078 UniProtKB Transmembrane 373 393 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12078 UniProtKB Transmembrane 448 468 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12078 UniProtKB Glycosylation 87 87 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P48232 1 102 +P48232 UniProtKB Chain 1 102 . . . ID=PRO_0000203445;Note=Biogenesis of lysosome-related organelles complex 1 subunit SNN1 +P48232 UniProtKB Coiled coil 71 102 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53823 1 222 +P53823 UniProtKB Chain 1 222 . . . ID=PRO_0000135620;Note=Probable pyridoxal 5'-phosphate synthase subunit SNO2 +P53823 UniProtKB Region 58 60 . . . Note=L-glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528 +P53823 UniProtKB Region 151 152 . . . Note=L-glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528 +P53823 UniProtKB Active site 91 91 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528 +P53823 UniProtKB Active site 197 197 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528 +P53823 UniProtKB Active site 199 199 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528 +P53823 UniProtKB Binding site 120 120 . . . Note=L-glutamine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528 +##sequence-region P25357 1 1226 +P25357 UniProtKB Chain 1 1226 . . . ID=PRO_0000197122;Note=Probable DNA-binding protein SNT1 +P25357 UniProtKB Domain 668 720 . . . Note=SANT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00624 +P25357 UniProtKB Domain 884 938 . . . Note=HTH myb-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +P25357 UniProtKB DNA binding 911 934 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00625 +P25357 UniProtKB Coiled coil 539 591 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25357 UniProtKB Compositional bias 28 159 . . . Note=Ser-rich +P25357 UniProtKB Compositional bias 594 599 . . . Note=Poly-Ser +P25357 UniProtKB Modified residue 187 187 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25357 UniProtKB Modified residue 395 395 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25357 UniProtKB Modified residue 796 796 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P25357 UniProtKB Modified residue 1037 1037 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25357 UniProtKB Sequence conflict 305 305 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25357 UniProtKB Sequence conflict 375 375 . . . Note=S->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25357 UniProtKB Sequence conflict 404 404 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25357 UniProtKB Sequence conflict 435 435 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25357 UniProtKB Sequence conflict 442 442 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25357 UniProtKB Sequence conflict 482 482 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25357 UniProtKB Sequence conflict 513 513 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25357 UniProtKB Sequence conflict 644 644 . . . Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25357 UniProtKB Sequence conflict 766 766 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25357 UniProtKB Sequence conflict 806 806 . . . Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25357 UniProtKB Sequence conflict 831 831 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25357 UniProtKB Sequence conflict 846 846 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25357 UniProtKB Sequence conflict 851 851 . . . Note=D->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25357 UniProtKB Sequence conflict 855 857 . . . Note=AVQ->GVR;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q03782 1 492 +Q03782 UniProtKB Chain 1 492 . . . ID=PRO_0000232634;Note=56 kDa U1 small nuclear ribonucleoprotein component +Q03782 UniProtKB Mutagenesis 125 125 . . . Note=Loss of function. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9630245;Dbxref=PMID:9630245 +##sequence-region Q08826 1 162 +Q08826 UniProtKB Chain 1 162 . . . ID=PRO_0000213805;Note=Sorting nexin-3 +Q08826 UniProtKB Domain 38 161 . . . Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147 +Q08826 UniProtKB Binding site 81 81 . . . Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14514667;Dbxref=PMID:14514667 +Q08826 UniProtKB Binding site 83 83 . . . Note=Phosphatidylinositol 3-phosphate%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14514667;Dbxref=PMID:14514667 +Q08826 UniProtKB Binding site 112 112 . . . Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14514667;Dbxref=PMID:14514667 +Q08826 UniProtKB Binding site 127 127 . . . Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14514667;Dbxref=PMID:14514667 +Q08826 UniProtKB Beta strand 36 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OCS +Q08826 UniProtKB Beta strand 50 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OCU +Q08826 UniProtKB Beta strand 57 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OCS +Q08826 UniProtKB Beta strand 74 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OCS +Q08826 UniProtKB Helix 82 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OCS +Q08826 UniProtKB Helix 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OCU +Q08826 UniProtKB Helix 121 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OCS +Q08826 UniProtKB Helix 142 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OCS +Q08826 UniProtKB Helix 149 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OCS +##sequence-region P43545 1 298 +P43545 UniProtKB Chain 1 298 . . . ID=PRO_0000109360;Note=Probable pyridoxal 5'-phosphate synthase subunit SNZ3 +P43545 UniProtKB Region 234 235 . . . Note=D-ribose 5-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080 +P43545 UniProtKB Active site 78 78 . . . Note=Schiff-base intermediate with D-ribose 5-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080 +P43545 UniProtKB Binding site 21 21 . . . Note=D-ribose 5-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080 +P43545 UniProtKB Binding site 150 150 . . . Note=D-ribose 5-phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080 +P43545 UniProtKB Binding site 213 213 . . . Note=D-ribose 5-phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080 +##sequence-region P50278 1 321 +P50278 UniProtKB Chain 1 321 . . . ID=PRO_0000090082;Note=6-phosphogluconolactonase-like protein 1 +P50278 UniProtKB Modified residue 65 65 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P50278 UniProtKB Modified residue 68 68 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P50278 UniProtKB Modified residue 320 320 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P38858 1 249 +P38858 UniProtKB Chain 1 249 . . . ID=PRO_0000090084;Note=6-phosphogluconolactonase 3 +##sequence-region P53165 1 657 +P53165 UniProtKB Chain 1 657 . . . ID=PRO_0000202764;Note=SAGA-associated factor 73 +P53165 UniProtKB Domain 220 286 . . . Note=SCA7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00838 +P53165 UniProtKB Compositional bias 141 150 . . . Note=Poly-Asp +P53165 UniProtKB Compositional bias 153 162 . . . Note=Poly-Asp +P53165 UniProtKB Compositional bias 466 476 . . . Note=Poly-Gln +P53165 UniProtKB Compositional bias 517 526 . . . Note=Poly-Gln +P53165 UniProtKB Beta strand 7 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FK5 +P53165 UniProtKB Helix 13 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P53165 UniProtKB Turn 19 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FJC +P53165 UniProtKB Beta strand 28 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FJC +P53165 UniProtKB Helix 32 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P53165 UniProtKB Helix 36 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P53165 UniProtKB Beta strand 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P53165 UniProtKB Helix 51 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P53165 UniProtKB Beta strand 70 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P53165 UniProtKB Beta strand 76 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P53165 UniProtKB Turn 79 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P53165 UniProtKB Beta strand 84 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FK5 +P53165 UniProtKB Helix 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +P53165 UniProtKB Turn 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +##sequence-region Q12212 1 622 +Q12212 UniProtKB Signal peptide 1 27 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12212 UniProtKB Chain 28 622 . . . ID=PRO_0000042719;Note=Protein SIA1 +##sequence-region Q08199 1 421 +Q08199 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08199 UniProtKB Chain 20 421 . . . ID=PRO_0000223364;Note=Nucleotide exchange factor SIL1 +Q08199 UniProtKB Motif 418 421 . . . Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10138 +Q08199 UniProtKB Glycosylation 105 105 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08199 UniProtKB Glycosylation 181 181 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08199 UniProtKB Glycosylation 215 215 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08199 UniProtKB Glycosylation 233 233 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08199 UniProtKB Glycosylation 315 315 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08199 UniProtKB Glycosylation 333 333 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08199 UniProtKB Mutagenesis 365 369 . . . Note=Abrogates interaction with KAR2. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10958688;Dbxref=PMID:10958688 +Q08199 UniProtKB Sequence conflict 51 51 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08199 UniProtKB Helix 127 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +Q08199 UniProtKB Helix 145 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +Q08199 UniProtKB Helix 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +Q08199 UniProtKB Helix 165 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +Q08199 UniProtKB Helix 190 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +Q08199 UniProtKB Helix 208 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +Q08199 UniProtKB Helix 221 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +Q08199 UniProtKB Helix 241 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +Q08199 UniProtKB Helix 266 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +Q08199 UniProtKB Turn 276 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +Q08199 UniProtKB Helix 280 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +Q08199 UniProtKB Helix 306 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +Q08199 UniProtKB Helix 321 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +Q08199 UniProtKB Helix 338 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +Q08199 UniProtKB Helix 356 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +Q08199 UniProtKB Helix 363 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +Q08199 UniProtKB Helix 389 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +Q08199 UniProtKB Turn 403 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QML +##sequence-region P40472 1 476 +P40472 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40472 UniProtKB Chain 20 476 . . . ID=PRO_0000033465;Note=Probable secreted beta-glucosidase SIM1 +P40472 UniProtKB Compositional bias 58 113 . . . Note=Ala-rich +P40472 UniProtKB Compositional bias 81 204 . . . Note=Ser-rich +P40472 UniProtKB Glycosylation 423 423 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40472 UniProtKB Natural variant 60 66 . . . Note=In strain: SK1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P40472 UniProtKB Natural variant 174 185 . . . Note=In strain: SK1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P40472 UniProtKB Sequence conflict 85 88 . . . Note=ADSS->GIA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P11978 1 1358 +P11978 UniProtKB Chain 1 1358 . . . ID=PRO_0000097769;Note=Regulatory protein SIR4 +P11978 UniProtKB Coiled coil 1271 1347 . . . . +P11978 UniProtKB Modified residue 692 692 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P11978 UniProtKB Cross-link 1128 1128 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15542864;Dbxref=PMID:15542864 +P11978 UniProtKB Natural variant 994 994 . . . Note=P->L +P11978 UniProtKB Helix 808 821 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO +P11978 UniProtKB Helix 829 837 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO +P11978 UniProtKB Turn 846 848 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO +P11978 UniProtKB Turn 854 857 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO +P11978 UniProtKB Turn 861 863 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO +P11978 UniProtKB Helix 864 866 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO +P11978 UniProtKB Helix 869 872 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO +P11978 UniProtKB Beta strand 879 883 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IAO +P11978 UniProtKB Helix 1273 1342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PL5 +P11978 UniProtKB Turn 1343 1345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PL5 +##sequence-region P36169 1 355 +P36169 UniProtKB Chain 1 355 . . . ID=PRO_0000203230;Note=Suppressor of lethality of KEX2 GAS1 double null mutant protein 1 +P36169 UniProtKB Topological domain 1 8 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36169 UniProtKB Transmembrane 9 29 . . . Note=Helical%3B Signal-anchor for type III membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36169 UniProtKB Topological domain 30 355 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36169 UniProtKB Modified residue 142 142 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36169 UniProtKB Modified residue 273 273 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:18407956 +##sequence-region P32790 1 1244 +P32790 UniProtKB Chain 1 1244 . . . ID=PRO_0000071943;Note=Actin cytoskeleton-regulatory complex protein SLA1 +P32790 UniProtKB Domain 8 69 . . . Note=SH3 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P32790 UniProtKB Domain 70 132 . . . Note=SH3 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P32790 UniProtKB Domain 353 415 . . . Note=SH3 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00192 +P32790 UniProtKB Repeat 868 874 . . . Note=1 +P32790 UniProtKB Repeat 877 883 . . . Note=2 +P32790 UniProtKB Repeat 887 893 . . . Note=3 +P32790 UniProtKB Repeat 923 929 . . . Note=4 +P32790 UniProtKB Repeat 945 951 . . . Note=5 +P32790 UniProtKB Repeat 1003 1009 . . . Note=6 +P32790 UniProtKB Repeat 1020 1026 . . . Note=7 +P32790 UniProtKB Repeat 1031 1037 . . . Note=8 +P32790 UniProtKB Repeat 1048 1054 . . . Note=9 +P32790 UniProtKB Repeat 1065 1071 . . . Note=10 +P32790 UniProtKB Repeat 1084 1090 . . . Note=11 +P32790 UniProtKB Repeat 1129 1135 . . . Note=12 +P32790 UniProtKB Repeat 1155 1161 . . . Note=13 +P32790 UniProtKB Repeat 1170 1176 . . . Note=14 +P32790 UniProtKB Repeat 1185 1191 . . . Note=15 +P32790 UniProtKB Repeat 1200 1206 . . . Note=16 +P32790 UniProtKB Region 868 1205 . . . Note=16 X 7 AA approximate repeats of T-G-G-A-M-M-P +P32790 UniProtKB Modified residue 447 447 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32790 UniProtKB Modified residue 449 449 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32790 UniProtKB Modified residue 454 454 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32790 UniProtKB Modified residue 799 799 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32790 UniProtKB Modified residue 831 831 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32790 UniProtKB Modified residue 858 858 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32790 UniProtKB Modified residue 887 887 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32790 UniProtKB Modified residue 904 904 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32790 UniProtKB Modified residue 984 984 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32790 UniProtKB Modified residue 993 993 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32790 UniProtKB Modified residue 996 996 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32790 UniProtKB Modified residue 1075 1075 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32790 UniProtKB Cross-link 471 471 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32790 UniProtKB Cross-link 548 548 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32790 UniProtKB Beta strand 357 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1Q +P32790 UniProtKB Beta strand 379 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1Q +P32790 UniProtKB Beta strand 389 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1Q +P32790 UniProtKB Turn 397 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1Q +P32790 UniProtKB Beta strand 402 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1Q +P32790 UniProtKB Helix 407 409 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1Q +P32790 UniProtKB Beta strand 410 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V1Q +P32790 UniProtKB Turn 413 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2JT4 +P32790 UniProtKB Beta strand 497 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBP +P32790 UniProtKB Beta strand 508 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBP +P32790 UniProtKB Beta strand 520 524 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBP +P32790 UniProtKB Beta strand 530 534 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBP +P32790 UniProtKB Helix 540 550 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBP +P32790 UniProtKB Helix 555 557 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HBP +P32790 UniProtKB Helix 657 663 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IDW +P32790 UniProtKB Helix 668 680 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IDW +P32790 UniProtKB Helix 685 690 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IDW +P32790 UniProtKB Helix 693 698 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IDW +P32790 UniProtKB Helix 703 716 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3IDW +##sequence-region P47037 1 1230 +P47037 UniProtKB Chain 1 1230 . . . ID=PRO_0000119015;Note=Structural maintenance of chromosomes protein 3 +P47037 UniProtKB Nucleotide binding 32 39 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47037 UniProtKB Region 483 684 . . . Note=Flexible hinge +P47037 UniProtKB Coiled coil 172 482 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47037 UniProtKB Coiled coil 685 1041 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47037 UniProtKB Compositional bias 1126 1161 . . . Note=Ala/Asp-rich (DA-box) +P47037 UniProtKB Modified residue 112 112 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18614053;Dbxref=PMID:18614053 +P47037 UniProtKB Modified residue 113 113 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18614053;Dbxref=PMID:18614053 +P47037 UniProtKB Beta strand 6 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Beta strand 14 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Beta strand 25 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Helix 38 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Beta strand 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Helix 58 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Beta strand 68 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Beta strand 77 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Turn 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Turn 118 121 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Helix 125 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Beta strand 142 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Helix 152 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Helix 159 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Helix 172 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Helix 239 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Helix 976 980 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Helix 982 988 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Helix 998 1059 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Beta strand 1065 1069 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Beta strand 1109 1113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Beta strand 1121 1123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Helix 1128 1143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Beta strand 1149 1153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Turn 1154 1159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Helix 1162 1176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Beta strand 1179 1184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Helix 1188 1190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Turn 1191 1193 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Beta strand 1198 1203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Beta strand 1206 1210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +P47037 UniProtKB Helix 1214 1221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4UX3 +##sequence-region Q02260 1 146 +Q02260 UniProtKB Chain 1 146 . . . ID=PRO_0000122206;Note=Small nuclear ribonucleoprotein Sm D1 +Q02260 UniProtKB Motif 128 144 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02260 UniProtKB Helix 3 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q02260 UniProtKB Beta strand 12 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q02260 UniProtKB Beta strand 24 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q02260 UniProtKB Beta strand 38 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q02260 UniProtKB Beta strand 80 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q02260 UniProtKB Turn 89 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q02260 UniProtKB Beta strand 92 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q02260 UniProtKB Helix 103 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P38925 1 575 +P38925 UniProtKB Chain 1 575 . . . ID=PRO_0000212605;Note=Manganese transporter SMF1 +P38925 UniProtKB Topological domain 1 70 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Transmembrane 71 91 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Topological domain 92 108 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Transmembrane 109 129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Topological domain 130 156 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Transmembrane 157 177 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Topological domain 178 179 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Transmembrane 180 200 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Topological domain 201 218 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Transmembrane 219 239 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Topological domain 240 266 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Transmembrane 267 287 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Topological domain 288 344 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Transmembrane 345 365 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Topological domain 366 396 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Transmembrane 397 417 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Topological domain 418 463 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Transmembrane 464 484 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Topological domain 485 543 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Transmembrane 544 564 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Topological domain 565 575 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38925 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P38925 UniProtKB Cross-link 33 33 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38925 UniProtKB Cross-link 34 34 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P38925 UniProtKB Sequence conflict 305 305 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38925 UniProtKB Sequence conflict 416 416 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04007 1 877 +Q04007 UniProtKB Chain 1 877 . . . ID=PRO_0000253835;Note=SRP-independent targeting protein 1 +Q04007 UniProtKB Coiled coil 412 441 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04007 UniProtKB Compositional bias 482 495 . . . Note=Poly-Asp +Q04007 UniProtKB Compositional bias 690 823 . . . Note=Asn-rich +Q04007 UniProtKB Modified residue 309 309 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04007 UniProtKB Modified residue 310 310 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04007 UniProtKB Modified residue 311 311 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04007 UniProtKB Modified residue 332 332 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q04007 UniProtKB Modified residue 334 334 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q04007 UniProtKB Modified residue 692 692 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q04007 UniProtKB Modified residue 694 694 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04007 UniProtKB Modified residue 706 706 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +Q04007 UniProtKB Modified residue 841 841 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q04007 UniProtKB Cross-link 668 668 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q04007 UniProtKB Cross-link 670 670 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P38956 1 169 +P38956 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38956 UniProtKB Chain 2 169 . . . ID=PRO_0000072004;Note=Transcription regulatory protein SNF11 +P38956 UniProtKB Repeat 28 31 . . . Note=1-1 +P38956 UniProtKB Repeat 32 35 . . . Note=1-2 +P38956 UniProtKB Repeat 36 39 . . . Note=1-3 +P38956 UniProtKB Repeat 40 43 . . . Note=1-4 +P38956 UniProtKB Repeat 44 47 . . . Note=1-5 +P38956 UniProtKB Repeat 48 51 . . . Note=1-6 +P38956 UniProtKB Repeat 76 80 . . . Note=2-1 +P38956 UniProtKB Repeat 160 165 . . . Note=2-2 +P38956 UniProtKB Region 28 51 . . . Note=6 X 4 AA tandem repeats of N-[AT]-[NT]-A +P38956 UniProtKB Region 76 165 . . . Note=2 X 5 AA repeats of L-L-A-R-V +P38956 UniProtKB Compositional bias 93 102 . . . Note=Poly-Asn +P38956 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P22082 1 1703 +P22082 UniProtKB Chain 1 1703 . . . ID=PRO_0000074358;Note=Transcription regulatory protein SNF2 +P22082 UniProtKB Domain 247 282 . . . Note=QLQ;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01001 +P22082 UniProtKB Domain 588 661 . . . Note=HSA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00549 +P22082 UniProtKB Domain 779 944 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P22082 UniProtKB Domain 1091 1254 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P22082 UniProtKB Domain 1568 1638 . . . Note=Bromo;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 +P22082 UniProtKB Nucleotide binding 792 799 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P22082 UniProtKB DNA binding 1446 1456 . . . Note=A.T hook 1 +P22082 UniProtKB DNA binding 1502 1513 . . . Note=A.T hook 2 +P22082 UniProtKB DNA binding 1516 1526 . . . Note=A.T hook 3 +P22082 UniProtKB Motif 894 897 . . . Note=DEGH box +P22082 UniProtKB Compositional bias 55 68 . . . Note=Gln-rich +P22082 UniProtKB Compositional bias 207 239 . . . Note=Ala/Gln-rich +P22082 UniProtKB Modified residue 358 358 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P22082 UniProtKB Modified residue 383 383 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P22082 UniProtKB Modified residue 716 716 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P22082 UniProtKB Modified residue 1340 1340 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P22082 UniProtKB Cross-link 543 543 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P22082 UniProtKB Helix 593 657 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4I6M +##sequence-region P46950 1 547 +P46950 UniProtKB Chain 1 547 . . . ID=PRO_0000072007;Note=Nitrosoguanidine resistance protein SNG1 +P46950 UniProtKB Transmembrane 109 129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46950 UniProtKB Transmembrane 159 179 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46950 UniProtKB Transmembrane 318 338 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46950 UniProtKB Transmembrane 363 383 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46950 UniProtKB Transmembrane 394 414 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46950 UniProtKB Transmembrane 418 438 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46950 UniProtKB Transmembrane 457 477 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46950 UniProtKB Transmembrane 488 508 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46950 UniProtKB Modified residue 91 91 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P46950 UniProtKB Sequence conflict 117 117 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53127 1 1403 +P53127 UniProtKB Chain 1 1403 . . . ID=PRO_0000202742;Note=E3 ubiquitin-protein ligase SNT2 +P53127 UniProtKB Domain 121 258 . . . Note=BAH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00370 +P53127 UniProtKB Domain 555 606 . . . Note=SANT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00624 +P53127 UniProtKB Zinc finger 317 369 . . . Note=PHD-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 +P53127 UniProtKB Zinc finger 1038 1097 . . . Note=PHD-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 +P53127 UniProtKB Zinc finger 1041 1095 . . . Note=RING-type%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 +P53127 UniProtKB Zinc finger 1105 1153 . . . Note=C2HC pre-PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01146 +P53127 UniProtKB Zinc finger 1177 1231 . . . Note=PHD-type 3%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01146 +##sequence-region P39990 1 126 +P39990 UniProtKB Chain 1 126 . . . ID=PRO_0000136777;Note=13 kDa ribonucleoprotein-associated protein +P39990 UniProtKB Mutagenesis 59 59 . . . Note=Impairs binding to U4 snRNA%2C but not U3 snoRNA. Causes pre-mRNA splicing and pre-rRNA processing defects. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14730029;Dbxref=PMID:14730029 +P39990 UniProtKB Mutagenesis 81 81 . . . Note=Impairs binding to U4 snRNA%2C but not U3 snoRNA%2C and causes pre rRNA processing defects and an accumulation of unspliced U3 snoRNA%3B when associated with A-84. V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14730029;Dbxref=PMID:14730029 +P39990 UniProtKB Mutagenesis 84 84 . . . Note=Impairs binding to U4 snRNA%2C but not U3 snoRNA%2C and causes pre rRNA processing defects and an accumulation of unspliced U3 snoRNA%3B when associated with L-81. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14730029;Dbxref=PMID:14730029 +P39990 UniProtKB Helix 14 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT +P39990 UniProtKB Beta strand 33 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT +P39990 UniProtKB Helix 37 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT +P39990 UniProtKB Beta strand 49 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT +P39990 UniProtKB Helix 61 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT +P39990 UniProtKB Helix 66 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT +P39990 UniProtKB Beta strand 78 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT +P39990 UniProtKB Helix 84 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT +P39990 UniProtKB Beta strand 98 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT +P39990 UniProtKB Helix 110 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4NUT +##sequence-region Q04053 1 625 +Q04053 UniProtKB Chain 1 625 . . . ID=PRO_0000213834;Note=Sorting nexin-41 +Q04053 UniProtKB Domain 98 235 . . . Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147 +Q04053 UniProtKB Coiled coil 437 469 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04053 UniProtKB Coiled coil 539 563 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04053 UniProtKB Compositional bias 54 84 . . . Note=Ser-rich +Q04053 UniProtKB Compositional bias 497 508 . . . Note=Ser-rich +Q04053 UniProtKB Binding site 153 153 . . . Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04053 UniProtKB Binding site 155 155 . . . Note=Phosphatidylinositol 3-phosphate%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04053 UniProtKB Binding site 179 179 . . . Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04053 UniProtKB Binding site 202 202 . . . Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q03148 1 297 +Q03148 UniProtKB Chain 1 297 . . . ID=PRO_0000109358;Note=Pyridoxal 5'-phosphate synthase subunit SNZ1 +Q03148 UniProtKB Region 235 236 . . . Note=D-ribose 5-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080 +Q03148 UniProtKB Active site 80 80 . . . Note=Schiff-base intermediate with D-ribose 5-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080 +Q03148 UniProtKB Binding site 23 23 . . . Note=D-ribose 5-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080 +Q03148 UniProtKB Binding site 152 152 . . . Note=D-ribose 5-phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080 +Q03148 UniProtKB Binding site 164 164 . . . Note=Glyceraldehyde 3-phosphate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20919991;Dbxref=PMID:20919991 +Q03148 UniProtKB Binding site 214 214 . . . Note=D-ribose 5-phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080 +Q03148 UniProtKB Mutagenesis 116 116 . . . Note=No effect. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20919991;Dbxref=PMID:20919991 +Q03148 UniProtKB Mutagenesis 117 117 . . . Note=No activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20919991;Dbxref=PMID:20919991 +Q03148 UniProtKB Mutagenesis 136 137 . . . Note=No pyridoxal 5'-phosphate synthesis activity. Retains ability to isomerize dihydroxyacetone phosphate to glyceraldehyde 3-phosphate. RR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20919991;Dbxref=PMID:20919991 +Q03148 UniProtKB Mutagenesis 148 148 . . . Note=No activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20919991;Dbxref=PMID:20919991 +Q03148 UniProtKB Mutagenesis 164 164 . . . Note=No pyridoxal 5'-phosphate synthesis activity. Retains ability to isomerize dihydroxyacetone phosphate to glyceraldehyde 3-phosphate. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20919991;Dbxref=PMID:20919991 +Q03148 UniProtKB Mutagenesis 240 240 . . . Note=No effect. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20919991;Dbxref=PMID:20919991 +Q03148 UniProtKB Helix 4 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FEM +Q03148 UniProtKB Turn 15 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FEM +Q03148 UniProtKB Beta strand 20 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Helix 27 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Beta strand 39 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Helix 48 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Turn 53 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Helix 63 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Beta strand 77 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Helix 86 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Beta strand 98 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Helix 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Beta strand 124 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Helix 131 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Beta strand 143 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Beta strand 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O06 +Q03148 UniProtKB Helix 157 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Helix 179 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Helix 193 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Beta strand 209 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Helix 218 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Beta strand 232 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Helix 236 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Beta strand 241 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FEM +Q03148 UniProtKB Helix 244 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Turn 257 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Helix 261 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O07 +Q03148 UniProtKB Helix 280 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FEM +##sequence-region P53438 1 785 +P53438 UniProtKB Chain 1 785 . . . ID=PRO_0000072036;Note=Protein SOK2 +P53438 UniProtKB Domain 414 520 . . . Note=HTH APSES-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630 +P53438 UniProtKB DNA binding 448 469 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630 +P53438 UniProtKB Compositional bias 38 45 . . . Note=Poly-Gln +P53438 UniProtKB Compositional bias 148 151 . . . Note=Poly-Tyr +P53438 UniProtKB Compositional bias 169 172 . . . Note=Poly-Tyr +P53438 UniProtKB Compositional bias 206 217 . . . Note=Poly-Gln +P53438 UniProtKB Compositional bias 331 335 . . . Note=Poly-Gln +P53438 UniProtKB Compositional bias 526 532 . . . Note=Poly-Ser +P53438 UniProtKB Modified residue 771 771 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P37262 1 315 +P37262 UniProtKB Chain 1 315 . . . ID=PRO_0000090083;Note=6-phosphogluconolactonase-like protein 2 +P37262 UniProtKB Modified residue 42 42 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P37262 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50278 +##sequence-region P38128 1 452 +P38128 UniProtKB Chain 1 452 . . . ID=PRO_0000199441;Note=Transcription factor SMP1 +P38128 UniProtKB Domain 3 57 . . . Note=MADS-box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00251 +P38128 UniProtKB DNA binding 58 87 . . . Note=Mef2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38128 UniProtKB Compositional bias 99 105 . . . Note=Poly-Arg +##sequence-region P31109 1 117 +P31109 UniProtKB Chain 1 117 . . . ID=PRO_0000206744;Note=Synaptobrevin homolog 1 +P31109 UniProtKB Topological domain 1 94 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31109 UniProtKB Transmembrane 95 111 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31109 UniProtKB Topological domain 112 117 . . . Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31109 UniProtKB Domain 28 88 . . . Note=v-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00290 +P31109 UniProtKB Lipidation 95 95 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15973437;Dbxref=PMID:15973437 +P31109 UniProtKB Cross-link 63 63 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P31109 UniProtKB Helix 27 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B5N +##sequence-region P33328 1 115 +P33328 UniProtKB Chain 1 115 . . . ID=PRO_0000206745;Note=Synaptobrevin homolog 2 +P33328 UniProtKB Topological domain 1 93 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33328 UniProtKB Transmembrane 94 112 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33328 UniProtKB Topological domain 113 115 . . . Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33328 UniProtKB Domain 27 87 . . . Note=v-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00290 +P33328 UniProtKB Modified residue 58 58 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P33328 UniProtKB Lipidation 94 94 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33328 UniProtKB Cross-link 62 62 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P33328 UniProtKB Sequence conflict 115 115 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53628 1 566 +P53628 UniProtKB Chain 1 566 . . . ID=PRO_0000072005;Note=Transcription regulatory protein SNF12 +##sequence-region Q12420 1 587 +Q12420 UniProtKB Chain 1 587 . . . ID=PRO_0000232635;Note=66 kDa U4/U6.U5 small nuclear ribonucleoprotein component +Q12420 UniProtKB Compositional bias 218 224 . . . Note=Poly-Glu +Q12420 UniProtKB Modified residue 268 268 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q12420 UniProtKB Helix 9 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLU +Q12420 UniProtKB Helix 40 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PLV +##sequence-region P40317 1 901 +P40317 UniProtKB Chain 1 901 . . . ID=PRO_0000072035;Note=Protein SOK1 +P40317 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40317 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40317 UniProtKB Modified residue 191 191 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40317 UniProtKB Modified residue 193 193 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40317 UniProtKB Modified residue 245 245 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40317 UniProtKB Sequence conflict 645 645 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25808 1 606 +P25808 UniProtKB Chain 1 606 . . . ID=PRO_0000055065;Note=ATP-dependent rRNA helicase SPB4 +P25808 UniProtKB Domain 38 224 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P25808 UniProtKB Domain 248 404 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P25808 UniProtKB Nucleotide binding 51 58 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P25808 UniProtKB Coiled coil 539 582 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25808 UniProtKB Motif 7 35 . . . Note=Q motif;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25808 UniProtKB Motif 172 175 . . . Note=DEAD box;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25808 UniProtKB Modified residue 254 254 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P25808 UniProtKB Mutagenesis 360 360 . . . Note=Leads to accumulation of 35S and 27SB pre-rRNAs and a net 40S ribosomal subunit defect. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21825077;Dbxref=PMID:21825077 +##sequence-region P46965 1 94 +P46965 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P46965 UniProtKB Chain 2 94 . . . ID=PRO_0000215162;Note=Signal peptidase complex subunit SPC1 +P46965 UniProtKB Topological domain 2 28 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46965 UniProtKB Transmembrane 29 49 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46965 UniProtKB Topological domain 50 50 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46965 UniProtKB Transmembrane 51 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46965 UniProtKB Topological domain 72 94 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46965 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P38915 1 602 +P38915 UniProtKB Chain 1 602 . . . ID=PRO_0000051226;Note=Transcription factor SPT8 +P38915 UniProtKB Repeat 173 212 . . . Note=WD 1 +P38915 UniProtKB Repeat 305 346 . . . Note=WD 2 +P38915 UniProtKB Repeat 415 454 . . . Note=WD 3 +P38915 UniProtKB Repeat 506 544 . . . Note=WD 4 +P38915 UniProtKB Repeat 560 600 . . . Note=WD 5 +P38915 UniProtKB Compositional bias 1 76 . . . Note=Asp/Glu-rich (highly acidic) +P38915 UniProtKB Modified residue 85 85 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38915 UniProtKB Modified residue 108 108 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38915 UniProtKB Modified residue 123 123 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38915 UniProtKB Modified residue 131 131 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38915 UniProtKB Modified residue 451 451 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q03707 1 834 +Q03707 UniProtKB Chain 1 834 . . . ID=PRO_0000072188;Note=Inner nuclear membrane protein SRC1 +Q03707 UniProtKB Transmembrane 455 475 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03707 UniProtKB Transmembrane 708 728 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03707 UniProtKB Compositional bias 117 129 . . . Note=Poly-Asp +Q03707 UniProtKB Modified residue 78 78 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03707 UniProtKB Modified residue 80 80 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q03707 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q03707 UniProtKB Modified residue 181 181 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03707 UniProtKB Modified residue 203 203 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03707 UniProtKB Modified residue 204 204 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q03707 UniProtKB Modified residue 206 206 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q03707 UniProtKB Modified residue 301 301 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03707 UniProtKB Modified residue 394 394 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03707 UniProtKB Modified residue 427 427 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q99176 1 213 +Q99176 UniProtKB Chain 1 213 . . . ID=PRO_0000072191;Note=Protein SRN2 +Q99176 UniProtKB Domain 128 213 . . . Note=VPS37 C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00646 +Q99176 UniProtKB Mutagenesis 67 67 . . . Note=Defective in ESCRT-I cargo sorting. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384 +Q99176 UniProtKB Mutagenesis 75 75 . . . Note=Defective in ESCRT-I cargo sorting. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384 +Q99176 UniProtKB Mutagenesis 79 79 . . . Note=Defective in ESCRT-I cargo sorting. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384 +Q99176 UniProtKB Mutagenesis 88 88 . . . Note=Defective in ESCRT-I cargo sorting%3B when associated with D-99. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384 +Q99176 UniProtKB Mutagenesis 92 92 . . . Note=Defective in ESCRT-I cargo sorting%3B when associated with D-102. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384 +Q99176 UniProtKB Mutagenesis 95 95 . . . Note=Defective in ESCRT-I cargo sorting%3B when associated with D-99. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384 +Q99176 UniProtKB Mutagenesis 99 99 . . . Note=Defective in ESCRT-I cargo sorting%3B when associated with D-88. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384 +Q99176 UniProtKB Mutagenesis 99 99 . . . Note=Defective in ESCRT-I cargo sorting%3B when associated with D-95. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384 +Q99176 UniProtKB Mutagenesis 102 102 . . . Note=Defective in ESCRT-I cargo sorting%3B when associated with D-92. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384 +Q99176 UniProtKB Mutagenesis 181 181 . . . Note=Abolishes ESCRT-I complex assembly%3B class E phenotype (malformed late MVB)%3B when associated with R-185. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16615894;Dbxref=PMID:16615894 +Q99176 UniProtKB Mutagenesis 185 185 . . . Note=Abolishes ESCRT-I complex assembly%3B class E phenotype (malformed late MVB)%3B when associated with R-181. I->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16615894;Dbxref=PMID:16615894 +Q99176 UniProtKB Sequence conflict 90 90 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q99176 UniProtKB Sequence conflict 140 140 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q99176 UniProtKB Sequence conflict 143 143 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q99176 UniProtKB Helix 23 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +Q99176 UniProtKB Helix 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +Q99176 UniProtKB Helix 62 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +Q99176 UniProtKB Helix 72 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +Q99176 UniProtKB Helix 79 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +Q99176 UniProtKB Helix 86 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +Q99176 UniProtKB Beta strand 144 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +Q99176 UniProtKB Helix 147 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +Q99176 UniProtKB Helix 178 205 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +##sequence-region P36057 1 244 +P36057 UniProtKB Chain 1 244 . . . ID=PRO_0000101230;Note=Signal recognition particle receptor subunit beta +P36057 UniProtKB Transmembrane 7 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36057 UniProtKB Nucleotide binding 45 53 . . . Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654246;Dbxref=PMID:12654246 +P36057 UniProtKB Nucleotide binding 66 69 . . . Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654246;Dbxref=PMID:12654246 +P36057 UniProtKB Nucleotide binding 154 157 . . . Note=GTP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654246;Dbxref=PMID:12654246 +P36057 UniProtKB Binding site 90 90 . . . Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12654246;Dbxref=PMID:12654246 +P36057 UniProtKB Beta strand 40 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P36057 UniProtKB Helix 51 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P36057 UniProtKB Beta strand 73 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P36057 UniProtKB Helix 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P36057 UniProtKB Beta strand 84 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P36057 UniProtKB Helix 92 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P36057 UniProtKB Helix 96 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P36057 UniProtKB Helix 106 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P36057 UniProtKB Beta strand 109 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P36057 UniProtKB Helix 126 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P36057 UniProtKB Beta strand 149 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P36057 UniProtKB Helix 164 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P36057 UniProtKB Helix 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P36057 UniProtKB Beta strand 217 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P36057 UniProtKB Beta strand 221 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P36057 UniProtKB Turn 228 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P36057 UniProtKB Helix 234 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +##sequence-region Q06688 1 274 +Q06688 UniProtKB Chain 1 274 . . . ID=PRO_0000186127;Note=SRR1-like protein BER1 +##sequence-region Q03175 1 343 +Q03175 UniProtKB Chain 1 343 . . . ID=PRO_0000123760;Note=Dehydrodolichyl diphosphate synthase complex subunit SRT1 +##sequence-region P39931 1 234 +P39931 UniProtKB Signal peptide 1 22 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39931 UniProtKB Chain 23 234 . . . ID=PRO_0000022420;Note=Protein SSP120 +P39931 UniProtKB Domain 52 87 . . . Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P39931 UniProtKB Domain 108 143 . . . Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 +P39931 UniProtKB Modified residue 212 212 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P38353 1 490 +P38353 UniProtKB Chain 1 490 . . . ID=PRO_0000131811;Note=Sec sixty-one protein homolog +P38353 UniProtKB Topological domain 1 32 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Topological domain 54 121 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Transmembrane 122 142 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Topological domain 143 146 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Transmembrane 147 167 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Topological domain 168 174 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Transmembrane 175 195 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Topological domain 196 242 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Transmembrane 243 263 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Topological domain 264 293 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Transmembrane 294 314 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Topological domain 315 339 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Transmembrane 340 360 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Topological domain 361 361 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Transmembrane 362 382 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Topological domain 383 421 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Transmembrane 422 442 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Topological domain 443 449 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Transmembrane 450 470 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38353 UniProtKB Topological domain 471 490 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53172 1 527 +P53172 UniProtKB Chain 1 527 . . . ID=PRO_0000202767;Note=Protein SDS23 +P53172 UniProtKB Domain 101 162 . . . Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +P53172 UniProtKB Domain 185 243 . . . Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +P53172 UniProtKB Domain 272 330 . . . Note=CBS 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +P53172 UniProtKB Domain 335 391 . . . Note=CBS 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 +P53172 UniProtKB Modified residue 9 9 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53172 UniProtKB Modified residue 42 42 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P53172 UniProtKB Modified residue 46 46 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P53172 UniProtKB Modified residue 430 430 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P53172 UniProtKB Sequence conflict 180 180 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53172 UniProtKB Sequence conflict 180 180 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53172 UniProtKB Sequence conflict 180 180 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12118 1 346 +Q12118 UniProtKB Chain 1 346 . . . ID=PRO_0000106370;Note=Small glutamine-rich tetratricopeptide repeat-containing protein 2 +Q12118 UniProtKB Repeat 102 135 . . . Note=TPR 1 +Q12118 UniProtKB Repeat 136 169 . . . Note=TPR 2 +Q12118 UniProtKB Repeat 170 203 . . . Note=TPR 3 +Q12118 UniProtKB Repeat 205 229 . . . Note=TPR 4 +Q12118 UniProtKB Modified residue 308 308 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12118 UniProtKB Helix 5 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZDM +Q12118 UniProtKB Helix 27 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZDM +Q12118 UniProtKB Helix 48 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZDM +Q12118 UniProtKB Helix 51 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZDM +Q12118 UniProtKB Helix 58 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZDM +Q12118 UniProtKB Helix 69 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LXB +##sequence-region P38200 1 338 +P38200 UniProtKB Chain 1 338 . . . ID=PRO_0000202460;Note=Mitotic spindle-associated protein SHE1 +P38200 UniProtKB Modified residue 165 165 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40486 1 507 +P40486 UniProtKB Chain 1 507 . . . ID=PRO_0000202966;Note=Protein SHQ1 +P40486 UniProtKB Domain 1 91 . . . Note=CS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00547 +P40486 UniProtKB Beta strand 6 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD +P40486 UniProtKB Beta strand 12 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD +P40486 UniProtKB Beta strand 28 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD +P40486 UniProtKB Beta strand 32 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD +P40486 UniProtKB Beta strand 39 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD +P40486 UniProtKB Beta strand 47 52 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD +P40486 UniProtKB Beta strand 64 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD +P40486 UniProtKB Turn 69 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD +P40486 UniProtKB Beta strand 73 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD +P40486 UniProtKB Helix 93 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3EUD +P40486 UniProtKB Helix 172 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 179 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Turn 185 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 196 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 201 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 218 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 233 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 241 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 250 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 275 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 296 315 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Turn 316 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 324 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 333 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 364 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Beta strand 379 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 385 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 403 418 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Turn 421 424 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 425 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 431 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 444 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 463 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Beta strand 467 471 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Turn 476 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZV0 +P40486 UniProtKB Beta strand 483 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +P40486 UniProtKB Helix 488 504 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZUZ +##sequence-region P36024 1 562 +P36024 UniProtKB Chain 1 562 . . . ID=PRO_0000182037;Note=Phosphopantothenoylcysteine decarboxylase subunit SIS2 +P36024 UniProtKB Compositional bias 496 553 . . . Note=Asp/Glu-rich (highly acidic) +P36024 UniProtKB Modified residue 47 47 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P36024 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P36024 UniProtKB Modified residue 54 54 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P36024 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:19779198 +P36024 UniProtKB Modified residue 155 155 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36024 UniProtKB Mutagenesis 378 378 . . . Note=Abolishes PPCDC activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19915539;Dbxref=PMID:19915539 +##sequence-region Q12469 1 655 +Q12469 UniProtKB Chain 1 655 . . . ID=PRO_0000086656;Note=Serine/threonine-protein kinase SKM1 +Q12469 UniProtKB Domain 3 118 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +Q12469 UniProtKB Domain 123 136 . . . Note=CRIB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00057 +Q12469 UniProtKB Domain 360 639 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12469 UniProtKB Nucleotide binding 366 374 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12469 UniProtKB Active site 507 507 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q12469 UniProtKB Binding site 406 406 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q12469 UniProtKB Sequence conflict 150 150 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12469 UniProtKB Sequence conflict 303 303 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12469 UniProtKB Sequence conflict 306 306 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12469 UniProtKB Sequence conflict 320 320 . . . Note=H->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12469 UniProtKB Sequence conflict 322 322 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12469 UniProtKB Sequence conflict 452 452 . . . Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12469 UniProtKB Sequence conflict 468 468 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38889 1 622 +P38889 UniProtKB Chain 1 622 . . . ID=PRO_0000081404;Note=Transcription factor SKN7 +P38889 UniProtKB Domain 378 492 . . . Note=Response regulatory;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00169 +P38889 UniProtKB DNA binding 86 190 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38889 UniProtKB Modified residue 427 427 . . . Note=4-aspartylphosphate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00169,ECO:0000269|PubMed:9843501;Dbxref=PMID:9843501 +P38889 UniProtKB Mutagenesis 427 427 . . . Note=No activity. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7957083,ECO:0000269|PubMed:8598053;Dbxref=PMID:7957083,PMID:8598053 +P38889 UniProtKB Mutagenesis 427 427 . . . Note=Augments activity. D->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7957083,ECO:0000269|PubMed:8598053;Dbxref=PMID:7957083,PMID:8598053 +P38889 UniProtKB Mutagenesis 427 427 . . . Note=Diminishes activity. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7957083,ECO:0000269|PubMed:8598053;Dbxref=PMID:7957083,PMID:8598053 +P38889 UniProtKB Mutagenesis 427 427 . . . Note=No activity. D->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7957083,ECO:0000269|PubMed:8598053;Dbxref=PMID:7957083,PMID:8598053 +P38889 UniProtKB Sequence conflict 45 45 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02100 1 647 +Q02100 UniProtKB Chain 1 647 . . . ID=PRO_0000076517;Note=CRE-binding bZIP protein SKO1 +Q02100 UniProtKB Domain 429 492 . . . Note=bZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +Q02100 UniProtKB Region 430 451 . . . Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +Q02100 UniProtKB Region 454 461 . . . Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +Q02100 UniProtKB Modified residue 94 94 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02100 UniProtKB Modified residue 113 113 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q02100 UniProtKB Modified residue 399 399 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q02100 UniProtKB Modified residue 558 558 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P34252 1 453 +P34252 UniProtKB Chain 1 453 . . . ID=PRO_0000071952;Note=DNA replication regulator SLD2 +P34252 UniProtKB Modified residue 84 84 . . . Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16619031;Dbxref=PMID:16619031 +P34252 UniProtKB Mutagenesis 84 84 . . . Note=No interaction with DPB11. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16619031;Dbxref=PMID:16619031 +P34252 UniProtKB Mutagenesis 100 100 . . . Note=No interaction with DPB11. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16619031;Dbxref=PMID:16619031 +P34252 UniProtKB Mutagenesis 208 208 . . . Note=Normal interaction with DPB11. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16619031;Dbxref=PMID:16619031 +P34252 UniProtKB Mutagenesis 241 241 . . . Note=Reduced interaction with DPB11. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16619031;Dbxref=PMID:16619031 +##sequence-region P53251 1 210 +P53251 UniProtKB Chain 1 210 . . . ID=PRO_0000202808;Note=Ribosome biogenesis protein SLX9 +##sequence-region Q04964 1 104 +Q04964 UniProtKB Chain 1 104 . . . ID=PRO_0000071974;Note=Ribonucleotide reductase inhibitor protein SML1 +Q04964 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q04964 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine%3B by DUN1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14684746;Dbxref=PMID:14684746 +Q04964 UniProtKB Modified residue 58 58 . . . Note=Phosphoserine%3B by DUN1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14684746;Dbxref=PMID:14684746 +Q04964 UniProtKB Modified residue 60 60 . . . Note=Phosphoserine%3B by DUN1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14684746;Dbxref=PMID:14684746 +Q04964 UniProtKB Disulfide bond 14 14 . . . Note=Interchain +Q04964 UniProtKB Mutagenesis 56 61 . . . Note=Increased stability following gamma-irradiation and loss of phosphorylation by DUN1. Causes lethality in rnr1-W688G strain which has a mutation in RNR1. SASASS->AAAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20566477;Dbxref=PMID:20566477 +##sequence-region Q12306 1 101 +Q12306 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q12306 UniProtKB Chain 2 98 . . . ID=PRO_0000035963;Note=Ubiquitin-like protein SMT3 +Q12306 UniProtKB Propeptide 99 101 . . . ID=PRO_0000035964 +Q12306 UniProtKB Domain 22 98 . . . Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214 +Q12306 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q12306 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950 +Q12306 UniProtKB Modified residue 4 4 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q12306 UniProtKB Cross-link 98 98 . . . Note=Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) +Q12306 UniProtKB Beta strand 22 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UF8 +Q12306 UniProtKB Beta strand 34 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UF8 +Q12306 UniProtKB Helix 46 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UF8 +Q12306 UniProtKB Helix 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UF8 +Q12306 UniProtKB Beta strand 64 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UF8 +Q12306 UniProtKB Beta strand 70 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V60 +Q12306 UniProtKB Turn 78 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UF8 +Q12306 UniProtKB Beta strand 87 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UF8 +##sequence-region P32364 1 656 +P32364 UniProtKB Chain 1 656 . . . ID=PRO_0000125454;Note=Kinesin-related protein SMY1 +P32364 UniProtKB Domain 27 364 . . . Note=Kinesin motor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283 +P32364 UniProtKB Nucleotide binding 114 121 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00283 +P32364 UniProtKB Modified residue 583 583 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P32909 1 740 +P32909 UniProtKB Chain 1 740 . . . ID=PRO_0000071996;Note=Protein SMY2 +P32909 UniProtKB Domain 205 261 . . . Note=GYF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00101 +P32909 UniProtKB Coiled coil 369 440 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32909 UniProtKB Compositional bias 576 627 . . . Note=Thr-rich +P32909 UniProtKB Modified residue 12 12 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32909 UniProtKB Modified residue 96 96 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32909 UniProtKB Modified residue 129 129 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P32909 UniProtKB Modified residue 311 311 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32909 UniProtKB Modified residue 545 545 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32909 UniProtKB Modified residue 602 602 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P32909 UniProtKB Beta strand 207 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K3V +P32909 UniProtKB Beta strand 217 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K3V +P32909 UniProtKB Helix 223 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K3V +P32909 UniProtKB Beta strand 240 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K3V +P32909 UniProtKB Beta strand 250 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K3V +P32909 UniProtKB Helix 260 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K3V +P32909 UniProtKB Helix 274 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3K3V +##sequence-region Q06091 1 175 +Q06091 UniProtKB Chain 1 175 . . . ID=PRO_0000071999;Note=Pre-mRNA-splicing factor SNT309 +Q06091 UniProtKB Turn 5 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q06091 UniProtKB Helix 14 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q06091 UniProtKB Helix 53 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q06091 UniProtKB Beta strand 74 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q06091 UniProtKB Helix 83 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q06091 UniProtKB Helix 104 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q06091 UniProtKB Helix 112 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P56508 1 79 +P56508 UniProtKB Chain 1 79 . . . ID=PRO_0000193989;Note=Protein SNA2 +P56508 UniProtKB Topological domain 1 6 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P56508 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P56508 UniProtKB Topological domain 28 32 . . . Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P56508 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P56508 UniProtKB Topological domain 54 79 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P56508 UniProtKB Modified residue 71 71 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P56508 UniProtKB Modified residue 77 77 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q03144 1 224 +Q03144 UniProtKB Chain 1 224 . . . ID=PRO_0000135619;Note=Pyridoxal 5'-phosphate synthase subunit SNO1 +Q03144 UniProtKB Region 67 69 . . . Note=L-glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528 +Q03144 UniProtKB Region 160 161 . . . Note=L-glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528 +Q03144 UniProtKB Active site 100 100 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528 +Q03144 UniProtKB Active site 203 203 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528 +Q03144 UniProtKB Active site 205 205 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528 +Q03144 UniProtKB Binding site 129 129 . . . Note=L-glutamine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528 +##sequence-region Q04902 1 237 +Q04902 UniProtKB Chain 1 237 . . . ID=PRO_0000157853;Note=Probable glutathione-independent glyoxalase SNO4 +Q04902 UniProtKB Active site 138 138 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04432 +Q04902 UniProtKB Active site 139 139 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04432 +Q04902 UniProtKB Active site 170 170 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q04432 +##sequence-region Q12368 1 194 +Q12368 UniProtKB Chain 1 194 . . . ID=PRO_0000232633;Note=23 kDa U4/U6.U5 small nuclear ribonucleoprotein component +Q12368 UniProtKB Zinc finger 80 104 . . . Note=C2H2-type +##sequence-region P00447 1 233 +P00447 UniProtKB Transit peptide 1 26 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6 +P00447 UniProtKB Chain 27 233 . . . ID=PRO_0000032888;Note=Superoxide dismutase [Mn]%2C mitochondrial +P00447 UniProtKB Metal binding 52 52 . . . Note=Manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00447 UniProtKB Metal binding 107 107 . . . Note=Manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00447 UniProtKB Metal binding 194 194 . . . Note=Manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00447 UniProtKB Metal binding 198 198 . . . Note=Manganese;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00447 UniProtKB Modified residue 147 147 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P00447 UniProtKB Modified residue 149 149 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17761666;Dbxref=PMID:17761666 +P00447 UniProtKB Helix 37 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E +P00447 UniProtKB Turn 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E +P00447 UniProtKB Helix 46 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E +P00447 UniProtKB Helix 56 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E +P00447 UniProtKB Helix 84 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E +P00447 UniProtKB Helix 117 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E +P00447 UniProtKB Turn 120 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E +P00447 UniProtKB Helix 127 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E +P00447 UniProtKB Helix 140 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E +P00447 UniProtKB Beta strand 156 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E +P00447 UniProtKB Helix 166 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E +P00447 UniProtKB Beta strand 172 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E +P00447 UniProtKB Beta strand 187 194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E +P00447 UniProtKB Helix 197 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E +P00447 UniProtKB Helix 201 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E +P00447 UniProtKB Helix 208 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E +P00447 UniProtKB Helix 216 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E +P00447 UniProtKB Helix 221 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F6E +##sequence-region P53315 1 255 +P53315 UniProtKB Chain 1 255 . . . ID=PRO_0000090085;Note=6-phosphogluconolactonase 4 +##sequence-region P23201 1 1466 +P23201 UniProtKB Chain 1 1466 . . . ID=PRO_0000072090;Note=Protein SPA2 +P23201 UniProtKB Repeat 818 825 . . . Note=1 +P23201 UniProtKB Repeat 826 834 . . . Note=2 +P23201 UniProtKB Repeat 835 843 . . . Note=3 +P23201 UniProtKB Repeat 860 868 . . . Note=4 +P23201 UniProtKB Repeat 875 883 . . . Note=5 +P23201 UniProtKB Repeat 884 892 . . . Note=6 +P23201 UniProtKB Repeat 893 901 . . . Note=7 +P23201 UniProtKB Repeat 902 910 . . . Note=8 +P23201 UniProtKB Repeat 911 919 . . . Note=9 +P23201 UniProtKB Repeat 920 928 . . . Note=10 +P23201 UniProtKB Repeat 929 937 . . . Note=11 +P23201 UniProtKB Repeat 938 946 . . . Note=12 +P23201 UniProtKB Repeat 947 953 . . . Note=13 +P23201 UniProtKB Repeat 954 961 . . . Note=14 +P23201 UniProtKB Repeat 962 970 . . . Note=15 +P23201 UniProtKB Repeat 971 979 . . . Note=16 +P23201 UniProtKB Repeat 980 988 . . . Note=17 +P23201 UniProtKB Repeat 989 997 . . . Note=18 +P23201 UniProtKB Repeat 998 1006 . . . Note=19 +P23201 UniProtKB Repeat 1007 1015 . . . Note=20 +P23201 UniProtKB Repeat 1036 1044 . . . Note=21 +P23201 UniProtKB Repeat 1045 1053 . . . Note=22 +P23201 UniProtKB Repeat 1054 1062 . . . Note=23 +P23201 UniProtKB Repeat 1072 1080 . . . Note=24 +P23201 UniProtKB Repeat 1081 1087 . . . Note=25 +P23201 UniProtKB Region 818 1087 . . . Note=25 X 9 AA approximate tandem repeats +P23201 UniProtKB Coiled coil 286 388 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23201 UniProtKB Coiled coil 1169 1189 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23201 UniProtKB Coiled coil 1275 1302 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23201 UniProtKB Modified residue 182 182 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P23201 UniProtKB Modified residue 183 183 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P23201 UniProtKB Modified residue 220 220 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P23201 UniProtKB Modified residue 254 254 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P23201 UniProtKB Modified residue 274 274 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P23201 UniProtKB Modified residue 301 301 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P23201 UniProtKB Modified residue 585 585 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P23201 UniProtKB Modified residue 599 599 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P23201 UniProtKB Modified residue 646 646 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P23201 UniProtKB Modified residue 817 817 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P23201 UniProtKB Modified residue 820 820 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P23201 UniProtKB Modified residue 865 865 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P23201 UniProtKB Modified residue 883 883 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P23201 UniProtKB Modified residue 910 910 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P23201 UniProtKB Modified residue 937 937 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950 +P23201 UniProtKB Modified residue 961 961 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198 +P23201 UniProtKB Modified residue 979 979 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P23201 UniProtKB Modified residue 1053 1053 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P23201 UniProtKB Modified residue 1056 1056 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P23201 UniProtKB Modified residue 1080 1080 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P23201 UniProtKB Modified residue 1173 1173 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P23201 UniProtKB Modified residue 1179 1179 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P23201 UniProtKB Modified residue 1180 1180 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P23201 UniProtKB Modified residue 1251 1251 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P23201 UniProtKB Modified residue 1263 1263 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region Q04969 1 178 +Q04969 UniProtKB Chain 1 178 . . . ID=PRO_0000203253;Note=Signal peptidase complex subunit SPC2 +Q04969 UniProtKB Topological domain 1 37 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04969 UniProtKB Transmembrane 38 58 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04969 UniProtKB Topological domain 59 67 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04969 UniProtKB Transmembrane 68 88 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04969 UniProtKB Topological domain 89 178 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36131 1 295 +P36131 UniProtKB Chain 1 295 . . . ID=PRO_0000211554;Note=DASH complex subunit SPC34 +P36131 UniProtKB Coiled coil 223 295 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36131 UniProtKB Modified residue 199 199 . . . Note=Phosphothreonine%3B by IPL1;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000269|PubMed:12408861;Dbxref=PMID:17330950,PMID:12408861 +##sequence-region Q08204 1 1093 +Q08204 UniProtKB Chain 1 1093 . . . ID=PRO_0000119020;Note=Structural maintenance of chromosomes protein 5 +Q08204 UniProtKB Nucleotide binding 69 76 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08204 UniProtKB Region 442 650 . . . Note=Flexible hinge +Q08204 UniProtKB Coiled coil 208 354 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08204 UniProtKB Coiled coil 404 441 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08204 UniProtKB Coiled coil 651 757 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08204 UniProtKB Coiled coil 884 926 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08204 UniProtKB Compositional bias 986 1021 . . . Note=Ala/Asp-rich (DA-box) +Q08204 UniProtKB Helix 307 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +Q08204 UniProtKB Turn 740 742 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +Q08204 UniProtKB Helix 743 808 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3HTK +##sequence-region Q12749 1 1114 +Q12749 UniProtKB Chain 1 1114 . . . ID=PRO_0000119022;Note=Structural maintenance of chromosomes protein 6 +Q12749 UniProtKB Nucleotide binding 109 116 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12749 UniProtKB Region 530 695 . . . Note=Flexible hinge +Q12749 UniProtKB Coiled coil 259 529 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12749 UniProtKB Coiled coil 696 969 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12749 UniProtKB Motif 35 39 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12749 UniProtKB Compositional bias 1019 1054 . . . Note=Ala/Asp-rich (DA-box) +##sequence-region Q06217 1 110 +Q06217 UniProtKB Chain 1 110 . . . ID=PRO_0000122213;Note=Small nuclear ribonucleoprotein Sm D2 +Q06217 UniProtKB Helix 16 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q06217 UniProtKB Helix 32 40 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q06217 UniProtKB Beta strand 43 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q06217 UniProtKB Beta strand 53 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q06217 UniProtKB Beta strand 67 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q06217 UniProtKB Beta strand 87 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q06217 UniProtKB Turn 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q06217 UniProtKB Beta strand 101 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P47057 1 423 +P47057 UniProtKB Chain 1 423 . . . ID=PRO_0000213818;Note=Sorting nexin-4 +P47057 UniProtKB Domain 29 157 . . . Note=PX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00147 +P47057 UniProtKB Coiled coil 217 252 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47057 UniProtKB Coiled coil 346 381 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47057 UniProtKB Binding site 78 78 . . . Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47057 UniProtKB Binding site 80 80 . . . Note=Phosphatidylinositol 3-phosphate%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47057 UniProtKB Binding site 104 104 . . . Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47057 UniProtKB Binding site 123 123 . . . Note=Phosphatidylinositol 3-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47057 UniProtKB Mutagenesis 79 79 . . . Note=Abolishes the intracellular punctate localization and decreases the cytoplasm to vacuole transport. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12048214;Dbxref=PMID:12048214 +P47057 UniProtKB Sequence conflict 292 304 . . . Note=QLIKLKDQKQIDY->PDQIERPETDRL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38282 1 291 +P38282 UniProtKB Chain 1 291 . . . ID=PRO_0000202498;Note=Pre-mRNA-splicing factor SPP381 +##sequence-region P53540 1 846 +P53540 UniProtKB Chain 1 846 . . . ID=PRO_0000078123;Note=Spindle pole body component SPC98 +P53540 UniProtKB Modified residue 124 124 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53540 UniProtKB Modified residue 136 136 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P50088 1 95 +P50088 UniProtKB Chain 1 95 . . . ID=PRO_0000202853;Note=Stationary phase gene 1 protein +P50088 UniProtKB Transmembrane 20 38 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40092 1 148 +P40092 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40092 UniProtKB Chain 20 127 . . . ID=PRO_0000014317;Note=Uncharacterized cell wall protein SPI1 +P40092 UniProtKB Propeptide 128 148 . . . ID=PRO_0000372448;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40092 UniProtKB Compositional bias 61 124 . . . Note=Thr-rich +P40092 UniProtKB Lipidation 127 127 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40092 UniProtKB Glycosylation 41 41 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40092 UniProtKB Glycosylation 59 59 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53541 1 631 +P53541 UniProtKB Signal peptide 1 17 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53541 UniProtKB Chain 18 631 . . . ID=PRO_0000120569;Note=Putative meiotic phospholipase SPO1 +P53541 UniProtKB Transmembrane 376 396 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53541 UniProtKB Domain 24 631 . . . Note=PLA2c;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00555 +P53541 UniProtKB Region 24 67 . . . Note=Required for lipid-binding and function in meiosis +P53541 UniProtKB Glycosylation 233 233 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53541 UniProtKB Glycosylation 293 293 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53541 UniProtKB Glycosylation 303 303 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53541 UniProtKB Glycosylation 500 500 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53541 UniProtKB Glycosylation 536 536 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53541 UniProtKB Glycosylation 560 560 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53541 UniProtKB Glycosylation 563 563 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53541 UniProtKB Glycosylation 572 572 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53541 UniProtKB Mutagenesis 103 103 . . . Note=In SPO1-1%3B defective in sporulation at 34 degrees Celsius. I->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10855497;Dbxref=PMID:10855497 +P53541 UniProtKB Mutagenesis 122 122 . . . Note=Loss of function. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10855497;Dbxref=PMID:10855497 +##sequence-region P40031 1 143 +P40031 UniProtKB Chain 1 143 . . . ID=PRO_0000072141;Note=Sporulation-specific protein 73 +##sequence-region P32572 1 300 +P32572 UniProtKB Chain 1 300 . . . ID=PRO_0000074227;Note=Sporulation protein SPS18 +P32572 UniProtKB Domain 11 130 . . . Note=Arf-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288 +P32572 UniProtKB Zinc finger 28 51 . . . Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00288 +P32572 UniProtKB Sequence conflict 106 106 . . . Note=R->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32572 UniProtKB Sequence conflict 132 132 . . . Note=R->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32572 UniProtKB Sequence conflict 201 201 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32572 UniProtKB Sequence conflict 230 230 . . . Note=Q->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P35209 1 758 +P35209 UniProtKB Chain 1 758 . . . ID=PRO_0000072162;Note=Protein SPT21 +P35209 UniProtKB Compositional bias 127 144 . . . Note=Asp/Glu-rich (acidic) +P35209 UniProtKB Compositional bias 672 682 . . . Note=Asp/Glu-rich (acidic) +P35209 UniProtKB Modified residue 454 454 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region P42948 1 560 +P42948 UniProtKB Chain 1 560 . . . ID=PRO_0000097697;Note=SET domain-containing protein 4 +P42948 UniProtKB Domain 346 475 . . . Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 +P42948 UniProtKB Zinc finger 160 210 . . . Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 +##sequence-region Q99287 1 776 +Q99287 UniProtKB Chain 1 776 . . . ID=PRO_0000155140;Note=Protein SEY1 +Q99287 UniProtKB Topological domain 1 681 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03109 +Q99287 UniProtKB Transmembrane 682 702 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03109 +Q99287 UniProtKB Topological domain 703 705 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03109 +Q99287 UniProtKB Transmembrane 706 726 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03109 +Q99287 UniProtKB Topological domain 727 776 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03109 +Q99287 UniProtKB Domain 34 263 . . . Note=GB1/RHD3-type G +Q99287 UniProtKB Nucleotide binding 44 51 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03109 +Q99287 UniProtKB Mutagenesis 50 50 . . . Note=Abolishes GTP binding. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19665976;Dbxref=PMID:19665976 +##sequence-region Q06168 1 426 +Q06168 UniProtKB Chain 1 426 . . . ID=PRO_0000205962;Note=Chromatin structure-remodeling complex subunit SFH1 +Q06168 UniProtKB Region 201 242 . . . Note=Interaction with STH1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9154831;Dbxref=PMID:9154831 +Q06168 UniProtKB Modified residue 78 78 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P32432 1 683 +P32432 UniProtKB Chain 1 683 . . . ID=PRO_0000046851;Note=Transcription factor SFP1 +P32432 UniProtKB Zinc finger 598 623 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P32432 UniProtKB Zinc finger 659 683 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P32432 UniProtKB Region 230 458 . . . Note=Prion domain (PrD) +P32432 UniProtKB Compositional bias 532 555 . . . Note=Poly-Asp +##sequence-region P25554 1 259 +P25554 UniProtKB Chain 1 259 . . . ID=PRO_0000202539;Note=SAGA-associated factor 29 +P25554 UniProtKB Domain 121 255 . . . Note=SGF29 C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00851 +P25554 UniProtKB Region 163 165 . . . Note=Histone H3K4me3 N-terminus binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874 +P25554 UniProtKB Region 207 210 . . . Note=Histone H3K4me3 N-terminus binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874 +P25554 UniProtKB Region 229 232 . . . Note=Histone H3K4me3 binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874 +P25554 UniProtKB Binding site 205 205 . . . Note=Histone H3K4me3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874 +P25554 UniProtKB Binding site 212 212 . . . Note=Histone H3K4me3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874 +P25554 UniProtKB Modified residue 139 139 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +P25554 UniProtKB Mutagenesis 163 163 . . . Note=Reduces histone H3 acetylation. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874 +P25554 UniProtKB Mutagenesis 165 165 . . . Note=Reduces histone H3 acetylation. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874 +P25554 UniProtKB Mutagenesis 205 205 . . . Note=Reduces histone H3 acetylation. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874 +P25554 UniProtKB Mutagenesis 210 210 . . . Note=Reduces histone H3 acetylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874 +P25554 UniProtKB Mutagenesis 212 212 . . . Note=Reduces histone H3 acetylation. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874 +P25554 UniProtKB Mutagenesis 229 229 . . . Note=Reduces histone H3 acetylation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21685874;Dbxref=PMID:21685874 +P25554 UniProtKB Beta strand 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6 +P25554 UniProtKB Beta strand 130 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6 +P25554 UniProtKB Turn 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP8 +P25554 UniProtKB Beta strand 144 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6 +P25554 UniProtKB Turn 154 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6 +P25554 UniProtKB Beta strand 158 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6 +P25554 UniProtKB Beta strand 174 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6 +P25554 UniProtKB Helix 180 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6 +P25554 UniProtKB Beta strand 183 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6 +P25554 UniProtKB Beta strand 200 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6 +P25554 UniProtKB Beta strand 209 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6 +P25554 UniProtKB Beta strand 225 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6 +P25554 UniProtKB Beta strand 232 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP8 +P25554 UniProtKB Beta strand 239 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6 +P25554 UniProtKB Helix 243 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6 +P25554 UniProtKB Beta strand 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6 +P25554 UniProtKB Helix 250 253 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MP6 +##sequence-region Q06236 1 168 +Q06236 UniProtKB Transit peptide 1 23 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06236 UniProtKB Chain 24 168 . . . ID=PRO_0000268180;Note=Mitochondrial inner membrane protein SHH4 +Q06236 UniProtKB Topological domain 24 65 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08749 +Q06236 UniProtKB Transmembrane 66 86 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06236 UniProtKB Topological domain 87 92 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08749 +Q06236 UniProtKB Transmembrane 93 113 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06236 UniProtKB Topological domain 114 120 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08749 +Q06236 UniProtKB Transmembrane 121 141 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06236 UniProtKB Topological domain 142 168 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08749 +Q06236 UniProtKB Metal binding 101 101 . . . Note=Iron (heme axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37298 +Q06236 UniProtKB Binding site 112 112 . . . Note=Ubiquinone;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37298 +##sequence-region P38957 1 223 +P38957 UniProtKB Chain 1 223 . . . ID=PRO_0000202593;Note=Suppressor of hydroxyurea sensitivity protein 2 +##sequence-region P22579 1 1536 +P22579 UniProtKB Chain 1 1536 . . . ID=PRO_0000121544;Note=Transcriptional regulatory protein SIN3 +P22579 UniProtKB Domain 217 287 . . . Note=PAH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00810 +P22579 UniProtKB Domain 404 474 . . . Note=PAH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00810 +P22579 UniProtKB Domain 656 727 . . . Note=PAH 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00810 +P22579 UniProtKB Compositional bias 480 519 . . . Note=Gln-rich +P22579 UniProtKB Modified residue 137 137 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P22579 UniProtKB Modified residue 303 303 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P22579 UniProtKB Modified residue 304 304 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P22579 UniProtKB Modified residue 316 316 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P22579 UniProtKB Modified residue 1046 1046 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P22579 UniProtKB Sequence conflict 510 510 . . . Note=Q->QAQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P34164 1 415 +P34164 UniProtKB Initiator methionine 1 1 . . . Note=Removed +P34164 UniProtKB Chain 2 415 . . . ID=PRO_0000204375;Note=SNF1 protein kinase subunit beta-2 +P34164 UniProtKB Region 154 335 . . . Note=Kinase-interacting sequence (KIS)%3B required for interaction with SNF1 +P34164 UniProtKB Region 336 415 . . . Note=Association with SNF1 kinase complex (ASC) domain%3B required for interaction with SNF4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9121458;Dbxref=PMID:9121458 +P34164 UniProtKB Modified residue 66 66 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34164 UniProtKB Modified residue 298 298 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34164 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12562756;Dbxref=PMID:12562756 +P34164 UniProtKB Mutagenesis 2 2 . . . Note=Changes protein distribution from the plasma membrane to the cytoplasm and nucleus and alters the cellular life span. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12562756;Dbxref=PMID:12562756 +P34164 UniProtKB Beta strand 164 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV +P34164 UniProtKB Beta strand 177 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV +P34164 UniProtKB Helix 182 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV +P34164 UniProtKB Beta strand 196 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV +P34164 UniProtKB Beta strand 202 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV +P34164 UniProtKB Beta strand 210 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV +P34164 UniProtKB Beta strand 222 224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV +P34164 UniProtKB Beta strand 231 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV +P34164 UniProtKB Beta strand 240 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QLV +P34164 UniProtKB Beta strand 305 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P34164 UniProtKB Helix 311 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P34164 UniProtKB Helix 316 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P34164 UniProtKB Helix 336 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P34164 UniProtKB Helix 345 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P34164 UniProtKB Helix 349 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P34164 UniProtKB Helix 375 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P34164 UniProtKB Beta strand 380 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TDH +P34164 UniProtKB Beta strand 390 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +P34164 UniProtKB Beta strand 402 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3T4N +##sequence-region P40210 1 489 +P40210 UniProtKB Chain 1 489 . . . ID=PRO_0000203303;Note=Protein SIP5 +P40210 UniProtKB Modified residue 13 13 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40210 UniProtKB Modified residue 183 183 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P40210 UniProtKB Modified residue 433 433 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40210 UniProtKB Modified residue 436 436 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40210 UniProtKB Modified residue 438 438 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P53955 1 656 +P53955 UniProtKB Chain 1 656 . . . ID=PRO_0000203453;Note=Phosphatidylinositol 4%2C5-bisphosphate-binding protein SLM2 +P53955 UniProtKB Domain 445 555 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +P53955 UniProtKB Motif 640 645 . . . Note=PXIXIT-like%2C required for interaction with CNA1 and CNA2%2C and calcineurin-dependent dephosphorylation +P53955 UniProtKB Modified residue 626 626 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53955 UniProtKB Modified residue 649 649 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53955 UniProtKB Modified residue 653 653 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q12098 1 748 +Q12098 UniProtKB Chain 1 748 . . . ID=PRO_0000270574;Note=Structure-specific endonuclease subunit SLX4 +Q12098 UniProtKB Compositional bias 568 573 . . . Note=Poly-Glu +Q12098 UniProtKB Modified residue 72 72 . . . Note=Phosphothreonine%3B by ATR and ATM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17636031;Dbxref=PMID:17636031 +Q12098 UniProtKB Modified residue 113 113 . . . Note=Phosphothreonine%3B by ATR and ATM;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12098 UniProtKB Modified residue 289 289 . . . Note=Phosphoserine%3B by ATR and ATM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17636031;Dbxref=PMID:17636031 +Q12098 UniProtKB Modified residue 319 319 . . . Note=Phosphothreonine%3B by ATR and ATM;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12098 UniProtKB Modified residue 329 329 . . . Note=Phosphoserine%3B by ATR and ATM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17636031;Dbxref=PMID:17636031 +Q12098 UniProtKB Modified residue 355 355 . . . Note=Phosphoserine%3B by ATR and ATM;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P22215 1 453 +P22215 UniProtKB Chain 1 453 . . . ID=PRO_0000206785;Note=Uncharacterized transporter SLY41 +P22215 UniProtKB Topological domain 1 110 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22215 UniProtKB Transmembrane 111 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22215 UniProtKB Topological domain 132 172 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22215 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22215 UniProtKB Topological domain 194 201 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22215 UniProtKB Transmembrane 202 222 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22215 UniProtKB Topological domain 223 234 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22215 UniProtKB Transmembrane 235 255 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22215 UniProtKB Topological domain 256 269 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22215 UniProtKB Transmembrane 270 290 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22215 UniProtKB Topological domain 291 332 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22215 UniProtKB Transmembrane 333 353 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22215 UniProtKB Topological domain 354 371 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22215 UniProtKB Transmembrane 372 392 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22215 UniProtKB Topological domain 393 413 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22215 UniProtKB Transmembrane 414 434 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22215 UniProtKB Topological domain 435 453 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P22215 UniProtKB Sequence conflict 34 34 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P22215 UniProtKB Sequence conflict 339 339 . . . Note=C->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40167 1 298 +P40167 UniProtKB Chain 1 298 . . . ID=PRO_0000203397;Note=Sporulation-specific with a leucine zipper motif protein 1 +##sequence-region P40548 1 159 +P40548 UniProtKB Chain 1 159 . . . ID=PRO_0000088881;Note=HSP70 co-chaperone SNL1 +P40548 UniProtKB Topological domain 1 12 . . . Note=Perinuclear space +P40548 UniProtKB Transmembrane 13 35 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40548 UniProtKB Topological domain 36 159 . . . Note=Cytoplasmic +P40548 UniProtKB Domain 73 159 . . . Note=BAG;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00369 +P40548 UniProtKB Compositional bias 42 63 . . . Note=Lys-rich +P40548 UniProtKB Mutagenesis 112 112 . . . Note=Strongly reduces interaction with HSP70 family members. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12105220;Dbxref=PMID:12105220 +P40548 UniProtKB Mutagenesis 141 141 . . . Note=Strongly reduces interaction with HSP70 family members. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12105220;Dbxref=PMID:12105220 +##sequence-region Q12034 1 447 +Q12034 UniProtKB Chain 1 447 . . . ID=PRO_0000207614;Note=Protein SLF1 +Q12034 UniProtKB Domain 265 368 . . . Note=HTH La-type RNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00332 +Q12034 UniProtKB Sequence conflict 118 118 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P54867 1 378 +P54867 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54867 UniProtKB Chain 22 378 . . . ID=PRO_0000041483;Note=Protein SLG1 +P54867 UniProtKB Topological domain 22 264 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54867 UniProtKB Transmembrane 265 285 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54867 UniProtKB Topological domain 286 378 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54867 UniProtKB Domain 22 110 . . . Note=WSC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00558 +P54867 UniProtKB Compositional bias 125 255 . . . Note=Thr-rich +P54867 UniProtKB Modified residue 331 331 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P54867 UniProtKB Modified residue 353 353 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198 +P54867 UniProtKB Glycosylation 65 65 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54867 UniProtKB Mutagenesis 303 303 . . . Note=Sensitive to alkali. Fails to restore normal levels of SLT2 phosphorylation upon alkaline stress. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17088254;Dbxref=PMID:17088254 +P54867 UniProtKB Mutagenesis 319 319 . . . Note=No phosphorylation%3B when associated with A-320. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15470108;Dbxref=PMID:15470108 +P54867 UniProtKB Mutagenesis 320 320 . . . Note=No phosphorylation%3B when associated with A-319. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15470108;Dbxref=PMID:15470108 +P54867 UniProtKB Mutagenesis 322 322 . . . Note=No phosphorylation%3B when associated with A-323. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15470108;Dbxref=PMID:15470108 +P54867 UniProtKB Mutagenesis 323 323 . . . Note=No phosphorylation%3B when associated with A-322. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15470108;Dbxref=PMID:15470108 +##sequence-region P40485 1 686 +P40485 UniProtKB Chain 1 686 . . . ID=PRO_0000202965;Note=Phosphatidylinositol 4%2C5-bisphosphate-binding protein SLM1 +P40485 UniProtKB Domain 468 581 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 +P40485 UniProtKB Coiled coil 296 381 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40485 UniProtKB Motif 673 678 . . . Note=PXIXIT-like%2C required for interaction with CNA1 and CNA2%2C and calcineurin-dependent dephosphorylation +P40485 UniProtKB Compositional bias 45 63 . . . Note=Poly-Gln +P40485 UniProtKB Compositional bias 133 136 . . . Note=Poly-Asn +P40485 UniProtKB Compositional bias 166 172 . . . Note=Poly-Gln +P40485 UniProtKB Modified residue 145 145 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40485 UniProtKB Modified residue 150 150 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40485 UniProtKB Modified residue 153 153 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40485 UniProtKB Mutagenesis 477 478 . . . Note=In SLM1-PHM2%3B reduces phosphoinositide binding by 95%25%3B when associated with A-487. RR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15689497;Dbxref=PMID:15689497 +P40485 UniProtKB Mutagenesis 483 483 . . . Note=In SLM1-PHM1%3B reduces phosphoinositide binding by 80%25 and causes mislocalization to the cytoplasm%3B when associated with A-487. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15372071,ECO:0000269|PubMed:15689497;Dbxref=PMID:15372071,PMID:15689497 +P40485 UniProtKB Mutagenesis 487 487 . . . Note=In SLM1-PHM1%3B reduces phosphoinositide binding by 80%25 and causes mislocalization to the cytoplasm%3B when associated with A-483. In SLM1-PHM2%3B reduces phosphoinositide binding by 95%25%3B when associated with 477-AA-478. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15372071,ECO:0000269|PubMed:15689497;Dbxref=PMID:15372071,PMID:15689497 +P40485 UniProtKB Beta strand 470 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H +P40485 UniProtKB Turn 480 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H +P40485 UniProtKB Beta strand 484 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H +P40485 UniProtKB Beta strand 494 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H +P40485 UniProtKB Turn 505 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H +P40485 UniProtKB Beta strand 512 516 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H +P40485 UniProtKB Helix 517 519 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H +P40485 UniProtKB Beta strand 520 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H +P40485 UniProtKB Beta strand 530 533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3NSU +P40485 UniProtKB Beta strand 542 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H +P40485 UniProtKB Beta strand 558 562 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H +P40485 UniProtKB Helix 566 579 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4A6H +##sequence-region P39928 1 1220 +P39928 UniProtKB Chain 1 1220 . . . ID=PRO_0000081405;Note=Osmosensing histidine protein kinase SLN1 +P39928 UniProtKB Topological domain 1 22 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39928 UniProtKB Transmembrane 23 46 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39928 UniProtKB Topological domain 47 333 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39928 UniProtKB Transmembrane 334 354 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39928 UniProtKB Topological domain 355 1220 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39928 UniProtKB Domain 573 928 . . . Note=Histidine kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00107 +P39928 UniProtKB Domain 1089 1210 . . . Note=Response regulatory;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00169 +P39928 UniProtKB Metal binding 1094 1094 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39928 UniProtKB Metal binding 1095 1095 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39928 UniProtKB Metal binding 1144 1144 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39928 UniProtKB Metal binding 1195 1195 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P39928 UniProtKB Modified residue 502 502 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39928 UniProtKB Modified residue 576 576 . . . Note=Phosphohistidine%3B by autocatalysis;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00107,ECO:0000269|PubMed:8808622;Dbxref=PMID:8808622 +P39928 UniProtKB Modified residue 758 758 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39928 UniProtKB Modified residue 833 833 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P39928 UniProtKB Modified residue 1041 1041 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39928 UniProtKB Modified residue 1044 1044 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P39928 UniProtKB Modified residue 1144 1144 . . . Note=4-aspartylphosphate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00169,ECO:0000269|PubMed:8808622;Dbxref=PMID:8808622 +P39928 UniProtKB Glycosylation 100 100 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39928 UniProtKB Glycosylation 138 138 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39928 UniProtKB Glycosylation 142 142 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39928 UniProtKB Glycosylation 181 181 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39928 UniProtKB Glycosylation 224 224 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39928 UniProtKB Glycosylation 272 272 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39928 UniProtKB Mutagenesis 576 576 . . . Note=Inactive. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8183345;Dbxref=PMID:8183345 +P39928 UniProtKB Mutagenesis 891 891 . . . Note=In SLN1-1%3B slow growth. G->D +P39928 UniProtKB Mutagenesis 1144 1144 . . . Note=Inactive. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8183345;Dbxref=PMID:8183345 +P39928 UniProtKB Beta strand 1090 1093 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +P39928 UniProtKB Helix 1097 1109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +P39928 UniProtKB Beta strand 1115 1120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +P39928 UniProtKB Helix 1121 1134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +P39928 UniProtKB Beta strand 1139 1143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +P39928 UniProtKB Beta strand 1148 1150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +P39928 UniProtKB Helix 1152 1162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +P39928 UniProtKB Beta strand 1169 1174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +P39928 UniProtKB Helix 1178 1186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +P39928 UniProtKB Beta strand 1190 1196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +P39928 UniProtKB Helix 1199 1209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2R25 +##sequence-region P42900 1 643 +P42900 UniProtKB Sequence conflict 103 103 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38241 1 364 +P38241 UniProtKB Chain 1 364 . . . ID=PRO_0000212432;Note=Pre-mRNA-splicing factor SLT11 +P38241 UniProtKB Turn 4 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P38241 UniProtKB Beta strand 24 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P38241 UniProtKB Beta strand 35 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P38241 UniProtKB Beta strand 48 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P38241 UniProtKB Helix 63 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P38241 UniProtKB Turn 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P38241 UniProtKB Turn 78 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P38241 UniProtKB Helix 84 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P38241 UniProtKB Beta strand 94 97 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P38241 UniProtKB Helix 108 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P38241 UniProtKB Helix 121 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P38241 UniProtKB Beta strand 204 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P38241 UniProtKB Beta strand 212 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P38241 UniProtKB Helix 216 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P38241 UniProtKB Beta strand 240 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P38241 UniProtKB Turn 244 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P38241 UniProtKB Beta strand 248 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P38241 UniProtKB Helix 256 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P38324 1 304 +P38324 UniProtKB Chain 1 304 . . . ID=PRO_0000202517;Note=Structure-specific endonuclease subunit SLX1 +P38324 UniProtKB Domain 12 95 . . . Note=GIY-YIG;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03100 +P38324 UniProtKB Zinc finger 218 282 . . . Note=SLX1-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03100 +##sequence-region Q12267 1 1418 +Q12267 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12267 UniProtKB Chain 2 1418 . . . ID=PRO_0000119018;Note=Structural maintenance of chromosomes protein 4 +Q12267 UniProtKB Nucleotide binding 185 192 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12267 UniProtKB Region 674 848 . . . Note=Flexible hinge +Q12267 UniProtKB Coiled coil 345 673 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12267 UniProtKB Coiled coil 849 1172 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12267 UniProtKB Coiled coil 1224 1263 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12267 UniProtKB Compositional bias 1323 1358 . . . Note=Ala/Asp-rich (DA-box) +Q12267 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q12267 UniProtKB Modified residue 43 43 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12267 UniProtKB Modified residue 113 113 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12267 UniProtKB Helix 562 681 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Beta strand 688 691 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Helix 692 694 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Beta strand 695 698 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Helix 700 702 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Helix 703 709 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Helix 711 714 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Beta strand 715 719 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Helix 721 734 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Beta strand 738 744 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Helix 758 760 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Turn 764 767 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Beta strand 768 772 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Helix 773 775 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Helix 778 782 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Beta strand 784 787 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Helix 794 797 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Beta strand 800 803 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Beta strand 806 808 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Beta strand 821 823 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Beta strand 832 834 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Helix 850 883 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Helix 886 910 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Turn 911 913 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Helix 914 925 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +Q12267 UniProtKB Helix 929 947 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +##sequence-region P41808 1 388 +P41808 UniProtKB Chain 1 388 . . . ID=PRO_0000186339;Note=Sporulation-specific mitogen-activated protein kinase SMK1 +P41808 UniProtKB Domain 38 337 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P41808 UniProtKB Nucleotide binding 44 52 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P41808 UniProtKB Motif 207 209 . . . Note=TXY +P41808 UniProtKB Compositional bias 384 387 . . . Note=Poly-Ser +P41808 UniProtKB Active site 166 166 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P41808 UniProtKB Binding site 69 69 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +##sequence-region P18480 1 905 +P18480 UniProtKB Chain 1 905 . . . ID=PRO_0000205955;Note=SWI/SNF chromatin-remodeling complex subunit SNF5 +P18480 UniProtKB Compositional bias 31 270 . . . Note=Gln-rich +P18480 UniProtKB Compositional bias 72 132 . . . Note=Pro-rich +P18480 UniProtKB Compositional bias 272 324 . . . Note=Pro-rich +P18480 UniProtKB Compositional bias 489 588 . . . Note=Asp/Glu-rich (acidic) +P18480 UniProtKB Compositional bias 714 882 . . . Note=Pro-rich +P18480 UniProtKB Compositional bias 755 798 . . . Note=Arg/Lys-rich (basic) +P18480 UniProtKB Modified residue 818 818 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P18480 UniProtKB Sequence conflict 564 564 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P18480 UniProtKB Sequence conflict 564 564 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12483 1 233 +Q12483 UniProtKB Chain 1 233 . . . ID=PRO_0000215214;Note=Vacuolar-sorting protein SNF8 +Q12483 UniProtKB Coiled coil 23 46 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P43544 1 222 +P43544 UniProtKB Chain 1 222 . . . ID=PRO_0000135621;Note=Probable pyridoxal 5'-phosphate synthase subunit SNO3 +P43544 UniProtKB Region 58 60 . . . Note=L-glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528 +P43544 UniProtKB Region 151 152 . . . Note=L-glutamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528 +P43544 UniProtKB Active site 91 91 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528 +P43544 UniProtKB Active site 197 197 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528 +P43544 UniProtKB Active site 199 199 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528 +P43544 UniProtKB Binding site 120 120 . . . Note=L-glutamine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P37528 +##sequence-region P32568 1 1501 +P32568 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32568 UniProtKB Chain 2 1501 . . . ID=PRO_0000093441;Note=Protein SNQ2 +P32568 UniProtKB Transmembrane 521 541 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32568 UniProtKB Transmembrane 554 574 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32568 UniProtKB Transmembrane 600 620 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32568 UniProtKB Transmembrane 628 648 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32568 UniProtKB Transmembrane 664 680 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32568 UniProtKB Transmembrane 771 789 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32568 UniProtKB Transmembrane 1190 1212 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32568 UniProtKB Transmembrane 1216 1236 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32568 UniProtKB Transmembrane 1277 1296 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32568 UniProtKB Transmembrane 1333 1352 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32568 UniProtKB Transmembrane 1455 1475 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32568 UniProtKB Domain 161 410 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P32568 UniProtKB Domain 853 1095 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P32568 UniProtKB Nucleotide binding 889 896 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P32568 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32568 UniProtKB Modified residue 26 26 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P32568 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32568 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P32568 UniProtKB Modified residue 80 80 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P32568 UniProtKB Modified residue 86 86 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P32568 UniProtKB Modified residue 1153 1153 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32568 UniProtKB Glycosylation 273 273 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32568 UniProtKB Glycosylation 334 334 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32568 UniProtKB Glycosylation 518 518 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32568 UniProtKB Glycosylation 730 730 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32568 UniProtKB Glycosylation 874 874 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32568 UniProtKB Glycosylation 1401 1401 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32568 UniProtKB Sequence conflict 78 78 . . . Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53207 1 620 +P53207 UniProtKB Chain 1 620 . . . ID=PRO_0000202781;Note=U1 small nuclear ribonucleoprotein component SNU71 +P53207 UniProtKB Coiled coil 296 385 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53207 UniProtKB Modified residue 512 512 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P53207 UniProtKB Modified residue 514 514 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region P53824 1 298 +P53824 UniProtKB Chain 1 298 . . . ID=PRO_0000109359;Note=Probable pyridoxal 5'-phosphate synthase subunit SNZ2 +P53824 UniProtKB Region 234 235 . . . Note=D-ribose 5-phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080 +P53824 UniProtKB Active site 78 78 . . . Note=Schiff-base intermediate with D-ribose 5-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080 +P53824 UniProtKB Binding site 21 21 . . . Note=D-ribose 5-phosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080 +P53824 UniProtKB Binding site 150 150 . . . Note=D-ribose 5-phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080 +P53824 UniProtKB Binding site 213 213 . . . Note=D-ribose 5-phosphate%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O59080 +##sequence-region Q04748 1 898 +Q04748 UniProtKB Transit peptide 1 31 . . . Note=Mitochondrion;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q04748 UniProtKB Chain 32 898 . . . ID=PRO_0000203280;Note=Protein SOV1%2C mitochondrial +##sequence-region Q12133 1 184 +Q12133 UniProtKB Chain 1 184 . . . ID=PRO_0000218951;Note=Signal peptidase complex subunit SPC3 +Q12133 UniProtKB Topological domain 1 14 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12133 UniProtKB Transmembrane 15 35 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12133 UniProtKB Topological domain 36 184 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12133 UniProtKB Glycosylation 102 102 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12133 UniProtKB Glycosylation 173 173 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P36094 1 363 +P36094 UniProtKB Chain 1 363 . . . ID=PRO_0000072109;Note=Spindle pole body component SPC42 +P36094 UniProtKB Coiled coil 60 137 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36094 UniProtKB Coiled coil 249 298 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36094 UniProtKB Modified residue 213 213 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P36094 UniProtKB Modified residue 217 217 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P36094 UniProtKB Modified residue 284 284 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36094 UniProtKB Modified residue 329 329 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36094 UniProtKB Helix 68 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2Q6Q +##sequence-region Q12074 1 293 +Q12074 UniProtKB Chain 1 293 . . . ID=PRO_0000156462;Note=Spermidine synthase +Q12074 UniProtKB Domain 12 248 . . . Note=PABS +Q12074 UniProtKB Region 150 151 . . . Note=S-adenosylmethioninamine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12074 UniProtKB Region 168 171 . . . Note=Putrescine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12074 UniProtKB Active site 168 168 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12074 UniProtKB Binding site 44 44 . . . Note=S-adenosylmethioninamine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12074 UniProtKB Binding site 74 74 . . . Note=Putrescine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12074 UniProtKB Binding site 75 75 . . . Note=S-adenosylmethioninamine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12074 UniProtKB Binding site 99 99 . . . Note=S-adenosylmethioninamine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12074 UniProtKB Binding site 119 119 . . . Note=S-adenosylmethioninamine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12074 UniProtKB Binding site 168 168 . . . Note=S-adenosylmethioninamine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12074 UniProtKB Binding site 236 236 . . . Note=Putrescine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q04438 1 115 +Q04438 UniProtKB Chain 1 115 . . . ID=PRO_0000203290;Note=Stationary phase protein 4 +##sequence-region P17123 1 173 +P17123 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P17123 UniProtKB Chain 2 173 . . . ID=PRO_0000072133;Note=Sporulation-specific protein 12 +P17123 UniProtKB Region 159 173 . . . Note=Negative-charged tail +P17123 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P17123 UniProtKB Modified residue 118 118 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P17123 UniProtKB Modified residue 125 125 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q04359 1 397 +Q04359 UniProtKB Chain 1 397 . . . ID=PRO_0000213614;Note=Sporulation-specific protein 20 +Q04359 UniProtKB Domain 330 392 . . . Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202 +Q04359 UniProtKB Region 4 50 . . . Note=Inhibitory region +Q04359 UniProtKB Region 51 95 . . . Note=Positive regulatory region +Q04359 UniProtKB Mutagenesis 66 66 . . . Note=Strong decrease of the sporulation rate and loss of lipid binding%3B when associated with E-68%3B E-71 and E-73. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14742704;Dbxref=PMID:14742704 +Q04359 UniProtKB Mutagenesis 67 67 . . . Note=Strong decrease of the sporulation rate. L->P%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14742704;Dbxref=PMID:14742704 +Q04359 UniProtKB Mutagenesis 68 68 . . . Note=Strong decrease of the sporulation rate and loss of lipid binding%3B when associated with E-66%3B E-71 and E-73. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14742704;Dbxref=PMID:14742704 +Q04359 UniProtKB Mutagenesis 70 70 . . . Note=Strong decrease of the sporulation rate. L->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14742704;Dbxref=PMID:14742704 +Q04359 UniProtKB Mutagenesis 71 71 . . . Note=Strong decrease of the sporulation rate and loss of lipid binding%3B when associated with E-66%3B E-68 and E-73. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14742704;Dbxref=PMID:14742704 +Q04359 UniProtKB Mutagenesis 73 73 . . . Note=Strong decrease of the sporulation rate and loss of lipid binding%3B when associated with E-66%3B E-68 and E-71. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14742704;Dbxref=PMID:14742704 +Q04359 UniProtKB Sequence conflict 59 59 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02521 1 185 +Q02521 UniProtKB Chain 1 185 . . . ID=PRO_0000218529;Note=Pre-mRNA-splicing factor SPP2 +Q02521 UniProtKB Domain 100 149 . . . Note=G-patch +Q02521 UniProtKB Mutagenesis 109 109 . . . Note=Loss of the interaction with PRP2. L->E%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15542821;Dbxref=PMID:15542821 +Q02521 UniProtKB Mutagenesis 109 109 . . . Note=Restores interactions with PRP2 mutants. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15542821;Dbxref=PMID:15542821 +Q02521 UniProtKB Sequence conflict 68 69 . . . Note=KK->GG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q02521 UniProtKB Sequence conflict 143 143 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q02521 UniProtKB Sequence conflict 149 149 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P50875 1 604 +P50875 UniProtKB Chain 1 604 . . . ID=PRO_0000072161;Note=Transcription factor SPT20 +P50875 UniProtKB Compositional bias 157 162 . . . Note=Poly-Gln +P50875 UniProtKB Compositional bias 235 240 . . . Note=Poly-Ser +P50875 UniProtKB Compositional bias 422 425 . . . Note=Poly-Ser +P50875 UniProtKB Compositional bias 454 463 . . . Note=Poly-Ala +P50875 UniProtKB Compositional bias 552 559 . . . Note=Poly-Asn +P50875 UniProtKB Modified residue 446 446 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P50875 UniProtKB Modified residue 516 516 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P50875 UniProtKB Sequence conflict 293 293 . . . Note=Y->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06132 1 899 +Q06132 UniProtKB Chain 1 899 . . . ID=PRO_0000269652;Note=Suppressor of glycerol defect protein 1 +Q06132 UniProtKB Domain 335 540 . . . Note=MIF4G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00698 +Q06132 UniProtKB Domain 644 781 . . . Note=MI;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00698 +Q06132 UniProtKB Modified residue 736 736 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P33335 1 543 +P33335 UniProtKB Chain 1 543 . . . ID=PRO_0000173422;Note=Protein SGE1 +P33335 UniProtKB Topological domain 1 8 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Transmembrane 9 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Topological domain 30 41 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Topological domain 63 79 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Transmembrane 80 100 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Topological domain 101 103 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Transmembrane 104 124 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Topological domain 125 131 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Transmembrane 132 152 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Topological domain 153 162 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Transmembrane 163 183 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Topological domain 184 227 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Transmembrane 228 248 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Topological domain 249 255 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Transmembrane 256 276 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Topological domain 277 300 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Transmembrane 301 321 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Topological domain 322 341 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Transmembrane 342 362 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Topological domain 363 373 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Transmembrane 374 394 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Topological domain 395 399 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Transmembrane 400 420 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Topological domain 421 443 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Transmembrane 444 464 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Topological domain 465 508 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Transmembrane 509 529 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Topological domain 530 543 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33335 UniProtKB Sequence conflict 429 429 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P33335 UniProtKB Sequence conflict 447 486 . . . Note=KSLGFAFGGNMGAMIFTASLKNQMRSSQLNIPQFTSVETL->NPWALRLEGYGGNDIHCITQKPDALFPIKHTTIYVCRNT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P35187 1 1447 +P35187 UniProtKB Chain 1 1447 . . . ID=PRO_0000205057;Note=ATP-dependent helicase SGS1 +P35187 UniProtKB Domain 687 864 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P35187 UniProtKB Domain 886 1035 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P35187 UniProtKB Domain 1272 1351 . . . Note=HRDC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00328 +P35187 UniProtKB Nucleotide binding 714 721 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P35187 UniProtKB Motif 808 811 . . . Note=DEAH box +P35187 UniProtKB Compositional bias 631 639 . . . Note=Asp/Glu-rich (highly acidic) +P35187 UniProtKB Mutagenesis 31 31 . . . Note=In allele sgs1-34%3B temperature-sensitive. Q->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12228808;Dbxref=PMID:12228808 +P35187 UniProtKB Mutagenesis 980 980 . . . Note=In allele sgs1-35%3B temperature-sensitive. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12228808;Dbxref=PMID:12228808 +P35187 UniProtKB Mutagenesis 987 987 . . . Note=In allele sgs1-36%3B temperature-sensitive. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12228808;Dbxref=PMID:12228808 +P35187 UniProtKB Helix 1274 1291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8B +P35187 UniProtKB Beta strand 1292 1295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8B +P35187 UniProtKB Helix 1303 1312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8B +P35187 UniProtKB Helix 1317 1320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8B +P35187 UniProtKB Helix 1321 1323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8B +P35187 UniProtKB Helix 1328 1333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8B +P35187 UniProtKB Helix 1334 1336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8B +P35187 UniProtKB Helix 1338 1347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8B +P35187 UniProtKB Turn 1348 1350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1D8B +##sequence-region Q04487 1 196 +Q04487 UniProtKB Transit peptide 1 53 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04487 UniProtKB Chain 54 196 . . . ID=PRO_0000003639;Note=Mitochondrial inner membrane protein SHH3 +Q04487 UniProtKB Topological domain 54 97 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33421 +Q04487 UniProtKB Transmembrane 98 118 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04487 UniProtKB Topological domain 119 137 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33421 +Q04487 UniProtKB Transmembrane 138 160 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04487 UniProtKB Topological domain 161 174 . . . Note=Mitochondrial matrix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33421 +Q04487 UniProtKB Transmembrane 175 195 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04487 UniProtKB Topological domain 196 196 . . . Note=Mitochondrial intermembrane;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33421 +Q04487 UniProtKB Metal binding 154 154 . . . Note=Iron (heme axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33421 +Q04487 UniProtKB Binding site 91 91 . . . Note=Ubiquinone;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33421 +Q04487 UniProtKB Binding site 95 95 . . . Note=Ubiquinone;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P33421 +##sequence-region P06701 1 978 +P06701 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15454564;Dbxref=PMID:15454564 +P06701 UniProtKB Chain 2 978 . . . ID=PRO_0000097768;Note=Regulatory protein SIR3 +P06701 UniProtKB Domain 48 188 . . . Note=BAH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00370 +P06701 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15454564;Dbxref=PMID:15454564 +P06701 UniProtKB Mutagenesis 2 2 . . . Note=No acetylation%2C reduced silencing activity. A->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15454564;Dbxref=PMID:15454564 +P06701 UniProtKB Mutagenesis 2 2 . . . Note=No acetylation%2C No silencing activity. A->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15454564;Dbxref=PMID:15454564 +P06701 UniProtKB Mutagenesis 2 2 . . . Note=No effect. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15454564;Dbxref=PMID:15454564 +P06701 UniProtKB Mutagenesis 2 2 . . . Note=Reduced silencing activity. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15454564;Dbxref=PMID:15454564 +P06701 UniProtKB Sequence conflict 74 74 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06701 UniProtKB Sequence conflict 331 331 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06701 UniProtKB Sequence conflict 335 335 . . . Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06701 UniProtKB Sequence conflict 405 405 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06701 UniProtKB Sequence conflict 421 421 . . . Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06701 UniProtKB Sequence conflict 429 430 . . . Note=NE->KK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06701 UniProtKB Sequence conflict 497 497 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06701 UniProtKB Sequence conflict 587 587 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06701 UniProtKB Sequence conflict 597 597 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06701 UniProtKB Sequence conflict 669 669 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06701 UniProtKB Sequence conflict 704 704 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06701 UniProtKB Sequence conflict 712 712 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06701 UniProtKB Sequence conflict 726 726 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06701 UniProtKB Sequence conflict 828 828 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06701 UniProtKB Sequence conflict 830 830 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06701 UniProtKB Sequence conflict 925 925 . . . Note=Q->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P06701 UniProtKB Beta strand 2 4 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FVU +P06701 UniProtKB Helix 5 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KUI +P06701 UniProtKB Beta strand 11 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Beta strand 18 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Beta strand 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KUI +P06701 UniProtKB Beta strand 27 30 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TU4 +P06701 UniProtKB Turn 31 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TU4 +P06701 UniProtKB Beta strand 37 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Turn 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KUI +P06701 UniProtKB Beta strand 55 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Turn 61 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Beta strand 65 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Beta strand 79 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TU4 +P06701 UniProtKB Beta strand 84 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Helix 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Helix 98 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Helix 107 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Helix 116 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Beta strand 131 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Helix 143 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Beta strand 146 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Beta strand 151 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Turn 155 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Beta strand 159 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4JJN +P06701 UniProtKB Turn 167 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Beta strand 170 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Turn 179 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KUD +P06701 UniProtKB Beta strand 184 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4KUI +P06701 UniProtKB Helix 189 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Helix 201 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FL7 +P06701 UniProtKB Helix 465 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OWT +P06701 UniProtKB Helix 535 568 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Beta strand 574 578 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Helix 583 598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Turn 599 603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Beta strand 608 614 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Helix 622 632 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Helix 643 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Helix 655 657 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Beta strand 660 666 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Beta strand 669 671 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Helix 675 685 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Beta strand 691 696 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Helix 704 708 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Helix 711 714 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Beta strand 717 721 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Helix 727 741 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Beta strand 745 749 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Beta strand 755 757 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Beta strand 773 776 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Helix 782 796 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Helix 799 820 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Beta strand 831 833 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Helix 837 843 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TE6 +P06701 UniProtKB Helix 851 856 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO +P06701 UniProtKB Helix 860 873 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO +P06701 UniProtKB Beta strand 874 876 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO +P06701 UniProtKB Beta strand 880 882 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO +P06701 UniProtKB Helix 883 896 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO +P06701 UniProtKB Helix 901 910 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO +P06701 UniProtKB Helix 920 923 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO +P06701 UniProtKB Helix 928 937 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO +P06701 UniProtKB Beta strand 940 945 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO +P06701 UniProtKB Beta strand 947 949 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO +P06701 UniProtKB Beta strand 952 956 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO +P06701 UniProtKB Helix 959 968 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO +P06701 UniProtKB Helix 970 972 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3ZCO +##sequence-region P34226 1 696 +P34226 UniProtKB Chain 1 693 . . . ID=PRO_0000071940;Note=Protein SKT5 +P34226 UniProtKB Propeptide 694 696 . . . ID=PRO_0000396725;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P34226 UniProtKB Repeat 271 306 . . . Note=Sel1-like 1 +P34226 UniProtKB Repeat 307 342 . . . Note=Sel1-like 2 +P34226 UniProtKB Repeat 343 382 . . . Note=Sel1-like 3 +P34226 UniProtKB Repeat 386 423 . . . Note=Sel1-like 4 +P34226 UniProtKB Repeat 424 460 . . . Note=Sel1-like 5 +P34226 UniProtKB Repeat 461 498 . . . Note=Sel1-like 6 +P34226 UniProtKB Repeat 499 534 . . . Note=Sel1-like 7 +P34226 UniProtKB Modified residue 148 148 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P34226 UniProtKB Modified residue 561 561 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P34226 UniProtKB Modified residue 563 563 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34226 UniProtKB Modified residue 564 564 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34226 UniProtKB Modified residue 693 693 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P34226 UniProtKB Lipidation 693 693 . . . Note=S-farnesyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P34226 UniProtKB Sequence conflict 350 350 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P34226 UniProtKB Sequence conflict 643 643 . . . Note=Q->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q08457 1 257 +Q08457 UniProtKB Chain 1 257 . . . ID=PRO_0000237650;Note=Mitochondrial morphogenesis protein SLD7 +Q08457 UniProtKB Helix 182 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3X38 +Q08457 UniProtKB Helix 208 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3X38 +Q08457 UniProtKB Helix 224 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3X38 +Q08457 UniProtKB Helix 240 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3X38 +##sequence-region P53304 1 468 +P53304 UniProtKB Chain 1 468 . . . ID=PRO_0000202846;Note=N-acetyltransferase SLI1 +##sequence-region Q08581 1 821 +Q08581 UniProtKB Chain 1 821 . . . ID=PRO_0000270573;Note=Kinetochore protein SLK19 +Q08581 UniProtKB Coiled coil 310 821 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08581 UniProtKB Site 77 78 . . . Note=Cleavage%3B by ESP1 +Q08581 UniProtKB Modified residue 7 7 . . . Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q08581 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q08581 UniProtKB Modified residue 189 189 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q08581 UniProtKB Modified residue 201 201 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q08581 UniProtKB Modified residue 216 216 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q08581 UniProtKB Modified residue 273 273 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q08581 UniProtKB Modified residue 283 283 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q08581 UniProtKB Mutagenesis 77 77 . . . Note=No cleavage by ESP1. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11533655;Dbxref=PMID:11533655 +Q08581 UniProtKB Mutagenesis 78 78 . . . Note=Destabilizes%3B not detectable in anaphase cells%3B spindle becomes thin and fragile. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11533655;Dbxref=PMID:11533655 +##sequence-region Q12232 1 587 +Q12232 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12232 UniProtKB Chain 22 587 . . . ID=PRO_0000237659;Note=Uncharacterized protein SLP1 +Q12232 UniProtKB Topological domain 22 541 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23275891;Dbxref=PMID:23275891 +Q12232 UniProtKB Transmembrane 542 562 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12232 UniProtKB Topological domain 563 587 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:23275891;Dbxref=PMID:23275891 +Q12232 UniProtKB Domain 163 331 . . . Note=SUN;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00802 +Q12232 UniProtKB Glycosylation 25 25 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +Q12232 UniProtKB Glycosylation 378 378 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +Q12232 UniProtKB Glycosylation 381 381 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +Q12232 UniProtKB Glycosylation 408 408 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +Q12232 UniProtKB Glycosylation 448 448 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +Q12232 UniProtKB Glycosylation 486 486 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +##sequence-region P32380 1 944 +P32380 UniProtKB Chain 1 944 . . . ID=PRO_0000057993;Note=Spindle pole body component 110 +P32380 UniProtKB Region 900 927 . . . Note=Calmodulin-binding +P32380 UniProtKB Coiled coil 164 791 . . . . +P32380 UniProtKB Motif 54 59 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32380 UniProtKB Motif 726 731 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32380 UniProtKB Motif 742 747 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32380 UniProtKB Compositional bias 731 944 . . . Note=Arg/Tyr-rich +P32380 UniProtKB Modified residue 18 18 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32380 UniProtKB Modified residue 60 60 . . . Note=Phosphoserine%3B by MPS1;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:11278681;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198,PMID:11278681 +P32380 UniProtKB Modified residue 64 64 . . . Note=Phosphothreonine%3B by MPS1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278681;Dbxref=PMID:11278681 +P32380 UniProtKB Modified residue 68 68 . . . Note=Phosphothreonine%3B by MPS1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278681;Dbxref=PMID:11278681 +P32380 UniProtKB Modified residue 80 80 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32380 UniProtKB Modified residue 529 529 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32380 UniProtKB Mutagenesis 91 91 . . . Note=Leads to a mild increase in the proportion of preanaphase spindles at the expense of elongated spindles. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17213332;Dbxref=PMID:17213332 +P32380 UniProtKB Helix 901 933 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4DS7 +##sequence-region P25582 1 841 +P25582 UniProtKB Chain 1 841 . . . ID=PRO_0000155604;Note=27S pre-rRNA (guanosine(2922)-2'-O)-methyltransferase +P25582 UniProtKB Coiled coil 360 389 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03163 +P25582 UniProtKB Compositional bias 704 841 . . . Note=Lys-rich +P25582 UniProtKB Active site 159 159 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03163 +P25582 UniProtKB Binding site 58 58 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03163 +P25582 UniProtKB Binding site 60 60 . . . Note=S-adenosyl-L-methionine%3B via amide nitrogen;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03163 +P25582 UniProtKB Binding site 78 78 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03163 +P25582 UniProtKB Binding site 94 94 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03163 +P25582 UniProtKB Binding site 119 119 . . . Note=S-adenosyl-L-methionine;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03163 +P25582 UniProtKB Modified residue 455 455 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P25582 UniProtKB Modified residue 464 464 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25582 UniProtKB Modified residue 529 529 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P25582 UniProtKB Mutagenesis 52 52 . . . Note=Abolishes methyltransferase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14636587;Dbxref=PMID:14636587 +##sequence-region P38863 1 823 +P38863 UniProtKB Chain 1 823 . . . ID=PRO_0000078117;Note=Spindle pole body component SPC97 +##sequence-region Q04398 1 127 +Q04398 UniProtKB Chain 1 127 . . . ID=PRO_0000072121;Note=Stationary phase protein 3 +Q04398 UniProtKB Transmembrane 29 49 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04398 UniProtKB Transmembrane 63 83 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04398 UniProtKB Compositional bias 23 87 . . . Note=Phe-rich +Q04398 UniProtKB Glycosylation 86 86 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P33419 1 253 +P33419 UniProtKB Chain 1 253 . . . ID=PRO_0000096846;Note=Spindle pole component 29 +P33419 UniProtKB Modified residue 18 18 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P33419 UniProtKB Modified residue 65 65 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P33419 UniProtKB Modified residue 240 240 . . . Note=Phosphothreonine%3B by MPS1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19269975;Dbxref=PMID:19269975 +P33419 UniProtKB Mutagenesis 240 240 . . . Note=Lead to defects in spindle pole body assembly. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19269975;Dbxref=PMID:19269975 +##sequence-region Q06160 1 661 +Q06160 UniProtKB Chain 1 661 . . . ID=PRO_0000233011;Note=Protein SPH1 +Q06160 UniProtKB Sequence conflict 141 141 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06160 UniProtKB Sequence conflict 281 281 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06160 UniProtKB Sequence conflict 316 316 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06160 UniProtKB Sequence conflict 377 378 . . . Note=AS->TF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06160 UniProtKB Sequence conflict 400 400 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06160 UniProtKB Sequence conflict 431 431 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06160 UniProtKB Sequence conflict 541 541 . . . Note=F->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06160 UniProtKB Sequence conflict 576 576 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06160 UniProtKB Sequence conflict 580 580 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q06160 UniProtKB Sequence conflict 651 651 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P23179 1 398 +P23179 UniProtKB Chain 1 398 . . . ID=PRO_0000145473;Note=Meiosis-specific protein SPO11 +P23179 UniProtKB Active site 135 135 . . . Note=Nucleophile;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9121560;Dbxref=PMID:9121560 +P23179 UniProtKB Metal binding 233 233 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q57815 +P23179 UniProtKB Metal binding 288 288 . . . Note=Magnesium;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q57815 +P23179 UniProtKB Mutagenesis 135 135 . . . Note=Loss of activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9121560;Dbxref=PMID:9121560 +##sequence-region P23624 1 291 +P23624 UniProtKB Chain 1 291 . . . ID=PRO_0000072134;Note=Meiosis-specific protein SPO13 +P23624 UniProtKB Motif 3 6 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03029 1 223 +Q03029 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03029 UniProtKB Chain 21 198 . . . ID=PRO_0000019590;Note=Sporulation-specific protein 19 +Q03029 UniProtKB Propeptide 199 223 . . . ID=PRO_0000372457;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03029 UniProtKB Compositional bias 116 121 . . . Note=Poly-Glu +Q03029 UniProtKB Lipidation 198 198 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40511 1 975 +P40511 UniProtKB Chain 1 975 . . . ID=PRO_0000072137;Note=Sporulation-specific protein 22 +##sequence-region P45819 1 413 +P45819 UniProtKB Chain 1 413 . . . ID=PRO_0000072142;Note=Sporulation-specific protein 74 +P45819 UniProtKB Sequence conflict 328 328 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P18410 1 259 +P18410 UniProtKB Chain 1 259 . . . ID=PRO_0000072145;Note=Sporulation-specific protein SPO7 +P18410 UniProtKB Topological domain 1 72 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18410 UniProtKB Transmembrane 73 93 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18410 UniProtKB Topological domain 94 106 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18410 UniProtKB Transmembrane 107 127 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P18410 UniProtKB Topological domain 128 259 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38904 1 1435 +P38904 UniProtKB Chain 1 1435 . . . ID=PRO_0000072147;Note=Protein SPP41 +P38904 UniProtKB Domain 171 190 . . . Note=UIM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00213 +P38904 UniProtKB Motif 683 699 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38904 UniProtKB Modified residue 1014 1014 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38904 UniProtKB Modified residue 1067 1067 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38904 UniProtKB Cross-link 981 981 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15166219;Dbxref=PMID:15166219 +P38904 UniProtKB Cross-link 1154 1154 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15166219;Dbxref=PMID:15166219 +##sequence-region P32603 1 445 +P32603 UniProtKB Signal peptide 1 21 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32603 UniProtKB Chain 22 445 . . . ID=PRO_0000007898;Note=Sporulation-specific glucan 1%2C3-beta-glucosidase +P32603 UniProtKB Active site 233 233 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32603 UniProtKB Active site 335 335 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32603 UniProtKB Glycosylation 201 201 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P41901 1 512 +P41901 UniProtKB Chain 1 512 . . . ID=PRO_0000173502;Note=Sporulation-regulated protein 3 +P41901 UniProtKB Domain 106 365 . . . Note=Septin-type G +P41901 UniProtKB Nucleotide binding 116 123 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41901 UniProtKB Nucleotide binding 247 255 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41901 UniProtKB Coiled coil 376 406 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41901 UniProtKB Coiled coil 451 496 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41901 UniProtKB Binding site 168 168 . . . Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41901 UniProtKB Binding site 315 315 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P41901 UniProtKB Sequence conflict 26 26 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41901 UniProtKB Sequence conflict 250 250 . . . Note=L->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41901 UniProtKB Sequence conflict 263 263 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41901 UniProtKB Sequence conflict 317 317 . . . Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P41901 UniProtKB Sequence conflict 481 481 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32573 1 292 +P32573 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9268358;Dbxref=PMID:9268358 +P32573 UniProtKB Chain 2 292 . . . ID=PRO_0000054565;Note=Peroxisomal 2%2C4-dienoyl-CoA reductase SPS19 +P32573 UniProtKB Nucleotide binding 29 53 . . . Note=NADP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32573 UniProtKB Motif 290 292 . . . Note=Microbody targeting signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32573 UniProtKB Cross-link 188 188 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P08458 1 490 +P08458 UniProtKB Chain 1 490 . . . ID=PRO_0000086679;Note=Sporulation-specific protein 1 +P08458 UniProtKB Domain 18 272 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P08458 UniProtKB Nucleotide binding 24 32 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P08458 UniProtKB Active site 141 141 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P08458 UniProtKB Binding site 47 47 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P08458 UniProtKB Sequence conflict 454 454 . . . Note=N->NVN;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08458 UniProtKB Sequence conflict 469 469 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32558 1 1035 +P32558 UniProtKB Chain 1 1035 . . . ID=PRO_0000089448;Note=FACT complex subunit SPT16 +P32558 UniProtKB Coiled coil 208 234 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32558 UniProtKB Coiled coil 636 666 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32558 UniProtKB Coiled coil 959 983 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32558 UniProtKB Compositional bias 958 1021 . . . Note=Asp/Glu-rich (acidic) +P32558 UniProtKB Modified residue 526 526 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32558 UniProtKB Modified residue 765 765 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32558 UniProtKB Mutagenesis 565 565 . . . Note=In spt16-4%3B induces a spt phenotype characterized by depletion of many mRNAs%3B when associated with L-570. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11432837;Dbxref=PMID:11432837 +P32558 UniProtKB Mutagenesis 570 570 . . . Note=In spt16-4%3B induces a spt phenotype characterized by depletion of many mRNAs%3B when associated with S-565. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11432837;Dbxref=PMID:11432837 +P32558 UniProtKB Mutagenesis 836 836 . . . Note=In cdc68-1%3B induces a spt phenotype characterized by depletion of many mRNAs. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9832518;Dbxref=PMID:9832518 +P32558 UniProtKB Mutagenesis 848 850 . . . Note=In spt16-7%3B induces a spt phenotype characterized by depletion of many mRNAs. TTD->IIY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11432837;Dbxref=PMID:11432837 +P32558 UniProtKB Mutagenesis 920 920 . . . Note=In spt16-6%3B induces a spt phenotype characterized by depletion of many mRNAs. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11432837;Dbxref=PMID:11432837 +P32558 UniProtKB Helix 8 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Helix 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Beta strand 30 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Helix 47 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Beta strand 61 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Beta strand 71 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Helix 78 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Helix 85 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Beta strand 92 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIP +P32558 UniProtKB Beta strand 99 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Helix 110 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Beta strand 129 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Helix 142 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Beta strand 161 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Helix 166 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Helix 178 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Helix 214 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Helix 224 226 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Helix 228 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Helix 250 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Beta strand 253 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Beta strand 260 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Beta strand 277 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Beta strand 283 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Beta strand 292 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Beta strand 301 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Helix 311 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Helix 338 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Helix 354 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Beta strand 365 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Beta strand 369 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Helix 375 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Beta strand 378 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Beta strand 393 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Turn 406 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIT +P32558 UniProtKB Beta strand 412 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Beta strand 431 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Helix 440 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3BIQ +P32558 UniProtKB Beta strand 679 686 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Beta strand 689 691 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Beta strand 696 700 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Beta strand 702 707 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Helix 712 714 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Beta strand 717 720 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Helix 721 723 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Beta strand 724 730 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Beta strand 735 750 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Beta strand 753 763 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Helix 790 818 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Turn 819 821 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Beta strand 825 827 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Helix 830 832 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Beta strand 834 841 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Beta strand 843 847 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Beta strand 849 854 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Beta strand 856 859 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Beta strand 861 864 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Helix 865 867 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Beta strand 868 874 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Beta strand 881 891 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Beta strand 897 903 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Helix 904 906 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Helix 907 916 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Beta strand 921 923 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +P32558 UniProtKB Helix 931 939 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4IOY +##sequence-region P35210 1 1082 +P35210 UniProtKB Chain 1 1082 . . . ID=PRO_0000067076;Note=Protein SPT23 +P35210 UniProtKB Domain 508 585 . . . Note=IPT/TIG +P35210 UniProtKB Repeat 709 738 . . . Note=ANK 1 +P35210 UniProtKB Repeat 742 771 . . . Note=ANK 2 +P35210 UniProtKB Modified residue 468 468 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P35210 UniProtKB Sequence conflict 715 715 . . . Note=H->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32914 1 102 +P32914 UniProtKB Chain 1 102 . . . ID=PRO_0000210338;Note=Transcription elongation factor SPT4 +P32914 UniProtKB Zinc finger 7 27 . . . Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32914 UniProtKB Mutagenesis 10 10 . . . Note=Loss of function. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8649393;Dbxref=PMID:8649393 +P32914 UniProtKB Beta strand 4 7 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU +P32914 UniProtKB Turn 8 10 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU +P32914 UniProtKB Beta strand 12 15 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU +P32914 UniProtKB Helix 16 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU +P32914 UniProtKB Turn 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU +P32914 UniProtKB Helix 28 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU +P32914 UniProtKB Helix 39 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU +P32914 UniProtKB Beta strand 42 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU +P32914 UniProtKB Beta strand 46 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU +P32914 UniProtKB Turn 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU +P32914 UniProtKB Helix 59 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU +P32914 UniProtKB Beta strand 71 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU +P32914 UniProtKB Helix 84 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2EXU +##sequence-region P53866 1 767 +P53866 UniProtKB Chain 1 767 . . . ID=PRO_0000203388;Note=Protein SQS1 +P53866 UniProtKB Domain 594 656 . . . Note=R3H +P53866 UniProtKB Domain 720 767 . . . Note=G-patch;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00092 +P53866 UniProtKB Modified residue 105 105 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53866 UniProtKB Modified residue 217 217 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53866 UniProtKB Modified residue 255 255 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53866 UniProtKB Modified residue 334 334 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53866 UniProtKB Modified residue 343 343 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53866 UniProtKB Modified residue 345 345 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P25648 1 1427 +P25648 UniProtKB Chain 1 1427 . . . ID=PRO_0000072183;Note=Mediator of RNA polymerase II transcription subunit 12 +##sequence-region P24276 1 1250 +P24276 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P24276 UniProtKB Chain 2 1250 . . . ID=PRO_0000166424;Note=Protein SSD1 +P24276 UniProtKB Compositional bias 60 67 . . . Note=Poly-Gln +P24276 UniProtKB Compositional bias 71 74 . . . Note=Poly-Gln +P24276 UniProtKB Compositional bias 135 141 . . . Note=Poly-Asn +P24276 UniProtKB Compositional bias 214 217 . . . Note=Poly-Pro +P24276 UniProtKB Compositional bias 527 530 . . . Note=Poly-Glu +P24276 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P24276 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P24276 UniProtKB Modified residue 164 164 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P24276 UniProtKB Modified residue 183 183 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P24276 UniProtKB Modified residue 227 227 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P24276 UniProtKB Modified residue 286 286 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P24276 UniProtKB Modified residue 322 322 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P24276 UniProtKB Modified residue 491 491 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P24276 UniProtKB Modified residue 492 492 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P24276 UniProtKB Modified residue 688 688 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P32343 1 579 +P32343 UniProtKB Chain 1 579 . . . ID=PRO_0000203153;Note=Protein SSH4 +P32343 UniProtKB Topological domain 1 44 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32343 UniProtKB Transmembrane 45 65 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32343 UniProtKB Topological domain 66 579 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32343 UniProtKB Domain 166 364 . . . Note=B30.2/SPRY;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00548 +P32343 UniProtKB Compositional bias 490 557 . . . Note=Asn-rich +P32343 UniProtKB Modified residue 358 358 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P32343 UniProtKB Glycosylation 212 212 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32343 UniProtKB Glycosylation 356 356 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32343 UniProtKB Glycosylation 430 430 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32343 UniProtKB Glycosylation 507 507 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32343 UniProtKB Glycosylation 557 557 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32343 UniProtKB Glycosylation 575 575 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32343 UniProtKB Cross-link 367 367 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q02794 1 444 +Q02794 UniProtKB Chain 1 444 . . . ID=PRO_0000072260;Note=Protein STD1 +Q02794 UniProtKB Compositional bias 26 78 . . . Note=Asn-rich +Q02794 UniProtKB Sequence conflict 139 139 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06010 1 1027 +Q06010 UniProtKB Chain 1 1027 . . . ID=PRO_0000074418;Note=A-factor-processing enzyme +Q06010 UniProtKB Active site 121 121 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10096 +Q06010 UniProtKB Metal binding 118 118 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10096 +Q06010 UniProtKB Metal binding 122 122 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10096 +Q06010 UniProtKB Metal binding 199 199 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10096 +##sequence-region P15705 1 589 +P15705 UniProtKB Chain 1 589 . . . ID=PRO_0000106341;Note=Heat shock protein STI1 +P15705 UniProtKB Repeat 5 38 . . . Note=TPR 1 +P15705 UniProtKB Repeat 40 73 . . . Note=TPR 2 +P15705 UniProtKB Repeat 74 107 . . . Note=TPR 3 +P15705 UniProtKB Domain 138 177 . . . Note=STI1 1 +P15705 UniProtKB Repeat 262 295 . . . Note=TPR 4 +P15705 UniProtKB Repeat 297 328 . . . Note=TPR 5 +P15705 UniProtKB Repeat 336 369 . . . Note=TPR 6 +P15705 UniProtKB Repeat 396 429 . . . Note=TPR 7 +P15705 UniProtKB Repeat 430 463 . . . Note=TPR 8 +P15705 UniProtKB Repeat 465 492 . . . Note=TPR 9 +P15705 UniProtKB Domain 537 576 . . . Note=STI1 2 +P15705 UniProtKB Modified residue 227 227 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P15705 UniProtKB Cross-link 99 99 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P15705 UniProtKB Cross-link 168 168 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P15705 UniProtKB Cross-link 384 384 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P15705 UniProtKB Helix 133 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLV +P15705 UniProtKB Beta strand 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLV +P15705 UniProtKB Helix 142 147 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLV +P15705 UniProtKB Helix 152 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLV +P15705 UniProtKB Helix 160 169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLV +P15705 UniProtKB Helix 174 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLV +P15705 UniProtKB Turn 178 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLV +P15705 UniProtKB Helix 182 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLV +P15705 UniProtKB Turn 193 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLV +P15705 UniProtKB Helix 262 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UQ3 +P15705 UniProtKB Helix 278 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UQ3 +P15705 UniProtKB Helix 296 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UQ3 +P15705 UniProtKB Helix 311 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UQ3 +P15705 UniProtKB Helix 332 348 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UQ3 +P15705 UniProtKB Helix 352 365 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UQ3 +P15705 UniProtKB Helix 369 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UQ3 +P15705 UniProtKB Helix 395 408 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UPV +P15705 UniProtKB Helix 412 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UPV +P15705 UniProtKB Helix 430 442 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UPV +P15705 UniProtKB Helix 446 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UPV +P15705 UniProtKB Helix 464 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UPV +P15705 UniProtKB Helix 480 498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UPV +P15705 UniProtKB Turn 499 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UPV +P15705 UniProtKB Helix 503 516 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UPV +P15705 UniProtKB Helix 527 536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLW +P15705 UniProtKB Helix 538 544 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLW +P15705 UniProtKB Helix 548 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLW +P15705 UniProtKB Helix 560 568 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLW +P15705 UniProtKB Helix 570 581 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LLW +##sequence-region P38960 1 494 +P38960 UniProtKB Chain 1 494 . . . ID=PRO_0000072279;Note=Protein STN1 +P38960 UniProtKB DNA binding 62 159 . . . Note=OB +P38960 UniProtKB Region 311 397 . . . Note=Winged helix-turn-helix (wHTH) 1 +P38960 UniProtKB Region 396 494 . . . Note=Winged helix-turn-helix (wHTH) 2 +P38960 UniProtKB Mutagenesis 397 397 . . . Note=Modest telomere elongation phenotype. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20008938;Dbxref=PMID:20008938 +P38960 UniProtKB Mutagenesis 466 466 . . . Note=Elongated telomeres. W->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20008938;Dbxref=PMID:20008938 +P38960 UniProtKB Mutagenesis 466 466 . . . Note=Elongated telomeres and severe growth defects. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20008938;Dbxref=PMID:20008938 +P38960 UniProtKB Helix 315 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY +P38960 UniProtKB Beta strand 326 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY +P38960 UniProtKB Helix 333 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY +P38960 UniProtKB Helix 340 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY +P38960 UniProtKB Helix 365 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY +P38960 UniProtKB Beta strand 385 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY +P38960 UniProtKB Turn 391 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY +P38960 UniProtKB Beta strand 395 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY +P38960 UniProtKB Helix 399 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY +P38960 UniProtKB Beta strand 421 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY +P38960 UniProtKB Helix 427 434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY +P38960 UniProtKB Helix 441 458 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY +P38960 UniProtKB Turn 460 462 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY +P38960 UniProtKB Beta strand 463 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY +P38960 UniProtKB Beta strand 482 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY +P38960 UniProtKB Turn 491 493 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KEY +##sequence-region Q00947 1 519 +Q00947 UniProtKB Zinc finger 160 182 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q00947 UniProtKB Zinc finger 188 223 . . . Note=C2H2-type 2%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q00947 UniProtKB Zinc finger 240 265 . . . Note=C2H2-type 3%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q00947 UniProtKB Region 16 35 . . . Note=I +Q00947 UniProtKB Region 65 97 . . . Note=II +Q00947 UniProtKB Mutagenesis 9 66 . . . Note=In ASI13-1%3B dominant active and constitutively nuclear localized transcription factor. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12502738;Dbxref=PMID:12502738 +Q00947 UniProtKB Mutagenesis 27 32 . . . Note=In STP1-133%3B impairs cytoplasmic retention%2C resulting in a dominant active transcription factor. Activates transcription also in its unprocessed form%3B when associated with A-66. LVSGVI->AASGAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15314160;Dbxref=PMID:15314160 +Q00947 UniProtKB Mutagenesis 65 65 . . . Note=No effect. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15314160;Dbxref=PMID:15314160 +Q00947 UniProtKB Mutagenesis 66 66 . . . Note=In STP1-102%3B prevents proteolytic processing. Activates transcription also in its unprocessed form%3B when associated with 27-AASGAA-32. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15314160;Dbxref=PMID:15314160 +Q00947 UniProtKB Mutagenesis 67 67 . . . Note=No effect. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15314160;Dbxref=PMID:15314160 +##sequence-region P38989 1 1170 +P38989 UniProtKB Chain 1 1170 . . . ID=PRO_0000119013;Note=Structural maintenance of chromosomes protein 2 +P38989 UniProtKB Nucleotide binding 32 39 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38989 UniProtKB Region 470 677 . . . Note=Flexible hinge +P38989 UniProtKB Coiled coil 172 469 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38989 UniProtKB Coiled coil 678 1027 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38989 UniProtKB Compositional bias 1084 1119 . . . Note=Ala/Asp-rich (DA-box) +P38989 UniProtKB Helix 455 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Helix 473 495 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Helix 498 501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Beta strand 523 526 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Helix 527 529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Helix 536 540 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Helix 541 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Helix 549 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Beta strand 555 559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Helix 560 568 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Beta strand 576 580 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Turn 581 583 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Helix 591 600 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Beta strand 604 607 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Helix 608 611 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Helix 616 618 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Helix 619 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Beta strand 629 634 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Helix 635 642 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Beta strand 650 653 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Turn 654 656 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Beta strand 657 660 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Turn 661 663 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Beta strand 664 668 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Helix 676 705 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Turn 706 711 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Helix 714 721 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Turn 722 726 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +P38989 UniProtKB Helix 727 734 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4RSI +##sequence-region P14359 1 133 +P14359 UniProtKB Chain 1 133 . . . ID=PRO_0000193990;Note=Protein SNA3 +P14359 UniProtKB Topological domain 1 16 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14359 UniProtKB Transmembrane 17 37 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14359 UniProtKB Topological domain 38 48 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14359 UniProtKB Transmembrane 49 69 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14359 UniProtKB Topological domain 70 133 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P14359 UniProtKB Cross-link 125 125 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P38839 1 148 +P38839 UniProtKB Chain 1 148 . . . ID=PRO_0000202920;Note=Putative cyclin-dependent kinase inhibitor SPL2 +P38839 UniProtKB Modified residue 59 59 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38839 UniProtKB Modified residue 86 86 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P38839 UniProtKB Sequence conflict 58 58 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P35184 1 431 +P35184 UniProtKB Chain 1 431 . . . ID=PRO_0000051227;Note=Ribosome assembly protein SQT1 +P35184 UniProtKB Repeat 63 102 . . . Note=WD 1 +P35184 UniProtKB Repeat 107 146 . . . Note=WD 2 +P35184 UniProtKB Repeat 149 192 . . . Note=WD 3 +P35184 UniProtKB Repeat 199 243 . . . Note=WD 4 +P35184 UniProtKB Repeat 309 348 . . . Note=WD 5 +P35184 UniProtKB Repeat 350 387 . . . Note=WD 6 +P35184 UniProtKB Beta strand 58 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 68 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 75 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 89 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 101 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 112 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 121 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 131 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Helix 140 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 144 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 157 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 164 166 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 169 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 179 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Turn 186 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 191 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 204 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 220 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 230 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Turn 235 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 240 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Helix 246 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Turn 249 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 256 261 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Helix 264 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Turn 267 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 273 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 281 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Turn 288 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 294 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 305 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AMS +P35184 UniProtKB Helix 309 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 314 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Turn 321 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 325 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 333 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Turn 340 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 345 350 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 355 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 364 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 374 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Turn 379 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 384 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 395 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 413 419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +P35184 UniProtKB Beta strand 424 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4ZOX +##sequence-region Q12516 1 437 +Q12516 UniProtKB Chain 1 437 . . . ID=PRO_0000240873;Note=Regulator of phospholipase D SRF1 +Q12516 UniProtKB Topological domain 1 267 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12516 UniProtKB Transmembrane 268 288 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12516 UniProtKB Topological domain 289 308 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12516 UniProtKB Transmembrane 309 329 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12516 UniProtKB Topological domain 330 348 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12516 UniProtKB Transmembrane 349 369 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12516 UniProtKB Topological domain 370 403 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12516 UniProtKB Transmembrane 404 424 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12516 UniProtKB Topological domain 425 437 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12516 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q12516 UniProtKB Modified residue 167 167 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12516 UniProtKB Glycosylation 297 297 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12516 UniProtKB Glycosylation 385 385 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12020 1 392 +Q12020 UniProtKB Chain 1 392 . . . ID=PRO_0000270577;Note=Protein SRL2 +Q12020 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12020 UniProtKB Modified residue 139 139 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P36167 1 246 +P36167 UniProtKB Chain 1 246 . . . ID=PRO_0000203228;Note=Protein SRL3 +P36167 UniProtKB Modified residue 212 212 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P25567 1 434 +P25567 UniProtKB Chain 1 434 . . . ID=PRO_0000207615;Note=RNA-binding protein SRO9 +P25567 UniProtKB Domain 255 351 . . . Note=HTH La-type RNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00332 +P25567 UniProtKB Compositional bias 168 171 . . . Note=Poly-Gln +P25567 UniProtKB Compositional bias 174 184 . . . Note=His-rich +P25567 UniProtKB Compositional bias 222 226 . . . Note=Poly-Asn +P25567 UniProtKB Modified residue 55 55 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25567 UniProtKB Modified residue 148 148 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25567 UniProtKB Modified residue 422 422 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P25567 UniProtKB Cross-link 156 156 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25567 UniProtKB Cross-link 301 301 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25567 UniProtKB Cross-link 342 342 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P25567 UniProtKB Cross-link 352 352 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P20424 1 541 +P20424 UniProtKB Chain 1 541 . . . ID=PRO_0000101203;Note=Signal recognition particle subunit SRP54 +P20424 UniProtKB Nucleotide binding 116 123 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20424 UniProtKB Nucleotide binding 198 202 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20424 UniProtKB Nucleotide binding 256 259 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P20424 UniProtKB Region 1 303 . . . Note=G-domain +P20424 UniProtKB Region 304 541 . . . Note=M-domain +P20424 UniProtKB Sequence conflict 136 136 . . . Note=R->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36077 1 127 +P36077 UniProtKB Chain 1 127 . . . ID=PRO_0000211435;Note=Sulfiredoxin +P36077 UniProtKB Disulfide bond 84 84 . . . Note=Interchain (with C-48 in TSA1)%3B transient;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14586471;Dbxref=PMID:14586471 +P36077 UniProtKB Mutagenesis 48 48 . . . Note=Minor effect on formation of disulfide bond with TSA1 and reduction of cysteine-sulfinic acid. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14586471;Dbxref=PMID:14586471 +P36077 UniProtKB Mutagenesis 84 84 . . . Note=Abolishes formation of disulfide bond with TSA1 and reduction of cysteine-sulfinic acid. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14586471;Dbxref=PMID:14586471 +P36077 UniProtKB Mutagenesis 106 106 . . . Note=No effect on formation of disulfide bond with TSA1 and reduction of cysteine-sulfinic acid. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14586471;Dbxref=PMID:14586471 +##sequence-region Q08646 1 371 +Q08646 UniProtKB Chain 1 371 . . . ID=PRO_0000072217;Note=Sporulation-specific protein 2 +Q08646 UniProtKB Natural variant 62 62 . . . Note=In strain: SK1. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12073037;Dbxref=PMID:12073037 +Q08646 UniProtKB Natural variant 88 88 . . . Note=In strain: SK1. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12073037;Dbxref=PMID:12073037 +##sequence-region P42845 1 420 +P42845 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P42845 UniProtKB Chain 2 420 . . . ID=PRO_0000072251;Note=Protein STB1 +P42845 UniProtKB Region 2 70 . . . Note=Interaction with SWI6 +P42845 UniProtKB Compositional bias 156 159 . . . Note=Poly-Asn +P42845 UniProtKB Compositional bias 165 169 . . . Note=Poly-Asn +P42845 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P42845 UniProtKB Modified residue 7 7 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P42845 UniProtKB Modified residue 72 72 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P42845 UniProtKB Modified residue 99 99 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +P42845 UniProtKB Modified residue 102 102 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P42845 UniProtKB Modified residue 419 419 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P38699 1 743 +P38699 UniProtKB Chain 1 743 . . . ID=PRO_0000114978;Note=Protein STB5 +P38699 UniProtKB DNA binding 22 49 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +##sequence-region P32584 1 239 +P32584 UniProtKB Chain 1 239 . . . ID=PRO_0000209899;Note=Protein-S-isoprenylcysteine O-methyltransferase +P32584 UniProtKB Topological domain 1 23 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32584 UniProtKB Transmembrane 24 44 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32584 UniProtKB Topological domain 45 47 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32584 UniProtKB Transmembrane 48 68 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32584 UniProtKB Topological domain 69 88 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32584 UniProtKB Transmembrane 89 109 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32584 UniProtKB Topological domain 110 110 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32584 UniProtKB Transmembrane 111 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32584 UniProtKB Topological domain 132 182 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32584 UniProtKB Transmembrane 183 203 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32584 UniProtKB Topological domain 204 239 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03497 1 939 +Q03497 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q03497 UniProtKB Chain 2 939 . . . ID=PRO_0000086686;Note=Serine/threonine-protein kinase STE20 +Q03497 UniProtKB Domain 337 350 . . . Note=CRIB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00057 +Q03497 UniProtKB Domain 620 871 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03497 UniProtKB Nucleotide binding 626 634 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03497 UniProtKB Region 434 499 . . . Note=BEM1-binding +Q03497 UniProtKB Active site 739 739 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q03497 UniProtKB Binding site 649 649 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03497 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q03497 UniProtKB Modified residue 87 87 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03497 UniProtKB Modified residue 165 165 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03497 UniProtKB Modified residue 167 167 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03497 UniProtKB Modified residue 169 169 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:16428446;Dbxref=PMID:17330950,PMID:19779198,PMID:16428446 +Q03497 UniProtKB Modified residue 203 203 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q03497 UniProtKB Modified residue 418 418 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16428446;Dbxref=PMID:16428446 +Q03497 UniProtKB Modified residue 502 502 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03497 UniProtKB Modified residue 547 547 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:10359756;Dbxref=PMID:19779198,PMID:10359756 +Q03497 UniProtKB Modified residue 562 562 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:10359756;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198,PMID:10359756 +Q03497 UniProtKB Modified residue 573 573 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10359756;Dbxref=PMID:10359756 +Q03497 UniProtKB Modified residue 585 585 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000269|PubMed:10359756,ECO:0000269|PubMed:16428446;Dbxref=PMID:17330950,PMID:10359756,PMID:16428446 +Q03497 UniProtKB Modified residue 773 773 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10359756;Dbxref=PMID:10359756 +Q03497 UniProtKB Modified residue 924 924 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03497 UniProtKB Modified residue 927 927 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03497 UniProtKB Mutagenesis 338 338 . . . Note=Reduces interaction with CDC42. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11940652;Dbxref=PMID:11940652 +Q03497 UniProtKB Mutagenesis 345 345 . . . Note=Reduces interaction with CDC42. H->A%2CD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11940652,ECO:0000269|PubMed:12586692;Dbxref=PMID:11940652,PMID:12586692 +Q03497 UniProtKB Mutagenesis 348 348 . . . Note=Reduces interaction with CDC42. H->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12586692;Dbxref=PMID:12586692 +Q03497 UniProtKB Mutagenesis 475 475 . . . Note=Impairs interaction with BEM1%3B when associated with A-477. P->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15743816;Dbxref=PMID:15743816 +Q03497 UniProtKB Mutagenesis 477 477 . . . Note=Impairs interaction with BEM1%3B when associated with G-475. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15743816;Dbxref=PMID:15743816 +Q03497 UniProtKB Mutagenesis 649 649 . . . Note=Impairs phosphorylation of STE11 and histone H2B and mating efficiency. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15652479,ECO:0000269|PubMed:7608157;Dbxref=PMID:15652479,PMID:7608157 +Q03497 UniProtKB Mutagenesis 777 777 . . . Note=Impairs autophosphorylation and mating efficiency. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7608157;Dbxref=PMID:7608157 +Q03497 UniProtKB Sequence conflict 19 19 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03497 UniProtKB Sequence conflict 134 134 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q03497 UniProtKB Sequence conflict 271 271 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P06783 1 470 +P06783 UniProtKB Chain 1 470 . . . ID=PRO_0000195079;Note=Pheromone a factor receptor +P06783 UniProtKB Topological domain 1 5 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06783 UniProtKB Transmembrane 6 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06783 UniProtKB Topological domain 24 29 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06783 UniProtKB Transmembrane 30 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06783 UniProtKB Topological domain 54 70 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06783 UniProtKB Transmembrane 71 98 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06783 UniProtKB Topological domain 99 116 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06783 UniProtKB Transmembrane 117 134 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06783 UniProtKB Topological domain 135 155 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06783 UniProtKB Transmembrane 156 183 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06783 UniProtKB Topological domain 184 205 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06783 UniProtKB Transmembrane 206 228 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06783 UniProtKB Topological domain 229 266 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06783 UniProtKB Transmembrane 267 285 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06783 UniProtKB Topological domain 286 470 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P06783 UniProtKB Region 300 470 . . . Note=Hydrophilic +##sequence-region P32917 1 917 +P32917 UniProtKB Chain 1 917 . . . ID=PRO_0000072266;Note=Protein STE5 +P32917 UniProtKB Compositional bias 775 876 . . . Note=Asp/Glu-rich (acidic) +P32917 UniProtKB Modified residue 329 329 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P32917 UniProtKB Sequence conflict 331 332 . . . Note=LG->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32917 UniProtKB Sequence conflict 341 343 . . . Note=NSI->TLS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32917 UniProtKB Sequence conflict 821 821 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32917 UniProtKB Helix 45 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KGN +P32917 UniProtKB Helix 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KGN +P32917 UniProtKB Turn 52 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KGN +P32917 UniProtKB Helix 55 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KGN +P32917 UniProtKB Helix 59 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KGN +P32917 UniProtKB Turn 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2KGN +P32917 UniProtKB Helix 593 604 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE +P32917 UniProtKB Beta strand 608 616 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE +P32917 UniProtKB Helix 618 620 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE +P32917 UniProtKB Beta strand 622 624 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F2H +P32917 UniProtKB Helix 625 640 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE +P32917 UniProtKB Beta strand 645 650 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE +P32917 UniProtKB Beta strand 653 660 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE +P32917 UniProtKB Helix 661 664 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE +P32917 UniProtKB Helix 668 672 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE +P32917 UniProtKB Helix 673 676 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE +P32917 UniProtKB Helix 685 692 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE +P32917 UniProtKB Beta strand 701 707 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE +P32917 UniProtKB Turn 713 715 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE +P32917 UniProtKB Helix 717 719 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE +P32917 UniProtKB Helix 723 725 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE +P32917 UniProtKB Beta strand 735 741 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE +P32917 UniProtKB Turn 748 750 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4F2H +P32917 UniProtKB Beta strand 755 758 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE +P32917 UniProtKB Helix 760 770 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3FZE +##sequence-region P12866 1 1290 +P12866 UniProtKB Chain 1 1290 . . . ID=PRO_0000093370;Note=Alpha-factor-transporting ATPase +P12866 UniProtKB Topological domain 1 25 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Transmembrane 26 46 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Topological domain 47 75 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Transmembrane 76 96 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Topological domain 97 150 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Transmembrane 151 171 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Topological domain 172 173 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Transmembrane 174 194 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Topological domain 195 262 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Transmembrane 263 283 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Topological domain 284 296 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Transmembrane 297 317 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Topological domain 318 715 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Transmembrane 716 736 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Topological domain 737 763 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Transmembrane 764 784 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Topological domain 785 838 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Transmembrane 839 859 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Topological domain 860 865 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Transmembrane 866 886 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Topological domain 887 945 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Transmembrane 946 966 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Topological domain 967 981 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Transmembrane 982 1002 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Topological domain 1003 1290 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12866 UniProtKB Domain 27 319 . . . Note=ABC transmembrane type-1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P12866 UniProtKB Domain 357 603 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P12866 UniProtKB Domain 717 1007 . . . Note=ABC transmembrane type-1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 +P12866 UniProtKB Domain 1052 1287 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P12866 UniProtKB Nucleotide binding 392 399 . . . Note=ATP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P12866 UniProtKB Nucleotide binding 1087 1094 . . . Note=ATP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 +P12866 UniProtKB Glycosylation 61 61 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P12866 UniProtKB Cross-link 1022 1022 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +P12866 UniProtKB Mutagenesis 392 392 . . . Note=0.8%25 mating activity. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1935899;Dbxref=PMID:1935899 +P12866 UniProtKB Mutagenesis 398 398 . . . Note=25%25 mating activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1935899;Dbxref=PMID:1935899 +P12866 UniProtKB Mutagenesis 398 398 . . . Note=1%25 mating activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1935899;Dbxref=PMID:1935899 +P12866 UniProtKB Mutagenesis 509 509 . . . Note=0.5%25 mating activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1935899;Dbxref=PMID:1935899 +P12866 UniProtKB Mutagenesis 1087 1087 . . . Note=0.3%25 mating activity. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1935899;Dbxref=PMID:1935899 +P12866 UniProtKB Mutagenesis 1093 1093 . . . Note=26%25 mating activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1935899;Dbxref=PMID:1935899 +P12866 UniProtKB Mutagenesis 1093 1093 . . . Note=15%25 mating activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1935899;Dbxref=PMID:1935899 +P12866 UniProtKB Mutagenesis 1193 1193 . . . Note=6%25 mating activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1935899;Dbxref=PMID:1935899 +##sequence-region P06784 1 515 +P06784 UniProtKB Chain 1 515 . . . ID=PRO_0000086688;Note=Serine/threonine-protein kinase STE7 +P06784 UniProtKB Domain 191 466 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P06784 UniProtKB Nucleotide binding 197 205 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P06784 UniProtKB Active site 331 331 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P06784 UniProtKB Binding site 220 220 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P06784 UniProtKB Modified residue 359 359 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8131746;Dbxref=PMID:8131746 +P06784 UniProtKB Modified residue 363 363 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8131746;Dbxref=PMID:8131746 +P06784 UniProtKB Mutagenesis 353 353 . . . Note=No loss of activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8131746;Dbxref=PMID:8131746 +P06784 UniProtKB Mutagenesis 359 359 . . . Note=Inactivation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8131746;Dbxref=PMID:8131746 +P06784 UniProtKB Mutagenesis 363 363 . . . Note=Inactivation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8131746;Dbxref=PMID:8131746 +##sequence-region P39932 1 569 +P39932 UniProtKB Chain 1 569 . . . ID=PRO_0000050461;Note=Sugar transporter STL1 +P39932 UniProtKB Topological domain 1 29 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Transmembrane 30 50 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Topological domain 51 79 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Transmembrane 80 100 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Topological domain 101 107 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Transmembrane 108 128 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Topological domain 129 129 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Transmembrane 130 150 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Topological domain 151 168 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Transmembrane 169 189 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Topological domain 190 203 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Transmembrane 204 224 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Topological domain 225 291 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Transmembrane 292 312 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Topological domain 313 330 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Transmembrane 331 351 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Topological domain 352 358 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Transmembrane 359 379 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Topological domain 380 389 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Transmembrane 390 410 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Topological domain 411 426 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Transmembrane 427 447 . . . Note=Helical%3B Name%3D11;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Topological domain 448 453 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Transmembrane 454 474 . . . Note=Helical%3B Name%3D12;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Topological domain 475 569 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Glycosylation 197 197 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Glycosylation 319 319 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39932 UniProtKB Sequence conflict 237 237 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P09959 1 803 +P09959 UniProtKB Chain 1 803 . . . ID=PRO_0000067071;Note=Regulatory protein SWI6 +P09959 UniProtKB Repeat 318 346 . . . Note=ANK 1 +P09959 UniProtKB Repeat 347 383 . . . Note=ANK 2 +P09959 UniProtKB Repeat 384 469 . . . Note=ANK 3 +P09959 UniProtKB Repeat 470 498 . . . Note=ANK 4 +P09959 UniProtKB Repeat 499 514 . . . Note=ANK 5 +P09959 UniProtKB Compositional bias 631 640 . . . Note=Glu-rich (acidic) +P09959 UniProtKB Modified residue 149 149 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P09959 UniProtKB Modified residue 160 160 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000269|PubMed:14993267;Dbxref=PMID:17287358,PMID:14993267 +P09959 UniProtKB Modified residue 176 176 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P09959 UniProtKB Modified residue 179 179 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P09959 UniProtKB Modified residue 182 182 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P09959 UniProtKB Modified residue 547 547 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P09959 UniProtKB Beta strand 3 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV +P09959 UniProtKB Beta strand 16 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV +P09959 UniProtKB Turn 24 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV +P09959 UniProtKB Beta strand 29 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV +P09959 UniProtKB Helix 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV +P09959 UniProtKB Helix 35 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV +P09959 UniProtKB Helix 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV +P09959 UniProtKB Helix 58 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV +P09959 UniProtKB Beta strand 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV +P09959 UniProtKB Helix 84 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV +P09959 UniProtKB Turn 97 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV +P09959 UniProtKB Helix 101 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV +P09959 UniProtKB Beta strand 104 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2XFV +P09959 UniProtKB Beta strand 214 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Turn 225 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Helix 244 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Helix 292 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Helix 321 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Helix 331 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Helix 354 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Helix 363 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Helix 370 377 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Helix 378 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Helix 391 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Helix 405 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Helix 422 424 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Beta strand 427 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Helix 448 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Helix 455 461 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Turn 462 464 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Helix 473 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Helix 483 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +P09959 UniProtKB Helix 506 509 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1SW6 +##sequence-region P46655 1 708 +P46655 UniProtKB Chain 1 708 . . . ID=PRO_0000119739;Note=Glutamate--tRNA ligase%2C cytoplasmic +P46655 UniProtKB Nucleotide binding 437 441 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46655 UniProtKB Region 106 115 . . . Note=Interaction with ARC1 +P46655 UniProtKB Region 141 157 . . . Note=Interaction with ARC1 +P46655 UniProtKB Region 205 207 . . . Note=Glutamate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46655 UniProtKB Region 382 386 . . . Note=Glutamate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46655 UniProtKB Motif 210 219 . . . Note="HIGH" region +P46655 UniProtKB Motif 437 441 . . . Note="KMSKS" region +P46655 UniProtKB Binding site 215 215 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46655 UniProtKB Binding site 241 241 . . . Note=Glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46655 UniProtKB Binding site 400 400 . . . Note=Glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46655 UniProtKB Binding site 403 403 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P46655 UniProtKB Modified residue 300 300 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P46655 UniProtKB Mutagenesis 148 148 . . . Note=Abolishes interaction with ARC1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16914447;Dbxref=PMID:16914447 +P46655 UniProtKB Sequence conflict 209 209 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46655 UniProtKB Sequence conflict 473 473 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46655 UniProtKB Sequence conflict 510 510 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46655 UniProtKB Sequence conflict 546 546 . . . Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46655 UniProtKB Beta strand 3 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA +P46655 UniProtKB Helix 16 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA +P46655 UniProtKB Beta strand 32 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA +P46655 UniProtKB Beta strand 41 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSM +P46655 UniProtKB Beta strand 45 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA +P46655 UniProtKB Helix 55 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA +P46655 UniProtKB Turn 63 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA +P46655 UniProtKB Helix 72 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA +P46655 UniProtKB Turn 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA +P46655 UniProtKB Helix 91 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA +P46655 UniProtKB Turn 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRK +P46655 UniProtKB Helix 119 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA +P46655 UniProtKB Helix 134 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA +P46655 UniProtKB Helix 144 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA +P46655 UniProtKB Helix 157 160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA +P46655 UniProtKB Helix 162 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HRA +##sequence-region P53277 1 215 +P53277 UniProtKB Chain 1 215 . . . ID=PRO_0000072381;Note=Pre-mRNA-splicing factor SYF2 +P53277 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53277 UniProtKB Modified residue 124 124 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53277 UniProtKB Modified residue 125 125 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53277 UniProtKB Helix 97 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53277 UniProtKB Beta strand 147 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53277 UniProtKB Helix 161 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +P53277 UniProtKB Helix 198 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P11972 1 698 +P11972 UniProtKB Chain 1 698 . . . ID=PRO_0000204173;Note=Protein SST2 +P11972 UniProtKB Domain 273 358 . . . Note=DEP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00066 +P11972 UniProtKB Domain 420 689 . . . Note=RGS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00171 +P11972 UniProtKB Region 10 203 . . . Note=Fungal-DR +P11972 UniProtKB Modified residue 252 252 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P11972 UniProtKB Modified residue 408 408 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P11972 UniProtKB Modified residue 539 539 . . . Note=Phosphoserine%3B by MAPK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10593933;Dbxref=PMID:10593933 +P11972 UniProtKB Modified residue 587 587 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P11972 UniProtKB Sequence conflict 616 616 . . . Note=H->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11972 UniProtKB Sequence conflict 644 644 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P41930 1 458 +P41930 UniProtKB Chain 1 458 . . . ID=PRO_0000072229;Note=Sulfite efflux pump SSU1 +P41930 UniProtKB Topological domain 1 11 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Transmembrane 12 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Topological domain 33 48 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Transmembrane 49 69 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Topological domain 70 89 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Transmembrane 90 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Topological domain 111 135 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Topological domain 157 176 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Transmembrane 177 197 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Topological domain 198 220 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Transmembrane 221 241 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Topological domain 242 252 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Transmembrane 253 275 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Topological domain 276 309 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Transmembrane 310 330 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Topological domain 331 350 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Transmembrane 351 371 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Topological domain 372 387 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Transmembrane 388 408 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Topological domain 409 458 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41930 UniProtKB Modified residue 444 444 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P41930 UniProtKB Modified residue 448 448 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P41930 UniProtKB Modified residue 450 450 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P41930 UniProtKB Natural variant 19 19 . . . Note=In strain: Ba194%2C CECT 10233%2C M5-7A%2C M5-7B%2C M7-8D%2C MMR2-1%2C MMR2-3%2C MMW1-12%2C ORM1-1%2C Sgu52E%2C Y-9%2C YPS396%2C YPS400%2C YPS598%2C YPS600%2C YPS602%2C YPS604%2C YPS606%2C YPS608 and YPS610. M->V +P41930 UniProtKB Natural variant 52 52 . . . Note=In strain: ATCC 76625 / YPH499%2C Ba194%2C Bb32%2C M1-2A%2C M2-8%2C M5-7A%2C M5-7B%2C M7-8D%2C MMR2-1%2C MMR2-3%2C MMR2-5%2C MMW1-15%2C MMW1-15h2%2C MMW1-2%2C MMW1-2h2%2C MMW1-12%2C ORM1-1%2C S288c/ YPH1%2C Sgu52E%2C Sgu52F%2C Y-9%2C YPS396%2C YPS400%2C YPS598%2C YPS600%2C YPS602%2C YPS604%2C YPS606%2C YPS608 and YPS610. A->T +P41930 UniProtKB Natural variant 90 90 . . . Note=In strain: Ba194%2C Bb32%2C M1-2A%2C M2-8%2C M5-7A%2C M5-7B%2C M7-8D%2C MMR2-5%2C MMW1-15h2%2C MMW1-2h2%2C Sgu52E%2C Sgu52F and Y-9. N->S +P41930 UniProtKB Natural variant 122 122 . . . Note=In strain: Bb32%2C M1-2A%2C M2-8%2C MMR2-5%2C MMW1-15h2%2C MMW1-2h2 and Sgu52F. A->S +P41930 UniProtKB Natural variant 157 157 . . . Note=In strain: Ba194%2C Bb32%2C M1-2A%2C M2-8%2C M5-7A%2C M5-7B%2C M7-8D%2C MMR2-1%2C MMR2-3%2C MMR2-5%2C MMW1-12%2C MMW1-15h2%2C MMW1-2h2%2C ORM1-1%2C Sgu52E%2C Sgu52F%2C Y-9%2C YPS396%2C YPS400%2C YPS598%2C YPS600%2C YPS602%2C YPS604%2C YPS606%2C YPS608 and YPS610. P->S +P41930 UniProtKB Natural variant 164 164 . . . Note=In strain: Bb32%2C M1-2A%2C M2-8%2C MMR2-5%2C MMW1-15h2%2C MMW1-2h2 and Sgu52F. Y->H +P41930 UniProtKB Natural variant 191 191 . . . Note=In strain: ATCC 76625 / YPH499%2CMMW1-15%2C MMW1-2 and S288c / YPH1. A->T +P41930 UniProtKB Natural variant 344 344 . . . Note=In strain: Sgu52F. G->E +P41930 UniProtKB Natural variant 345 345 . . . Note=In strain: ATCC 76625 / YPH499%2C MMW1-15 and MMW1-2. K->R +##sequence-region P50104 1 949 +P50104 UniProtKB Chain 1 949 . . . ID=PRO_0000114980;Note=Probable transcriptional regulatory protein STB4 +P50104 UniProtKB DNA binding 87 113 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +##sequence-region P53394 1 754 +P53394 UniProtKB Chain 1 754 . . . ID=PRO_0000080192;Note=Putative sulfate transporter YPR003C +P53394 UniProtKB Topological domain 1 118 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Transmembrane 119 139 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Topological domain 140 146 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Transmembrane 147 167 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Topological domain 168 172 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Topological domain 194 199 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Transmembrane 200 220 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Topological domain 221 232 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Transmembrane 233 253 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Topological domain 254 282 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Transmembrane 283 303 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Topological domain 304 317 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Transmembrane 318 338 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Topological domain 339 370 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Transmembrane 371 391 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Topological domain 392 410 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Transmembrane 411 431 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Topological domain 432 450 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Transmembrane 451 471 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Topological domain 472 474 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Transmembrane 475 495 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Topological domain 496 517 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Transmembrane 518 538 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Topological domain 539 754 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53394 UniProtKB Domain 574 725 . . . Note=STAS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00198 +##sequence-region P08153 1 709 +P08153 UniProtKB Chain 1 709 . . . ID=PRO_0000046855;Note=Transcriptional factor SWI5 +P08153 UniProtKB Zinc finger 550 574 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P08153 UniProtKB Zinc finger 580 604 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P08153 UniProtKB Zinc finger 609 632 . . . Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P08153 UniProtKB DNA binding 647 659 . . . Note=A.T hook +P08153 UniProtKB Motif 635 659 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08153 UniProtKB Modified residue 225 225 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P08153 UniProtKB Modified residue 278 278 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P08153 UniProtKB Modified residue 300 300 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P08153 UniProtKB Modified residue 339 339 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P08153 UniProtKB Modified residue 376 376 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P08153 UniProtKB Modified residue 488 488 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P08153 UniProtKB Modified residue 492 492 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P08153 UniProtKB Modified residue 505 505 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:18407956 +P08153 UniProtKB Modified residue 522 522 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:1652372;Dbxref=PMID:19779198,PMID:1652372 +P08153 UniProtKB Modified residue 646 646 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17287358,ECO:0000269|PubMed:1652372;Dbxref=PMID:17287358,PMID:1652372 +P08153 UniProtKB Modified residue 664 664 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1652372;Dbxref=PMID:1652372 +P08153 UniProtKB Mutagenesis 522 522 . . . Note=Constitutive nuclear entry%3B when associated with A-646 and A-664. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1652372;Dbxref=PMID:1652372 +P08153 UniProtKB Mutagenesis 646 646 . . . Note=Constitutive nuclear entry%3B when associated with A-522 and A-664. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1652372;Dbxref=PMID:1652372 +P08153 UniProtKB Mutagenesis 664 664 . . . Note=Constitutive nuclear entry%3B when associated with A-522 and A-646. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1652372;Dbxref=PMID:1652372 +P08153 UniProtKB Sequence conflict 514 514 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08153 UniProtKB Helix 538 540 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NCS +P08153 UniProtKB Beta strand 543 545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NCS +P08153 UniProtKB Turn 546 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NCS +P08153 UniProtKB Beta strand 549 551 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NCS +P08153 UniProtKB Beta strand 563 566 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NCS +P08153 UniProtKB Helix 567 574 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NCS +P08153 UniProtKB Turn 575 577 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NCS +P08153 UniProtKB Beta strand 591 594 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZFD +P08153 UniProtKB Helix 595 601 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZFD +P08153 UniProtKB Helix 602 604 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ZFD +##sequence-region Q12379 1 170 +Q12379 UniProtKB Chain 1 170 . . . ID=PRO_0000072352;Note=Anaphase-promoting complex subunit SWM1 +Q12379 UniProtKB Compositional bias 2 5 . . . Note=Poly-Ser +##sequence-region P43554 1 623 +P43554 UniProtKB Chain 1 623 . . . ID=PRO_0000076350;Note=SWI/SNF global transcription activator complex subunit SWP82 +##sequence-region Q05471 1 1514 +Q05471 UniProtKB Chain 1 1514 . . . ID=PRO_0000074375;Note=Helicase SWR1 +Q05471 UniProtKB Domain 339 411 . . . Note=HSA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00549 +Q05471 UniProtKB Domain 708 873 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q05471 UniProtKB Domain 1247 1400 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q05471 UniProtKB Nucleotide binding 721 728 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q05471 UniProtKB Motif 824 827 . . . Note=DEAH box +Q05471 UniProtKB Helix 353 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5I9E +Q05471 UniProtKB Helix 602 605 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4M6B +##sequence-region P53852 1 767 +P53852 UniProtKB Chain 1 767 . . . ID=PRO_0000159553;Note=Cysteine--tRNA ligase +P53852 UniProtKB Motif 65 75 . . . Note="HIGH" region +P53852 UniProtKB Motif 427 431 . . . Note="KMSKS" region +P53852 UniProtKB Metal binding 63 63 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53852 UniProtKB Metal binding 369 369 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53852 UniProtKB Metal binding 394 394 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53852 UniProtKB Metal binding 398 398 . . . Note=Zinc;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53852 UniProtKB Binding site 430 430 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53852 UniProtKB Modified residue 326 326 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +##sequence-region P15179 1 658 +P15179 UniProtKB Chain 1 658 . . . ID=PRO_0000111015;Note=Aspartate--tRNA ligase%2C mitochondrial +P15179 UniProtKB Nucleotide binding 248 250 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15179 UniProtKB Nucleotide binding 604 607 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15179 UniProtKB Region 226 229 . . . Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15179 UniProtKB Binding site 198 198 . . . Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15179 UniProtKB Binding site 248 248 . . . Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15179 UniProtKB Binding site 553 553 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P15179 UniProtKB Binding site 560 560 . . . Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P23615 1 1451 +P23615 UniProtKB Chain 1 1451 . . . ID=PRO_0000072173;Note=Transcription elongation factor SPT6 +P23615 UniProtKB Domain 1257 1354 . . . Note=SH2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00191 +P23615 UniProtKB Motif 8 12 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23615 UniProtKB Motif 77 85 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23615 UniProtKB Motif 120 125 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23615 UniProtKB Compositional bias 1 484 . . . Note=Asp/Glu-rich (acidic) +P23615 UniProtKB Modified residue 94 94 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P23615 UniProtKB Modified residue 134 134 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P23615 UniProtKB Modified residue 136 136 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P23615 UniProtKB Modified residue 148 148 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P23615 UniProtKB Modified residue 155 155 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P23615 UniProtKB Modified residue 206 206 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P23615 UniProtKB Modified residue 295 295 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P23615 UniProtKB Helix 239 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OAK +P23615 UniProtKB Helix 256 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3OAK +P23615 UniProtKB Helix 301 308 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 312 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Beta strand 320 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 324 329 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 330 332 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Turn 334 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 341 359 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 368 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 388 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 396 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Beta strand 402 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI +P23615 UniProtKB Helix 411 441 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 446 454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 465 476 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 478 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 502 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 511 515 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 521 530 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Beta strand 541 543 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI +P23615 UniProtKB Helix 545 554 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Turn 555 559 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 568 583 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 586 598 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Beta strand 599 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 608 613 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Turn 615 617 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Turn 619 625 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 633 636 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 639 649 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Beta strand 652 659 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 662 673 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 681 733 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Beta strand 740 744 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI +P23615 UniProtKB Beta strand 750 754 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Turn 760 762 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Beta strand 765 770 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Beta strand 776 782 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 793 806 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Beta strand 809 813 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 819 833 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Beta strand 839 841 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI +P23615 UniProtKB Beta strand 846 848 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 854 858 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 861 866 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 872 885 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 887 892 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 896 900 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 908 910 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 913 931 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 935 939 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 942 945 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 946 950 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 956 968 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 978 981 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 987 993 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Turn 994 996 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 1015 1018 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 1023 1025 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 1026 1036 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 1041 1050 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 1055 1062 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 1066 1070 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 1075 1086 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 1091 1102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Beta strand 1103 1105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI +P23615 UniProtKB Helix 1117 1125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Turn 1129 1131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI +P23615 UniProtKB Beta strand 1137 1145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI +P23615 UniProtKB Beta strand 1150 1153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI +P23615 UniProtKB Beta strand 1159 1162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI +P23615 UniProtKB Beta strand 1166 1169 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI +P23615 UniProtKB Turn 1177 1179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI +P23615 UniProtKB Beta strand 1185 1194 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI +P23615 UniProtKB Helix 1195 1197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI +P23615 UniProtKB Beta strand 1199 1203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI +P23615 UniProtKB Helix 1206 1209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSI +P23615 UniProtKB Turn 1222 1224 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Helix 1227 1246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSF +P23615 UniProtKB Turn 1247 1249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK +P23615 UniProtKB Beta strand 1253 1255 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L3T +P23615 UniProtKB Helix 1264 1271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK +P23615 UniProtKB Beta strand 1279 1283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK +P23615 UniProtKB Turn 1285 1287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L3T +P23615 UniProtKB Beta strand 1288 1298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK +P23615 UniProtKB Beta strand 1301 1311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK +P23615 UniProtKB Beta strand 1313 1317 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSJ +P23615 UniProtKB Beta strand 1320 1324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK +P23615 UniProtKB Beta strand 1327 1331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK +P23615 UniProtKB Helix 1332 1338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK +P23615 UniProtKB Helix 1340 1351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK +P23615 UniProtKB Helix 1361 1372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK +P23615 UniProtKB Beta strand 1380 1385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK +P23615 UniProtKB Beta strand 1387 1389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK +P23615 UniProtKB Beta strand 1392 1400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK +P23615 UniProtKB Beta strand 1406 1412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK +P23615 UniProtKB Beta strand 1414 1419 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK +P23615 UniProtKB Beta strand 1422 1426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK +P23615 UniProtKB Helix 1427 1437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PSK +##sequence-region Q08673 1 210 +Q08673 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08673 UniProtKB Chain 20 210 . . . ID=PRO_0000270576;Note=Cell wall protein SRL1 +Q08673 UniProtKB Compositional bias 25 208 . . . Note=Thr-rich +Q08673 UniProtKB Glycosylation 23 23 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08673 UniProtKB Glycosylation 174 174 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08673 UniProtKB Glycosylation 200 200 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08673 UniProtKB Glycosylation 206 206 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03085 1 281 +Q03085 UniProtKB Chain 1 281 . . . ID=PRO_0000269762;Note=Oxidoreductase-like protein SRL4 +##sequence-region P10080 1 294 +P10080 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P10080 UniProtKB Chain 2 294 . . . ID=PRO_0000081964;Note=Single-stranded nucleic acid-binding protein +P10080 UniProtKB Domain 37 119 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P10080 UniProtKB Domain 186 274 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 +P10080 UniProtKB Region 131 151 . . . Note=RNA-binding RGG-box;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P10080 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P10080 UniProtKB Modified residue 91 91 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P10080 UniProtKB Modified residue 119 119 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P10080 UniProtKB Modified residue 242 242 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P10080 UniProtKB Modified residue 244 244 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P10080 UniProtKB Sequence conflict 162 162 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53599 1 1579 +P53599 UniProtKB Chain 1 1579 . . . ID=PRO_0000086682;Note=MAP kinase kinase kinase SSK2 +P53599 UniProtKB Domain 1266 1558 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53599 UniProtKB Nucleotide binding 1272 1280 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53599 UniProtKB Active site 1390 1390 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P53599 UniProtKB Binding site 1295 1295 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P53599 UniProtKB Modified residue 57 57 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53599 UniProtKB Modified residue 62 62 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53599 UniProtKB Modified residue 78 78 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53599 UniProtKB Modified residue 118 118 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53599 UniProtKB Modified residue 290 290 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53599 UniProtKB Modified residue 1424 1424 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q07084 1 712 +Q07084 UniProtKB Chain 1 712 . . . ID=PRO_0000081406;Note=Osmolarity two-component system protein SSK1 +Q07084 UniProtKB Domain 505 647 . . . Note=Response regulatory;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00169 +Q07084 UniProtKB Modified residue 110 110 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q07084 UniProtKB Modified residue 195 195 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q07084 UniProtKB Modified residue 327 327 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q07084 UniProtKB Modified residue 351 351 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07084 UniProtKB Modified residue 368 368 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q07084 UniProtKB Modified residue 380 380 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q07084 UniProtKB Modified residue 554 554 . . . Note=4-aspartylphosphate;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00169,ECO:0000269|PubMed:8808622;Dbxref=PMID:8808622 +Q07084 UniProtKB Modified residue 673 673 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950;Dbxref=PMID:17287358,PMID:17330950 +Q07084 UniProtKB Modified residue 693 693 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q07084 UniProtKB Modified residue 703 703 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q07084 UniProtKB Modified residue 706 706 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07084 UniProtKB Mutagenesis 554 554 . . . Note=Activates. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8183345;Dbxref=PMID:8183345 +Q07084 UniProtKB Sequence conflict 181 181 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32867 1 290 +P32867 UniProtKB Chain 1 290 . . . ID=PRO_0000210274;Note=Protein SSO1 +P32867 UniProtKB Topological domain 1 265 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32867 UniProtKB Transmembrane 266 287 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32867 UniProtKB Topological domain 288 290 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32867 UniProtKB Domain 190 252 . . . Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202 +P32867 UniProtKB Sequence conflict 97 97 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32867 UniProtKB Sequence conflict 105 105 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32867 UniProtKB Helix 31 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FIO +P32867 UniProtKB Helix 70 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FIO +P32867 UniProtKB Turn 105 107 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FIO +P32867 UniProtKB Helix 109 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FIO +P32867 UniProtKB Helix 157 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FIO +P32867 UniProtKB Helix 166 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1FIO +P32867 UniProtKB Helix 190 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3B5N +##sequence-region Q12427 1 513 +Q12427 UniProtKB Chain 1 513 . . . ID=PRO_0000072254;Note=Protein STB3 +Q12427 UniProtKB Modified residue 254 254 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P36085 1 766 +P36085 UniProtKB Chain 1 766 . . . ID=PRO_0000072255;Note=Protein STB6 +P36085 UniProtKB Modified residue 514 514 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region D6VTK4 1 431 +D6VTK4 UniProtKB Chain 1 431 . . . ID=PRO_0000195068;Note=Pheromone alpha factor receptor +D6VTK4 UniProtKB Transmembrane 51 73 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +D6VTK4 UniProtKB Transmembrane 80 102 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +D6VTK4 UniProtKB Transmembrane 133 155 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +D6VTK4 UniProtKB Transmembrane 162 184 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +D6VTK4 UniProtKB Transmembrane 209 231 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +D6VTK4 UniProtKB Transmembrane 244 266 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +D6VTK4 UniProtKB Transmembrane 276 298 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +D6VTK4 UniProtKB Modified residue 310 310 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +D6VTK4 UniProtKB Modified residue 315 315 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +D6VTK4 UniProtKB Modified residue 329 329 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +D6VTK4 UniProtKB Modified residue 331 331 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +D6VTK4 UniProtKB Modified residue 360 360 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +D6VTK4 UniProtKB Modified residue 363 363 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +D6VTK4 UniProtKB Modified residue 366 366 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:19779198 +D6VTK4 UniProtKB Modified residue 382 382 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +D6VTK4 UniProtKB Modified residue 385 385 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +D6VTK4 UniProtKB Modified residue 386 386 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +D6VTK4 UniProtKB Modified residue 411 411 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +D6VTK4 UniProtKB Modified residue 414 414 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +D6VTK4 UniProtKB Glycosylation 25 25 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11583169;Dbxref=PMID:11583169 +D6VTK4 UniProtKB Glycosylation 32 32 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11583169;Dbxref=PMID:11583169 +D6VTK4 UniProtKB Cross-link 374 374 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +D6VTK4 UniProtKB Cross-link 400 400 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +D6VTK4 UniProtKB Cross-link 422 422 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +D6VTK4 UniProtKB Sequence conflict 269 269 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +D6VTK4 UniProtKB Helix 39 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K9P +D6VTK4 UniProtKB Helix 80 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2K9P +D6VTK4 UniProtKB Helix 256 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PJD +##sequence-region P25344 1 346 +P25344 UniProtKB Chain 1 346 . . . ID=PRO_0000072265;Note=Protein STE50 +P25344 UniProtKB Domain 24 108 . . . Note=SAM +P25344 UniProtKB Domain 233 327 . . . Note=Ras-associating;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00166 +P25344 UniProtKB Modified residue 202 202 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P25344 UniProtKB Modified residue 244 244 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25344 UniProtKB Modified residue 248 248 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P25344 UniProtKB Turn 32 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UQV +P25344 UniProtKB Helix 37 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UQV +P25344 UniProtKB Helix 56 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UQV +P25344 UniProtKB Helix 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UQV +P25344 UniProtKB Helix 70 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UQV +P25344 UniProtKB Beta strand 82 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UQV +P25344 UniProtKB Helix 86 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UQV +##sequence-region P16965 1 84 +P16965 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6 +P16965 UniProtKB Chain 2 84 . . . ID=PRO_0000072269;Note=ATPase-stabilizing factor 15 kDa protein +P16965 UniProtKB Modified residue 28 28 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +P16965 UniProtKB Modified residue 69 69 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +P16965 UniProtKB Sequence conflict 15 15 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16965 UniProtKB Sequence conflict 27 27 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16965 UniProtKB Sequence conflict 55 55 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P16965 UniProtKB Sequence conflict 61 84 . . . Note=VFKKDRRGSNLQSHEQKFENVQKE->SVQER;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53312 1 427 +P53312 UniProtKB Transit peptide 1 30 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219 +P53312 UniProtKB Chain 31 427 . . . ID=PRO_0000033365;Note=Succinate--CoA ligase [ADP-forming] subunit beta%2C mitochondrial;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219 +P53312 UniProtKB Domain 39 284 . . . Note=ATP-grasp;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219 +P53312 UniProtKB Nucleotide binding 83 85 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219 +P53312 UniProtKB Region 361 363 . . . Note=Substrate binding%3B shared with subunit alpha;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219 +P53312 UniProtKB Metal binding 236 236 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219 +P53312 UniProtKB Metal binding 253 253 . . . Note=Magnesium;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219 +P53312 UniProtKB Binding site 76 76 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219 +P53312 UniProtKB Binding site 144 144 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219 +P53312 UniProtKB Binding site 304 304 . . . Note=Substrate%3B shared with subunit alpha;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03219 +P53312 UniProtKB Modified residue 102 102 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P53312 UniProtKB Modified residue 263 263 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53312 UniProtKB Modified residue 276 276 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q06524 1 206 +Q06524 UniProtKB Transit peptide 1 24 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06524 UniProtKB Chain 25 206 . . . ID=PRO_0000270578;Note=Protein SUE1%2C mitochondrial +##sequence-region P38359 1 859 +P38359 UniProtKB Chain 1 859 . . . ID=PRO_0000080184;Note=Sulfate permease 1 +P38359 UniProtKB Transmembrane 94 114 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Transmembrane 116 136 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Transmembrane 148 168 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Transmembrane 206 226 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Transmembrane 234 254 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Transmembrane 292 312 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Transmembrane 332 352 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Transmembrane 395 415 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Transmembrane 428 448 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Transmembrane 468 488 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Transmembrane 525 545 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Domain 630 808 . . . Note=STAS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00198 +P38359 UniProtKB Glycosylation 51 51 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Glycosylation 93 93 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Glycosylation 358 358 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Glycosylation 391 391 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Glycosylation 630 630 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Glycosylation 653 653 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Glycosylation 718 718 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38359 UniProtKB Sequence conflict 87 87 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38359 UniProtKB Sequence conflict 457 457 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q05515 1 481 +Q05515 UniProtKB Chain 1 481 . . . ID=PRO_0000072336;Note=Survival factor 1 +Q05515 UniProtKB Compositional bias 200 256 . . . Note=Glu-rich +Q05515 UniProtKB Compositional bias 359 395 . . . Note=Glu-rich +##sequence-region Q03088 1 825 +Q03088 UniProtKB Chain 1 825 . . . ID=PRO_0000072340;Note=Styryl dye vacuolar localization protein 3 +Q03088 UniProtKB Coiled coil 366 423 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03088 UniProtKB Compositional bias 629 755 . . . Note=Asn-rich +Q03088 UniProtKB Modified residue 471 471 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +Q03088 UniProtKB Modified residue 496 496 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03088 UniProtKB Modified residue 551 551 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q03088 UniProtKB Modified residue 662 662 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03088 UniProtKB Modified residue 739 739 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03088 UniProtKB Modified residue 756 756 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03088 UniProtKB Modified residue 757 757 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q06677 1 668 +Q06677 UniProtKB Chain 1 668 . . . ID=PRO_0000270621;Note=Auxilin-like clathrin uncoating factor SWA2 +Q06677 UniProtKB Domain 140 180 . . . Note=UBA +Q06677 UniProtKB Repeat 374 407 . . . Note=TPR 1 +Q06677 UniProtKB Repeat 412 445 . . . Note=TPR 2 +Q06677 UniProtKB Repeat 467 500 . . . Note=TPR 3 +Q06677 UniProtKB Domain 603 668 . . . Note=J +Q06677 UniProtKB Region 1 100 . . . Note=CB1 +Q06677 UniProtKB Region 238 302 . . . Note=CB2 +Q06677 UniProtKB Region 303 362 . . . Note=CB3 +Q06677 UniProtKB Modified residue 52 52 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q06677 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06677 UniProtKB Modified residue 264 264 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06677 UniProtKB Modified residue 308 308 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q06677 UniProtKB Modified residue 312 312 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q06677 UniProtKB Mutagenesis 388 388 . . . Note=In SWA2-1/SWA2-TPR%3B partial loss of clathrin disassembly function. In SWA2-TPR-J%3B complete loss of clathrin disassembly function%3B when associated with 631-AAA-633. G->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11084334,ECO:0000269|PubMed:16687570;Dbxref=PMID:11084334,PMID:16687570 +Q06677 UniProtKB Mutagenesis 631 633 . . . Note=In SWA2-J%3B abolishes ATPase stimulation activity. In SWA2-TPR-J%3B complete loss of clathrin disassembly function%3B when associated with R-388. HPD->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16687570;Dbxref=PMID:16687570 +Q06677 UniProtKB Helix 140 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGY +Q06677 UniProtKB Helix 158 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGY +Q06677 UniProtKB Helix 171 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1PGY +##sequence-region Q12104 1 458 +Q12104 UniProtKB Chain 1 458 . . . ID=PRO_0000237661;Note=Transcriptional protein SWT1 +Q12104 UniProtKB Domain 130 262 . . . Note=PINc +Q12104 UniProtKB Mutagenesis 1 115 . . . Note=Fully functional%3B when associated with deletion of 260-L--T-458. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17030511;Dbxref=PMID:17030511 +Q12104 UniProtKB Mutagenesis 260 458 . . . Note=Fully functional%3B when associated with deletion of 1-M--K-115. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17030511;Dbxref=PMID:17030511 +Q12104 UniProtKB Helix 326 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ +Q12104 UniProtKB Helix 354 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ +Q12104 UniProtKB Turn 358 361 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ +Q12104 UniProtKB Helix 370 379 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ +Q12104 UniProtKB Turn 380 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ +Q12104 UniProtKB Helix 385 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ +Q12104 UniProtKB Turn 389 391 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ +Q12104 UniProtKB Helix 396 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ +Q12104 UniProtKB Helix 404 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ +Q12104 UniProtKB Helix 413 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ +Q12104 UniProtKB Turn 431 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ +Q12104 UniProtKB Helix 436 454 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4PQZ +##sequence-region P53135 1 668 +P53135 UniProtKB Chain 1 668 . . . ID=PRO_0000071954;Note=DNA replication regulator SLD3 +P53135 UniProtKB Compositional bias 276 279 . . . Note=Poly-Leu +P53135 UniProtKB Helix 157 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3 +P53135 UniProtKB Helix 176 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3 +P53135 UniProtKB Helix 183 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3 +P53135 UniProtKB Turn 197 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3 +P53135 UniProtKB Helix 200 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3 +P53135 UniProtKB Helix 215 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3 +P53135 UniProtKB Helix 226 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3 +P53135 UniProtKB Helix 234 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3 +P53135 UniProtKB Helix 258 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3 +P53135 UniProtKB Helix 288 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3 +P53135 UniProtKB Helix 339 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3 +P53135 UniProtKB Helix 373 380 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3 +P53135 UniProtKB Helix 390 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3 +P53135 UniProtKB Helix 398 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3 +P53135 UniProtKB Beta strand 403 406 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3 +P53135 UniProtKB Helix 407 417 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3WI3 +##sequence-region P38343 1 150 +P38343 UniProtKB Chain 1 150 . . . ID=PRO_0000202528;Note=Protein SLM6 +P38343 UniProtKB Topological domain 1 76 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38343 UniProtKB Transmembrane 77 97 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38343 UniProtKB Topological domain 98 104 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38343 UniProtKB Transmembrane 105 125 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38343 UniProtKB Topological domain 126 150 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P32828 1 619 +P32828 UniProtKB Chain 1 619 . . . ID=PRO_0000083954;Note=E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX5 +P32828 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32828 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q02651 1 245 +Q02651 UniProtKB Chain 1 245 . . . ID=PRO_0000071964;Note=Spore membrane assembly protein 1 +##sequence-region Q04658 1 369 +Q04658 UniProtKB Chain 1 369 . . . ID=PRO_0000203252;Note=Spore membrane assembly protein 2 +Q04658 UniProtKB Topological domain 1 6 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04658 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04658 UniProtKB Topological domain 28 220 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04658 UniProtKB Transmembrane 221 241 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04658 UniProtKB Topological domain 242 265 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04658 UniProtKB Transmembrane 266 286 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04658 UniProtKB Topological domain 287 319 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04658 UniProtKB Transmembrane 320 340 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04658 UniProtKB Topological domain 341 369 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q08817 1 791 +Q08817 UniProtKB Chain 1 791 . . . ID=PRO_0000270575;Note=Leucine-rich repeat-containing protein SOG2 +Q08817 UniProtKB Repeat 43 64 . . . Note=LRR 1 +Q08817 UniProtKB Repeat 67 88 . . . Note=LRR 2 +Q08817 UniProtKB Repeat 90 111 . . . Note=LRR 3 +Q08817 UniProtKB Repeat 113 134 . . . Note=LRR 4 +Q08817 UniProtKB Repeat 138 159 . . . Note=LRR 5 +Q08817 UniProtKB Repeat 163 183 . . . Note=LRR 6 +Q08817 UniProtKB Modified residue 214 214 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P39543 1 234 +P39543 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39543 UniProtKB Chain 19 234 . . . ID=PRO_0000014332;Note=Protein SOP4 +P39543 UniProtKB Topological domain 19 188 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39543 UniProtKB Transmembrane 189 209 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39543 UniProtKB Topological domain 210 234 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39543 UniProtKB Glycosylation 35 35 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39543 UniProtKB Glycosylation 53 53 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39543 UniProtKB Glycosylation 85 85 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39543 UniProtKB Glycosylation 115 115 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39543 UniProtKB Glycosylation 170 170 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53148 1 917 +P53148 UniProtKB Chain 1 917 . . . ID=PRO_0000202755;Note=Spindle pole body component SPC105 +P53148 UniProtKB Modified residue 77 77 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53148 UniProtKB Modified residue 356 356 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P53148 UniProtKB Modified residue 380 380 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P53148 UniProtKB Beta strand 170 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BL0 +##sequence-region Q01684 1 191 +Q01684 UniProtKB Chain 1 191 . . . ID=PRO_0000072148;Note=Sporulation-specific protein +Q01684 UniProtKB Sequence conflict 4 4 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q01684 UniProtKB Sequence conflict 4 4 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P06844 1 337 +P06844 UniProtKB Chain 1 337 . . . ID=PRO_0000072166;Note=Protein SPT3 +P06844 UniProtKB Modified residue 270 270 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P06844 UniProtKB Natural variant 76 76 . . . Note=In strain: CLIB 556 and CLIB 630. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P06844 UniProtKB Natural variant 93 93 . . . Note=In strain: CLIB 556 and CLIB 630. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P06844 UniProtKB Natural variant 120 120 . . . Note=In strain: CLIB 413 haplotype Ha2. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P06844 UniProtKB Natural variant 134 134 . . . Note=In strain: R13 haplotype Ha2. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +P06844 UniProtKB Natural variant 318 318 . . . Note=In strain: YIIc12 haplotype Ha2 and YIIc17. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15087486;Dbxref=PMID:15087486 +##sequence-region P38687 1 599 +P38687 UniProtKB Chain 1 599 . . . ID=PRO_0000135232;Note=Signal recognition particle subunit SRP68 +##sequence-region P32916 1 621 +P32916 UniProtKB Chain 1 621 . . . ID=PRO_0000101216;Note=Signal recognition particle receptor subunit alpha homolog +P32916 UniProtKB Nucleotide binding 404 411 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32916 UniProtKB Nucleotide binding 510 514 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32916 UniProtKB Nucleotide binding 572 575 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32916 UniProtKB Region 1 158 . . . Note=SRX +P32916 UniProtKB Modified residue 239 239 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32916 UniProtKB Modified residue 523 523 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32916 UniProtKB Sequence conflict 499 499 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32916 UniProtKB Beta strand 4 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P32916 UniProtKB Beta strand 13 19 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P32916 UniProtKB Helix 27 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P32916 UniProtKB Helix 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P32916 UniProtKB Helix 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P32916 UniProtKB Beta strand 58 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P32916 UniProtKB Beta strand 74 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P32916 UniProtKB Turn 81 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P32916 UniProtKB Beta strand 85 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P32916 UniProtKB Helix 96 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P32916 UniProtKB Helix 118 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P32916 UniProtKB Beta strand 127 129 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P32916 UniProtKB Turn 140 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +P32916 UniProtKB Helix 145 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NRJ +##sequence-region P12954 1 1174 +P12954 UniProtKB Chain 1 1174 . . . ID=PRO_0000102071;Note=ATP-dependent DNA helicase SRS2 +P12954 UniProtKB Domain 14 316 . . . Note=UvrD-like helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00560 +P12954 UniProtKB Domain 317 654 . . . Note=UvrD-like helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00617 +P12954 UniProtKB Nucleotide binding 38 43 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00560 +P12954 UniProtKB Region 222 243 . . . Note=Leucine-zipper +P12954 UniProtKB Binding site 314 314 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P12954 UniProtKB Modified residue 833 833 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P12954 UniProtKB Sequence conflict 173 182 . . . Note=IKKQISKLKS->TQETDIKAKI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12954 UniProtKB Sequence conflict 534 548 . . . Note=YEYLYKDGKKKNDQL->VRILGTRMVRKKMSQF;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P12954 UniProtKB Helix 1152 1160 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V62 +P12954 UniProtKB Beta strand 1170 1172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3V62 +##sequence-region P13130 1 326 +P13130 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13130 UniProtKB Chain 19 326 . . . ID=PRO_0000022419;Note=Sporulation-specific wall maturation protein +P13130 UniProtKB Domain 19 324 . . . Note=Asparaginase/glutaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01068 +P13130 UniProtKB Glycosylation 26 26 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13130 UniProtKB Glycosylation 50 50 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13130 UniProtKB Glycosylation 58 58 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13130 UniProtKB Glycosylation 64 64 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13130 UniProtKB Glycosylation 76 76 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13130 UniProtKB Glycosylation 108 108 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13130 UniProtKB Glycosylation 181 181 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13130 UniProtKB Glycosylation 190 190 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13130 UniProtKB Glycosylation 199 199 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13130 UniProtKB Glycosylation 205 205 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13130 UniProtKB Glycosylation 248 248 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P13130 UniProtKB Glycosylation 281 281 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39073 1 555 +P39073 UniProtKB Chain 1 555 . . . ID=PRO_0000086784;Note=Meiotic mRNA stability protein kinase SSN3 +P39073 UniProtKB Domain 75 463 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P39073 UniProtKB Nucleotide binding 81 89 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P39073 UniProtKB Active site 286 286 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P39073 UniProtKB Binding site 183 183 . . . Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39073 UniProtKB Mutagenesis 183 183 . . . Note=In UME5-4%3B loss of activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8164691;Dbxref=PMID:8164691 +P39073 UniProtKB Mutagenesis 304 304 . . . Note=Abrogates kinase activity and transcriptional repression. D->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10360183,ECO:0000269|PubMed:11226276,ECO:0000269|PubMed:11331604,ECO:0000269|PubMed:12200444,ECO:0000269|PubMed:12520306,ECO:0000269|PubMed:15240822,ECO:0000269|PubMed:9702190;Dbxref=PMID:10360183,PMID:11226276,PMID:11331604,PMID:12200444,PMID:12520306,PMID:15240822,PMID:9702190 +##sequence-region P47821 1 323 +P47821 UniProtKB Chain 1 323 . . . ID=PRO_0000080428;Note=RNA polymerase II holoenzyme cyclin-like subunit +P47821 UniProtKB Domain 45 176 . . . Note=Cyclin N-terminal +##sequence-region P22213 1 666 +P22213 UniProtKB Chain 1 666 . . . ID=PRO_0000206299;Note=Protein SLY1 +P22213 UniProtKB Repeat 106 142 . . . Note=1 +P22213 UniProtKB Repeat 220 257 . . . Note=2 +P22213 UniProtKB Repeat 436 474 . . . Note=3 +P22213 UniProtKB Repeat 478 514 . . . Note=4 +P22213 UniProtKB Region 106 514 . . . Note=4 X approximate repeats +P22213 UniProtKB Natural variant 532 532 . . . Note=In SLY1-20 mutant. E->K +P22213 UniProtKB Helix 14 26 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Turn 27 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 43 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 54 58 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 60 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Turn 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 72 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 80 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 93 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 106 118 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 121 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 134 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 150 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 153 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 163 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 170 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 178 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 185 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 191 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 215 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 220 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 223 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 260 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 266 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 271 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 280 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 295 297 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 317 319 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 328 331 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 332 335 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 336 360 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 388 412 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Turn 413 415 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 417 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 429 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 447 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 467 478 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Turn 479 481 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 486 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 529 533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Turn 534 536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 540 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 543 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 557 566 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 573 579 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 582 585 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 589 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 593 595 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 604 611 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 616 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Beta strand 635 643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +P22213 UniProtKB Helix 646 659 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1MQS +##sequence-region P38778 1 549 +P38778 UniProtKB Chain 1 549 . . . ID=PRO_0000212606;Note=Manganese transporter SMF2 +P38778 UniProtKB Transmembrane 91 109 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38778 UniProtKB Transmembrane 130 147 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38778 UniProtKB Transmembrane 161 185 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38778 UniProtKB Transmembrane 196 214 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38778 UniProtKB Transmembrane 312 332 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38778 UniProtKB Transmembrane 350 372 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38778 UniProtKB Transmembrane 432 452 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38778 UniProtKB Transmembrane 521 541 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07549 1 140 +Q07549 UniProtKB Chain 1 140 . . . ID=PRO_0000193988;Note=Protein SNA4 +Q07549 UniProtKB Topological domain 1 8 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07549 UniProtKB Transmembrane 9 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07549 UniProtKB Topological domain 30 41 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07549 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07549 UniProtKB Topological domain 63 140 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07549 UniProtKB Modified residue 134 134 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q07549 UniProtKB Lipidation 2 2 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107 +Q07549 UniProtKB Lipidation 3 3 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107 +Q07549 UniProtKB Lipidation 5 5 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107 +Q07549 UniProtKB Lipidation 7 7 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107 +Q07549 UniProtKB Lipidation 8 8 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16751107;Dbxref=PMID:16751107 +Q07549 UniProtKB Cross-link 128 128 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q04477 1 213 +Q04477 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q04477 UniProtKB Chain 2 213 . . . ID=PRO_0000203294;Note=Kinetochore protein SPC24 +Q04477 UniProtKB Coiled coil 54 123 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04477 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q04477 UniProtKB Helix 11 20 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +Q04477 UniProtKB Helix 24 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +Q04477 UniProtKB Helix 157 167 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J +Q04477 UniProtKB Beta strand 170 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J +Q04477 UniProtKB Helix 174 176 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J +Q04477 UniProtKB Beta strand 178 181 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J +Q04477 UniProtKB Turn 185 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +Q04477 UniProtKB Beta strand 190 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J +Q04477 UniProtKB Turn 197 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FV4 +Q04477 UniProtKB Helix 200 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J +##sequence-region P40014 1 221 +P40014 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40014 UniProtKB Chain 2 221 . . . ID=PRO_0000202622;Note=Kinetochore protein SPC25 +P40014 UniProtKB Coiled coil 9 112 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40014 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40014 UniProtKB Helix 4 6 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P40014 UniProtKB Helix 7 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5TCS +P40014 UniProtKB Helix 133 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J +P40014 UniProtKB Beta strand 147 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J +P40014 UniProtKB Beta strand 153 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J +P40014 UniProtKB Beta strand 158 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J +P40014 UniProtKB Beta strand 169 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J +P40014 UniProtKB Beta strand 175 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J +P40014 UniProtKB Beta strand 180 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J +P40014 UniProtKB Helix 190 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J +P40014 UniProtKB Helix 206 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5T6J +##sequence-region P39723 1 622 +P39723 UniProtKB Chain 1 622 . . . ID=PRO_0000202421;Note=Spindle pole component SPC72 +P39723 UniProtKB Sequence conflict 302 302 . . . Note=N->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P42933 1 373 +P42933 UniProtKB Chain 1 373 . . . ID=PRO_0000203324;Note=Stationary phase protein 5 +P42933 UniProtKB Sequence conflict 43 43 . . . Note=N->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P42933 UniProtKB Sequence conflict 47 50 . . . Note=FVTW->LALG;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P17122 1 198 +P17122 UniProtKB Chain 1 198 . . . ID=PRO_0000072136;Note=Sporulation-specific protein 16 +##sequence-region Q03012 1 353 +Q03012 UniProtKB Chain 1 353 . . . ID=PRO_0000059338;Note=COMPASS component SPP1 +Q03012 UniProtKB Zinc finger 22 72 . . . Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 +Q03012 UniProtKB Compositional bias 246 251 . . . Note=Poly-Lys +Q03012 UniProtKB Modified residue 87 87 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P25380 1 463 +P25380 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25380 UniProtKB Chain 26 440 . . . ID=PRO_0000202550;Note=Sporulation-specific protein 22 +P25380 UniProtKB Propeptide 441 463 . . . ID=PRO_0000277472;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25380 UniProtKB Repeat 127 147 . . . Note=LRR 1 +P25380 UniProtKB Repeat 185 206 . . . Note=LRR 2 +P25380 UniProtKB Repeat 207 233 . . . Note=LRR 3 +P25380 UniProtKB Repeat 251 275 . . . Note=LRR 4 +P25380 UniProtKB Repeat 302 325 . . . Note=LRR 5 +P25380 UniProtKB Lipidation 440 440 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25380 UniProtKB Glycosylation 256 256 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25380 UniProtKB Glycosylation 314 314 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25380 UniProtKB Glycosylation 327 327 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P35208 1 640 +P35208 UniProtKB Chain 1 640 . . . ID=PRO_0000072160;Note=Protein SPT10 +P35208 UniProtKB Domain 121 259 . . . Note=N-acetyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00532 +P35208 UniProtKB Mutagenesis 388 388 . . . Note=Loss of complementation of the suppression phenotype. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8138180;Dbxref=PMID:8138180 +##sequence-region P27692 1 1063 +P27692 UniProtKB Chain 1 1063 . . . ID=PRO_0000208477;Note=Transcription elongation factor SPT5 +P27692 UniProtKB Domain 382 415 . . . Note=KOW 1 +P27692 UniProtKB Domain 533 560 . . . Note=KOW 2 +P27692 UniProtKB Domain 584 615 . . . Note=KOW 3 +P27692 UniProtKB Domain 799 832 . . . Note=KOW 4 +P27692 UniProtKB Repeat 931 936 . . . Note=1 +P27692 UniProtKB Repeat 937 942 . . . Note=2 +P27692 UniProtKB Repeat 948 953 . . . Note=3 +P27692 UniProtKB Repeat 958 963 . . . Note=4 +P27692 UniProtKB Repeat 969 974 . . . Note=5 +P27692 UniProtKB Repeat 975 980 . . . Note=6 +P27692 UniProtKB Repeat 981 986 . . . Note=7 +P27692 UniProtKB Repeat 987 992 . . . Note=8 +P27692 UniProtKB Repeat 1000 1005 . . . Note=9 +P27692 UniProtKB Repeat 1009 1014 . . . Note=10 +P27692 UniProtKB Repeat 1015 1020 . . . Note=11 +P27692 UniProtKB Repeat 1032 1037 . . . Note=12 +P27692 UniProtKB Repeat 1043 1048 . . . Note=13 +P27692 UniProtKB Repeat 1052 1057 . . . Note=14 +P27692 UniProtKB Repeat 1058 1063 . . . Note=15 +P27692 UniProtKB Region 931 1063 . . . Note=15 X 6 AA tandem repeats of S-[TA]-W-G-G-[AQ] +P27692 UniProtKB Compositional bias 148 167 . . . Note=Asp/Glu-rich (acidic) +P27692 UniProtKB Compositional bias 189 199 . . . Note=Asp/Glu-rich (acidic) +P27692 UniProtKB Modified residue 35 35 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P27692 UniProtKB Modified residue 133 133 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P27692 UniProtKB Modified residue 136 136 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P27692 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P27692 UniProtKB Modified residue 219 219 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P27692 UniProtKB Beta strand 387 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK +P27692 UniProtKB Turn 394 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK +P27692 UniProtKB Beta strand 399 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK +P27692 UniProtKB Beta strand 409 416 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK +P27692 UniProtKB Turn 422 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK +P27692 UniProtKB Helix 442 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK +P27692 UniProtKB Helix 453 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK +P27692 UniProtKB Helix 461 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK +P27692 UniProtKB Beta strand 464 468 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK +P27692 UniProtKB Beta strand 471 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK +P27692 UniProtKB Beta strand 477 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK +P27692 UniProtKB Beta strand 483 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK +P27692 UniProtKB Helix 490 492 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK +P27692 UniProtKB Helix 502 507 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTK +P27692 UniProtKB Beta strand 539 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL +P27692 UniProtKB Turn 546 549 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL +P27692 UniProtKB Beta strand 551 566 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL +P27692 UniProtKB Beta strand 573 576 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL +P27692 UniProtKB Helix 577 579 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL +P27692 UniProtKB Beta strand 580 582 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL +P27692 UniProtKB Beta strand 589 592 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL +P27692 UniProtKB Turn 596 599 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL +P27692 UniProtKB Beta strand 601 608 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL +P27692 UniProtKB Beta strand 611 616 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL +P27692 UniProtKB Turn 617 619 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL +P27692 UniProtKB Beta strand 620 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL +P27692 UniProtKB Helix 627 629 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YTL +##sequence-region P39015 1 273 +P39015 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7 +P39015 UniProtKB Chain 2 273 . . . ID=PRO_0000072278;Note=Suppressor protein STM1 +P39015 UniProtKB Compositional bias 38 54 . . . Note=Pro-rich +P39015 UniProtKB Compositional bias 77 102 . . . Note=Ser/Thr-rich +P39015 UniProtKB Compositional bias 119 141 . . . Note=Ala-rich +P39015 UniProtKB Compositional bias 147 164 . . . Note=Asn/Gln-rich +P39015 UniProtKB Compositional bias 225 250 . . . Note=Arg/Asn/Gly-rich +P39015 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7 +P39015 UniProtKB Modified residue 55 55 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P39015 UniProtKB Modified residue 118 118 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P39015 UniProtKB Modified residue 229 229 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P39015 UniProtKB Cross-link 46 46 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P39015 UniProtKB Cross-link 121 121 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P39015 UniProtKB Cross-link 171 171 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P39015 UniProtKB Cross-link 184 184 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P39015 UniProtKB Sequence conflict 133 133 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39015 UniProtKB Sequence conflict 171 171 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39015 UniProtKB Sequence conflict 177 177 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39015 UniProtKB Helix 44 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P39015 UniProtKB Helix 56 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P39015 UniProtKB Helix 67 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P39015 UniProtKB Helix 78 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P39015 UniProtKB Beta strand 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P39015 UniProtKB Beta strand 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U56 +P39015 UniProtKB Helix 103 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P39015 UniProtKB Helix 113 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P39015 UniProtKB Helix 116 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +P39015 UniProtKB Turn 136 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3U +P39015 UniProtKB Helix 156 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U4R +##sequence-region Q05937 1 343 +Q05937 UniProtKB Chain 1 343 . . . ID=PRO_0000270565;Note=Zinc finger protein STP3 +Q05937 UniProtKB Zinc finger 169 191 . . . Note=C2H2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q05937 UniProtKB Compositional bias 36 111 . . . Note=Ser-rich +Q05937 UniProtKB Modified residue 71 71 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q05937 UniProtKB Modified residue 111 111 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +##sequence-region Q07351 1 490 +Q07351 UniProtKB Chain 1 490 . . . ID=PRO_0000270566;Note=Zinc finger protein STP4 +Q07351 UniProtKB Zinc finger 304 326 . . . Note=C2H2-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q07351 UniProtKB Modified residue 153 153 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07351 UniProtKB Modified residue 155 155 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38163 1 1010 +P38163 UniProtKB Chain 1 1010 . . . ID=PRO_0000051221;Note=Lethal(2) giant larvae protein homolog SRO77 +P38163 UniProtKB Repeat 47 80 . . . Note=WD 1 +P38163 UniProtKB Repeat 87 122 . . . Note=WD 2 +P38163 UniProtKB Repeat 127 163 . . . Note=WD 3 +P38163 UniProtKB Repeat 182 215 . . . Note=WD 4 +P38163 UniProtKB Repeat 240 275 . . . Note=WD 5 +P38163 UniProtKB Repeat 299 364 . . . Note=WD 6 +P38163 UniProtKB Repeat 372 407 . . . Note=WD 7 +P38163 UniProtKB Repeat 431 504 . . . Note=WD 8 +P38163 UniProtKB Repeat 518 595 . . . Note=WD 9 +P38163 UniProtKB Repeat 602 637 . . . Note=WD 10 +P38163 UniProtKB Repeat 649 700 . . . Note=WD 11 +P38163 UniProtKB Repeat 709 763 . . . Note=WD 12 +P38163 UniProtKB Repeat 768 815 . . . Note=WD 13 +P38163 UniProtKB Repeat 829 852 . . . Note=WD 14 +P38163 UniProtKB Sequence conflict 130 130 . . . Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38163 UniProtKB Sequence conflict 130 130 . . . Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38163 UniProtKB Sequence conflict 135 135 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38163 UniProtKB Sequence conflict 135 135 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38163 UniProtKB Sequence conflict 260 260 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38163 UniProtKB Sequence conflict 260 260 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38163 UniProtKB Sequence conflict 834 834 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38163 UniProtKB Sequence conflict 834 834 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38163 UniProtKB Sequence conflict 858 858 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38163 UniProtKB Sequence conflict 858 858 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38163 UniProtKB Sequence conflict 943 943 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38163 UniProtKB Sequence conflict 943 943 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12038 1 1033 +Q12038 UniProtKB Chain 1 1033 . . . ID=PRO_0000072008;Note=Lethal(2) giant larvae protein homolog SRO7 +Q12038 UniProtKB Repeat 81 114 . . . Note=WD 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788 +Q12038 UniProtKB Repeat 121 156 . . . Note=WD 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788 +Q12038 UniProtKB Repeat 161 197 . . . Note=WD 3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788 +Q12038 UniProtKB Repeat 216 249 . . . Note=WD 4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788 +Q12038 UniProtKB Repeat 274 309 . . . Note=WD 5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788 +Q12038 UniProtKB Repeat 333 397 . . . Note=WD 6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788 +Q12038 UniProtKB Repeat 405 440 . . . Note=WD 7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788 +Q12038 UniProtKB Repeat 464 538 . . . Note=WD 8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788 +Q12038 UniProtKB Repeat 552 631 . . . Note=WD 9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788 +Q12038 UniProtKB Repeat 638 673 . . . Note=WD 10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788 +Q12038 UniProtKB Repeat 685 736 . . . Note=WD 11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788 +Q12038 UniProtKB Repeat 745 799 . . . Note=WD 12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788 +Q12038 UniProtKB Repeat 804 851 . . . Note=WD 13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788 +Q12038 UniProtKB Repeat 865 888 . . . Note=WD 14;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392788;Dbxref=PMID:17392788 +Q12038 UniProtKB Compositional bias 49 52 . . . Note=Poly-Ser +Q12038 UniProtKB Modified residue 591 591 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12038 UniProtKB Modified residue 602 602 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12038 UniProtKB Beta strand 66 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 80 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Turn 87 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 91 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 99 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 110 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 121 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Turn 128 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 131 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 140 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Turn 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 150 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 161 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 171 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 182 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Turn 187 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 191 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Helix 200 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 207 209 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 216 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 223 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 235 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Turn 240 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 244 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 274 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 283 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 295 299 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Turn 300 302 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 305 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 333 341 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 347 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 365 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Helix 376 378 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Helix 381 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 392 397 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 400 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 405 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Helix 417 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 425 431 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 436 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Turn 441 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Helix 450 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Helix 455 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Turn 461 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 464 473 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Helix 474 482 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 505 514 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 517 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Turn 528 532 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 535 538 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Helix 539 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 546 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 551 557 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Turn 558 561 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 562 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 572 579 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Helix 603 605 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 609 612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Helix 614 616 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 622 631 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 637 643 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 647 653 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 656 662 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Turn 663 666 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 667 673 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Helix 674 676 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 685 694 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 698 709 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 712 721 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Helix 723 725 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 727 736 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 745 750 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Turn 751 753 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Helix 761 765 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Helix 766 769 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 775 780 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 782 788 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 795 799 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 804 815 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 817 819 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 821 831 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 834 840 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Turn 841 843 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 846 851 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Helix 858 861 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 872 875 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Beta strand 877 888 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Turn 915 917 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Helix 927 935 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +Q12038 UniProtKB Helix 945 949 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OAJ +##sequence-region P32583 1 406 +P32583 UniProtKB Chain 1 406 . . . ID=PRO_0000072192;Note=Suppressor protein SRP40 +P32583 UniProtKB Compositional bias 25 314 . . . Note=Asp/Ser-rich +P32583 UniProtKB Modified residue 133 133 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P32583 UniProtKB Modified residue 289 289 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P32583 UniProtKB Modified residue 293 293 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32583 UniProtKB Modified residue 394 394 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 +P32583 UniProtKB Sequence conflict 400 400 . . . Note=G->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38931 1 1420 +P38931 UniProtKB Chain 1 1420 . . . ID=PRO_0000072215;Note=Mediator of RNA polymerase II transcription subunit 13 +P38931 UniProtKB Compositional bias 526 529 . . . Note=Poly-Asn +P38931 UniProtKB Compositional bias 657 664 . . . Note=Poly-Glu +P38931 UniProtKB Compositional bias 813 816 . . . Note=Poly-Ser +P38931 UniProtKB Compositional bias 1005 1008 . . . Note=Poly-Leu +P38931 UniProtKB Compositional bias 1121 1136 . . . Note=Poly-Gln +P38931 UniProtKB Modified residue 370 370 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P38931 UniProtKB Modified residue 375 375 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38931 UniProtKB Modified residue 425 425 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38931 UniProtKB Modified residue 601 601 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38931 UniProtKB Modified residue 608 608 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:15225552;Dbxref=PMID:19779198,PMID:15225552 +P38931 UniProtKB Modified residue 636 636 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38931 UniProtKB Modified residue 748 748 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38931 UniProtKB Mutagenesis 608 608 . . . Note=Loss of function%3B when associated with A-1236. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15225552;Dbxref=PMID:15225552 +P38931 UniProtKB Mutagenesis 1236 1236 . . . Note=Loss of function%3B when associated with A-608. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15225552;Dbxref=PMID:15225552 +P38931 UniProtKB Sequence conflict 38 38 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38931 UniProtKB Sequence conflict 812 812 . . . Note=E->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38931 UniProtKB Sequence conflict 859 859 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38931 UniProtKB Sequence conflict 877 878 . . . Note=VK->GE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38931 UniProtKB Sequence conflict 887 887 . . . Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38931 UniProtKB Sequence conflict 1284 1284 . . . Note=Y->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38871 1 571 +P38871 UniProtKB Chain 1 571 . . . ID=PRO_0000072216;Note=Sporulation-specific protein 1 +P38871 UniProtKB Coiled coil 469 486 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38871 UniProtKB Coiled coil 542 566 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P37296 1 890 +P37296 UniProtKB Chain 1 890 . . . ID=PRO_0000119225;Note=V-type proton ATPase subunit a%2C Golgi isoform +P37296 UniProtKB Topological domain 1 450 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Transmembrane 451 469 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Topological domain 470 471 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Transmembrane 472 488 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Topological domain 489 502 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Transmembrane 503 532 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Topological domain 533 580 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Transmembrane 581 600 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Topological domain 601 618 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Transmembrane 619 639 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Topological domain 640 682 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Transmembrane 683 702 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Topological domain 703 779 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Transmembrane 780 804 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Topological domain 805 828 . . . Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Transmembrane 829 867 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Topological domain 868 890 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Coiled coil 113 154 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Coiled coil 297 347 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P37296 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P37296 UniProtKB Modified residue 223 223 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P37296 UniProtKB Modified residue 228 228 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P37296 UniProtKB Sequence conflict 805 805 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P31377 1 255 +P31377 UniProtKB Chain 1 255 . . . ID=PRO_0000210281;Note=Syntaxin-8 +P31377 UniProtKB Topological domain 1 234 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31377 UniProtKB Transmembrane 235 255 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P31377 UniProtKB Domain 164 228 . . . Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202 +P31377 UniProtKB Lipidation 238 238 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53598 1 329 +P53598 UniProtKB Transit peptide 1 24 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03222 +P53598 UniProtKB Chain 25 329 . . . ID=PRO_0000033351;Note=Succinate--CoA ligase [ADP-forming] subunit alpha%2C mitochondrial;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03222 +P53598 UniProtKB Region 45 48 . . . Note=Coenzyme A binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03222 +P53598 UniProtKB Region 124 126 . . . Note=Coenzyme A binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03222 +P53598 UniProtKB Active site 284 284 . . . Note=Tele-phosphohistidine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03222 +P53598 UniProtKB Binding site 71 71 . . . Note=Coenzyme A;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03222 +P53598 UniProtKB Binding site 189 189 . . . Note=Substrate%3B shared with subunit beta;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03222 +##sequence-region P36126 1 1683 +P36126 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +P36126 UniProtKB Chain 2 1683 . . . ID=PRO_0000218825;Note=Phospholipase D1 +P36126 UniProtKB Domain 291 487 . . . Note=PX +P36126 UniProtKB Domain 496 664 . . . Note=PH +P36126 UniProtKB Domain 791 818 . . . Note=PLD phosphodiesterase 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153 +P36126 UniProtKB Domain 1091 1118 . . . Note=PLD phosphodiesterase 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153 +P36126 UniProtKB Compositional bias 255 280 . . . Note=Asn-rich +P36126 UniProtKB Compositional bias 405 410 . . . Note=Poly-Asn +P36126 UniProtKB Compositional bias 628 633 . . . Note=Poly-Leu +P36126 UniProtKB Active site 796 796 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153 +P36126 UniProtKB Active site 798 798 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153 +P36126 UniProtKB Active site 803 803 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153 +P36126 UniProtKB Active site 1096 1096 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153 +P36126 UniProtKB Active site 1098 1098 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153 +P36126 UniProtKB Active site 1103 1103 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00153 +P36126 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:22814378;Dbxref=PMID:15665377,PMID:22814378 +P36126 UniProtKB Modified residue 8 8 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P36126 UniProtKB Modified residue 30 30 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P36126 UniProtKB Modified residue 145 145 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36126 UniProtKB Modified residue 1461 1461 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36126 UniProtKB Modified residue 1462 1462 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P33757 1 523 +P33757 UniProtKB Chain 1 523 . . . ID=PRO_0000202524;Note=Sporulation protein 23 +##sequence-region Q07798 1 868 +Q07798 UniProtKB Chain 1 868 . . . ID=PRO_0000072143;Note=Sporulation-specific protein 75 +Q07798 UniProtKB Topological domain 1 34 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Transmembrane 35 55 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Topological domain 56 127 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Transmembrane 128 148 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Topological domain 149 187 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Transmembrane 188 208 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Topological domain 209 481 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Transmembrane 482 502 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Topological domain 503 527 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Transmembrane 528 548 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Topological domain 549 569 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Transmembrane 570 590 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Topological domain 591 611 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Transmembrane 612 632 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Topological domain 633 660 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Transmembrane 661 683 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Topological domain 684 692 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Transmembrane 693 713 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Topological domain 714 730 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Transmembrane 731 751 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Topological domain 752 753 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Transmembrane 754 774 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Topological domain 775 868 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Glycosylation 2 2 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Glycosylation 184 184 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07798 UniProtKB Glycosylation 503 503 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04921 1 423 +Q04921 UniProtKB Chain 1 423 . . . ID=PRO_0000173501;Note=Sporulation-regulated protein 28 +Q04921 UniProtKB Domain 28 342 . . . Note=Septin-type G +Q04921 UniProtKB Nucleotide binding 38 45 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04921 UniProtKB Nucleotide binding 204 212 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04921 UniProtKB Coiled coil 384 417 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04921 UniProtKB Compositional bias 60 68 . . . Note=Poly-Asp +Q04921 UniProtKB Binding site 124 124 . . . Note=GTP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q04921 UniProtKB Binding site 291 291 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P08459 1 502 +P08459 UniProtKB Signal peptide 1 56 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08459 UniProtKB Chain 57 475 . . . ID=PRO_0000033195;Note=Sporulation-specific protein 2 +P08459 UniProtKB Propeptide 476 502 . . . ID=PRO_0000277471;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08459 UniProtKB Lipidation 475 475 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08459 UniProtKB Glycosylation 77 77 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08459 UniProtKB Glycosylation 135 135 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08459 UniProtKB Glycosylation 285 285 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08459 UniProtKB Glycosylation 303 303 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08459 UniProtKB Glycosylation 340 340 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08459 UniProtKB Glycosylation 343 343 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08459 UniProtKB Glycosylation 355 355 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P08459 UniProtKB Sequence conflict 203 203 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08459 UniProtKB Sequence conflict 210 210 . . . Note=I->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08459 UniProtKB Sequence conflict 324 324 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P09007 1 221 +P09007 UniProtKB Chain 1 221 . . . ID=PRO_0000083482;Note=Pre-rRNA-processing protein SRD1 +P09007 UniProtKB Zinc finger 168 193 . . . Note=GATA-type +P09007 UniProtKB Sequence conflict 106 106 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09007 UniProtKB Sequence conflict 192 192 . . . Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38789 1 453 +P38789 UniProtKB Chain 1 453 . . . ID=PRO_0000120259;Note=Ribosome biogenesis protein SSF1 +P38789 UniProtKB Domain 26 348 . . . Note=Brix;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00034 +P38789 UniProtKB Modified residue 301 301 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P39926 1 295 +P39926 UniProtKB Chain 1 295 . . . ID=PRO_0000210275;Note=Protein SSO2 +P39926 UniProtKB Topological domain 1 269 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39926 UniProtKB Transmembrane 270 291 . . . Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39926 UniProtKB Topological domain 292 295 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39926 UniProtKB Domain 194 256 . . . Note=t-SNARE coiled-coil homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00202 +P39926 UniProtKB Coiled coil 39 100 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39926 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39926 UniProtKB Modified residue 34 34 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P39926 UniProtKB Sequence conflict 222 222 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P39926 UniProtKB Helix 36 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M4Y +P39926 UniProtKB Helix 74 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M4Y +P39926 UniProtKB Turn 109 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LG4 +P39926 UniProtKB Helix 113 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M4Y +P39926 UniProtKB Beta strand 157 159 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LG4 +P39926 UniProtKB Helix 161 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M4Y +P39926 UniProtKB Beta strand 169 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M4Y +P39926 UniProtKB Turn 174 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5LG4 +P39926 UniProtKB Helix 192 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5M4Y +##sequence-region Q03770 1 852 +Q03770 UniProtKB Chain 1 852 . . . ID=PRO_0000054164;Note=SPS-sensor component SSY1 +Q03770 UniProtKB Topological domain 1 285 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Transmembrane 286 306 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Topological domain 307 329 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Transmembrane 330 350 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Topological domain 351 357 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Transmembrane 358 378 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Topological domain 379 400 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Transmembrane 401 421 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Topological domain 422 422 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Transmembrane 423 443 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Topological domain 444 500 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Transmembrane 501 521 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Topological domain 522 540 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Transmembrane 541 561 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Topological domain 562 623 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Transmembrane 624 644 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Topological domain 645 673 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Transmembrane 674 694 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Topological domain 695 703 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Transmembrane 704 724 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Topological domain 725 755 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Transmembrane 756 776 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Topological domain 777 784 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Transmembrane 785 805 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Topological domain 806 852 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03770 UniProtKB Mutagenesis 382 382 . . . Note=Constitutively active%2C up-regulates amino acid permease transcription in response to subthreshold concentrations of amino acids. T->H%2CL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14555474;Dbxref=PMID:14555474 +Q03770 UniProtKB Mutagenesis 382 382 . . . Note=In SSY1-102%3B constitutively active%2C up-regulates amino acid permease transcription in the absence of amino-acids. T->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14555474;Dbxref=PMID:14555474 +Q03770 UniProtKB Mutagenesis 382 382 . . . Note=Constitutively active%2C up-regulates amino acid permease transcription in the absence of amino acids. T->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14555474;Dbxref=PMID:14555474 +##sequence-region P38788 1 538 +P38788 UniProtKB Chain 1 538 . . . ID=PRO_0000078400;Note=Ribosome-associated complex subunit SSZ1 +P38788 UniProtKB Region 400 538 . . . Note=Peptide-binding domain;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38788 UniProtKB Modified residue 477 477 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P38788 UniProtKB Modified residue 480 480 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P38788 UniProtKB Mutagenesis 295 295 . . . Note=Increases readthrough in translation termination. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15456889;Dbxref=PMID:15456889 +P38788 UniProtKB Sequence conflict 208 208 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25379 1 360 +P25379 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P25379 UniProtKB Chain 2 360 . . . ID=PRO_0000185598;Note=Catabolic L-serine/threonine dehydratase +P25379 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P25379 UniProtKB Modified residue 37 37 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P25379 UniProtKB Sequence conflict 34 34 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25379 UniProtKB Sequence conflict 268 268 . . . Note=T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25379 UniProtKB Sequence conflict 317 318 . . . Note=GG->AS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P33894 1 931 +P33894 UniProtKB Chain 1 931 . . . ID=PRO_0000122420;Note=Dipeptidyl aminopeptidase A +P33894 UniProtKB Topological domain 1 119 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33894 UniProtKB Transmembrane 120 140 . . . Note=Helical%3B Signal-anchor for type II membrane protein +P33894 UniProtKB Topological domain 141 931 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33894 UniProtKB Active site 785 785 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33894 UniProtKB Active site 863 863 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33894 UniProtKB Active site 896 896 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P33894 UniProtKB Glycosylation 377 377 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33894 UniProtKB Glycosylation 814 814 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53538 1 206 +P53538 UniProtKB Chain 1 206 . . . ID=PRO_0000072230;Note=RNA polymerase II subunit A C-terminal domain phosphatase SSU72 +P53538 UniProtKB Sequence conflict 199 199 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53101 1 465 +P53101 UniProtKB Chain 1 465 . . . ID=PRO_0000114764;Note=Cystathionine beta-lyase +P53101 UniProtKB Modified residue 213 213 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q12325 1 893 +Q12325 UniProtKB Chain 1 893 . . . ID=PRO_0000080185;Note=Sulfate permease 2 +Q12325 UniProtKB Topological domain 1 131 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Transmembrane 132 152 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Topological domain 153 163 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Transmembrane 164 184 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Topological domain 185 188 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Transmembrane 189 209 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Topological domain 210 221 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Transmembrane 222 242 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Topological domain 243 244 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Transmembrane 245 265 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Topological domain 266 305 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Transmembrane 306 326 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Topological domain 327 350 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Transmembrane 351 371 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Topological domain 372 399 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Transmembrane 400 420 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Topological domain 421 443 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Transmembrane 444 464 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Topological domain 465 483 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Transmembrane 484 504 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Topological domain 505 532 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Transmembrane 533 551 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Topological domain 552 559 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Transmembrane 560 580 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Topological domain 581 893 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12325 UniProtKB Domain 676 854 . . . Note=STAS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00198 +##sequence-region P46676 1 1062 +P46676 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P46676 UniProtKB Chain 2 1062 . . . ID=PRO_0000072311;Note=Suppressor of mar1-1 protein +P46676 UniProtKB Compositional bias 464 467 . . . Note=Poly-Asn +P46676 UniProtKB Compositional bias 514 523 . . . Note=Poly-Ala +P46676 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P46676 UniProtKB Modified residue 378 378 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46676 UniProtKB Modified residue 379 379 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46676 UniProtKB Modified residue 628 628 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P46676 UniProtKB Modified residue 681 681 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P46676 UniProtKB Modified residue 697 697 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P46676 UniProtKB Modified residue 712 712 . . . Note=Phosphoserine%3B by ATM or ATR;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46676 UniProtKB Modified residue 738 738 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P46676 UniProtKB Modified residue 817 817 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P46676 UniProtKB Mutagenesis 988 988 . . . Note=Loss of function. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8754829;Dbxref=PMID:8754829 +P46676 UniProtKB Sequence conflict 1 20 . . . Note=MSENTTAPSDNITNEQRLPS->MNRDFRL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46676 UniProtKB Sequence conflict 30 30 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46676 UniProtKB Sequence conflict 408 408 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46676 UniProtKB Sequence conflict 523 523 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46676 UniProtKB Sequence conflict 826 826 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P36150 1 593 +P36150 UniProtKB Chain 1 593 . . . ID=PRO_0000150387;Note=Uroporphyrinogen-III C-methyltransferase +##sequence-region P53616 1 420 +P53616 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9748433;Dbxref=PMID:9748433 +P53616 UniProtKB Chain 25 420 . . . ID=PRO_0000033466;Note=Probable secreted beta-glucosidase SUN4 +P53616 UniProtKB Compositional bias 31 148 . . . Note=Ser/Thr-rich +P53616 UniProtKB Compositional bias 336 339 . . . Note=Poly-Ser +P53616 UniProtKB Glycosylation 395 395 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53616 UniProtKB Sequence conflict 299 299 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P33300 1 382 +P33300 UniProtKB Chain 1 382 . . . ID=PRO_0000072314;Note=Mannosyl phosphorylinositol ceramide synthase SUR1 +P33300 UniProtKB Topological domain 1 6 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33300 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33300 UniProtKB Topological domain 28 269 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33300 UniProtKB Transmembrane 270 290 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33300 UniProtKB Topological domain 291 382 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P33300 UniProtKB Modified residue 349 349 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P54003 1 302 +P54003 UniProtKB Chain 1 302 . . . ID=PRO_0000072317;Note=Protein SUR7 +P54003 UniProtKB Topological domain 1 10 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54003 UniProtKB Transmembrane 11 31 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54003 UniProtKB Topological domain 32 114 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54003 UniProtKB Transmembrane 115 135 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54003 UniProtKB Topological domain 136 145 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54003 UniProtKB Transmembrane 146 166 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54003 UniProtKB Topological domain 167 189 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54003 UniProtKB Transmembrane 190 210 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54003 UniProtKB Topological domain 211 302 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P54003 UniProtKB Modified residue 293 293 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P54003 UniProtKB Modified residue 301 301 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:19779198 +P54003 UniProtKB Glycosylation 47 47 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53937 1 143 +P53937 UniProtKB Chain 1 143 . . . ID=PRO_0000132210;Note=37S ribosomal protein SWS2%2C mitochondrial +##sequence-region Q08553 1 188 +Q08553 UniProtKB Chain 1 188 . . . ID=PRO_0000076351;Note=Protein SYC1 +##sequence-region P04802 1 557 +P04802 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:3902099,ECO:0000269|PubMed:9298649;Dbxref=PMID:3902099,PMID:9298649 +P04802 UniProtKB Chain 2 557 . . . ID=PRO_0000111014;Note=Aspartate--tRNA ligase%2C cytoplasmic +P04802 UniProtKB Nucleotide binding 325 327 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04802 UniProtKB Nucleotide binding 333 335 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04802 UniProtKB Nucleotide binding 528 531 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04802 UniProtKB Region 303 306 . . . Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04802 UniProtKB Binding site 281 281 . . . Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04802 UniProtKB Binding site 325 325 . . . Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04802 UniProtKB Binding site 478 478 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04802 UniProtKB Binding site 481 481 . . . Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04802 UniProtKB Binding site 485 485 . . . Note=Aspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04802 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P04802 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P04802 UniProtKB Modified residue 301 301 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P04802 UniProtKB Modified residue 502 502 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P04802 UniProtKB Modified residue 546 546 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P04802 UniProtKB Mutagenesis 273 273 . . . Note=Loss of activity%3B important for dimerization. P->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8248175;Dbxref=PMID:8248175 +P04802 UniProtKB Beta strand 73 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Helix 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Turn 101 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 108 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 122 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 135 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 145 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Helix 151 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 165 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 182 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Helix 208 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Helix 215 220 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Helix 228 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Helix 235 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Helix 242 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 274 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 280 284 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 288 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 294 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Helix 303 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 316 324 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 331 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ASZ +P04802 UniProtKB Beta strand 336 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Helix 352 372 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Helix 374 383 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 393 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ASY +P04802 UniProtKB Beta strand 398 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Helix 402 411 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 418 420 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ASY +P04802 UniProtKB Helix 424 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 441 446 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Helix 450 452 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 461 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ASZ +P04802 UniProtKB Beta strand 466 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 477 485 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Helix 489 498 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Turn 506 508 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Helix 509 515 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 522 528 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Helix 529 536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Helix 542 545 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1EOV +P04802 UniProtKB Beta strand 546 548 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ASY +##sequence-region P48525 1 536 +P48525 UniProtKB Chain 1 536 . . . ID=PRO_0000119740;Note=Glutamate--tRNA ligase%2C mitochondrial +P48525 UniProtKB Nucleotide binding 291 295 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P48525 UniProtKB Region 48 50 . . . Note=Glutamate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P48525 UniProtKB Region 235 239 . . . Note=Glutamate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P48525 UniProtKB Motif 53 61 . . . Note="HIGH" region +P48525 UniProtKB Motif 291 295 . . . Note="KMSKS" region +P48525 UniProtKB Binding site 58 58 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P48525 UniProtKB Binding site 84 84 . . . Note=Glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P48525 UniProtKB Binding site 253 253 . . . Note=Glutamate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P48525 UniProtKB Binding site 256 256 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P48525 UniProtKB Sequence conflict 464 464 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q02875 1 849 +Q02875 UniProtKB Chain 1 849 . . . ID=PRO_0000238645;Note=SMY2 homolog 2 +Q02875 UniProtKB Domain 149 205 . . . Note=GYF;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00101 +Q02875 UniProtKB Coiled coil 410 484 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02875 UniProtKB Compositional bias 637 720 . . . Note=Ser-rich +Q02875 UniProtKB Modified residue 350 350 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P39965 1 576 +P39965 UniProtKB Chain 1 576 . . . ID=PRO_0000139354;Note=Probable proline--tRNA ligase%2C mitochondrial +##sequence-region P54000 1 292 +P54000 UniProtKB Chain 1 292 . . . ID=PRO_0000215951;Note=RNA polymerase II transcriptional coactivator SUB1 +P54000 UniProtKB Modified residue 119 119 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P54000 UniProtKB Modified residue 268 268 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P54000 UniProtKB Modified residue 269 269 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P54000 UniProtKB Modified residue 289 289 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q07478 1 446 +Q07478 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q07478 UniProtKB Chain 2 446 . . . ID=PRO_0000055082;Note=ATP-dependent RNA helicase SUB2 +Q07478 UniProtKB Domain 93 268 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +Q07478 UniProtKB Domain 280 441 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +Q07478 UniProtKB Nucleotide binding 106 113 . . . Note=ATP +Q07478 UniProtKB Motif 62 90 . . . Note=Q motif +Q07478 UniProtKB Motif 215 218 . . . Note=DECD box +Q07478 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q07478 UniProtKB Modified residue 13 13 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q07478 UniProtKB Modified residue 37 37 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q07478 UniProtKB Modified residue 169 169 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q07478 UniProtKB Mutagenesis 8 8 . . . Note=No growth at 37 degrees Celsius%3B when associated with DEL-135. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156603;Dbxref=PMID:11156603 +Q07478 UniProtKB Mutagenesis 22 22 . . . Note=In SUB2-1%3B no growth at 16 and 37 degrees Celsius%3B when associated with G-83%3B M-142 and T-146. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156604;Dbxref=PMID:11156604 +Q07478 UniProtKB Mutagenesis 83 83 . . . Note=In SUB2-1%3B no growth at 16 and 37 degrees Celsius%3B when associated with G-22%3B M-142 and T-146. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156604;Dbxref=PMID:11156604 +Q07478 UniProtKB Mutagenesis 112 112 . . . Note=Lethal. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156602;Dbxref=PMID:11156602 +Q07478 UniProtKB Mutagenesis 122 122 . . . Note=In SUB2-201%3B no growth at 37 degrees Celsius%3B when associated with G-173 and F-403. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156603;Dbxref=PMID:11156603 +Q07478 UniProtKB Mutagenesis 135 135 . . . Note=No growth at 37 degrees Celsius%3B when associated with G-8. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156603;Dbxref=PMID:11156603 +Q07478 UniProtKB Mutagenesis 142 142 . . . Note=In SUB2-1%3B no growth at 16 and 37 degrees Celsius%3B when associated with G-22%3B G-83 and T-146. L->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156604;Dbxref=PMID:11156604 +Q07478 UniProtKB Mutagenesis 146 146 . . . Note=In SUB2-1%3B no growth at 16 and 37 degrees Celsius%3B when associated with G-22%3B G-83 and M-142. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156604;Dbxref=PMID:11156604 +Q07478 UniProtKB Mutagenesis 173 173 . . . Note=In SUB2-201%3B no growth at 37 degrees Celsius%3B when associated with R-122 and F-403. K->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156603;Dbxref=PMID:11156603 +Q07478 UniProtKB Mutagenesis 174 174 . . . Note=In SUB2-100%3B no growth at 37 degrees Celsius. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156602;Dbxref=PMID:11156602 +Q07478 UniProtKB Mutagenesis 215 215 . . . Note=Lethal. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156602;Dbxref=PMID:11156602 +Q07478 UniProtKB Mutagenesis 217 217 . . . Note=Lethal. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156602;Dbxref=PMID:11156602 +Q07478 UniProtKB Mutagenesis 247 247 . . . Note=Lethal. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156602;Dbxref=PMID:11156602 +Q07478 UniProtKB Mutagenesis 308 308 . . . Note=In SUB2-5%3B no growth at 16 degrees Celsius. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156604;Dbxref=PMID:11156604 +Q07478 UniProtKB Mutagenesis 403 403 . . . Note=In SUB2-201%3B no growth at 37 degrees Celsius%3B when associated with R-122 and G-173. K->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11156603;Dbxref=PMID:11156603 +Q07478 UniProtKB Helix 63 67 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 71 79 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 87 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Turn 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Beta strand 102 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Beta strand 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 113 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Beta strand 133 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 140 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Turn 154 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Beta strand 162 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 171 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Turn 181 183 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Beta strand 186 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 192 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Turn 200 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Beta strand 211 215 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 217 222 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 224 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Beta strand 239 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Turn 252 254 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 255 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Beta strand 266 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 273 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Beta strand 281 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 290 292 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 293 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Beta strand 307 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 316 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Beta strand 333 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Beta strand 338 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 342 353 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Beta strand 358 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 364 366 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Beta strand 367 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Beta strand 375 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 387 394 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 399 401 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Beta strand 404 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 413 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +Q07478 UniProtKB Helix 441 443 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5SUP +##sequence-region P31376 1 625 +P31376 UniProtKB Chain 1 625 . . . ID=PRO_0000072344;Note=SWR1-complex protein 3 +P31376 UniProtKB Compositional bias 34 56 . . . Note=Asp-rich +P31376 UniProtKB Compositional bias 175 262 . . . Note=Lys-rich +##sequence-region P53201 1 476 +P53201 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53201 UniProtKB Chain 2 476 . . . ID=PRO_0000072345;Note=SWR1-complex protein 4 +P53201 UniProtKB Domain 156 209 . . . Note=SANT +P53201 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P38326 1 303 +P38326 UniProtKB Chain 1 303 . . . ID=PRO_0000212513;Note=SWR1-complex protein 5 +P38326 UniProtKB Domain 217 294 . . . Note=BCNT-C;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00610 +P38326 UniProtKB Modified residue 209 209 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region Q06707 1 132 +Q06707 UniProtKB Chain 1 132 . . . ID=PRO_0000072346;Note=SWR1-complex protein 7 +##sequence-region P36104 1 329 +P36104 UniProtKB Chain 1 329 . . . ID=PRO_0000051253;Note=COMPASS component SWD2 +P36104 UniProtKB Repeat 25 64 . . . Note=WD 1 +P36104 UniProtKB Repeat 111 150 . . . Note=WD 2 +P36104 UniProtKB Repeat 152 191 . . . Note=WD 3 +P36104 UniProtKB Repeat 199 238 . . . Note=WD 4 +P36104 UniProtKB Repeat 246 287 . . . Note=WD 5 +P36104 UniProtKB Repeat 298 328 . . . Note=WD 6 +##sequence-region Q04175 1 944 +Q04175 UniProtKB Chain 1 944 . . . ID=PRO_0000269756;Note=Importin beta SMX1 +Q04175 UniProtKB Domain 25 97 . . . Note=Importin N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00115 +##sequence-region P15624 1 595 +P15624 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:338359;Dbxref=PMID:338359 +P15624 UniProtKB Chain 2 595 . . . ID=PRO_0000127023;Note=Phenylalanine--tRNA ligase beta subunit +P15624 UniProtKB Domain 292 370 . . . Note=B5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00816 +P15624 UniProtKB Region 86 90 . . . Note=CCA binding of tRNA;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P15624 UniProtKB Sequence conflict 18 18 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15624 UniProtKB Sequence conflict 426 426 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15624 UniProtKB Sequence conflict 544 544 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06817 1 618 +Q06817 UniProtKB Chain 1 618 . . . ID=PRO_0000073006;Note=Glycine--tRNA ligase 2 +Q06817 UniProtKB Nucleotide binding 219 221 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06817 UniProtKB Nucleotide binding 229 234 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06817 UniProtKB Nucleotide binding 347 348 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06817 UniProtKB Nucleotide binding 470 473 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06817 UniProtKB Region 234 238 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06817 UniProtKB Region 466 470 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06817 UniProtKB Binding site 101 101 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06817 UniProtKB Binding site 187 187 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06817 UniProtKB Binding site 325 325 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q06817 UniProtKB Binding site 325 325 . . . Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38088 1 690 +P38088 UniProtKB Transit peptide 1 24 . . . Note=Mitochondrion;Ontology_term=ECO:0000244,ECO:0000255;evidence=ECO:0000244|PubMed:22814378,ECO:0000255;Dbxref=PMID:22814378 +P38088 UniProtKB Chain 25 690 . . . ID=PRO_0000073005;Note=Glycine--tRNA ligase 1%2C mitochondrial +P38088 UniProtKB Nucleotide binding 283 285 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38088 UniProtKB Nucleotide binding 293 298 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38088 UniProtKB Nucleotide binding 410 411 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38088 UniProtKB Nucleotide binding 535 538 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38088 UniProtKB Region 298 302 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38088 UniProtKB Region 531 535 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38088 UniProtKB Binding site 132 132 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38088 UniProtKB Binding site 251 251 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38088 UniProtKB Binding site 388 388 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38088 UniProtKB Binding site 388 388 . . . Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38088 UniProtKB Modified residue 25 25 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P38088 UniProtKB Modified residue 226 226 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 +P38088 UniProtKB Modified residue 476 476 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38088 UniProtKB Modified residue 528 528 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38088 UniProtKB Modified residue 689 689 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38088 UniProtKB Alternative sequence 1 23 . . . ID=VSP_041147;Note=In isoform Cytoplasmic. Missing +P38088 UniProtKB Sequence conflict 586 587 . . . Note=TT->HH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38088 UniProtKB Sequence conflict 586 587 . . . Note=TT->HH;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q6WNK7 1 96 +Q6WNK7 UniProtKB Chain 1 96 . . . ID=PRO_0000227806;Note=Transcription and mRNA export factor SUS1 +Q6WNK7 UniProtKB Cross-link 68 68 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +Q6WNK7 UniProtKB Helix 7 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +Q6WNK7 UniProtKB Helix 21 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +Q6WNK7 UniProtKB Helix 38 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +Q6WNK7 UniProtKB Helix 58 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +Q6WNK7 UniProtKB Helix 75 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3MHS +Q6WNK7 UniProtKB Beta strand 93 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FK5 +##sequence-region P38869 1 228 +P38869 UniProtKB Chain 1 228 . . . ID=PRO_0000202934;Note=Protein SVP26 +P38869 UniProtKB Topological domain 1 1 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38869 UniProtKB Transmembrane 2 22 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38869 UniProtKB Topological domain 23 42 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38869 UniProtKB Transmembrane 43 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38869 UniProtKB Topological domain 60 88 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38869 UniProtKB Transmembrane 89 105 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38869 UniProtKB Topological domain 106 142 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38869 UniProtKB Transmembrane 143 166 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38869 UniProtKB Topological domain 167 228 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38869 UniProtKB Glycosylation 115 115 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39706 1 426 +P39706 UniProtKB Chain 1 426 . . . ID=PRO_0000051251;Note=COMPASS component SWD1 +P39706 UniProtKB Repeat 24 63 . . . Note=WD 1 +P39706 UniProtKB Repeat 70 109 . . . Note=WD 2 +P39706 UniProtKB Repeat 212 251 . . . Note=WD 3 +P39706 UniProtKB Repeat 264 307 . . . Note=WD 4 +P39706 UniProtKB Repeat 310 350 . . . Note=WD 5 +##sequence-region P38123 1 315 +P38123 UniProtKB Chain 1 315 . . . ID=PRO_0000051255;Note=COMPASS component SWD3 +P38123 UniProtKB Repeat 53 93 . . . Note=WD 1 +P38123 UniProtKB Repeat 94 133 . . . Note=WD 2 +P38123 UniProtKB Repeat 136 178 . . . Note=WD 3 +P38123 UniProtKB Repeat 187 228 . . . Note=WD 4 +P38123 UniProtKB Repeat 238 278 . . . Note=WD 5 +P38123 UniProtKB Repeat 285 314 . . . Note=WD 6 +##sequence-region P09547 1 1314 +P09547 UniProtKB Chain 1 1314 . . . ID=PRO_0000200596;Note=SWI/SNF chromatin-remodeling complex subunit SWI1 +P09547 UniProtKB Domain 406 493 . . . Note=ARID;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00355 +P09547 UniProtKB Zinc finger 1241 1258 . . . Note=C4-type +P09547 UniProtKB Region 1 323 . . . Note=Prion domain (PrD) +P09547 UniProtKB Compositional bias 337 524 . . . Note=Gln-rich +P09547 UniProtKB Beta strand 396 398 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LI6 +P09547 UniProtKB Beta strand 402 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LI6 +P09547 UniProtKB Helix 408 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KKX +P09547 UniProtKB Beta strand 426 429 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KKX +P09547 UniProtKB Beta strand 434 437 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KKX +P09547 UniProtKB Helix 442 447 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KKX +P09547 UniProtKB Turn 448 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KKX +P09547 UniProtKB Helix 453 456 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KKX +P09547 UniProtKB Helix 460 469 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KKX +P09547 UniProtKB Helix 474 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KKX +P09547 UniProtKB Turn 492 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KN5 +P09547 UniProtKB Beta strand 498 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1KN5 +##sequence-region P32591 1 825 +P32591 UniProtKB Chain 1 825 . . . ID=PRO_0000197123;Note=SWI/SNF complex subunit SWI3 +P32591 UniProtKB Domain 305 402 . . . Note=SWIRM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00247 +P32591 UniProtKB Domain 522 573 . . . Note=SANT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00624 +P32591 UniProtKB Region 694 722 . . . Note=Leucine-zipper +P32591 UniProtKB Compositional bias 1 304 . . . Note=Asp/Glu-rich (acidic) +P32591 UniProtKB Modified residue 88 88 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32591 UniProtKB Modified residue 185 185 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32591 UniProtKB Modified residue 235 235 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P32591 UniProtKB Modified residue 657 657 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32591 UniProtKB Mutagenesis 374 374 . . . Note=Loss of DNA-binding. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16461455;Dbxref=PMID:16461455 +P32591 UniProtKB Mutagenesis 383 383 . . . Note=Loss of DNA-binding%3B when associated with D-387. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16461455;Dbxref=PMID:16461455 +P32591 UniProtKB Mutagenesis 387 387 . . . Note=Loss of DNA-binding%3B when associated with D-383. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16461455;Dbxref=PMID:16461455 +P32591 UniProtKB Mutagenesis 392 392 . . . Note=Loss of DNA-binding. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16461455;Dbxref=PMID:16461455 +P32591 UniProtKB Helix 321 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FQ3 +P32591 UniProtKB Helix 328 330 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FQ3 +P32591 UniProtKB Helix 340 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FQ3 +P32591 UniProtKB Helix 364 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FQ3 +P32591 UniProtKB Helix 375 387 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FQ3 +P32591 UniProtKB Beta strand 390 393 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2FQ3 +##sequence-region P40825 1 983 +P40825 UniProtKB Transit peptide 1 24 . . . Note=Mitochondrion +P40825 UniProtKB Chain 25 983 . . . ID=PRO_0000075287;Note=Alanine--tRNA ligase%2C mitochondrial +P40825 UniProtKB Metal binding 625 625 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03133 +P40825 UniProtKB Metal binding 629 629 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03133 +P40825 UniProtKB Metal binding 744 744 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03133 +P40825 UniProtKB Metal binding 748 748 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03133 +P40825 UniProtKB Modified residue 504 504 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40825 UniProtKB Modified residue 975 975 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40825 UniProtKB Alternative sequence 1 25 . . . ID=VSP_040236;Note=In isoform Cytoplasmic. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40825 UniProtKB Sequence conflict 4 7 . . . Note=TTGL->NYRI;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40825 UniProtKB Sequence conflict 16 16 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40825 UniProtKB Sequence conflict 161 161 . . . Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40825 UniProtKB Sequence conflict 490 492 . . . Note=KDQ->RTK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40825 UniProtKB Sequence conflict 865 866 . . . Note=FE->LQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40528 1 902 +P40528 UniProtKB Chain 1 902 . . . ID=PRO_0000072382;Note=Protein SYG1 +P40528 UniProtKB Topological domain 1 404 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40528 UniProtKB Transmembrane 405 425 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40528 UniProtKB Topological domain 426 435 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40528 UniProtKB Transmembrane 436 456 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40528 UniProtKB Topological domain 457 497 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40528 UniProtKB Transmembrane 498 518 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40528 UniProtKB Topological domain 519 522 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40528 UniProtKB Transmembrane 523 543 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40528 UniProtKB Topological domain 544 554 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40528 UniProtKB Transmembrane 555 575 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40528 UniProtKB Topological domain 576 576 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40528 UniProtKB Transmembrane 577 599 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40528 UniProtKB Topological domain 600 732 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40528 UniProtKB Transmembrane 733 753 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40528 UniProtKB Topological domain 754 761 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40528 UniProtKB Transmembrane 762 782 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40528 UniProtKB Topological domain 783 902 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40528 UniProtKB Domain 1 303 . . . Note=SPX;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00714 +P40528 UniProtKB Domain 606 815 . . . Note=EXS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00712 +P40528 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40528 UniProtKB Modified residue 179 179 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40528 UniProtKB Modified residue 859 859 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P40528 UniProtKB Modified residue 860 860 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P47002 1 699 +P47002 UniProtKB Propeptide 1 381 . . . ID=PRO_0000377374;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16524914;Dbxref=PMID:16524914 +P47002 UniProtKB Chain 382 699 . . . ID=PRO_0000072232;Note=SPS-sensor serine protease component SSY5 +P47002 UniProtKB Region 459 699 . . . Note=Serine protease +P47002 UniProtKB Active site 465 465 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47002 UniProtKB Active site 545 545 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47002 UniProtKB Active site 640 640 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47002 UniProtKB Mutagenesis 131 131 . . . Note=In SSY5-13%3B constitutively active%2C confers 9.3%25 increased STP1 processing in the absence of amino acids. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16524914;Dbxref=PMID:16524914 +P47002 UniProtKB Mutagenesis 420 424 . . . Note=Prevents maturation and amino-acid-induced STP1 cleavage. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15509782;Dbxref=PMID:15509782 +P47002 UniProtKB Mutagenesis 512 512 . . . Note=In SSY5-6%3B constitutively active%2C confers 30%25 increased STP1 processing in the absence of amino acids. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15947203;Dbxref=PMID:15947203 +P47002 UniProtKB Mutagenesis 575 575 . . . Note=In SSY5-14%3B constitutively active%2C confers 30%25 increased STP1 processing in the absence of amino acids. F->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16524914;Dbxref=PMID:16524914 +P47002 UniProtKB Mutagenesis 576 576 . . . Note=In SSY5-15%3B constitutively active%2C confers 30%25 increased STP1 processing in the absence of amino acids. Q->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16524914;Dbxref=PMID:16524914 +P47002 UniProtKB Mutagenesis 581 581 . . . Note=In SSY5-18%3B constitutively active%2C confers 15.5%25 increased STP1 processing in the absence of amino acids%3B when associated with H-632. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16524914;Dbxref=PMID:16524914 +P47002 UniProtKB Mutagenesis 632 632 . . . Note=In SSY5-18%3B constitutively active%2C confers 15.5%25 increased STP1 processing in the absence of amino acids%3B when associated with N-581. P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16524914;Dbxref=PMID:16524914 +P47002 UniProtKB Mutagenesis 640 640 . . . Note=Impairs maturation and amino acid-induced STP1 cleavage. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15509782;Dbxref=PMID:15509782 +##sequence-region P46679 1 850 +P46679 UniProtKB Chain 1 850 . . . ID=PRO_0000072252;Note=Protein STB2 +P46679 UniProtKB Compositional bias 270 273 . . . Note=Poly-Gln +P46679 UniProtKB Compositional bias 541 544 . . . Note=Poly-Ser +P46679 UniProtKB Modified residue 594 594 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P46679 UniProtKB Modified residue 625 625 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P23561 1 717 +P23561 UniProtKB Chain 1 717 . . . ID=PRO_0000086684;Note=Serine/threonine-protein kinase STE11 +P23561 UniProtKB Domain 20 84 . . . Note=SAM;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00184 +P23561 UniProtKB Domain 415 712 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P23561 UniProtKB Nucleotide binding 421 429 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P23561 UniProtKB Active site 579 579 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P23561 UniProtKB Binding site 444 444 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P23561 UniProtKB Modified residue 323 323 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P23561 UniProtKB Modified residue 465 465 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P23561 UniProtKB Mutagenesis 59 59 . . . Note=Disrupts interaction with STE50 and abolishes signal transduction. I->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15327964;Dbxref=PMID:15327964 +P23561 UniProtKB Helix 24 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OW5 +P23561 UniProtKB Helix 36 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OW5 +P23561 UniProtKB Helix 49 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OW5 +P23561 UniProtKB Helix 57 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OW5 +P23561 UniProtKB Helix 68 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1OW5 +##sequence-region P01098 1 86 +P01098 UniProtKB Transit peptide 1 23 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:6194151;Dbxref=PMID:6194151 +P01098 UniProtKB Chain 24 86 . . . ID=PRO_0000002555;Note=ATPase-stabilizing factor 9 kDa%2C mitochondrial +P01098 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P39007 1 718 +P39007 UniProtKB Chain 1 718 . . . ID=PRO_0000072293;Note=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3 +P39007 UniProtKB Topological domain 1 8 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Transmembrane 9 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Topological domain 30 113 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Transmembrane 114 134 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Topological domain 135 168 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Transmembrane 169 189 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Topological domain 190 207 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Transmembrane 208 228 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Topological domain 229 240 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Transmembrane 241 261 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Topological domain 262 266 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Transmembrane 267 287 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Topological domain 288 296 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Transmembrane 297 316 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Topological domain 317 358 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Transmembrane 359 379 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Topological domain 380 385 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Transmembrane 386 403 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Topological domain 404 404 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Transmembrane 405 425 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Topological domain 426 443 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Transmembrane 444 464 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Topological domain 465 718 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Glycosylation 60 60 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Glycosylation 535 535 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Glycosylation 539 539 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39007 UniProtKB Mutagenesis 159 159 . . . Note=Temperature sensitive and staurosporine sensitive. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15781470;Dbxref=PMID:15781470 +P39007 UniProtKB Mutagenesis 160 160 . . . Note=Temperature sensitive and staurosporine sensitive. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15781470;Dbxref=PMID:15781470 +P39007 UniProtKB Mutagenesis 163 163 . . . Note=Temperature sensitive and staurosporine sensitive. G->R +P39007 UniProtKB Mutagenesis 164 164 . . . Note=Temperature sensitive and staurosporine sensitive. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15781470;Dbxref=PMID:15781470 +P39007 UniProtKB Mutagenesis 208 208 . . . Note=Lethal%3B abolishes interaction with OST1 and WBP1. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15781470;Dbxref=PMID:15781470 +P39007 UniProtKB Mutagenesis 210 210 . . . Note=Temperature sensitive and staurosporine sensitive. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15781470;Dbxref=PMID:15781470 +P39007 UniProtKB Mutagenesis 393 393 . . . Note=Staurosporine sensitive. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15781470;Dbxref=PMID:15781470 +P39007 UniProtKB Mutagenesis 404 404 . . . Note=Lethal%3B abolishes interaction with OST1 and WBP1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15781470;Dbxref=PMID:15781470 +P39007 UniProtKB Mutagenesis 516 519 . . . Note=Lethal%3B greatly reduces amount of OST1 in complex. WWDY->AAAA +P39007 UniProtKB Mutagenesis 516 516 . . . Note=Temperature-sensitive. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12359722;Dbxref=PMID:12359722 +P39007 UniProtKB Mutagenesis 517 517 . . . Note=Lethal. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12359722;Dbxref=PMID:12359722 +P39007 UniProtKB Mutagenesis 518 518 . . . Note=Lethal. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12359722;Dbxref=PMID:12359722 +P39007 UniProtKB Mutagenesis 519 519 . . . Note=Temperature-sensitive. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12359722;Dbxref=PMID:12359722 +P39007 UniProtKB Mutagenesis 520 520 . . . Note=Temperature-sensitive. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12359722;Dbxref=PMID:12359722 +P39007 UniProtKB Mutagenesis 554 556 . . . Note=Temperature-sensitive%3B reduces amount of OST1 in complex. EEK->AAA +P39007 UniProtKB Mutagenesis 592 594 . . . Note=Lethal%3B reduces glycosylation%3B greatly reduces amount of OST1 in complex. RIS->AAA +P39007 UniProtKB Mutagenesis 593 593 . . . Note=Temperature-sensitive. I->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12359722;Dbxref=PMID:12359722 +P39007 UniProtKB Helix 467 470 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Helix 472 474 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Turn 481 483 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Helix 491 503 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Beta strand 508 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Helix 512 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Turn 525 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Turn 531 535 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Helix 536 551 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Beta strand 552 555 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Helix 560 573 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Beta strand 578 581 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Helix 601 606 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Beta strand 611 616 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Helix 621 635 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Helix 646 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Turn 663 665 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Helix 666 670 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Helix 675 686 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Helix 692 695 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Helix 698 700 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Beta strand 705 708 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +P39007 UniProtKB Beta strand 712 716 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2LGZ +##sequence-region P38198 1 1513 +P38198 UniProtKB Chain 1 1513 . . . ID=PRO_0000072294;Note=Protein STU1 +P38198 UniProtKB Region 461 716 . . . Note=Interaction with microtubules +P38198 UniProtKB Modified residue 997 997 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38198 UniProtKB Modified residue 1018 1018 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38198 UniProtKB Modified residue 1047 1047 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38198 UniProtKB Modified residue 1063 1063 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38198 UniProtKB Modified residue 1167 1167 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region P46675 1 888 +P46675 UniProtKB Chain 1 888 . . . ID=PRO_0000072295;Note=Protein STU2 +P46675 UniProtKB Repeat 51 88 . . . Note=HEAT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46675 UniProtKB Repeat 175 216 . . . Note=HEAT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46675 UniProtKB Repeat 411 448 . . . Note=HEAT 3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46675 UniProtKB Repeat 453 490 . . . Note=HEAT 4;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46675 UniProtKB Repeat 503 541 . . . Note=HEAT 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00103 +P46675 UniProtKB Region 8 280 . . . Note=TOG 1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16567500;Dbxref=PMID:16567500 +P46675 UniProtKB Region 326 550 . . . Note=TOG 1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16567500;Dbxref=PMID:16567500 +P46675 UniProtKB Coiled coil 654 762 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46675 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P46675 UniProtKB Modified residue 277 277 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P46675 UniProtKB Modified residue 813 813 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P46675 UniProtKB Mutagenesis 23 23 . . . Note=Disrupts interaction with tubulin heterodimer. Impairs polymerase activity under microtubule stress. W->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17355870,ECO:0000269|PubMed:22904013;Dbxref=PMID:17355870,PMID:22904013 +P46675 UniProtKB Mutagenesis 69 69 . . . Note=Impairs polymerase activity under microtubule stress. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22904013;Dbxref=PMID:22904013 +P46675 UniProtKB Mutagenesis 116 116 . . . Note=Decreases interaction with tubulin heterodimer. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17355870;Dbxref=PMID:17355870 +P46675 UniProtKB Mutagenesis 151 151 . . . Note=Disrupts interaction with tubulin heterodimer. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17355870;Dbxref=PMID:17355870 +P46675 UniProtKB Mutagenesis 200 200 . . . Note=No effect on polymerase activity under normal conditions but impairs polymerase activity under microtubule stress. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22904013,ECO:0000269|PubMed:25097237;Dbxref=PMID:22904013,PMID:25097237 +P46675 UniProtKB Mutagenesis 341 341 . . . Note=Disrupts interaction with tubulin heterodimer. Impairs polymerase activity under microtubule stress. W->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22904013,ECO:0000269|PubMed:25097237;Dbxref=PMID:22904013,PMID:25097237 +P46675 UniProtKB Mutagenesis 519 519 . . . Note=Disrupts interaction with tubulin heterodimer. No effect on polymerase activity under normal conditions but impairs polymerase activity under microtubule stress. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22904013,ECO:0000269|PubMed:25097237;Dbxref=PMID:22904013,PMID:25097237 +P46675 UniProtKB Helix 14 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P46675 UniProtKB Helix 23 38 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P46675 UniProtKB Helix 58 63 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P46675 UniProtKB Helix 69 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P46675 UniProtKB Helix 93 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P46675 UniProtKB Helix 117 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P46675 UniProtKB Beta strand 134 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P46675 UniProtKB Helix 138 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P46675 UniProtKB Helix 145 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P46675 UniProtKB Helix 153 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P46675 UniProtKB Turn 171 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P46675 UniProtKB Helix 177 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P46675 UniProtKB Helix 185 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P46675 UniProtKB Helix 188 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P46675 UniProtKB Helix 197 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P46675 UniProtKB Helix 231 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P46675 UniProtKB Helix 256 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P46675 UniProtKB Helix 325 327 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +P46675 UniProtKB Helix 332 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +P46675 UniProtKB Helix 341 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +P46675 UniProtKB Helix 356 358 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +P46675 UniProtKB Helix 370 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +P46675 UniProtKB Helix 386 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +P46675 UniProtKB Turn 405 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +P46675 UniProtKB Helix 410 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +P46675 UniProtKB Helix 423 425 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +P46675 UniProtKB Helix 429 445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +P46675 UniProtKB Helix 456 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +P46675 UniProtKB Helix 471 487 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +P46675 UniProtKB Helix 493 499 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +P46675 UniProtKB Turn 500 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +P46675 UniProtKB Helix 503 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +P46675 UniProtKB Helix 516 533 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +P46675 UniProtKB Helix 536 538 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +P46675 UniProtKB Helix 539 544 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +P46675 UniProtKB Helix 547 558 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2QK1 +##sequence-region P32911 1 108 +P32911 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32911 UniProtKB Chain 2 108 . . . ID=PRO_0000130566;Note=Eukaryotic translation initiation factor eIF-1 +P32911 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P32911 UniProtKB Beta strand 26 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM +P32911 UniProtKB Beta strand 34 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2OGH +P32911 UniProtKB Beta strand 38 44 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM +P32911 UniProtKB Beta strand 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM +P32911 UniProtKB Helix 51 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM +P32911 UniProtKB Beta strand 67 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM +P32911 UniProtKB Turn 72 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM +P32911 UniProtKB Beta strand 77 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM +P32911 UniProtKB Helix 86 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM +P32911 UniProtKB Beta strand 100 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3JAM +##sequence-region Q12286 1 268 +Q12286 UniProtKB Chain 1 268 . . . ID=PRO_0000115015;Note=Sterol uptake protein 2 +##sequence-region P32580 1 737 +P32580 UniProtKB Transit peptide 1 25 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32580 UniProtKB Chain 26 737 . . . ID=PRO_0000013306;Note=ATP-dependent RNA helicase SUV3%2C mitochondrial +P32580 UniProtKB Domain 226 365 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P32580 UniProtKB Domain 390 546 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P32580 UniProtKB Nucleotide binding 239 246 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P32580 UniProtKB Mutagenesis 272 272 . . . Note=In suv3-1%3B probably excised introns are less efficiently released. V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1379722;Dbxref=PMID:1379722 +P32580 UniProtKB Sequence conflict 165 165 . . . Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32580 UniProtKB Sequence conflict 664 664 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12254 1 260 +Q12254 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12254 UniProtKB Chain 20 260 . . . ID=PRO_0000022450;Note=Protein SVS1 +Q12254 UniProtKB Glycosylation 23 23 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12254 UniProtKB Glycosylation 249 249 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12254 UniProtKB Glycosylation 256 256 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04629 1 336 +Q04629 UniProtKB Chain 1 336 . . . ID=PRO_0000212994;Note=Palmitoyltransferase SWF1 +Q04629 UniProtKB Topological domain 1 2 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04629 UniProtKB Transmembrane 3 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04629 UniProtKB Topological domain 24 50 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04629 UniProtKB Transmembrane 51 71 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04629 UniProtKB Topological domain 72 86 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04629 UniProtKB Transmembrane 87 107 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04629 UniProtKB Topological domain 108 179 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04629 UniProtKB Transmembrane 180 200 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04629 UniProtKB Topological domain 201 216 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04629 UniProtKB Transmembrane 217 237 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04629 UniProtKB Topological domain 238 336 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04629 UniProtKB Domain 134 184 . . . Note=DHHC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00067 +Q04629 UniProtKB Mutagenesis 164 164 . . . Note=Loss of function. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15973437;Dbxref=PMID:15973437 +##sequence-region P08425 1 469 +P08425 UniProtKB Transit peptide 1 17 . . . Note=Mitochondrion +P08425 UniProtKB Chain 18 469 . . . ID=PRO_0000035817;Note=Phenylalanine--tRNA ligase%2C mitochondrial +P08425 UniProtKB Domain 372 469 . . . Note=FDX-ACB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00778 +P08425 UniProtKB Region 126 129 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08425 UniProtKB Region 162 164 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08425 UniProtKB Region 169 171 . . . Note=Substrate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08425 UniProtKB Binding site 155 155 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08425 UniProtKB Binding site 302 302 . . . Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08425 UniProtKB Binding site 329 329 . . . Note=Substrate%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P08425 UniProtKB Sequence conflict 86 86 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P08425 UniProtKB Sequence conflict 233 233 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P15180 1 591 +P15180 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P15180 UniProtKB Chain 2 591 . . . ID=PRO_0000152771;Note=Lysine--tRNA ligase%2C cytoplasmic +P15180 UniProtKB Compositional bias 33 61 . . . Note=Lys-rich (basic) +P15180 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P15180 UniProtKB Modified residue 30 30 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P15180 UniProtKB Modified residue 62 62 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P15180 UniProtKB Cross-link 308 308 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P15180 UniProtKB Cross-link 577 577 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P15180 UniProtKB Mutagenesis 488 488 . . . Note=In GCD5-1%3B defects in lysine-binding. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1505029;Dbxref=PMID:1505029 +P15180 UniProtKB Sequence conflict 22 22 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15180 UniProtKB Sequence conflict 51 51 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15180 UniProtKB Sequence conflict 111 111 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15180 UniProtKB Sequence conflict 162 162 . . . Note=C->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15180 UniProtKB Sequence conflict 165 165 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15180 UniProtKB Sequence conflict 259 259 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15180 UniProtKB Sequence conflict 430 432 . . . Note=ILV->VLA;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15180 UniProtKB Sequence conflict 591 591 . . . Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q04048 1 859 +Q04048 UniProtKB Chain 1 859 . . . ID=PRO_0000205737;Note=Pre-mRNA-splicing factor SYF1 +Q04048 UniProtKB Repeat 17 49 . . . Note=HAT 1 +Q04048 UniProtKB Repeat 52 84 . . . Note=HAT 2 +Q04048 UniProtKB Repeat 88 108 . . . Note=HAT 3 +Q04048 UniProtKB Repeat 123 157 . . . Note=HAT 4 +Q04048 UniProtKB Repeat 177 219 . . . Note=HAT 5 +Q04048 UniProtKB Repeat 238 271 . . . Note=HAT 6 +Q04048 UniProtKB Repeat 427 459 . . . Note=HAT 7 +Q04048 UniProtKB Repeat 461 482 . . . Note=HAT 8 +Q04048 UniProtKB Repeat 520 554 . . . Note=HAT 9 +Q04048 UniProtKB Repeat 599 633 . . . Note=HAT 10 +Q04048 UniProtKB Repeat 639 675 . . . Note=HAT 11 +Q04048 UniProtKB Repeat 685 718 . . . Note=HAT 12 +Q04048 UniProtKB Repeat 720 754 . . . Note=HAT 13 +Q04048 UniProtKB Repeat 756 790 . . . Note=HAT 14 +Q04048 UniProtKB Helix 570 578 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q04048 UniProtKB Helix 585 597 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q04048 UniProtKB Helix 602 611 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q04048 UniProtKB Turn 612 614 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q04048 UniProtKB Helix 616 635 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q04048 UniProtKB Helix 641 652 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q04048 UniProtKB Helix 664 675 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q04048 UniProtKB Helix 680 688 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q04048 UniProtKB Helix 707 719 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +Q04048 UniProtKB Helix 723 733 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5GMK +##sequence-region P07263 1 546 +P07263 UniProtKB Transit peptide 1 20 . . . Note=Mitochondrion +P07263 UniProtKB Chain 21 546 . . . ID=PRO_0000035804;Note=Histidine--tRNA ligase%2C mitochondrial +P07263 UniProtKB Alternative sequence 1 20 . . . ID=VSP_018907;Note=In isoform Cytoplasmic. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07263 UniProtKB Sequence conflict 476 478 . . . Note=AAE->TTK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07263 UniProtKB Sequence conflict 476 478 . . . Note=AAE->TTK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06563 1 197 +Q06563 UniProtKB Chain 1 197 . . . ID=PRO_0000234417;Note=Protein SYM1 +Q06563 UniProtKB Transmembrane 20 40 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06563 UniProtKB Transmembrane 55 75 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06563 UniProtKB Transmembrane 97 117 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06563 UniProtKB Transmembrane 137 157 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06563 UniProtKB Mutagenesis 54 54 . . . Note=Almost abolishes function. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16582910;Dbxref=PMID:16582910 +Q06563 UniProtKB Mutagenesis 54 54 . . . Note=Loss of function. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16582910;Dbxref=PMID:16582910 +Q06563 UniProtKB Mutagenesis 172 172 . . . Note=Loss of function. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16582910;Dbxref=PMID:16582910 +##sequence-region Q05506 1 607 +Q05506 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q05506 UniProtKB Chain 2 607 . . . ID=PRO_0000151664;Note=Arginine--tRNA ligase%2C cytoplasmic +Q05506 UniProtKB Region 59 60 . . . Note=Interaction with tRNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11060012;Dbxref=PMID:11060012 +Q05506 UniProtKB Region 106 111 . . . Note=Interaction with tRNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11060012;Dbxref=PMID:11060012 +Q05506 UniProtKB Region 148 153 . . . Note=L-arginine binding;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1BS2,ECO:0000244|PDB:1F7U,ECO:0000269|PubMed:11060012,ECO:0000269|PubMed:9736621;Dbxref=PMID:11060012,PMID:9736621 +Q05506 UniProtKB Region 484 498 . . . Note=Interaction with tRNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11060012;Dbxref=PMID:11060012 +Q05506 UniProtKB Motif 151 162 . . . Note="HIGH" region +Q05506 UniProtKB Binding site 162 162 . . . Note=L-arginine;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PDB:1BS2,ECO:0000269|PubMed:9736621;Dbxref=PMID:9736621 +Q05506 UniProtKB Binding site 347 347 . . . Note=L-arginine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1BS2,ECO:0000244|PDB:1F7U,ECO:0000269|PubMed:11060012,ECO:0000269|PubMed:9736621;Dbxref=PMID:11060012,PMID:9736621 +Q05506 UniProtKB Binding site 351 351 . . . Note=L-arginine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1BS2,ECO:0000244|PDB:1F7U,ECO:0000269|PubMed:11060012,ECO:0000269|PubMed:9736621;Dbxref=PMID:11060012,PMID:9736621 +Q05506 UniProtKB Binding site 375 375 . . . Note=L-arginine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PDB:1BS2,ECO:0000244|PDB:1F7U,ECO:0000269|PubMed:11060012,ECO:0000269|PubMed:9736621;Dbxref=PMID:11060012,PMID:9736621 +Q05506 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q05506 UniProtKB Modified residue 15 15 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q05506 UniProtKB Helix 3 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 19 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Turn 27 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 31 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 51 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 55 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 64 66 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Beta strand 68 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 73 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 83 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Turn 97 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Beta strand 100 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Beta strand 109 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 116 130 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 131 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Beta strand 144 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 160 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 163 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Beta strand 182 190 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 194 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 209 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 216 233 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Beta strand 235 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BS2 +Q05506 UniProtKB Turn 240 242 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Beta strand 243 245 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 246 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 260 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Beta strand 289 293 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 294 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 299 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Beta strand 315 318 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Beta strand 321 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 326 328 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Turn 331 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Beta strand 335 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Turn 341 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1BS2 +Q05506 UniProtKB Helix 347 362 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Beta strand 365 370 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 373 375 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 376 388 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 392 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Beta strand 397 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Beta strand 405 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Turn 410 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 418 434 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 437 440 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 446 463 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 475 479 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Beta strand 482 485 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 486 502 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Turn 503 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 508 511 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 516 518 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 522 531 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 534 544 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 547 567 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +Q05506 UniProtKB Helix 575 599 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1F7U +##sequence-region P07284 1 462 +P07284 UniProtKB Chain 1 462 . . . ID=PRO_0000122199;Note=Serine--tRNA ligase%2C cytoplasmic +P07284 UniProtKB Nucleotide binding 279 281 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07284 UniProtKB Nucleotide binding 366 369 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07284 UniProtKB Region 246 248 . . . Note=Serine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07284 UniProtKB Binding site 295 295 . . . Note=ATP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07284 UniProtKB Binding site 302 302 . . . Note=Serine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07284 UniProtKB Binding site 404 404 . . . Note=Serine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07284 UniProtKB Sequence conflict 224 224 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40150 1 613 +P40150 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P40150 UniProtKB Chain 2 613 . . . ID=PRO_0000078390;Note=Ribosome-associated molecular chaperone SSB2 +P40150 UniProtKB Nucleotide binding 16 18 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5 +P40150 UniProtKB Nucleotide binding 205 207 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5 +P40150 UniProtKB Nucleotide binding 271 278 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5 +P40150 UniProtKB Region 2 391 . . . Note=Nucleotide binding domain (NBD);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5 +P40150 UniProtKB Region 392 402 . . . Note=Inter-domain linker;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5 +P40150 UniProtKB Region 403 613 . . . Note=Substrate binding domain (SBD);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5 +P40150 UniProtKB Region 516 612 . . . Note=Lid domain (SBDalpha);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5 +P40150 UniProtKB Region 601 613 . . . Note=Required for interaction with ribosomes;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27917864;Dbxref=PMID:27917864 +P40150 UniProtKB Motif 428 430 . . . Note=Contributes to ribosome binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27917864;Dbxref=PMID:27917864 +P40150 UniProtKB Motif 574 582 . . . Note=Nuclear export signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11484 +P40150 UniProtKB Binding site 73 73 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5 +P40150 UniProtKB Binding site 342 342 . . . Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G0SCU5 +P40150 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P40150 UniProtKB Modified residue 47 47 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956;Dbxref=PMID:15665377,PMID:18407956 +P40150 UniProtKB Modified residue 431 431 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11484 +##sequence-region Q12153 1 453 +Q12153 UniProtKB Chain 1 453 . . . ID=PRO_0000120260;Note=Ribosome biogenesis protein SSF2 +Q12153 UniProtKB Domain 26 348 . . . Note=Brix;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00034 +##sequence-region P25390 1 1331 +P25390 UniProtKB Chain 1 1331 . . . ID=PRO_0000086681;Note=Serine/threonine-protein kinase SSK22 +P25390 UniProtKB Domain 1034 1310 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P25390 UniProtKB Nucleotide binding 1040 1048 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P25390 UniProtKB Active site 1158 1158 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P25390 UniProtKB Binding site 1063 1063 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +##sequence-region Q04673 1 461 +Q04673 UniProtKB Chain 1 461 . . . ID=PRO_0000046852;Note=Suppressor of stem-loop protein 1 +Q04673 UniProtKB Domain 125 304 . . . Note=VWFA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00219 +Q04673 UniProtKB Zinc finger 349 366 . . . Note=C4-type +Q04673 UniProtKB Sequence conflict 131 131 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q04673 UniProtKB Beta strand 125 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ +Q04673 UniProtKB Helix 134 137 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ +Q04673 UniProtKB Beta strand 139 143 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ +Q04673 UniProtKB Helix 145 163 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ +Q04673 UniProtKB Beta strand 168 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ +Q04673 UniProtKB Beta strand 178 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ +Q04673 UniProtKB Helix 189 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ +Q04673 UniProtKB Helix 210 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ +Q04673 UniProtKB Beta strand 231 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ +Q04673 UniProtKB Helix 247 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ +Q04673 UniProtKB Beta strand 260 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ +Q04673 UniProtKB Helix 271 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ +Q04673 UniProtKB Turn 280 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ +Q04673 UniProtKB Beta strand 288 291 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ +Q04673 UniProtKB Helix 294 305 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4WFQ +##sequence-region P13574 1 688 +P13574 UniProtKB Chain 1 688 . . . ID=PRO_0000072262;Note=Protein STE12 +P13574 UniProtKB DNA binding 57 167 . . . . +P13574 UniProtKB Modified residue 29 29 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P13574 UniProtKB Modified residue 214 214 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13574 UniProtKB Modified residue 226 226 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P13574 UniProtKB Modified residue 289 289 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P13574 UniProtKB Modified residue 400 400 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P47154 1 453 +P47154 UniProtKB Chain 1 453 . . . ID=PRO_0000138846;Note=CAAX prenyl protease 1 +P47154 UniProtKB Topological domain 1 12 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47154 UniProtKB Transmembrane 13 33 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47154 UniProtKB Topological domain 34 89 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47154 UniProtKB Transmembrane 90 110 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47154 UniProtKB Topological domain 111 121 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47154 UniProtKB Transmembrane 122 142 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47154 UniProtKB Topological domain 143 167 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47154 UniProtKB Transmembrane 168 188 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47154 UniProtKB Topological domain 189 197 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47154 UniProtKB Transmembrane 198 218 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47154 UniProtKB Topological domain 219 306 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47154 UniProtKB Transmembrane 307 327 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47154 UniProtKB Topological domain 328 357 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47154 UniProtKB Transmembrane 358 378 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47154 UniProtKB Topological domain 379 453 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47154 UniProtKB Active site 298 298 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P47154 UniProtKB Active site 394 394 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P47154 UniProtKB Metal binding 297 297 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P47154 UniProtKB Metal binding 301 301 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +P47154 UniProtKB Metal binding 390 390 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095 +##sequence-region P32597 1 1359 +P32597 UniProtKB Chain 1 1359 . . . ID=PRO_0000074361;Note=Nuclear protein STH1/NPS1 +P32597 UniProtKB Domain 307 383 . . . Note=HSA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00549 +P32597 UniProtKB Domain 482 647 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 +P32597 UniProtKB Domain 795 956 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 +P32597 UniProtKB Domain 1270 1340 . . . Note=Bromo;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 +P32597 UniProtKB Nucleotide binding 495 502 . . . Note=ATP;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32597 UniProtKB Motif 597 600 . . . Note=DEGH box +P32597 UniProtKB Compositional bias 1198 1247 . . . Note=Lys-rich +P32597 UniProtKB Modified residue 38 38 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32597 UniProtKB Mutagenesis 505 505 . . . Note=Temperature-sensitive. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9799253;Dbxref=PMID:9799253 +P32597 UniProtKB Mutagenesis 646 646 . . . Note=Temperature-sensitive. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9799253;Dbxref=PMID:9799253 +P32597 UniProtKB Mutagenesis 763 763 . . . Note=Temperature-sensitive. Reduced sporulation efficiency. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10320476;Dbxref=PMID:10320476 +P32597 UniProtKB Mutagenesis 792 792 . . . Note=Complete inactivation. K->E +P32597 UniProtKB Mutagenesis 806 806 . . . Note=Temperature-sensitive%3B when associated with M-881. Altered cell cycle distribution. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9799253;Dbxref=PMID:9799253 +P32597 UniProtKB Mutagenesis 881 881 . . . Note=Temperature-sensitive%3B when associated with L-806. Altered cell cycle distribution. T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9799253;Dbxref=PMID:9799253 +P32597 UniProtKB Sequence conflict 105 106 . . . Note=DK->NE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32597 UniProtKB Sequence conflict 144 144 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32597 UniProtKB Sequence conflict 227 227 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32597 UniProtKB Sequence conflict 546 546 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32597 UniProtKB Sequence conflict 566 566 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32597 UniProtKB Sequence conflict 1010 1010 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32597 UniProtKB Sequence conflict 1074 1080 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32597 UniProtKB Sequence conflict 1114 1114 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32597 UniProtKB Sequence conflict 1157 1157 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32597 UniProtKB Sequence conflict 1221 1221 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32597 UniProtKB Sequence conflict 1246 1246 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25604 1 385 +P25604 UniProtKB Chain 1 385 . . . ID=PRO_0000082605;Note=Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease +P25604 UniProtKB Domain 12 161 . . . Note=UEV;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00652 +P25604 UniProtKB Domain 322 385 . . . Note=SB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00644 +P25604 UniProtKB Coiled coil 272 300 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25604 UniProtKB Compositional bias 155 201 . . . Note=Pro-rich +P25604 UniProtKB Mutagenesis 85 85 . . . Note=No interaction of the ESCRT-I complex with ubiquitin. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11511343;Dbxref=PMID:11511343 +P25604 UniProtKB Mutagenesis 254 254 . . . Note=Defective in ESCRT-I cargo sorting%3B reduces MVB12 localization to MVBs%3B abolishes interaction with MVB12%3B reduces interaction with SRN2. M->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384 +P25604 UniProtKB Mutagenesis 286 286 . . . Note=Defective in ESCRT-I cargo sorting. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17442384;Dbxref=PMID:17442384 +P25604 UniProtKB Mutagenesis 345 345 . . . Note=Abolishes ESCRT-I complex assembly%3B class E phenotype (malformed late MVBs). L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16615894;Dbxref=PMID:16615894 +P25604 UniProtKB Mutagenesis 371 371 . . . Note=Abolishes ESCRT-I complex assembly%3B class E phenotype (malformed late MVBs). F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16615894;Dbxref=PMID:16615894 +P25604 UniProtKB Helix 11 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q +P25604 UniProtKB Turn 22 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q +P25604 UniProtKB Helix 28 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q +P25604 UniProtKB Beta strand 45 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q +P25604 UniProtKB Beta strand 59 70 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q +P25604 UniProtKB Beta strand 73 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R42 +P25604 UniProtKB Beta strand 80 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q +P25604 UniProtKB Turn 89 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q +P25604 UniProtKB Beta strand 97 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q +P25604 UniProtKB Helix 102 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q +P25604 UniProtKB Turn 107 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q +P25604 UniProtKB Helix 116 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q +P25604 UniProtKB Beta strand 124 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q +P25604 UniProtKB Helix 129 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q +P25604 UniProtKB Helix 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q +P25604 UniProtKB Helix 141 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3R3Q +P25604 UniProtKB Helix 219 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +P25604 UniProtKB Helix 248 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +P25604 UniProtKB Helix 254 289 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +P25604 UniProtKB Helix 291 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +P25604 UniProtKB Helix 314 316 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2P22 +P25604 UniProtKB Helix 323 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6M +P25604 UniProtKB Helix 356 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6M +P25604 UniProtKB Turn 382 384 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2F6M +##sequence-region P38704 1 541 +P38704 UniProtKB Zinc finger 204 226 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P38704 UniProtKB Zinc finger 232 267 . . . Note=C2H2-type 2%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P38704 UniProtKB Zinc finger 284 309 . . . Note=C2H2-type 3%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P38704 UniProtKB Region 13 32 . . . Note=I +P38704 UniProtKB Region 73 105 . . . Note=II +P38704 UniProtKB Mutagenesis 2 74 . . . Note=Dominant active transcription factor. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12502738;Dbxref=PMID:12502738 +P38704 UniProtKB Sequence conflict 101 101 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38637 1 319 +P38637 UniProtKB Chain 1 319 . . . ID=PRO_0000079792;Note=Tethering factor for nuclear proteasome STS1 +P38637 UniProtKB Compositional bias 43 49 . . . Note=Poly-Glu +P38637 UniProtKB Compositional bias 303 308 . . . Note=Poly-Asn +P38637 UniProtKB Sequence conflict 231 231 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P37297 1 1900 +P37297 UniProtKB Chain 1 1900 . . . ID=PRO_0000088835;Note=Phosphatidylinositol 4-kinase STT4 +P37297 UniProtKB Domain 1345 1530 . . . Note=PIK helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00878 +P37297 UniProtKB Domain 1643 1882 . . . Note=PI3K/PI4K;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00269 +P37297 UniProtKB Region 1531 1648 . . . Note=Pleckstrin homology (PH) domain conferring phosphoinositide binding specificity;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P37297 UniProtKB Modified residue 459 459 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P32579 1 426 +P32579 UniProtKB Chain 1 426 . . . ID=PRO_0000202013;Note=Threonylcarbamoyl-AMP synthase +P32579 UniProtKB Domain 49 252 . . . Note=YrdC-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00518 +P32579 UniProtKB Compositional bias 225 313 . . . Note=Gly-rich +P32579 UniProtKB Binding site 72 72 . . . Note=L-threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32579 UniProtKB Binding site 95 95 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32579 UniProtKB Binding site 99 99 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32579 UniProtKB Binding site 104 104 . . . Note=L-threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32579 UniProtKB Binding site 170 170 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32579 UniProtKB Binding site 174 174 . . . Note=L-threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32579 UniProtKB Binding site 194 194 . . . Note=L-threonine%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32579 UniProtKB Binding site 196 196 . . . Note=ATP%3B via amide nitrogen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32579 UniProtKB Binding site 204 204 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32579 UniProtKB Binding site 234 234 . . . Note=L-threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32579 UniProtKB Binding site 248 248 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32579 UniProtKB Binding site 292 292 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32579 UniProtKB Mutagenesis 70 70 . . . Note=Reduces t(6)A37 formation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P32579 UniProtKB Mutagenesis 93 93 . . . Note=Severely impairs t(6)A37 formation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P32579 UniProtKB Mutagenesis 95 95 . . . Note=Severely impairs t(6)A37 formation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P32579 UniProtKB Mutagenesis 107 107 . . . Note=In SUA5-1%3B suppresses a translation initiation defect in a CYC1 allele at an aberrant ATG codon. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1325384;Dbxref=PMID:1325384 +P32579 UniProtKB Mutagenesis 174 174 . . . Note=Severely impairs t(6)A37 formation. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P32579 UniProtKB Mutagenesis 196 196 . . . Note=Severely impairs t(6)A37 formation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P32579 UniProtKB Mutagenesis 198 198 . . . Note=Severely impairs t(6)A37 formation. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P32579 UniProtKB Mutagenesis 234 234 . . . Note=Severely impairs t(6)A37 formation. S->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23620299;Dbxref=PMID:23620299 +P32579 UniProtKB Mutagenesis 423 423 . . . Note=No phenotypes. C->S +##sequence-region P53032 1 299 +P53032 UniProtKB Chain 1 299 . . . ID=PRO_0000115014;Note=Sterol uptake protein 1 +##sequence-region P32944 1 819 +P32944 UniProtKB Chain 1 819 . . . ID=PRO_0000086727;Note=Mitosis inhibitor protein kinase SWE1 +P32944 UniProtKB Domain 444 794 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32944 UniProtKB Nucleotide binding 450 458 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32944 UniProtKB Compositional bias 88 96 . . . Note=Poly-Glu +P32944 UniProtKB Active site 579 579 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P32944 UniProtKB Metal binding 584 584 . . . Note=Magnesium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32944 UniProtKB Metal binding 597 597 . . . Note=Magnesium%3B via carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32944 UniProtKB Binding site 473 473 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P32944 UniProtKB Modified residue 36 36 . . . Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15037762,ECO:0000269|PubMed:16096060;Dbxref=PMID:15037762,PMID:16096060 +P32944 UniProtKB Modified residue 45 45 . . . Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 63 63 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 70 70 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 74 74 . . . Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 102 102 . . . Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762 +P32944 UniProtKB Modified residue 105 105 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 111 111 . . . Note=Phosphoserine%3B by CDC5%2C CDC28 and CLA4;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15037762,ECO:0000269|PubMed:16096060;Dbxref=PMID:15037762,PMID:16096060 +P32944 UniProtKB Modified residue 118 118 . . . Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15037762,ECO:0000269|PubMed:16096060;Dbxref=PMID:15037762,PMID:16096060 +P32944 UniProtKB Modified residue 121 121 . . . Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 124 124 . . . Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 127 127 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 131 131 . . . Note=Phosphothreonine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762 +P32944 UniProtKB Modified residue 133 133 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 136 136 . . . Note=Phosphoserine%3B by CDC28 and CLA4;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15037762,ECO:0000269|PubMed:16096060;Dbxref=PMID:15037762,PMID:16096060 +P32944 UniProtKB Modified residue 156 156 . . . Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762 +P32944 UniProtKB Modified residue 169 169 . . . Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762 +P32944 UniProtKB Modified residue 196 196 . . . Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 201 201 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 225 225 . . . Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762 +P32944 UniProtKB Modified residue 254 254 . . . Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762 +P32944 UniProtKB Modified residue 262 262 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 263 263 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 266 266 . . . Note=Phosphoserine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 280 280 . . . Note=Phosphothreonine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762 +P32944 UniProtKB Modified residue 284 284 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 294 294 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 312 312 . . . Note=Phosphoserine%3B by CLA4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762 +P32944 UniProtKB Modified residue 345 345 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 367 367 . . . Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 373 373 . . . Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 379 379 . . . Note=Phosphoserine%3B by CDC5 and CLA4;Ontology_term=ECO:0000244,ECO:0000269,ECO:0000269;evidence=ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:15037762,ECO:0000269|PubMed:16096060;Dbxref=PMID:19779198,PMID:15037762,PMID:16096060 +P32944 UniProtKB Modified residue 384 384 . . . Note=Phosphothreonine%3B by CDC28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Modified residue 395 395 . . . Note=Phosphoserine%3B by CDC5 and CLA4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762 +P32944 UniProtKB Modified residue 438 438 . . . Note=Phosphoserine%3B by CDC5 and CLA4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762 +P32944 UniProtKB Modified residue 610 610 . . . Note=Phosphoserine%3B by CDC5;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15037762,ECO:0000269|PubMed:16096060;Dbxref=PMID:15037762,PMID:16096060 +P32944 UniProtKB Modified residue 629 629 . . . Note=Phosphothreonine%3B by CDC5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762 +P32944 UniProtKB Modified residue 688 688 . . . Note=Phosphothreonine%3B by CDC5 and CLA4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15037762;Dbxref=PMID:15037762 +P32944 UniProtKB Modified residue 692 692 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096060;Dbxref=PMID:16096060 +P32944 UniProtKB Cross-link 741 741 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P32944 UniProtKB Mutagenesis 318 328 . . . Note=Impairs interaction with HSL7 and prevents bud neck localization and degradation. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757 +P32944 UniProtKB Mutagenesis 320 320 . . . Note=Prevents degradation. L->P%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757 +P32944 UniProtKB Mutagenesis 324 324 . . . Note=Prevents degradation. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757 +P32944 UniProtKB Mutagenesis 327 327 . . . Note=Prevents degradation. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757 +P32944 UniProtKB Mutagenesis 328 328 . . . Note=Prevents degradation. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757 +P32944 UniProtKB Mutagenesis 331 331 . . . Note=Prevents degradation. L->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757 +P32944 UniProtKB Mutagenesis 332 332 . . . Note=Prevents degradation. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757 +P32944 UniProtKB Mutagenesis 473 473 . . . Note=Loss of catalytic activity. K->A%2CP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10454545;Dbxref=PMID:10454545 +P32944 UniProtKB Mutagenesis 797 797 . . . Note=Prevents degradation. E->K%2CV%2CG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757 +P32944 UniProtKB Mutagenesis 806 806 . . . Note=Prevents degradation. I->T%2CA%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757 +P32944 UniProtKB Mutagenesis 807 807 . . . Note=Prevents degradation. Q->R%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12388757;Dbxref=PMID:12388757 +##sequence-region P25302 1 1093 +P25302 UniProtKB Chain 1 1093 . . . ID=PRO_0000067069;Note=Regulatory protein SWI4 +P25302 UniProtKB Domain 37 147 . . . Note=HTH APSES-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630 +P25302 UniProtKB Repeat 520 549 . . . Note=ANK 1 +P25302 UniProtKB Repeat 641 670 . . . Note=ANK 2 +P25302 UniProtKB DNA binding 71 92 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00630 +P25302 UniProtKB Compositional bias 201 727 . . . Note=Asn/Gln-rich +P25302 UniProtKB Modified residue 255 255 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25302 UniProtKB Modified residue 806 806 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P25302 UniProtKB Sequence conflict 175 175 . . . Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25302 UniProtKB Sequence conflict 431 431 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P25302 UniProtKB Sequence conflict 1054 1054 . . . Note=A->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P15625 1 503 +P15625 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P15625 UniProtKB Chain 2 503 . . . ID=PRO_0000126828;Note=Phenylalanine--tRNA ligase alpha subunit +P15625 UniProtKB Region 2 173 . . . Note=Contains the major tRNA-Phe binding sites +P15625 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P15625 UniProtKB Sequence conflict 177 177 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P15625 UniProtKB Sequence conflict 289 289 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P32048 1 576 +P32048 UniProtKB Transit peptide 1 30 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32048 UniProtKB Chain 31 576 . . . ID=PRO_0000035812;Note=Lysine--tRNA ligase%2C mitochondrial +##sequence-region P11325 1 894 +P11325 UniProtKB Transit peptide 1 9 . . . Note=Mitochondrion +P11325 UniProtKB Chain 10 894 . . . ID=PRO_0000035810;Note=Leucine--tRNA ligase%2C mitochondrial +P11325 UniProtKB Motif 56 66 . . . Note="HIGH" region +P11325 UniProtKB Motif 646 650 . . . Note="KMSKS" region +P11325 UniProtKB Binding site 649 649 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q07395 1 620 +Q07395 UniProtKB Chain 1 620 . . . ID=PRO_0000248459;Note=Synchronized import protein 1 +Q07395 UniProtKB Repeat 25 64 . . . Note=ARM 1 +Q07395 UniProtKB Repeat 66 106 . . . Note=ARM 2 +Q07395 UniProtKB Repeat 181 221 . . . Note=ARM 3 +Q07395 UniProtKB Repeat 258 299 . . . Note=ARM 4 +Q07395 UniProtKB Repeat 340 386 . . . Note=ARM 5 +Q07395 UniProtKB Repeat 435 470 . . . Note=ARM 6 +Q07395 UniProtKB Repeat 471 510 . . . Note=ARM 7 +Q07395 UniProtKB Repeat 564 607 . . . Note=ARM 8 +##sequence-region P07806 1 1104 +P07806 UniProtKB Transit peptide 1 47 . . . Note=Mitochondrion +P07806 UniProtKB Chain 48 1104 . . . ID=PRO_0000035839;Note=Valine--tRNA ligase%2C mitochondrial +P07806 UniProtKB Motif 190 200 . . . Note="HIGH" region +P07806 UniProtKB Motif 703 707 . . . Note="KMSKS" region +P07806 UniProtKB Binding site 706 706 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P07806 UniProtKB Modified residue 73 73 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P07806 UniProtKB Modified residue 294 294 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P07806 UniProtKB Modified residue 332 332 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P07806 UniProtKB Modified residue 707 707 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P07806 UniProtKB Modified residue 1003 1003 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P07806 UniProtKB Alternative sequence 1 46 . . . ID=VSP_018910;Note=In isoform Cytoplasmic. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07806 UniProtKB Sequence conflict 147 147 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07806 UniProtKB Sequence conflict 540 540 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P41895 1 735 +P41895 UniProtKB Chain 1 735 . . . ID=PRO_0000211234;Note=Transcription initiation factor IIF subunit alpha +P41895 UniProtKB Compositional bias 455 580 . . . Note=Asp/Glu-rich (acidic) +P41895 UniProtKB Modified residue 198 198 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P41895 UniProtKB Modified residue 200 200 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P41895 UniProtKB Modified residue 515 515 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P41895 UniProtKB Modified residue 560 560 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P41895 UniProtKB Modified residue 562 562 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P41895 UniProtKB Modified residue 571 571 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P41895 UniProtKB Modified residue 655 655 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17330950,PMID:18407956 +P41895 UniProtKB Sequence conflict 238 238 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12030 1 206 +Q12030 UniProtKB Chain 1 206 . . . ID=PRO_0000118901;Note=Transcription initiation factor TFIID subunit 10 +Q12030 UniProtKB Domain 47 194 . . . Note=Histone-fold +Q12030 UniProtKB Compositional bias 147 172 . . . Note=Gln-rich +Q12030 UniProtKB Modified residue 58 58 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12030 UniProtKB Modified residue 146 146 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P35189 1 244 +P35189 UniProtKB Chain 1 244 . . . ID=PRO_0000211241;Note=Transcription initiation factor TFIID subunit 14 +P35189 UniProtKB Domain 8 115 . . . Note=YEATS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00376 +P35189 UniProtKB Cross-link 181 181 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P35189 UniProtKB Sequence conflict 116 116 . . . Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P35189 UniProtKB Beta strand 3 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL +P35189 UniProtKB Beta strand 30 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL +P35189 UniProtKB Beta strand 40 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L7E +P35189 UniProtKB Beta strand 45 47 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5D7E +P35189 UniProtKB Beta strand 51 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL +P35189 UniProtKB Beta strand 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL +P35189 UniProtKB Beta strand 66 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL +P35189 UniProtKB Beta strand 76 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL +P35189 UniProtKB Beta strand 86 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL +P35189 UniProtKB Helix 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL +P35189 UniProtKB Beta strand 97 103 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL +P35189 UniProtKB Beta strand 107 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL +P35189 UniProtKB Helix 125 131 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL +P35189 UniProtKB Turn 132 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3QRL +##sequence-region P23255 1 1407 +P23255 UniProtKB Chain 1 1407 . . . ID=PRO_0000118867;Note=Transcription initiation factor TFIID subunit 2 +P23255 UniProtKB Region 1285 1350 . . . Note=Highly charged +P23255 UniProtKB Coiled coil 304 337 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P23255 UniProtKB Compositional bias 52 55 . . . Note=Poly-Ile +P23255 UniProtKB Compositional bias 259 334 . . . Note=Asp/Glu-rich (acidic) +P23255 UniProtKB Modified residue 158 158 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P23255 UniProtKB Modified residue 161 161 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P23255 UniProtKB Modified residue 163 163 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P23255 UniProtKB Modified residue 318 318 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P23255 UniProtKB Sequence conflict 323 323 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12297 1 353 +Q12297 UniProtKB Chain 1 353 . . . ID=PRO_0000118868;Note=Transcription initiation factor TFIID subunit 3 +Q12297 UniProtKB Domain 11 78 . . . Note=Histone-fold +Q12297 UniProtKB Coiled coil 289 309 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12297 UniProtKB Modified residue 237 237 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q12297 UniProtKB Modified residue 310 310 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q12297 UniProtKB Modified residue 346 346 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38992 1 349 +P38992 UniProtKB Chain 1 349 . . . ID=PRO_0000072316;Note=Sphingolipid C4-hydroxylase SUR2 +P38992 UniProtKB Transmembrane 9 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38992 UniProtKB Transmembrane 50 70 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38992 UniProtKB Transmembrane 99 119 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38992 UniProtKB Transmembrane 148 168 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38992 UniProtKB Transmembrane 209 229 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40342 1 146 +P40342 UniProtKB Chain 1 146 . . . ID=PRO_0000203468;Note=Nucleolar protein SWM2 +##sequence-region P53873 1 357 +P53873 UniProtKB Chain 1 357 . . . ID=PRO_0000203403;Note=Protein SWT21 +##sequence-region P09436 1 1072 +P09436 UniProtKB Chain 1 1072 . . . ID=PRO_0000098604;Note=Isoleucine--tRNA ligase%2C cytoplasmic +P09436 UniProtKB Motif 47 57 . . . Note="HIGH" region +P09436 UniProtKB Motif 602 606 . . . Note="KMSKS" region +P09436 UniProtKB Binding site 605 605 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P09436 UniProtKB Modified residue 829 829 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P09436 UniProtKB Modified residue 1059 1059 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P09436 UniProtKB Cross-link 486 486 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P09436 UniProtKB Sequence conflict 551 551 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09436 UniProtKB Sequence conflict 588 588 . . . Note=N->KS;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09436 UniProtKB Sequence conflict 693 695 . . . Note=DRW->AEM;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09436 UniProtKB Sequence conflict 706 706 . . . Note=F->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09436 UniProtKB Sequence conflict 747 747 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P48526 1 1002 +P48526 UniProtKB Chain 1 1002 . . . ID=PRO_0000098605;Note=Isoleucine--tRNA ligase%2C mitochondrial +P48526 UniProtKB Motif 94 104 . . . Note="HIGH" region +P48526 UniProtKB Motif 668 672 . . . Note="KMSKS" region +P48526 UniProtKB Binding site 671 671 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P48526 UniProtKB Sequence conflict 437 437 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P48526 UniProtKB Sequence conflict 672 672 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P48526 UniProtKB Sequence conflict 806 806 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q06836 1 1226 +Q06836 UniProtKB Chain 1 1226 . . . ID=PRO_0000270620;Note=Arf guanine nucleotide exchange factor SYT1 +Q06836 UniProtKB Domain 405 620 . . . Note=SEC7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00189 +Q06836 UniProtKB Domain 844 1074 . . . Note=PH +Q06836 UniProtKB Compositional bias 232 239 . . . Note=Poly-Ser +Q06836 UniProtKB Compositional bias 654 742 . . . Note=Ser-rich +Q06836 UniProtKB Modified residue 277 277 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +Q06836 UniProtKB Modified residue 369 369 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region P53040 1 516 +P53040 UniProtKB Chain 1 516 . . . ID=PRO_0000118878;Note=Transcription initiation factor TFIID subunit 6 +P53040 UniProtKB Domain 6 75 . . . Note=Histone-fold +##sequence-region Q05027 1 157 +Q05027 UniProtKB Chain 1 157 . . . ID=PRO_0000118896;Note=Transcription initiation factor TFIID subunit 9 +Q05027 UniProtKB Domain 30 97 . . . Note=Histone-fold +##sequence-region P25638 1 111 +P25638 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P25638 UniProtKB Chain 2 111 . . . ID=PRO_0000106352;Note=TPR repeat-containing protein associated with Hsp90 +P25638 UniProtKB Repeat 4 37 . . . Note=TPR 1 +P25638 UniProtKB Repeat 39 71 . . . Note=TPR 2 +P25638 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P25638 UniProtKB Helix 3 16 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGQ +P25638 UniProtKB Helix 20 33 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGQ +P25638 UniProtKB Helix 38 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGQ +P25638 UniProtKB Helix 54 65 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGQ +P25638 UniProtKB Helix 71 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU +P25638 UniProtKB Helix 76 90 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGQ +P25638 UniProtKB Beta strand 92 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU +P25638 UniProtKB Beta strand 98 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CGU +P25638 UniProtKB Beta strand 105 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2L6J +##sequence-region P15019 1 335 +P15019 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P15019 UniProtKB Chain 2 335 . . . ID=PRO_0000173574;Note=Transaldolase +P15019 UniProtKB Active site 144 144 . . . Note=Schiff-base intermediate with substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8109173;Dbxref=PMID:8109173 +P15019 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9298649;Dbxref=PMID:9298649 +P15019 UniProtKB Sequence conflict 221 221 . . . Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P25345 1 492 +##sequence-region P13188 1 809 +P13188 UniProtKB Chain 1 809 . . . ID=PRO_0000195866;Note=Glutamine--tRNA ligase +P13188 UniProtKB Nucleotide binding 259 261 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00962 +P13188 UniProtKB Nucleotide binding 265 271 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00962 +P13188 UniProtKB Nucleotide binding 488 489 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00962 +P13188 UniProtKB Nucleotide binding 496 498 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00962 +P13188 UniProtKB Motif 258 268 . . . Note="HIGH" region +P13188 UniProtKB Motif 495 499 . . . Note="KMSKS" region +P13188 UniProtKB Binding site 291 291 . . . Note=L-glutamine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00962 +P13188 UniProtKB Binding site 440 440 . . . Note=L-glutamine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00962 +P13188 UniProtKB Binding site 459 459 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00962 +P13188 UniProtKB Modified residue 378 378 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P13188 UniProtKB Sequence conflict 179 179 . . . Note=G->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13188 UniProtKB Helix 4 13 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4 +P13188 UniProtKB Helix 18 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4 +P13188 UniProtKB Helix 28 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4 +P13188 UniProtKB Helix 49 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4 +P13188 UniProtKB Helix 70 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4 +P13188 UniProtKB Helix 85 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4 +P13188 UniProtKB Helix 99 101 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4 +P13188 UniProtKB Helix 104 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4 +P13188 UniProtKB Turn 110 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4 +P13188 UniProtKB Helix 119 132 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4 +P13188 UniProtKB Helix 134 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4 +P13188 UniProtKB Helix 141 144 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4 +P13188 UniProtKB Helix 145 153 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4 +P13188 UniProtKB Helix 156 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4 +P13188 UniProtKB Helix 166 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4 +P13188 UniProtKB Helix 183 185 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3TL4 +P13188 UniProtKB Helix 222 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 238 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 241 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 253 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 260 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 267 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 285 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 300 312 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 318 322 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 323 326 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 327 339 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 343 346 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 350 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 373 376 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 379 390 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 400 403 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 412 414 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 418 422 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Turn 428 430 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 435 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 440 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 456 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 460 465 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 466 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 483 486 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 489 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 498 506 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 509 512 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 521 527 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 531 541 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 548 551 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 552 566 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 572 581 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 590 597 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 601 603 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 605 610 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 612 617 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 618 620 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 632 634 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 639 641 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 648 655 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 661 668 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 692 694 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 698 706 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 709 713 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 715 717 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 722 725 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 730 739 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 743 748 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 755 758 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Helix 771 773 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 776 778 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Turn 779 781 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 782 786 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 792 794 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +P13188 UniProtKB Beta strand 796 801 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4H3S +##sequence-region P32774 1 122 +P32774 UniProtKB Chain 1 122 . . . ID=PRO_0000194053;Note=Transcription initiation factor IIA subunit 2 +P32774 UniProtKB Modified residue 95 95 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P32774 UniProtKB Modified residue 102 102 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32774 UniProtKB Mutagenesis 27 27 . . . Note=Decreases ability to interact with TAF11 and support growth on galactose-containing medium. Unable to support cell viability in a strain deleted for TOA2%3B when associated with A-69. I->A%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238911;Dbxref=PMID:11238911 +P32774 UniProtKB Mutagenesis 41 41 . . . Note=Decreases ability to interact with Toa1 and TAF11%2C display mutant growth phenotypes and defects in transcription in vivo. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11238911;Dbxref=PMID:11238911 +P32774 UniProtKB Mutagenesis 69 69 . . . Note=Unable to support cell viability in a strain deleted for TOA2%3B when associated with A-27 or K-27. Y->A +P32774 UniProtKB Helix 9 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2 +P32774 UniProtKB Helix 14 28 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2 +P32774 UniProtKB Helix 34 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2 +P32774 UniProtKB Beta strand 59 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2 +P32774 UniProtKB Beta strand 75 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2 +P32774 UniProtKB Beta strand 104 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1NH2 +##sequence-region P36421 1 394 +P36421 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7 +P36421 UniProtKB Chain 2 394 . . . ID=PRO_0000055676;Note=Tyrosine--tRNA ligase%2C cytoplasmic +P36421 UniProtKB Motif 48 56 . . . Note="HIGH" region +P36421 UniProtKB Motif 227 231 . . . Note="KMSKS" region +P36421 UniProtKB Motif 360 378 . . . Note=Nuclear localization signal +P36421 UniProtKB Binding site 43 43 . . . Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36421 UniProtKB Binding site 170 170 . . . Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36421 UniProtKB Binding site 174 174 . . . Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36421 UniProtKB Binding site 177 177 . . . Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36421 UniProtKB Binding site 192 192 . . . Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P36421 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7 +P36421 UniProtKB Modified residue 235 235 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36421 UniProtKB Modified residue 359 359 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36421 UniProtKB Mutagenesis 43 43 . . . Note=Decreases catalytic activity for L-tyrosine 400-fold%2C but allows the utilization of 3-iodo-L-tyrosine and other 3-modified tyrosines as substrates. Y->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11530018;Dbxref=PMID:11530018 +P36421 UniProtKB Mutagenesis 364 368 . . . Note=Abolishes nuclear localization. KKAKK->EEAEE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11359929;Dbxref=PMID:11359929 +P36421 UniProtKB Helix 9 17 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Beta strand 21 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 26 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Beta strand 41 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 54 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 57 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Beta strand 72 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 79 84 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Turn 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 93 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Beta strand 120 123 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 125 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 131 141 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 146 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Turn 153 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 166 180 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Beta strand 184 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 190 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 193 202 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 203 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Beta strand 212 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 243 252 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 264 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 273 278 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Beta strand 280 282 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Beta strand 288 290 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 294 296 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Beta strand 300 304 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 305 313 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 319 343 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +P36421 UniProtKB Helix 345 354 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2DLC +##sequence-region P36100 1 482 +P36100 UniProtKB Chain 1 482 . . . ID=PRO_0000211225;Note=Transcription initiation factor IIE subunit alpha +P36100 UniProtKB Domain 9 99 . . . Note=HTH TFE/IIEalpha-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00676 +P36100 UniProtKB Zinc finger 124 152 . . . Note=C4-type;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36100 UniProtKB Compositional bias 374 482 . . . Note=Asp/Glu-rich (highly acidic) +P36100 UniProtKB Compositional bias 374 392 . . . Note=Poly-Glu +##sequence-region Q9URQ3 1 322 +Q9URQ3 UniProtKB Chain 1 322 . . . ID=PRO_0000171741;Note=tRNA-specific adenosine deaminase subunit TAD3 +Q9URQ3 UniProtKB Domain 162 283 . . . Note=CMP/dCMP-type deaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01083 +##sequence-region Q04226 1 346 +Q04226 UniProtKB Chain 1 346 . . . ID=PRO_0000118907;Note=Transcription initiation factor TFIID subunit 11 +Q04226 UniProtKB Domain 131 329 . . . Note=Histone-fold +Q04226 UniProtKB Modified residue 236 236 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q04226 UniProtKB Modified residue 238 238 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38129 1 798 +P38129 UniProtKB Chain 1 798 . . . ID=PRO_0000051260;Note=Transcription initiation factor TFIID subunit 5 +P38129 UniProtKB Domain 56 88 . . . Note=LisH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00126 +P38129 UniProtKB Repeat 464 503 . . . Note=WD 1 +P38129 UniProtKB Repeat 523 562 . . . Note=WD 2 +P38129 UniProtKB Repeat 565 604 . . . Note=WD 3 +P38129 UniProtKB Repeat 607 646 . . . Note=WD 4 +P38129 UniProtKB Repeat 649 688 . . . Note=WD 5 +P38129 UniProtKB Repeat 692 731 . . . Note=WD 6 +P38129 UniProtKB Coiled coil 329 349 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38129 UniProtKB Compositional bias 3 48 . . . Note=Gln-rich +P38129 UniProtKB Modified residue 299 299 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38129 UniProtKB Modified residue 411 411 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38129 UniProtKB Modified residue 415 415 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38129 UniProtKB Modified residue 787 787 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P38129 UniProtKB Helix 152 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49 +P38129 UniProtKB Turn 168 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49 +P38129 UniProtKB Helix 171 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49 +P38129 UniProtKB Helix 194 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49 +P38129 UniProtKB Helix 205 208 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49 +P38129 UniProtKB Helix 209 217 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49 +P38129 UniProtKB Turn 218 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49 +P38129 UniProtKB Helix 225 230 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49 +P38129 UniProtKB Helix 232 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49 +P38129 UniProtKB Beta strand 242 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49 +P38129 UniProtKB Helix 248 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49 +P38129 UniProtKB Helix 262 264 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49 +P38129 UniProtKB Helix 266 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49 +P38129 UniProtKB Beta strand 277 281 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2J49 +##sequence-region Q03750 1 510 +Q03750 UniProtKB Chain 1 510 . . . ID=PRO_0000118887;Note=Transcription initiation factor TFIID subunit 8 +Q03750 UniProtKB Domain 37 103 . . . Note=Histone-fold +Q03750 UniProtKB Coiled coil 142 165 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03750 UniProtKB Coiled coil 346 383 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03750 UniProtKB Modified residue 269 269 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P09733 1 447 +P09733 UniProtKB Chain 1 447 . . . ID=PRO_0000048239;Note=Tubulin alpha-1 chain +P09733 UniProtKB Nucleotide binding 143 149 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P09733 UniProtKB Sequence conflict 94 94 . . . Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09733 UniProtKB Sequence conflict 327 327 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P09733 UniProtKB Beta strand 4 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Helix 10 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Beta strand 34 36 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Beta strand 47 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Turn 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Beta strand 54 56 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Beta strand 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Beta strand 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Beta strand 66 72 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Helix 73 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Turn 83 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Turn 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Beta strand 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Helix 104 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Helix 112 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Beta strand 135 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Turn 146 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Helix 149 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Turn 162 164 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Beta strand 165 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Helix 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Helix 184 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Beta strand 196 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Beta strand 200 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Helix 207 216 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Helix 225 239 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Helix 241 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Helix 253 260 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Beta strand 262 265 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P09733 UniProtKB Beta strand 270 274 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Helix 289 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Helix 299 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Beta strand 302 306 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Beta strand 313 323 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Helix 326 338 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Beta strand 352 357 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Beta strand 365 369 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Beta strand 373 382 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Helix 383 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Helix 386 400 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Turn 401 405 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Helix 406 410 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Turn 411 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P09733 UniProtKB Helix 417 436 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +##sequence-region P32613 1 152 +P32613 UniProtKB Chain 1 152 . . . ID=PRO_0000202605;Note=TRAPP-associated protein TCA17 +P32613 UniProtKB Sequence conflict 2 2 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P32613 UniProtKB Beta strand 6 11 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6 +P32613 UniProtKB Beta strand 17 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6 +P32613 UniProtKB Helix 33 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6 +P32613 UniProtKB Beta strand 57 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6 +P32613 UniProtKB Beta strand 64 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6 +P32613 UniProtKB Beta strand 72 78 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6 +P32613 UniProtKB Turn 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6 +P32613 UniProtKB Beta strand 85 91 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6 +P32613 UniProtKB Helix 92 94 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6 +P32613 UniProtKB Helix 99 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6 +P32613 UniProtKB Helix 125 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6 +P32613 UniProtKB Helix 130 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6 +P32613 UniProtKB Helix 149 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PR6 +##sequence-region P42943 1 550 +P42943 UniProtKB Chain 1 550 . . . ID=PRO_0000128372;Note=T-complex protein 1 subunit eta +##sequence-region Q6B2U8 1 126 +Q6B2U8 UniProtKB Chain 1 126 . . . ID=PRO_0000268622;Note=Topoisomerase I damage affected protein 8 +Q6B2U8 UniProtKB Domain 1 110 . . . Note=PA14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01164 +##sequence-region Q04545 1 1251 +Q04545 UniProtKB Chain 1 1251 . . . ID=PRO_0000046864;Note=Probable transcription factor TDA9 +Q04545 UniProtKB Zinc finger 61 83 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q04545 UniProtKB Zinc finger 89 112 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +Q04545 UniProtKB Modified residue 527 527 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +Q04545 UniProtKB Modified residue 603 603 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P34163 1 548 +P34163 UniProtKB Chain 1 548 . . . ID=PRO_0000090379;Note=Sterol esterase TGL1 +P34163 UniProtKB Topological domain 1 13 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34163 UniProtKB Transmembrane 14 34 . . . Note=Helical%3B Signal-anchor for type III membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34163 UniProtKB Topological domain 35 548 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34163 UniProtKB Domain 107 402 . . . Note=AB hydrolase-1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P34163 UniProtKB Active site 201 201 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P34163 UniProtKB Active site 369 369 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P34163 UniProtKB Active site 396 396 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P34163 UniProtKB Modified residue 462 462 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34163 UniProtKB Modified residue 466 466 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34163 UniProtKB Modified residue 521 521 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P34163 UniProtKB Modified residue 538 538 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34163 UniProtKB Modified residue 539 539 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P34163 UniProtKB Cross-link 246 246 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region Q12043 1 749 +Q12043 UniProtKB Chain 1 749 . . . ID=PRO_0000270918;Note=Lipase 5 +Q12043 UniProtKB Transmembrane 183 203 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12043 UniProtKB Domain 183 388 . . . Note=PNPLA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161 +Q12043 UniProtKB Motif 214 218 . . . Note=GXSXG;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161 +Q12043 UniProtKB Active site 216 216 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161 +Q12043 UniProtKB Active site 375 375 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01161 +Q12043 UniProtKB Modified residue 645 645 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q12043 UniProtKB Glycosylation 270 270 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12043 UniProtKB Glycosylation 289 289 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12043 UniProtKB Glycosylation 297 297 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12043 UniProtKB Glycosylation 304 304 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12043 UniProtKB Glycosylation 321 321 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12043 UniProtKB Glycosylation 474 474 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12043 UniProtKB Glycosylation 589 589 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12043 UniProtKB Glycosylation 680 680 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12043 UniProtKB Glycosylation 714 714 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12043 UniProtKB Glycosylation 742 742 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38714 1 643 +P38714 UniProtKB Motif 188 198 . . . Note="HIGH" region +P38714 UniProtKB Sequence conflict 499 499 . . . Note=M->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38705 1 446 +P38705 UniProtKB Chain 1 446 . . . ID=PRO_0000122200;Note=Serine--tRNA ligase%2C mitochondrial +P38705 UniProtKB Nucleotide binding 284 286 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38705 UniProtKB Nucleotide binding 371 374 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38705 UniProtKB Region 251 253 . . . Note=Serine binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38705 UniProtKB Binding site 300 300 . . . Note=ATP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38705 UniProtKB Binding site 307 307 . . . Note=Serine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38705 UniProtKB Binding site 407 407 . . . Note=Serine;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P04801 1 734 +P04801 UniProtKB Chain 1 734 . . . ID=PRO_0000101125;Note=Threonine--tRNA ligase%2C cytoplasmic +P04801 UniProtKB Modified residue 195 195 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04801 UniProtKB Modified residue 289 289 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P04801 UniProtKB Modified residue 297 297 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P04801 UniProtKB Modified residue 381 381 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P04801 UniProtKB Modified residue 453 453 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P04801 UniProtKB Modified residue 457 457 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P04801 UniProtKB Modified residue 460 460 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P04801 UniProtKB Modified residue 605 605 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P04801 UniProtKB Sequence conflict 9 9 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04801 UniProtKB Sequence conflict 18 18 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04801 UniProtKB Sequence conflict 502 502 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q12109 1 432 +Q12109 UniProtKB Chain 1 432 . . . ID=PRO_0000136744;Note=Tryptophan--tRNA ligase%2C cytoplasmic +Q12109 UniProtKB Motif 111 120 . . . Note="HIGH" region +Q12109 UniProtKB Motif 295 299 . . . Note="KMSKS" region +Q12109 UniProtKB Sequence conflict 87 87 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q12109 UniProtKB Helix 47 54 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 61 71 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 77 80 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Beta strand 83 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 90 99 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Beta strand 104 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Beta strand 112 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT3 +Q12109 UniProtKB Helix 118 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 121 134 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Beta strand 138 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 144 150 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 156 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Turn 172 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 177 179 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Beta strand 180 184 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 185 188 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 191 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 206 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 221 225 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 227 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 236 238 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Turn 240 243 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Beta strand 251 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 257 259 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 260 273 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Beta strand 279 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Beta strand 291 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3KT6 +Q12109 UniProtKB Helix 301 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 311 321 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 330 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Turn 340 342 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 344 352 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 356 367 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 373 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +Q12109 UniProtKB Helix 400 407 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2IP1 +##sequence-region P38854 1 504 +P38854 UniProtKB Chain 1 504 . . . ID=PRO_0000202928;Note=Topoisomerase I damage affected protein 11 +P38854 UniProtKB Coiled coil 179 231 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38854 UniProtKB Modified residue 236 236 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38854 UniProtKB Modified residue 244 244 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P38854 UniProtKB Modified residue 286 286 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region Q03533 1 586 +Q03533 UniProtKB Chain 1 586 . . . ID=PRO_0000086153;Note=Serine/threonine-protein kinase TDA1 +Q03533 UniProtKB Domain 39 351 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03533 UniProtKB Nucleotide binding 45 53 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03533 UniProtKB Active site 180 180 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +Q03533 UniProtKB Binding site 68 68 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +Q03533 UniProtKB Modified residue 504 504 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03533 UniProtKB Modified residue 509 509 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03533 UniProtKB Modified residue 518 518 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +Q03533 UniProtKB Modified residue 538 538 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +Q03533 UniProtKB Modified residue 578 578 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40045 1 126 +P40045 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P40045 UniProtKB Chain 2 126 . . . ID=PRO_0000202634;Note=Topoisomerase I damage affected protein 2 +P40045 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P47153 1 279 +P47153 UniProtKB Chain 1 279 . . . ID=PRO_0000185544;Note=Topoisomerase I damage affected protein 4 +P47153 UniProtKB Topological domain 1 32 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47153 UniProtKB Transmembrane 33 53 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47153 UniProtKB Topological domain 54 79 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47153 UniProtKB Transmembrane 80 100 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47153 UniProtKB Topological domain 101 110 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47153 UniProtKB Transmembrane 111 131 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47153 UniProtKB Topological domain 132 135 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47153 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47153 UniProtKB Topological domain 157 162 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47153 UniProtKB Transmembrane 163 183 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47153 UniProtKB Topological domain 184 192 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47153 UniProtKB Transmembrane 193 213 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47153 UniProtKB Topological domain 214 238 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47153 UniProtKB Transmembrane 239 259 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47153 UniProtKB Topological domain 260 279 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P47153 UniProtKB Domain 70 271 . . . Note=TLC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00205 +##sequence-region P07236 1 462 +P07236 UniProtKB Transit peptide 1 45 . . . Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P07236 UniProtKB Chain 46 462 . . . ID=PRO_0000035827;Note=Threonine--tRNA ligase%2C mitochondrial +P07236 UniProtKB Sequence conflict 265 265 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P07236 UniProtKB Helix 35 46 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Helix 63 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Beta strand 93 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Helix 97 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Turn 106 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Helix 110 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Beta strand 113 117 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UGQ +P07236 UniProtKB Beta strand 120 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UGQ +P07236 UniProtKB Beta strand 126 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Helix 133 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Helix 147 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Beta strand 151 156 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Beta strand 159 161 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Turn 166 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Turn 171 173 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Beta strand 176 187 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Helix 189 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Helix 192 207 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Turn 208 210 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Beta strand 225 229 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Helix 239 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Beta strand 260 263 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Beta strand 273 279 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Beta strand 285 295 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Helix 296 300 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Beta strand 316 325 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Helix 326 337 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Helix 343 345 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Beta strand 350 356 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Helix 360 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Beta strand 379 381 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4EO4 +P07236 UniProtKB Beta strand 394 396 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Helix 403 413 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Beta strand 416 421 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Helix 423 428 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Beta strand 431 435 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Helix 436 438 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Beta strand 443 445 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +P07236 UniProtKB Helix 447 459 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3UH0 +##sequence-region P46677 1 1066 +P46677 UniProtKB Chain 1 1066 . . . ID=PRO_0000118862;Note=Transcription initiation factor TFIID subunit 1 +P46677 UniProtKB Coiled coil 409 425 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46677 UniProtKB Coiled coil 944 1000 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P46677 UniProtKB Compositional bias 65 69 . . . Note=Poly-Asp +P46677 UniProtKB Helix 15 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B0A +P46677 UniProtKB Beta strand 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B0A +P46677 UniProtKB Helix 28 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4B0A +P46677 UniProtKB Helix 471 475 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Turn 478 480 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Beta strand 481 484 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Helix 488 491 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Turn 492 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Turn 498 501 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Beta strand 507 510 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Helix 518 521 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Helix 526 529 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Helix 533 536 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Beta strand 538 542 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Beta strand 544 553 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Beta strand 563 571 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Beta strand 584 591 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Turn 598 601 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Beta strand 610 615 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Beta strand 617 626 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Beta strand 632 640 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Beta strand 643 650 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Beta strand 653 658 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Beta strand 662 665 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Helix 673 694 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Helix 702 705 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Helix 713 720 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Turn 721 723 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Beta strand 724 726 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Turn 731 734 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Beta strand 735 738 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Helix 747 750 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Helix 751 753 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Helix 756 778 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Helix 782 790 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Helix 793 804 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Beta strand 820 824 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Helix 859 882 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Helix 888 891 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Helix 900 903 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Beta strand 914 922 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Beta strand 926 935 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +P46677 UniProtKB Helix 938 951 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +##sequence-region P02557 1 457 +P02557 UniProtKB Chain 1 457 . . . ID=PRO_0000048443;Note=Tubulin beta chain +P02557 UniProtKB Nucleotide binding 140 146 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P02557 UniProtKB Modified residue 278 278 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P02557 UniProtKB Modified residue 280 280 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P02557 UniProtKB Mutagenesis 100 100 . . . Note=Becomes sensitive to rhizoxin. V->N +P02557 UniProtKB Mutagenesis 390 390 . . . Note=Decreased microtubule stability. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28013290;Dbxref=PMID:28013290 +P02557 UniProtKB Mutagenesis 421 421 . . . Note=Increased microtubule polymerization and depolymerization rates. Increased microtubule stability. Decreased kinesin KIP3 subcellular location at microtubule plus ends. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23001566;Dbxref=PMID:23001566 +P02557 UniProtKB Sequence conflict 9 9 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02557 UniProtKB Sequence conflict 12 12 . . . Note=C->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02557 UniProtKB Sequence conflict 71 71 . . . Note=G->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02557 UniProtKB Sequence conflict 152 152 . . . Note=I->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02557 UniProtKB Sequence conflict 156 156 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02557 UniProtKB Sequence conflict 159 159 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P02557 UniProtKB Beta strand 4 9 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 10 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 42 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 46 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Beta strand 51 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Beta strand 59 61 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Beta strand 63 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 70 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 80 82 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P02557 UniProtKB Beta strand 83 85 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Beta strand 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 101 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Turn 108 112 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 113 125 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Beta strand 132 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 143 158 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Beta strand 162 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 181 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Beta strand 197 203 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 204 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 222 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 238 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Beta strand 242 244 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4FFB +P02557 UniProtKB Beta strand 245 247 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 250 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Beta strand 265 271 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 286 294 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 296 298 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Beta strand 299 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 305 307 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Beta strand 310 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 323 336 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 338 340 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Beta strand 345 347 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Beta strand 349 355 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Beta strand 362 371 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 372 374 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 375 389 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Turn 390 395 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 396 399 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Turn 400 402 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +P02557 UniProtKB Helix 405 426 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4U3J +##sequence-region P38114 1 1094 +P38114 UniProtKB Chain 1 1094 . . . ID=PRO_0000114992;Note=Uncharacterized transcriptional regulatory protein TBS1 +P38114 UniProtKB Transmembrane 755 775 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38114 UniProtKB DNA binding 107 137 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P38114 UniProtKB Compositional bias 935 991 . . . Note=Asn-rich +P38114 UniProtKB Compositional bias 985 1032 . . . Note=Asp-rich +##sequence-region Q12466 1 1186 +Q12466 UniProtKB Chain 1 1186 . . . ID=PRO_0000252271;Note=Tricalbin-1 +Q12466 UniProtKB Topological domain 1 106 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12466 UniProtKB Transmembrane 107 127 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12466 UniProtKB Topological domain 128 128 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12466 UniProtKB Transmembrane 129 149 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12466 UniProtKB Topological domain 150 1186 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12466 UniProtKB Domain 373 471 . . . Note=C2 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 +Q12466 UniProtKB Domain 645 741 . . . Note=C2 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 +Q12466 UniProtKB Domain 979 1078 . . . Note=C2 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 +Q12466 UniProtKB Coiled coil 795 822 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12466 UniProtKB Metal binding 1008 1008 . . . Note=Calcium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12466 UniProtKB Metal binding 1008 1008 . . . Note=Calcium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12466 UniProtKB Metal binding 1014 1014 . . . Note=Calcium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12466 UniProtKB Metal binding 1064 1064 . . . Note=Calcium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12466 UniProtKB Metal binding 1064 1064 . . . Note=Calcium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12466 UniProtKB Metal binding 1066 1066 . . . Note=Calcium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12466 UniProtKB Metal binding 1066 1066 . . . Note=Calcium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12466 UniProtKB Metal binding 1066 1066 . . . Note=Calcium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12466 UniProtKB Metal binding 1069 1069 . . . Note=Calcium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12466 UniProtKB Metal binding 1072 1072 . . . Note=Calcium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12466 UniProtKB Metal binding 1072 1072 . . . Note=Calcium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12466 UniProtKB Modified residue 1000 1000 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +##sequence-region Q03640 1 1545 +Q03640 UniProtKB Chain 1 1545 . . . ID=PRO_0000203249;Note=Tricalbin-3 +Q03640 UniProtKB Topological domain 1 206 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03640 UniProtKB Transmembrane 207 227 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03640 UniProtKB Topological domain 228 228 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03640 UniProtKB Transmembrane 229 249 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03640 UniProtKB Topological domain 250 1545 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03640 UniProtKB Domain 478 580 . . . Note=C2 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 +Q03640 UniProtKB Domain 785 881 . . . Note=C2 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 +Q03640 UniProtKB Domain 1121 1218 . . . Note=C2 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 +Q03640 UniProtKB Coiled coil 620 660 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03640 UniProtKB Coiled coil 937 972 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03640 UniProtKB Compositional bias 1316 1404 . . . Note=Ser-rich +Q03640 UniProtKB Metal binding 1150 1150 . . . Note=Calcium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03640 UniProtKB Metal binding 1150 1150 . . . Note=Calcium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03640 UniProtKB Metal binding 1156 1156 . . . Note=Calcium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03640 UniProtKB Metal binding 1204 1204 . . . Note=Calcium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03640 UniProtKB Metal binding 1204 1204 . . . Note=Calcium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03640 UniProtKB Metal binding 1206 1206 . . . Note=Calcium 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03640 UniProtKB Metal binding 1206 1206 . . . Note=Calcium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03640 UniProtKB Metal binding 1206 1206 . . . Note=Calcium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03640 UniProtKB Metal binding 1212 1212 . . . Note=Calcium 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03640 UniProtKB Metal binding 1212 1212 . . . Note=Calcium 3;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03640 UniProtKB Modified residue 67 67 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03640 UniProtKB Modified residue 112 112 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q03640 UniProtKB Modified residue 1340 1340 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03640 UniProtKB Modified residue 1342 1342 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03640 UniProtKB Modified residue 1346 1346 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03640 UniProtKB Modified residue 1350 1350 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:17761666,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:17761666,PMID:18407956,PMID:19779198 +Q03640 UniProtKB Modified residue 1354 1354 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q03640 UniProtKB Modified residue 1400 1400 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P36101 1 447 +P36101 UniProtKB Chain 1 447 . . . ID=PRO_0000120586;Note=tRNA threonylcarbamoyladenosine dehydratase 2 +P36101 UniProtKB Transmembrane 9 29 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36101 UniProtKB Transmembrane 86 106 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36101 UniProtKB Transmembrane 294 314 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P36101 UniProtKB Sequence conflict 41 41 . . . Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q99190 1 310 +Q99190 UniProtKB Chain 1 310 . . . ID=PRO_0000262739;Note=Very-long-chain enoyl-CoA reductase +Q99190 UniProtKB Topological domain 1 85 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99190 UniProtKB Transmembrane 86 106 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99190 UniProtKB Topological domain 107 141 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99190 UniProtKB Transmembrane 142 162 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99190 UniProtKB Topological domain 163 165 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99190 UniProtKB Transmembrane 166 186 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99190 UniProtKB Topological domain 187 201 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99190 UniProtKB Transmembrane 202 222 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99190 UniProtKB Topological domain 223 242 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99190 UniProtKB Transmembrane 243 265 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99190 UniProtKB Topological domain 266 268 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99190 UniProtKB Transmembrane 269 291 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99190 UniProtKB Topological domain 292 310 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q99190 UniProtKB Mutagenesis 81 81 . . . Note=In TSC13-1%3B reduces fatty acid elongation activity by 50%25. Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11113186;Dbxref=PMID:11113186 +##sequence-region P40533 1 473 +P40533 UniProtKB Chain 1 473 . . . ID=PRO_0000202993;Note=Protein TED1 +P40533 UniProtKB Topological domain 1 8 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40533 UniProtKB Transmembrane 9 29 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40533 UniProtKB Topological domain 30 451 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40533 UniProtKB Transmembrane 452 472 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40533 UniProtKB Topological domain 473 473 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40533 UniProtKB Glycosylation 38 38 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40533 UniProtKB Glycosylation 147 147 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40533 UniProtKB Glycosylation 229 229 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40533 UniProtKB Glycosylation 266 266 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40533 UniProtKB Glycosylation 307 307 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07921 1 160 +Q07921 UniProtKB Chain 1 160 . . . ID=PRO_0000270926;Note=Telomere length regulation protein TEN1 +##sequence-region P53065 1 400 +P53065 UniProtKB Chain 1 400 . . . ID=PRO_0000171777;Note=tRNA-specific adenosine deaminase 1 +P53065 UniProtKB Domain 76 400 . . . Note=A to I editase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00240 +P53065 UniProtKB Active site 103 103 . . . Note=Proton donor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00240 +P53065 UniProtKB Metal binding 101 101 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00240 +P53065 UniProtKB Metal binding 157 157 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00240 +P53065 UniProtKB Metal binding 223 223 . . . Note=Zinc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00240 +P53065 UniProtKB Binding site 108 108 . . . Note=Inositol hexakisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53065 UniProtKB Binding site 226 226 . . . Note=Inositol hexakisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53065 UniProtKB Binding site 232 232 . . . Note=Inositol hexakisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53065 UniProtKB Binding site 369 369 . . . Note=Inositol hexakisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53065 UniProtKB Binding site 375 375 . . . Note=Inositol hexakisphosphate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P47058 1 250 +P47058 UniProtKB Chain 1 250 . . . ID=PRO_0000171740;Note=tRNA-specific adenosine deaminase subunit TAD2 +P47058 UniProtKB Domain 1 119 . . . Note=CMP/dCMP-type deaminase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01083 +P47058 UniProtKB Active site 56 56 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47058 UniProtKB Metal binding 54 54 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47058 UniProtKB Metal binding 88 88 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P47058 UniProtKB Metal binding 91 91 . . . Note=Zinc%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q03761 1 539 +Q03761 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q03761 UniProtKB Chain 2 539 . . . ID=PRO_0000118909;Note=Transcription initiation factor TFIID subunit 12 +Q03761 UniProtKB Domain 413 490 . . . Note=Histone-fold +Q03761 UniProtKB Coiled coil 153 202 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03761 UniProtKB Coiled coil 239 285 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q03761 UniProtKB Compositional bias 116 309 . . . Note=Gln-rich +Q03761 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +Q03761 UniProtKB Modified residue 129 129 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q03761 UniProtKB Modified residue 286 286 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +##sequence-region P50105 1 388 +P50105 UniProtKB Chain 1 388 . . . ID=PRO_0000118871;Note=Transcription initiation factor TFIID subunit 4 +P50105 UniProtKB Domain 193 261 . . . Note=Histone-fold +P50105 UniProtKB Coiled coil 279 297 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P50105 UniProtKB Modified residue 36 36 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956 +P50105 UniProtKB Modified residue 49 49 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P50105 UniProtKB Modified residue 80 80 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P53072 1 289 +P53072 UniProtKB Chain 1 289 . . . ID=PRO_0000072426;Note=tRNA acetyltransferase TAN1 +P53072 UniProtKB Domain 146 259 . . . Note=THUMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00529 +P53072 UniProtKB Modified residue 72 72 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +##sequence-region P39076 1 527 +P39076 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P39076 UniProtKB Chain 2 527 . . . ID=PRO_0000128320;Note=T-complex protein 1 subunit beta +P39076 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P40413 1 562 +P40413 UniProtKB Chain 1 562 . . . ID=PRO_0000128354;Note=T-complex protein 1 subunit epsilon +P40413 UniProtKB Sequence conflict 3 3 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40413 UniProtKB Sequence conflict 27 27 . . . Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40413 UniProtKB Sequence conflict 58 58 . . . Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40413 UniProtKB Sequence conflict 92 92 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40413 UniProtKB Sequence conflict 274 279 . . . Note=CPFEPP->VHLNLL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40413 UniProtKB Sequence conflict 336 336 . . . Note=L->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P40413 UniProtKB Sequence conflict 488 488 . . . Note=G->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39079 1 546 +P39079 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P39079 UniProtKB Chain 2 546 . . . ID=PRO_0000128362;Note=T-complex protein 1 subunit zeta +P39079 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P39079 UniProtKB Modified residue 249 249 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +##sequence-region P42938 1 290 +P42938 UniProtKB Chain 1 290 . . . ID=PRO_0000214076;Note=Probable ATP-dependent kinase TDA10 +P42938 UniProtKB Nucleotide binding 38 45 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P42938 UniProtKB Helix 8 24 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Turn 25 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Beta strand 32 37 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Helix 44 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Helix 60 62 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Beta strand 65 69 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Helix 70 73 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Helix 77 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Turn 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Helix 91 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Beta strand 94 96 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Helix 104 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Beta strand 125 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Turn 133 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Helix 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Beta strand 147 152 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Beta strand 154 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Turn 172 174 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Beta strand 176 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Helix 182 195 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Turn 196 198 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Beta strand 204 212 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Helix 216 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Helix 238 246 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Helix 249 262 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Beta strand 265 275 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +P42938 UniProtKB Beta strand 281 287 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1ODF +##sequence-region P38758 1 523 +P38758 UniProtKB Chain 1 523 . . . ID=PRO_0000202886;Note=Putative oxidoreductase TDA3 +P38758 UniProtKB Compositional bias 156 212 . . . Note=Ser-rich +P38758 UniProtKB Modified residue 189 189 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38758 UniProtKB Modified residue 204 204 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38758 UniProtKB Modified residue 306 306 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region P53882 1 636 +P53882 UniProtKB Chain 1 636 . . . ID=PRO_0000203407;Note=Topoisomerase I damage affected protein 7 +P53882 UniProtKB Transmembrane 457 477 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53882 UniProtKB Compositional bias 15 381 . . . Note=Ser-rich +P53882 UniProtKB Compositional bias 325 408 . . . Note=Thr-rich +P53882 UniProtKB Modified residue 628 628 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P53882 UniProtKB Glycosylation 4 4 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53882 UniProtKB Glycosylation 257 257 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53882 UniProtKB Glycosylation 492 492 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53882 UniProtKB Glycosylation 557 557 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53882 UniProtKB Glycosylation 562 562 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53882 UniProtKB Glycosylation 626 626 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P53882 UniProtKB Cross-link 512 512 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +P53882 UniProtKB Sequence conflict 251 251 . . . Note=F->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P39933 1 429 +P39933 UniProtKB Chain 1 429 . . . ID=PRO_0000047086;Note=Transcription factor IIIA +P39933 UniProtKB Zinc finger 49 74 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P39933 UniProtKB Zinc finger 80 102 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P39933 UniProtKB Zinc finger 108 130 . . . Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P39933 UniProtKB Zinc finger 134 159 . . . Note=C2H2-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P39933 UniProtKB Zinc finger 163 186 . . . Note=C2H2-type 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P39933 UniProtKB Zinc finger 194 219 . . . Note=C2H2-type 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P39933 UniProtKB Zinc finger 222 244 . . . Note=C2H2-type 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P39933 UniProtKB Zinc finger 253 277 . . . Note=C2H2-type 8;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P39933 UniProtKB Zinc finger 365 389 . . . Note=C2H2-type 9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 +P39933 UniProtKB Compositional bias 24 43 . . . Note=Ser-rich +P39933 UniProtKB Compositional bias 321 327 . . . Note=Arg/Lys-rich (basic) +##sequence-region Q02939 1 513 +Q02939 UniProtKB Chain 1 513 . . . ID=PRO_0000119268;Note=RNA polymerase II transcription factor B subunit 2 +Q02939 UniProtKB Helix 448 450 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP +Q02939 UniProtKB Beta strand 452 460 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP +Q02939 UniProtKB Helix 465 477 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP +Q02939 UniProtKB Beta strand 481 485 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP +Q02939 UniProtKB Turn 486 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP +Q02939 UniProtKB Beta strand 490 494 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP +Q02939 UniProtKB Helix 495 497 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP +Q02939 UniProtKB Helix 498 505 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3DGP +##sequence-region Q12004 1 338 +Q12004 UniProtKB Chain 1 338 . . . ID=PRO_0000119275;Note=RNA polymerase II transcription factor B subunit 4 +Q12004 UniProtKB Zinc finger 289 308 . . . Note=C4-type +Q12004 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region P34111 1 1160 +P34111 UniProtKB Chain 1 1160 . . . ID=PRO_0000072497;Note=Transcription factor tau 138 kDa subunit +P34111 UniProtKB Modified residue 546 546 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P34111 UniProtKB Mutagenesis 349 349 . . . Note=In TSV115%3B thermosensitive. Level of TFIIIC and its affinity for tDNA reduced. tDNA binding activity very sensitive to mild heat treatments%2C and TFIIIC-DNA interaction inhibited at moderate salt concentrations. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8083243;Dbxref=PMID:8083243 +P34111 UniProtKB Helix 546 565 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIM +P34111 UniProtKB Beta strand 568 573 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIM +P34111 UniProtKB Helix 574 584 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIM +P34111 UniProtKB Helix 593 604 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIM +P34111 UniProtKB Beta strand 607 612 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIM +P34111 UniProtKB Turn 614 616 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIM +P34111 UniProtKB Beta strand 619 622 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIM +P34111 UniProtKB Helix 628 637 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5AIM +##sequence-region Q04372 1 366 +Q04372 UniProtKB Chain 1 366 . . . ID=PRO_0000218623;Note=Type 2A phosphatase-associated protein 42 +Q04372 UniProtKB Helix 4 18 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P +Q04372 UniProtKB Helix 29 50 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P +Q04372 UniProtKB Helix 62 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P +Q04372 UniProtKB Helix 67 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P +Q04372 UniProtKB Helix 75 83 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P +Q04372 UniProtKB Helix 93 120 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P +Q04372 UniProtKB Helix 126 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P +Q04372 UniProtKB Helix 143 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P +Q04372 UniProtKB Helix 156 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P +Q04372 UniProtKB Helix 199 231 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2V0P +##sequence-region P40085 1 556 +P40085 UniProtKB Chain 1 556 . . . ID=PRO_0000202654;Note=Endoplasmic reticulum membrane protein 65 +P40085 UniProtKB Topological domain 1 87 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P40085 UniProtKB Transmembrane 88 108 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40085 UniProtKB Topological domain 109 151 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P40085 UniProtKB Transmembrane 152 172 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40085 UniProtKB Topological domain 173 224 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P40085 UniProtKB Transmembrane 225 245 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40085 UniProtKB Topological domain 246 330 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P40085 UniProtKB Transmembrane 331 351 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40085 UniProtKB Topological domain 352 391 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P40085 UniProtKB Transmembrane 392 412 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40085 UniProtKB Topological domain 413 428 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 +P40085 UniProtKB Transmembrane 429 449 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P40085 UniProtKB Topological domain 450 556 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 +P40085 UniProtKB Modified residue 22 22 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P40085 UniProtKB Glycosylation 318 318 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 +##sequence-region P13393 1 240 +P13393 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2677740;Dbxref=PMID:2677740 +P13393 UniProtKB Chain 2 240 . . . ID=PRO_0000153990;Note=TATA-box-binding protein +P13393 UniProtKB Repeat 67 143 . . . Note=1 +P13393 UniProtKB Repeat 157 234 . . . Note=2 +P13393 UniProtKB Sequence conflict 50 50 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P13393 UniProtKB Beta strand 66 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB +P13393 UniProtKB Helix 82 88 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB +P13393 UniProtKB Beta strand 89 93 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB +P13393 UniProtKB Turn 96 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB +P13393 UniProtKB Beta strand 100 106 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB +P13393 UniProtKB Turn 107 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB +P13393 UniProtKB Beta strand 111 115 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB +P13393 UniProtKB Beta strand 119 128 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB +P13393 UniProtKB Helix 129 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB +P13393 UniProtKB Beta strand 153 165 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB +P13393 UniProtKB Helix 172 178 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB +P13393 UniProtKB Turn 179 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB +P13393 UniProtKB Beta strand 183 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1RM1 +P13393 UniProtKB Turn 187 189 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB +P13393 UniProtKB Beta strand 191 196 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB +P13393 UniProtKB Beta strand 198 200 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB +P13393 UniProtKB Beta strand 203 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB +P13393 UniProtKB Beta strand 210 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB +P13393 UniProtKB Helix 220 236 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1YTB +##sequence-region P38756 1 429 +P38756 UniProtKB Chain 1 429 . . . ID=PRO_0000120585;Note=tRNA threonylcarbamoyladenosine dehydratase 1 +P38756 UniProtKB Transmembrane 3 23 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38756 UniProtKB Transmembrane 74 94 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38756 UniProtKB Transmembrane 279 299 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38756 UniProtKB Modified residue 259 259 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +##sequence-region Q06466 1 467 +Q06466 UniProtKB Chain 1 467 . . . ID=PRO_0000259482;Note=Putative vacuolar protein sorting-associated protein TDA6 +Q06466 UniProtKB Transmembrane 8 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06466 UniProtKB Glycosylation 61 61 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06466 UniProtKB Glycosylation 124 124 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q06466 UniProtKB Glycosylation 141 141 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47988 1 759 +P47988 UniProtKB Chain 1 759 . . . ID=PRO_0000114982;Note=TY1 enhancer activator +P47988 UniProtKB DNA binding 70 96 . . . Note=Zn(2)-C6 fungal-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00227 +P47988 UniProtKB Motif 744 752 . . . Note=9aaTAD +P47988 UniProtKB Modified residue 22 22 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47988 UniProtKB Modified residue 755 755 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P47988 UniProtKB Sequence conflict 501 502 . . . Note=SV->RL;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P47988 UniProtKB Sequence conflict 519 519 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P18412 1 486 +P18412 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P18412 UniProtKB Chain 2 486 . . . ID=PRO_0000205941;Note=Ty transcription activator TEC1 +P18412 UniProtKB DNA binding 125 199 . . . Note=TEA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00505 +P18412 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P18412 UniProtKB Modified residue 325 325 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region P53038 1 688 +P53038 UniProtKB Chain 1 688 . . . ID=PRO_0000215561;Note=Telomere length regulation protein TEL2 +P53038 UniProtKB Modified residue 417 417 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53038 UniProtKB Modified residue 419 419 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53038 UniProtKB Natural variant 129 129 . . . Note=In TEL2-1%3B short telomere length. S->R +P53038 UniProtKB Mutagenesis 333 333 . . . Note=Does not inhibit interaction with TTI1 or TTI2. Inhibits interaction with TTI1 or TTI2%3B when associated with E-345. L->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20801936;Dbxref=PMID:20801936 +P53038 UniProtKB Mutagenesis 345 345 . . . Note=Does not inhibit weakly interaction with TTI1 or TTI2. Inhibits interaction with TTI1 or TTI2%3B when associated with Q-333. M->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20801936;Dbxref=PMID:20801936 +P53038 UniProtKB Sequence conflict 226 226 . . . Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53038 UniProtKB Helix 2 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Turn 6 8 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 12 23 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 32 41 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 43 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Turn 46 48 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 51 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 66 77 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 85 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 104 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 116 126 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 130 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Turn 136 138 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 141 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 166 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 179 186 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 187 191 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 195 206 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 210 218 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 221 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 231 241 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 246 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 252 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 261 268 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 273 288 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 293 309 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 313 320 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 323 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 338 351 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 382 385 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 430 433 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 437 444 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 456 467 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 476 489 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Turn 497 500 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 501 513 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 515 517 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 518 525 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 532 550 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 616 618 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 619 632 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 642 657 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Beta strand 659 663 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +P53038 UniProtKB Helix 664 681 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3O4Z +##sequence-region Q06163 1 884 +Q06163 UniProtKB Chain 1 884 . . . ID=PRO_0000054932;Note=Telomerase reverse transcriptase +Q06163 UniProtKB Domain 422 725 . . . Note=Reverse transcriptase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405 +Q06163 UniProtKB Metal binding 530 530 . . . Note=Magnesium%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405 +Q06163 UniProtKB Metal binding 670 670 . . . Note=Magnesium%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405 +Q06163 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405 +Q06163 UniProtKB Sequence conflict 162 162 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53851 1 422 +P53851 UniProtKB Chain 1 422 . . . ID=PRO_0000051482;Note=Protein TEX1 +P53851 UniProtKB Repeat 61 100 . . . Note=WD 1 +P53851 UniProtKB Repeat 158 197 . . . Note=WD 2 +P53851 UniProtKB Repeat 207 246 . . . Note=WD 3 +P53851 UniProtKB Repeat 251 290 . . . Note=WD 4 +P53851 UniProtKB Repeat 293 332 . . . Note=WD 5 +##sequence-region P32367 1 649 +P32367 UniProtKB Chain 1 649 . . . ID=PRO_0000209717;Note=Transcription factor tau 95 kDa subunit +P32367 UniProtKB Repeat 221 239 . . . Note=1 +P32367 UniProtKB Repeat 400 419 . . . Note=2 +P32367 UniProtKB Region 221 419 . . . Note=2 X repeats%2C Pro-rich +P32367 UniProtKB Motif 296 300 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P32367 UniProtKB Compositional bias 510 620 . . . Note=Asp/Glu-rich (acidic) +P32367 UniProtKB Modified residue 617 617 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P32367 UniProtKB Mutagenesis 447 447 . . . Note=Temperature-sensitive. TFCIII-DNA complexes present a shift in their 5' border%2C generate slow-migrating TFIIIB-DNA complexes upon stripping TFIIIC by heparin or heat treatment%2C and allow initiation at downstream sites. TFIIIC-DNA complexes highly unstable at high temperatures. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12533520;Dbxref=PMID:12533520 +##sequence-region P53215 1 237 +P53215 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P53215 UniProtKB Chain 2 237 . . . ID=PRO_0000202788;Note=tRNA(His) guanylyltransferase +P53215 UniProtKB Nucleotide binding 29 34 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53215 UniProtKB Nucleotide binding 76 77 . . . Note=GTP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53215 UniProtKB Metal binding 29 29 . . . Note=Magnesium 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53215 UniProtKB Metal binding 29 29 . . . Note=Magnesium 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53215 UniProtKB Metal binding 30 30 . . . Note=Magnesium 1%3B via carbonyl oxygen%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53215 UniProtKB Metal binding 77 77 . . . Note=Magnesium 1%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53215 UniProtKB Metal binding 77 77 . . . Note=Magnesium 2%3B catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P53215 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +##sequence-region Q07748 1 340 +Q07748 UniProtKB Chain 1 340 . . . ID=PRO_0000211621;Note=4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI13 +Q07748 UniProtKB Region 115 118 . . . Note=Pyridoxal phosphate binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534 +Q07748 UniProtKB Motif 195 199 . . . Note=CCCFC%3B essential for catalytic activity%2C may be the site of iron coordination;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534 +Q07748 UniProtKB Active site 66 66 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534 +Q07748 UniProtKB Modified residue 62 62 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P43534 +##sequence-region Q08975 1 551 +Q08975 UniProtKB Chain 1 551 . . . ID=PRO_0000192042;Note=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI21 +Q08975 UniProtKB Binding site 64 64 . . . Note=Substrate;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q08579 1 599 +Q08579 UniProtKB Chain 1 599 . . . ID=PRO_0000197928;Note=Thiamine transporter THI72 +Q08579 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08579 UniProtKB Transmembrane 78 98 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08579 UniProtKB Transmembrane 112 132 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08579 UniProtKB Transmembrane 174 194 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08579 UniProtKB Transmembrane 197 217 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08579 UniProtKB Transmembrane 280 300 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08579 UniProtKB Transmembrane 333 353 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08579 UniProtKB Transmembrane 372 392 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08579 UniProtKB Transmembrane 395 415 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08579 UniProtKB Transmembrane 447 467 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08579 UniProtKB Transmembrane 484 504 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q08579 UniProtKB Modified residue 560 560 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05998 +Q08579 UniProtKB Modified residue 572 572 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08485 +##sequence-region P41544 1 203 +P41544 UniProtKB Chain 1 203 . . . ID=PRO_0000213942;Note=Protein SYS1 +P41544 UniProtKB Topological domain 1 29 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41544 UniProtKB Transmembrane 30 52 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41544 UniProtKB Topological domain 53 78 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41544 UniProtKB Transmembrane 79 101 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41544 UniProtKB Topological domain 102 105 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41544 UniProtKB Transmembrane 106 125 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41544 UniProtKB Topological domain 126 131 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41544 UniProtKB Transmembrane 132 154 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41544 UniProtKB Topological domain 155 203 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P41544 UniProtKB Modified residue 192 192 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P41544 UniProtKB Cross-link 15 15 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14557538;Dbxref=PMID:14557538 +P41544 UniProtKB Sequence conflict 149 203 . . . Note=GTWTTRWRELRDTFFEGLVDPNEGEVGLVTPSQQHSNHSELEQSPIQLKDLESQI->ALT;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P41896 1 400 +P41896 UniProtKB Chain 1 400 . . . ID=PRO_0000211240;Note=Transcription initiation factor IIF subunit beta +P41896 UniProtKB Modified residue 28 28 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P41896 UniProtKB Modified residue 34 34 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P41896 UniProtKB Modified residue 56 56 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P41896 UniProtKB Sequence conflict 232 232 . . . Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q05021 1 590 +Q05021 UniProtKB Chain 1 590 . . . ID=PRO_0000118885;Note=Transcription initiation factor TFIID subunit 7 +Q05021 UniProtKB Coiled coil 427 549 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05021 UniProtKB Compositional bias 7 90 . . . Note=Lys-rich +Q05021 UniProtKB Compositional bias 200 203 . . . Note=Poly-Glu +Q05021 UniProtKB Compositional bias 304 571 . . . Note=Asp/Glu-rich +Q05021 UniProtKB Modified residue 99 99 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +Q05021 UniProtKB Modified residue 101 101 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +Q05021 UniProtKB Modified residue 104 104 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +Q05021 UniProtKB Beta strand 97 100 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +Q05021 UniProtKB Beta strand 112 119 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +Q05021 UniProtKB Helix 126 135 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +Q05021 UniProtKB Beta strand 141 145 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +Q05021 UniProtKB Beta strand 147 155 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +Q05021 UniProtKB Beta strand 158 175 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +Q05021 UniProtKB Beta strand 177 197 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +Q05021 UniProtKB Helix 201 204 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +Q05021 UniProtKB Turn 215 219 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +Q05021 UniProtKB Helix 221 223 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +Q05021 UniProtKB Helix 224 234 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +Q05021 UniProtKB Helix 238 240 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +Q05021 UniProtKB Helix 245 249 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +Q05021 UniProtKB Helix 251 256 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +Q05021 UniProtKB Helix 267 269 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +Q05021 UniProtKB Turn 270 276 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +Q05021 UniProtKB Helix 283 301 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +Q05021 UniProtKB Beta strand 302 311 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4OY2 +##sequence-region P40468 1 2376 +P40468 UniProtKB Chain 1 2376 . . . ID=PRO_0000072430;Note=Cell morphogenesis protein PAG1 +P40468 UniProtKB Modified residue 141 141 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40468 UniProtKB Modified residue 1144 1144 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40468 UniProtKB Modified residue 2264 2264 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 +P40468 UniProtKB Modified residue 2267 2267 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40468 UniProtKB Modified residue 2355 2355 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +##sequence-region Q8TGM6 1 124 +Q8TGM6 UniProtKB Chain 1 124 . . . ID=PRO_0000072432;Note=Protein TAR1 +##sequence-region P38967 1 592 +P38967 UniProtKB Chain 1 592 . . . ID=PRO_0000054160;Note=Tryptophan permease +P38967 UniProtKB Topological domain 1 87 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Transmembrane 88 108 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Topological domain 109 113 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Transmembrane 114 134 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Topological domain 135 160 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Transmembrane 161 181 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Topological domain 182 192 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Transmembrane 193 213 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Topological domain 214 226 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Transmembrane 227 247 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Topological domain 248 266 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Transmembrane 267 287 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Topological domain 288 306 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Transmembrane 307 327 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Topological domain 328 358 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Transmembrane 359 379 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Topological domain 380 404 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Transmembrane 405 425 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Topological domain 426 428 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Transmembrane 429 449 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Topological domain 450 472 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Transmembrane 473 493 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Topological domain 494 514 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Transmembrane 515 535 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Topological domain 536 592 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38967 UniProtKB Sequence conflict 187 187 . . . Note=Q->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47030 1 604 +P47030 UniProtKB Chain 1 604 . . . ID=PRO_0000203050;Note=Protein TAX4 +P47030 UniProtKB Domain 469 559 . . . Note=EH +P47030 UniProtKB Compositional bias 182 239 . . . Note=Ser-rich +P47030 UniProtKB Compositional bias 397 422 . . . Note=His-rich +##sequence-region P26637 1 1090 +P26637 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P26637 UniProtKB Chain 2 1090 . . . ID=PRO_0000152155;Note=Leucine--tRNA ligase%2C cytoplasmic +P26637 UniProtKB Motif 66 76 . . . Note="HIGH" region +P26637 UniProtKB Motif 729 733 . . . Note="KMSKS" region +P26637 UniProtKB Binding site 732 732 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P26637 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P26637 UniProtKB Modified residue 142 142 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P00958 1 751 +P00958 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:3905796,ECO:0000269|PubMed:6371805;Dbxref=PMID:3905796,PMID:6371805 +P00958 UniProtKB Chain 2 751 . . . ID=PRO_0000139269;Note=Methionine--tRNA ligase%2C cytoplasmic +P00958 UniProtKB Region 36 92 . . . Note=Interaction with ARC1 +P00958 UniProtKB Motif 205 215 . . . Note="HIGH" region +P00958 UniProtKB Motif 525 529 . . . Note="KMSKS" region +P00958 UniProtKB Binding site 411 411 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P00958 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:3905796,ECO:0000269|PubMed:6371805;Dbxref=PMID:3905796,PMID:6371805 +P00958 UniProtKB Mutagenesis 63 63 . . . Note=Abolishes interaction with ARC1. A->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16914447;Dbxref=PMID:16914447 +P00958 UniProtKB Mutagenesis 502 502 . . . Note=In mes1%3B renders the protein unstable in vitro%2C elevates the KM for methionine in vivo. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3312199;Dbxref=PMID:3312199 +P00958 UniProtKB Mutagenesis 584 584 . . . Note=Abolishes aminoacylation activity. N->D%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1915850;Dbxref=PMID:1915850 +P00958 UniProtKB Mutagenesis 588 588 . . . Note=Abolishes aminoacylation activity. R->A%2CK%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1915850;Dbxref=PMID:1915850 +P00958 UniProtKB Sequence conflict 122 122 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00958 UniProtKB Sequence conflict 122 122 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P00958 UniProtKB Beta strand 3 5 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN +P00958 UniProtKB Beta strand 10 12 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN +P00958 UniProtKB Helix 15 31 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN +P00958 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN +P00958 UniProtKB Helix 61 68 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN +P00958 UniProtKB Turn 73 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN +P00958 UniProtKB Helix 78 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN +P00958 UniProtKB Turn 87 89 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN +P00958 UniProtKB Helix 90 92 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN +P00958 UniProtKB Beta strand 93 95 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN +P00958 UniProtKB Helix 98 111 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN +P00958 UniProtKB Helix 122 142 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN +P00958 UniProtKB Helix 148 157 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2HSN +##sequence-region P22438 1 575 +P22438 UniProtKB Chain 1 575 . . . ID=PRO_0000139272;Note=Methionine--tRNA ligase%2C mitochondrial +P22438 UniProtKB Motif 20 32 . . . Note="HIGH" region +P22438 UniProtKB Motif 341 345 . . . Note="KMSKS" region +P22438 UniProtKB Binding site 344 344 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P22438 UniProtKB Sequence conflict 14 14 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P04803 1 379 +P04803 UniProtKB Chain 1 379 . . . ID=PRO_0000136745;Note=Tryptophan--tRNA ligase%2C mitochondrial +P04803 UniProtKB Nucleotide binding 48 51 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UGM6 +P04803 UniProtKB Nucleotide binding 196 198 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UGM6 +P04803 UniProtKB Nucleotide binding 244 248 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UGM6 +P04803 UniProtKB Motif 43 51 . . . Note="HIGH" region +P04803 UniProtKB Motif 244 248 . . . Note="KMSKS" region +P04803 UniProtKB Binding site 42 42 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UGM6 +P04803 UniProtKB Binding site 184 184 . . . Note=L-tryptophan;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UGM6 +P04803 UniProtKB Binding site 235 235 . . . Note=ATP%3B via amide nitrogen and carbonyl oxygen;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UGM6 +P04803 UniProtKB Binding site 247 247 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P04803 UniProtKB Sequence conflict 268 271 . . . Note=KIRK->RLE;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P04803 UniProtKB Sequence conflict 371 379 . . . Note=ADIHKIMGF->PTFIK;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P48527 1 492 +P48527 UniProtKB Motif 94 103 . . . Note="HIGH" region +P48527 UniProtKB Motif 303 307 . . . Note="KMSKS" region +P48527 UniProtKB Binding site 89 89 . . . Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Z4 +P48527 UniProtKB Binding site 93 93 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Z4 +P48527 UniProtKB Binding site 133 133 . . . Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Z4 +P48527 UniProtKB Binding site 239 239 . . . Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Z4 +P48527 UniProtKB Binding site 243 243 . . . Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Z4 +P48527 UniProtKB Binding site 246 246 . . . Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Z4 +P48527 UniProtKB Binding site 265 265 . . . Note=Tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2Z4 +P48527 UniProtKB Binding site 306 306 . . . Note=ATP;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P36145 1 328 +P36145 UniProtKB Chain 1 328 . . . ID=PRO_0000211230;Note=Transcription initiation factor IIE subunit beta +P36145 UniProtKB DNA binding 113 187 . . . Note=TFIIE beta;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00682 +P36145 UniProtKB Compositional bias 86 93 . . . Note=Asp/Glu-rich (acidic) +P36145 UniProtKB Compositional bias 294 311 . . . Note=Arg/Lys-rich (basic) +P36145 UniProtKB Modified residue 52 52 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P36145 UniProtKB Modified residue 97 97 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P36145 UniProtKB Modified residue 106 106 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P36145 UniProtKB Sequence conflict 248 248 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P11747 1 167 +P11747 UniProtKB Chain 1 167 . . . ID=PRO_0000118912;Note=Transcription initiation factor TFIID subunit 13 +P11747 UniProtKB Domain 10 74 . . . Note=Histone-fold +P11747 UniProtKB Coiled coil 109 129 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P11747 UniProtKB Compositional bias 113 136 . . . Note=Asp/Glu-rich (acidic) +P11747 UniProtKB Modified residue 131 131 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P11747 UniProtKB Sequence conflict 137 138 . . . Note=AA->GV;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P11747 UniProtKB Sequence conflict 158 158 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P53228 1 333 +P53228 UniProtKB Chain 1 333 . . . ID=PRO_0000173575;Note=Transaldolase NQM1 +P53228 UniProtKB Active site 144 144 . . . Note=Schiff-base intermediate with substrate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10019 +P53228 UniProtKB Sequence conflict 290 290 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P53228 UniProtKB Helix 15 21 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Beta strand 25 29 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 33 35 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 37 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Beta strand 42 45 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 48 55 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 58 60 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 61 74 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 78 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Beta strand 105 108 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 111 113 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 117 133 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 138 140 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Beta strand 141 146 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 149 162 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Beta strand 166 171 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 174 182 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Beta strand 186 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 193 201 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Turn 209 211 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 213 228 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Beta strand 233 237 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 242 248 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Beta strand 251 257 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 258 266 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 277 280 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 281 283 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 294 303 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +P53228 UniProtKB Helix 305 333 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3CQ0 +##sequence-region P38085 1 619 +P38085 UniProtKB Chain 1 619 . . . ID=PRO_0000054162;Note=Valine/tyrosine/tryptophan amino-acid permease 1 +P38085 UniProtKB Topological domain 1 99 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Transmembrane 100 120 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Topological domain 121 122 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Transmembrane 123 143 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Topological domain 144 172 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Transmembrane 173 193 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Topological domain 194 204 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Transmembrane 205 225 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Topological domain 226 233 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Transmembrane 234 254 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Topological domain 255 281 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Transmembrane 282 302 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Topological domain 303 320 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Transmembrane 321 341 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Topological domain 342 368 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Transmembrane 369 389 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Topological domain 390 422 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Transmembrane 423 443 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Topological domain 444 446 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Transmembrane 447 467 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Topological domain 468 499 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Transmembrane 500 520 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Topological domain 521 529 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Transmembrane 530 550 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Topological domain 551 619 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38085 UniProtKB Modified residue 13 13 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38085 UniProtKB Modified residue 80 80 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P38085 UniProtKB Modified residue 84 84 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:17330950,PMID:18407956,PMID:19779198 +P38085 UniProtKB Cross-link 39 39 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P48606 1 106 +P48606 UniProtKB Chain 1 106 . . . ID=PRO_0000080045;Note=Tubulin-specific chaperone A +P48606 UniProtKB Modified residue 94 94 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:15665377,ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:15665377,PMID:18407956,PMID:19779198 +P48606 UniProtKB Helix 5 39 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSD +P48606 UniProtKB Helix 45 81 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSD +P48606 UniProtKB Beta strand 85 87 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSD +P48606 UniProtKB Helix 90 104 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1QSD +##sequence-region P46670 1 268 +P46670 UniProtKB Chain 1 268 . . . ID=PRO_0000089762;Note=Tubulin-specific chaperone C +P46670 UniProtKB Domain 98 255 . . . Note=C-CAP/cofactor C-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00659 +P46670 UniProtKB Sequence conflict 66 66 . . . Note=E->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46670 UniProtKB Beta strand 103 105 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA +P46670 UniProtKB Beta strand 107 110 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA +P46670 UniProtKB Beta strand 116 122 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA +P46670 UniProtKB Beta strand 124 127 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA +P46670 UniProtKB Beta strand 136 148 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA +P46670 UniProtKB Beta strand 150 154 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA +P46670 UniProtKB Beta strand 157 170 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA +P46670 UniProtKB Beta strand 172 177 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA +P46670 UniProtKB Beta strand 184 192 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA +P46670 UniProtKB Beta strand 194 199 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA +P46670 UniProtKB Beta strand 208 214 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA +P46670 UniProtKB Beta strand 216 221 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA +P46670 UniProtKB Helix 222 227 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA +P46670 UniProtKB Beta strand 228 232 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA +P46670 UniProtKB Beta strand 248 251 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA +P46670 UniProtKB Helix 256 258 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA +P46670 UniProtKB Helix 260 267 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5CYA +##sequence-region P38707 1 554 +P38707 UniProtKB Chain 1 554 . . . ID=PRO_0000176501;Note=Asparagine--tRNA ligase%2C cytoplasmic +##sequence-region P09734 1 445 +P09734 UniProtKB Chain 1 445 . . . ID=PRO_0000048240;Note=Tubulin alpha-3 chain +P09734 UniProtKB Nucleotide binding 143 149 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53904 1 254 +P53904 UniProtKB Chain 1 254 . . . ID=PRO_0000083536;Note=Tubulin-specific chaperone B +P53904 UniProtKB Domain 182 225 . . . Note=CAP-Gly;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00045 +##sequence-region P53378 1 473 +P53378 UniProtKB Chain 1 473 . . . ID=PRO_0000048481;Note=Tubulin gamma chain +P53378 UniProtKB Nucleotide binding 143 149 . . . Note=GTP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P48231 1 1178 +P48231 UniProtKB Chain 1 1178 . . . ID=PRO_0000203444;Note=Tricalbin-2 +P48231 UniProtKB Topological domain 1 98 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P48231 UniProtKB Transmembrane 99 119 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48231 UniProtKB Topological domain 120 120 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P48231 UniProtKB Transmembrane 121 141 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48231 UniProtKB Topological domain 142 1178 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P48231 UniProtKB Domain 365 463 . . . Note=C2 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 +P48231 UniProtKB Domain 637 733 . . . Note=C2 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 +P48231 UniProtKB Domain 970 1070 . . . Note=C2 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 +P48231 UniProtKB Coiled coil 784 821 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P48231 UniProtKB Modified residue 991 991 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12466 +P48231 UniProtKB Natural variant 11 13 . . . Note=In strain: SK1. DQI->EQV +P48231 UniProtKB Natural variant 121 121 . . . Note=In strain: SK1. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P48231 UniProtKB Natural variant 528 528 . . . Note=In strain: SK1. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +P48231 UniProtKB Natural variant 691 692 . . . Note=In strain: SK1. IE->MK +P48231 UniProtKB Natural variant 1159 1159 . . . Note=In strain: SK1. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16273108;Dbxref=PMID:16273108 +##sequence-region P12612 1 559 +P12612 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P12612 UniProtKB Chain 2 559 . . . ID=PRO_0000128315;Note=T-complex protein 1 subunit alpha +P12612 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22814378;Dbxref=PMID:22814378 +P12612 UniProtKB Mutagenesis 48 48 . . . Note=Temperature-sensitive. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7908441;Dbxref=PMID:7908441 +P12612 UniProtKB Sequence conflict 530 530 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P47079 1 568 +P47079 UniProtKB Chain 1 568 . . . ID=PRO_0000128378;Note=T-complex protein 1 subunit theta +P47079 UniProtKB Modified residue 505 505 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P47079 UniProtKB Cross-link 15 15 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131 +##sequence-region O13513 1 116 +O13513 UniProtKB Chain 1 116 . . . ID=PRO_0000299656;Note=Putative uncharacterized protein YAL056C-A +##sequence-region O13511 1 128 +O13511 UniProtKB Chain 1 128 . . . ID=PRO_0000248430;Note=Uncharacterized protein YAL065C +O13511 UniProtKB Transmembrane 105 127 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39728 1 267 +P39728 UniProtKB Chain 1 267 . . . ID=PRO_0000202418;Note=Uncharacterized protein YAL037W +##sequence-region P39725 1 102 +P39725 UniProtKB Chain 1 102 . . . ID=PRO_0000202420;Note=Putative uncharacterized protein YAL045C +##sequence-region Q8TGU6 1 64 +Q8TGU6 UniProtKB Chain 1 64 . . . ID=PRO_0000248437;Note=Uncharacterized protein YBR182C-A +##sequence-region Q12260 1 438 +Q12260 UniProtKB Chain 1 438 . . . ID=PRO_0000279275;Note=Transposon Ty2-B Gag polyprotein +Q12260 UniProtKB Chain 1 397 . . . ID=PRO_0000279276;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12260 UniProtKB Peptide 398 438 . . . ID=PRO_0000279277;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12260 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12260 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q8TGU5 1 39 +Q8TGU5 UniProtKB Chain 1 39 . . . ID=PRO_0000248445;Note=Uncharacterized protein YBR296C-A +##sequence-region P38311 1 105 +P38311 UniProtKB Chain 1 105 . . . ID=PRO_0000202511;Note=Uncharacterized protein YBR209W +P38311 UniProtKB Transmembrane 29 49 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38321 1 900 +P38321 UniProtKB Chain 1 900 . . . ID=PRO_0000202515;Note=Uncharacterized protein YBR225W +P38321 UniProtKB Modified residue 105 105 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P38331 1 238 +P38331 UniProtKB Chain 1 238 . . . ID=PRO_0000202522;Note=HD domain-containing protein YBR242W +P38331 UniProtKB Domain 77 183 . . . Note=HD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01175 +##sequence-region P38178 1 141 +P38178 UniProtKB Chain 1 141 . . . ID=PRO_0000202446;Note=Putative uncharacterized protein YBL083C +##sequence-region P38168 1 104 +P38168 UniProtKB Chain 1 104 . . . ID=PRO_0000202440;Note=Putative uncharacterized protein YBL100C +P38168 UniProtKB Transmembrane 77 98 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38240 1 142 +P38240 UniProtKB Chain 1 142 . . . ID=PRO_0000202477;Note=Putative uncharacterized membrane protein YBR064W +P38240 UniProtKB Topological domain 1 9 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38240 UniProtKB Transmembrane 10 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38240 UniProtKB Topological domain 31 41 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38240 UniProtKB Transmembrane 42 62 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38240 UniProtKB Topological domain 63 101 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38240 UniProtKB Transmembrane 102 122 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38240 UniProtKB Topological domain 123 142 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38276 1 179 +P38276 UniProtKB Chain 1 179 . . . ID=PRO_0000208926;Note=UPF0303 protein YBR137W +P38276 UniProtKB Sequence conflict 110 110 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38276 UniProtKB Sequence conflict 110 110 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38276 UniProtKB Helix 6 14 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC +P38276 UniProtKB Helix 19 27 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC +P38276 UniProtKB Beta strand 30 32 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC +P38276 UniProtKB Helix 36 53 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC +P38276 UniProtKB Beta strand 54 57 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC +P38276 UniProtKB Beta strand 60 64 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC +P38276 UniProtKB Beta strand 70 75 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC +P38276 UniProtKB Helix 82 98 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC +P38276 UniProtKB Helix 102 109 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC +P38276 UniProtKB Turn 114 116 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC +P38276 UniProtKB Turn 122 124 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC +P38276 UniProtKB Beta strand 131 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC +P38276 UniProtKB Turn 137 139 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC +P38276 UniProtKB Beta strand 143 151 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC +P38276 UniProtKB Helix 154 168 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC +P38276 UniProtKB Turn 169 172 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4CLC +##sequence-region P25565 1 263 +P25565 UniProtKB Chain 1 263 . . . ID=PRO_0000202537;Note=Putative uncharacterized protein YCL002C +P25565 UniProtKB Transmembrane 1 21 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25565 UniProtKB Transmembrane 38 58 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25565 UniProtKB Transmembrane 82 102 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25565 UniProtKB Transmembrane 118 138 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25565 UniProtKB Transmembrane 151 171 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25565 UniProtKB Transmembrane 196 216 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25565 UniProtKB Transmembrane 230 250 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P25561 1 117 +P25561 UniProtKB Chain 1 117 . . . ID=PRO_0000202540;Note=Putative uncharacterized protein YCL021W +##sequence-region O13527 1 1196 +O13527 UniProtKB Chain 1 1196 . . . ID=PRO_0000278977;Note=Truncated transposon Ty1-A Gag-Pol polyprotein +O13527 UniProtKB Chain 1 658 . . . ID=PRO_0000278980;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +O13527 UniProtKB Chain 659 1196 . . . ID=PRO_0000278981;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +O13527 UniProtKB Domain 101 276 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +O13527 UniProtKB Domain 779 917 . . . Note=Reverse transcriptase Ty1/copia-type +O13527 UniProtKB Domain 1051 1193 . . . Note=RNase H Ty1/copia-type +O13527 UniProtKB Motif 619 653 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +O13527 UniProtKB Metal binding 112 112 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +O13527 UniProtKB Metal binding 177 177 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +O13527 UniProtKB Metal binding 787 787 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +O13527 UniProtKB Metal binding 868 868 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +O13527 UniProtKB Metal binding 869 869 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +O13527 UniProtKB Metal binding 1051 1051 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +O13527 UniProtKB Metal binding 1093 1093 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +O13527 UniProtKB Metal binding 1126 1126 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +O13527 UniProtKB Site 658 659 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P0C5L1 1 78 +P0C5L1 UniProtKB Chain 1 78 . . . ID=PRO_0000309009;Note=Putative uncharacterized protein YBL068W-A +##sequence-region Q7M4S9 1 792 +Q7M4S9 UniProtKB Chain 1 792 . . . ID=PRO_0000248431;Note=Uncharacterized protein YBL113C +Q7M4S9 UniProtKB Repeat 91 102 . . . Note=1 +Q7M4S9 UniProtKB Repeat 103 114 . . . Note=2 +Q7M4S9 UniProtKB Repeat 115 126 . . . Note=3 +Q7M4S9 UniProtKB Repeat 127 138 . . . Note=4 +Q7M4S9 UniProtKB Repeat 139 150 . . . Note=5 +Q7M4S9 UniProtKB Repeat 151 162 . . . Note=6 +Q7M4S9 UniProtKB Repeat 163 174 . . . Note=7 +Q7M4S9 UniProtKB Repeat 175 186 . . . Note=8 +Q7M4S9 UniProtKB Repeat 187 198 . . . Note=9 +Q7M4S9 UniProtKB Repeat 199 210 . . . Note=10 +Q7M4S9 UniProtKB Repeat 211 222 . . . Note=11 +Q7M4S9 UniProtKB Repeat 223 234 . . . Note=12 +Q7M4S9 UniProtKB Repeat 235 246 . . . Note=13 +Q7M4S9 UniProtKB Repeat 247 258 . . . Note=14 +Q7M4S9 UniProtKB Repeat 259 270 . . . Note=15 +Q7M4S9 UniProtKB Repeat 271 282 . . . Note=16 +Q7M4S9 UniProtKB Repeat 283 294 . . . Note=17 +Q7M4S9 UniProtKB Repeat 295 306 . . . Note=18 +Q7M4S9 UniProtKB Repeat 307 318 . . . Note=19 +Q7M4S9 UniProtKB Repeat 319 330 . . . Note=20 +Q7M4S9 UniProtKB Repeat 331 342 . . . Note=21 +Q7M4S9 UniProtKB Repeat 343 354 . . . Note=22 +Q7M4S9 UniProtKB Repeat 355 366 . . . Note=23 +Q7M4S9 UniProtKB Repeat 367 378 . . . Note=24 +Q7M4S9 UniProtKB Repeat 379 390 . . . Note=25 +Q7M4S9 UniProtKB Region 91 390 . . . Note=25 X 12 AA tandem repeat of N-[SV]-[RS]-T-[NS]-A-T-T-T-[AE]-[ST]-[IT] +##sequence-region P0C5L4 1 52 +P0C5L4 UniProtKB Chain 1 52 . . . ID=PRO_0000309012;Note=Uncharacterized protein YBR121C-A +##sequence-region Q8TGK5 1 160 +Q8TGK5 UniProtKB Chain 1 160 . . . ID=PRO_0000299783;Note=Putative UPF0479 protein YBL113W-A +Q8TGK5 UniProtKB Transmembrane 39 59 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q8TGK5 UniProtKB Transmembrane 136 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E755 1 54 +Q3E755 UniProtKB Signal peptide 1 13 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E755 UniProtKB Chain 14 54 . . . ID=PRO_0000248440;Note=Uncharacterized protein YBR200W-A +##sequence-region Q8TGQ3 1 39 +Q8TGQ3 UniProtKB Chain 1 39 . . . ID=PRO_0000299796;Note=Putative uncharacterized protein YBR223W-A +##sequence-region P38296 1 124 +P38296 UniProtKB Chain 1 124 . . . ID=PRO_0000202504;Note=Putative uncharacterized protein YBR178W +##sequence-region P38327 1 119 +P38327 UniProtKB Chain 1 119 . . . ID=PRO_0000202519;Note=Putative uncharacterized protein YBR232C +P38327 UniProtKB Transmembrane 61 80 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38327 UniProtKB Transmembrane 87 103 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38354 1 144 +P38354 UniProtKB Chain 1 144 . . . ID=PRO_0000202534;Note=Putative uncharacterized protein YBR285W +P38354 UniProtKB Sequence conflict 55 55 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38354 UniProtKB Sequence conflict 55 55 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P38354 UniProtKB Sequence conflict 55 55 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38362 1 165 +P38362 UniProtKB Chain 1 165 . . . ID=PRO_0000202536;Note=Putative uncharacterized protein YBR300C +P38362 UniProtKB Transmembrane 10 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E778 1 34 +Q3E778 UniProtKB Chain 1 34 . . . ID=PRO_0000248439;Note=Uncharacterized protein YBR196C-B +##sequence-region P32788 1 280 +P32788 UniProtKB Chain 1 280 . . . ID=PRO_0000076536;Note=Uncharacterized protein YBL010C +P32788 UniProtKB Domain 225 264 . . . Note=bZIP +P32788 UniProtKB Region 225 240 . . . Note=Basic motif;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P32788 UniProtKB Region 250 264 . . . Note=Leucine-zipper;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38177 1 466 +P38177 UniProtKB Chain 1 466 . . . ID=PRO_0000202445;Note=Uncharacterized protein YBL086C +P38177 UniProtKB Domain 8 206 . . . Note=NT-C2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38177 UniProtKB Modified residue 433 433 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17287358,ECO:0000244|PubMed:19779198;Dbxref=PMID:17287358,PMID:19779198 +P38177 UniProtKB Modified residue 439 439 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P38177 UniProtKB Sequence conflict 318 318 . . . Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38171 1 102 +P38171 UniProtKB Chain 1 102 . . . ID=PRO_0000014308;Note=Putative uncharacterized protein YBL096C +##sequence-region P38214 1 139 +P38214 UniProtKB Chain 1 139 . . . ID=PRO_0000202468;Note=Putative uncharacterized protein YBR012C +##sequence-region P38315 1 674 +P38315 UniProtKB Chain 1 674 . . . ID=PRO_0000066150;Note=YAP1-binding protein 1 +P38315 UniProtKB Compositional bias 613 616 . . . Note=Poly-Leu +P38315 UniProtKB Natural variant 7 7 . . . Note=In strain: W303-1a. I->L +P38315 UniProtKB Natural variant 328 328 . . . Note=In strain: W303-1a. F->V +P38315 UniProtKB Natural variant 343 343 . . . Note=In strain: W303-1a. K->E +P38315 UniProtKB Natural variant 570 570 . . . Note=In strain: W303-1a. N->D +##sequence-region P38267 1 160 +P38267 UniProtKB Chain 1 160 . . . ID=PRO_0000202487;Note=Putative uncharacterized membrane protein YBR113W +P38267 UniProtKB Topological domain 1 33 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38267 UniProtKB Transmembrane 34 54 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38267 UniProtKB Topological domain 55 68 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38267 UniProtKB Transmembrane 69 89 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38267 UniProtKB Topological domain 90 119 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38267 UniProtKB Transmembrane 120 140 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38267 UniProtKB Topological domain 141 160 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38275 1 133 +P38275 UniProtKB Chain 1 133 . . . ID=PRO_0000202492;Note=Putative uncharacterized protein YBR134W +##sequence-region P34215 1 104 +P34215 UniProtKB Chain 1 104 . . . ID=PRO_0000202495;Note=Uncharacterized protein YBR144C +##sequence-region Q96VH2 1 84 +Q96VH2 UniProtKB Chain 1 84 . . . ID=PRO_0000248412;Note=Putative pelota-like protein YCL001W-B +##sequence-region P25571 1 164 +P25571 UniProtKB Chain 1 164 . . . ID=PRO_0000202544;Note=Putative uncharacterized protein YCL041C +##sequence-region P25350 1 157 +P25350 UniProtKB Chain 1 157 . . . ID=PRO_0000202560;Note=Uncharacterized protein YCR006C +##sequence-region Q3E7Z7 1 40 +Q3E7Z7 UniProtKB Chain 1 40 . . . ID=PRO_0000242622;Note=Uncharacterized protein YDR003W-A +Q3E7Z7 UniProtKB Compositional bias 14 17 . . . Note=Poly-Lys +##sequence-region Q12281 1 103 +Q12281 UniProtKB Chain 1 103 . . . ID=PRO_0000299848;Note=Putative uncharacterized protein YDL032w +##sequence-region Q07793 1 1604 +Q07793 UniProtKB Chain 1 1604 . . . ID=PRO_0000279017;Note=Transposon Ty1-DR4 Gag-Pol polyprotein +Q07793 UniProtKB Chain 1 401 . . . ID=PRO_0000279018;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07793 UniProtKB Chain 402 582 . . . ID=PRO_0000279019;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07793 UniProtKB Chain 583 1217 . . . ID=PRO_0000279020;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07793 UniProtKB Chain 1218 1604 . . . ID=PRO_0000279021;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07793 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q07793 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +Q07793 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07793 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q07793 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07793 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q07793 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q07793 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q07793 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q07793 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q07793 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q07793 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07793 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07793 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07793 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region Q12082 1 118 +Q12082 UniProtKB Chain 1 118 . . . ID=PRO_0000240875;Note=Uncharacterized protein YDL157C%2C mitochondrial +##sequence-region Q12148 1 100 +Q12148 UniProtKB Chain 1 100 . . . ID=PRO_0000299861;Note=Putative uncharacterized protein YDL163W +##sequence-region Q03983 1 463 +Q03983 UniProtKB Chain 1 463 . . . ID=PRO_0000202588;Note=Uncharacterized protein YDR179W-A +##sequence-region P48568 1 277 +P48568 UniProtKB Chain 1 277 . . . ID=PRO_0000202589;Note=Uncharacterized protein YDL186W +P48568 UniProtKB Compositional bias 51 54 . . . Note=Poly-Arg +P48568 UniProtKB Compositional bias 240 252 . . . Note=Poly-Gln +P48568 UniProtKB Sequence conflict 273 273 . . . Note=F->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q2V2P9 1 66 +Q2V2P9 UniProtKB Chain 1 66 . . . ID=PRO_0000253829;Note=Uncharacterized protein YDR119W-A +Q2V2P9 UniProtKB Transmembrane 39 61 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03787 1 373 +Q03787 UniProtKB Chain 1 373 . . . ID=PRO_0000253841;Note=Uncharacterized protein YDR249C +##sequence-region Q05612 1 105 +Q05612 UniProtKB Chain 1 105 . . . ID=PRO_0000299881;Note=Uncharacterized protein YDR278C +Q05612 UniProtKB Transmembrane 64 84 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q05497 1 695 +Q05497 UniProtKB Chain 1 695 . . . ID=PRO_0000164255;Note=Uncharacterized transporter YDR338C +Q05497 UniProtKB Transmembrane 237 257 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05497 UniProtKB Transmembrane 265 285 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05497 UniProtKB Transmembrane 313 333 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05497 UniProtKB Transmembrane 344 364 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05497 UniProtKB Transmembrane 380 400 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05497 UniProtKB Transmembrane 408 428 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05497 UniProtKB Transmembrane 457 477 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05497 UniProtKB Transmembrane 488 508 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05497 UniProtKB Transmembrane 531 551 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05497 UniProtKB Transmembrane 565 585 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05497 UniProtKB Transmembrane 604 624 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05497 UniProtKB Transmembrane 633 653 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q05497 UniProtKB Modified residue 113 113 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region Q3E6R5 1 114 +Q3E6R5 UniProtKB Chain 1 114 . . . ID=PRO_0000253850;Note=Uncharacterized mitochondrial outer membrane protein YDR381C-A +Q3E6R5 UniProtKB Transmembrane 13 30 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P87266 1 191 +P87266 UniProtKB Chain 1 191 . . . ID=PRO_0000299890;Note=Putative uncharacterized protein YDR413C +P87266 UniProtKB Transmembrane 12 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P87266 UniProtKB Transmembrane 48 68 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P87266 UniProtKB Transmembrane 92 112 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P87266 UniProtKB Transmembrane 168 188 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P87266 UniProtKB Compositional bias 57 185 . . . Note=Ser-rich +##sequence-region Q8TGP5 1 62 +Q8TGP5 UniProtKB Chain 1 62 . . . ID=PRO_0000299897;Note=Putative uncharacterized protein YDR464C-A +##sequence-region P87274 1 156 +P87274 UniProtKB Chain 1 156 . . . ID=PRO_0000299903;Note=Putative uncharacterized protein YDR526C +P87274 UniProtKB Transmembrane 21 41 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P87274 UniProtKB Transmembrane 54 74 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P87274 UniProtKB Transmembrane 80 100 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P87261 1 201 +P87261 UniProtKB Chain 1 201 . . . ID=PRO_0000299905;Note=Putative uncharacterized protein YDR537C +##sequence-region P0CL37 1 159 +P0CL37 UniProtKB Chain 1 159 . . . ID=PRO_0000299784;Note=Putative UPF0479 protein YDR545C-A +P0CL37 UniProtKB Transmembrane 38 58 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL37 UniProtKB Transmembrane 135 155 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CL37 UniProtKB Compositional bias 102 105 . . . Note=Poly-Ser +##sequence-region Q02896 1 317 +Q02896 UniProtKB Chain 1 317 . . . ID=PRO_0000212465;Note=Alkaline ceramidase YDC1 +Q02896 UniProtKB Topological domain 1 42 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02896 UniProtKB Transmembrane 43 60 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02896 UniProtKB Topological domain 61 66 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02896 UniProtKB Transmembrane 67 89 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02896 UniProtKB Topological domain 90 98 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02896 UniProtKB Transmembrane 99 121 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02896 UniProtKB Topological domain 122 133 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02896 UniProtKB Transmembrane 134 156 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02896 UniProtKB Topological domain 157 159 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02896 UniProtKB Transmembrane 160 182 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02896 UniProtKB Topological domain 183 202 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02896 UniProtKB Transmembrane 203 225 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02896 UniProtKB Topological domain 226 239 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02896 UniProtKB Transmembrane 240 262 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q02896 UniProtKB Topological domain 263 317 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40057 1 128 +P40057 UniProtKB Chain 1 128 . . . ID=PRO_0000202638;Note=Uncharacterized protein YER084W +P40057 UniProtKB Sequence conflict 57 57 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P40093 1 338 +P40093 UniProtKB Chain 1 338 . . . ID=PRO_0000213487;Note=UPF0160 protein YER156C +##sequence-region Q3E838 1 28 +Q3E838 UniProtKB Chain 1 28 . . . ID=PRO_0000245374;Note=Uncharacterized protein YFR012W-A +##sequence-region P43541 1 151 +P43541 UniProtKB Chain 1 151 . . . ID=PRO_0000211372;Note=Putative UPF0320 protein YFL063W +##sequence-region P43600 1 232 +P43600 UniProtKB Chain 1 232 . . . ID=PRO_0000202689;Note=Uncharacterized protein YFR020W +P43600 UniProtKB Glycosylation 25 25 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43600 UniProtKB Glycosylation 26 26 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43600 UniProtKB Glycosylation 53 53 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43600 UniProtKB Glycosylation 77 77 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P43600 UniProtKB Glycosylation 163 163 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0C5N1 1 53 +P0C5N1 UniProtKB Chain 1 53 . . . ID=PRO_0000309029;Note=Uncharacterized protein YGL014C-A +##sequence-region P53185 1 909 +P53185 UniProtKB Chain 1 909 . . . ID=PRO_0000096613;Note=Uncharacterized protein YGL036W +P53185 UniProtKB Compositional bias 377 387 . . . Note=Poly-Asn +P53185 UniProtKB Compositional bias 394 405 . . . Note=Poly-Thr +P53185 UniProtKB Compositional bias 406 413 . . . Note=Poly-Asn +P53185 UniProtKB Compositional bias 758 763 . . . Note=Poly-Gln +P53185 UniProtKB Modified residue 856 856 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P53185 UniProtKB Modified residue 898 898 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region O13515 1 117 +O13515 UniProtKB Signal peptide 1 20 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13515 UniProtKB Chain 21 117 . . . ID=PRO_0000299654;Note=Putative uncharacterized protein YAL034C-B +##sequence-region O13514 1 125 +O13514 UniProtKB Chain 1 125 . . . ID=PRO_0000299655;Note=Putative uncharacterized protein YAL042C-A +O13514 UniProtKB Transmembrane 96 113 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PYD0 1 140 +A0A023PYD0 UniProtKB Chain 1 140 . . . ID=PRO_0000430974;Note=Putative uncharacterized membrane protein YAL059C-A +A0A023PYD0 UniProtKB Transmembrane 42 62 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PYD0 UniProtKB Transmembrane 65 85 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PYD0 UniProtKB Transmembrane 96 116 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P0CX18 1 203 +P0CX18 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX18 UniProtKB Chain 24 184 . . . ID=PRO_0000202945;Note=Putative GPI-anchored protein YAR066W +P0CX18 UniProtKB Propeptide 185 203 . . . ID=PRO_0000409753;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX18 UniProtKB Compositional bias 25 57 . . . Note=Ser-rich +P0CX18 UniProtKB Lipidation 184 184 . . . Note=GPI-anchor amidated asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX18 UniProtKB Glycosylation 28 28 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX18 UniProtKB Glycosylation 138 138 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P47118 1 141 +P47118 UniProtKB Chain 1 141 . . . ID=PRO_0000203099;Note=Uncharacterized protein YAE1 +##sequence-region P0CX90 1 67 +P0CX90 UniProtKB Chain 1 67 . . . ID=PRO_0000202431;Note=Uncharacterized protein YAR061W +##sequence-region P0CX92 1 97 +P0CX92 UniProtKB Chain 1 97 . . . ID=PRO_0000202435;Note=Putative uncharacterized protein YAR069C +P0CX92 UniProtKB Transmembrane 5 25 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX92 UniProtKB Transmembrane 27 47 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P0CX92 UniProtKB Transmembrane 77 97 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P40574 1 245 +P40574 UniProtKB Chain 1 245 . . . ID=PRO_0000076525;Note=AP-1-like transcription factor YAP5 +P40574 UniProtKB Domain 58 121 . . . Note=bZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P40574 UniProtKB Region 63 82 . . . Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P40574 UniProtKB Region 86 114 . . . Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 +P40574 UniProtKB Sequence conflict 173 173 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region Q3E756 1 94 +Q3E756 UniProtKB Chain 1 94 . . . ID=PRO_0000248433;Note=UPF0768 protein YBL029C-A +##sequence-region P0C5L0 1 52 +P0C5L0 UniProtKB Chain 1 52 . . . ID=PRO_0000309008;Note=Putative uncharacterized protein YBR056C-B +P0C5L0 UniProtKB Compositional bias 28 34 . . . Note=Poly-Gln +##sequence-region P34220 1 418 +P34220 UniProtKB Chain 1 418 . . . ID=PRO_0000201994;Note=Deoxyribonuclease Tat-D +P34220 UniProtKB Metal binding 185 185 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P34220 UniProtKB Metal binding 185 185 . . . Note=Divalent metal cation 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P34220 UniProtKB Metal binding 226 226 . . . Note=Divalent metal cation 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P34220 UniProtKB Metal binding 277 277 . . . Note=Divalent metal cation 2;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P34220 UniProtKB Metal binding 327 327 . . . Note=Divalent metal cation 1;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P34220 UniProtKB Mutagenesis 185 185 . . . Note=Reduces enzymatic activities by 50%25. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15657035;Dbxref=PMID:15657035 +P34220 UniProtKB Mutagenesis 325 325 . . . Note=Reduces enzymatic activities by 50%25. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15657035;Dbxref=PMID:15657035 +P34220 UniProtKB Mutagenesis 327 327 . . . Note=Reduces enzymatic activities by almost 95%25. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15657035;Dbxref=PMID:15657035 +P34220 UniProtKB Sequence conflict 278 278 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region P38185 1 102 +P38185 UniProtKB Chain 1 102 . . . ID=PRO_0000202450;Note=Uncharacterized protein YBL071C +P38185 UniProtKB Transmembrane 77 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38183 1 143 +P38183 UniProtKB Chain 1 143 . . . ID=PRO_0000202448;Note=Putative uncharacterized protein YBL077W +##sequence-region P38173 1 110 +P38173 UniProtKB Chain 1 110 . . . ID=PRO_0000202443;Note=Putative uncharacterized protein YBL094C +P38173 UniProtKB Transmembrane 21 41 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38173 UniProtKB Transmembrane 63 83 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P53169 1 641 +P53169 UniProtKB Chain 1 641 . . . ID=PRO_0000066151;Note=YAP1-binding protein 2 +##sequence-region P38256 1 230 +P38256 UniProtKB Chain 1 230 . . . ID=PRO_0000202483;Note=Uncharacterized protein YBR096W +##sequence-region P25577 1 312 +P25577 UniProtKB Signal peptide 1 19 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +P25577 UniProtKB Chain 20 312 . . . ID=PRO_0000014312;Note=Uncharacterized protein YCL049C +P25577 UniProtKB Compositional bias 286 292 . . . Note=Poly-Glu +##sequence-region P25601 1 146 +P25601 UniProtKB Chain 1 146 . . . ID=PRO_0000203504;Note=Putative transposon Ty5-1 protein YCL075W +##sequence-region P25616 1 317 +P25616 UniProtKB Chain 1 317 . . . ID=PRO_0000202562;Note=UPF0655 protein YCR015C +##sequence-region P25629 1 148 +P25629 UniProtKB Chain 1 148 . . . ID=PRO_0000202570;Note=Putative uncharacterized protein YCR049C +##sequence-region P25630 1 102 +P25630 UniProtKB Chain 1 102 . . . ID=PRO_0000202571;Note=Uncharacterized protein YCR050C +##sequence-region P25608 1 368 +P25608 UniProtKB Chain 1 368 . . . ID=PRO_0000202585;Note=Uncharacterized protein YCR102C +##sequence-region Q2V2Q0 1 85 +Q2V2Q0 UniProtKB Chain 1 85 . . . ID=PRO_0000248455;Note=Putative uncharacterized protein YDL007C-A +##sequence-region Q12185 1 396 +Q12185 UniProtKB Chain 1 396 . . . ID=PRO_0000208208;Note=Uncharacterized acyltransferase YDR018C +Q12185 UniProtKB Transmembrane 27 47 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12185 UniProtKB Transmembrane 69 89 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12185 UniProtKB Transmembrane 123 143 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12185 UniProtKB Transmembrane 372 392 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12185 UniProtKB Motif 117 122 . . . Note=HXXXXD motif +##sequence-region Q12352 1 117 +Q12352 UniProtKB Chain 1 117 . . . ID=PRO_0000299850;Note=Putative uncharacterized protein YDL041W +Q12352 UniProtKB Transmembrane 76 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q03831 1 136 +Q03831 UniProtKB Chain 1 136 . . . ID=PRO_0000299872;Note=Putative uncharacterized protein YDR095C +##sequence-region Q03856 1 440 +Q03856 UniProtKB Chain 1 440 . . . ID=PRO_0000279006;Note=Transposon Ty1-DR1 Gag polyprotein +Q03856 UniProtKB Chain 1 401 . . . ID=PRO_0000279007;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03856 UniProtKB Peptide 402 440 . . . ID=PRO_0000279008;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03856 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03856 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q03856 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03856 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region Q07541 1 149 +Q07541 UniProtKB Chain 1 149 . . . ID=PRO_0000240867;Note=Uncharacterized protein YDL121C +Q07541 UniProtKB Topological domain 1 6 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07541 UniProtKB Transmembrane 7 27 . . . Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07541 UniProtKB Topological domain 28 149 . . . Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region O74302 1 440 +O74302 UniProtKB Chain 1 440 . . . ID=PRO_0000279022;Note=Transposon Ty1-DR4 Gag polyprotein +O74302 UniProtKB Chain 1 401 . . . ID=PRO_0000279023;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +O74302 UniProtKB Peptide 402 440 . . . ID=PRO_0000279024;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +O74302 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +O74302 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +O74302 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +O74302 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region P0CX70 1 440 +P0CX70 UniProtKB Chain 1 440 . . . ID=PRO_0000279037;Note=Transposon Ty1-DR6 Gag polyprotein +P0CX70 UniProtKB Chain 1 401 . . . ID=PRO_0000279038;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX70 UniProtKB Peptide 402 440 . . . ID=PRO_0000279039;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX70 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX70 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +P0CX70 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P0CX70 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12441 +##sequence-region Q12027 1 708 +Q12027 UniProtKB Chain 1 708 . . . ID=PRO_0000240880;Note=Uncharacterized protein YDL176W +##sequence-region Q03964 1 440 +Q03964 UniProtKB Chain 1 440 . . . ID=PRO_0000279040;Note=Transposon Ty1-DR2 Gag polyprotein +Q03964 UniProtKB Chain 1 401 . . . ID=PRO_0000279041;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03964 UniProtKB Peptide 402 440 . . . ID=PRO_0000279042;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03964 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03964 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q3E818 1 50 +Q3E818 UniProtKB Chain 1 50 . . . ID=PRO_0000253836;Note=Uncharacterized protein YDR194W-A +##sequence-region Q12424 1 762 +Q12424 UniProtKB Signal peptide 1 26 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Chain 27 762 . . . ID=PRO_0000242480;Note=Putative cation exchanger YDL206W +Q12424 UniProtKB Topological domain 27 30 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Transmembrane 31 51 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Topological domain 52 102 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Transmembrane 103 123 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Topological domain 124 156 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Transmembrane 157 177 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Topological domain 178 178 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Transmembrane 179 199 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Topological domain 200 501 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Transmembrane 502 522 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Topological domain 523 554 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Transmembrane 555 575 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Topological domain 576 589 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Transmembrane 590 610 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Topological domain 611 615 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Transmembrane 616 636 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Topological domain 637 650 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Transmembrane 651 671 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Topological domain 672 709 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Transmembrane 710 730 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Topological domain 731 738 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Transmembrane 739 759 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Topological domain 760 762 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Glycosylation 28 28 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Glycosylation 148 148 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Glycosylation 280 280 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Glycosylation 329 329 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12424 UniProtKB Glycosylation 645 645 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q07629 1 317 +Q07629 UniProtKB Chain 1 317 . . . ID=PRO_0000242482;Note=Uncharacterized membrane protein YDL218W +Q07629 UniProtKB Topological domain 1 13 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07629 UniProtKB Transmembrane 14 34 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07629 UniProtKB Topological domain 35 49 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07629 UniProtKB Transmembrane 50 70 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07629 UniProtKB Topological domain 71 71 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07629 UniProtKB Transmembrane 72 92 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07629 UniProtKB Topological domain 93 133 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07629 UniProtKB Transmembrane 134 154 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07629 UniProtKB Topological domain 155 317 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07629 UniProtKB Compositional bias 239 259 . . . Note=Thr-rich +Q07629 UniProtKB Glycosylation 43 43 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q07629 UniProtKB Glycosylation 129 129 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04923 1 97 +Q04923 UniProtKB Chain 1 97 . . . ID=PRO_0000299877;Note=Putative uncharacterized protein YDR220C +##sequence-region A0A023PZA9 1 115 +A0A023PZA9 UniProtKB Chain 1 115 . . . ID=PRO_0000430984;Note=Putative uncharacterized protein YDR230W +##sequence-region Q99303 1 438 +Q99303 UniProtKB Chain 1 438 . . . ID=PRO_0000279305;Note=Transposon Ty2-DR3 Gag polyprotein +Q99303 UniProtKB Chain 1 397 . . . ID=PRO_0000279306;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99303 UniProtKB Peptide 398 438 . . . ID=PRO_0000279307;Note=Gag-p4;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99303 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q99303 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q07791 1 1770 +Q07791 UniProtKB Chain 1 1770 . . . ID=PRO_0000279300;Note=Transposon Ty2-DR3 Gag-Pol polyprotein +Q07791 UniProtKB Chain 1 397 . . . ID=PRO_0000279301;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07791 UniProtKB Chain 398 578 . . . ID=PRO_0000279302;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07791 UniProtKB Chain 579 1232 . . . ID=PRO_0000279303;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07791 UniProtKB Chain 1233 1770 . . . ID=PRO_0000279304;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07791 UniProtKB Domain 656 831 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q07791 UniProtKB Domain 1353 1491 . . . Note=Reverse transcriptase Ty1/copia-type +Q07791 UniProtKB Domain 1625 1767 . . . Note=RNase H Ty1/copia-type +Q07791 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07791 UniProtKB Region 579 636 . . . Note=Integrase-type zinc finger-like +Q07791 UniProtKB Motif 1193 1227 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07791 UniProtKB Active site 457 457 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07791 UniProtKB Metal binding 667 667 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q07791 UniProtKB Metal binding 732 732 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q07791 UniProtKB Metal binding 1361 1361 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q07791 UniProtKB Metal binding 1442 1442 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q07791 UniProtKB Metal binding 1443 1443 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q07791 UniProtKB Metal binding 1625 1625 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q07791 UniProtKB Metal binding 1667 1667 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q07791 UniProtKB Metal binding 1700 1700 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q07791 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07791 UniProtKB Site 578 579 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q07791 UniProtKB Site 1232 1233 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region Q05510 1 147 +Q05510 UniProtKB Chain 1 147 . . . ID=PRO_0000299885;Note=Uncharacterized protein YDR344C +##sequence-region P0C5M1 1 34 +P0C5M1 UniProtKB Chain 1 34 . . . ID=PRO_0000309019;Note=Uncharacterized protein YDR371C-A +##sequence-region Q04162 1 555 +Q04162 UniProtKB Chain 1 555 . . . ID=PRO_0000252274;Note=Probable metabolite transport protein YDR387C +Q04162 UniProtKB Topological domain 1 39 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Transmembrane 40 60 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Topological domain 61 83 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Transmembrane 84 104 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Topological domain 105 118 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Transmembrane 119 139 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Topological domain 140 140 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Transmembrane 141 161 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Topological domain 162 168 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Transmembrane 169 189 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Topological domain 190 200 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Transmembrane 201 221 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Topological domain 222 356 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Transmembrane 357 377 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Topological domain 378 384 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Transmembrane 385 405 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Topological domain 406 413 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Transmembrane 414 434 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Topological domain 435 440 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Transmembrane 441 461 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Topological domain 462 474 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Transmembrane 475 497 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Topological domain 498 506 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Transmembrane 507 527 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Topological domain 528 555 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q04162 UniProtKB Compositional bias 315 318 . . . Note=Poly-Ser +##sequence-region P87268 1 125 +P87268 UniProtKB Chain 1 125 . . . ID=PRO_0000299891;Note=Putative uncharacterized protein YDR426C +##sequence-region A0A023PYD7 1 172 +A0A023PYD7 UniProtKB Chain 1 172 . . . ID=PRO_0000430986;Note=Putative uncharacterized membrane protein YDR187C +A0A023PYD7 UniProtKB Transmembrane 109 129 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q12187 1 109 +Q12187 UniProtKB Chain 1 109 . . . ID=PRO_0000299864;Note=Putative uncharacterized protein YDL196W +Q12187 UniProtKB Transmembrane 19 39 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q12187 UniProtKB Transmembrane 53 73 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q04597 1 100 +Q04597 UniProtKB Chain 1 100 . . . ID=PRO_0000277620;Note=Uncharacterized protein YDR114C +##sequence-region A0A023PZ94 1 102 +A0A023PZ94 UniProtKB Chain 1 102 . . . ID=PRO_0000430972;Note=Putative uncharacterized membrane protein YAL031W-A +A0A023PZ94 UniProtKB Transmembrane 28 48 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZ94 UniProtKB Transmembrane 81 101 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGV0 1 26 +Q8TGV0 UniProtKB Chain 1 26 . . . ID=PRO_0000248426;Note=Uncharacterized protein YAR035C-A +Q8TGV0 UniProtKB Sequence conflict 24 24 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +Q8TGV0 UniProtKB Sequence conflict 24 24 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 +##sequence-region A0A023PZE2 1 109 +A0A023PZE2 UniProtKB Chain 1 109 . . . ID=PRO_0000430973;Note=Putative uncharacterized membrane protein YAL047W-A +A0A023PZE2 UniProtKB Transmembrane 24 44 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PZE2 UniProtKB Transmembrane 68 88 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGR8 1 324 +Q8TGR8 UniProtKB Chain 1 324 . . . ID=PRO_0000299746;Note=Putative uncharacterized protein YAL037C-B +##sequence-region O13512 1 126 +O13512 UniProtKB Chain 1 126 . . . ID=PRO_0000248429;Note=Uncharacterized membrane protein YAL064W-B +O13512 UniProtKB Topological domain 1 28 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13512 UniProtKB Transmembrane 29 49 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13512 UniProtKB Topological domain 50 75 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13512 UniProtKB Transmembrane 76 96 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13512 UniProtKB Topological domain 97 97 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13512 UniProtKB Transmembrane 98 118 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +O13512 UniProtKB Topological domain 119 126 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39711 1 94 +P39711 UniProtKB Chain 1 94 . . . ID=PRO_0000202425;Note=Putative uncharacterized protein YAL064W +##sequence-region P14680 1 807 +P14680 UniProtKB Chain 1 807 . . . ID=PRO_0000086828;Note=Dual specificity protein kinase YAK1 +P14680 UniProtKB Domain 369 704 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P14680 UniProtKB Nucleotide binding 375 383 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P14680 UniProtKB Compositional bias 56 85 . . . Note=Gln-rich +P14680 UniProtKB Active site 496 496 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 +P14680 UniProtKB Binding site 398 398 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 +P14680 UniProtKB Modified residue 38 38 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P14680 UniProtKB Modified residue 115 115 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14680 UniProtKB Modified residue 118 118 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14680 UniProtKB Modified residue 127 127 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 +P14680 UniProtKB Modified residue 206 206 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14680 UniProtKB Modified residue 240 240 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14680 UniProtKB Modified residue 245 245 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14680 UniProtKB Modified residue 247 247 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P14680 UniProtKB Modified residue 288 288 . . . Note=Phosphothreonine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P14680 UniProtKB Modified residue 295 295 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17287358;Dbxref=PMID:17287358 +P14680 UniProtKB Modified residue 530 530 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:17330950,ECO:0000244|PubMed:19779198,ECO:0000269|PubMed:10816418;Dbxref=PMID:17330950,PMID:19779198,PMID:10816418 +##sequence-region P46683 1 200 +P46683 UniProtKB Chain 1 200 . . . ID=PRO_0000067079;Note=Ankyrin repeat-containing protein YAR1 +P46683 UniProtKB Repeat 49 78 . . . Note=ANK 1 +P46683 UniProtKB Repeat 92 121 . . . Note=ANK 2 +P46683 UniProtKB Modified residue 78 78 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P46683 UniProtKB Sequence conflict 118 118 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 +P46683 UniProtKB Helix 10 22 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P46683 UniProtKB Helix 25 34 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P46683 UniProtKB Helix 38 43 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P46683 UniProtKB Turn 47 49 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P46683 UniProtKB Helix 53 59 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P46683 UniProtKB Helix 63 76 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P46683 UniProtKB Helix 79 86 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P46683 UniProtKB Helix 96 102 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P46683 UniProtKB Helix 106 114 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P46683 UniProtKB Helix 130 136 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +P46683 UniProtKB Helix 140 149 . . . Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4BSZ +##sequence-region Q3E794 1 53 +Q3E794 UniProtKB Chain 1 53 . . . ID=PRO_0000248435;Note=Uncharacterized protein YBR072C-A +##sequence-region P90471 1 74 +P90471 UniProtKB Chain 1 74 . . . ID=PRO_0000299793;Note=Putative uncharacterized protein YBR109W-A +P90471 UniProtKB Transmembrane 15 32 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q6B113 1 34 +Q6B113 UniProtKB Chain 1 34 . . . ID=PRO_0000299791;Note=Putative uncharacterized protein YBL107W-A +##sequence-region Q12491 1 1770 +Q12491 UniProtKB Chain 1 1770 . . . ID=PRO_0000279270;Note=Transposon Ty2-B Gag-Pol polyprotein +Q12491 UniProtKB Chain 1 397 . . . ID=PRO_0000279271;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12491 UniProtKB Chain 398 578 . . . ID=PRO_0000279272;Note=Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12491 UniProtKB Chain 579 1232 . . . ID=PRO_0000279273;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12491 UniProtKB Chain 1233 1770 . . . ID=PRO_0000279274;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12491 UniProtKB Domain 656 831 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12491 UniProtKB Domain 1353 1491 . . . Note=Reverse transcriptase Ty1/copia-type +Q12491 UniProtKB Domain 1625 1767 . . . Note=RNase H Ty1/copia-type +Q12491 UniProtKB Region 295 397 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12491 UniProtKB Region 579 636 . . . Note=Integrase-type zinc finger-like +Q12491 UniProtKB Motif 1193 1227 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12491 UniProtKB Active site 457 457 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12491 UniProtKB Metal binding 667 667 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12491 UniProtKB Metal binding 732 732 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12491 UniProtKB Metal binding 1361 1361 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12491 UniProtKB Metal binding 1442 1442 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12491 UniProtKB Metal binding 1443 1443 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12491 UniProtKB Metal binding 1625 1625 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12491 UniProtKB Metal binding 1667 1667 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12491 UniProtKB Metal binding 1700 1700 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q12491 UniProtKB Site 397 398 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12491 UniProtKB Site 578 579 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q12491 UniProtKB Site 1232 1233 . . . Note=Cleavage%3B by Ty2 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38317 1 127 +P38317 UniProtKB Chain 1 127 . . . ID=PRO_0000202513;Note=Uncharacterized protein YBR219C +P38317 UniProtKB Transmembrane 64 84 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38317 UniProtKB Transmembrane 101 118 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38322 1 136 +P38322 UniProtKB Chain 1 136 . . . ID=PRO_0000202516;Note=Putative uncharacterized protein YBR226C +##sequence-region P38357 1 123 +P38357 UniProtKB Chain 1 123 . . . ID=PRO_0000202535;Note=Uncharacterized protein YBR292C +P38357 UniProtKB Transmembrane 25 45 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38357 UniProtKB Transmembrane 78 98 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38350 1 133 +P38350 UniProtKB Chain 1 133 . . . ID=PRO_0000202533;Note=Putative uncharacterized protein YBR277C +##sequence-region P38188 1 114 +P38188 UniProtKB Chain 1 114 . . . ID=PRO_0000202452;Note=Putative uncharacterized protein YBL065W +##sequence-region P38184 1 103 +P38184 UniProtKB Chain 1 103 . . . ID=PRO_0000202449;Note=Putative uncharacterized protein YBL073W +##sequence-region Q8TGQ1 1 68 +Q8TGQ1 UniProtKB Chain 1 68 . . . ID=PRO_0000299838;Note=Putative uncharacterized protein YCR047W-A +##sequence-region Q96VG6 1 88 +Q96VG6 UniProtKB Chain 1 88 . . . ID=PRO_0000299840;Note=Putative uncharacterized protein YCR097W-A +Q96VG6 UniProtKB Transmembrane 27 46 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q96VG6 UniProtKB Transmembrane 61 83 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PXB0 1 110 +A0A023PXB0 UniProtKB Chain 1 110 . . . ID=PRO_0000430970;Note=Putative uncharacterized protein YAR019W-A +##sequence-region O42831 1 157 +O42831 UniProtKB Chain 1 157 . . . ID=PRO_0000248413;Note=Putative inosine-5'-monophosphate dehydrogenase-like protein YAR075W +##sequence-region A0A023PYC6 1 104 +A0A023PYC6 UniProtKB Signal peptide 1 25 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +A0A023PYC6 UniProtKB Chain 26 104 . . . ID=PRO_0000430975;Note=Putative uncharacterized membrane protein YAL016C-A +A0A023PYC6 UniProtKB Transmembrane 79 99 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P39548 1 234 +P39548 UniProtKB Chain 1 234 . . . ID=PRO_0000207529;Note=DUP240 protein YAR028W +P39548 UniProtKB Topological domain 1 47 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39548 UniProtKB Transmembrane 48 68 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39548 UniProtKB Topological domain 69 76 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39548 UniProtKB Transmembrane 77 97 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39548 UniProtKB Topological domain 98 234 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P39548 UniProtKB Cross-link 217 217 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:22106047;Dbxref=PMID:22106047 +##sequence-region P0CX88 1 111 +P0CX88 UniProtKB Chain 1 111 . . . ID=PRO_0000202430;Note=Putative uncharacterized protein YAR060C +##sequence-region P0CI66 1 198 +P0CI66 UniProtKB Chain 1 198 . . . ID=PRO_0000202432;Note=Putative uncharacterized protein YAR062W +P0CI66 UniProtKB Domain 1 110 . . . Note=PA14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01164 +P0CI66 UniProtKB Compositional bias 133 198 . . . Note=Ser/Thr-rich +##sequence-region P39564 1 161 +P39564 UniProtKB Chain 1 161 . . . ID=PRO_0000202434;Note=Uncharacterized protein YAR068W +##sequence-region P40917 1 295 +P40917 UniProtKB Chain 1 295 . . . ID=PRO_0000076524;Note=AP-1-like transcription factor YAP4 +P40917 UniProtKB Domain 237 295 . . . Note=bZIP +P40917 UniProtKB Region 239 260 . . . Note=Basic motif;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40917 UniProtKB Region 262 271 . . . Note=Leucine-zipper;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P40917 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40917 UniProtKB Modified residue 89 89 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40917 UniProtKB Modified residue 196 196 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P39710 1 102 +P39710 UniProtKB Chain 1 102 . . . ID=PRO_0000202426;Note=Putative uncharacterized protein YAL066W +##sequence-region Q3E821 1 79 +Q3E821 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E821 UniProtKB Chain 25 79 . . . ID=PRO_0000248434;Note=Uncharacterized protein YBL008W-A +Q3E821 UniProtKB Glycosylation 33 33 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q3E7Y5 1 667 +Q3E7Y5 UniProtKB Chain 1 667 . . . ID=PRO_0000248406;Note=Uncharacterized helicase-like protein YBL111C +Q3E7Y5 UniProtKB Domain 375 552 . . . Note=Helicase ATP-binding +Q3E7Y5 UniProtKB Nucleotide binding 388 395 . . . Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E7Y5 UniProtKB Motif 498 501 . . . Note=DEAH box +##sequence-region Q8TGU7 1 68 +Q8TGU7 UniProtKB Chain 1 68 . . . ID=PRO_0000299747;Note=Uncharacterized protein YBR126W-A +Q8TGU7 UniProtKB Transmembrane 24 44 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGQ5 1 29 +Q8TGQ5 UniProtKB Chain 1 29 . . . ID=PRO_0000299794;Note=Putative uncharacterized protein YBR131C-A +##sequence-region P0C5L5 1 24 +P0C5L5 UniProtKB Chain 1 24 . . . ID=PRO_0000309013;Note=Putative uncharacterized protein YBR191W-A +##sequence-region P0C268 1 59 +P0C268 UniProtKB Chain 1 59 . . . ID=PRO_0000268624;Note=Uncharacterized protein YBL039W-B +##sequence-region Q3E820 1 49 +Q3E820 UniProtKB Chain 1 49 . . . ID=PRO_0000248438;Note=Uncharacterized protein YBR196C-A +Q3E820 UniProtKB Transmembrane 6 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38190 1 124 +P38190 UniProtKB Chain 1 124 . . . ID=PRO_0000202455;Note=Putative uncharacterized protein YBL053W +P38190 UniProtKB Transmembrane 27 51 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38186 1 106 +P38186 UniProtKB Chain 1 106 . . . ID=PRO_0000202451;Note=Putative uncharacterized protein YBL070C +P38186 UniProtKB Transmembrane 43 63 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +P38186 UniProtKB Transmembrane 86 106 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38081 1 501 +P38081 UniProtKB Chain 1 501 . . . ID=PRO_0000184055;Note=Uncharacterized glycosyl hydrolase YBR056W +P38081 UniProtKB Active site 236 236 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250 +P38081 UniProtKB Active site 333 333 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 +##sequence-region P38252 1 199 +P38252 UniProtKB Chain 1 199 . . . ID=PRO_0000202480;Note=Putative uncharacterized protein YBR089W +P38252 UniProtKB Transmembrane 21 38 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P38258 1 127 +P38258 UniProtKB Chain 1 127 . . . ID=PRO_0000202484;Note=Putative uncharacterized protein YBR099C +P38258 UniProtKB Transmembrane 84 103 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region P25572 1 119 +P25572 UniProtKB Chain 1 119 . . . ID=PRO_0000202545;Note=Putative uncharacterized protein YCL042W +##sequence-region Q12448 1 114 +Q12448 UniProtKB Chain 1 114 . . . ID=PRO_0000299849;Note=Putative uncharacterized protein YDL034W +##sequence-region Q3E6R4 1 66 +Q3E6R4 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E6R4 UniProtKB Chain 19 42 . . . ID=PRO_0000253883;Note=Uncharacterized protein YDR524C-B +Q3E6R4 UniProtKB Propeptide 43 66 . . . ID=PRO_0000253884;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E6R4 UniProtKB Lipidation 42 42 . . . Note=GPI-anchor amidated glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E6R4 UniProtKB Glycosylation 20 20 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E6R4 UniProtKB Glycosylation 24 24 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E6R4 UniProtKB Glycosylation 27 27 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E6R4 UniProtKB Glycosylation 30 30 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +Q3E6R4 UniProtKB Glycosylation 33 33 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region A0A023PZF2 1 135 +A0A023PZF2 UniProtKB Chain 1 135 . . . ID=PRO_0000430990;Note=Uncharacterized protein YEL009C-A +##sequence-region Q3E7B0 1 37 +Q3E7B0 UniProtKB Chain 1 37 . . . ID=PRO_0000245370;Note=Uncharacterized protein YER053C-A +Q3E7B0 UniProtKB Transmembrane 1 21 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 +##sequence-region Q8TGR4 1 48 +Q8TGR4 UniProtKB Chain 1 48 . . . ID=PRO_0000299658;Note=Putative uncharacterized protein YER088W-B +##sequence-region Q03612 1 1755 +Q03612 UniProtKB Chain 1 1755 . . . ID=PRO_0000279043;Note=Transposon Ty1-ER1 Gag-Pol polyprotein +Q03612 UniProtKB Chain 1 401 . . . ID=PRO_0000279044;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03612 UniProtKB Chain 402 582 . . . ID=PRO_0000279045;Note=Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03612 UniProtKB Chain 583 1217 . . . ID=PRO_0000279046;Note=Integrase;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03612 UniProtKB Chain 1218 1755 . . . ID=PRO_0000279047;Note=Reverse transcriptase/ribonuclease H;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03612 UniProtKB Domain 660 835 . . . Note=Integrase catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03612 UniProtKB Domain 1338 1476 . . . Note=Reverse transcriptase Ty1/copia-type +Q03612 UniProtKB Domain 1610 1752 . . . Note=RNase H Ty1/copia-type +Q03612 UniProtKB Region 299 401 . . . Note=RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03612 UniProtKB Region 583 640 . . . Note=Integrase-type zinc finger-like +Q03612 UniProtKB Motif 1178 1212 . . . Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03612 UniProtKB Compositional bias 64 146 . . . Note=Pro-rich +Q03612 UniProtKB Active site 461 461 . . . Note=For protease activity%3B shared with dimeric partner;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094 +Q03612 UniProtKB Metal binding 671 671 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03612 UniProtKB Metal binding 736 736 . . . Note=Magnesium%3B catalytic%3B for integrase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03612 UniProtKB Metal binding 1346 1346 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03612 UniProtKB Metal binding 1427 1427 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03612 UniProtKB Metal binding 1428 1428 . . . Note=Magnesium%3B catalytic%3B for reverse transcriptase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03612 UniProtKB Metal binding 1610 1610 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03612 UniProtKB Metal binding 1652 1652 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03612 UniProtKB Metal binding 1685 1685 . . . Note=Magnesium%3B catalytic%3B for RNase H activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00457 +Q03612 UniProtKB Site 401 402 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03612 UniProtKB Site 582 583 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03612 UniProtKB Site 1217 1218 . . . Note=Cleavage%3B by Ty1 protease;Ontology_term=ECO:0000250;evidence=ECO:0000250 +Q03612 UniProtKB Modified residue 416 416 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99231 +##sequence-region P40103 1 239 +P40103 UniProtKB Chain 1 239 . . . ID=PRO_0000202664;Note=Uncharacterized protein YER188W +##sequence-region P40104 1 122 +P40104 UniProtKB Chain 1 122 . . . ID=PRO_0000202665;Note=Uncharacterized protein YER189W +##sequence-region P32622 1 495 +P32622 UniProtKB Chain 1 495 . . . ID=PRO_0000120717;Note=ATP-NADH kinase YEF1 +##sequence-region P40052 1 210 +P40052 UniProtKB Chain 1 210 . . . ID=PRO_0000202636;Note=Uncharacterized protein YER079W +P40052 UniProtKB Modified residue 18 18 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40052 UniProtKB Modified residue 39 39 . . . Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:18407956,ECO:0000244|PubMed:19779198;Dbxref=PMID:18407956,PMID:19779198 +P40052 UniProtKB Modified residue 41 41 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40052 UniProtKB Modified residue 57 57 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:15665377;Dbxref=PMID:15665377 +P40052 UniProtKB Modified residue 60 60 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:17330950;Dbxref=PMID:17330950 +P40052 UniProtKB Modified residue 178 178 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +P40052 UniProtKB Modified residue 189 189 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:18407956;Dbxref=PMID:18407956 +P40052 UniProtKB Modified residue 192 192 . . . Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19779198;Dbxref=PMID:19779198 +##sequence-region P40560 1 513 +P40560 UniProtKB Chain 1 513 . . . ID=PRO_0000067246;Note=Ankyrin repeat-containing protein YIL001W +P40560 UniProtKB Repeat 8 37 . . . Note=ANK 1 +P40560 UniProtKB Repeat 41 70 . . . Note=ANK 2 +P40560 UniProtKB Domain 122 179 . . . Note=BTB 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00037 +P40560 UniProtKB Domain 274 360 . . . Note=BTB 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00037 +##sequence-region P40536 1 118 +P40536 UniProtKB Chain 1 118 . . . ID=PRO_0000202995;Note=Putative uncharacterized protein YIL032C +##sequence-region E2QC18 1 100 +##sequence-region E9PAE8 1 55 +##sequence-region E9PAE4 1 146 +E9PAE4 UniProtKB Transmembrane 31 55 . . . Note=Helical;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:Phobius +##sequence-region E9PAD8 1 89 +E9PAD8 UniProtKB Transmembrane 64 84 . . . Note=Helical;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:Phobius +##sequence-region E9PAE3 1 403 +E9PAE3 UniProtKB Domain 233 403 . . . Note=Integrase catalytic;Ontology_term=ECO:0000259;evidence=ECO:0000259|PROSITE:PS50994 +##sequence-region E9PAE7 1 61 +##sequence-region E9PAD6 1 88 +E9PAD6 UniProtKB Transmembrane 6 32 . . . Note=Helical;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:Phobius +E9PAD6 UniProtKB Transmembrane 52 72 . . . Note=Helical;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:Phobius +##sequence-region E9PAF1 1 94 diff --git a/test_files/yeastID.txt b/test_files/yeastID.txt new file mode 100644 index 0000000..7bd016d --- /dev/null +++ b/test_files/yeastID.txt @@ -0,0 +1,6730 @@ +Entry Gene names (ordered locus ) Gene names (primary ) +P12688 YKL126W YPK1 +P25491 YNL064C YDJ1 +P16521 YLR249W YEF3 +P11484 YDL229W SSB1 +P39940 YER125W RSP5 +Q04437 YMR106C YKU80 +Q06224 YLR277C YSH1 +P32795 YPR024W YME1 +Q06102 YPR107C YTH1 +P02829 YPL240C HSP82 +P38801 YHR081W LRP1 +P40009 YER005W YND1 +P10591 YAL005C SSA1 +P38340 YBR261C TAE1 +P41800 YLL006W MMM1 +P00546 YBR160W CDC28 +P15108 YMR186W HSC82 +P31539 YLL026W HSP104 +P25623 YCR030C SYP1 +P08539 YHR005C GPA1 +P32502 YLR291C GCD7 +P15442 YDR283C GCN2 +P10592 YLL024C SSA2 +P06782 YDR477W SNF1 +P22147 YGL173C XRN1 +P32598 YER133W GLC7 +P53230 YGR046W TAM41 +Q06510 YPR140W TAZ1 +Q02457 YPL128C TBF1 +P39078 YDL143W CCT4 +Q3E7C1 YDR079C-A TFB5 +Q06339 YDR362C TFC6 +Q12308 YPL007C TFC8 +Q06490 YPR121W THI22 +Q04083 YDR438W THI74 +P35202 YOR143C THI80 +Q08231 YOL072W THP1 +P16120 YCR053W THR4 +P40328 YPL074W YTA6 +P39077 YJL014W CCT3 +P35691 YKL056C TMA19 +P38987 YML064C TEM1 +P53916 YNL128W TEP1 +P29055 YPR086W SUA7 +P29056 YGR246C BRF1 +P38141 YBR240C THI2 +P32318 YGR144W THI4 +P32897 YNR017W TIM23 +Q08144 YOL018C TLG2 +P07273 YGL043W DST1 +P54857 YDR058C TGL2 +Q12052 YPL157W TGS1 +P00927 YER086W ILV1 +P41338 YPL028W ERG10 +P57744 YJR135W-A TIM8 +O74700 YEL020W-A TIM9 +Q12218 YOR009W TIR4 +Q04562 YDR107C TMN2 +P53507 YNL070W TOM7 +Q07904 YLR004C THI73 +Q05998 YLR237W THI7 +P40040 YER063W THO1 +P53552 YNL139C THO2 +O13539 YHR167W THP2 +Q07914 YLR008C PAM18 +P39515 YJL143W TIM17 +Q01852 YIL022W TIM44 +P27654 YBR067C TIP1 +P10863 YER011W TIR1 +P54837 YML012W ERV25 +P32802 YLR083C EMP70 +Q06417 YLR426W TDA5 +Q03290 YDR460W TFB3 +P46678 YNL039W BDP1 +Q12415 YOR110W TFC7 +P40308 YMR313C TGL3 +P42883 YNL332W THI12 +Q08224 YOL055C THI20 +P40340 YGR270W YTA7 +P38228 YBR044C TCM62 +Q08921 YPL180W TCO89 +P32776 YDR311W TFB1 +P33339 YGR047C TFC4 +Q08686 YOR251C TUM1 +P42949 YJL104W PAM16 +Q12328 YDL217C TIM22 +P33315 YBR117C TKL2 +Q12239 YOL107W +Q03525 YMR269W TMA23 +Q04600 YDR117C TMA64 +P36165 YKR089C TGL4 +P47183 YJR156C THI11 +Q07471 YDL080C THI3 +P43534 YFL058W THI5 +P41835 YPL214C THI6 +P27796 YIL160C POT1 +P87108 YHR005C-A TIM10 +P33891 YGL145W TIP20 +P89886 YER007C-A TMA20 +Q12049 YPR045C THP3 +P40462 YIL137C TMA108 +P36142 YKR051W +Q12513 YDL110C TMA17 +P53840 YNL273W TOF1 +P40310 YJL093C TOK1 +Q03280 YDR457W TOM1 +P35180 YGR082W TOM20 +P23644 YMR203W TOM40 +P80967 YPR133W-A TOM5 +P38825 YHR117W TOM71 +P32830 YBR091C TIM12 +P53299 YGR181W TIM13 +Q08749 YOR297C TIM18 +P53220 YGR033C TIM21 +P33890 YOR010C TIR2 +Q08422 YOR052C TMC1 +P40071 YER113C TMN3 +P32773 YOR194C TOA1 +P04786 YOL006C TOP1 +P06786 YNL088W TOP2 +P35169 YJR066W TOR1 +P53147 YGL096W TOS8 +Q12272 YOL102C TPT1 +Q06177 YLR327C TMA10 +Q12116 YDR105C TMS1 +P13099 YLR234W TOP3 +P49334 YNL131W TOM22 +P38288 YBR162C TOS1 +P43637 YGL179C TOS3 +Q03796 YMR156C TPP1 +P53738 YNR046W TRM112 +P12685 YJL129C TRK1 +Q12400 YOL093W TRM10 +Q12463 YOL124C TRM11 +P15565 YDR120C TRM1 +Q02648 YPL030W TRM44 +P41814 YNL062C GCD10 +Q08687 YOR252W TMA16 +Q3E764 YLR262C-A TMA7 +P32643 YER175C TMT1 +P32600 YKL203C TOR2 +P17536 YNL079C TPM1 +P53099 YGL186C TPN1 +P53283 YGR138C TPO2 +Q12256 YOR273C TPO4 +Q03496 YMR259C TRM732 +Q05024 YMR233W TRI1 +P33753 YKR056W TRM2 +P38793 YHR070W TRM5 +P09880 YJL087C TRL1 +P46944 YDR108W TRS85 +P22217 YLR043C TRX1 +P34760 YML028W TSA1 +P40061 YER093C TSC11 +Q02776 YPL063W TIM50 +P40552 YIL011W TIR3 +Q12000 YOR091W TMA46 +Q06266 YLR183C TOS4 +Q07824 YLL028W TPO1 +P47045 YJL054W TIM54 +Q12199 YPR040W TIP41 +P23254 YPR074C TKL1 +Q03322 YDR468C TLG1 +P53322 YGR260W TNA1 +Q08919 YPL176C TRE1 +Q03774 YDR165W TRM82 +P38334 YBR254C TRS20 +P32893 YGR166W TRS65 +Q02208 YKR010C TOF2 +P07213 YNL121C TOM70 +P48560 YNL300W TOS6 +P00942 YDR050C TPI1 +P40414 YIL138C TPM2 +Q06451 YPR156C TPO3 +P36029 YKL174C TPO5 +Q04183 YDR407C TRS120 +Q03660 YMR218C TRS130 +P38342 YBR265W TSC10 +P38427 YML100W TSL1 +P50078 YGR221C TOS2 +P53257 YGR096W TPC1 +Q00764 YBR126C TPS1 +P35172 YBR001C NTH2 +Q07527 YDL112W TRM3 +Q02721 YLR329W REC102 +P34219 YBL054W TOD6 +P33448 YOR045W TOM6 +P38811 YHR099W TRA1 +Q08693 YOR256C TRE2 +P48561 YNL299W TRF5 +P28584 YKR050W TRK2 +Q12383 YOL125W TRM13 +P25040 YOL022C TSR4 +P36164 YKR088C TVP38 +P33122 YOR344C TYE7 +P06785 YOR074C CDC21 +P0CF16 YML003W +P21734 YDR177W UBC1 +P33296 YER100W UBC6 +P36026 YKR098C UBP11 +P38237 YBR058C UBP14 +P32571 YDR069C DOA4 +P40453 YIL156W UBP7 +P19812 YGR184C UBR1 +Q07963 YLR024C UBR2 +Q04228 YML013W UBX2 +Q06682 YDR330W UBX5 +Q03337 YDR472W TRS31 +Q07381 YDL060W TSR1 +P20049 YBR166C TYR1 +P07285 YDR354W TRP4 +Q03784 YDR246W TRS23 +P25372 YCR083W TRX3 +P29509 YDR353W TRR1 +P47168 YJR136C TTI2 +P38962 YDR084C TVP23 +P22803 YGR209C TRX2 +P38254 YBR094W PBY1 +P29340 YGR133W PEX4 +Q12094 YOR006C TSR3 +Q08747 YOR295W UAF30 +P14682 YDR054C CDC34 +P40032 YER049W TPA1 +P31688 YDR074W TPS2 +P38426 YMR261C TPS3 +P46959 YJL125C GCD14 +P38238 YBR061C TRM7 +P49957 YML014W TRM9 +Q12009 YDL201W TRM8 +P00912 YDR007W TRP1 +Q03860 YDR100W TVP15 +P53250 YGR080W TWF1 +P00899 YER090W TRP2 +P00937 YKL211C TRP3 +P00931 YGL026C TRP5 +Q3E790 YBR058C-A TSC3 +Q04767 YMR071C TVP18 +Q99394 YOR115C TRS33 +Q04120 YDR453C TSA2 +Q06672 YLR435W TSR2 +P36097 YKL033W TTI1 +P16649 YCR084C TUP1 +P32356 YDR001C NTH1 +P38816 YHR106W TRR2 +P53044 YGR048W UFD1 +P33202 YKL010C UFD4 +P26370 YDL170W UGA3 +P36137 YKR044W UIP5 +Q02724 YPL020C ULP1 +Q05776 YLR193C UPS1 +P28274 YBL039C URA7 +P38627 YJR103W URA8 +Q05946 YLR222C UTP13 +Q04305 YMR093W UTP15 +P40362 YJL069C UTP18 +P35194 YBL004W UTP20 +P40498 YIL091C UTP25 +Q02354 YDR449C UTP6 +Q08474 YOR068C VAM10 +P16140 YBR127C VMA2 +P38358 YBR293W VBA2 +Q04602 YDR119W VBA4 +P39538 YJL197W UBP12 +Q01477 YER151C UBP3 +P39967 YER098W UBP9 +Q12229 YDL091C UBX3 +P47049 YJL048C UBX6 +P40554 YIL008W URM1 +Q04500 YML093W UTP14 +Q12339 YOR004W UTP23 +P43123 YDL103C QRI1 +P52490 YDR092W UBC13 +Q02159 YMR022W UBC7 +Q12059 YPL003W ULA1 +Q08562 YOR191W ULS1 +Q03010 YPL139C UME1 +P25386 YDL058W USO1 +P42945 YJL109C UTP10 +Q06078 YLR409C UTP21 +P53254 YGR090W UTP22 +Q04177 YDR398W UTP5 +P53276 YGR128C UTP8 +P21373 YJR049C UTR1 +P35127 YJR099W YUH1 +Q01476 YOR124C UBP2 +P43593 YFR010W UBP6 +P50102 YMR223W UBP8 +P54730 YMR067C UBX4 +P36135 YKR042W UTH1 +Q12220 YLR129W DIP2 +Q06679 YDR324C UTP4 +P38882 YHR196W UTP9 +P25591 YCL063W VAC17 +Q07468 YDL077C VAM6 +P17255 YDL185W VMA1 +P38152 YBR291C CTP1 +Q04235 YML005W TRM12 +P06104 YGL058W RAD6 +P39944 YER144C UBP5 +P38349 YBR273C UBX7 +P47108 YJR041C URB2 +P53146 YGL098W USE1 +P53177 YGL050W TYW3 +P22515 YKL210W UBA1 +Q99344 YPR066W UBA3 +P52492 YOR339C UBC11 +P52491 YLR306W UBC12 +P15732 YDR059C UBC5 +P38187 YBL067C UBP13 +P25037 YDL122W UBP1 +P38290 YBR165W UBS1 +P32861 YKL035W UGP1 +P38709 YHL012W +P38293 YBR173C UMP1 +Q08960 YPL207W TYW1 +Q08282 YOL141W PPM2 +P38820 YHR111W UBA4 +P15731 YBR082C UBC4 +P28263 YEL012W UBC8 +P34223 YBL058W SHP1 +Q04511 YML088W UFO1 +P40537 YIL031W ULP2 +Q12151 YDR213W UPC2 +P36096 YKL034W TUL1 +Q06412 YLR425W TUS1 +P38319 YBR223C TDP1 +P53874 YNL186W UBP10 +P08067 YEL024W RIP1 +P41834 YOR075W UFE1 +P0CF17 YML002W +P52488 YDR390C UBA2 +P50623 YDL064W UBC9 +P0CG63 YLL039C UBI4 +P50101 YMR304W UBP15 +Q02863 YPL072W UBP16 +P32837 YDL210W UGA4 +Q03327 YDR470C UGO1 +P39547 YAR027W UIP3 +Q04006 YDR185C UPS3 +P12887 YML021C UNG1 +P18562 YHR128W FUR1 +Q04411 YDR520C URC2 +P27515 YNR012W URK1 +P32366 YLR447C VMA6 +P40003 YEL005C VAB2 +Q06708 YLR386W VAC14 +Q99385 YDL128W VCX1 +P53058 YGL258W VEL1 +P54860 YDL190C UFD2 +P32772 YDL169C UGX2 +Q08926 YPL186C UIP4 +P43604 YFR026C ULI1 +P39001 YDR207C UME6 +P48412 YGR072W UPF3 +P35200 YLR168C UPS2 +Q12208 YLR132C USB1 +P34247 YKL099C UTP11 +Q02931 YPL126W NAN1 +P40055 YER082C UTP7 +P32630 YEL035C UTR5 +P39111 YGR020C VMA7 +Q12063 YDL193W NUS1 +P34241 YKL014C URB1 +P23202 YNL229C URE2 +Q03714 YML029W USA1 +P41807 YPR036W VMA13 +P25515 YEL027W VMA3 +P36172 YKR105C VBA5 +P04840 YNL055C POR1 +P40157 YNL212W VID27 +Q06685 YLR410W VIP1 +Q04311 YDR049W VMS1 +P38067 YBR006W UGA2 +Q04179 YDR400W URH1 +Q3E7B6 YCL005W-A VMA9 +P39968 YEL013W VAC8 +P32912 YGL212W VAM7 +Q05934 YLR373C VID22 +Q12241 YOR106W VAM3 +P23642 YML115C VAN1 +P32610 YEL051W VMA8 +P48836 YHR039C-A VMA10 +P32319 YBL017C PEP1 +P32913 YOR132W VPS17 +Q04272 YMR077C VPS20 +Q05919 YLR360W VPS38 +P39702 YAL002W VPS8 +P32842 YPL234C VMA11 +P38329 YBR235W VHC1 +P40522 YIL056W VHR1 +Q08438 YOR054C VHS3 +P53285 YGR141W VPS62 +P53142 YGL104C VPS73 +Q06525 YPR152C URN1 +Q12132 YPL230W USV1 +P53950 YNL054W VAC7 +P40041 YER064C VHR2 +P23968 YHR026W VMA16 +P40478 YIL114C POR2 +O13549 YLR261C VPS63 +P47161 YJR126C VPS70 +P37370 YLR337C VRP1 +Q03631 YML076C WAR1 +P31412 YKL080W VMA5 +P22203 YOR332W VMA4 +Q04301 YMR088C VBA1 +P25594 YCL069W VBA3 +Q03785 YDR247W VHS1 +P53262 YGR106C VOA1 +P32563 YOR270C VPH1 +P47142 YJR102C VPS25 +P38959 YDR080W VPS41 +P38932 YGL095C VPS45 +Q12071 YDR027C VPS54 +P47111 YJR044C VPS55 +Q12016 YOL129W VPS68 +Q06385 YDR372C VPS74 +Q07655 YDL224C WHI4 +P40080 YER128W VFA1 +P41806 YGR105W VMA21 +P42839 YNL321W VNX1 +P39904 YDR484W VPS52 +Q03913 YDR136C VPS61 +Q03433 YML041C VPS71 +P54787 YML097C VPS9 +Q06263 YLR181C VTA1 +P47165 YJR133W XPT1 +P53076 YGL227W VID30 +P22219 YBR097W VPS15 +P21576 YKR001C VPS1 +Q02767 YPL065W VPS28 +P22543 YLR240W VPS34 +Q06696 YLR417W VPS36 +Q92331 YOR069W VPS5 +Q04338 YMR197C VTI1 +P40151 YNL218W MGS1 +P39102 YLR090W XDJ1 +P38759 YHR012W VPS29 +O13584 YPR087W VPS69 +P40438 YIL173W VTH1 +P40890 YJL222W VTH2 +Q08831 YOR359W VTS1 +P12611 YOR043W WHI2 +P34761 YNL197C WHI3 +P40463 YIL135C VHS2 +Q12045 YPL253C VIK1 +P32341 YKL119C VPH2 +Q07878 YLL040C VPS13 +Q03390 YDR486C VPS60 +P53853 YNL246W VPS75 +Q12215 YOL105C WSC3 +Q03944 YDR200C VPS64 +Q08924 YPL183C RTT10 +P38739 YHL028W WSC4 +P43582 YFL010C WWM1 +P40489 YIL101C XBP1 +Q07993 YLR070C XYL2 +P53241 YGR065C VHT1 +P40547 YIL017C VID28 +P38784 YHR060W VMA22 +P38735 YHL035C VMR1 +P20795 YLR396C VPS33 +P34110 YJL154C VPS35 +P23643 YDR495C VPS3 +P52917 YPR173C VPS4 +Q02725 YPL019C VTC3 +P47075 YJL012C VTC4 +Q12416 YOR083W WHI5 +P38838 YHR134W WSS1 +Q12363 YOR230W WTM1 +P36095 YKL041W VPS24 +P40343 YNR006W VPS27 +P36116 YKR020W VPS51 +P47061 YJL029C VPS53 +O13554 YLR322W VPS65 +Q03388 YDR485C VPS72 +P40046 YER072W VTC1 +P43585 YFL004W VTC2 +P53832 YNL283C WSC2 +P33418 YKL205W LOS1 +Q12206 YOR229W WTM2 +P42826 YGR194C XKS1 +P33301 YDR369C XRS2 +Q02792 YOR048C RAT1 +P30822 YGR218W CRM1 +Q03308 YPL045W VPS16 +P36017 YOR089C VPS21 +Q03897 YDR128W MTC5 +P38189 YBL062W +P38216 YBR016W +P38239 YBR062C +P38243 YBR071W +P32386 YLL048C YBT1 +P38109 YBR139W +Q96VG8 YCR038W-A +P25383 YCL020W TY2A-C +P25349 YCR004C YCP4 +P25617 YCR016W +P25351 YCR023C +P25361 YCR043C +P25639 YCR061W +Q12489 YDL012C 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YPR142C +Q12346 YPR071W +Q12303 YLR121C YPS3 +P0CD97 YER039C-A +P41920 YDR002W YRB1 +Q12172 YOR162C YRR1 +P25036 YOR003W YSP3 +Q12024 YOR272W YTM1 +Q08245 YOL109W ZEO1 +P53061 YGL249W ZIP2 +P53831 YNL285W +P0C5Q8 YNL067W-A +P53717 YNR005C +P53750 YNR064C +P53752 YNR066C +P53981 YNL010W +P53975 YNL019C +P53928 YNL109W +P53910 YNL140C +P53891 YNL165W +P53884 YNL174W +P53876 YNL184C +P53870 YNL193W +P40166 YNL198C +P40152 YNL217W +P53864 YNL226W +Q12351 YOR012W +Q08172 YOL024W +Q3E824 YOR020W-A +Q08222 YOL050C +Q08232 YOL073C +Q6B0V7 YPR002C-A +Q06104 YPR109W +Q12458 YDR368W YPR1 +P32329 YLR120C YPS1 +P01123 YFL038C YPT1 +P40105 YER190W YRF1-2 +P0CX15 YPL283C YRF1-7 +Q12340 YOR172W YRM1 +P47043 YJL056C ZAP1 +P54786 YML109W ZDS2 +P25650 YCR085W +P25657 YCR099C +P25606 YCR100C +Q12210 YDL009C +Q12111 YDR029W +Q12025 YDR056C +Q07435 YDL068W +P38966 YDR089W +Q07530 YDL114W +Q04608 YDR124W +Q03899 YDR131C +A0A023PZA4 YDR154C +Q07613 YDL187C +Q12121 YDL211C +Q07658 YDL228C +Q3E763 YDR246W-A +P87283 YDR274C +Q05530 YDR286C +P87288 YDR327W +P0C289 YDR034C-A +O13523 YDR401W +P87267 YDR417C +Q04093 YDR444W +P87264 YDR467C +Q8TGR7 YDR510C-A +P87263 YER066C-A +A0A023PYE9 YER087C-A +A0A023PXJ7 YER107W-A +A0A023PXD5 YER147C-A +A0A023PZC7 YER152W-A +A0A023PZH1 YER165C-A +P40101 YER186C +P0C0V2 YER188C-A +P0C270 YER138W-A +A0A023PXC2 YEL053W-A +A0A023PXJ3 YER076W-A +P39994 YEL020C +P39983 YEL057C +P39973 YEL074W +P40022 YER034W +P35723 YKL065C YET1 +P39959 YER130C +P10356 YER152C +Q03187 YFL013W-A +Q8TGR2 YFR034W-A +P0CX63 YFL002W-A TY2B-F +P43578 YFL015C +P43566 YFL032W +P43599 YFR018C +Q3E802 YGL006W-A +P0C5N2 YGR122C-A +Q8TGT9 YGR146C-A +P53208 YGR015C +P53210 YGR017W +P53222 YGR035C +P53247 YGR073C +Q12173 YGR109W-A TY3A-G +P53269 YGR115C +P53284 YGR139W +P53293 YGR168C +P53300 YGR182C +P50089 YGR237C +P53325 YGR265W +P53342 YGR293C +P33199 YGL015C +P53183 YGL039W +P53155 YGL082W +P53133 YGL117W +P38616 YNL160W YGP1 +P53103 YGL182C +P53092 YGL199C +P53054 YGL262W +A0A023PYH5 YHR193C-A +P0CX89 YHR212C +P0CL34 YHR219C-A +P0C5N8 YHR180W-A +P38729 YHL042W +P38721 YHL050C +P38776 YHR048W YHK8 +P38829 YHR122W +P40556 YIL006W YIA6 +P40524 YIL054W +P40503 YIL086C +P28625 YMR152W YIM1 +P40449 YIL161W +P40587 YIR043C +P47105 YJR037W +P47107 YJR039W +P47099 YJR028W TY1A-JR2 +P47115 YJR056C +P40355 YJR061W +P47132 YJR087W +P47181 YJR154W +P47066 YJL022W +P47053 YJL043W +P47038 YJL064W +P0CL26 YJL222W-A +P46987 YJL181W +P40896 YJL213W +P47091 YJR018W +Q2V2P3 YKL023C-A +Q12336 YLL059C +Q12259 YLR108C +Q12327 YLR124W +P0C2I8 YLR256W-A TY1A-LR4 +O13561 YLR169W +O13562 YLR171W +Q06247 YLR173W +Q06252 YLR179C +O13530 YLR198C +O13532 YLR217W +P0C5P7 YLR222C-A +Q05947 YLR224W +P0C2J6 YLR424C-B TY2A-LR2 +Q05881 YLR287C +O13543 YLR294C +Q05899 YLR297W +Q06158 YLR311C +Q06170 YLR326W +Q06127 YLR334C +O94086 YLR349W +O13565 YLR358C +Q7LIF1 YLR366W +O13556 YLR462W +P0CL38 YLR466C-A +Q04978 YML053C +Q12204 YOR022C +Q08419 YOR050C +Q08486 YOR072W +Q08994 YPR203W +Q08974 YPL257W +Q08989 YPL277C +P0CX20 YDR545W YRF1-1 +P0CX21 YLR467W YRF1-5 +P42844 YNL310C ZIM17 +Q8TGS0 YOR161C-C +Q08543 YOR170W +Q08604 YOR199W +Q08748 YOR296W +Q12444 YOR309C +Q08816 YOR352W +Q08909 YOR385W +Q8TGJ0 YOR394C-A +Q8TGL4 YOR161W-B +Q8TGL3 YOR186C-A +Q08259 YOL118C +Q12070 YOR024W +Q08900 YOR376W +Q12274 YOR097C +A5Z2X5 YPR010C-A +Q04203 YPR012W +Q12531 YPR015C +Q02606 YPL014W +Q12492 YPR064W +P0C5R6 YPR074W-A +Q02872 YPL108W +Q06107 YPR114W +Q12414 YPL257W-B TY1B-PL +Q08916 YPL142C +P0C5R7 YPR169W-A +Q06595 YPR196W +Q08964 YPL216W +P0CL31 YPL283W-A +Q12010 YOL092W YPQ1 +O13559 YLR466W YRF1-4 +P32793 YHR016C YSC84 +P0C074 YNL138W-A YSF3 +P26725 YJL139C YUR1 +P53735 YNR039C ZRG17 +P20107 YMR243C ZRC1 +P32804 YGL255W ZRT1 +P34240 YKL175W ZRT3 +P0CX14 YGR296W YRF1-3 +Q06681 YDR326C YSP2 +P40341 YMR089C YTA12 +P31383 YAL016W TPD3 +Q08361 YOL165C AAD15 +P43547 YFL056C AAD6 +P15891 YCR088W ABP1 +P39970 YER045C ACA1 +P32316 YBL015W ACH1 +Q01574 YAL054C ACS1 +Q00362 YGL190C CDC55 +P47096 YJR025C BNA1 +P42884 YNL331C AAD14 +P32357 YBL074C AAR2 +P47146 YJR108W ABM1 +Q12031 YPR006C ICL2 +P07248 YDR216W ADR1 +P39925 YER017C AFG3 +P38903 YOR014W RTS1 +P47129 YJR083C ACF4 +P14164 YKL112W ABF1 +P40535 YIL036W CST6 +P31787 YGR037C ACB1 +P53930 YNL107W YAF9 +P32317 YEL052W AFG1 +P32323 YNR044W AGA1 +Q12482 YPR021C AGC1 +Q04412 YDR524C AGE1 +P38090 YBR132C AGP2 +P03876 Q0055 AI2 +Q12471 YOL136C PFK27 +P53319 YGR256W GND2 +P23542 YLR027C AAT2 +Q07622 YDL203C ACK1 +Q03771 YDR161W ACL4 +Q07747 YDL243C AAD4 +P08521 YOR302W +P21192 YLR131C ACE2 +P47182 YJR155W AAD10 +P25612 YCR107W AAD3 +P37898 YHR047C AAP1 +P28240 YER065C ICL1 +P38720 YHR183W GND1 +Q02895 YPL088W AAD16 +Q01802 YKL106W AAT1 +Q08641 YOR239W ABP140 +P47177 YJR149W +P40433 YIL107C PFK26 +P12904 YGL115W SNF4 +Q02486 YMR072W ABF2 +Q00955 YNR016C ACC1 +P40529 YIL044C AGE2 +P52923 YNR074C AIF1 +P23180 YHL021C AIM17 +P38884 YHR198C AIM18 +P40451 YIL158W AIM20 +P32858 YKL037W AIM26 +Q03673 YMR003W AIM34 +Q03798 YMR157C AIM36 +Q12032 YOR215C AIM41 +P38305 YBR194W AIM4 +P46680 YMR092C AIP1 +P52893 YLR089C ALT1 +P47019 YJL122W ALB1 +P40047 YER073W ALD5 +P53178 YGL047W ALG13 +P38179 YBL082C ALG3 +Q06497 YPR128C ANT1 +P38856 YHR161C YAP1801 +Q12028 YPR029C APL4 +P38065 YBL037W APL3 +P53886 YNL172W APC1 +Q12440 YLR127C APC2 +Q12449 YDR214W AHA1 +Q9ZZX0 Q0075 AI5_BETA +P47015 YJL131C AIM23 +P36154 YKR074W AIM29 +Q08223 YOL053W AIM39 +Q07716 YDL237W AIM6 +P47771 YMR170C ALD2 +P54114 YMR169C ALD3 +P46367 YOR374W ALD4 +P38242 YBR070C ALG14 +P40350 YPL227C ALG5 +P40351 YOR067C ALG8 +P43633 YGL021W ALK1 +P32459 YIR032C DAL3 +Q08269 YOL130W ALR1 +P14904 YKL103C APE1 +P47064 YJL024C APS3 +P60010 YFL039C ACT1 +P25371 YCR011C ADP1 +P25613 YCR010C ADY2 +P33304 YDR085C AFR1 +P22149 YGL071W AFT1 +P87275 YER093C-A AIM11 +P53109 YGL160W AIM14 +P47140 YJR100C AIM25 +P39721 YAL049C AIM2 +Q04689 YML050W AIM32 +P53730 YNR030W ALG12 +P43636 YGL065C ALG2 +P32789 YBL009W ALK2 +P43553 YFL050C ALR2 +P47029 YJL084C ALY2 +P50082 YGR225W AMA1 +P38285 YBR158W AMN1 +P40502 YIL087C AIM19 +P40563 YIR003W AIM21 +P40053 YER080W AIM9 +P25335 YIR029W DAL2 +Q00776 YPL259C APM1 +P35181 YLR170C APS1 +P16550 YCL050C APA1 +P38281 YBR151W APD1 +P40532 YIL040W APQ12 +P53909 YNL141W AAH1 +Q2V2Q1 YCL058W-A ADF1 +P00330 YOL086C ADH1 +P00331 YMR303C ADH2 +P10127 YGL256W ADH4 +Q04894 YMR318C ADH6 +P47143 YJR105W ADO1 +Q01976 YBR111C YSA1 +P18239 YBL030C PET9 +P18238 YBR085W AAC3 +Q07732 YDL239C ADY3 +P32493 YMR064W AEP1 +P22136 YMR282C AEP2 +Q08957 YPL202C AFT2 +P43548 YFL055W AGP3 +P25649 YCR082W AHC2 +P29589 YHR093W AHT1 +P38266 YBR108W AIM3 +Q99299 YPL158C AIM44 +P38885 YHR199C AIM46 +P53954 YNL048W ALG11 +Q12001 YOR002W ALG6 +P53868 YNL219C ALG9 +P38313 YBR211C AME1 +P39533 YJL200C ACO2 +P52910 YLR153C ACS2 +P48360 YDR376W ARH1 +P25376 YCL025C AGP1 +P10869 YER052C HOM3 +Q08548 YOR175C ALE1 +P36117 YKR021W ALY1 +P22580 YDR242W AMD2 +P38113 YBR145W ADH5 +P04710 YMR056C AAC1 +P47127 YJR080C AIM24 +Q12013 YOR034C AKR2 +P52892 YDR111C ALT2 +P14540 YKL060C FBA1 +P50076 YGR227W DIE2 +P32375 YIR027C DAL1 +P54783 YML086C ALO1 +P38971 YNL270C ALP1 +Q08981 YPL267W ACM1 +P13711 YGL205W POX1 +P32463 YKL192C ACP1 +Q02336 YDR448W ADA2 +P07246 YMR083W ADH3 +P25377 YCR105W ADH7 +Q12184 YPL252C YAH1 +P38872 YHR185C PFS1 +Q05955 YLR227C ADY4 +Q12089 YPL005W AEP3 +Q99222 YOR129C AFI1 +P32781 YGL032C AGA2 +P38628 YEL058W PCM1 +P43567 YFL030W AGX1 +Q04516 YML087C AIM33 +Q12476 YDL175C AIR2 +P21147 YGL055W OLE1 +P19414 YLR304C ACO1 +Q03233 YMR184W ADD37 +P32794 YLR397C AFG2 +Q12433 YOR023C AHC1 +P38013 YLR109W AHP1 +P03875 Q0050 AI1 +Q12156 YDR063W AIM7 +P40507 YIL079C AIR1 +P39010 YDR264C AKR1 +P38207 YBL019W APN2 +Q12354 YLR118C +Q08702 YOR258W HNT3 +Q04212 YMR041C ARA2 +P38724 YHL047C ARN2 +P38840 YHR137W ARO9 +Q04549 YDR106W ARP10 +P80428 YJL081C ARP4 +P40467 YIL130W ASG1 +P34233 YKL185W ASH1 +Q06834 YPR093C ASR1 +P49435 YML022W APT1 +P07347 YHR013C ARD1 +P18544 YOL140W ARG8 +P53974 YNL020C ARK1 +P38116 YBR164C ARL1 +P38696 YHR129C ARP1 +Q06597 YPR200C ARR2 +P40994 YOR094W ARF3 +Q04728 YMR062C ARG7 +P07249 YMR042W ARG80 +P38731 YHL040C ARN1 +P53090 YGL202W ARO8 +P32449 YBR249C ARO4 +P53946 YNL059C ARP5 +Q12386 YOR141C ARP8 +Q05123 YMR033W ARP9 +P38328 YBR234C ARC40 +P53731 YNR035C ARC35 +P32447 YJL115W ASF1 +P38986 YDR321W ASP1 +P40024 YER036C ARB1 +P11076 YDL192W ARF1 +P00812 YPL111W CAR1 +P08566 YDR127W ARO1 +P15274 YML035C AMD1 +Q08951 YPL195W APL5 +P22108 YDR530C APA2 +Q04601 YDR118W APC4 +Q08683 YOR249C APC5 +Q12107 YLR102C APC9 +P53933 YNL094W APP1 +P47036 YJL075C APQ13 +P36973 YDR441C APT2 +P25628 YCR048W ARE1 +P53111 YGL157W ARI1 +P36090 YKL047W ANR2 +P46682 YGR261C APL6 +Q12157 YDL008W APC11 +Q04413 YDR525W API2 +P04076 YHR018C ARG4 +P08019 YIL099W SGA1 +P32629 YEL036C ANP1 +P38832 YHR126C ANS1 +P38153 YBR288C APM3 +P37302 YBR286W APE3 +P53940 YNL077W APJ1 +P38700 YHL019C APM2 +P22936 YKL114C APN1 +P53943 YNL065W AQR1 +P0CD90 YLL052C AQY2 +Q04371 YMR027W +Q06408 YDR380W ARO10 +Q04052 YDR421W ARO80 +P38080 YBR059C AKL1 +P54115 YPL061W ALD6 +P16661 YBR110W ALG1 +P36000 YKL135C APL2 +P19880 YML007W YAP1 +P27351 YJR005W APL1 +Q99186 YOL062C APM4 +P53068 YGL240W DOC1 +P0CD91 YPR192W AQY1 +P38115 YBR149W ARA1 +P46672 YGL105W ARC1 +P53309 YGR241C YAP1802 +Q00381 YJR058C APS2 +P24813 YDR423C CAD1 +Q8TGM5 YLR154W-E ART3 +Q03862 YDR101C ARX1 +P22768 YOL058W ARG1 +P13586 YGL167C PMR1 +Q12675 YDR093W DNF2 +P40527 YIL048W NEO1 +P16639 YGL017W ATE1 +P38316 YBR217W ATG12 +Q06628 YPR185W ATG13 +Q06671 YLR431C ATG23 +P46989 YJL178C ATG27 +P01097 YDL181W INH1 +P21306 YPL271W ATP15 +P00830 YJR121W ATP2 +P05626 YPL078C ATP4 +Q07879 YLL042C ATG10 +Q07528 YDL113C ATG20 +Q12421 YDR022C ATG31 +Q99325 YOR152C ATG40 +P48016 YPR026W ATH1 +Q12233 YPR020W ATP20 +P38111 YBR136W MEC1 +Q08409 YOR011W AUS1 +Q12500 YLR114C AVL9 +Q05933 YLR370C ARC18 +P0CX79 YLR160C ASP3-4 +P39945 YER101C AST2 +P53296 YGR177C ATF2 +Q12527 YPR049C ATG11 +P38270 YBR128C ATG14 +P25641 YCR068W ATG15 +Q03818 YMR159C ATG16 +Q06410 YLR423C ATG17 +P35193 YOL082W ATG19 +P53104 YGL180W ATG1 +Q06159 YLR312C ATG39 +P53867 YNL223W ATG4 +Q12380 YPL149W ATG5 +P53722 YNR020C ATP23 +Q12092 YPL166W ATG29 +P40458 YIL146C ATG32 +P46983 YJL185C ATG36 +Q12048 YPL250C ATG41 +P38862 YHR171W ATG7 +P38182 YBL078C ATG8 +Q12691 YDR038C ENA5 +P32453 YNL315C ATP11 +P00854 Q0085 ATP6 +Q12165 YDL004W ATP16 +Q06405 YDR377W ATP17 +P31386 YAL020C ATS1 +P38636 YNL259C ATX1 +P40851 YPR122W AXL1 +Q06541 YLR242C ARV1 +Q06822 YPR085C ASA1 +P46993 YJL170C ASG7 +P54074 YMR119W ASI1 +P48361 YGR097W ASK10 +P32660 YER166W DNF1 +Q12674 YMR162C DNF3 +Q03153 YMR098C ATP25 +P30902 YKL016C ATP7 +P00856 Q0080 ATP8 +Q12406 YPR034W ARP7 +P40518 YIL062C ARC15 +Q06598 YPR201W ARR3 +Q8TGM7 YLR154W-A ART2 +P35734 YKL052C ASK1 +P35183 YBL069W AST1 +P40353 YOR377W ATF1 +P53855 YNL242W ATG2 +Q12292 YOL083W ATG34 +Q05789 YLR211C ATG38 +Q01896 YDR039C ENA2 +P22135 YJL180C ATP12 +P38360 YBR295W PCA1 +P32450 YFL010W-A AUA1 +P36107 YKL004W AUR1 +P39981 YEL064C AVT2 +P36062 YKL146W AVT3 +P53629 YNR019W ARE2 +P19146 YDL137W ARF2 +P14843 YDR035W ARO3 +P32448 YDL197C ASF2 +P53895 YNL159C ASI2 +Q04489 YML096W +P49089 YPR145W ASN1 +P49090 YGR124W ASN2 +P43601 YFR021W ATG18 +Q02887 YPL100W ATG21 +P25568 YCL038C ATG22 +Q06485 YLR356W ATG33 +P40344 YNR007C ATG3 +P32907 YNR002C ATO2 +Q12349 YLR295C ATP14 +P32454 YKL157W APE2 +P05085 YML099C ARG81 +P32381 YDL029W ARP2 +P47117 YJR065C ARP3 +Q12509 YLR085C ARP6 +P33204 YKL013C ARC19 +P53244 YGR068C ART5 +P53983 YNL008C ASI3 +P0CZ17 YLR155C ASP3-1 +P38929 YGL006W PMC1 +P39524 YAL026C DRS2 +P39986 YEL031W SPF1 +Q01217 YER069W ARG5,6 +Q02804 YPL051W ARL3 +P28777 YGL148W ARO2 +P18634 YLR392C ART10 +P50275 YOR058C ASE1 +P0CX77 YLR157C ASP3-2 +P0CX78 YLR158C ASP3-3 +P40416 YMR301C ATM1 +P81450 YML081C-A ATP18 +Q06321 YLR189C ATG26 +Q12142 YDL149W ATG9 +P38110 YBL088C TEL1 +P13587 YDR040C ENA1 +Q12359 YDR384C ATO3 +P18496 YLR393W ATP10 +P81451 YOL077W-A ATP19 +P61829 Q0130 OLI1 +P22035 YKR099W BAS1 +Q05029 YMR237W BCH1 +P35817 YLR399C BDF1 +P39714 YAL060W BDH1 +P50273 YDR350C ATP22 +P07251 YBL099W ATP1 +P09457 YDR298C ATP5 +P13090 YML116W ATR1 +Q12067 YOR079C ATX2 +Q12128 YOR134W BAG7 +Q01389 YJL095W BCK1 +P32839 YDR375C BCS1 +P39713 YAL061W BDH2 +Q08347 YOL164W BDS1 +P38077 YBR039W ATP3 +P81449 YDR322C-A TIM11 +Q12226 YLL063C AYT1 +P41815 YDR046C BAP3 +P47068 YJL020C BBC1 +Q08236 YOL078W AVO1 +P47082 YJR001W AVT1 +P38176 YBL089W AVT5 +P50080 YGR224W AZR1 +P38084 YBR068C BAP2 +P39960 YER155C BEM2 +P36149 YKR068C BET3 +P47134 YJR089W BIR1 +P47041 YJL058C BIT61 +Q99177 YPR057W BRR1 +P53062 YGL247W BRR6 +Q08235 YOL077C BRX1 +Q05611 YDR275W BSC2 +Q08280 YOL137W BSC6 +P47176 YJR148W BAT2 +P15703 YGR282C BGL2 +P50277 YNR058W BIO3 +Q08965 YPL217C BMS1 +P47039 YJL060W BNA3 +P40450 YIL159W BNR1 +Q07457 YDL074C BRE1 +Q07660 YDL231C BRE4 +Q12140 YDL037C BSC1 +P53755 YNR069C BSC5 +Q06604 YPR171W BSP1 +P25627 YCR047C BUD23 +P50944 YNL101W AVT4 +P40501 YIL088C AVT7 +P41696 YOR113W AZF1 +Q12365 YPL255W BBP1 +Q3E793 YAL044W-A BOL1 +P38928 YIL140W AXL2 +P36122 YKR027W BCH2 +P33306 YER167W BCK2 +Q07442 YDL070W BDF2 +P53858 YNL233W BNI4 +P53958 YNL042W BOP3 +Q06338 YDR361C BCP1 +P47113 YJR053W BFA1 +P40013 YER016W BIM1 +P38346 YBR270C BIT2 +P35727 YKL061W BLI1 +P40471 YIL124W AYR1 +P29366 YBR200W BEM1 +P39011 YPL161C BEM4 +Q03630 YML077W BET5 +P38813 YHR101C BIG1 +P53744 YNR056C BIO5 +P43583 YFL007W BLM10 +P47040 YJL059W YHC3 +P41695 YGR188C BUB1 +P39988 YEL029C BUD16 +Q04347 YMR014W BUD22 +P85052 YER014C-A BUD25 +P33314 YKL092C BUD2 +P47136 YJR092W BUD4 +P41697 YLR319C BUD6 +P38822 YHR114W BZZ1 +Q04749 YMR068W AVO2 +P40074 YER119C AVT6 +P12630 YIL015W BAR1 +Q12186 YLR116W MSL5 +P38891 YHR208W BAT1 +P38772 YHR040W BCD1 +P32873 YPL115C BEM3 +P22804 YIL004C BET1 +Q06631 YDR299W BFR2 +P11709 YCL029C BIK1 +P32451 YGR286C BIO2 +P40493 YIL096C BMT5 +P39724 YAL046C BOL3 +P26449 YOR026W BUB3 +Q08492 YOR078W BUD21 +Q05949 YLR226W BUR2 +P40580 YIR036C IRC24 +P09440 YBR084W MIS1 +P43569 YFL028C CAF16 +P53615 YNL036W NCE103 +P07252 YJL209W CBP1 +P0C155 YOL153C +P27614 YJL172W CPS1 +P00729 YMR297W PRC1 +P14905 YDR197W CBS2 +P34730 YDR099W BMH2 +P38041 YBL085W BOI1 +P48558 YNL305C BXI1 +P53836 YNL278W CAF120 +P39101 YER048C CAJ1 +P17555 YNL138W SRV2 +P06787 YBR109C CMD1 +P27825 YAL058W CNE1 +P04817 YEL063C CAN1 +P28495 YKL007W CAP1 +P34237 YKL179C COY1 +P15202 YDR256C CTA1 +P53630 YNR057C BIO4 +Q06071 YLR408C BLS1 +Q01532 YNL239W LAP3 +P29311 YER177W BMH1 +P48445 YDL141W BPL1 +P48582 YPL084W BRO1 +P32639 YER172C BRR2 +O13558 YLR465C BSC3 +Q07992 YLR062C BUD28 +Q12064 YDL151C BUD30 +P25558 YCL014W BUD3 +Q12191 YDL099W BUG1 +Q03758 YML111W BUL2 +P12962 YOR276W CAF20 +P03965 YJR109C CPA2 +P38278 YBR141C BMT2 +Q12291 YLR063W BMT6 +P53890 YNL166C BNI5 +P39969 YER114C BOI2 +P43132 YLR015W BRE2 +P53841 YNL269W BSC4 +P38356 YBR290W BSD2 +O94143 YJL188C BUD19 +Q08004 YLR074C BUD20 +Q03783 YDR241W BUD26 +P43573 YFL023W BUD27 +P53323 YGR262C BUD32 +P41698 YLR353W BUD8 +P53226 YGR041W BUD9 +P48524 YMR275C BUL1 +P07245 YGR204W ADE3 +P36076 YKL088W CAB3 +Q03941 YDR196C CAB5 +P13517 YIL034C CAP2 +P07258 YOR303W CPA1 +P38995 YDR270W CCC2 +Q02948 YPL120W VPS30 +P38934 YOR198C BFR1 +Q06333 YDR357C CNL1 +Q04199 YML102W CAC2 +Q06150 YLR267W BOP2 +P53741 YNR051C BRE5 +P43571 YFL025C BST1 +P36130 YKR036C CAF4 +P41832 YNL271C BNI1 +P50084 YGR230W BNS1 +P53838 YNL275W BOR1 +P25385 YLR078C BOS1 +P14772 YLL015W BPT1 +P38770 YHR036W BRL1 +P53194 YGL007W BRP1 +P53286 YGR142W BTN2 +P53727 YNR027W BUD17 +P25337 YCR063W BUD31 +P25300 YCR038C BUD5 +Q08754 YOR299W BUD7 +P23293 YPR161C SGV1 +P36106 YKL005C BYE1 +Q05791 YLR215C CDC123 +P32797 YDL220C CDC13 +P25656 YCR094W CDC50 +P09119 YJL194W CDC6 +P53197 YGL003C CDH1 +P47112 YJR046W TAH11 +Q12453 YOR112W CEX1 +Q06632 YDR301W CFT1 +P13365 YAL040C CLN3 +P53188 YGL029W CGR1 +P07267 YPL154C PEP4 +P39113 YMR280C CAT8 +P35203 YMR094W CTF13 +P32582 YGR155W CYS4 +P21269 YER168C CCA1 +Q06703 YLR308W CDA2 +P27636 YAR019C CDC15 +P40986 YDR182W CDC1 +P04821 YLR310C CDC25 +P25694 YDL126C CDC48 +P06243 YDL017W CDC7 +P53829 YNL288W CAF40 +P43568 YFL029C CAK1 +P53223 YGR036C CAX4 +P40969 YMR168C CEP3 +P53894 YNL161W CBK1 +P03874 YHL038C CBP2 +P11433 YAL041W CDC24 +P38042 YBL084C CDC27 +Q06549 YLR245C CDD1 +P20438 YPL256C CLN2 +P24869 YPR119W CLB2 +P80235 YAR035W YAT1 +P32796 YML042W CAT2 +P25296 YKL190W CNB1 +P07253 YBR120C CBP6 +P36038 YKL208W CBT1 +P37366 YPR025C CCL1 +P37267 YGR174C CBP4 +P48237 YGR150C CCM1 +P31384 YAL021C CCR4 +Q12127 YLR110C CCW12 +P32457 YLR314C CDC3 +Q06697 YLR418C CDC73 +P41733 YLR459W GAB1 +P17106 YJR060W CBF1 +Q03702 YKL011C CCE1 +P38273 YBR131W CCZ1 +Q06702 YLR307W CDA1 +P25342 YCR002C CDC10 +P32468 YHR107C CDC12 +P09798 YKL022C CDC16 +P16522 YHR166C CDC23 +P06704 YOR257W CDC31 +P53082 YGL220W BOL2 +P25356 YCR032W BPH1 +P26448 YMR055C BUB2 +P27637 YAR014C BUD14 +P47158 YJR122W IBA57 +P53934 YNL092W +P06115 YGR088W CTT1 +P32504 YGR140W CBF2 +P33322 YLR175W CBF5 +P14066 YDL069C CBS1 +P50077 YGR217W CCH1 +P00431 YKR066C CCP1 +Q7LHD1 YDR134C CCW22 +P21560 YPL215W CBP3 +P19073 YLR229C CDC42 +P32458 YJR076C CDC11 +P14724 YFR036W CDC26 +P06101 YDR168W CDC37 +Q12018 YDL132W CDC53 +P38910 YOR020C HSP10 +P47818 YLR220W CCC1 +P06182 YAL039C CYC3 +P40202 YMR038C CCS1 +O13547 YLR390W-A CCW14 +Q00684 YFR028C CDC14 +P26309 YGL116W CDC20 +O13297 YPL228W CET1 +P20437 YMR199W CLN1 +P29029 YLR286C CTS1 +P32178 YPR060C ARO7 +Q12114 YLR330W CHS5 +P38843 YHR142W CHS7 +P35190 YGL215W CLG1 +Q03654 YMR213W CEF1 +Q12102 YLR115W CFT2 +P24868 YGR108W CLB1 +P24870 YDL155W CLB3 +P30283 YPR120C CLB5 +P43634 YLR098C CHA4 +P22516 YPL008W CHL1 +Q08032 YLR103C CDC45 +P07834 YFL009W CDC4 +P32562 YMR001C CDC5 +P36012 YKL049C CSE4 +Q03705 YML036W CGI121 +P24871 YLR210W CLB4 +P38221 YBR029C CDS1 +P39525 YER061C CEM1 +P40558 YIL003W CFD1 +P32656 YER163C GCG1 +Q05583 YDR267C CIA1 +P53280 YGR134W CAF130 +P32943 YGR109C CLB6 +P08004 YNL192W CHS1 +P14180 YBR038W CHS2 +P38147 YBR274W CHK1 +P38907 YDR254W CHL4 +P40955 YJL099W CHS6 +P20486 YBR135W CKS1 +P53264 YGR110W CLD1 +P38323 YBR227C MCX1 +P33313 YBR155W CNS1 +Q3E823 YPL189C-A COA2 +Q3E7B2 YJL062W-A COA3 +Q3E846 YMR244C-A COA6 +Q12309 YLR117C CLF1 +Q08685 YOR250C CLP1 +P32657 YER164W CHD1 +Q06350 YDR371W CTS2 +P05374 YGR157W CHO2 +P29465 YBR023C CHS3 +P40019 YER030W CHZ1 +P43635 YPR001W CIT3 +Q07897 YLR003C CMS1 +Q01649 YMR198W CIK1 +P40987 YOR349W CIN1 +P27895 YEL061C CIN8 +P48562 YNL298W CLA4 +P22137 YGL206C CHC1 +D6W196 YNL083W SAL1 +Q08058 YOL008W COQ10 +P53318 YGR255C COQ6 +Q05779 YLR201C COQ9 +Q06156 YLR272C YCS4 +P53079 YGL223C COG1 +P38779 YHR052W CIC1 +P00890 YNR001C CIT1 +Q3E7A9 YMR194C-B CMC4 +Q12510 YDL156W CMR1 +Q06680 YDR325W YCG1 +P39110 YMR138W CIN4 +P47001 YJL158C CIS3 +Q03690 YMR012W CLU1 +P53865 YNL225C CNM67 +P41810 YDR238C SEC26 +P40509 YIL076W SEC28 +O13525 YDR204W COQ4 +P41735 YOR125C CAT5 +Q01519 YLR038C COX12 +Q03048 YLL050C COF1 +P53622 YDL145C COP1 +P00401 Q0045 COX1 +P32344 YLR204W QRI5 +P38287 YBR161W CSH1 +P43639 YGL019W CKB1 +P46946 YGL175C SAE2 +P32074 YNL287W SEC21 +Q05892 YLR290C COQ11 +P18900 YBR003W COQ1 +P27697 YGL119W COQ8 +P52924 YNR075W COS10 +P43542 YFL062W COS4 +P53344 YGR295C COS6 +P32798 YOR316C COT1 +P47081 YJL003W COX16 +Q12287 YLL009C COX17 +P04037 YGL187C COX4 +P00424 YNL052W COX5A +P00425 YIL111W COX5B +P04039 YLR395C COX8 +P10614 YHR007C ERG11 +P17898 YNL130C CPT1 +P08679 YCR005C CIT2 +P17891 YGR167W CLC1 +P53332 YGR277C CAB4 +P43618 YFR046C CNN1 +P40452 YIL157C COA1 +Q05809 YLR218C COA4 +P53600 YPL010W RET3 +P53239 YGR062C COX18 +Q3E731 YLL018C-A COX19 +P00410 Q0250 COX2 +P00420 Q0275 COX3 +P41811 YGL137W SEC27 +P27680 YOL096C COQ3 +P49017 YML110C COQ5 +P53053 YGL263W COS12 +P0CX13 YML132W COS3 +Q07788 YDL248W COS7 +P39103 YML129C COX14 +P38170 YBL097W BRN1 +Q06096 YPR105C COG4 +P53195 YGL005C COG7 +Q04935 YDR231C COX20 +Q3E7A4 YBL059C-A CMC2 +P53951 YNL051W COG5 +P43621 YFR051C RET2 +P32378 YNR041C COQ2 +P00427 YHR051W COX6 +P21595 YDR402C DIT2 +P38930 YOR039W CKB2 +P40465 YIL132C CSM2 +Q06705 YLR380W CSR1 +P47976 YDR151C CTH1 +Q03957 YKL139W CTK1 +P38428 YMR264W CUE1 +P40094 YER157W COG3 +P53959 YNL041C COG6 +Q06440 YLR429W CRN1 +P53822 YNL336W COS1 +P47187 YJR161C COS5 +P38723 YHL048W COS8 +P21592 YPL172C COX10 +P40086 YER141W COX15 +P10174 YMR256C COX7 +Q12150 YLR087C CSF1 +P15790 YIL035C CKA1 +P19454 YOR061W CKA2 +Q12748 YLR381W CTF3 +P47977 YLR136C TIS11 +Q08923 YPL181W CTI6 +Q12734 YPR030W CSR2 +Q06032 YLR394W CST9 +Q02732 YPL018W CTF19 +P46962 YJL006C CTK2 +Q03220 YMR180C CTL1 +P38818 YHR109W CTM1 +P41817 YPL177C CUP9 +P53333 YGR278W CWC22 +P25603 YCL007C CWH36 +P25618 YCR017C CWH43 +P53271 YGR120C COG2 +Q04632 YML071C COG8 +P07255 YDL067C COX9 +P36064 YKL137W CMC1 +P38845 YHR146W CRP1 +P41902 YOR031W CRS5 +P33307 YGL238W CSE1 +P43497 YKL096W-A CWP2 +P0CX12 YBR302C COS2 +P36034 YKL219W COS9 +P19516 YPL132W COX11 +P32799 YGL191W COX13 +P38824 YHR116W COX23 +P53314 YGR247W CPD1 +Q12289 YOR100C CRC1 +P38892 YHR209W CRG1 +P53968 YNL027W CRZ1 +Q08054 YOL007C CSI2 +Q12348 YOL117W RRI2 +P14306 YLR178C TFS1 +P53301 YGR189C CRH1 +Q06538 YLR241W CSC1 +P35206 YBR036C CSG2 +P25651 YCR086W CSM1 +Q08955 YPL200W CSM4 +P47130 YJR084W CSN12 +Q12468 YDL216C RRI1 +P25355 YCR054C CTR86 +P53923 YNL119W NCS2 +P53830 YNL286W CUS2 +P00044 YJR048W CYC1 +P32898 YDR430C CYM1 +P32623 YEL040W UTR2 +Q05790 YLR213C CRR1 +P38308 YBR203W COS111 +Q04368 YMR025W CSI1 +P49573 YPR124W CTR1 +P38865 YHR175W CTR2 +P89105 YOL145C CTR9 +Q04201 YML101C CUE4 +Q08412 YOR042W CUE5 +P47050 YJL047C RTT101 +P28320 YKL095W YJU2 +P53854 YNL245C CWC25 +Q12046 YDL209C CWC2 +P53008 YGL027C CWH41 +P28319 YKL096W CWP1 +Q07560 YDL142C CRD1 +Q08226 YOL063C CRT10 +P53859 YNL232W CSL4 +Q03981 YDR179C CSN9 +P38226 YBR042C CST26 +P36075 YKL090W CUE2 +Q06469 YPR158W CUR1 +P21657 YIR023W DAL81 +P47179 YJR151C DAN4 +P22204 YGR092W DBF2 +P36120 YKR024C DBP7 +P24309 YKL149C DBR1 +P32347 YDR047W HEM12 +P36091 YKL046C DCW1 +Q99321 YOR163W DDP1 +P53899 YNL155W CUZ1 +P08678 YJL005W CYR1 +P00163 Q0105 COB +P53206 YGR012W +Q00873 YKL087C CYT2 +P43550 YFL053W DAK2 +P47178 YJR150C DAN1 +P18962 YHR028C DAP2 +P47005 YJL149W DAS1 +Q12084 YDR020C DAS2 +Q12517 YOL149W DCP1 +Q12123 YOR173W DCS2 +P06773 YHR144C DCD1 +P38877 YHR191C CTF8 +P46963 YML112W CTK3 +Q06686 YLR411W CTR3 +P53088 YGL211W NCS6 +P53137 YGL110C CUE3 +P15315 YGL166W CUP2 +Q03772 YDR163W CWC15 +P46947 YGL174W BUD13 +Q02770 YPL064C CWC27 +P07143 YOR065W CYT1 +P38909 YOR037W CYC2 +P15365 YJR152W DAL5 +P26343 YKR034W DAL80 +Q12091 YPL170W DAP1 +P24784 YPL119C DBP1 +Q06218 YLR276C DBP9 +Q04895 YIR028W DAL4 +Q12389 YDL031W DBP10 +P24783 YNL112W DBP2 +P20447 YGL078C DBP3 +P20449 YOR046C DBP5 +P53734 YNR038W DBP6 +P21182 YOL052C SPE2 +P25559 YCL016C DCC1 +P08432 YKL184W SPE1 +Q05924 YLR361C DCR2 +P06634 YOR204W DED1 +P38307 YBR201W DER1 +Q04930 YDR223W CRF1 +Q04659 YMR048W CSM3 +P40512 YIL071C PCI8 +P49956 YMR078C CTF18 +Q01454 YPR135W CTF4 +Q03375 YDR482C CWC21 +P53769 YLR323C CWC24 +P00045 YEL039C CYC7 +P47103 YJR032W CPR7 +P35176 YDR304C CPR5 +P14832 YDR155C CPR1 +P31373 YAL012W CYS3 +Q12248 YDR016C DAD1 +P69850 YBR233W-A DAD3 +P25334 YCR069W CPR4 +P06106 YLR303W MET17 +P38719 YHR169W DBP8 +P32460 YIR030C DCG1 +P0CH63 YFL061W DDI2 +Q99288 YDR051C DET1 +Q05080 YMR032W HOF1 +P53728 YNR028W CPR8 +P23285 YHR057C CPR2 +P25719 YML078W CPR3 +P21705 YNL314W DAL82 +P20448 YJL033W HCA4 +Q08558 YOR180C DCI1 +P40087 YER143W DDI1 +P69851 YDR320C-A DAD4 +P32328 YPR111W DBF20 +P33750 YLL011W SOF1 +P53550 YNL118C DCP2 +P18899 YMR173W DDR48 +P31385 YAL013W DEP1 +P36108 YKL002W DID4 +P52868 YGL128C CWC23 +P40312 YNL111C CYB5 +P14922 YBR112C CYC8 +Q07533 YDL117W CYK3 +P36162 YKR083C DAD2 +P53267 YGR113W DAM1 +P13483 YML113W DAT1 +P53202 YGR003W CUL3 +Q02554 YMR240C CUS1 +P00175 YML054C CYB2 +P54838 YML070W DAK1 +Q12382 YOR311C DGK1 +Q3E808 YNL130C-A DGR1 +P21623 YDR403W DIT1 +P54861 YLL001W DNM1 +P40059 YER088C DOT6 +P47027 YJL090C DPB11 +P32469 YLR172C DPH5 +P38332 YBR246W RRT2 +P32892 YLL008W DRS1 +P23501 YKR053C YSR3 +P53720 YNR015W SMM1 +P07262 YOR375C GDH1 +P37298 YDR178W SDH4 +Q08496 YOR080W DIA2 +Q12086 YDR263C DIN7 +P04819 YDL164C CDC9 +Q08387 YOR005C DNL4 +P38821 YHR113W APE4 +P38774 YHR044C DOG1 +Q03921 YDR141C DOP1 +P46957 YJR006W POL31 +P15801 YOR330C MIP1 +P36152 YKR071C DRE2 +Q04792 YMR250W GAD1 +P35732 YKL054C DEF1 +Q99234 YOR030W DFG16 +P32330 YKL121W DGR2 +P39708 YAL062W GDH3 +Q04603 YDR121W DPB4 +Q3E840 YBL071W-A KTI11 +P39517 YDL160C DHH1 +Q04217 YMR128W ECM16 +P35497 YJR159W SOR1 +O13577 YLR437C DIF1 +P40318 YIL030C SSM4 +P47110 YJR043C POL32 +P14284 YPL167C REV3 +P53255 YGR093W DRN1 +P32325 YDR052C DBF4 +P47089 YJR014W TMA22 +Q12743 YDR411C DFM1 +Q07786 YDL246C SOR2 +P38791 YHR068W DYS1 +Q03373 YDR480W DIG2 +P40366 YJL065C DLS1 +Q06819 YPR082C DIB1 +P40564 YIR004W DJP1 +P39976 YEL071W DLD3 +Q04216 YMR126C DLT1 +Q03652 YMR211W DML1 +P31116 YJR139C HOM6 +Q06143 YLR348C DIC1 +P36037 YKL213C DOA1 +P33309 YNL001W DOM34 +Q12395 YLR128W DCN1 +Q06151 YLR270W DCS1 +P0CH64 YNL335W DDI3 +P89113 YOL052C-A DDR2 +P54005 YMR316W DIA1 +P69771 YKR035W-A DID2 +P32891 YDL174C DLD1 +P09624 YFL018C LPD1 +Q07505 YDL086W +P38823 YHR115C DMA1 +P25453 YER179W DMC1 +P43595 YFR012W DCV1 +Q08949 YPL194W DDC1 +P40526 YIL049W DFG10 +Q05031 YMR238W DFG5 +Q08650 YOR245C DGA1 +P13663 YDR158W HOM2 +P33327 YDL215C GDH2 +P36009 YKL078W DHR2 +Q03063 YPL049C DIG1 +P41819 YPL266W DIM1 +P53388 YPL265W DIP5 +P46681 YDL178W DLD2 +P53924 YNL116W DMA2 +P38859 YHR164C DNA2 +P53871 YNL191W DUG3 +Q04110 YDR446W ECM11 +Q06011 YLR390W ECM19 +Q03214 YMR176W ECM5 +P33412 YGR007W ECT1 +P40023 YER035W EDC2 +P02994 YPR080W; YBR118W TEF1; TEF2 +P25039 YLR069C MEF1 +P38347 YBR271W EFM2 +P40516 YIL064W EFM4 +P53970 YNL024C EFM6 +Q03653 YMR212C EFR3 +P09032 YOR260W GCD1 +Q05610 YDR273W DON1 +P32461 YKL191W DPH2 +P38121 YBL035C POL12 +P13382 YNL102W POL1 +Q05521 YDR284C DPP1 +Q08729 YOR264W DSE3 +P48510 YMR276W DSK2 +P40568 YIR010W DSN1 +P33413 YHL016C DUR3 +Q06063 YLR405W DUS4 +P47128 YJR082C EAF6 +P36049 YKL172W EBP2 +P48235 YGR146C ECL1 +Q04623 YDR125C ECM18 +P32525 YJL201W ECM25 +Q99252 YOR092W ECM3 +Q3E705 YGR271C-A EFG1 +P53168 YGL061C DUO1 +Q06053 YLR401C DUS3 +P36041 YKL204W EAP1 +P38195 YBL043W ECM13 +P35195 YBL001C ECM15 +P47144 YJR106W ECM27 +Q02202 YKR004C ECM9 +P38073 YBR033W EDS1 +P42835 YNL327W EGT2 +P47120 YJR070C LIA1 +P27344 YBR278W DPB3 +P40487 YIL103W DPH1 +Q12429 YLR143W DPH6 +Q08225 YOL057W +P47013 YJL134W LCB3 +P38844 YHR143W DSE2 +P39112 YMR287C DSS1 +P38125 YBR180W DTR1 +P43616 YFR044C DUG1 +P32528 YBR208C DUR1,2 +P33317 YBR252W DUT1 +P36022 YKR054C DYN1 +P53759 YML080W DUS1 +Q06349 YDR370C DXO1 +P53063 YGL246C RAI1 +Q06337 YDR359C EAF1 +P39995 YEL018W EAF5 +P53911 YNL136W EAF7 +Q03212 YMR171C EAR1 +Q05871 YLR284C ECI1 +P38167 YBL101C ECM21 +P38737 YHL030W ECM29 +P38246 YBR076W ECM8 +P38732 YHL039W EFM1 +P53235 YGR054W +P32497 YMR309C NIP1 +Q12050 YOR144C ELG1 +P25574 YCL045C EMC1 +P47133 YJR088C EMC2 +P53095 YGL196W DSD1 +P40077 YER124C DSE1 +P0CX08 YEL070W DSF1 +Q04949 YMR299C DYN3 +Q12432 YPR023C EAF3 +Q03466 YDR206W EBS1 +P32471 YAL003W EFB1 +P29547 YPL048W CAM1 +P32324 YOR133W; YDR385W EFT1; EFT2 +P47163 YJR129C EFM3 +P53200 YGR001C EFM5 +Q05874 YLR285W NNT1 +P54858 YDR068W DOS2 +P40553 YIL010W DOT5 +P24482 YPR175W DPB2 +P25615 YCR014C POL4 +P39985 YEL055C POL5 +P21951 YNL262W POL2 +P38213 YBR007C DSF2 +P53847 YNL258C DSL1 +Q02647 YDR424C DYN2 +P07807 YOR236W DFR1 +Q06673 YLR436C ECM30 +P38728 YHL043W ECM34 +Q05902 YLR299W ECM38 +P38773 YHR043C DOG2 +Q04089 YDR440W DOT1 +P47138 YJR097W JJJ3 +P14020 YPR183W DPM1 +P15436 YDL102W POL3 +P32601 YPR017C DSS4 +Q07648 YDL219W DTD1 +P38149 YBR281C DUG2 +P39009 YDL101C DUN1 +Q04067 YDR429C TIF35 +Q03764 YDR147W EKI1 +Q02884 YPL101W ELP4 +Q04409 YDR516C EMI2 +P38333 YBR247C ENP1 +P43572 YFL024C EPL1 +P41912 YOL110W SHR5 +P32352 YMR202W ERG2 +P54781 YMR015C ERG5 +P62651 YPL096C-A ERI1 +P43613 YFR041C ERJ5 +P53080 YGL222C EDC1 +P39998 YEL015W EDC3 +P14741 YKR026C GCN3 +P32501 YDR211W GCD6 +Q05775 YLR192C HCR1 +P36053 YKL160W ELF1 +P25358 YCR034W ELO2 +P39013 YNL084C END3 +P32626 YEL038W UTR4 +Q05785 YLR206W ENT2 +P53246 YGR071C ENV11 +Q12003 YPL236C ENV7 +O13529 YHR021W-A ECM12 +P39715 YAL059W ECM1 +Q02710 YPL021W ECM23 +P34216 YBL047C EDE1 +P36008 YKL081W TEF4 +P53978 YNL014W HEF3 +P12754 YGR083C GCD2 +P32801 YKL048C ELM1 +P42935 YGR200C ELP2 +P40540 YIL027C EMC5 +Q12431 YLL014W EMC6 +P42842 YNL313C EMW1 +P18414 YBL040C ERD2 +Q06551 YLR246W ERF2 +P32476 YGR175C ERG1 +P53199 YGL001C ERG26 +P0CX10 YOR393W ERR1 +P53337 YGR284C ERV29 +Q12168 YLR144C ACF2 +Q99382 YLR065C ENV10 +P22140 YHR123W EPT1 +P38819 YHR110W ERP5 +P38312 YBR210W ERV15 +Q08649 YOR244W ESA1 +Q06340 YDR363W ESC2 +Q06344 YDR365C ESF1 +P22696 YJR017C ESS1 +P32474 YDR518W EUG1 +P02992 YOR187W TUF1 +Q06706 YLR384C IKI3 +Q02908 YPL086C ELP3 +P00925 YHR174W ENO2 +Q12518 YDL161W ENT1 +P47160 YJR125C ENT3 +Q03769 YDR153C ENT5 +Q08651 YOR246C ENV9 +P25340 YGL012W ERG4 +P25087 YML008C ERG6 +P24521 YMR220W ERG8 +Q12450 YOR016C ERP4 +P40456 YIL151C ESL1 +Q03018 YGR098C ESP1 +Q07872 YLL038C ENT4 +P40557 YIL005W EPS1 +P38767 YHR032W ERC1 +P32462 YNL280C ERG24 +P38604 YHR072W ERG7 +P53198 YGL002W ERP6 +P0CX11 YPL281C ERR2 +Q04651 YML067C ERV41 +P36168 YKR096W ESL2 +Q03096 YIL009C-A EST3 +P38836 YHR132C ECM14 +Q05958 YLR228C ECM22 +P32644 YER176W ECM32 +P38248 YBR078W ECM33 +Q06200 YLR443W ECM7 +P43605 YFR027W ECO1 +P38249 YBR079C RPG1 +P40217 YMR146C TIF34 +Q05050 YMR031C EIS1 +P40319 YLR372W ELO3 +P53861 YNL230C ELA1 +P43555 YFL048C EMP47 +P53753 YNR067C DSE4 +P06103 YOR361C PRT1 +P39540 YJL196C ELO1 +P38874 YHR187W IKI1 +P53073 YGL231C EMC4 +Q12396 YLR080W EMP46 +P00924 YGR254W ENO1 +P32353 YLR056W ERG3 +Q12403 YDL018C ERP3 +Q12284 YPR037C ERV2 +Q12480 YPR004C AIM45 +Q03071 YPL046C ELC1 +Q04868 YMR312W ELP6 +P36039 YKL207W EMC3 +Q04406 YDR512C EMI1 +P32803 YGL200C EMP24 +Q08299 YOL158C ENB1 +P53938 YNL080C EOS1 +P16151 YDR414C ERD1 +Q12452 YLR100W ERG27 +Q05359 YAR002C-A ERP1 +P38748 YHL010C ETP1 +P38071 YBR026C ETR1 +P23776 YLR300W EXG1 +P52911 YDR261C EXG2 +Q04660 YMR049C ERB1 +P05453 YDR172W SUP35 +P42222 YMR323W ERR3 +P38140 YBR239C ERT1 +P27882 YGR029W ERV1 +P39727 YAL042W ERV46 +P19097 YPL231W FAS2 +Q12283 YOR221C MCT1 +P53917 YNL127W FAR11 +P21268 YJL157C FAR1 +P43592 YFR008W FAR7 +P15646 YDL014W NOP1 +Q03034 YDR539W FDC1 +P29704 YHR190W ERG9 +P26793 YKL113C RAD27 +P40988 YMR319C FET4 +P53918 YNL125C ESBP6 +Q08119 YOL017W ESC8 +P17214 YLR233C EST1 +Q08822 YOR356W CIR2 +P35731 YKL055C OAR1 +P38913 YDL045C FAD1 +P38224 YBR040W FIG1 +P40020 YER032W FIR1 +Q08906 YOR382W FIT2 +P12385 YBR143C SUP45 +P40030 YER044C ERG28 +Q03103 YML130C ERO1 +P39704 YAL007C ERP2 +P17261 YCR075C ERS1 +P53173 YGL054C ERV14 +Q03661 YMR219W ESC1 +P53743 YNR054C ESF2 +P42940 YGR207C CIR1 +Q08421 YOR051C ETT1 +P39875 YOR033C EXO1 +P38289 YBR163W EXO5 +P38261 YBR102C EXO84 +P09201 YLR377C FBP1 +P34756 YFR019W FAB1 +P32771 YDL168W SFA1 +P32604 YJL155C FBP26 +Q12099 YDR021W FAL1 +Q04952 YMR306W FKS3 +P36170 YKR102W FLO10 +P08640 YIR019C FLO11 +P32768 YAR050W FLO1 +Q08023 YLR077W FMP25 +P43557 YFL046W FMP32 +P53233 YGR052W FMP48 +P50264 YMR020W FMS1 +P40546 YIL019W FAF1 +P46671 YMR052W FAR3 +Q05040 YMR029C FAR8 +P38137 YBR222C PCS60 +Q12178 YPR062W FCY1 +P25621 YCR028C FEN2 +Q08907 YOR383C FIT3 +P19658 YJL085W EXO70 +P53971 YNL023C FAP1 +Q05498 YDR339C FCF1 +Q03254 YMR277W FCP1 +Q12119 YER060W-A FCY22 +Q06001 YLR238W FAR10 +P17064 YER056C FCY2 +P0CF35 YPL275W FDH2 +P39676 YGR234W YHB1 +P07149 YKL182W FAS1 +P40039 YER060W FCY21 +Q08991 YPL279C FEX2 +P25653 YCR089W FIG2 +P42837 YNL325C FIG4 +P38911 YML074C FPR3 +P20081 YNL135C FPR1 +P38631 YLR342W FKS1 +P40068 YER109C FLO8 +P53279 YGR131W FHN1 +Q08645 YOR241W MET7 +P08524 YJL167W ERG20 +Q07825 YLL029W FRA1 +P32791 YLR214W FRE1 +P53746 YNR060W FRE4 +P08417 YPL262W FUM1 +P28003 YAL034C FUN19 +P11412 YNL241C ZWF1 +P04385 YBR020W GAL1 +P04386 YPL248C GAL4 +Q04739 YER027C GAL83 +P39719 YAL053W FLC2 +P32785 YBL013W FMT1 +Q02207 YKR009C FOX2 +P36033 YKL220C FRE2 +Q12473 YLL051C FRE6 +Q12333 YOL152W FRE7 +P12709 YBR196C PGI1 +P17649 YGR019W UGA1 +P38225 YBR041W FAT1 +P38993 YMR058W FET3 +Q08913 YOR390W FEX1 +P39521 YPR104C FHL1 +P32472 YDR519W FPR2 +P53121 YGL139W FLC3 +P40491 YIL098C FMC1 +Q12497 YDR070C FMP16 +P40008 YER004W FMP52 +P22007 YDL090C RAM1 +O13329 YDR110W FOB1 +Q08911 YOR388C FDH1 +P40466 YIL131C FKH1 +Q08967 YPL221W FLC1 +P53739 YNR047W FPK1 +P23900 YLL043W FPS1 +Q05015 YMR222C FSH2 +Q99369 YOR280C FSH3 +P38310 YBR207W FTH1 +Q12247 YLR068W FYV7 +P32805 YGL254W FZF1 +P00358 YJR009C TDH2 +P00359 YGR192C TDH3 +P40569 YIR013C GAT4 +P38260 YBR101C FES1 +P43561 YFL041W FET5 +P41813 YNL068C FKH2 +P40989 YGR032W GSC2 +Q12676 YMR113W FOL3 +Q08905 YOR381W FRE3 +Q08908 YOR384W FRE5 +Q12209 YLR047C FRE8 +Q03002 YPL141C FRK1 +P37261 YCL026C-A FRM2 +P32599 YDR129C SAC6 +Q03898 YDR130C FIN1 +Q04433 YDR534C FIT1 +P39712 YAL063C FLO9 +P03870 R0010W FLP1 +P38124 YBR008C FLR1 +Q06179 YLR454W FMP27 +P46998 YJL161W FMP33 +P53889 YNL168C FMP41 +Q07651 YDL222C FMP45 +P31380 YAL019W FUN30 +Q12035 YLR051C FCF2 +Q06205 YLR449W FPR4 +P38866 YHR176W FMO1 +Q08968 YPL222W FMP40 +Q04991 YMR221C FMP42 +P29703 YKL019W RAM2 +P53848 YNL256W FOL1 +P38894 YHR211W FLO5 +P40464 YIL134W FLX1 +P38231 YBR047W FMP23 +Q02883 YPL103C FMP30 +A0A023PZB3 YER038W-A FMP49 +Q12029 YOR271C FSF1 +P25659 YCR076C FUB1 +P16892 YBL016W FUS3 +P38783 YHR059W FYV4 +P53913 YNL133C FYV6 +P45976 YJR093C FIP1 +P40515 YIL065C FIS1 +P40098 YER182W FMP10 +P36141 YKR049C FMP46 +P36001 YKL132C RMA1 +P40099 YER183C FAU1 +P04397 YBR019C GAL10 +P13181 YLR081W GAL2 +P13045 YDR009W GAL3 +P43574 YFL021W GAT1 +P39012 YLR088W GAA1 +P28006 YOR178C GAC1 +P41913 YOR355W GDS1 +Q08622 YOR205C GEP3 +P40056 YER083C GET2 +P14742 YKL104C GFA1 +P40036 YER054C GIP2 +P39732 YAL031C GIP4 +P53849 YNL255C GIS2 +P25346 YCR098C GIT1 +Q12315 YDL207W GLE1 +P36143 YKR058W GLG1 +P38777 YHR049W FSH1 +P05316 YBR021W FUR4 +Q05670 YMR232W FUS2 +Q08559 YOR183W FYV12 +P25585 YCL058C FYV5 +P46949 YGR196C FYV8 +P00360 YJL052W TDH1 +P08431 YBR018C GAL7 +P04387 YML051W GAL80 +P25555 YCL011C GBP2 +P51601 YGR267C FOL2 +Q07928 YLR013W GAT3 +P33893 YBL080C PET112 +P43535 YFR009W GCN20 +P53171 YGL057C GEP7 +P53192 YGL020C GET1 +Q12154 YDL100C GET3 +Q04839 YMR255W GFD1 +P22146 YMR307W GAS1 +Q06135 YLR343W GAS2 +P18851 YOR212W STE4 +P39993 YEL022W GEA2 +P25370 YCL036W GFD2 +Q12051 YPL069C BTS1 +Q06648 YDR309C GIC2 +Q03833 YDR096W GIS1 +P38196 YBL042C FUI1 +P11710 YCL027W FUS1 +P40492 YIL097W FYV10 +Q99341 YDR024W FYV1 +P38297 YBR179C FZO1 +P53260 YGR102C GTF1 +P18852 YJR086W STE18 +P38301 YBR187W GDT1 +P47102 YJR031C GEA1 +P38988 YDL198C GGC1 +Q04233 YML006C GIS4 +Q07540 YDL120W YFH1 +P32614 YEL047C FRD1 +P36088 YKL069W +P40088 YER145C FTR1 +P18411 YAL008W FUN14 +P31381 YAL022C FUN26 +P19145 YKR039W GAP1 +P28007 YHR089C GAR1 +Q03655 YMR215W GAS3 +P40209 YMR136W GAT2 +P39726 YAL044C GCV3 +Q08271 YOL132W GAS4 +Q08193 YOL030W GAS5 +Q03557 YMR293C HER2 +P38011 YMR116C ASC1 +P07261 YPL075W GCR1 +P14065 YOR120W GCY1 +P32775 YEL011W GLC3 +P17695 YDR513W GRX2 +P37303 YEL046C GLY1 +P32191 YIL155C GUT2 +P38875 YHR188C GPI16 +P46961 YPL076W GPI2 +P40106 YER062C GPP2 +P35197 YDL226C GCS1 +Q12393 YLR091W GEP5 +P25596 YCL073C GEX1 +Q03016 YPL137C GIP3 +Q05926 YLR364W GRX8 +P03069 YEL009C GCN4 +Q03330 YGR252W GCN5 +Q01722 YNL199C GCR2 +P32621 YEL042W GDA1 +Q02979 YPL110C GDE1 +Q99339 YLL065W +P38229 YBR045C GIP1 +Q03768 YDR152W GIR2 +P38068 YBR014C GRX7 +P37291 YLR058C SHM2 +P40107 YGL225W VRG4 +P0CE11 YER039C HVG1 +P43577 YFL017C GNA1 +Q03554 YMR292W GOT1 +P10823 YER020W GPA2 +Q08886 YOR371C GPB1 +P40066 YER107C GLE2 +Q05584 YDR272W GLO2 +P38682 YER122C GLO3 +P32190 YHL032C GUT1 +Q12438 YDL010W GRX6 +P48813 YDR508C GNP1 +P53839 YNL274C GOR1 +Q00055 YDL022W GPD1 +Q06636 YDR302W GPI11 +P47088 YJR013W GPI14 +Q04082 YDR437W GPI19 +P32363 YPL175W SPT14 +Q08726 YOR262W GPN2 +P40581 YIR037W HYR1 +P33892 YGL195W GCN1 +P49095 YMR189W GCV2 +P37020 YJR040W GEF1 +P38812 YHR100C GEP4 +Q12125 YOR164C GET4 +P36173 YKR106W GEX2 +Q06336 YDR358W GGA1 +P38817 YHR108W GGA2 +P25569 YCL039W GID7 +P32642 YER174C GRX4 +P38138 YBR229C ROT2 +Q04924 YDR221W GTB1 +P48015 YDR019C GCV1 +Q06625 YPR184W GDB1 +P39958 YER136W GDI1 +Q12434 YDL135C RDI1 +P39722 YAL048C GEM1 +P38785 YHR061C GIC1 +Q12418 YLR094C GIS3 +P41818 YMR311C GLC8 +P47011 YJL137C GLG2 +P38263 YBR105C VID24 +P40208 YMR135C GID8 +Q12263 YDR507C GIN4 +P32288 YPR035W GLN1 +Q12320 YOR040W GLO4 +P25373 YCL035C GRX1 +Q12680 YDL171C GLT1 +P37292 YBR263W SHM1 +Q03786 YDR248C +P30777 YGL142C GPI10 +Q07830 YLL031C GPI13 +P53306 YGR216C GPI1 +Q06543 YLR243W GPN3 +P41277 YIL053W GPP1 +P18494 YER040W GLN3 +Q03835 YDR098C GRX3 +Q02784 YPL059W GRX5 +P32784 YBL011W SCT1 +P07286 YBR243C ALG7 +P36148 YKR067W GPT2 +Q04410 YDR517W GRH1 +Q08929 YPL189W GUP2 +Q04322 YMR192W GYL1 +P48365 YDL234C GYP7 +P23337 YFR015C GSY1 +P04911 YDR225W HTA1 +P02294 YBL002W HTB2 +P40857 YJL097W PHS1 +P25333 YCR008W SAT4 +Q04399 YDR506C GMC1 +P38736 YHL031C GOS1 +P39717 YAL056W GPB2 +Q08969 YPL223C GRE1 +P38715 YHR104W GRE3 +P53154 YGL084C GUP1 +P40531 YIL041W GVP36 +Q08484 YOR070C GYP1 +P48566 YNL293W MSB3 +Q12753 YPR008W HAA1 +P41546 YFL031W HAC1 +P42950 YJL103C GSM1 +P32835 YLR293C GSP1 +Q07729 YDL238C GUD1 +P53551 YPL127C HHO1 +P14064 YKL109W HAP4 +Q12341 YPL001W HAT1 +P38523 YOR232W MGE1 +P41921 YPL091W GLR1 +P32836 YOR185C GSP2 +Q00582 YML121W GTR1 +P53290 YGR163W GTR2 +P39996 YEL017W GTT3 +P38970 YJL165C HAL5 +P53973 YNL021W HDA1 +P38199 YBL032W HEK2 +Q12361 YDL035C GPR1 +P24814 YJR090C GRR1 +Q04697 YML048W GSF2 +P40582 YIR038C GTT1 +Q12390 YLL060C GTT2 +P32806 YJL044C GYP6 +P43570 YFL027C GYP8 +Q96VH4 YCL026C-B HBN1 +Q12096 YOR320C GNT1 +P46984 YJL184W GON7 +P53130 YGL121C GPG1 +P23797 YMR281W GPI12 +Q04080 YDR434W GPI17 +P38211 YBR004C GPI18 +P40367 YJL062W LAS21 +P47122 YJR072C NPA3 +P38143 YBR244W GPX2 +Q12068 YOL151W GRE2 +Q08220 YOL049W GSH2 +Q04806 YMR251W GTO3 +P40956 YGL181W GTS1 +P38625 YMR217W GUA1 +P46943 YLR289W GUF1 +P42944 YJL110C GZF3 +Q12180 YOL089C HAL9 +Q05580 YDR266C HEL2 +P36014 YKL026C GPX1 +Q07845 YLL035W GRC3 +P47026 YJL091C GWT1 +P53258 YGR100W MDR1 +Q12344 YPL249C GYP5 +P27472 YLR258W GSY2 +Q06201 YLR445W GMC2 +P36125 YKR030W GMH1 +P41911 YOL059W GPD2 +P53961 YNL038W GPI15 +P49018 YDR331W GPI8 +P16474 YJL034W KAR2 +P32477 YJL101C GSH1 +P48239 YGR154C GTO1 +P36156 YKR076W ECM4 +P00815 YCL030C HIS4 +P53187 YGL033W HOP2 +Q12214 YPR068C HOS1 +Q01448 YBR215W HPC2 +Q05905 YLR301W HRI1 +Q05549 YDR291W HRQ1 +P09950 YDR232W HEM1 +P28789 YDL205C HEM3 +Q12276 YOR227W HER1 +P41809 YDR420W HKR1 +P0CY07 YCL066W HMLALPHA1 +P54839 YML126C ERG13 +P40480 YIL112W HOS4 +P48570 YDL182W LYS20 +P36078 YKL084W HOT13 +Q99332 YOR324C FRT1 +P17629 YDR138W HPR1 +P47171 YJR140C HIR3 +P48353 YMR161W HLJ1 +Q04429 YDR528W HLR1 +P12683 YML075C HMG1 +P0CY13 YCR096C HMRA2 +Q12398 YOR032C HMS1 +P40545 YIL020C HIS6 +P33734 YBR248C HIS7 +P38635 YFR025C HIS2 +Q03937 YDR014W-A HED1 +P51979 YGL251C HFM1 +P06633 YOR202W HIS3 +P02293 YDR224C HTB1 +P13434 YBL021C HAP3 +P32769 YKR084C HBS1 +Q07653 YDL223C HBT1 +P25364 YCR065W HCM1 +Q06623 YPR179C HDA3 +Q12060 YPL254W HFI1 +Q12373 YLL022C HIF1 +P53834 YNL281W HCH1 +Q03281 YDR458C HEH2 +P36113 YKR017C HEL1 +P06174 YOR278W HEM4 +P46973 YJR055W HIT1 +P0CY11 YCR097W HMRA1 +Q06629 YDR295C HDA2 +P05373 YGL040C HEM2 +P11353 YDR044W HEM13 +P04912 YBL003C HTA2 +Q12692 YOL012C HTZ1 +P61830 YBR010W; YNL031C HHT1; HHT2 +P02309 YBR009C; YNL030W HHF1; HHF2 +Q01766 YPR005C HAL1 +P0CE41 YLR256W HAP1 +P06774 YGL237C HAP2 +Q02516 YOR358W HAP5 +Q03532 YMR290C HAS1 +P39984 YEL056W HAT2 +P34243 YKL017C HCS1 +P16622 YOR176W HEM15 +P35843 YOR237W HES1 +Q04458 YMR110C HFD1 +P39982 YEL059W HHY1 +P32480 YOR038C HIR2 +P00498 YER055C HIS1 +Q04344 YDL125C HNT1 +P49775 YDR305C HNT2 +P40481 YIL110W HPM1 +Q05787 YLR207W HRD3 +Q99383 YOL123W HRP1 +P29295 YPL204W HRR25 +Q06674 YDR317W HIM1 +P32479 YBL008W HIR1 +P07172 YIL116W HIS5 +P40037 YER057C HMF1 +Q03973 YDR174W HMO1 +P19807 YGL077C HNM1 +P47124 YJR075W HOC1 +Q9URQ5 YCR020W-B HTL1 +P45820 YGL168W HUR1 +P32874 YMR207C HFA1 +P38074 YBR034C HMT1 +P32339 YLR205C HMX1 +P53096 YGL194C HOS2 +Q02959 YPL116W HOS3 +P32478 YJL159W HSP150 +P34244 YKL101W HSL1 +P32590 YBR169C SSE2 +P40985 YJR036C HUL4 +P53982 YNL009W IDP3 +P48362 YGR187C HGH1 +P06775 YGR191W HIP1 +P12684 YLR450W HMG2 +P53389 YNR055C HOL1 +Q05164 YOL155C HPF1 +P38753 YHL002W HSE1 +P10961 YGL073W HSF1 +Q99181 YOR319W HSH49 +P22943 YFL014W HSP12 +P53687 YOR025W HST3 +P32485 YLR113W HOG1 +Q12122 YDL131W LYS21 +Q03213 YMR172W HOT1 +P39734 YAL028W FRT2 +Q12347 YLR097C HRT3 +P15992 YBR072W HSP26 +P25619 YCR021C HSP30 +Q08992 YPL280W HSP32 +P40325 YGR268C HUA1 +Q6Q546 YNR032C-A HUB1 +Q12345 YLR052W IES3 +P39730 YAL035W FUN12 +Q04432 YDR533C HSP31 +Q12329 YDR171W HSP42 +Q05931 YLR369W SSQ1 +P38790 YHR067W HTD2 +P53119 YGL141W HUL5 +P39924 YEL069C HXT13 +P54854 YDL245C HXT15 +P32465 YHR094C HXT1 +P32466 YDR345C HXT3 +P38695 YHR096C HXT5 +P39004 YDR342C HXT7 +P32464 YKL189W HYM1 +P41734 YOR126C IAH1 +P46958 YJL146W IDS2 +P40060 YER092W IES5 +P20459 YJR007W SUI2 +P28817 YDR036C EHD3 +P0CY09 YCL067C HMLALPHA2 +Q12039 YOL095C HMI1 +P20050 YIL072W HOP1 +Q05827 YMR251W-A HOR7 +Q06592 YPR193C HPA2 +Q04178 YDR399W HPT1 +P38922 YNL004W HRB1 +Q08109 YOL013C HRD1 +Q08732 YOR267C HRK1 +P69852 YKL138C-A HSK3 +Q08914 YOR391C HSP33 +P50079 YGR223C HSV2 +Q6Q5K6 YML058W-A HUG1 +P04806 YFR053C HXK1 +P04807 YGL253W HXK2 +Q12134 YOR284W HUA2 +Q12520 YPL244C HUT1 +Q12385 YLR099C ICT1 +P15496 YPL117C IDI1 +P09064 YPL237W SUI3 +P10081 YKR059W; YJL138C TIF1; TIF2 +P39936 YGL049C TIF4632 +P47175 YJR147W HMS2 +P09932 YDL227C HO +P39979 YEL066W HPA3 +P38348 YBR272C HSM3 +P19882 YLR259C HSP60 +P22202 YER103W SSA4 +P33416 YDR258C HSP78 +P53685 YOL068C HST1 +P53686 YPL015C HST2 +P54862 YOL156W HXT11 +P42833 YNL318C HXT14 +P47185 YJR158W HXT16 +P40886 YJL214W HXT8 +P53688 YDR191W HST4 +P53892 YNL164C IBD2 +P40499 YIL090W ICE2 +P40051 YER078C ICP55 +P38284 YBR157C ICS2 +Q04329 YMR195W ICY1 +P38274 YBR133C HSL7 +P09435 YBL075C SSA3 +P0CS90 YJR045C SSC1 +P39987 YEL030W ECM10 +P28834 YNL037C IDH1 +P41939 YLR174W IDP2 +P25038 YOL023W IFM1 +P19211 YJR047C ANB1 +Q12522 YPR016C TIF6 +P06168 YLR355C ILV5 +P39567 YAR073W IMD1 +P50095 YLR432W IMD3 +Q02888 YPL099C INA17 +Q03824 YMR163C INP2 +Q12271 YOR109W INP53 +P00724 YIL162W SUC2 +P28239 YMR267W PPA2 +P32589 YPL106C SSE1 +P17709 YCL040W GLK1 +P43581 YFL011W HXT10 +P40441 YIL170W HXT12 +P53631 YNR072W HXT17 +P23585 YMR011W HXT2 +P32467 YHR092C HXT4 +P39003 YDR343C HXT6 +P40885 YJL219W HXT9 +P47125 YJR078W BNA2 +P43598 YFR017C IGD1 +P39522 YJR016C ILV3 +Q02821 YNL189W SRP1 +P40069 YER110C KAP123 +P32581 YJL106W IME2 +P25626 YCR046C IMG1 +P46972 YMR035W IMP2 +P53941 YNL075W IMP4 +Q03694 YMR204C INP1 +Q08630 YOR235W IRC13 +Q04772 YMR073C IRC21 +P47046 YJL051W IRC8 +P28241 YOR136W IDH2 +P40154 YNL215W IES2 +P32617 YEL044W IES6 +P47170 YJR138W IML1 +Q05533 YDR287W INM2 +P53901 YNL152W INN1 +P50942 YNL106C INP52 +Q12072 YLR095C IOC2 +Q04213 YMR044W IOC4 +P07250 YDR173C ARG82 +P38954 YDR072C IPT1 +P47034 YJL077C ICS3 +P07260 YOL139C CDC33 +P39520 YLR223C IFH1 +P25605 YCL009C ILV6 +P07342 YMR108W ILV2 +P21954 YDL066W IDP1 +P43579 YFL013C IES1 +Q08561 YOR189W IES4 +P38912 YMR260C TIF11 +P32481 YER025W GCD11 +P39935 YGR162W TIF4631 +P23301 YEL034W HYP2 +Q9P305 YHR132W-A IGO2 +P47042 YJL057C IKS1 +P47155 YJR118C ILM1 +P38217 YBR017C KAP104 +P21190 YJR094C IME1 +P41833 YGL192W IME4 +P53219 YGR031W IMO32 +P32899 YHR148W IMP3 +P40573 YIR017C MET28 +Q03081 YPL038W MET31 +P47169 YJR137C MET5 +P05694 YER091C MET6 +P10659 YLR180W SAM1 +Q04922 YDR219C MFB1 +P32787 YJR144W MGM101 +P28321 YKL094W YJU3 +P32266 YOR211C MGM1 +P26188 YDL200C MGT1 +Q04472 YMR115W MGR3 +P36046 YKL195W MIA40 +P50945 YNL100W MIC27 +P39943 YER028C MIG3 +Q08176 YOL026C MIM1 +Q04341 YDR031W MIX14 +P38920 YMR167W MLH1 +P40457 YIL149C MLP2 +P53102 YGL183C MND1 +P24720 YOR350C MNE1 +P18408 YPR167C MET16 +Q07684 YDL233W MFG1 +P53152 YGL087C MMS2 +P38888 YHR204W MNL1 +P41821 YNL291C MID1 +P53035 YGL209W MIG2 +P32491 YPL140C MKK2 +P34072 YNL076W MKS1 +Q06580 YPR188C MLC2 +P32047 YNL074C MLF3 +Q12372 YLL061W MMP1 +Q06324 YLR190W MMR1 +P46982 YJL186W MNN5 +P39107 YPL050C MNN9 +P40549 YIL014W MNT3 +P53745 YNR059W MNT4 +P43563 YFL034C-B MOB2 +P23641 YJR077C MIR1 +P47083 YJR002W MPP10 +Q03667 YMR002W MIX17 +P38162 YBL107C MIX23 +Q06211 YPR164W MMS1 +Q12205 YLR057W MNL2 +P46985 YJL183W MNN11 +P38069 YBR015C MNN2 +P53129 YGL124C MON1 +P53311 YGR243W MPC3 +P0CD99 YDL247W MPH2 +P23748 YMR036C MIH1 +P53379 YDR144C MKC7 +Q06164 YLR320W MMS22 +P40577 YIR025W MND2 +P39106 YER001W MNN1 +P36044 YKL201C MNN4 +P35724 YKL064W MNR2 +P53059 YGL257C MNT2 +P53157 YGL080W MPC1 +Q12411 YOL091W SPO21 +Q01926 YOR334W MRS2 +P47084 YJR003C MRX12 +P53869 YNL211C MRX7 +Q07980 YLR035C MLH2 +P38257 YBR098W MMS4 +P40484 YIL106W MOB1 +P54785 YMR070W MOT3 +P41940 YDL055C PSA1 +P40562 YIR002C MPH1 +P0CE00 YJR160C MPH3 +P53725 YNR024W MPP6 +P53159 YGL075C MPS2 +Q08471 YOR066W MSA1 +P08593 YPR134W MSS18 +P40990 YDL107W MSS2 +Q07938 YLR017W MEU1 +Q03218 YMR177W MMT1 +Q08970 YPL224C MMT2 +P07884 YOR274W MOD5 +P38191 YBL049W MOH1 +P32333 YPL082C MOT1 +P32829 YMR224C MRE11 +P53166 YGL064C MRH4 +P40185 YIL051C MMF1 +P50108 YDR245W MNN10 +P53163 YGL068W MNP1 +P32906 YJR131W MNS1 +P47123 YJR074W MOG1 +P53583 YNL249C MPA43 +P38857 YHR162W MPC2 +Q12404 YOR288C MPD1 +P35728 YKL059C MPE1 +P40364 YJL066C MPM1 +P54199 YDL028C MPS1 +P47069 YJL019W MPS3 +P39016 YGL178W MPT5 +P25336 YCR092C MSH3 +P53045 YGR060W ERG25 +P22148 YOL116W MSN1 +P52918 YDR335W MSN5 +P33748 YMR037C MSN2 +P40029 YER042W MXR1 +Q03825 YMR164C MSS11 +P36066 YKL133C +Q3E829 YDL160C-A MHF2 +P38341 YBR262C MIC12 +P36112 YKR016W MIC60 +P40850 YNL085W MKT1 +Q08925 YPL184C MRN1 +P33201 YKL009W MRT4 +Q05648 YDR282C MRX10 +P40050 YER077C MRX1 +P48564 YNL295W MRX6 +P15424 YDR194C MSS116 +Q08818 YOR354C MSC6 +P25846 YHR120W MSH1 +P40965 YFL003C MSH4 +Q12175 YDL154W MSH5 +P40567 YIR009W MSL1 +P53604 YNR049C MSO1 +P20676 YOR098C NUP1 +Q02199 YGL172W NUP49 +Q12454 YDR067C OCA6 +P31755 YGL038C OCH1 +Q99297 YOR222W ODC2 +P38325 YBR230C OM14 +Q07521 YDL096C OPI6 +Q06593 YPR194C OPT2 +P50874 YNL261W ORC5 +Q06144 YLR350W ORM2 +P21375 YJR051W OSM1 +Q03723 YML019W OST6 +Q02795 YMR149W SWP1 +Q08692 YOR255W OSW1 +P43558 YFL044C OTU1 +P32336 YOR373W NUD1 +P38738 YHL029C OCA5 +P16387 YER178W PDA1 +P16547 YIL136W OM45 +Q06810 YPR075C OPY2 +P54784 YML065W ORC1 +Q99380 YDL232W OST4 +P53136 YGL111W NSA1 +P52891 YDL116W NUP84 +P07991 YLR438W CAR2 +P20967 YIL125W KGD1 +P16451 YGR193C PDX1 +Q06668 YDR316W OMS1 +A0A023PZI1 YPR044C OPI11 +P87286 YDR360W OPI7 +P38271 YBR129C OPY1 +Q02630 YMR047C NUP116 +P33895 YOL069W NUF2 +Q12255 YLR093C NYV1 +P25366 YCR095C OCA4 +P19262 YDR148C KGD2 +P12695 YNL071W LAT1 +P54790 YLL004W ORC3 +Q12375 YOR130C ORT1 +P48439 YOR085W OST3 +P05150 YJL088W ARG3 +P52593 YML103C NUP188 +Q02803 YPL052W OAZ1 +P21957 YHL020C OPI1 +P54791 YPR162C ORC4 +P33400 YHL027W RIM101 +P38351 YBR279W PAF1 +Q12033 YOR275C RIM20 +P37304 YDR251W PAM1 +P53010 YGL094C PAN2 +P36102 YKL025C PAN3 +Q03050 YDR542W PAU10 +P0CE89 YIL176C PAU14 +P0CE88 YJL223C PAU1 +Q07987 YLR037C PAU23 +P0CE90 YNR076W PAU6 +P53298 YGR179C OKP1 +P28273 YKL215C OXP1 +P40897 YJL212C OPT1 +P32833 YBR060C ORC2 +P33751 YDR538W PAD1 +P32567 YMR165C PAH1 +P36129 YKR035C OPI8 +P38826 YHR118C ORC6 +Q12447 YDR071C PAA1 +Q05518 YDR348C PAL1 +P53179 YGL045W RIM8 +P48565 YNL294C RIM21 +Q04734 YMR063W RIM9 +P36147 YKR065C PAM17 +P32521 YIR006C PAN1 +P40459 YIL145C PAN6 +Q08202 YOL032W OPI10 +O94084 YLR338W OPI9 +P54964 YLR059C REX2 +Q12451 YDL019C OSH2 +Q02201 YKR003W OSH6 +P38122 YBR176W ECM31 +P50946 YNL099C OCA1 +P36163 YKR087C OMA1 +P33767 YEL002C WBP1 +Q12202 YLR054C OSW2 +P43611 YFR039C OSW7 +P32263 YER023W PRO3 +P40960 YDR488C PAC11 +P39937 YER007W PAC2 +P41543 YJL002C OST1 +P46964 YOR103C OST2 +Q08952 YPL196W OXR1 +P41816 YPL171C OYE3 +P38725 YHL046C PAU13 +P0CE91 YLL064C PAU18 +P0CE87 YPL282C PAU22 +P25610 YCR104W PAU3 +P40091 YER149C PEA2 +P25625 YCR044C PER1 +Q12144 YLR064W PER33 +Q92316 YGL226C-A OST5 +P40219 YMR148W OSW5 +P39952 YER154W OXA1 +Q03558 YHR179W OYE2 +Q04430 YDR531W CAB1 +P25644 YCR077C PAT1 +P35994 YKL224C PAU16 +P53427 YLR461W PAU4 +P39545 YAR020C PAU7 +Q12524 YLR151C PCD1 +P38126 YBR186W PCH2 +P53124 YGL134W PCL10 +P24867 YNL289W PCL1 +Q08966 YPL219W PCL8 +P15873 YBR088C POL30 +P40345 YNR008W LRO1 +P37254 YNR033W ABZ1 +P38794 YHR071W PCL5 +P53259 YGR101W PCP1 +P26263 YGR087C PDC6 +P22434 YGL248W PDE1 +P06776 YOR360C PDE2 +Q03266 YMR289W ABZ2 +P53632 YOL115W PAP2 +P29468 YKR002W PAP1 +Q12515 YDL173W PAR32 +P40186 YIL050W PCL7 +P17967 YCL043C PDI1 +P40530 YIL042C PKP1 +P12383 YGL013C PDR1 +P33200 YBL005W PDR3 +P33302 YOR153W PDR5 +P53224 YGR038W ORM1 +P35845 YAR042W SWH1 +P38713 YHR073W OSH3 +P38755 YHR001W OSH7 +P38747 YHL013C OTU2 +P38787 YHR063C PAN5 +Q07362 YDL053C PBP4 +P08018 YJL128C PBS2 +P25693 YDL127W PCL2 +Q12477 YDL179W PCL9 +P13259 YGR202C PCT1 +P32896 YDR081C PDC2 +Q99220 YDR057W YOS9 +P04147 YER165W PAB1 +P53343 YGR294W PAU12 +Q12370 YLL025W PAU17 +Q08322 YOL161C PAU20 +P38155 YBR301W PAU24 +P0CE92 YAL068C PAU8 +P25580 YCL052C PBN1 +P10963 YKR097W PCK1 +P40038 YER059W PCL6 +P40550 YIL013C PDR11 +Q04182 YDR406W PDR15 +P53756 YNR070W PDR18 +Q04264 YMR076C PDS5 +P36139 YKR046C PET10 +Q12462 YOL147C PEX11 +P53112 YGL153W PEX14 +P24004 YKL197C PEX1 +Q03370 YDR479C PEX29 +P39108 YDR142C PEX7 +P48363 YGR078C PAC10 +Q04493 YML094W GIM5 +P53170 YGL059W PKP2 +P53860 YNL231C PDR16 +P38075 YBR035C PDX3 +P25362 YCR020C PET18 +P80667 YLR191W PEX13 +P50091 YGR239C PEX21 +P25584 YCL056C PEX34 +P47116 YJR059W PTK2 +P29461 YOR208W PTP2 +P07244 YGL234W ADE5,7 +P54113 YLR028C ADE16 +P53294 YGR169C PUS6 +Q12069 YDL036C PUS9 +P09368 YLR142W PUT1 +P03962 YEL021W URA3 +Q9ZZX9 Q0010 +Q9ZZW4 Q0142 +Q9ZZW2 Q0144 +P43122 YDL104C QRI7 +P41903 YJR019C TES1 +P25339 YGL014W PUF4 +Q06991 YLR414C PUN1 +P38972 YGR061C ADE6 +P53167 YGL063W PUS2 +P11154 YGL062W PYC1 +P28272 YKL216W URA1 +Q9ZZV8 Q0297 +Q12355 YDR055W PST1 +P39927 YGR156W PTI1 +P27616 YAR015W ADE1 +Q05911 YLR359W ADE13 +Q35811 Q0092 +Q9ZZW1 Q0182 +P04046 YMR300C ADE4 +P38009 YMR120C ADE17 +Q06244 YLR165C PUS5 +P25502 YKL015W PUT3 +P08525 YJL166W QCR8 +P38230 YBR046C ZTA1 +P06838 YML095C RAD10 +P32641 YER173W RAD24 +Q00578 YIL143C SSL2 +Q04231 YML011C RAD33 +P14736 YER162C RAD4 +P06778 YML032C RAD52 +P22216 YPL153C RAD53 +P38953 YDR076W RAD55 +P06779 YJR052W RAD7 +P32864 YOR370C MRS6 +Q06891 R0030W RAF1 +P25635 YCR057C PWP2 +P34230 YKL188C PXA2 +P32327 YBR218C PYC2 +P13298 YML106W URA5 +P37299 YHR001W-A QCR10 +P07256 YBL045C COR1 +P06777 YPL022W RAD1 +P32628 YEL037C RAD23 +P06839 YER171W RAD3 +Q12270 YPL246C RBD2 +P50086 YGR232W NAS6 +P53037 YGR170W PSD2 +P31374 YAL017W PSK1 +Q02771 YER058W PET117 +P32606 YOR017W PET127 +P32522 YLR067C PET309 +Q01329 YAL043C PTA1 +Q04373 YDR496C PUF6 +P80210 YNL220W ADE12 +Q02256 YIR026C YVH1 +P21304 YLR196W PWP1 +P30620 YMR137C PSO2 +P50896 YDR505C PSP1 +P36082 YKL076C PSY1 +Q12318 YLR376C PSY3 +P47065 YJL023C PET130 +Q02772 YJR034W PET191 +P07390 YNR045W PET494 +P34222 YBL057C PTH2 +P04161 YDR408C ADE8 +Q12488 YDR013W PSF1 +P31115 YFL001W DEG1 +Q08647 YOR243C PUS7 +P39006 YNL169C PSD1 +P25044 YDL230W PTP1 +P40048 YER075C PTP3 +P40454 YIL153W RRD1 +P32588 YNL016W PUB1 +Q12221 YPR042C PUF2 +Q07807 YLL013C PUF3 +P21264 YOR128C ADE2 +P41909 YPL147W PXA1 +P36166 YKR090W PXL1 +P53335 YGR280C PXR1 +P05737 YGL076C RPL7A +P17076 YHL033C RPL8A +P10622 YDL130W RPP1B +P53060 YGL250W RMR1 +P36159 YKR079C TRZ1 +P53118 YGL144C ROG1 +P51862 YLR371W ROM2 +P32529 YJR063W RPA12 +Q01080 YNL248C RPA49 +P27999 YGL070C RPB9 +P47076 YJL011C RPC17 +P05738 YGL147C RPL9A +Q02204 YKR006C MRPL13 +P22354 YKR085C MRPL20 +Q12508 YDR255C RMD5 +P40993 YDR478W SNM1 +Q02933 YPL123C RNY1 +P25042 YPR065W ROX1 +P10964 YOR341W RPA190 +P40422 YHR143W-A RPC10 +P07703 YPR110C RPC40 +P38902 YOL005C RPB11 +P16370 YIL021W RPB3 +P34087 YDR404C RPB7 +Q12189 YOR095C RKI1 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+P38849 YHR151C MTC6 +P0CX81 YHR055C CUP1-2 +Q02046 YKR080W MTD1 +Q03151 YMR097C MTG1 +P47095 YJR024C MDE1 +Q04149 YDR386W MUS81 +P40959 YMR004W MVP1 +P36006 YKL129C MYO3 +P47018 YJL123C MTC1 +P53077 YGL226W MTC3 +P53320 YGR257C MTM1 +P32377 YNR043W MVD1 +P23059 YCR020C-A MAK31 +P32505 YGL122C NAB2 +P40314 YDR252W BTT1 +P43619 YFR047C BNA6 +Q03455 YDR205W MSC2 +P25847 YOL090W MSH2 +P28737 YGR028W MSP1 +P53176 YGL051W MST27 +Q03920 YDR140W MTQ2 +P48240 YGR158C MTR3 +Q12093 YDL033C SLM3 +P36084 YKL074C MUD2 +P32335 YLR203C MSS51 +P39552 YAR033W MST28 +P0CY08 YCR039C MATALPHA2 +P34246 YKL098W MTC2 +P38335 YBR255W MTC4 +P32633 YEL033W MTC7 +P46151 YPL023C MET12 +P53128 YGL125W MET13 +Q06489 YPR118W MRI1 +Q06106 YPR112C MRD1 +Q12117 YDR033W MRH1 +P50873 YDL079C MRK1 +P35719 YKL142W MRP8 +P47007 YJL147C MRX5 +Q07349 YDL027C MRX9 +P13712 YBR195C MSI1 +Q03162 YMR100W MUB1 +P50276 YGR055W MUP1 +P38994 YDR208W MSS4 +Q03429 YDR493W MZM1 +Q02642 YPL037C EGD1 +Q99316 YOL088C MPD2 +Q06390 YDR374C PHO92 +P25588 YCL061C MRC1 +Q06815 YPR079W MRL1 +P25270 YOR201C MRM1 +P53123 YGL136C MRM2 +O75012 YDL045W-A MRP10 +P10566 YJL133W MRS3 +Q03079 YPL041C MRX11 +P38172 YBL095W MRX3 +P36157 YKR077W MSA2 +P32334 YGR014W MSB2 +P38694 YHR039C MSC7 +P10849 YDL044C MTF2 +P38860 YHR168W MTG2 +P35198 YDR277C MTH1 +Q03677 YMR009W ADI1 +P53070 YGL236C MTO1 +P53944 YNL063W MTQ1 +P34232 YKL186C MTR2 +P48563 YNL297C MON2 +Q05812 YLR219W MSC3 +P53214 YGR023W MTL1 +Q08550 YOR177C MPC54 +P29952 YER003C PMI40 +P11914 YHR024C MAS2 +P10507 YLR163C MAS1 +P07266 YIR021W MRS1 +P23500 YKR052C MRS4 +Q12467 YPL168W MRX4 +Q05473 YDR336W MRX8 +P21339 YOR188W MSB1 +Q12317 YOL112W MSB4 +Q03104 YML128C MSC1 +P38590 YNL053W MSG5 +Q03834 YDR097C MSH6 +P33749 YKL062W MSN4 +Q99189 YOR160W MTR10 +P47047 YJL050W MTR4 +P39731 YAL034W-A MTW1 +Q08750 YOR298W MUM3 +P19524 YOR326W MYO2 +P32492 YAL029C MYO4 +P37293 YGR147C NAT2 +Q06504 YPR131C NAT3 +Q08689 YOR253W NAT5 +Q08920 YPL178W CBC2 +P16603 YHR042W NCP1 +Q06389 YDR373W FRQ1 +Q12366 YOL104C NDJ1 +P38757 YHR004C NEM1 +Q03264 YMR285C NGL2 +P0CX80 YHR053C CUP1-1 +P14908 YMR228W MTF1 +P08964 YHR023W MYO1 +Q04439 YMR109W MYO5 +Q12387 YOL076W MDM20 +P38795 YHR074W QNS1 +P12945 YDL040C NAT1 +P52919 YLR457C NBP1 +Q12163 YDR162C NBP2 +Q12374 YPR155C NCA2 +Q02866 YPL070W MUK1 +Q02197 YEL053C MAK10 +Q8TGN9 YGR031C-A NAG1 +P27929 YNL137C NAM9 +P25293 YKR048C NAP1 +Q02820 YJL205C NCE101 +Q06568 YLR254C NDL1 +P38236 YBR057C MUM2 +P38734 YHL036W MUP3 +P42939 YGR206W MVB12 +P25566 YCL033C MXR2 +Q04751 YMR069W NAT4 +Q03735 YML117W NAB6 +P53919 YNL124W NAF1 +P40360 YJL071W ARG2 +P30771 YMR080C NAM7 +Q08229 YOL070C NBA1 +P52920 YGL091C NBP35 +P46955 YJL116C NCA3 +P34160 YMR125W STO1 +P38205 YBL024W NCL1 +Q07500 YDL085W NDE2 +Q03503 YPR051W MAK3 +P38996 YPL190C NAB3 +P38879 YHR193C EGD2 +P23503 YNL240C NAR1 +Q3E7Y6 YHR199C-A NBL1 +Q12207 YPR149W NCE102 +Q08887 YOR372C NDD1 +P36010 YKL067W YNK1 +P25374 YCL017C NFS1 +Q99271 YLR138W NHA1 +Q00539 YHR086W NAM8 +P53914 YNL132W KRE33 +P40096 YER159C BUR6 +P32500 YML031W NDC1 +P40460 YIL144W NDC80 +P32831 YBR212W NGR1 +P32340 YML120C NDI1 +P39744 YOR206W NOC2 +P25353 YCR026C NPP1 +P53718 YNR009W NRM1 +Q08485 YOR071C NRT1 +P38632 YEL019C MMS21 +Q05541 YDR288W NSE3 +P53898 YNL156C NSG2 +Q12457 YDR026C NSI1 +P36052 YKL162C +Q06148 YLR265C NEJ1 +P25382 YCR072C RSA4 +P38798 YHR077C NMD2 +P47149 YJR112W NNF1 +P36059 YKL151C +P40165 YNL200C +Q06162 YLR315W NKP2 +P48234 YGR145W ENP2 +Q07623 YDL213C NOP6 +P38082 YBR066C NRG2 +P27476 YGR159C NSR1 +Q08214 YOL043C NTG2 +P40215 YMR145C NDE1 +Q03210 YML118W NGL3 +P32495 YDL208W NHP2 +Q04121 YDR456W NHX1 +P34077 YFR002W NIC96 +P32770 YDL167C NRP1 +Q12181 YPR048W TAH18 +P53317 YGR251W NOP19 +P37838 YPL043W NOP4 +Q12080 YPL146C NOP53 +P33755 YBR170C NPL4 +P22211 YNL183C NPR1 +P39683 YOR209C NPT1 +P53915 YNL129W NRK1 +P53935 YNL091W NST1 +Q12311 YPR031W NTO1 +Q02629 YKL068W NUP100 +Q92317 YDR397C NCB2 +P38626 YIL043C CBR1 +P38830 YHR124W NDT80 +P33420 YPL174C NIP100 +P40447 YIL164C NIT1 +P49954 YLR351C NIT3 +Q06178 YLR328W NMA1 +P38861 YHR170W NMD3 +P46970 YJR132W NMD5 +Q08213 YOL042W NGL1 +P53939 YNL078W NIS1 +P34909 YER068W MOT2 +P32494 YDR176W NGG1 +P11633 YBR089C-A NHP6B +P47016 YJL126W NIT2 +Q6Q547 YHR072W-A NOP10 +Q99207 YDL148C NOP14 +Q01560 YDR432W NPL3 +Q12499 YOR310C NOP58 +P47077 YJL010C NOP9 +P39923 YEL062W NPR2 +P53164 YGL067W NPY1 +Q08972 YPL226W NEW1 +P0CE68 YKR103W NFT1 +P32860 YKL040C NFU1 +Q03435 YDL002C NHP10 +P53081 YGL221C NIF3 +P53920 YNL123W NMA111 +Q12129 YLR363C NMD4 +P53253 YGR089W NNF2 +Q08444 YOR056C NOB1 +Q06512 YPR144C NOC4 +Q08208 YOL041C NOP12 +Q12460 YLR197W NOP56 +Q12408 YDL046W NPC2 +Q06287 YLR186W EMG1 +P47035 YJL076W NET1 +P11632 YPR052C NHP6A +Q07896 YLR002C NOC3 +Q03790 YMR153W NUP53 +P46673 YJR042W NUP85 +P36023 YKR064W OAF3 +Q03028 YPL134C ODC1 +P32473 YBR221C PDB1 +P53397 YML060W OGG1 +Q08962 YPL211W NIP7 +Q12493 YDR383C NKP1 +P14743 YLR195C NMT1 +P36003 YKL171W NNK1 +Q02892 YPL093W NOG1 +P06100 YDL165W CDC36 +Q12514 YPR072W NOT5 +P38742 YHL023C NPR3 +Q03718 YML023C NSE5 +P32499 YLR335W NUP2 +P49686 YDR192C NUP42 +P48837 YGR119C NUP57 +Q05166 YDL088C ASM4 +Q12066 YDL089W NUR1 +P32332 YKL120W OAC1 +P39720 YAL051W OAF1 +P53949 YNL056W OCA2 +Q07913 YLR007W NSE1 +P38837 YHR133C NSG1 +Q12143 YPL233W NSL1 +P14907 YJL041W NSP1 +P35729 YKL057C NUP120 +P40064 YER105C NUP157 +P40477 YIL115C NUP159 +P08466 YJL208C NUC1 +P40010 YER006W NUG1 +Q00402 YDR150W NUM1 +P39705 YAR002W NUP60 +P40368 YJL061W NUP82 +P38881 YHR195W NVJ1 +P40354 YJR062C NTA1 +P38302 YBR188C NTC20 +P31378 YAL015C NTG1 +P49687 YGL092W NUP145 +P38219 YBR025C OLA1 +P53204 YGR010W NMA2 +P53883 YNL175C NOP13 +P53927 YNL110C NOP15 +P25655 YCR093W CDC39 +P06102 YIL038C NOT3 +P39997 YEL016C NPP2 +P53617 YNL251C NRD1 +P40007 YER002W NOP16 +P40991 YNL061W NOP2 +Q08287 YOL144W NOP8 +P40078 YER126C NSA2 +P43124 YDL105W NSE4 +Q04958 YML059C NTE1 +P33331 YER009W NTF2 +P36118 YKR022C NTR2 +P36161 YKR082W NUP133 +P38181 YBL079W NUP170 +P47054 YJL039C NUP192 +P53742 YNR053C NOG2 +Q12200 YPL006W NCR1 +Q03125 YDR043C NRG1 +P39081 YDR228C PCF11 +P51533 YOR328W PDR10 +Q02785 YPL058C PDR12 +P38855 YHR160C PEX18 +Q07418 YDL065C PEX19 +Q06169 YLR324W PEX30 +P40005 YEL003W GIM4 +Q08959 YPL206C PGC1 +Q05637 YDR281C PHM6 +P07269 YDL106C PHO2 +P17442 YGR233C PHO81 +P25360 YCR037C PHO87 +Q06216 YLR273C PIG1 +P38768 YHR034C PIH1 +Q12057 YOR104W PIN2 +P46999 YJL160C PIR5 +Q03407 YDR490C PKH1 +P39105 YMR008C PLB1 +Q03674 YMR006C PLB2 +P32383 YPL268W PLC1 +Q12511 YOR090C PTC5 +P25646 YCR079W PTC6 +P53844 YNL264C PDR17 +P27801 YLR148W PEP3 +P40335 YJL053W PEP8 +Q99373 YPL159C PET20 +Q04370 YMR026C PEX12 +Q08215 YOL044W PEX15 +P53203 YGR004W PEX31 +P33760 YNL329C PEX6 +P42836 YNL326C PFA3 +Q12006 YOL003C PFA4 +Q03289 YDR459C PFA5 +P46988 YJL179W PFD1 +P52553 YLR200W YKE2 +P32452 YNL316C PHA2 +P07270 YFR034C PHO4 +P20052 YOL001W PHO80 +P38361 YBR296C PHO89 +P06738 YPR160W GPH1 +P40187 YIL045W PIG2 +Q06149 YLR266C PDR8 +Q06608 YPR172W +P12868 YMR231W PEP5 +P39684 YFR023W PES4 +Q12252 YOL084W PHM7 +P53297 YGR178C PBP1 +P38151 YBR233W PBP2 +P06169 YLR044C PDC1 +P38848 YHR150W PEX28 +P32800 YJL210W PEX2 +P38292 YBR168W PEX32 +P28795 YDR329C PEX3 +P35056 YDR244W PEX5 +P53900 YNL153C GIM3 +P53872 YNL190W +P53896 YNL158W PGA1 +Q12746 YML125C PGA3 +P25578 YCL004W PGS1 +P18898 YGL155W CDC43 +P39535 YJL198W PHO90 +P05066 YOR386W PHR1 +P32854 YOR036W PEP12 +P38921 YNL003C PET8 +P40155 YNL214W PEX17 +Q02969 YPL112C PEX25 +Q08580 YOR193W PEX27 +P53248 YGR077C PEX8 +P53903 YNL149C PGA2 +P40025 YER037W PHM8 +Q06651 YDR313C PIB1 +P07271 YML061C PIF1 +P19657 YPL036W PMA2 +P87284 YDR276C PMP3 +P14242 YNL082W PMS1 +P47190 YOR321W PMT3 +P52867 YDL093W PMT5 +P42934 YGR199W PMT6 +Q05788 YLR209C PNP1 +P47180 YJR153W PGU1 +P37012 YMR105C PGM2 +Q03262 YMR278W PRM15 +P40961 YGR132C PHB1 +P50085 YGR231C PHB2 +P36093 YKL043W PHD1 +P50947 YNL097C PHO23 +P25297 YML123C PHO84 +P46956 YJL117W PHO86 +P38264 YBR106W PHO88 +P27514 YNR013C PHO91 +Q03306 YDR466W PKH3 +P33333 YDL052C SLC1 +P05030 YGL008C PMA1 +P53238 YGR058W PEF1 +P32609 YDR323C PEP7 +P53261 YGR103W NOP7 +P39718 YAL055W PEX22 +P16861 YGR240C PFK1 +P16862 YMR205C PFK2 +P00560 YCR012W PGK1 +P33401 YKL127W PGM1 +P0CE93 YGL261C PAU11 +P40585 YIR041W PAU15 +P0CE85 YMR325W PAU19 +P0CE86 YOR394W PAU21 +P32612 YEL049W PAU2 +P43575 YFL020C PAU5 +Q3E770 YBL108C-A PAU9 +Q3E833 YKR095W-A PCC1 +P16467 YLR134W PDC5 +P10834 YGR222W PET54 +Q05568 YDR265W PEX10 +P38244 YBR074W PFF1 +P42841 YNL317W PFS2 +Q00618 YJL031C BET4 +P20133 YPR176C BET2 +P38744 YHL018W +P39104 YNL267W PIK1 +P53252 YGR086C PIL1 +Q03178 YKL164C PIR1 +Q03180 YKL163W PIR3 +P06197 YPR113W PIS1 +Q12236 YOL100W PKH2 +Q03880 YMR123W PKR1 +P52960 YOR363C PIP2 +Q04383 YDR501W PLM2 +P38197 YBL036C +Q07930 YLR016C PML1 +Q12412 YOR161C PNS1 +Q07951 YLR021W IRC25 +P25576 YCL047C POF1 +Q04049 YDR419W RAD30 +Q12445 YLR018C POM34 +P28005 YAL033W POP5 +P23287 YLR433C CNA1 +P39966 YER089C PTC2 +P53691 YLR216C CPR6 +Q12326 YOL056W GPM3 +Q02890 YPL096W PNG1 +P53833 YNL282W POP3 +P38208 YBL018C POP8 +P20604 YDL047W SIT4 +P32345 YDR075W PPH3 +P11491 YDR481C PHO8 +Q04004 YDR183W PLP1 +P32634 YER132C PMD1 +P35999 YKL134C OCT1 +P32903 YCR024C-A PMP1 +Q06644 YDR307W PMT7 +P53184 YGL037C PNC1 +Q99216 YOR145C PNO1 +P19881 YDL236W PHO13 +P36040 YKL206C ADD66 +Q12164 YLL023C POM33 +P32838 YNR032W PPG1 +P38693 YHR215W PHO12 +Q08108 YOL011W PLB3 +P05375 YJR073C OPI3 +P41812 YNL221C POP1 +Q06494 YPR127W +P00950 YKL152C GPM1 +P33775 YDL095W PMT1 +P31382 YAL023C PMT2 +P46971 YJR143C PMT4 +P39685 YMR129W POM152 +Q05778 YLR199C PBA1 +Q12245 YPL144W POC4 +P23594 YDL134C PPH21 +P38797 YHR076W PTC7 +P00635 YBR093C PHO5 +P40035 YER053C PIC2 +P38969 YOR266W PNT1 +P40473 YIL122W POG1 +P39008 YNR052C POP2 +P17157 YPL031C PHO85 +P53191 YGL023C PIB2 +Q03760 YML107C PML39 +P07283 YFL045C SEC53 +P40975 YEL017C-A PMP2 +P36069 YKL128C PMU1 +P38218 YBR022W POA1 +Q04636 YML069W POB3 +P38336 YBR257W POP4 +P53218 YGR030C POP6 +P38291 YBR167C POP7 +P23595 YDL188C PPH22 +P35182 YDL006W PTC1 +P34221 YBL056W PTC3 +P40164 YNL201C PSY2 +P35842 YAR071W PHO11 +Q04705 YML047C PRM6 +P39551 YAR031W PRM9 +P32264 YDR300C PRO1 +P53549 YOR259C RPT4 +Q01939 YGL048C RPT6 +P25375 YCL057W PRD1 +P47032 YJL079C PRY1 +Q06892 YPL188W POS5 +P40506 YIL083C CAB2 +P38796 YHR075C PPE1 +Q04119 YDR452W PPN1 +P42946 YJL108C PRM10 +Q12498 YPL156C PRM4 +P32524 YJL203W PRP21 +P20053 YPR178W PRP4 +Q06449 YPR154W PIN3 +P34217 YBL051C PIN4 +Q12017 YOR281C PLP2 +Q12008 YDL021W GPM2 +P36110 YKR013W PRY2 +P30657 YFR050C PRE4 +Q12161 YOL054W PSH1 +P40555 YIL007C NAS2 +P08456 YER026C CHO1 +P36002 YKL198C PTK1 +P40100 YER185W PUG1 +P28708 YKL116C PRR1 +P23639 YML092C PRE8 +P50109 YML017W PSP2 +Q07949 YLR019W PSR2 +Q12335 YDR032C PST2 +P38958 YDR079W PET100 +P08468 YMR257C PET111 +P10355 YER153C PET122 +Q12461 YPL152W RRD2 +P32901 YKR093W PTR2 +P43606 YFR029W PTR3 +P38089 YBR125C PTC4 +P38193 YBL046W PSY4 +P38698 YHR201C PPX1 +P20457 YKL045W PRI2 +Q12459 YDL039C PRM7 +P38876 YHR189W PTH1 +P32857 YKL039W PTM1 +Q07350 YDL043C PRP11 +P40968 YDR364C CDC40 +P23394 YDR243C PRP28 +P25043 YOR157C PUP1 +P22141 YER012W PRE1 +P30656 YPR103W PRE2 +P23724 YBL041W PRE7 +P53043 YGR123C PPT1 +P33329 YDR436W PPZ2 +P10363 YIR008C PRI1 +P40494 YIL095W PRK1 +P53835 YNL279W PRM1 +P49704 YGR091W PRP31 +P28004 YAL032C PRP45 +P19735 YBR055C PRP6 +P33334 YHR165C PRP8 +P21243 YGL011C SCL1 +P21242 YOR362C PRE10 +P07272 YLR014C PPR1 +P38148 YBR276C PPS1 +P26570 YML016C PPZ1 +P49960 YMR268C PRP24 +P39682 YML046W PRP39 +P33203 YKL012W PRP40 +P40303 YOL038W PRE6 +P38624 YJL001W PRE3 +P25451 YER094C PUP3 +P40359 YJL072C PSF2 +Q08217 YOL045W PSK2 +P14747 YML057W CMP2 +P24031 YBR092C PHO3 +P52290 YDL024C DIA3 +P40347 YPR073C LTP1 +P40012 YER014W HEM14 +P32945 YPL179W PPQ1 +Q12036 YPL148C PPT2 +P40534 YIL037C PRM2 +Q08931 YPL192C PRM3 +P40476 YIL117C PRM5 +P53174 YGL053W PRM8 +P07274 YOR122C PFY1 +P15938 YKR086W PRP16 +P33411 YGR006W PRP18 +Q00723 YGR075C PRP38 +Q03776 YDR235W PRP42 +P53131 YGL120C PRP43 +P21372 YBR237W PRP5 +P19736 YDL030W PRP9 +Q12310 YDL214C PRR2 +P40327 YDL007W RPT2 +P33297 YOR117W RPT5 +P33298 YDR394W RPT3 +P09232 YEL060C PRB1 +P23638 YGR135W PRE9 +P53633 YNL044W YIP3 +P54885 YOR323C PRO2 +P32523 YLL036C PRP19 +P24384 YER013W PRP22 +P20095 YNR011C PRP2 +Q03338 YDR473C PRP3 +Q12417 YPL151C PRP46 +Q12428 YPR002W PDH1 +P33299 YKL145W RPT1 +P34227 YBL064C PRX1 +P47033 YJL078C PRY3 +P32379 YGR253C PUP2 +P40302 YMR314W PRE5 +Q12146 YOL146W PSF3 +Q07800 YLL010C PSR1 +Q12211 YPL212C PUS1 +P48567 YNL292W PUS4 +P07275 YHR037W PUT2 +P15380 YOR348C PUT4 +P07259 YJL130C URA2 +Q9ZZX8 Q0017 +P22289 YGR183C QCR9 +P32849 YLR032W RAD5 +P14737 YDR217C RAD9 +P20051 YLR420W URA4 +P07257 YPR191W QCR2 +P00128 YDR529C QCR7 +P40475 YIL120W QDR1 +P40474 YIL121W QDR2 +P38227 YBR043C QDR3 +P48581 YOR368W RAD17 +P40352 YJR035W RAD26 +Q12223 YDL059C RAD59 +P21827 YGL097W SRM1 +P53972 YNL022C RCM1 +P30402 YMR271C URA10 +Q9ZZX7 Q0032 +Q9ZZW3 Q0143 +P00127 YFR033C QCR6 +P07276 YGR258C RAD2 +Q12465 YLR084C RAX2 +A0A0B7P221 YCL054W-A RDT1 +P21651 YJR021C REC107 +P31244 YBR114W RAD16 +P25301 YDR004W RAD57 +Q99359 YDR014W RAD61 +P11938 YNL216W RAP1 +P53295 YGR173W RBG2 +Q06835 YPR094W RDS3 +Q08096 YOL010W RCL1 +Q03446 YDR003W RCR2 +P39531 YJL204C RCY1 +Q08904 YOR380W RDR1 +P03872 R0040C REP2 +P25560 YCL001W RER1 +P43556 YFL047W RGD2 +P06780 YPR165W RHO1 +Q06665 YDR314C RAD34 +P25454 YER095W RAD51 +Q03956 YDR202C RAV2 +Q05672 YDL189W RBS1 +P25332 YCR036W RBK1 +Q08273 YOL133W HRT1 +Q03530 YMR274C RCE1 +P38622 YGL158W RCK1 +P32841 YMR133W REC114 +P21538 YBR049C REB1 +P42073 YDR195W REF2 +P28519 YMR201C RAD14 +P10862 YCR066W RAD18 +Q12021 YDR030C RAD28 +P12753 YNL250W RAD50 +P32863 YGL163C RAD54 +Q08760 YOR301W RAX1 +Q03713 YML030W RCF1 +Q12044 YOR220W RCN2 +Q04779 YMR075W RCO1 +P38212 YBR005W RCR1 +P25611 YCR106W RDS1 +P19541 YPL133C RDS2 +P14291 YLR263W RED1 +P40893 YJL217W REE1 +Q00816 YDR028C REG1 +Q06709 YLR387C REH1 +P38344 YBR267W REI1 +Q12090 YLR107W REX3 +Q04418 YDR527W RBA50 +P39729 YAL036C RBG1 +P53721 YNR018W RCF2 +P38623 YLR248W RCK2 +P36054 YKL159C RCN1 +P38086 YBR073W RDH54 +Q08742 YOR286W RDL2 +P33323 YHR157W REC104 +Q12188 YPR007C REC8 +P38232 YBR050C REG2 +P01119 YOR101W RAS1 +P01120 YNL098C RAS2 +P47104 YJR033C RAV1 +Q12192 YOR279C RFM1 +P40043 YER067W RGI1 +P32862 YKL038W RGT1 +P25378 YCR027C RHB1 +Q12305 YOR285W RDL1 +P53331 YGR276C RNH70 +Q08237 YOL080C REX4 +P38630 YOR217W RFC1 +P38629 YNL290W RFC3 +Q99188 YOR107W RGS2 +Q06624 YPR180W AOS1 +P40395 YLR039C RIC1 +P43565 YFL033C RIM15 +Q08003 YLR073C RFU1 +P39083 YOR127W RGA1 +Q06108 YPR115W RGC1 +P16664 YDR137W RGP1 +Q12300 YDL138W RGT2 +P21524 YER070W RNR1 +Q07844 YLL034C RIX7 +P26785 YNL069C RPL16B +P46990 YJL177W RPL17B +P38222 YBR030W RKM3 +P36105 YKL006W RPL14A +P0CX49 YOL120C RPL18A +P0CX24 YOR312C RPL20B +Q12672 YPL079W RPL21B +P0CX41 YBL087C RPL23A +P35196 YBR002C RER2 +P30775 YGL143C MRF1 +P53893 YNL163C RIA1 +Q06208 YLR453C RIF2 +Q03778 YDR236C FMN1 +Q03792 YMR154C RIM13 +Q08961 YPL208W RKM1 +P22336 YAR007C RFA1 +P26754 YNL312W RFA2 +P26755 YJL173C RFA3 +P40348 YJR068W RFC2 +P40339 YOL094C RFC4 +P38251 YBR087W RFC5 +P06781 YNL090W RHO2 +Q12362 YOL066C RIB2 +Q3E757 YGR085C RPL11B +P03871 R0020C REP1 +P12689 YOR346W REV1 +P38206 YBL020W RFT1 +Q00453 YMR182C RGM1 +P50861 YOL143C RIB4 +P38234 YBR052C RFS1 +P48743 YLR176C RFX1 +Q06407 YDR379W RGA2 +P38339 YBR260C RGD1 +P40160 YNL207W RIO2 +P49723 YGR180C RNR4 +P38145 YBR256C RIB5 +P40188 YIL057C RGI2 +Q00245 YIL118W RHO3 +P53879 YNL180C RHO5 +P09938 YJL026W RNR2 +P21672 YIL066C RNR3 +P26784 YIL133C RPL16A +P38066 YBL033C RIB1 +Q99258 YDR487C RIB3 +P29539 YBR275C RIF1 +P38127 YBR192W RIM2 +P23796 YMR283C RIT1 +P38883 YHR197W RIX1 +P0CX53 YEL054C RPL12A +Q12690 YDL082W RPL13A +P05748 YLR029C RPL15A +P38927 YIL139C REV7 +Q00246 YKR055W RHO4 +P33312 YBR153W RIB7 +P38615 YMR139W RIM11 +P32445 YCR028C-A RIM1 +Q12196 YOR119C RIO1 +Q12504 YDR257C RKM4 +Q12367 YLR137W RKM5 +P41805 YLR075W RPL10 +P38741 YHL024W RIM4 +P0C0W9 YPR102C RPL11A +P0CX54 YDR418W RPL12B +P54780 YMR121C RPL15B +P0CX44 YGL135W RPL1B +P0CX23 YMR242C RPL20A +P05749 YLR061W RPL22A +P24000 YGR148C RPL24B +P0C2H6 YHR010W RPL27A +P0CX46 YIL018W RPL2B +P0C2H8 YDL075W RPL31A +P51402 YDR500C RPL37B +P0CX45 YFR031C-A RPL2A +P14120 YGL030W RPL30 +P05744 YPL143W RPL33A +P87262 YER056C-A RPL34A +P0CX84 YDL191W RPL35A +P05745 YMR194W RPL36A +P49626 YDR012W RPL4B +Q02753 YBR191W RPL21A +P0CX82 YBR084C-A RPL19A +P56628 YFL034C-A RPL22B +P0CX83 YBL027W RPL19B +P36144 YKR060W UTP30 +P05743 YLR344W RPL26A +Q03942 YDR198C RKM2 +P40212 YMR142C RPL13B +P38754 YHL001W RPL14B +P05740 YKL180W RPL17A +P0CX50 YNL301C RPL18B +P0CX43 YPL220W RPL1A +P04449 YGL031C RPL24A +P53221 YGR034W RPL26B +P0C2H7 YDR471W RPL27B +P41056 YOR234C RPL33B +Q12338 YLR154C RNH203 +P32385 YLL046C RNP1 +P25367 YCL028W RNQ1 +Q02555 YMR239C RNT1 +P39956 YER169W RPH1 +P23250 YIL119C RPI1 +P38886 YHR200W RPN10 +P53196 YGL004C RPN14 +P40011 YER010C +P35178 YDR087C RRP1 +Q08285 YOL142W RRP40 +Q05636 YDR280W RRP45 +Q05022 YMR229C RRP5 +P25368 YCL031C RRP7 +P25381 YCR045C RRT12 +P32611 YEL050C RML2 +P53942 YNL072W RNH201 +P45818 YGL171W ROK1 +P36121 YKR025W RPC37 +P32565 YIL075C RPN2 +P36523 YLR312W-A MRPL15 +P36526 YBR282W MRPL27 +P14063 YKL138C MRPL31 +P02381 Q0140 VAR1 +Q03441 YDL001W RMD1 +P53140 YGL107C RMD9 +Q12530 YLR145W RMP1 +Q03305 YDR465C RMT2 +Q04740 YMR234W RNH1 +P22138 YPR010C RPA135 +P20435 YPR187W RPO26 +P28000 YNL113W RPC19 +P04050 YDL140C RPO21 +P20433 YJL140W RPB4 +Q02773 YML091C RPM2 +Q04847 YMR258C ROY1 +P50106 YDR156W RPA14 +P04051 YOR116C RPO31 +P32349 YPR190C RPC82 +P17890 YNL151C RPC31 +P35718 YKL144C RPC25 +P46969 YJL121C RPE1 +Q03465 YDL020C RPN4 +Q12377 YDL097C RPN6 +Q06506 YPR137W RRP9 +P40042 YER066W RRT13 +Q07829 YLL030C RRT7 +Q08745 YOR293W RPS10A +P46784 YMR230W RPS10B +P0CX48 YBR048W RPS11B +P40693 YNL002C RLP7 +Q04599 YDR116C MRPL1 +P32904 YHR147C MRPL6 +P31334 YGR220C MRPL9 +P36521 YDL202W MRPL11 +P53875 YNL185C MRPL19 +P36525 YMR193W MRPL24 +Q06678 YDR322W MRPL35 +P19956 YMR225C MRPL44 +P40858 YJL096W MRPL49 +P25298 YMR061W RNA14 +Q02805 YOR018W ROD1 +P43602 YFR022W ROG3 +P53046 YGR070W ROM1 +Q03691 YMR200W ROT1 +P47006 YJL148W RPA34 +P46669 YOR340C RPA43 +P20434 YBR154C RPB5 +P20436 YOR224C RPB8 +P22139 YOR210W RPB10 +Q04307 YDR045C RPC11 +P25441 YDL150W RPC53 +Q12167 YDR065W RRG1 +Q12754 YPL012W RRP12 +Q06511 YPR143W RRP15 +P32786 YBL014C RRN6 +P25359 YCR035C RRP43 +P50943 YNL105W RRT16 +P53117 YGL146C RRT6 +Q01855 YOL040C RPS15 +P38701 YHL015W RPS20 +P0C0V8 YKR057W RPS21A +P08518 YOR151C RPB2 +P32561 YNL330C RPD3 +P38805 YHR088W RPF1 +P43588 YFR004W RPN11 +P38764 YHR027C RPN1 +P40016 YER021W RPN3 +P13433 YFL036W RPO41 +Q06109 YPR116W RRG8 +Q02983 YLR141W RRN5 +P38204 YBL025W RRN10 +P40992 YJL025W RRN7 +P0CX47 YDR025W RPS11A +P22276 YOR207C RET1 +P32910 YNR003C RPC34 +P36160 YKR081C RPF2 +O13563 YLR421C RPN13 +Q08723 YOR261C RPN8 +Q12532 YPL009C RQC2 +P53437 YMR270C RRN9 +Q04031 YDR412W RRP17 +P38961 YDR083W RRP8 +P40571 YIR015W RPR2 +P39677 YJL102W MEF2 +Q08774 YOR305W RRG7 +Q04712 YML043C RRN11 +P36080 YKL082C RRP14 +P46948 YGR195W SKI6 +Q12277 YDL111C RRP42 +P53256 YGR095C RRP46 +P40470 YIL127C RRT14 +P43607 YFR032C RRT5 +Q08219 YOL048C RRT8 +P07281 YNL302C RPS19B +Q3E792 YGR027C RPS25A +P39939 YER131W RPS26B +P41058 YDL061C RPS29B +P26783 YJR123W RPS5 +P48164 YNL096C RPS7B +Q06488 YLR357W RSC2 +P43609 YFR037C RSC8 +Q03246 YMR188C MRPS17 +P36056 YKL155C RSM22 +Q03976 YDR175C RSM24 +Q02950 YPL118W MRP51 +Q03919 YDR139C RUB1 +Q12464 YPL235W RVB2 +Q3E754 YJL136C RPS21B +P0CX31 YER074W RPS24A +Q08932 YPL193W RSA1 +P38781 YHR056C RSC30 +Q05043 YMR030W RSF1 +Q03430 YDR494W RSM28 +Q03201 YDR041W RSM10 +P38175 YBL090W MRP21 +P21771 YDR337W MRPS28 +P38786 YHR062C RPP1 +Q05468 YDR333C RQC1 +Q04225 YMR131C RRB1 +P38771 YHR038W RRF1 +P40156 YNL213C RRG9 +P38766 YHR031C RRM3 +P36070 YKL125W RRN3 +P38712 YHR065C RRP3 +Q08162 YOL021C DIS3 +P48589 YOR369C RPS12 +P07280 YOL121C RPS19A +P23248 YML063W RPS1B +P39516 YJL191W RPS14B +P0CX52 YDL083C RPS16B +P0CX56 YML026C RPS18B +P0CX29 YGR118W RPS23A +P0CX32 YIL069C RPS24B +P0C0T4 YLR333C RPS25B +P0CX35 YJR145C RPS4A +P32832 YMR091C NPL6 +Q03124 YML127W RSC9 +Q04693 YML049C RSE1 +P38792 YHR069C RRP4 +Q12149 YOR001W RRP6 +Q08746 YOR294W RRS1 +P38192 YBL048W RRT1 +P0C0W1 YJL190C RPS22A +P35997 YKL156W RPS27A +P0C0X0 YLR264W RPS28B +P25443 YGL123W RPS2 +P0CX34 YOR182C RPS30B +Q05942 YLR221C RSA3 +P53236 YGR056W RSC1 +Q02206 YKR008W RSC4 +P33442 YLR441C RPS1A +P0CX37 YPL090C RPS6A +P0CX40 YER102W RPS8B +Q08417 YOR049C RSB1 +P46974 YJR127C RSF2 +P40033 YER050C RSM18 +Q03516 YMR266W RSN1 +P32905 YGR214W RPS0A +P38120 YBR146W MRPS9 +P40063 YER104W RTT105 +P40161 YNL206C RTT106 +Q07794 YLL002W RTT109 +P53732 YNR036C MRPS12 +P53064 YGL244W RTF1 +P0CX30 YPR132W RPS23B +P41057 YLR388W RPS29A +P05750 YNL178W RPS3 +O13516 YPL081W RPS9A +Q07979 YLR033W RSC58 +Q12481 YOR287C RRP36 +Q3E811 YLR162W-A RRT15 +P05756 YDR064W RPS13 +P06367 YCR031C RPS14A +P39938 YGL189C RPS26A +P38711 YHR021C RPS27B +P05759 YLR167W RPS31 +P0CX51 YMR143W RPS16A +P14127 YDR447C RPS17B +P0CX55 YDR450W RPS18A +Q3E7Y3 YLR367W RPS22B +Q3E7X9 YOR167C RPS28A +P0CX33 YLR287C-A RPS30A +P0CX36 YHR203C RPS4B +P0CX38 YBR181C RPS6B +P0CX39 YBL072C RPS8A +P05755 YBR189W RPS9B +P02407 YML024W RPS17A +Q06639 YDR303C RSC3 +P40018 YER029C SMB1 +O14464 YPL183W-A RTC6 +P38165 YBL103C RTG3 +Q12443 YDL204W RTN2 +Q05900 YLR298C YHC1 +P26786 YOR096W RPS7A +P25632 YCR052W RSC6 +P28778 YKL003C MRP17 +Q05543 YDR289C RTT103 +P53305 YGR215W RSM27 +P19955 YFR049W YMR31 +Q12751 YMR185W RTP1 +P17558 YOR158W PET123 +Q12378 YDR066C RTR2 +Q12330 YOR159C SME1 +P38850 YHR154W RTT107 +P42847 YNL306W MRPS18 +Q01163 YGL129C RSM23 +P40496 YIL093C RSM25 +P53292 YGR165W MRPS35 +Q08281 YOL138C RTC1 +P40084 YER139C RTR1 +Q00916 YIL061C SNP1 +P32605 YBR119W MUD1 +Q08963 YPL213W LEA1 +P54999 YPR182W SMX3 +P25343 YCR009C RVS161 +P22470 YDR143C SAN1 +P53330 YGR275W RTT102 +Q02608 YPL013C MRPS16 +P53047 YGR213C RTA1 +P53850 YNL254C RTC4 +Q12108 YOR118W RTC5 +P32608 YGL252C RTG2 +Q04947 YDR233C RTN1 +P40962 YOR077W RTS2 +P20606 YPL218W SAR1 +P28707 YKL117W SBA1 +P06105 YJL080C SCP160 +P52871 YER019C-A SBH2 +P40541 YIL026C IRR1 +P03878 Q0065 AI4 +P03877 Q0060 AI3 +P11792 YHR205W SCH9 +P10663 YPR166C MRP2 +P47150 YJR113C RSM7 +P12686 YGR084C MRP13 +P53733 YNR037C RSM19 +P47141 YJR101W RSM26 +P32607 YOL067C RTG1 +Q03940 YDR190C RVB1 +P40204 YFL017W-A SMX2 +P32915 YLR378C SEC61 +P52870 YER087C-B SBH1 +Q12158 YDL003W MCD1 +P34758 YOR329C SCD5 +P21801 YLL041C SDH2 +Q07534 YDL119C HEM25 +P43612 YFR040W SAP155 +P17121 YDR389W SAC7 +Q12136 YDL153C SAS10 +Q04002 YDR180W SCC2 +P40090 YER147C SCC4 +P45978 YPR129W SCD6 +P03882 Q0160 SCEI +P32564 YGR049W SCM4 +Q04951 YMR305C SCW10 +Q03323 YDR469W SDC1 +P13856 YGR152C RSR1 +P46654 YLR048W RPS0B +P10662 YDR347W MRP1 +P32902 YHL004W MRP4 +P33759 YBR251W MRPS5 +Q03799 YMR158W MRPS8 +Q12100 YDL025C RTK1 +P53289 YGR161C RTS3 +Q12242 YOR138C RUP1 +P39743 YDR388W RVS167 +P38255 YBR095C RXT2 +P50110 YMR060C SAM37 +P40856 YJL098W SAP185 +P89114 YHR079C-A SAE3 +P38352 YBR280C SAF1 +P20840 YJR004C SAG1 +P39954 YER043C SAH1 +Q08985 YPL273W SAM4 +Q08873 YOR367W SCP1 +P40075 YER120W SCS2 +Q08230 YOL071W SDH5 +P40357 YGR009C SEC9 +Q01589 YDR077W SED1 +Q01590 YLR026C SED5 +P34228 YBL066C SEF1 +P16658 YLR105C SEN2 +P36123 YKR028W SAP190 +P32368 YKL212W SAC1 +P46674 YDR159W SAC3 +P43589 YFR005C SAD1 +P14693 YHR083W SAM35 +Q08986 YPL274W SAM3 +P53969 YNL026W SAM50 +P38429 YMR263W SAP30 +Q04003 YDR181C SAS4 +P53324 YGR263C SAY1 +P38814 YHR103W SBE22 +P42223 YDR351W SBE2 +P25303 YMR214W SCJ1 +P47052 YJL045W +P36047 YKL193C SDS22 +Q06245 YLR166C SEC10 +P48415 YPL085W SEC16 +P18759 YBR080C SEC18 +P28791 YDR498C SEC20 +P15303 YPR181C SEC23 +P17065 YNL272C SEC2 +P38968 YDL195W SEC31 +P21825 YPL094C SEC62 +P33754 YBR171W SEC66 +P39742 YLR292C SEC72 +Q04675 YMR059W SEN15 +Q00416 YLR430W SEN1 +P47008 YJL145W SFH5 +Q05567 YDR294C DPL1 +P36136 YKR043C SHB17 +P39000 YER096W SHC1 +Q02774 YDL212W SHR3 +Q07657 YDL225W SHS1 +P38751 YHL006C SHU1 +P50263 YMR175W SIP18 +P38717 YNL257C SIP3 +P06700 YDL042C SIR2 +P32900 YHR149C SKG6 +P35207 YLR398C SKI2 +P17883 YPR189W SKI3 +Q08491 YOR076C SKI7 +P42843 YNL311C SKP2 +P53327 YGR271W SLH1 +P38247 YBR077C SLM4 +Q00772 YHR030C SLT2 +P32908 YFL008W SMC1 +P32566 YGR229C SMI1 +Q04174 YOR149C SMP3 +P38990 YER129W SAK1 +P39955 YER047C SAP1 +P53036 YGL229C SAP4 +Q99314 YOR213C SAS5 +Q00711 YKL148C SDH1 +Q04491 YLR208W SEC13 +P24280 YMR079W SEC14 +P29478 YML105C SEC65 +Q02825 YPL083C SEN54 +P40510 YIL074C SER33 +P46995 YJL168C SET2 +Q08446 YOR057W SGT1 +P53266 YGR112W SHY1 +P38634 YLR079W SIC1 +P38262 YBR103W SIF2 +Q12216 YOR156C NFI1 +Q06315 YLR187W SKG3 +P38314 YBR214W SDS24 +P38164 YBL104C SEA4 +Q12745 YLR440C SEC39 +P33332 YER008C SEC3 +P89102 YDR166C SEC5 +P38890 YHR207C SET5 +Q12507 YOR315W SFG1 +P40363 YJL068C +P47166 YJR134C SGM1 +P32578 YDR422C SIP1 +Q02793 YGL213C SKI8 +P33336 YGR143W SKN1 +Q12505 YPL026C SKS1 +Q03656 YMR216C SKY1 +Q03406 YDR489W SLD5 +P38283 YBR156C SLI15 +P38345 YBR269C SDH8 +P38804 YHR087W RTC3 +Q07953 YLR022C SDO1 +P40479 YIL113W SDP1 +P53078 YGL224C SDT1 +P20048 YMR013C SEC59 +P14906 YOR254C SEC63 +Q04279 YMR086W SEG1 +P53011 YGL100W SEH1 +O94742 YDR363W-A SEM1 +P53953 YNL049C SFB2 +P43682 YKL006C-A SFT1 +P38166 YBL102W SFT2 +P40561 YIR001C SGN1 +Q08490 YOR073W SGO1 +P46954 YJL089W SIP4 +P21691 YKR101W SIR1 +P39980 YEL065W SIT1 +P53965 YNL032W SIW14 +Q04195 YDR409W SIZ1 +Q3E784 YER180C-A SLO1 +Q02775 YDR088C SLU7 +P40072 YER116C SLX8 +Q12334 YDL139C SCM3 +P23833 YBR037C SCO1 +P38072 YBR024W SCO2 +P11655 YNR026C SEC12 +P22224 YGL233W SEC15 +P30619 YDR164C SEC1 +P22214 YLR268W SEC22 +P07560 YFL005W SEC4 +P11075 YDR170C SEC7 +P32855 YPR055W SEC8 +P40316 YDR113C PDS1 +P25365 YCR067C SED4 +P39707 YAR008W SEN34 +P40054 YER081W SER3 +P42941 YGR208W SER2 +P36124 YKR029C SET3 +Q12529 YPL165C SET6 +Q12314 YOR021C SFM1 +P53313 YGR245C SDA1 +P33421 YKL141W SDH3 +P32602 YBL050W SEC17 +P40482 YIL109C SEC24 +P32844 YIL068C SEC6 +P34250 YKL105C SEG2 +P49955 YMR288W HSH155 +Q03067 YPL047W SGF11 +P53075 YGL228W SHE10 +P36068 YKL130C SHE2 +P38272 YBR130C SHE3 +Q04172 YDR393W SHE9 +P35179 YDR086C SSS1 +Q6Q595 YBL091C-A SCS22 +P53012 YGL126W SCS3 +P53189 YGL028C SCW11 +P53334 YGR279C SCW4 +P53009 YGL083W SCY1 +Q06058 YLR404W SEI1 +P39709 YAL067C SEO1 +P33330 YOR184W SER1 +P38827 YHR119W SET1 +Q12369 YLL003W SFI1 +P35735 YKL051W SFK1 +P20134 YOR140W SFL1 +Q12234 YOR216C RUD3 +Q07458 YDL076C RXT3 +P34218 YBL052C SAS3 +P40963 YMR127C SAS2 +P39735 YAL027W SAW1 +Q9ZZX1 Q0070 AI5_ALPHA +P36048 YKL173W SNU114 +P10870 YDL194W SNF3 +P18888 YHL025W SNF6 +P39929 YLR025W SNF7 +P00445 YJR104C SOD1 +Q05676 YEL059C-A SOM1 +Q06411 YLR424W SPP382 +Q03954 YDR201W SPC19 +Q03868 YDR104C SPO71 +Q06134 YLR341W SPO77 +P09937 YOR313C SPS4 +Q12455 YLR146C SPE4 +P06843 YER161C SPT2 +P35177 YBR081C SPT7 +P38985 YDL092W SRP14 +P32342 YKL122C SRP21 +P38688 YPL210C SRP72 +Q03529 YMR272C SCS7 +Q3E785 YDR379C-A SDH6 +Q04401 YDR511W SDH7 +P40505 YIL084C SDS3 +P15367 YIR022W SEC11 +P38810 YHR098C SFB3 +P33303 YJR095W SFC1 +P51534 YOR035C SHE4 +P38337 YBR258C SHG1 +P40073 YER118C SHO1 +P25294 YNL007C SIS1 +P52286 YDR328C SKP1 +P33338 YNL243W SLA2 +P43321 YLR147C SMD3 +Q12078 YLR034C SMF3 +P48232 YNL086W SNN1 +P53823 YNL334C SNO2 +P25357 YCR033W SNT1 +Q03782 YDR240C SNU56 +Q08826 YOR357C SNX3 +P43545 YFL059W SNZ3 +P50278 YNR034W SOL1 +P38858 YHR163W SOL3 +P53165 YGL066W SGF73 +Q12212 YOR137C SIA1 +Q08199 YOL031C SIL1 +P40472 YIL123W SIM1 +P11978 YDR227W SIR4 +P36169 YKR100C SKG1 +P32790 YBL007C SLA1 +P47037 YJL074C SMC3 +Q02260 YGR074W SMD1 +P38925 YOL122C SMF1 +Q04007 YDR186C SND1 +P38956 YDR073W SNF11 +P22082 YOR290C SNF2 +P46950 YGR197C SNG1 +P53127 YGL131C SNT2 +P39990 YEL026W SNU13 +Q04053 YDR425W SNX41 +Q03148 YMR096W SNZ1 +P53438 YMR016C SOK2 +P37262 YCR073W-A SOL2 +P38128 YBR182C SMP1 +P31109 YAL030W SNC1 +P33328 YOR327C SNC2 +P53628 YNR023W SNF12 +Q12420 YOR308C SNU66 +P40317 YDR006C SOK1 +P25808 YFL002C SPB4 +P46965 YJR010C-A SPC1 +P38915 YLR055C SPT8 +Q03707 YML034W SRC1 +Q99176 YLR119W SRN2 +P36057 YKL154W SRP102 +Q06688 YLR412W BER1 +Q03175 YMR101C SRT1 +P39931 YLR250W SSP120 +P38353 YBR283C SSH1 +P53172 YGL056C SDS23 +Q12118 YOR007C SGT2 +P38200 YBL031W SHE1 +P40486 YIL104C SHQ1 +P36024 YKR072C SIS2 +Q12469 YOL113W SKM1 +P38889 YHR206W SKN7 +Q02100 YNL167C SKO1 +P34252 YKL108W SLD2 +P53251 YGR081C SLX9 +Q04964 YML058W SML1 +Q12306 YDR510W SMT3 +P32364 YKL079W SMY1 +P32909 YBR172C SMY2 +Q06091 YPR101W SNT309 +P56508 YDR525W-A SNA2 +Q03144 YMR095C SNO1 +Q04902 YMR322C SNO4 +Q12368 YDL098C SNU23 +P00447 YHR008C SOD2 +P53315 YGR248W SOL4 +P23201 YLL021W SPA2 +Q04969 YML055W SPC2 +P36131 YKR037C SPC34 +Q08204 YOL034W SMC5 +Q12749 YLR383W SMC6 +Q06217 YLR275W SMD2 +P47057 YJL036W SNX4 +P38282 YBR152W SPP381 +P53540 YNL126W SPC98 +P50088 YGR236C SPG1 +P40092 YER150W SPI1 +P53541 YNL012W SPO1 +P40031 YER046W SPO73 +P32572 YNL204C SPS18 +P35209 YMR179W SPT21 +P42948 YJL105W SET4 +Q99287 YOR165W SEY1 +Q06168 YLR321C SFH1 +P32432 YLR403W SFP1 +P25554 YCL010C SGF29 +Q06236 YLR164W SHH4 +P38957 YDR078C SHU2 +P22579 YOL004W SIN3 +P34164 YGL208W SIP2 +P40210 YMR140W SIP5 +P53955 YNL047C SLM2 +Q12098 YLR135W SLX4 +P22215 YOR307C SLY41 +P40167 YNL196C SLZ1 +P40548 YIL016W SNL1 +Q12034 YDR515W SLF1 +P54867 YOR008C SLG1 +P40485 YIL105C SLM1 +P39928 YIL147C SLN1 +P42900 YLR139C SLS1 +P38241 YBR065C ECM2 +P38324 YBR228W SLX1 +Q12267 YLR086W SMC4 +P41808 YPR054W SMK1 +P18480 YBR289W SNF5 +Q12483 YPL002C SNF8 +P43544 YFL060C SNO3 +P32568 YDR011W SNQ2 +P53207 YGR013W SNU71 +P53824 YNL333W SNZ2 +Q04748 YMR066W SOV1 +Q12133 YLR066W SPC3 +P36094 YKL042W SPC42 +Q12074 YPR069C SPE3 +Q04438 YMR107W SPG4 +P17123 YHR152W SPO12 +Q04359 YMR017W SPO20 +Q02521 YOR148C SPP2 +P50875 YOL148C SPT20 +Q06132 YLR336C SGD1 +P33335 YPR198W SGE1 +P35187 YMR190C SGS1 +Q04487 YMR118C SHH3 +P06701 YLR442C SIR3 +P34226 YBL061C SKT5 +Q08457 YOR060C SLD7 +P53304 YGR212W SLI1 +Q08581 YOR195W SLK19 +Q12232 YOR154W SLP1 +P32380 YDR356W SPC110 +P25582 YCL054W SPB1 +P38863 YHR172W SPC97 +Q04398 YDR504C SPG3 +P33419 YPL124W SPC29 +Q06160 YLR313C SPH1 +P23179 YHL022C SPO11 +P23624 YHR014W SPO13 +Q03029 YPL130W SPO19 +P40511 YIL073C SPO22 +P45819 YGL170C SPO74 +P18410 YAL009W SPO7 +P38904 YDR464W SPP41 +P32603 YOR190W SPR1 +P41901 YGR059W SPR3 +P32573 YNL202W SPS19 +P08458 YDR523C SPS1 +P32558 YGL207W SPT16 +P35210 YKL020C SPT23 +P32914 YGR063C SPT4 +P53866 YNL224C SQS1 +P25648 YCR081W SRB8 +P24276 YDR293C SSD1 +P32343 YKL124W SSH4 +Q02794 YOR047C STD1 +Q06010 YLR389C STE23 +P15705 YOR027W STI1 +P38960 YDR082W STN1 +Q00947 YDR463W STP1 +P38989 YFR031C SMC2 +P14359 YJL151C SNA3 +P38839 YHR136C SPL2 +P35184 YIR012W SQT1 +Q12516 YDL133W SRF1 +Q12020 YLR082C SRL2 +P36167 YKR091W SRL3 +P25567 YCL037C SRO9 +P20424 YPR088C SRP54 +P36077 YKL086W SRX1 +Q08646 YOR242C SSP2 +P42845 YNL309W STB1 +P38699 YHR178W STB5 +P32584 YDR410C STE14 +Q03497 YHL007C STE20 +P06783 YKL178C STE3 +P32917 YDR103W STE5 +P12866 YKL209C STE6 +P06784 YDL159W STE7 +P39932 YDR536W STL1 +P09959 YLR182W SWI6 +P46655 YGL245W GUS1 +P53277 YGR129W SYF2 +P11972 YLR452C SST2 +P41930 YPL092W SSU1 +P50104 YMR019W STB4 +P53394 YPR003C +P08153 YDR146C SWI5 +Q12379 YDR260C SWM1 +P43554 YFL049W SWP82 +Q05471 YDR334W SWR1 +P53852 YNL247W +P15179 YPL104W MSD1 +P23615 YGR116W SPT6 +Q08673 YOR247W SRL1 +Q03085 YPL033C SRL4 +P10080 YHL034C SBP1 +P53599 YNR031C SSK2 +Q07084 YLR006C SSK1 +P32867 YPL232W SSO1 +Q12427 YDR169C STB3 +P36085 YKL072W STB6 +D6VTK4 YFL026W STE2 +P25344 YCL032W STE50 +P16965 YGR008C STF2 +P53312 YGR244C LSC2 +Q06524 YPR151C SUE1 +P38359 YBR294W SUL1 +Q05515 YDR346C SVF1 +Q03088 YPL032C SVL3 +Q06677 YDR320C SWA2 +Q12104 YOR166C SWT1 +P53135 YGL113W SLD3 +P38343 YBR266C SLM6 +P32828 YDL013W SLX5 +Q02651 YPL027W SMA1 +Q04658 YML066C SMA2 +Q08817 YOR353C SOG2 +P39543 YJL192C SOP4 +P53148 YGL093W SPC105 +Q01684 YER115C SPR6 +P06844 YDR392W SPT3 +P38687 YPL243W SRP68 +P32916 YDR292C SRP101 +P12954 YJL092W SRS2 +P13130 YHR139C SPS100 +P39073 YPL042C SSN3 +P47821 YNL025C SSN8 +P22213 YDR189W SLY1 +P38778 YHR050W SMF2 +Q07549 YDL123W SNA4 +Q04477 YMR117C SPC24 +P40014 YER018C SPC25 +P39723 YAL047C SPC72 +P42933 YMR191W SPG5 +P17122 YHR153C SPO16 +Q03012 YPL138C SPP1 +P25380 YCL048W SPS22 +P35208 YJL127C SPT10 +P27692 YML010W SPT5 +P39015 YLR150W STM1 +Q05937 YLR375W STP3 +Q07351 YDL048C STP4 +P38163 YBL106C SRO77 +Q12038 YPR032W SRO7 +P32583 YKR092C SRP40 +P38931 YDR443C SSN2 +P38871 YHR184W SSP1 +P37296 YMR054W STV1 +P31377 YAL014C SYN8 +P53598 YOR142W LSC1 +P36126 YKR031C SPO14 +P33757 YBR250W SPO23 +Q07798 YLL005C SPO75 +Q04921 YDR218C SPR28 +P08459 YDR522C SPS2 +P09007 YCR018C SRD1 +P38789 YHR066W SSF1 +P39926 YMR183C SSO2 +Q03770 YDR160W SSY1 +P38788 YHR064C SSZ1 +P25379 YCL064C CHA1 +P33894 YOR219C STE13 +P53538 YNL222W SSU72 +P53101 YGL184C STR3 +Q12325 YLR092W SUL2 +P46676 YDR310C SUM1 +P36150 YKR069W MET1 +P53616 YNL066W SUN4 +P33300 YPL057C SUR1 +P54003 YML052W SUR7 +P53937 YNL081C SWS2 +Q08553 YOR179C SYC1 +P04802 YLL018C DPS1 +P48525 YOL033W MSE1 +Q02875 YPL105C SYH1 +P39965 YER087W AIM10 +P54000 YMR039C SUB1 +Q07478 YDL084W SUB2 +P31376 YAL011W SWC3 +P53201 YGR002C SWC4 +P38326 YBR231C SWC5 +Q06707 YLR385C SWC7 +P36104 YKL018W SWD2 +Q04175 YDR395W SXM1 +P15624 YLR060W FRS1 +Q06817 YPR081C GRS2 +P38088 YBR121C GRS1 +Q6WNK7 YBR111W-A SUS1 +P38869 YHR181W SVP26 +P39706 YAR003W SWD1 +P38123 YBR175W SWD3 +P09547 YPL016W SWI1 +P32591 YJL176C SWI3 +P40825 YOR335C ALA1 +P40528 YIL047C SYG1 +P47002 YJL156C SSY5 +P46679 YMR053C STB2 +P23561 YLR362W STE11 +P01098 YDL130W-A STF1 +P39007 YGL022W STT3 +P38198 YBL034C STU1 +P46675 YLR045C STU2 +P32911 YNL244C SUI1 +Q12286 YPR009W SUT2 +P32580 YPL029W SUV3 +Q12254 YPL163C SVS1 +Q04629 YDR126W SWF1 +P08425 YPR047W MSF1 +P15180 YDR037W KRS1 +Q04048 YDR416W SYF1 +P07263 YPR033C HTS1 +Q06563 YLR251W SYM1 +Q05506 YDR341C +P07284 YDR023W SES1 +P40150 YNL209W SSB2 +Q12153 YDR312W SSF2 +P25390 YCR073C SSK22 +Q04673 YLR005W SSL1 +P13574 YHR084W STE12 +P47154 YJR117W STE24 +P32597 YIL126W STH1 +P25604 YCL008C STP22 +P38704 YHR006W STP2 +P38637 YIR011C STS1 +P37297 YLR305C STT4 +P32579 YGL169W SUA5 +P53032 YGL162W SUT1 +P32944 YJL187C SWE1 +P25302 YER111C SWI4 +P15625 YFL022C FRS2 +P32048 YNL073W MSK1 +P11325 YLR382C NAM2 +Q07395 YDL063C SYO1 +P07806 YGR094W VAS1 +P41895 YGR186W TFG1 +Q12030 YDR167W TAF10 +P35189 YPL129W TAF14 +P23255 YCR042C TAF2 +Q12297 YPL011C TAF3 +P38992 YDR297W SUR2 +P40342 YNR004W SWM2 +P53873 YNL187W SWT21 +P09436 YBL076C ILS1 +P48526 YPL040C ISM1 +Q06836 YPR095C SYT1 +P53040 YGL112C TAF6 +Q05027 YMR236W TAF9 +P25638 YCR060W TAH1 +P15019 YLR354C TAL1 +P25345 YCR024C SLM5 +P13188 YOR168W GLN4 +P32774 YKL058W TOA2 +P36421 YGR185C TYS1 +P36100 YKL028W TFA1 +Q9URQ3 YLR316C TAD3 +Q04226 YML015C TAF11 +P38129 YBR198C TAF5 +Q03750 YML114C TAF8 +P09733 YML085C TUB1 +P32613 YEL048C TCA17 +P42943 YJL111W CCT7 +Q6B2U8 YAL064C-A TDA8 +Q04545 YML081W TDA9 +P34163 YKL140W TGL1 +Q12043 YOR081C TGL5 +P38714 YHR091C MSR1 +P38705 YHR011W DIA4 +P04801 YIL078W THS1 +Q12109 YOL097C WRS1 +P38854 YHR159W TDA11 +Q03533 YMR291W TDA1 +P40045 YER071C TDA2 +P47153 YJR116W TDA4 +P07236 YKL194C MST1 +P46677 YGR274C TAF1 +P02557 YFL037W TUB2 +P38114 YBR150C TBS1 +Q12466 YOR086C TCB1 +Q03640 YML072C TCB3 +P36101 YKL027W TCD2 +Q99190 YDL015C TSC13 +P40533 YIL039W TED1 +Q07921 YLR010C TEN1 +P53065 YGL243W TAD1 +P47058 YJL035C TAD2 +Q03761 YDR145W TAF12 +P50105 YMR005W TAF4 +P53072 YGL232W TAN1 +P39076 YIL142W CCT2 +P40413 YJR064W CCT5 +P39079 YDR188W CCT6 +P42938 YGR205W TDA10 +P38758 YHR009C TDA3 +P53882 YNL176C TDA7 +P39933 YPR186C PZF1 +Q02939 YPL122C TFB2 +Q12004 YPR056W TFB4 +P34111 YAL001C TFC3 +Q04372 YMR028W TAP42 +P40085 YER140W EMP65 +P13393 YER148W SPT15 +P38756 YHR003C TCD1 +Q06466 YPR157W TDA6 +P47988 YOR337W TEA1 +P18412 YBR083W TEC1 +P53038 YGR099W TEL2 +Q06163 YLR318W EST2 +P53851 YNL253W TEX1 +P32367 YBR123C TFC1 +P53215 YGR024C THG1 +Q07748 YDL244W THI13 +Q08975 YPL258C THI21 +Q08579 YOR192C THI72 +P41544 YJL004C SYS1 +P41896 YGR005C TFG2 +Q05021 YMR227C TAF7 +P40468 YIL129C TAO3 +Q8TGM6 YLR154W-C TAR1 +P38967 YOL020W TAT2 +P47030 YJL083W TAX4 +P26637 YPL160W CDC60 +P00958 YGR264C MES1 +P22438 YGR171C MSM1 +P04803 YDR268W MSW1 +P48527 YPL097W MSY1 +P36145 YKR062W TFA2 +P11747 YML098W TAF13 +P53228 YGR043C NQM1 +P38085 YBR069C TAT1 +P48606 YOR265W RBL2 +P46670 YPL241C CIN2 +P38707 YHR019C DED81 +P09734 YML124C TUB3 +P53904 YNL148C ALF1 +P53378 YLR212C TUB4 +P48231 YNL087W TCB2 +P12612 YDR212W TCP1 +P47079 YJL008C CCT8 +O13513 YAL056C-A +O13511 YAL065C +P39728 YAL037W +P39725 YAL045C +Q8TGU6 YBR182C-A +Q12260 YBL100W-A TY2A-B +Q8TGU5 YBR296C-A +P38311 YBR209W +P38321 YBR225W +P38331 YBR242W +P38178 YBL083C +P38168 YBL100C +P38240 YBR064W +P38276 YBR137W +P25565 YCL002C +P25561 YCL021W +O13527 YAR009C TY1B-A +P0C5L1 YBL068W-A +Q7M4S9 YBL113C +P0C5L4 YBR121C-A +Q8TGK5 YBL113W-A +Q3E755 YBR200W-A +Q8TGQ3 YBR223W-A +P38296 YBR178W +P38327 YBR232C +P38354 YBR285W +P38362 YBR300C +Q3E778 YBR196C-B +P32788 YBL010C +P38177 YBL086C +P38171 YBL096C +P38214 YBR012C +P38315 YBR216C YBP1 +P38267 YBR113W +P38275 YBR134W +P34215 YBR144C +Q96VH2 YCL001W-B +P25571 YCL041C +P25350 YCR006C +Q3E7Z7 YDR003W-A +Q12281 YDL032W +Q07793 YDR261C-D TY1B-DR4 +Q12082 YDL157C +Q12148 YDL163W +Q03983 YDR179W-A +P48568 YDL186W +Q2V2P9 YDR119W-A +Q03787 YDR249C +Q05612 YDR278C +Q05497 YDR338C +Q3E6R5 YDR381C-A +P87266 YDR413C +Q8TGP5 YDR464C-A +P87274 YDR526C +P87261 YDR537C +P0CL37 YDR545C-A +Q02896 YPL087W YDC1 +P40057 YER084W +P40093 YER156C +Q3E838 YFR012W-A +P43541 YFL063W +P43600 YFR020W +P0C5N1 YGL014C-A +P53185 YGL036W +O13515 YAL034C-B +O13514 YAL042C-A +A0A023PYD0 YAL059C-A +P0CX18 YAR066W +P47118 YJR067C YAE1 +P0CX90 YAR061W +P0CX92 YAR069C +P40574 YIR018W YAP5 +Q3E756 YBL029C-A +P0C5L0 YBR056C-B +P34220 YBL055C +P38185 YBL071C +P38183 YBL077W +P38173 YBL094C +P53169 YGL060W YBP2 +P38256 YBR096W +P25577 YCL049C +P25601 YCL075W TY5B +P25616 YCR015C +P25629 YCR049C +P25630 YCR050C +P25608 YCR102C +Q2V2Q0 YDL007C-A +Q12185 YDR018C +Q12352 YDL041W +Q03831 YDR095C +Q03856 YDR098C-A TY1A-DR1 +Q07541 YDL121C +O74302 YDR261C-C TY1A-DR4 +P0CX70 YDR365W-A TY1A-DR6 +Q12027 YDL176W +Q03964 YDR170W-A TY1A-DR2 +Q3E818 YDR194W-A +Q12424 YDL206W +Q07629 YDL218W +Q04923 YDR220C +A0A023PZA9 YDR230W +Q99303 YDR261W-A TY2A-DR3 +Q07791 YDR261W-B TY2B-DR3 +Q05510 YDR344C +P0C5M1 YDR371C-A +Q04162 YDR387C +P87268 YDR426C +A0A023PYD7 YDR187C +Q12187 YDL196W +Q04597 YDR114C +A0A023PZ94 YAL031W-A +Q8TGV0 YAR035C-A +A0A023PZE2 YAL047W-A +Q8TGR8 YAL037C-B +O13512 YAL064W-B +P39711 YAL064W +P14680 YJL141C YAK1 +P46683 YPL239W YAR1 +Q3E794 YBR072C-A +P90471 YBR109W-A +Q6B113 YBL107W-A +Q12491 YBL100W-B TY2B-B +P38317 YBR219C +P38322 YBR226C +P38357 YBR292C +P38350 YBR277C +P38188 YBL065W +P38184 YBL073W +Q8TGQ1 YCR047W-A +Q96VG6 YCR097W-A +A0A023PXB0 YAR019W-A +O42831 YAR075W +A0A023PYC6 YAL016C-A +P39548 YAR028W +P0CX88 YAR060C +P0CI66 YAR062W +P39564 YAR068W +P40917 YOR028C CIN5 +P39710 YAL066W +Q3E821 YBL008W-A +Q3E7Y5 YBL111C +Q8TGU7 YBR126W-A +Q8TGQ5 YBR131C-A +P0C5L5 YBR191W-A +P0C268 YBL039W-B +Q3E820 YBR196C-A +P38190 YBL053W +P38186 YBL070C +P38081 YBR056W +P38252 YBR089W +P38258 YBR099C +P25572 YCL042W +Q12448 YDL034W +Q3E6R4 YDR524C-B +A0A023PZF2 YEL009C-A +Q3E7B0 YER053C-A +Q8TGR4 YER088W-B +Q03612 YER138C TY1B-ER1 +P40103 YER188W +P40104 YER189W +P32622 YEL041W YEF1 +P40052 YER079W +P40560 YIL001W +P40536 YIL032C +E2QC18 +E9PAE8 +E9PAE4 +E9PAD8 +E9PAE3 truncated TYB +E9PAE7 +E9PAD6 +E9PAF1 diff --git a/tests/tests.py b/tests/tests.py index 6ab075a..b4af723 100644 --- a/tests/tests.py +++ b/tests/tests.py @@ -58,8 +58,8 @@ def test_data(self): except: shutil.copy(os.path.join(ref_dir, 'uniprot_mod_raw.txt'), '.') self.assertTrue(os.path.isfile('uniprot_mod_raw.txt')) - self.c.clean('uniprot_mod_raw.txt') # produces PTMs.txt + self.assertTrue(os.path.isfile('PTMs.txt')) if self.store_ref: shutil.copy('PTMs.txt', ref_dir) # saving the reference data diff --git a/ymap/ymap.py b/ymap/ymap.py index 959bd34..860dc9d 100644 --- a/ymap/ymap.py +++ b/ymap/ymap.py @@ -280,7 +280,7 @@ def clean(self, UniProt_file): if p > str(0): # PTMs.txt is already open under out and being opened again and again... # this could cause problems check if you cannot just remove all the opens... - # out = open('PTMs.txt', 'a') + #out = open('PTMs.txt', 'a') out.write(p+'\n') continue if line[2] == 'Glycosylation': @@ -289,7 +289,7 @@ def clean(self, UniProt_file): gg = gg[2].split('=') p1 = line[0]+'\t'+line[4]+'\t'+gg[1] if p1 > str(0): - # out = open('PTMs.txt', 'a+') + #out = open('PTMs.txt', 'a+') out.write(p1+'\n') continue if line[2] == 'Modified': From 53dbd48fabcf9eefaebcca60ff396712ed84d553 Mon Sep 17 00:00:00 2001 From: Michiel van Setten Date: Fri, 20 Oct 2017 16:15:38 +0200 Subject: [PATCH 4/4] reference files --- tests/tests.py | 23 +++++------------------ ymap/ymap.py | 29 ++++++++++++++--------------- 2 files changed, 19 insertions(+), 33 deletions(-) diff --git a/tests/tests.py b/tests/tests.py index b4af723..730f978 100644 --- a/tests/tests.py +++ b/tests/tests.py @@ -31,7 +31,7 @@ def setUp(self): self.test_dir = tempfile.mkdtemp() os.chdir(self.test_dir) self.c = YGtPM() - self.store_ref = False + # self.store_ref = False # at various places out put is compared to stored reference files. put this to true # to regenerate all reference files @@ -44,39 +44,26 @@ def test_class_creation(self): testing the creation of YGtPM """ self.assertIsInstance(self.c, YGtPM) + self.c.pTMdata() + self.assertTrue(os.path.isfile('uniprot_mod_raw.txt')) def test_data(self): """ testing the steps in data() """ - self.assertIsInstance(self.c, YGtPM) - try: # the actual download can only be performed a limit number of times per hour - raise RuntimeError # this is to prevent connecting the database during development comment for real tesing - self.c.pTMdata() - if self.store_ref: - shutil.copy('uniprot_mod_raw.txt', ref_dir) # saving the reference data - except: - shutil.copy(os.path.join(ref_dir, 'uniprot_mod_raw.txt'), '.') - self.assertTrue(os.path.isfile('uniprot_mod_raw.txt')) - self.c.clean('uniprot_mod_raw.txt') # produces PTMs.txt + shutil.copy(os.path.join(ref_dir, 'uniprot_mod_raw.txt'), '.') # saving the reference data + self.c.clean('uniprot_mod_raw.txt') # produces PTMs.txt self.assertTrue(os.path.isfile('PTMs.txt')) - if self.store_ref: - shutil.copy('PTMs.txt', ref_dir) # saving the reference data self.assertTrue(filecmp.cmp('PTMs.txt', os.path.join(ref_dir, 'PTMs.txt'))) self.c.iD() self.assertTrue(os.path.isfile('yeastID.txt')) - if self.store_ref: - shutil.copy('yeastID.txt', ref_dir) # saving the reference data self.assertTrue(filecmp.cmp('yeastID.txt', os.path.join(ref_dir, 'yeastID.txt'))) self.c.pmap('yeastID.txt', 'PTMs.txt') self.assertTrue(os.path.isfile('PTM_id_file.txt')) - if self.store_ref: - shutil.copy('PTM_id_file.txt', ref_dir) # saving the reference data self.assertTrue(filecmp.cmp('PTM_id_file.txt', os.path.join(ref_dir, 'PTM_id_file.txt'))) - self.assertTrue(False) def test_ymap_proteins(self): self.assertTrue(True) diff --git a/ymap/ymap.py b/ymap/ymap.py index 860dc9d..412680d 100644 --- a/ymap/ymap.py +++ b/ymap/ymap.py @@ -31,14 +31,14 @@ from __future__ import absolute_import from __future__ import division from __future__ import unicode_literals -#try: -# from builtins import next -# from builtins import str -# from builtins import range -# from builtins import object -# from builtins import bytes -#except ImportError: -# pass +try: + from builtins import next + from builtins import str + from builtins import range + from builtins import object + from builtins import bytes +except ImportError: + pass import os import sys import math @@ -1050,27 +1050,27 @@ def data(): except IOError: pass try: - m = c.pmap('yeastID.txt', 'PTMs.txt') + c.pmap('yeastID.txt', 'PTMs.txt') except IOError: pass try: - d = c.dclean('uniprot_mod_raw.txt') + c.dclean('uniprot_mod_raw.txt') except IOError: pass try: - dm = c.d_map('yeastID.txt', 'domains.txt') + c.d_map('yeastID.txt', 'domains.txt') except IOError: pass try: - ab = c.ab('uniprot_mod_raw.txt') + c.ab('uniprot_mod_raw.txt') except IOError: pass try: - ii = c.id('bact.txt', 'yeast_id.txt') + c.id('bact.txt', 'yeast_id.txt') except IOError: pass try: - bio=c.bioGrid() + c.bioGrid() except IOError: pass try: @@ -1696,4 +1696,3 @@ def path(): pass else: print ("to run a function seek help") -